data_9LNV
# 
_entry.id   9LNV 
# 
_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   9LNV         pdb_00009lnv 10.2210/pdb9lnv/pdb 
WWPDB D_1300056064 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_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                        9LNV 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 allenwu1991@163.com Wu   Chengyong ? 'principal investigator/group leader' 0000-0003-4674-442X 
3 593672467@qq.com    Wang Yuxi      ? 'principal investigator/group leader' 0000-0002-4056-5829 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wu, C.Y.'   1 ? 
'Wang, Y.X.' 2 ? 
'Chen, Q.F.' 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 structure of T2R-TTL-YQVB6 Complex' 
_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 'Wu, C.Y.'   1 ? 
primary 'Wang, Y.X.' 2 ? 
primary 'Chen, Q.F.' 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 'Detyrosinated tubulin alpha-1B chain' 50041.273 2  ? ? ? ? 
2  polymer     man 'Tubulin beta chain'                   49999.887 2  ? ? ? ? 
3  polymer     man Stathmin-4                             16844.162 1  ? ? ? ? 
4  polymer     man 'Tubulin tyrosine ligase'              44378.496 1  ? ? ? ? 
5  non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"            523.180   2  ? ? ? ? 
6  non-polymer syn 'MAGNESIUM ION'                        24.305    2  ? ? ? ? 
7  non-polymer syn 'CALCIUM ION'                          40.078    2  ? ? ? ? 
8  non-polymer syn "10'-fluorovinblastine"                828.965   1  ? ? ? ? 
9  non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"             443.201   2  ? ? ? ? 
10 water       nat water                                  18.015    15 ? ? ? ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        'Stathmin-like protein B3,RB3' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
A,C ? 
2 'polypeptide(L)' no no 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
D,B ? 
3 'polypeptide(L)' no no 
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
E   ? 
4 'polypeptide(L)' no no 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHHHHHH
;
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHHHHHH
;
F   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5  "GUANOSINE-5'-TRIPHOSPHATE" GTP   
6  'MAGNESIUM ION'             MG    
7  'CALCIUM ION'               CA    
8  "10'-fluorovinblastine"     A1EPR 
9  "GUANOSINE-5'-DIPHOSPHATE"  GDP   
10 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   ARG n 
1 3   GLU n 
1 4   CYS n 
1 5   ILE n 
1 6   SER n 
1 7   ILE n 
1 8   HIS n 
1 9   VAL n 
1 10  GLY n 
1 11  GLN n 
1 12  ALA n 
1 13  GLY n 
1 14  VAL n 
1 15  GLN n 
1 16  ILE n 
1 17  GLY n 
1 18  ASN n 
1 19  ALA n 
1 20  CYS n 
1 21  TRP n 
1 22  GLU n 
1 23  LEU n 
1 24  TYR n 
1 25  CYS n 
1 26  LEU n 
1 27  GLU n 
1 28  HIS n 
1 29  GLY n 
1 30  ILE n 
1 31  GLN n 
1 32  PRO n 
1 33  ASP n 
1 34  GLY n 
1 35  GLN n 
1 36  MET n 
1 37  PRO n 
1 38  SER n 
1 39  ASP n 
1 40  LYS n 
1 41  THR n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  GLY n 
1 46  ASP n 
1 47  ASP n 
1 48  SER n 
1 49  PHE n 
1 50  ASN n 
1 51  THR n 
1 52  PHE n 
1 53  PHE n 
1 54  SER n 
1 55  GLU n 
1 56  THR n 
1 57  GLY n 
1 58  ALA n 
1 59  GLY n 
1 60  LYS n 
1 61  HIS n 
1 62  VAL n 
1 63  PRO n 
1 64  ARG n 
1 65  ALA n 
1 66  VAL n 
1 67  PHE n 
1 68  VAL n 
1 69  ASP n 
1 70  LEU n 
1 71  GLU n 
1 72  PRO n 
1 73  THR n 
1 74  VAL n 
1 75  ILE n 
1 76  ASP n 
1 77  GLU n 
1 78  VAL n 
1 79  ARG n 
1 80  THR n 
1 81  GLY n 
1 82  THR n 
1 83  TYR n 
1 84  ARG n 
1 85  GLN n 
1 86  LEU n 
1 87  PHE n 
1 88  HIS n 
1 89  PRO n 
1 90  GLU n 
1 91  GLN n 
1 92  LEU n 
1 93  ILE n 
1 94  THR n 
1 95  GLY n 
1 96  LYS n 
1 97  GLU n 
1 98  ASP n 
1 99  ALA n 
1 100 ALA n 
1 101 ASN n 
1 102 ASN n 
1 103 TYR n 
1 104 ALA n 
1 105 ARG n 
1 106 GLY n 
1 107 HIS n 
1 108 TYR n 
1 109 THR n 
1 110 ILE n 
1 111 GLY n 
1 112 LYS n 
1 113 GLU n 
1 114 ILE n 
1 115 ILE n 
1 116 ASP n 
1 117 LEU n 
1 118 VAL n 
1 119 LEU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 ARG n 
1 124 LYS n 
1 125 LEU n 
1 126 ALA n 
1 127 ASP n 
1 128 GLN n 
1 129 CYS n 
1 130 THR n 
1 131 GLY n 
1 132 LEU n 
1 133 GLN n 
1 134 GLY n 
1 135 PHE n 
1 136 LEU n 
1 137 VAL n 
1 138 PHE n 
1 139 HIS n 
1 140 SER n 
1 141 PHE n 
1 142 GLY n 
1 143 GLY n 
1 144 GLY n 
1 145 THR n 
1 146 GLY n 
1 147 SER n 
1 148 GLY n 
1 149 PHE n 
1 150 THR n 
1 151 SER n 
1 152 LEU n 
1 153 LEU n 
1 154 MET n 
1 155 GLU n 
1 156 ARG n 
1 157 LEU n 
1 158 SER n 
1 159 VAL n 
1 160 ASP n 
1 161 TYR n 
1 162 GLY n 
1 163 LYS n 
1 164 LYS n 
1 165 SER n 
1 166 LYS n 
1 167 LEU n 
1 168 GLU n 
1 169 PHE n 
1 170 SER n 
1 171 ILE n 
1 172 TYR n 
1 173 PRO n 
1 174 ALA n 
1 175 PRO n 
1 176 GLN n 
1 177 VAL n 
1 178 SER n 
1 179 THR n 
1 180 ALA n 
1 181 VAL n 
1 182 VAL n 
1 183 GLU n 
1 184 PRO n 
1 185 TYR n 
1 186 ASN n 
1 187 SER n 
1 188 ILE n 
1 189 LEU n 
1 190 THR n 
1 191 THR n 
1 192 HIS n 
1 193 THR n 
1 194 THR n 
1 195 LEU n 
1 196 GLU n 
1 197 HIS n 
1 198 SER n 
1 199 ASP n 
1 200 CYS n 
1 201 ALA n 
1 202 PHE n 
1 203 MET n 
1 204 VAL n 
1 205 ASP n 
1 206 ASN n 
1 207 GLU n 
1 208 ALA n 
1 209 ILE n 
1 210 TYR n 
1 211 ASP n 
1 212 ILE n 
1 213 CYS n 
1 214 ARG n 
1 215 ARG n 
1 216 ASN n 
1 217 LEU n 
1 218 ASP n 
1 219 ILE n 
1 220 GLU n 
1 221 ARG n 
1 222 PRO n 
1 223 THR n 
1 224 TYR n 
1 225 THR n 
1 226 ASN n 
1 227 LEU n 
1 228 ASN n 
1 229 ARG n 
1 230 LEU n 
1 231 ILE n 
1 232 SER n 
1 233 GLN n 
1 234 ILE n 
1 235 VAL n 
1 236 SER n 
1 237 SER n 
1 238 ILE n 
1 239 THR n 
1 240 ALA n 
1 241 SER n 
1 242 LEU n 
1 243 ARG n 
1 244 PHE n 
1 245 ASP n 
1 246 GLY n 
1 247 ALA n 
1 248 LEU n 
1 249 ASN n 
1 250 VAL n 
1 251 ASP n 
1 252 LEU n 
1 253 THR n 
1 254 GLU n 
1 255 PHE n 
1 256 GLN n 
1 257 THR n 
1 258 ASN n 
1 259 LEU n 
1 260 VAL n 
1 261 PRO n 
1 262 TYR n 
1 263 PRO n 
1 264 ARG n 
1 265 ILE n 
1 266 HIS n 
1 267 PHE n 
1 268 PRO n 
1 269 LEU n 
1 270 ALA n 
1 271 THR n 
1 272 TYR n 
1 273 ALA n 
1 274 PRO n 
1 275 VAL n 
1 276 ILE n 
1 277 SER n 
1 278 ALA n 
1 279 GLU n 
1 280 LYS n 
1 281 ALA n 
1 282 TYR n 
1 283 HIS n 
1 284 GLU n 
1 285 GLN n 
1 286 LEU n 
1 287 SER n 
1 288 VAL n 
1 289 ALA n 
1 290 GLU n 
1 291 ILE n 
1 292 THR n 
1 293 ASN n 
1 294 ALA n 
1 295 CYS n 
1 296 PHE n 
1 297 GLU n 
1 298 PRO n 
1 299 ALA n 
1 300 ASN n 
1 301 GLN n 
1 302 MET n 
1 303 VAL n 
1 304 LYS n 
1 305 CYS n 
1 306 ASP n 
1 307 PRO n 
1 308 ARG n 
1 309 HIS n 
1 310 GLY n 
1 311 LYS n 
1 312 TYR n 
1 313 MET n 
1 314 ALA n 
1 315 CYS n 
1 316 CYS n 
1 317 LEU n 
1 318 LEU n 
1 319 TYR n 
1 320 ARG n 
1 321 GLY n 
1 322 ASP n 
1 323 VAL n 
1 324 VAL n 
1 325 PRO n 
1 326 LYS n 
1 327 ASP n 
1 328 VAL n 
1 329 ASN n 
1 330 ALA n 
1 331 ALA n 
1 332 ILE n 
1 333 ALA n 
1 334 THR n 
1 335 ILE n 
1 336 LYS n 
1 337 THR n 
1 338 LYS n 
1 339 ARG n 
1 340 SER n 
1 341 ILE n 
1 342 GLN n 
1 343 PHE n 
1 344 VAL n 
1 345 ASP n 
1 346 TRP n 
1 347 CYS n 
1 348 PRO n 
1 349 THR n 
1 350 GLY n 
1 351 PHE n 
1 352 LYS n 
1 353 VAL n 
1 354 GLY n 
1 355 ILE n 
1 356 ASN n 
1 357 TYR n 
1 358 GLN n 
1 359 PRO n 
1 360 PRO n 
1 361 THR n 
1 362 VAL n 
1 363 VAL n 
1 364 PRO n 
1 365 GLY n 
1 366 GLY n 
1 367 ASP n 
1 368 LEU n 
1 369 ALA n 
1 370 LYS n 
1 371 VAL n 
1 372 GLN n 
1 373 ARG n 
1 374 ALA n 
1 375 VAL n 
1 376 CYS n 
1 377 MET n 
1 378 LEU n 
1 379 SER n 
1 380 ASN n 
1 381 THR n 
1 382 THR n 
1 383 ALA n 
1 384 ILE n 
1 385 ALA n 
1 386 GLU n 
1 387 ALA n 
1 388 TRP n 
1 389 ALA n 
1 390 ARG n 
1 391 LEU n 
1 392 ASP n 
1 393 HIS n 
1 394 LYS n 
1 395 PHE n 
1 396 ASP n 
1 397 LEU n 
1 398 MET n 
1 399 TYR n 
1 400 ALA n 
1 401 LYS n 
1 402 ARG n 
1 403 ALA n 
1 404 PHE n 
1 405 VAL n 
1 406 HIS n 
1 407 TRP n 
1 408 TYR n 
1 409 VAL n 
1 410 GLY n 
1 411 GLU n 
1 412 GLY n 
1 413 MET n 
1 414 GLU n 
1 415 GLU n 
1 416 GLY n 
1 417 GLU n 
1 418 PHE n 
1 419 SER n 
1 420 GLU n 
1 421 ALA n 
1 422 ARG n 
1 423 GLU n 
1 424 ASP n 
1 425 MET n 
1 426 ALA n 
1 427 ALA n 
1 428 LEU n 
1 429 GLU n 
1 430 LYS n 
1 431 ASP n 
1 432 TYR n 
1 433 GLU n 
1 434 GLU n 
1 435 VAL n 
1 436 GLY n 
1 437 VAL n 
1 438 ASP n 
1 439 SER n 
1 440 VAL n 
1 441 GLU n 
1 442 GLY n 
1 443 GLU n 
1 444 GLY n 
1 445 GLU n 
1 446 GLU n 
1 447 GLU n 
1 448 GLY n 
1 449 GLU n 
1 450 GLU n 
2 1   MET n 
2 2   ARG n 
2 3   GLU n 
2 4   ILE n 
2 5   VAL n 
2 6   HIS n 
2 7   ILE n 
2 8   GLN n 
2 9   ALA n 
2 10  GLY n 
2 11  GLN n 
2 12  CYS n 
2 13  GLY n 
2 14  ASN n 
2 15  GLN n 
2 16  ILE n 
2 17  GLY n 
2 18  ALA n 
2 19  LYS n 
2 20  PHE n 
2 21  TRP n 
2 22  GLU n 
2 23  VAL n 
2 24  ILE n 
2 25  SER n 
2 26  ASP n 
2 27  GLU n 
2 28  HIS n 
2 29  GLY n 
2 30  ILE n 
2 31  ASP n 
2 32  PRO n 
2 33  THR n 
2 34  GLY n 
2 35  SER n 
2 36  TYR n 
2 37  HIS n 
2 38  GLY n 
2 39  ASP n 
2 40  SER n 
2 41  ASP n 
2 42  LEU n 
2 43  GLN n 
2 44  LEU n 
2 45  GLU n 
2 46  ARG n 
2 47  ILE n 
2 48  ASN n 
2 49  VAL n 
2 50  TYR n 
2 51  TYR n 
2 52  ASN n 
2 53  GLU n 
2 54  ALA n 
2 55  THR n 
2 56  GLY n 
2 57  ASN n 
2 58  LYS n 
2 59  TYR n 
2 60  VAL n 
2 61  PRO n 
2 62  ARG n 
2 63  ALA n 
2 64  ILE n 
2 65  LEU n 
2 66  VAL n 
2 67  ASP n 
2 68  LEU n 
2 69  GLU n 
2 70  PRO n 
2 71  GLY n 
2 72  THR n 
2 73  MET n 
2 74  ASP n 
2 75  SER n 
2 76  VAL n 
2 77  ARG n 
2 78  SER n 
2 79  GLY n 
2 80  PRO n 
2 81  PHE n 
2 82  GLY n 
2 83  GLN n 
2 84  ILE n 
2 85  PHE n 
2 86  ARG n 
2 87  PRO n 
2 88  ASP n 
2 89  ASN n 
2 90  PHE n 
2 91  VAL n 
2 92  PHE n 
2 93  GLY n 
2 94  GLN n 
2 95  SER n 
2 96  GLY n 
2 97  ALA n 
2 98  GLY n 
2 99  ASN n 
2 100 ASN n 
2 101 TRP n 
2 102 ALA n 
2 103 LYS n 
2 104 GLY n 
2 105 HIS n 
2 106 TYR n 
2 107 THR n 
2 108 GLU n 
2 109 GLY n 
2 110 ALA n 
2 111 GLU n 
2 112 LEU n 
2 113 VAL n 
2 114 ASP n 
2 115 SER n 
2 116 VAL n 
2 117 LEU n 
2 118 ASP n 
2 119 VAL n 
2 120 VAL n 
2 121 ARG n 
2 122 LYS n 
2 123 GLU n 
2 124 SER n 
2 125 GLU n 
2 126 SER n 
2 127 CYS n 
2 128 ASP n 
2 129 CYS n 
2 130 LEU n 
2 131 GLN n 
2 132 GLY n 
2 133 PHE n 
2 134 GLN n 
2 135 LEU n 
2 136 THR n 
2 137 HIS n 
2 138 SER n 
2 139 LEU n 
2 140 GLY n 
2 141 GLY n 
2 142 GLY n 
2 143 THR n 
2 144 GLY n 
2 145 SER n 
2 146 GLY n 
2 147 MET n 
2 148 GLY n 
2 149 THR n 
2 150 LEU n 
2 151 LEU n 
2 152 ILE n 
2 153 SER n 
2 154 LYS n 
2 155 ILE n 
2 156 ARG n 
2 157 GLU n 
2 158 GLU n 
2 159 TYR n 
2 160 PRO n 
2 161 ASP n 
2 162 ARG n 
2 163 ILE n 
2 164 MET n 
2 165 ASN n 
2 166 THR n 
2 167 PHE n 
2 168 SER n 
2 169 VAL n 
2 170 MET n 
2 171 PRO n 
2 172 SER n 
2 173 PRO n 
2 174 LYS n 
2 175 VAL n 
2 176 SER n 
2 177 ASP n 
2 178 THR n 
2 179 VAL n 
2 180 VAL n 
2 181 GLU n 
2 182 PRO n 
2 183 TYR n 
2 184 ASN n 
2 185 ALA n 
2 186 THR n 
2 187 LEU n 
2 188 SER n 
2 189 VAL n 
2 190 HIS n 
2 191 GLN n 
2 192 LEU n 
2 193 VAL n 
2 194 GLU n 
2 195 ASN n 
2 196 THR n 
2 197 ASP n 
2 198 GLU n 
2 199 THR n 
2 200 TYR n 
2 201 CYS n 
2 202 ILE n 
2 203 ASP n 
2 204 ASN n 
2 205 GLU n 
2 206 ALA n 
2 207 LEU n 
2 208 TYR n 
2 209 ASP n 
2 210 ILE n 
2 211 CYS n 
2 212 PHE n 
2 213 ARG n 
2 214 THR n 
2 215 LEU n 
2 216 LYS n 
2 217 LEU n 
2 218 THR n 
2 219 THR n 
2 220 PRO n 
2 221 THR n 
2 222 TYR n 
2 223 GLY n 
2 224 ASP n 
2 225 LEU n 
2 226 ASN n 
2 227 HIS n 
2 228 LEU n 
2 229 VAL n 
2 230 SER n 
2 231 ALA n 
2 232 THR n 
2 233 MET n 
2 234 SER n 
2 235 GLY n 
2 236 VAL n 
2 237 THR n 
2 238 THR n 
2 239 CYS n 
2 240 LEU n 
2 241 ARG n 
2 242 PHE n 
2 243 PRO n 
2 244 GLY n 
2 245 GLN n 
2 246 LEU n 
2 247 ASN n 
2 248 ALA n 
2 249 ASP n 
2 250 LEU n 
2 251 ARG n 
2 252 LYS n 
2 253 LEU n 
2 254 ALA n 
2 255 VAL n 
2 256 ASN n 
2 257 MET n 
2 258 VAL n 
2 259 PRO n 
2 260 PHE n 
2 261 PRO n 
2 262 ARG n 
2 263 LEU n 
2 264 HIS n 
2 265 PHE n 
2 266 PHE n 
2 267 MET n 
2 268 PRO n 
2 269 GLY n 
2 270 PHE n 
2 271 ALA n 
2 272 PRO n 
2 273 LEU n 
2 274 THR n 
2 275 SER n 
2 276 ARG n 
2 277 GLY n 
2 278 SER n 
2 279 GLN n 
2 280 GLN n 
2 281 TYR n 
2 282 ARG n 
2 283 ALA n 
2 284 LEU n 
2 285 THR n 
2 286 VAL n 
2 287 PRO n 
2 288 GLU n 
2 289 LEU n 
2 290 THR n 
2 291 GLN n 
2 292 GLN n 
2 293 MET n 
2 294 PHE n 
2 295 ASP n 
2 296 SER n 
2 297 LYS n 
2 298 ASN n 
2 299 MET n 
2 300 MET n 
2 301 ALA n 
2 302 ALA n 
2 303 CYS n 
2 304 ASP n 
2 305 PRO n 
2 306 ARG n 
2 307 HIS n 
2 308 GLY n 
2 309 ARG n 
2 310 TYR n 
2 311 LEU n 
2 312 THR n 
2 313 VAL n 
2 314 ALA n 
2 315 ALA n 
2 316 ILE n 
2 317 PHE n 
2 318 ARG n 
2 319 GLY n 
2 320 ARG n 
2 321 MET n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLU n 
2 326 VAL n 
2 327 ASP n 
2 328 GLU n 
2 329 GLN n 
2 330 MET n 
2 331 LEU n 
2 332 ASN n 
2 333 VAL n 
2 334 GLN n 
2 335 ASN n 
2 336 LYS n 
2 337 ASN n 
2 338 SER n 
2 339 SER n 
2 340 TYR n 
2 341 PHE n 
2 342 VAL n 
2 343 GLU n 
2 344 TRP n 
2 345 ILE n 
2 346 PRO n 
2 347 ASN n 
2 348 ASN n 
2 349 VAL n 
2 350 LYS n 
2 351 THR n 
2 352 ALA n 
2 353 VAL n 
2 354 CYS n 
2 355 ASP n 
2 356 ILE n 
2 357 PRO n 
2 358 PRO n 
2 359 ARG n 
2 360 GLY n 
2 361 LEU n 
2 362 LYS n 
2 363 MET n 
2 364 SER n 
2 365 ALA n 
2 366 THR n 
2 367 PHE n 
2 368 ILE n 
2 369 GLY n 
2 370 ASN n 
2 371 SER n 
2 372 THR n 
2 373 ALA n 
2 374 ILE n 
2 375 GLN n 
2 376 GLU n 
2 377 LEU n 
2 378 PHE n 
2 379 LYS n 
2 380 ARG n 
2 381 ILE n 
2 382 SER n 
2 383 GLU n 
2 384 GLN n 
2 385 PHE n 
2 386 THR n 
2 387 ALA n 
2 388 MET n 
2 389 PHE n 
2 390 ARG n 
2 391 ARG n 
2 392 LYS n 
2 393 ALA n 
2 394 PHE n 
2 395 LEU n 
2 396 HIS n 
2 397 TRP n 
2 398 TYR n 
2 399 THR n 
2 400 GLY n 
2 401 GLU n 
2 402 GLY n 
2 403 MET n 
2 404 ASP n 
2 405 GLU n 
2 406 MET n 
2 407 GLU n 
2 408 PHE n 
2 409 THR n 
2 410 GLU n 
2 411 ALA n 
2 412 GLU n 
2 413 SER n 
2 414 ASN n 
2 415 MET n 
2 416 ASN n 
2 417 ASP n 
2 418 LEU n 
2 419 VAL n 
2 420 SER n 
2 421 GLU n 
2 422 TYR n 
2 423 GLN n 
2 424 GLN n 
2 425 TYR n 
2 426 GLN n 
2 427 ASP n 
2 428 ALA n 
2 429 THR n 
2 430 ALA n 
2 431 ASP n 
2 432 GLU n 
2 433 GLN n 
2 434 GLY n 
2 435 GLU n 
2 436 PHE n 
2 437 GLU n 
2 438 GLU n 
2 439 GLU n 
2 440 GLU n 
2 441 GLY n 
2 442 GLU n 
2 443 ASP n 
2 444 GLU n 
2 445 ALA n 
3 1   MET n 
3 2   ALA n 
3 3   ASP n 
3 4   MET n 
3 5   GLU n 
3 6   VAL n 
3 7   ILE n 
3 8   GLU n 
3 9   LEU n 
3 10  ASN n 
3 11  LYS n 
3 12  CYS n 
3 13  THR n 
3 14  SER n 
3 15  GLY n 
3 16  GLN n 
3 17  SER n 
3 18  PHE n 
3 19  GLU n 
3 20  VAL n 
3 21  ILE n 
3 22  LEU n 
3 23  LYS n 
3 24  PRO n 
3 25  PRO n 
3 26  SER n 
3 27  PHE n 
3 28  ASP n 
3 29  GLY n 
3 30  VAL n 
3 31  PRO n 
3 32  GLU n 
3 33  PHE n 
3 34  ASN n 
3 35  ALA n 
3 36  SER n 
3 37  LEU n 
3 38  PRO n 
3 39  ARG n 
3 40  ARG n 
3 41  ARG n 
3 42  ASP n 
3 43  PRO n 
3 44  SER n 
3 45  LEU n 
3 46  GLU n 
3 47  GLU n 
3 48  ILE n 
3 49  GLN n 
3 50  LYS n 
3 51  LYS n 
3 52  LEU n 
3 53  GLU n 
3 54  ALA n 
3 55  ALA n 
3 56  GLU n 
3 57  GLU n 
3 58  ARG n 
3 59  ARG n 
3 60  LYS n 
3 61  TYR n 
3 62  GLN n 
3 63  GLU n 
3 64  ALA n 
3 65  GLU n 
3 66  LEU n 
3 67  LEU n 
3 68  LYS n 
3 69  HIS n 
3 70  LEU n 
3 71  ALA n 
3 72  GLU n 
3 73  LYS n 
3 74  ARG n 
3 75  GLU n 
3 76  HIS n 
3 77  GLU n 
3 78  ARG n 
3 79  GLU n 
3 80  VAL n 
3 81  ILE n 
3 82  GLN n 
3 83  LYS n 
3 84  ALA n 
3 85  ILE n 
3 86  GLU n 
3 87  GLU n 
3 88  ASN n 
3 89  ASN n 
3 90  ASN n 
3 91  PHE n 
3 92  ILE n 
3 93  LYS n 
3 94  MET n 
3 95  ALA n 
3 96  LYS n 
3 97  GLU n 
3 98  LYS n 
3 99  LEU n 
3 100 ALA n 
3 101 GLN n 
3 102 LYS n 
3 103 MET n 
3 104 GLU n 
3 105 SER n 
3 106 ASN n 
3 107 LYS n 
3 108 GLU n 
3 109 ASN n 
3 110 ARG n 
3 111 GLU n 
3 112 ALA n 
3 113 HIS n 
3 114 LEU n 
3 115 ALA n 
3 116 ALA n 
3 117 MET n 
3 118 LEU n 
3 119 GLU n 
3 120 ARG n 
3 121 LEU n 
3 122 GLN n 
3 123 GLU n 
3 124 LYS n 
3 125 ASP n 
3 126 LYS n 
3 127 HIS n 
3 128 ALA n 
3 129 GLU n 
3 130 GLU n 
3 131 VAL n 
3 132 ARG n 
3 133 LYS n 
3 134 ASN n 
3 135 LYS n 
3 136 GLU n 
3 137 LEU n 
3 138 LYS n 
3 139 GLU n 
3 140 GLU n 
3 141 ALA n 
3 142 SER n 
3 143 ARG n 
4 1   MET n 
4 2   TYR n 
4 3   THR n 
4 4   PHE n 
4 5   VAL n 
4 6   VAL n 
4 7   ARG n 
4 8   ASP n 
4 9   GLU n 
4 10  ASN n 
4 11  SER n 
4 12  SER n 
4 13  VAL n 
4 14  TYR n 
4 15  ALA n 
4 16  GLU n 
4 17  VAL n 
4 18  SER n 
4 19  ARG n 
4 20  LEU n 
4 21  LEU n 
4 22  LEU n 
4 23  ALA n 
4 24  THR n 
4 25  GLY n 
4 26  GLN n 
4 27  TRP n 
4 28  LYS n 
4 29  ARG n 
4 30  LEU n 
4 31  ARG n 
4 32  LYS n 
4 33  ASP n 
4 34  ASN n 
4 35  PRO n 
4 36  ARG n 
4 37  PHE n 
4 38  ASN n 
4 39  LEU n 
4 40  MET n 
4 41  LEU n 
4 42  GLY n 
4 43  GLU n 
4 44  ARG n 
4 45  ASN n 
4 46  ARG n 
4 47  LEU n 
4 48  PRO n 
4 49  PHE n 
4 50  GLY n 
4 51  ARG n 
4 52  LEU n 
4 53  GLY n 
4 54  HIS n 
4 55  GLU n 
4 56  PRO n 
4 57  GLY n 
4 58  LEU n 
4 59  VAL n 
4 60  GLN n 
4 61  LEU n 
4 62  VAL n 
4 63  ASN n 
4 64  TYR n 
4 65  TYR n 
4 66  ARG n 
4 67  GLY n 
4 68  ALA n 
4 69  ASP n 
4 70  LYS n 
4 71  LEU n 
4 72  CYS n 
4 73  ARG n 
4 74  LYS n 
4 75  ALA n 
4 76  SER n 
4 77  LEU n 
4 78  VAL n 
4 79  LYS n 
4 80  LEU n 
4 81  ILE n 
4 82  LYS n 
4 83  THR n 
4 84  SER n 
4 85  PRO n 
4 86  GLU n 
4 87  LEU n 
4 88  SER n 
4 89  GLU n 
4 90  SER n 
4 91  CYS n 
4 92  THR n 
4 93  TRP n 
4 94  PHE n 
4 95  PRO n 
4 96  GLU n 
4 97  SER n 
4 98  TYR n 
4 99  VAL n 
4 100 ILE n 
4 101 TYR n 
4 102 PRO n 
4 103 THR n 
4 104 ASN n 
4 105 LEU n 
4 106 LYS n 
4 107 THR n 
4 108 PRO n 
4 109 VAL n 
4 110 ALA n 
4 111 PRO n 
4 112 ALA n 
4 113 GLN n 
4 114 ASN n 
4 115 GLY n 
4 116 ILE n 
4 117 ARG n 
4 118 HIS n 
4 119 LEU n 
4 120 ILE n 
4 121 ASN n 
4 122 ASN n 
4 123 THR n 
4 124 ARG n 
4 125 THR n 
4 126 ASP n 
4 127 GLU n 
4 128 ARG n 
4 129 GLU n 
4 130 VAL n 
4 131 PHE n 
4 132 LEU n 
4 133 ALA n 
4 134 ALA n 
4 135 TYR n 
4 136 ASN n 
4 137 ARG n 
4 138 ARG n 
4 139 ARG n 
4 140 GLU n 
4 141 GLY n 
4 142 ARG n 
4 143 GLU n 
4 144 GLY n 
4 145 ASN n 
4 146 VAL n 
4 147 TRP n 
4 148 ILE n 
4 149 ALA n 
4 150 LYS n 
4 151 SER n 
4 152 SER n 
4 153 ALA n 
4 154 GLY n 
4 155 ALA n 
4 156 LYS n 
4 157 GLY n 
4 158 GLU n 
4 159 GLY n 
4 160 ILE n 
4 161 LEU n 
4 162 ILE n 
4 163 SER n 
4 164 SER n 
4 165 GLU n 
4 166 ALA n 
4 167 SER n 
4 168 GLU n 
4 169 LEU n 
4 170 LEU n 
4 171 ASP n 
4 172 PHE n 
4 173 ILE n 
4 174 ASP n 
4 175 GLU n 
4 176 GLN n 
4 177 GLY n 
4 178 GLN n 
4 179 VAL n 
4 180 HIS n 
4 181 VAL n 
4 182 ILE n 
4 183 GLN n 
4 184 LYS n 
4 185 TYR n 
4 186 LEU n 
4 187 GLU n 
4 188 LYS n 
4 189 PRO n 
4 190 LEU n 
4 191 LEU n 
4 192 LEU n 
4 193 GLU n 
4 194 PRO n 
4 195 GLY n 
4 196 HIS n 
4 197 ARG n 
4 198 LYS n 
4 199 PHE n 
4 200 ASP n 
4 201 ILE n 
4 202 ARG n 
4 203 SER n 
4 204 TRP n 
4 205 VAL n 
4 206 LEU n 
4 207 VAL n 
4 208 ASP n 
4 209 HIS n 
4 210 LEU n 
4 211 TYR n 
4 212 ASN n 
4 213 ILE n 
4 214 TYR n 
4 215 LEU n 
4 216 TYR n 
4 217 ARG n 
4 218 GLU n 
4 219 GLY n 
4 220 VAL n 
4 221 LEU n 
4 222 ARG n 
4 223 THR n 
4 224 SER n 
4 225 SER n 
4 226 GLU n 
4 227 PRO n 
4 228 TYR n 
4 229 ASN n 
4 230 SER n 
4 231 ALA n 
4 232 ASN n 
4 233 PHE n 
4 234 GLN n 
4 235 ASP n 
4 236 LYS n 
4 237 THR n 
4 238 CYS n 
4 239 HIS n 
4 240 LEU n 
4 241 THR n 
4 242 ASN n 
4 243 HIS n 
4 244 CYS n 
4 245 ILE n 
4 246 GLN n 
4 247 LYS n 
4 248 GLU n 
4 249 TYR n 
4 250 SER n 
4 251 LYS n 
4 252 ASN n 
4 253 TYR n 
4 254 GLY n 
4 255 ARG n 
4 256 TYR n 
4 257 GLU n 
4 258 GLU n 
4 259 GLY n 
4 260 ASN n 
4 261 GLU n 
4 262 MET n 
4 263 PHE n 
4 264 PHE n 
4 265 GLU n 
4 266 GLU n 
4 267 PHE n 
4 268 ASN n 
4 269 GLN n 
4 270 TYR n 
4 271 LEU n 
4 272 MET n 
4 273 ASP n 
4 274 ALA n 
4 275 LEU n 
4 276 ASN n 
4 277 THR n 
4 278 THR n 
4 279 LEU n 
4 280 GLU n 
4 281 ASN n 
4 282 SER n 
4 283 ILE n 
4 284 LEU n 
4 285 LEU n 
4 286 GLN n 
4 287 ILE n 
4 288 LYS n 
4 289 HIS n 
4 290 ILE n 
4 291 ILE n 
4 292 ARG n 
4 293 SER n 
4 294 CYS n 
4 295 LEU n 
4 296 MET n 
4 297 CYS n 
4 298 ILE n 
4 299 GLU n 
4 300 PRO n 
4 301 ALA n 
4 302 ILE n 
4 303 SER n 
4 304 THR n 
4 305 LYS n 
4 306 HIS n 
4 307 LEU n 
4 308 HIS n 
4 309 TYR n 
4 310 GLN n 
4 311 SER n 
4 312 PHE n 
4 313 GLN n 
4 314 LEU n 
4 315 PHE n 
4 316 GLY n 
4 317 PHE n 
4 318 ASP n 
4 319 PHE n 
4 320 MET n 
4 321 VAL n 
4 322 ASP n 
4 323 GLU n 
4 324 GLU n 
4 325 LEU n 
4 326 LYS n 
4 327 VAL n 
4 328 TRP n 
4 329 LEU n 
4 330 ILE n 
4 331 GLU n 
4 332 VAL n 
4 333 ASN n 
4 334 GLY n 
4 335 ALA n 
4 336 PRO n 
4 337 ALA n 
4 338 CYS n 
4 339 ALA n 
4 340 GLN n 
4 341 LYS n 
4 342 LEU n 
4 343 TYR n 
4 344 ALA n 
4 345 GLU n 
4 346 LEU n 
4 347 CYS n 
4 348 GLN n 
4 349 GLY n 
4 350 ILE n 
4 351 VAL n 
4 352 ASP n 
4 353 VAL n 
4 354 ALA n 
4 355 ILE n 
4 356 SER n 
4 357 SER n 
4 358 VAL n 
4 359 PHE n 
4 360 PRO n 
4 361 LEU n 
4 362 ALA n 
4 363 ASP n 
4 364 THR n 
4 365 GLY n 
4 366 GLN n 
4 367 LYS n 
4 368 THR n 
4 369 SER n 
4 370 GLN n 
4 371 PRO n 
4 372 THR n 
4 373 SER n 
4 374 ILE n 
4 375 PHE n 
4 376 ILE n 
4 377 LYS n 
4 378 LEU n 
4 379 HIS n 
4 380 HIS n 
4 381 HIS n 
4 382 HIS n 
4 383 HIS n 
4 384 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 450 pig           ? TUBA1B                 ? ? ? ? ? ? 'Sus scrofa'    9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 445 pig           ? 'TUBB2B, LOC100624785' ? ? ? ? ? ? 'Sus scrofa'    9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 143 'house mouse' ? Stmn4                  ? ? ? ? ? ? 'Mus musculus'  10090 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 384 chicken       ? TTL                    ? ? ? ? ? ? 'Gallus gallus' 9031  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EPR non-polymer         . "10'-fluorovinblastine"     ? 'C46 H57 F N4 O9'   828.965 
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 
CA    non-polymer         . 'CALCIUM ION'               ? 'Ca 2'              40.078  
CYS   'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GDP   'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
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  
GTP   non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
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 
MG    non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE   'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   CYS 4   4   4   CYS CYS A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  TRP 21  21  21  TRP TRP A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  HIS 61  61  61  HIS HIS A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  GLN 85  85  85  GLN GLN A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 CYS 200 200 200 CYS CYS A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 CYS 213 213 213 CYS CYS A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 ARG 264 264 264 ARG ARG A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 PRO 268 268 268 PRO PRO A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ILE 276 276 276 ILE ILE A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 GLN 285 285 285 GLN GLN A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 CYS 295 295 295 CYS CYS A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 GLU 297 297 297 GLU GLU A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 GLN 301 301 301 GLN GLN A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 CYS 305 305 305 CYS CYS A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 MET 313 313 313 MET MET A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 CYS 315 315 315 CYS CYS A . n 
A 1 316 CYS 316 316 316 CYS CYS A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 ARG 320 320 320 ARG ARG A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 GLN 342 342 342 GLN GLN A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 TRP 346 346 346 TRP TRP A . n 
A 1 347 CYS 347 347 347 CYS CYS A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 PRO 360 360 360 PRO PRO A . n 
A 1 361 THR 361 361 361 THR THR A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 ARG 373 373 373 ARG ARG A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 CYS 376 376 376 CYS CYS A . n 
A 1 377 MET 377 377 377 MET MET A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 THR 381 381 381 THR THR A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 TRP 388 388 388 TRP TRP A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 ARG 390 390 390 ARG ARG A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 LYS 401 401 401 LYS LYS A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 ALA 403 403 403 ALA ALA A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 VAL 405 405 405 VAL VAL A . n 
A 1 406 HIS 406 406 406 HIS HIS A . n 
A 1 407 TRP 407 407 407 TRP TRP A . n 
A 1 408 TYR 408 408 408 TYR TYR A . n 
A 1 409 VAL 409 409 409 VAL VAL A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 MET 413 413 413 MET MET A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 GLU 417 417 417 GLU GLU A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 SER 419 419 419 SER SER A . n 
A 1 420 GLU 420 420 420 GLU GLU A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 ARG 422 422 422 ARG ARG A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 MET 425 425 425 MET MET A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 TYR 432 432 432 TYR TYR A . n 
A 1 433 GLU 433 433 433 GLU GLU A . n 
A 1 434 GLU 434 434 434 GLU GLU A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 SER 439 439 439 SER SER A . n 
A 1 440 VAL 440 440 ?   ?   ?   A . n 
A 1 441 GLU 441 441 ?   ?   ?   A . n 
A 1 442 GLY 442 442 ?   ?   ?   A . n 
A 1 443 GLU 443 443 ?   ?   ?   A . n 
A 1 444 GLY 444 444 ?   ?   ?   A . n 
A 1 445 GLU 445 445 ?   ?   ?   A . n 
A 1 446 GLU 446 446 ?   ?   ?   A . n 
A 1 447 GLU 447 447 ?   ?   ?   A . n 
A 1 448 GLY 448 448 ?   ?   ?   A . n 
A 1 449 GLU 449 449 ?   ?   ?   A . n 
A 1 450 GLU 450 450 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET C . n 
B 1 2   ARG 2   2   2   ARG ARG C . n 
B 1 3   GLU 3   3   3   GLU GLU C . n 
B 1 4   CYS 4   4   4   CYS CYS C . n 
B 1 5   ILE 5   5   5   ILE ILE C . n 
B 1 6   SER 6   6   6   SER SER C . n 
B 1 7   ILE 7   7   7   ILE ILE C . n 
B 1 8   HIS 8   8   8   HIS HIS C . n 
B 1 9   VAL 9   9   9   VAL VAL C . n 
B 1 10  GLY 10  10  10  GLY GLY C . n 
B 1 11  GLN 11  11  11  GLN GLN C . n 
B 1 12  ALA 12  12  12  ALA ALA C . n 
B 1 13  GLY 13  13  13  GLY GLY C . n 
B 1 14  VAL 14  14  14  VAL VAL C . n 
B 1 15  GLN 15  15  15  GLN GLN C . n 
B 1 16  ILE 16  16  16  ILE ILE C . n 
B 1 17  GLY 17  17  17  GLY GLY C . n 
B 1 18  ASN 18  18  18  ASN ASN C . n 
B 1 19  ALA 19  19  19  ALA ALA C . n 
B 1 20  CYS 20  20  20  CYS CYS C . n 
B 1 21  TRP 21  21  21  TRP TRP C . n 
B 1 22  GLU 22  22  22  GLU GLU C . n 
B 1 23  LEU 23  23  23  LEU LEU C . n 
B 1 24  TYR 24  24  24  TYR TYR C . n 
B 1 25  CYS 25  25  25  CYS CYS C . n 
B 1 26  LEU 26  26  26  LEU LEU C . n 
B 1 27  GLU 27  27  27  GLU GLU C . n 
B 1 28  HIS 28  28  28  HIS HIS C . n 
B 1 29  GLY 29  29  29  GLY GLY C . n 
B 1 30  ILE 30  30  30  ILE ILE C . n 
B 1 31  GLN 31  31  31  GLN GLN C . n 
B 1 32  PRO 32  32  32  PRO PRO C . n 
B 1 33  ASP 33  33  33  ASP ASP C . n 
B 1 34  GLY 34  34  34  GLY GLY C . n 
B 1 35  GLN 35  35  35  GLN GLN C . n 
B 1 36  MET 36  36  36  MET MET C . n 
B 1 37  PRO 37  37  37  PRO PRO C . n 
B 1 38  SER 38  38  38  SER SER C . n 
B 1 39  ASP 39  39  39  ASP ASP C . n 
B 1 40  LYS 40  40  40  LYS LYS C . n 
B 1 41  THR 41  41  41  THR THR C . n 
B 1 42  ILE 42  42  42  ILE ILE C . n 
B 1 43  GLY 43  43  43  GLY GLY C . n 
B 1 44  GLY 44  44  44  GLY GLY C . n 
B 1 45  GLY 45  45  45  GLY GLY C . n 
B 1 46  ASP 46  46  46  ASP ASP C . n 
B 1 47  ASP 47  47  47  ASP ASP C . n 
B 1 48  SER 48  48  48  SER SER C . n 
B 1 49  PHE 49  49  49  PHE PHE C . n 
B 1 50  ASN 50  50  50  ASN ASN C . n 
B 1 51  THR 51  51  51  THR THR C . n 
B 1 52  PHE 52  52  52  PHE PHE C . n 
B 1 53  PHE 53  53  53  PHE PHE C . n 
B 1 54  SER 54  54  54  SER SER C . n 
B 1 55  GLU 55  55  55  GLU GLU C . n 
B 1 56  THR 56  56  56  THR THR C . n 
B 1 57  GLY 57  57  57  GLY GLY C . n 
B 1 58  ALA 58  58  58  ALA ALA C . n 
B 1 59  GLY 59  59  59  GLY GLY C . n 
B 1 60  LYS 60  60  60  LYS LYS C . n 
B 1 61  HIS 61  61  61  HIS HIS C . n 
B 1 62  VAL 62  62  62  VAL VAL C . n 
B 1 63  PRO 63  63  63  PRO PRO C . n 
B 1 64  ARG 64  64  64  ARG ARG C . n 
B 1 65  ALA 65  65  65  ALA ALA C . n 
B 1 66  VAL 66  66  66  VAL VAL C . n 
B 1 67  PHE 67  67  67  PHE PHE C . n 
B 1 68  VAL 68  68  68  VAL VAL C . n 
B 1 69  ASP 69  69  69  ASP ASP C . n 
B 1 70  LEU 70  70  70  LEU LEU C . n 
B 1 71  GLU 71  71  71  GLU GLU C . n 
B 1 72  PRO 72  72  72  PRO PRO C . n 
B 1 73  THR 73  73  73  THR THR C . n 
B 1 74  VAL 74  74  74  VAL VAL C . n 
B 1 75  ILE 75  75  75  ILE ILE C . n 
B 1 76  ASP 76  76  76  ASP ASP C . n 
B 1 77  GLU 77  77  77  GLU GLU C . n 
B 1 78  VAL 78  78  78  VAL VAL C . n 
B 1 79  ARG 79  79  79  ARG ARG C . n 
B 1 80  THR 80  80  80  THR THR C . n 
B 1 81  GLY 81  81  81  GLY GLY C . n 
B 1 82  THR 82  82  82  THR THR C . n 
B 1 83  TYR 83  83  83  TYR TYR C . n 
B 1 84  ARG 84  84  84  ARG ARG C . n 
B 1 85  GLN 85  85  85  GLN GLN C . n 
B 1 86  LEU 86  86  86  LEU LEU C . n 
B 1 87  PHE 87  87  87  PHE PHE C . n 
B 1 88  HIS 88  88  88  HIS HIS C . n 
B 1 89  PRO 89  89  89  PRO PRO C . n 
B 1 90  GLU 90  90  90  GLU GLU C . n 
B 1 91  GLN 91  91  91  GLN GLN C . n 
B 1 92  LEU 92  92  92  LEU LEU C . n 
B 1 93  ILE 93  93  93  ILE ILE C . n 
B 1 94  THR 94  94  94  THR THR C . n 
B 1 95  GLY 95  95  95  GLY GLY C . n 
B 1 96  LYS 96  96  96  LYS LYS C . n 
B 1 97  GLU 97  97  97  GLU GLU C . n 
B 1 98  ASP 98  98  98  ASP ASP C . n 
B 1 99  ALA 99  99  99  ALA ALA C . n 
B 1 100 ALA 100 100 100 ALA ALA C . n 
B 1 101 ASN 101 101 101 ASN ASN C . n 
B 1 102 ASN 102 102 102 ASN ASN C . n 
B 1 103 TYR 103 103 103 TYR TYR C . n 
B 1 104 ALA 104 104 104 ALA ALA C . n 
B 1 105 ARG 105 105 105 ARG ARG C . n 
B 1 106 GLY 106 106 106 GLY GLY C . n 
B 1 107 HIS 107 107 107 HIS HIS C . n 
B 1 108 TYR 108 108 108 TYR TYR C . n 
B 1 109 THR 109 109 109 THR THR C . n 
B 1 110 ILE 110 110 110 ILE ILE C . n 
B 1 111 GLY 111 111 111 GLY GLY C . n 
B 1 112 LYS 112 112 112 LYS LYS C . n 
B 1 113 GLU 113 113 113 GLU GLU C . n 
B 1 114 ILE 114 114 114 ILE ILE C . n 
B 1 115 ILE 115 115 115 ILE ILE C . n 
B 1 116 ASP 116 116 116 ASP ASP C . n 
B 1 117 LEU 117 117 117 LEU LEU C . n 
B 1 118 VAL 118 118 118 VAL VAL C . n 
B 1 119 LEU 119 119 119 LEU LEU C . n 
B 1 120 ASP 120 120 120 ASP ASP C . n 
B 1 121 ARG 121 121 121 ARG ARG C . n 
B 1 122 ILE 122 122 122 ILE ILE C . n 
B 1 123 ARG 123 123 123 ARG ARG C . n 
B 1 124 LYS 124 124 124 LYS LYS C . n 
B 1 125 LEU 125 125 125 LEU LEU C . n 
B 1 126 ALA 126 126 126 ALA ALA C . n 
B 1 127 ASP 127 127 127 ASP ASP C . n 
B 1 128 GLN 128 128 128 GLN GLN C . n 
B 1 129 CYS 129 129 129 CYS CYS C . n 
B 1 130 THR 130 130 130 THR THR C . n 
B 1 131 GLY 131 131 131 GLY GLY C . n 
B 1 132 LEU 132 132 132 LEU LEU C . n 
B 1 133 GLN 133 133 133 GLN GLN C . n 
B 1 134 GLY 134 134 134 GLY GLY C . n 
B 1 135 PHE 135 135 135 PHE PHE C . n 
B 1 136 LEU 136 136 136 LEU LEU C . n 
B 1 137 VAL 137 137 137 VAL VAL C . n 
B 1 138 PHE 138 138 138 PHE PHE C . n 
B 1 139 HIS 139 139 139 HIS HIS C . n 
B 1 140 SER 140 140 140 SER SER C . n 
B 1 141 PHE 141 141 141 PHE PHE C . n 
B 1 142 GLY 142 142 142 GLY GLY C . n 
B 1 143 GLY 143 143 143 GLY GLY C . n 
B 1 144 GLY 144 144 144 GLY GLY C . n 
B 1 145 THR 145 145 145 THR THR C . n 
B 1 146 GLY 146 146 146 GLY GLY C . n 
B 1 147 SER 147 147 147 SER SER C . n 
B 1 148 GLY 148 148 148 GLY GLY C . n 
B 1 149 PHE 149 149 149 PHE PHE C . n 
B 1 150 THR 150 150 150 THR THR C . n 
B 1 151 SER 151 151 151 SER SER C . n 
B 1 152 LEU 152 152 152 LEU LEU C . n 
B 1 153 LEU 153 153 153 LEU LEU C . n 
B 1 154 MET 154 154 154 MET MET C . n 
B 1 155 GLU 155 155 155 GLU GLU C . n 
B 1 156 ARG 156 156 156 ARG ARG C . n 
B 1 157 LEU 157 157 157 LEU LEU C . n 
B 1 158 SER 158 158 158 SER SER C . n 
B 1 159 VAL 159 159 159 VAL VAL C . n 
B 1 160 ASP 160 160 160 ASP ASP C . n 
B 1 161 TYR 161 161 161 TYR TYR C . n 
B 1 162 GLY 162 162 162 GLY GLY C . n 
B 1 163 LYS 163 163 163 LYS LYS C . n 
B 1 164 LYS 164 164 164 LYS LYS C . n 
B 1 165 SER 165 165 165 SER SER C . n 
B 1 166 LYS 166 166 166 LYS LYS C . n 
B 1 167 LEU 167 167 167 LEU LEU C . n 
B 1 168 GLU 168 168 168 GLU GLU C . n 
B 1 169 PHE 169 169 169 PHE PHE C . n 
B 1 170 SER 170 170 170 SER SER C . n 
B 1 171 ILE 171 171 171 ILE ILE C . n 
B 1 172 TYR 172 172 172 TYR TYR C . n 
B 1 173 PRO 173 173 173 PRO PRO C . n 
B 1 174 ALA 174 174 174 ALA ALA C . n 
B 1 175 PRO 175 175 175 PRO PRO C . n 
B 1 176 GLN 176 176 176 GLN GLN C . n 
B 1 177 VAL 177 177 177 VAL VAL C . n 
B 1 178 SER 178 178 178 SER SER C . n 
B 1 179 THR 179 179 179 THR THR C . n 
B 1 180 ALA 180 180 180 ALA ALA C . n 
B 1 181 VAL 181 181 181 VAL VAL C . n 
B 1 182 VAL 182 182 182 VAL VAL C . n 
B 1 183 GLU 183 183 183 GLU GLU C . n 
B 1 184 PRO 184 184 184 PRO PRO C . n 
B 1 185 TYR 185 185 185 TYR TYR C . n 
B 1 186 ASN 186 186 186 ASN ASN C . n 
B 1 187 SER 187 187 187 SER SER C . n 
B 1 188 ILE 188 188 188 ILE ILE C . n 
B 1 189 LEU 189 189 189 LEU LEU C . n 
B 1 190 THR 190 190 190 THR THR C . n 
B 1 191 THR 191 191 191 THR THR C . n 
B 1 192 HIS 192 192 192 HIS HIS C . n 
B 1 193 THR 193 193 193 THR THR C . n 
B 1 194 THR 194 194 194 THR THR C . n 
B 1 195 LEU 195 195 195 LEU LEU C . n 
B 1 196 GLU 196 196 196 GLU GLU C . n 
B 1 197 HIS 197 197 197 HIS HIS C . n 
B 1 198 SER 198 198 198 SER SER C . n 
B 1 199 ASP 199 199 199 ASP ASP C . n 
B 1 200 CYS 200 200 200 CYS CYS C . n 
B 1 201 ALA 201 201 201 ALA ALA C . n 
B 1 202 PHE 202 202 202 PHE PHE C . n 
B 1 203 MET 203 203 203 MET MET C . n 
B 1 204 VAL 204 204 204 VAL VAL C . n 
B 1 205 ASP 205 205 205 ASP ASP C . n 
B 1 206 ASN 206 206 206 ASN ASN C . n 
B 1 207 GLU 207 207 207 GLU GLU C . n 
B 1 208 ALA 208 208 208 ALA ALA C . n 
B 1 209 ILE 209 209 209 ILE ILE C . n 
B 1 210 TYR 210 210 210 TYR TYR C . n 
B 1 211 ASP 211 211 211 ASP ASP C . n 
B 1 212 ILE 212 212 212 ILE ILE C . n 
B 1 213 CYS 213 213 213 CYS CYS C . n 
B 1 214 ARG 214 214 214 ARG ARG C . n 
B 1 215 ARG 215 215 215 ARG ARG C . n 
B 1 216 ASN 216 216 216 ASN ASN C . n 
B 1 217 LEU 217 217 217 LEU LEU C . n 
B 1 218 ASP 218 218 218 ASP ASP C . n 
B 1 219 ILE 219 219 219 ILE ILE C . n 
B 1 220 GLU 220 220 220 GLU GLU C . n 
B 1 221 ARG 221 221 221 ARG ARG C . n 
B 1 222 PRO 222 222 222 PRO PRO C . n 
B 1 223 THR 223 223 223 THR THR C . n 
B 1 224 TYR 224 224 224 TYR TYR C . n 
B 1 225 THR 225 225 225 THR THR C . n 
B 1 226 ASN 226 226 226 ASN ASN C . n 
B 1 227 LEU 227 227 227 LEU LEU C . n 
B 1 228 ASN 228 228 228 ASN ASN C . n 
B 1 229 ARG 229 229 229 ARG ARG C . n 
B 1 230 LEU 230 230 230 LEU LEU C . n 
B 1 231 ILE 231 231 231 ILE ILE C . n 
B 1 232 SER 232 232 232 SER SER C . n 
B 1 233 GLN 233 233 233 GLN GLN C . n 
B 1 234 ILE 234 234 234 ILE ILE C . n 
B 1 235 VAL 235 235 235 VAL VAL C . n 
B 1 236 SER 236 236 236 SER SER C . n 
B 1 237 SER 237 237 237 SER SER C . n 
B 1 238 ILE 238 238 238 ILE ILE C . n 
B 1 239 THR 239 239 239 THR THR C . n 
B 1 240 ALA 240 240 240 ALA ALA C . n 
B 1 241 SER 241 241 241 SER SER C . n 
B 1 242 LEU 242 242 242 LEU LEU C . n 
B 1 243 ARG 243 243 243 ARG ARG C . n 
B 1 244 PHE 244 244 244 PHE PHE C . n 
B 1 245 ASP 245 245 245 ASP ASP C . n 
B 1 246 GLY 246 246 246 GLY GLY C . n 
B 1 247 ALA 247 247 247 ALA ALA C . n 
B 1 248 LEU 248 248 248 LEU LEU C . n 
B 1 249 ASN 249 249 249 ASN ASN C . n 
B 1 250 VAL 250 250 250 VAL VAL C . n 
B 1 251 ASP 251 251 251 ASP ASP C . n 
B 1 252 LEU 252 252 252 LEU LEU C . n 
B 1 253 THR 253 253 253 THR THR C . n 
B 1 254 GLU 254 254 254 GLU GLU C . n 
B 1 255 PHE 255 255 255 PHE PHE C . n 
B 1 256 GLN 256 256 256 GLN GLN C . n 
B 1 257 THR 257 257 257 THR THR C . n 
B 1 258 ASN 258 258 258 ASN ASN C . n 
B 1 259 LEU 259 259 259 LEU LEU C . n 
B 1 260 VAL 260 260 260 VAL VAL C . n 
B 1 261 PRO 261 261 261 PRO PRO C . n 
B 1 262 TYR 262 262 262 TYR TYR C . n 
B 1 263 PRO 263 263 263 PRO PRO C . n 
B 1 264 ARG 264 264 264 ARG ARG C . n 
B 1 265 ILE 265 265 265 ILE ILE C . n 
B 1 266 HIS 266 266 266 HIS HIS C . n 
B 1 267 PHE 267 267 267 PHE PHE C . n 
B 1 268 PRO 268 268 268 PRO PRO C . n 
B 1 269 LEU 269 269 269 LEU LEU C . n 
B 1 270 ALA 270 270 270 ALA ALA C . n 
B 1 271 THR 271 271 271 THR THR C . n 
B 1 272 TYR 272 272 272 TYR TYR C . n 
B 1 273 ALA 273 273 273 ALA ALA C . n 
B 1 274 PRO 274 274 274 PRO PRO C . n 
B 1 275 VAL 275 275 275 VAL VAL C . n 
B 1 276 ILE 276 276 276 ILE ILE C . n 
B 1 277 SER 277 277 277 SER SER C . n 
B 1 278 ALA 278 278 278 ALA ALA C . n 
B 1 279 GLU 279 279 279 GLU GLU C . n 
B 1 280 LYS 280 280 280 LYS LYS C . n 
B 1 281 ALA 281 281 281 ALA ALA C . n 
B 1 282 TYR 282 282 282 TYR TYR C . n 
B 1 283 HIS 283 283 283 HIS HIS C . n 
B 1 284 GLU 284 284 284 GLU GLU C . n 
B 1 285 GLN 285 285 285 GLN GLN C . n 
B 1 286 LEU 286 286 286 LEU LEU C . n 
B 1 287 SER 287 287 287 SER SER C . n 
B 1 288 VAL 288 288 288 VAL VAL C . n 
B 1 289 ALA 289 289 289 ALA ALA C . n 
B 1 290 GLU 290 290 290 GLU GLU C . n 
B 1 291 ILE 291 291 291 ILE ILE C . n 
B 1 292 THR 292 292 292 THR THR C . n 
B 1 293 ASN 293 293 293 ASN ASN C . n 
B 1 294 ALA 294 294 294 ALA ALA C . n 
B 1 295 CYS 295 295 295 CYS CYS C . n 
B 1 296 PHE 296 296 296 PHE PHE C . n 
B 1 297 GLU 297 297 297 GLU GLU C . n 
B 1 298 PRO 298 298 298 PRO PRO C . n 
B 1 299 ALA 299 299 299 ALA ALA C . n 
B 1 300 ASN 300 300 300 ASN ASN C . n 
B 1 301 GLN 301 301 301 GLN GLN C . n 
B 1 302 MET 302 302 302 MET MET C . n 
B 1 303 VAL 303 303 303 VAL VAL C . n 
B 1 304 LYS 304 304 304 LYS LYS C . n 
B 1 305 CYS 305 305 305 CYS CYS C . n 
B 1 306 ASP 306 306 306 ASP ASP C . n 
B 1 307 PRO 307 307 307 PRO PRO C . n 
B 1 308 ARG 308 308 308 ARG ARG C . n 
B 1 309 HIS 309 309 309 HIS HIS C . n 
B 1 310 GLY 310 310 310 GLY GLY C . n 
B 1 311 LYS 311 311 311 LYS LYS C . n 
B 1 312 TYR 312 312 312 TYR TYR C . n 
B 1 313 MET 313 313 313 MET MET C . n 
B 1 314 ALA 314 314 314 ALA ALA C . n 
B 1 315 CYS 315 315 315 CYS CYS C . n 
B 1 316 CYS 316 316 316 CYS CYS C . n 
B 1 317 LEU 317 317 317 LEU LEU C . n 
B 1 318 LEU 318 318 318 LEU LEU C . n 
B 1 319 TYR 319 319 319 TYR TYR C . n 
B 1 320 ARG 320 320 320 ARG ARG C . n 
B 1 321 GLY 321 321 321 GLY GLY C . n 
B 1 322 ASP 322 322 322 ASP ASP C . n 
B 1 323 VAL 323 323 323 VAL VAL C . n 
B 1 324 VAL 324 324 324 VAL VAL C . n 
B 1 325 PRO 325 325 325 PRO PRO C . n 
B 1 326 LYS 326 326 326 LYS LYS C . n 
B 1 327 ASP 327 327 327 ASP ASP C . n 
B 1 328 VAL 328 328 328 VAL VAL C . n 
B 1 329 ASN 329 329 329 ASN ASN C . n 
B 1 330 ALA 330 330 330 ALA ALA C . n 
B 1 331 ALA 331 331 331 ALA ALA C . n 
B 1 332 ILE 332 332 332 ILE ILE C . n 
B 1 333 ALA 333 333 333 ALA ALA C . n 
B 1 334 THR 334 334 334 THR THR C . n 
B 1 335 ILE 335 335 335 ILE ILE C . n 
B 1 336 LYS 336 336 336 LYS LYS C . n 
B 1 337 THR 337 337 337 THR THR C . n 
B 1 338 LYS 338 338 338 LYS LYS C . n 
B 1 339 ARG 339 339 339 ARG ARG C . n 
B 1 340 SER 340 340 340 SER SER C . n 
B 1 341 ILE 341 341 341 ILE ILE C . n 
B 1 342 GLN 342 342 342 GLN GLN C . n 
B 1 343 PHE 343 343 343 PHE PHE C . n 
B 1 344 VAL 344 344 344 VAL VAL C . n 
B 1 345 ASP 345 345 345 ASP ASP C . n 
B 1 346 TRP 346 346 346 TRP TRP C . n 
B 1 347 CYS 347 347 347 CYS CYS C . n 
B 1 348 PRO 348 348 348 PRO PRO C . n 
B 1 349 THR 349 349 349 THR THR C . n 
B 1 350 GLY 350 350 350 GLY GLY C . n 
B 1 351 PHE 351 351 351 PHE PHE C . n 
B 1 352 LYS 352 352 352 LYS LYS C . n 
B 1 353 VAL 353 353 353 VAL VAL C . n 
B 1 354 GLY 354 354 354 GLY GLY C . n 
B 1 355 ILE 355 355 355 ILE ILE C . n 
B 1 356 ASN 356 356 356 ASN ASN C . n 
B 1 357 TYR 357 357 357 TYR TYR C . n 
B 1 358 GLN 358 358 358 GLN GLN C . n 
B 1 359 PRO 359 359 359 PRO PRO C . n 
B 1 360 PRO 360 360 360 PRO PRO C . n 
B 1 361 THR 361 361 361 THR THR C . n 
B 1 362 VAL 362 362 362 VAL VAL C . n 
B 1 363 VAL 363 363 363 VAL VAL C . n 
B 1 364 PRO 364 364 364 PRO PRO C . n 
B 1 365 GLY 365 365 365 GLY GLY C . n 
B 1 366 GLY 366 366 366 GLY GLY C . n 
B 1 367 ASP 367 367 367 ASP ASP C . n 
B 1 368 LEU 368 368 368 LEU LEU C . n 
B 1 369 ALA 369 369 369 ALA ALA C . n 
B 1 370 LYS 370 370 370 LYS LYS C . n 
B 1 371 VAL 371 371 371 VAL VAL C . n 
B 1 372 GLN 372 372 372 GLN GLN C . n 
B 1 373 ARG 373 373 373 ARG ARG C . n 
B 1 374 ALA 374 374 374 ALA ALA C . n 
B 1 375 VAL 375 375 375 VAL VAL C . n 
B 1 376 CYS 376 376 376 CYS CYS C . n 
B 1 377 MET 377 377 377 MET MET C . n 
B 1 378 LEU 378 378 378 LEU LEU C . n 
B 1 379 SER 379 379 379 SER SER C . n 
B 1 380 ASN 380 380 380 ASN ASN C . n 
B 1 381 THR 381 381 381 THR THR C . n 
B 1 382 THR 382 382 382 THR THR C . n 
B 1 383 ALA 383 383 383 ALA ALA C . n 
B 1 384 ILE 384 384 384 ILE ILE C . n 
B 1 385 ALA 385 385 385 ALA ALA C . n 
B 1 386 GLU 386 386 386 GLU GLU C . n 
B 1 387 ALA 387 387 387 ALA ALA C . n 
B 1 388 TRP 388 388 388 TRP TRP C . n 
B 1 389 ALA 389 389 389 ALA ALA C . n 
B 1 390 ARG 390 390 390 ARG ARG C . n 
B 1 391 LEU 391 391 391 LEU LEU C . n 
B 1 392 ASP 392 392 392 ASP ASP C . n 
B 1 393 HIS 393 393 393 HIS HIS C . n 
B 1 394 LYS 394 394 394 LYS LYS C . n 
B 1 395 PHE 395 395 395 PHE PHE C . n 
B 1 396 ASP 396 396 396 ASP ASP C . n 
B 1 397 LEU 397 397 397 LEU LEU C . n 
B 1 398 MET 398 398 398 MET MET C . n 
B 1 399 TYR 399 399 399 TYR TYR C . n 
B 1 400 ALA 400 400 400 ALA ALA C . n 
B 1 401 LYS 401 401 401 LYS LYS C . n 
B 1 402 ARG 402 402 402 ARG ARG C . n 
B 1 403 ALA 403 403 403 ALA ALA C . n 
B 1 404 PHE 404 404 404 PHE PHE C . n 
B 1 405 VAL 405 405 405 VAL VAL C . n 
B 1 406 HIS 406 406 406 HIS HIS C . n 
B 1 407 TRP 407 407 407 TRP TRP C . n 
B 1 408 TYR 408 408 408 TYR TYR C . n 
B 1 409 VAL 409 409 409 VAL VAL C . n 
B 1 410 GLY 410 410 410 GLY GLY C . n 
B 1 411 GLU 411 411 411 GLU GLU C . n 
B 1 412 GLY 412 412 412 GLY GLY C . n 
B 1 413 MET 413 413 413 MET MET C . n 
B 1 414 GLU 414 414 414 GLU GLU C . n 
B 1 415 GLU 415 415 415 GLU GLU C . n 
B 1 416 GLY 416 416 416 GLY GLY C . n 
B 1 417 GLU 417 417 417 GLU GLU C . n 
B 1 418 PHE 418 418 418 PHE PHE C . n 
B 1 419 SER 419 419 419 SER SER C . n 
B 1 420 GLU 420 420 420 GLU GLU C . n 
B 1 421 ALA 421 421 421 ALA ALA C . n 
B 1 422 ARG 422 422 422 ARG ARG C . n 
B 1 423 GLU 423 423 423 GLU GLU C . n 
B 1 424 ASP 424 424 424 ASP ASP C . n 
B 1 425 MET 425 425 425 MET MET C . n 
B 1 426 ALA 426 426 426 ALA ALA C . n 
B 1 427 ALA 427 427 427 ALA ALA C . n 
B 1 428 LEU 428 428 428 LEU LEU C . n 
B 1 429 GLU 429 429 429 GLU GLU C . n 
B 1 430 LYS 430 430 430 LYS LYS C . n 
B 1 431 ASP 431 431 431 ASP ASP C . n 
B 1 432 TYR 432 432 432 TYR TYR C . n 
B 1 433 GLU 433 433 433 GLU GLU C . n 
B 1 434 GLU 434 434 434 GLU GLU C . n 
B 1 435 VAL 435 435 435 VAL VAL C . n 
B 1 436 GLY 436 436 436 GLY GLY C . n 
B 1 437 VAL 437 437 437 VAL VAL C . n 
B 1 438 ASP 438 438 438 ASP ASP C . n 
B 1 439 SER 439 439 439 SER SER C . n 
B 1 440 VAL 440 440 440 VAL VAL C . n 
B 1 441 GLU 441 441 ?   ?   ?   C . n 
B 1 442 GLY 442 442 ?   ?   ?   C . n 
B 1 443 GLU 443 443 ?   ?   ?   C . n 
B 1 444 GLY 444 444 ?   ?   ?   C . n 
B 1 445 GLU 445 445 ?   ?   ?   C . n 
B 1 446 GLU 446 446 ?   ?   ?   C . n 
B 1 447 GLU 447 447 ?   ?   ?   C . n 
B 1 448 GLY 448 448 ?   ?   ?   C . n 
B 1 449 GLU 449 449 ?   ?   ?   C . n 
B 1 450 GLU 450 450 ?   ?   ?   C . n 
C 2 1   MET 1   1   1   MET MET D . n 
C 2 2   ARG 2   2   2   ARG ARG D . n 
C 2 3   GLU 3   3   3   GLU GLU D . n 
C 2 4   ILE 4   4   4   ILE ILE D . n 
C 2 5   VAL 5   5   5   VAL VAL D . n 
C 2 6   HIS 6   6   6   HIS HIS D . n 
C 2 7   ILE 7   7   7   ILE ILE D . n 
C 2 8   GLN 8   8   8   GLN GLN D . n 
C 2 9   ALA 9   9   9   ALA ALA D . n 
C 2 10  GLY 10  10  10  GLY GLY D . n 
C 2 11  GLN 11  11  11  GLN GLN D . n 
C 2 12  CYS 12  12  12  CYS CYS D . n 
C 2 13  GLY 13  13  13  GLY GLY D . n 
C 2 14  ASN 14  14  14  ASN ASN D . n 
C 2 15  GLN 15  15  15  GLN GLN D . n 
C 2 16  ILE 16  16  16  ILE ILE D . n 
C 2 17  GLY 17  17  17  GLY GLY D . n 
C 2 18  ALA 18  18  18  ALA ALA D . n 
C 2 19  LYS 19  19  19  LYS LYS D . n 
C 2 20  PHE 20  20  20  PHE PHE D . n 
C 2 21  TRP 21  21  21  TRP TRP D . n 
C 2 22  GLU 22  22  22  GLU GLU D . n 
C 2 23  VAL 23  23  23  VAL VAL D . n 
C 2 24  ILE 24  24  24  ILE ILE D . n 
C 2 25  SER 25  25  25  SER SER D . n 
C 2 26  ASP 26  26  26  ASP ASP D . n 
C 2 27  GLU 27  27  27  GLU GLU D . n 
C 2 28  HIS 28  28  28  HIS HIS D . n 
C 2 29  GLY 29  29  29  GLY GLY D . n 
C 2 30  ILE 30  30  30  ILE ILE D . n 
C 2 31  ASP 31  31  31  ASP ASP D . n 
C 2 32  PRO 32  32  32  PRO PRO D . n 
C 2 33  THR 33  33  33  THR THR D . n 
C 2 34  GLY 34  34  34  GLY GLY D . n 
C 2 35  SER 35  35  35  SER SER D . n 
C 2 36  TYR 36  36  36  TYR TYR D . n 
C 2 37  HIS 37  37  37  HIS HIS D . n 
C 2 38  GLY 38  38  38  GLY GLY D . n 
C 2 39  ASP 39  39  39  ASP ASP D . n 
C 2 40  SER 40  40  40  SER SER D . n 
C 2 41  ASP 41  41  41  ASP ASP D . n 
C 2 42  LEU 42  42  42  LEU LEU D . n 
C 2 43  GLN 43  45  45  GLN GLN D . n 
C 2 44  LEU 44  46  46  LEU LEU D . n 
C 2 45  GLU 45  47  47  GLU GLU D . n 
C 2 46  ARG 46  48  48  ARG ARG D . n 
C 2 47  ILE 47  49  49  ILE ILE D . n 
C 2 48  ASN 48  50  50  ASN ASN D . n 
C 2 49  VAL 49  51  51  VAL VAL D . n 
C 2 50  TYR 50  52  52  TYR TYR D . n 
C 2 51  TYR 51  53  53  TYR TYR D . n 
C 2 52  ASN 52  54  54  ASN ASN D . n 
C 2 53  GLU 53  55  55  GLU GLU D . n 
C 2 54  ALA 54  56  56  ALA ALA D . n 
C 2 55  THR 55  57  57  THR THR D . n 
C 2 56  GLY 56  58  58  GLY GLY D . n 
C 2 57  ASN 57  59  59  ASN ASN D . n 
C 2 58  LYS 58  60  60  LYS LYS D . n 
C 2 59  TYR 59  61  61  TYR TYR D . n 
C 2 60  VAL 60  62  62  VAL VAL D . n 
C 2 61  PRO 61  63  63  PRO PRO D . n 
C 2 62  ARG 62  64  64  ARG ARG D . n 
C 2 63  ALA 63  65  65  ALA ALA D . n 
C 2 64  ILE 64  66  66  ILE ILE D . n 
C 2 65  LEU 65  67  67  LEU LEU D . n 
C 2 66  VAL 66  68  68  VAL VAL D . n 
C 2 67  ASP 67  69  69  ASP ASP D . n 
C 2 68  LEU 68  70  70  LEU LEU D . n 
C 2 69  GLU 69  71  71  GLU GLU D . n 
C 2 70  PRO 70  72  72  PRO PRO D . n 
C 2 71  GLY 71  73  73  GLY GLY D . n 
C 2 72  THR 72  74  74  THR THR D . n 
C 2 73  MET 73  75  75  MET MET D . n 
C 2 74  ASP 74  76  76  ASP ASP D . n 
C 2 75  SER 75  77  77  SER SER D . n 
C 2 76  VAL 76  78  78  VAL VAL D . n 
C 2 77  ARG 77  79  79  ARG ARG D . n 
C 2 78  SER 78  80  80  SER SER D . n 
C 2 79  GLY 79  81  81  GLY GLY D . n 
C 2 80  PRO 80  82  82  PRO PRO D . n 
C 2 81  PHE 81  83  83  PHE PHE D . n 
C 2 82  GLY 82  84  84  GLY GLY D . n 
C 2 83  GLN 83  85  85  GLN GLN D . n 
C 2 84  ILE 84  86  86  ILE ILE D . n 
C 2 85  PHE 85  87  87  PHE PHE D . n 
C 2 86  ARG 86  88  88  ARG ARG D . n 
C 2 87  PRO 87  89  89  PRO PRO D . n 
C 2 88  ASP 88  90  90  ASP ASP D . n 
C 2 89  ASN 89  91  91  ASN ASN D . n 
C 2 90  PHE 90  92  92  PHE PHE D . n 
C 2 91  VAL 91  93  93  VAL VAL D . n 
C 2 92  PHE 92  94  94  PHE PHE D . n 
C 2 93  GLY 93  95  95  GLY GLY D . n 
C 2 94  GLN 94  96  96  GLN GLN D . n 
C 2 95  SER 95  97  97  SER SER D . n 
C 2 96  GLY 96  98  98  GLY GLY D . n 
C 2 97  ALA 97  99  99  ALA ALA D . n 
C 2 98  GLY 98  100 100 GLY GLY D . n 
C 2 99  ASN 99  101 101 ASN ASN D . n 
C 2 100 ASN 100 102 102 ASN ASN D . n 
C 2 101 TRP 101 103 103 TRP TRP D . n 
C 2 102 ALA 102 104 104 ALA ALA D . n 
C 2 103 LYS 103 105 105 LYS LYS D . n 
C 2 104 GLY 104 106 106 GLY GLY D . n 
C 2 105 HIS 105 107 107 HIS HIS D . n 
C 2 106 TYR 106 108 108 TYR TYR D . n 
C 2 107 THR 107 109 109 THR THR D . n 
C 2 108 GLU 108 110 110 GLU GLU D . n 
C 2 109 GLY 109 111 111 GLY GLY D . n 
C 2 110 ALA 110 112 112 ALA ALA D . n 
C 2 111 GLU 111 113 113 GLU GLU D . n 
C 2 112 LEU 112 114 114 LEU LEU D . n 
C 2 113 VAL 113 115 115 VAL VAL D . n 
C 2 114 ASP 114 116 116 ASP ASP D . n 
C 2 115 SER 115 117 117 SER SER D . n 
C 2 116 VAL 116 118 118 VAL VAL D . n 
C 2 117 LEU 117 119 119 LEU LEU D . n 
C 2 118 ASP 118 120 120 ASP ASP D . n 
C 2 119 VAL 119 121 121 VAL VAL D . n 
C 2 120 VAL 120 122 122 VAL VAL D . n 
C 2 121 ARG 121 123 123 ARG ARG D . n 
C 2 122 LYS 122 124 124 LYS LYS D . n 
C 2 123 GLU 123 125 125 GLU GLU D . n 
C 2 124 SER 124 126 126 SER SER D . n 
C 2 125 GLU 125 127 127 GLU GLU D . n 
C 2 126 SER 126 128 128 SER SER D . n 
C 2 127 CYS 127 129 129 CYS CYS D . n 
C 2 128 ASP 128 130 130 ASP ASP D . n 
C 2 129 CYS 129 131 131 CYS CYS D . n 
C 2 130 LEU 130 132 132 LEU LEU D . n 
C 2 131 GLN 131 133 133 GLN GLN D . n 
C 2 132 GLY 132 134 134 GLY GLY D . n 
C 2 133 PHE 133 135 135 PHE PHE D . n 
C 2 134 GLN 134 136 136 GLN GLN D . n 
C 2 135 LEU 135 137 137 LEU LEU D . n 
C 2 136 THR 136 138 138 THR THR D . n 
C 2 137 HIS 137 139 139 HIS HIS D . n 
C 2 138 SER 138 140 140 SER SER D . n 
C 2 139 LEU 139 141 141 LEU LEU D . n 
C 2 140 GLY 140 142 142 GLY GLY D . n 
C 2 141 GLY 141 143 143 GLY GLY D . n 
C 2 142 GLY 142 144 144 GLY GLY D . n 
C 2 143 THR 143 145 145 THR THR D . n 
C 2 144 GLY 144 146 146 GLY GLY D . n 
C 2 145 SER 145 147 147 SER SER D . n 
C 2 146 GLY 146 148 148 GLY GLY D . n 
C 2 147 MET 147 149 149 MET MET D . n 
C 2 148 GLY 148 150 150 GLY GLY D . n 
C 2 149 THR 149 151 151 THR THR D . n 
C 2 150 LEU 150 152 152 LEU LEU D . n 
C 2 151 LEU 151 153 153 LEU LEU D . n 
C 2 152 ILE 152 154 154 ILE ILE D . n 
C 2 153 SER 153 155 155 SER SER D . n 
C 2 154 LYS 154 156 156 LYS LYS D . n 
C 2 155 ILE 155 157 157 ILE ILE D . n 
C 2 156 ARG 156 158 158 ARG ARG D . n 
C 2 157 GLU 157 159 159 GLU GLU D . n 
C 2 158 GLU 158 160 160 GLU GLU D . n 
C 2 159 TYR 159 161 161 TYR TYR D . n 
C 2 160 PRO 160 162 162 PRO PRO D . n 
C 2 161 ASP 161 163 163 ASP ASP D . n 
C 2 162 ARG 162 164 164 ARG ARG D . n 
C 2 163 ILE 163 165 165 ILE ILE D . n 
C 2 164 MET 164 166 166 MET MET D . n 
C 2 165 ASN 165 167 167 ASN ASN D . n 
C 2 166 THR 166 168 168 THR THR D . n 
C 2 167 PHE 167 169 169 PHE PHE D . n 
C 2 168 SER 168 170 170 SER SER D . n 
C 2 169 VAL 169 171 171 VAL VAL D . n 
C 2 170 MET 170 172 172 MET MET D . n 
C 2 171 PRO 171 173 173 PRO PRO D . n 
C 2 172 SER 172 174 174 SER SER D . n 
C 2 173 PRO 173 175 175 PRO PRO D . n 
C 2 174 LYS 174 176 176 LYS LYS D . n 
C 2 175 VAL 175 177 177 VAL VAL D . n 
C 2 176 SER 176 178 178 SER SER D . n 
C 2 177 ASP 177 179 179 ASP ASP D . n 
C 2 178 THR 178 180 180 THR THR D . n 
C 2 179 VAL 179 181 181 VAL VAL D . n 
C 2 180 VAL 180 182 182 VAL VAL D . n 
C 2 181 GLU 181 183 183 GLU GLU D . n 
C 2 182 PRO 182 184 184 PRO PRO D . n 
C 2 183 TYR 183 185 185 TYR TYR D . n 
C 2 184 ASN 184 186 186 ASN ASN D . n 
C 2 185 ALA 185 187 187 ALA ALA D . n 
C 2 186 THR 186 188 188 THR THR D . n 
C 2 187 LEU 187 189 189 LEU LEU D . n 
C 2 188 SER 188 190 190 SER SER D . n 
C 2 189 VAL 189 191 191 VAL VAL D . n 
C 2 190 HIS 190 192 192 HIS HIS D . n 
C 2 191 GLN 191 193 193 GLN GLN D . n 
C 2 192 LEU 192 194 194 LEU LEU D . n 
C 2 193 VAL 193 195 195 VAL VAL D . n 
C 2 194 GLU 194 196 196 GLU GLU D . n 
C 2 195 ASN 195 197 197 ASN ASN D . n 
C 2 196 THR 196 198 198 THR THR D . n 
C 2 197 ASP 197 199 199 ASP ASP D . n 
C 2 198 GLU 198 200 200 GLU GLU D . n 
C 2 199 THR 199 201 201 THR THR D . n 
C 2 200 TYR 200 202 202 TYR TYR D . n 
C 2 201 CYS 201 203 203 CYS CYS D . n 
C 2 202 ILE 202 204 204 ILE ILE D . n 
C 2 203 ASP 203 205 205 ASP ASP D . n 
C 2 204 ASN 204 206 206 ASN ASN D . n 
C 2 205 GLU 205 207 207 GLU GLU D . n 
C 2 206 ALA 206 208 208 ALA ALA D . n 
C 2 207 LEU 207 209 209 LEU LEU D . n 
C 2 208 TYR 208 210 210 TYR TYR D . n 
C 2 209 ASP 209 211 211 ASP ASP D . n 
C 2 210 ILE 210 212 212 ILE ILE D . n 
C 2 211 CYS 211 213 213 CYS CYS D . n 
C 2 212 PHE 212 214 214 PHE PHE D . n 
C 2 213 ARG 213 215 215 ARG ARG D . n 
C 2 214 THR 214 216 216 THR THR D . n 
C 2 215 LEU 215 217 217 LEU LEU D . n 
C 2 216 LYS 216 218 218 LYS LYS D . n 
C 2 217 LEU 217 219 219 LEU LEU D . n 
C 2 218 THR 218 220 220 THR THR D . n 
C 2 219 THR 219 221 221 THR THR D . n 
C 2 220 PRO 220 222 222 PRO PRO D . n 
C 2 221 THR 221 223 223 THR THR D . n 
C 2 222 TYR 222 224 224 TYR TYR D . n 
C 2 223 GLY 223 225 225 GLY GLY D . n 
C 2 224 ASP 224 226 226 ASP ASP D . n 
C 2 225 LEU 225 227 227 LEU LEU D . n 
C 2 226 ASN 226 228 228 ASN ASN D . n 
C 2 227 HIS 227 229 229 HIS HIS D . n 
C 2 228 LEU 228 230 230 LEU LEU D . n 
C 2 229 VAL 229 231 231 VAL VAL D . n 
C 2 230 SER 230 232 232 SER SER D . n 
C 2 231 ALA 231 233 233 ALA ALA D . n 
C 2 232 THR 232 234 234 THR THR D . n 
C 2 233 MET 233 235 235 MET MET D . n 
C 2 234 SER 234 236 236 SER SER D . n 
C 2 235 GLY 235 237 237 GLY GLY D . n 
C 2 236 VAL 236 238 238 VAL VAL D . n 
C 2 237 THR 237 239 239 THR THR D . n 
C 2 238 THR 238 240 240 THR THR D . n 
C 2 239 CYS 239 241 241 CYS CYS D . n 
C 2 240 LEU 240 242 242 LEU LEU D . n 
C 2 241 ARG 241 243 243 ARG ARG D . n 
C 2 242 PHE 242 244 244 PHE PHE D . n 
C 2 243 PRO 243 245 245 PRO PRO D . n 
C 2 244 GLY 244 246 246 GLY GLY D . n 
C 2 245 GLN 245 247 247 GLN GLN D . n 
C 2 246 LEU 246 248 248 LEU LEU D . n 
C 2 247 ASN 247 249 249 ASN ASN D . n 
C 2 248 ALA 248 250 250 ALA ALA D . n 
C 2 249 ASP 249 251 251 ASP ASP D . n 
C 2 250 LEU 250 252 252 LEU LEU D . n 
C 2 251 ARG 251 253 253 ARG ARG D . n 
C 2 252 LYS 252 254 254 LYS LYS D . n 
C 2 253 LEU 253 255 255 LEU LEU D . n 
C 2 254 ALA 254 256 256 ALA ALA D . n 
C 2 255 VAL 255 257 257 VAL VAL D . n 
C 2 256 ASN 256 258 258 ASN ASN D . n 
C 2 257 MET 257 259 259 MET MET D . n 
C 2 258 VAL 258 260 260 VAL VAL D . n 
C 2 259 PRO 259 261 261 PRO PRO D . n 
C 2 260 PHE 260 262 262 PHE PHE D . n 
C 2 261 PRO 261 263 263 PRO PRO D . n 
C 2 262 ARG 262 264 264 ARG ARG D . n 
C 2 263 LEU 263 265 265 LEU LEU D . n 
C 2 264 HIS 264 266 266 HIS HIS D . n 
C 2 265 PHE 265 267 267 PHE PHE D . n 
C 2 266 PHE 266 268 268 PHE PHE D . n 
C 2 267 MET 267 269 269 MET MET D . n 
C 2 268 PRO 268 270 270 PRO PRO D . n 
C 2 269 GLY 269 271 271 GLY GLY D . n 
C 2 270 PHE 270 272 272 PHE PHE D . n 
C 2 271 ALA 271 273 273 ALA ALA D . n 
C 2 272 PRO 272 274 274 PRO PRO D . n 
C 2 273 LEU 273 275 275 LEU LEU D . n 
C 2 274 THR 274 276 276 THR THR D . n 
C 2 275 SER 275 277 ?   ?   ?   D . n 
C 2 276 ARG 276 278 ?   ?   ?   D . n 
C 2 277 GLY 277 279 ?   ?   ?   D . n 
C 2 278 SER 278 280 ?   ?   ?   D . n 
C 2 279 GLN 279 281 ?   ?   ?   D . n 
C 2 280 GLN 280 282 ?   ?   ?   D . n 
C 2 281 TYR 281 283 ?   ?   ?   D . n 
C 2 282 ARG 282 284 284 ARG ARG D . n 
C 2 283 ALA 283 285 285 ALA ALA D . n 
C 2 284 LEU 284 286 286 LEU LEU D . n 
C 2 285 THR 285 287 287 THR THR D . n 
C 2 286 VAL 286 288 288 VAL VAL D . n 
C 2 287 PRO 287 289 289 PRO PRO D . n 
C 2 288 GLU 288 290 290 GLU GLU D . n 
C 2 289 LEU 289 291 291 LEU LEU D . n 
C 2 290 THR 290 292 292 THR THR D . n 
C 2 291 GLN 291 293 293 GLN GLN D . n 
C 2 292 GLN 292 294 294 GLN GLN D . n 
C 2 293 MET 293 295 295 MET MET D . n 
C 2 294 PHE 294 296 296 PHE PHE D . n 
C 2 295 ASP 295 297 297 ASP ASP D . n 
C 2 296 SER 296 298 298 SER SER D . n 
C 2 297 LYS 297 299 299 LYS LYS D . n 
C 2 298 ASN 298 300 300 ASN ASN D . n 
C 2 299 MET 299 301 301 MET MET D . n 
C 2 300 MET 300 302 302 MET MET D . n 
C 2 301 ALA 301 303 303 ALA ALA D . n 
C 2 302 ALA 302 304 304 ALA ALA D . n 
C 2 303 CYS 303 305 305 CYS CYS D . n 
C 2 304 ASP 304 306 306 ASP ASP D . n 
C 2 305 PRO 305 307 307 PRO PRO D . n 
C 2 306 ARG 306 308 308 ARG ARG D . n 
C 2 307 HIS 307 309 309 HIS HIS D . n 
C 2 308 GLY 308 310 310 GLY GLY D . n 
C 2 309 ARG 309 311 311 ARG ARG D . n 
C 2 310 TYR 310 312 312 TYR TYR D . n 
C 2 311 LEU 311 313 313 LEU LEU D . n 
C 2 312 THR 312 314 314 THR THR D . n 
C 2 313 VAL 313 315 315 VAL VAL D . n 
C 2 314 ALA 314 316 316 ALA ALA D . n 
C 2 315 ALA 315 317 317 ALA ALA D . n 
C 2 316 ILE 316 318 318 ILE ILE D . n 
C 2 317 PHE 317 319 319 PHE PHE D . n 
C 2 318 ARG 318 320 320 ARG ARG D . n 
C 2 319 GLY 319 321 321 GLY GLY D . n 
C 2 320 ARG 320 322 322 ARG ARG D . n 
C 2 321 MET 321 323 323 MET MET D . n 
C 2 322 SER 322 324 324 SER SER D . n 
C 2 323 MET 323 325 325 MET MET D . n 
C 2 324 LYS 324 326 326 LYS LYS D . n 
C 2 325 GLU 325 327 327 GLU GLU D . n 
C 2 326 VAL 326 328 328 VAL VAL D . n 
C 2 327 ASP 327 329 329 ASP ASP D . n 
C 2 328 GLU 328 330 330 GLU GLU D . n 
C 2 329 GLN 329 331 331 GLN GLN D . n 
C 2 330 MET 330 332 332 MET MET D . n 
C 2 331 LEU 331 333 333 LEU LEU D . n 
C 2 332 ASN 332 334 334 ASN ASN D . n 
C 2 333 VAL 333 335 335 VAL VAL D . n 
C 2 334 GLN 334 336 336 GLN GLN D . n 
C 2 335 ASN 335 337 337 ASN ASN D . n 
C 2 336 LYS 336 338 338 LYS LYS D . n 
C 2 337 ASN 337 339 339 ASN ASN D . n 
C 2 338 SER 338 340 340 SER SER D . n 
C 2 339 SER 339 341 341 SER SER D . n 
C 2 340 TYR 340 342 342 TYR TYR D . n 
C 2 341 PHE 341 343 343 PHE PHE D . n 
C 2 342 VAL 342 344 344 VAL VAL D . n 
C 2 343 GLU 343 345 345 GLU GLU D . n 
C 2 344 TRP 344 346 346 TRP TRP D . n 
C 2 345 ILE 345 347 347 ILE ILE D . n 
C 2 346 PRO 346 348 348 PRO PRO D . n 
C 2 347 ASN 347 349 349 ASN ASN D . n 
C 2 348 ASN 348 350 350 ASN ASN D . n 
C 2 349 VAL 349 351 351 VAL VAL D . n 
C 2 350 LYS 350 352 352 LYS LYS D . n 
C 2 351 THR 351 353 353 THR THR D . n 
C 2 352 ALA 352 354 354 ALA ALA D . n 
C 2 353 VAL 353 355 355 VAL VAL D . n 
C 2 354 CYS 354 356 356 CYS CYS D . n 
C 2 355 ASP 355 357 357 ASP ASP D . n 
C 2 356 ILE 356 358 358 ILE ILE D . n 
C 2 357 PRO 357 359 359 PRO PRO D . n 
C 2 358 PRO 358 360 360 PRO PRO D . n 
C 2 359 ARG 359 369 369 ARG ARG D . n 
C 2 360 GLY 360 370 370 GLY GLY D . n 
C 2 361 LEU 361 371 371 LEU LEU D . n 
C 2 362 LYS 362 372 372 LYS LYS D . n 
C 2 363 MET 363 373 373 MET MET D . n 
C 2 364 SER 364 374 374 SER SER D . n 
C 2 365 ALA 365 375 375 ALA ALA D . n 
C 2 366 THR 366 376 376 THR THR D . n 
C 2 367 PHE 367 377 377 PHE PHE D . n 
C 2 368 ILE 368 378 378 ILE ILE D . n 
C 2 369 GLY 369 379 379 GLY GLY D . n 
C 2 370 ASN 370 380 380 ASN ASN D . n 
C 2 371 SER 371 381 381 SER SER D . n 
C 2 372 THR 372 382 382 THR THR D . n 
C 2 373 ALA 373 383 383 ALA ALA D . n 
C 2 374 ILE 374 384 384 ILE ILE D . n 
C 2 375 GLN 375 385 385 GLN GLN D . n 
C 2 376 GLU 376 386 386 GLU GLU D . n 
C 2 377 LEU 377 387 387 LEU LEU D . n 
C 2 378 PHE 378 388 388 PHE PHE D . n 
C 2 379 LYS 379 389 389 LYS LYS D . n 
C 2 380 ARG 380 390 390 ARG ARG D . n 
C 2 381 ILE 381 391 391 ILE ILE D . n 
C 2 382 SER 382 392 392 SER SER D . n 
C 2 383 GLU 383 393 393 GLU GLU D . n 
C 2 384 GLN 384 394 394 GLN GLN D . n 
C 2 385 PHE 385 395 395 PHE PHE D . n 
C 2 386 THR 386 396 396 THR THR D . n 
C 2 387 ALA 387 397 397 ALA ALA D . n 
C 2 388 MET 388 398 398 MET MET D . n 
C 2 389 PHE 389 399 399 PHE PHE D . n 
C 2 390 ARG 390 400 400 ARG ARG D . n 
C 2 391 ARG 391 401 401 ARG ARG D . n 
C 2 392 LYS 392 402 402 LYS LYS D . n 
C 2 393 ALA 393 403 403 ALA ALA D . n 
C 2 394 PHE 394 404 404 PHE PHE D . n 
C 2 395 LEU 395 405 405 LEU LEU D . n 
C 2 396 HIS 396 406 406 HIS HIS D . n 
C 2 397 TRP 397 407 407 TRP TRP D . n 
C 2 398 TYR 398 408 408 TYR TYR D . n 
C 2 399 THR 399 409 409 THR THR D . n 
C 2 400 GLY 400 410 410 GLY GLY D . n 
C 2 401 GLU 401 411 411 GLU GLU D . n 
C 2 402 GLY 402 412 412 GLY GLY D . n 
C 2 403 MET 403 413 413 MET MET D . n 
C 2 404 ASP 404 414 414 ASP ASP D . n 
C 2 405 GLU 405 415 415 GLU GLU D . n 
C 2 406 MET 406 416 416 MET MET D . n 
C 2 407 GLU 407 417 417 GLU GLU D . n 
C 2 408 PHE 408 418 418 PHE PHE D . n 
C 2 409 THR 409 419 419 THR THR D . n 
C 2 410 GLU 410 420 420 GLU GLU D . n 
C 2 411 ALA 411 421 421 ALA ALA D . n 
C 2 412 GLU 412 422 422 GLU GLU D . n 
C 2 413 SER 413 423 423 SER SER D . n 
C 2 414 ASN 414 424 424 ASN ASN D . n 
C 2 415 MET 415 425 425 MET MET D . n 
C 2 416 ASN 416 426 426 ASN ASN D . n 
C 2 417 ASP 417 427 427 ASP ASP D . n 
C 2 418 LEU 418 428 428 LEU LEU D . n 
C 2 419 VAL 419 429 429 VAL VAL D . n 
C 2 420 SER 420 430 430 SER SER D . n 
C 2 421 GLU 421 431 431 GLU GLU D . n 
C 2 422 TYR 422 432 432 TYR TYR D . n 
C 2 423 GLN 423 433 433 GLN GLN D . n 
C 2 424 GLN 424 434 434 GLN GLN D . n 
C 2 425 TYR 425 435 435 TYR TYR D . n 
C 2 426 GLN 426 436 436 GLN GLN D . n 
C 2 427 ASP 427 437 437 ASP ASP D . n 
C 2 428 ALA 428 438 438 ALA ALA D . n 
C 2 429 THR 429 439 439 THR THR D . n 
C 2 430 ALA 430 440 440 ALA ALA D . n 
C 2 431 ASP 431 441 441 ASP ASP D . n 
C 2 432 GLU 432 442 ?   ?   ?   D . n 
C 2 433 GLN 433 443 ?   ?   ?   D . n 
C 2 434 GLY 434 444 ?   ?   ?   D . n 
C 2 435 GLU 435 445 ?   ?   ?   D . n 
C 2 436 PHE 436 446 ?   ?   ?   D . n 
C 2 437 GLU 437 447 ?   ?   ?   D . n 
C 2 438 GLU 438 448 ?   ?   ?   D . n 
C 2 439 GLU 439 449 ?   ?   ?   D . n 
C 2 440 GLU 440 450 ?   ?   ?   D . n 
C 2 441 GLY 441 451 ?   ?   ?   D . n 
C 2 442 GLU 442 452 ?   ?   ?   D . n 
C 2 443 ASP 443 453 ?   ?   ?   D . n 
C 2 444 GLU 444 454 ?   ?   ?   D . n 
C 2 445 ALA 445 455 ?   ?   ?   D . n 
D 3 1   MET 1   3   ?   ?   ?   E . n 
D 3 2   ALA 2   4   ?   ?   ?   E . n 
D 3 3   ASP 3   5   ?   ?   ?   E . n 
D 3 4   MET 4   6   6   MET MET E . n 
D 3 5   GLU 5   7   7   GLU GLU E . n 
D 3 6   VAL 6   8   8   VAL VAL E . n 
D 3 7   ILE 7   9   9   ILE ILE E . n 
D 3 8   GLU 8   10  10  GLU GLU E . n 
D 3 9   LEU 9   11  11  LEU LEU E . n 
D 3 10  ASN 10  12  12  ASN ASN E . n 
D 3 11  LYS 11  13  13  LYS LYS E . n 
D 3 12  CYS 12  14  14  CYS CYS E . n 
D 3 13  THR 13  15  15  THR THR E . n 
D 3 14  SER 14  16  16  SER SER E . n 
D 3 15  GLY 15  17  17  GLY GLY E . n 
D 3 16  GLN 16  18  18  GLN GLN E . n 
D 3 17  SER 17  19  19  SER SER E . n 
D 3 18  PHE 18  20  20  PHE PHE E . n 
D 3 19  GLU 19  21  21  GLU GLU E . n 
D 3 20  VAL 20  22  22  VAL VAL E . n 
D 3 21  ILE 21  23  23  ILE ILE E . n 
D 3 22  LEU 22  24  24  LEU LEU E . n 
D 3 23  LYS 23  25  25  LYS LYS E . n 
D 3 24  PRO 24  26  26  PRO PRO E . n 
D 3 25  PRO 25  27  27  PRO PRO E . n 
D 3 26  SER 26  28  28  SER SER E . n 
D 3 27  PHE 27  29  ?   ?   ?   E . n 
D 3 28  ASP 28  30  ?   ?   ?   E . n 
D 3 29  GLY 29  31  ?   ?   ?   E . n 
D 3 30  VAL 30  32  ?   ?   ?   E . n 
D 3 31  PRO 31  33  ?   ?   ?   E . n 
D 3 32  GLU 32  34  ?   ?   ?   E . n 
D 3 33  PHE 33  35  ?   ?   ?   E . n 
D 3 34  ASN 34  36  ?   ?   ?   E . n 
D 3 35  ALA 35  37  ?   ?   ?   E . n 
D 3 36  SER 36  38  ?   ?   ?   E . n 
D 3 37  LEU 37  39  ?   ?   ?   E . n 
D 3 38  PRO 38  40  ?   ?   ?   E . n 
D 3 39  ARG 39  41  ?   ?   ?   E . n 
D 3 40  ARG 40  42  ?   ?   ?   E . n 
D 3 41  ARG 41  43  ?   ?   ?   E . n 
D 3 42  ASP 42  44  44  ASP ASP E . n 
D 3 43  PRO 43  45  45  PRO PRO E . n 
D 3 44  SER 44  46  46  SER SER E . n 
D 3 45  LEU 45  47  47  LEU LEU E . n 
D 3 46  GLU 46  48  48  GLU GLU E . n 
D 3 47  GLU 47  49  49  GLU GLU E . n 
D 3 48  ILE 48  50  50  ILE ILE E . n 
D 3 49  GLN 49  51  51  GLN GLN E . n 
D 3 50  LYS 50  52  52  LYS LYS E . n 
D 3 51  LYS 51  53  53  LYS LYS E . n 
D 3 52  LEU 52  54  54  LEU LEU E . n 
D 3 53  GLU 53  55  55  GLU GLU E . n 
D 3 54  ALA 54  56  56  ALA ALA E . n 
D 3 55  ALA 55  57  57  ALA ALA E . n 
D 3 56  GLU 56  58  58  GLU GLU E . n 
D 3 57  GLU 57  59  59  GLU GLU E . n 
D 3 58  ARG 58  60  60  ARG ARG E . n 
D 3 59  ARG 59  61  61  ARG ARG E . n 
D 3 60  LYS 60  62  62  LYS LYS E . n 
D 3 61  TYR 61  63  63  TYR TYR E . n 
D 3 62  GLN 62  64  64  GLN GLN E . n 
D 3 63  GLU 63  65  65  GLU GLU E . n 
D 3 64  ALA 64  66  66  ALA ALA E . n 
D 3 65  GLU 65  67  67  GLU GLU E . n 
D 3 66  LEU 66  68  68  LEU LEU E . n 
D 3 67  LEU 67  69  69  LEU LEU E . n 
D 3 68  LYS 68  70  70  LYS LYS E . n 
D 3 69  HIS 69  71  71  HIS HIS E . n 
D 3 70  LEU 70  72  72  LEU LEU E . n 
D 3 71  ALA 71  73  73  ALA ALA E . n 
D 3 72  GLU 72  74  74  GLU GLU E . n 
D 3 73  LYS 73  75  75  LYS LYS E . n 
D 3 74  ARG 74  76  76  ARG ARG E . n 
D 3 75  GLU 75  77  77  GLU GLU E . n 
D 3 76  HIS 76  78  78  HIS HIS E . n 
D 3 77  GLU 77  79  79  GLU GLU E . n 
D 3 78  ARG 78  80  80  ARG ARG E . n 
D 3 79  GLU 79  81  81  GLU GLU E . n 
D 3 80  VAL 80  82  82  VAL VAL E . n 
D 3 81  ILE 81  83  83  ILE ILE E . n 
D 3 82  GLN 82  84  84  GLN GLN E . n 
D 3 83  LYS 83  85  85  LYS LYS E . n 
D 3 84  ALA 84  86  86  ALA ALA E . n 
D 3 85  ILE 85  87  87  ILE ILE E . n 
D 3 86  GLU 86  88  88  GLU GLU E . n 
D 3 87  GLU 87  89  89  GLU GLU E . n 
D 3 88  ASN 88  90  90  ASN ASN E . n 
D 3 89  ASN 89  91  91  ASN ASN E . n 
D 3 90  ASN 90  92  92  ASN ASN E . n 
D 3 91  PHE 91  93  93  PHE PHE E . n 
D 3 92  ILE 92  94  94  ILE ILE E . n 
D 3 93  LYS 93  95  95  LYS LYS E . n 
D 3 94  MET 94  96  96  MET MET E . n 
D 3 95  ALA 95  97  97  ALA ALA E . n 
D 3 96  LYS 96  98  98  LYS LYS E . n 
D 3 97  GLU 97  99  99  GLU GLU E . n 
D 3 98  LYS 98  100 100 LYS LYS E . n 
D 3 99  LEU 99  101 101 LEU LEU E . n 
D 3 100 ALA 100 102 102 ALA ALA E . n 
D 3 101 GLN 101 103 103 GLN GLN E . n 
D 3 102 LYS 102 104 104 LYS LYS E . n 
D 3 103 MET 103 105 105 MET MET E . n 
D 3 104 GLU 104 106 106 GLU GLU E . n 
D 3 105 SER 105 107 107 SER SER E . n 
D 3 106 ASN 106 108 108 ASN ASN E . n 
D 3 107 LYS 107 109 109 LYS LYS E . n 
D 3 108 GLU 108 110 110 GLU GLU E . n 
D 3 109 ASN 109 111 111 ASN ASN E . n 
D 3 110 ARG 110 112 112 ARG ARG E . n 
D 3 111 GLU 111 113 113 GLU GLU E . n 
D 3 112 ALA 112 114 114 ALA ALA E . n 
D 3 113 HIS 113 115 115 HIS HIS E . n 
D 3 114 LEU 114 116 116 LEU LEU E . n 
D 3 115 ALA 115 117 117 ALA ALA E . n 
D 3 116 ALA 116 118 118 ALA ALA E . n 
D 3 117 MET 117 119 119 MET MET E . n 
D 3 118 LEU 118 120 120 LEU LEU E . n 
D 3 119 GLU 119 121 121 GLU GLU E . n 
D 3 120 ARG 120 122 122 ARG ARG E . n 
D 3 121 LEU 121 123 123 LEU LEU E . n 
D 3 122 GLN 122 124 124 GLN GLN E . n 
D 3 123 GLU 123 125 125 GLU GLU E . n 
D 3 124 LYS 124 126 126 LYS LYS E . n 
D 3 125 ASP 125 127 127 ASP ASP E . n 
D 3 126 LYS 126 128 128 LYS LYS E . n 
D 3 127 HIS 127 129 129 HIS HIS E . n 
D 3 128 ALA 128 130 130 ALA ALA E . n 
D 3 129 GLU 129 131 131 GLU GLU E . n 
D 3 130 GLU 130 132 132 GLU GLU E . n 
D 3 131 VAL 131 133 133 VAL VAL E . n 
D 3 132 ARG 132 134 134 ARG ARG E . n 
D 3 133 LYS 133 135 135 LYS LYS E . n 
D 3 134 ASN 134 136 136 ASN ASN E . n 
D 3 135 LYS 135 137 137 LYS LYS E . n 
D 3 136 GLU 136 138 138 GLU GLU E . n 
D 3 137 LEU 137 139 139 LEU LEU E . n 
D 3 138 LYS 138 140 140 LYS LYS E . n 
D 3 139 GLU 139 141 ?   ?   ?   E . n 
D 3 140 GLU 140 142 ?   ?   ?   E . n 
D 3 141 ALA 141 143 ?   ?   ?   E . n 
D 3 142 SER 142 144 ?   ?   ?   E . n 
D 3 143 ARG 143 145 ?   ?   ?   E . n 
E 4 1   MET 1   1   1   MET MET F . n 
E 4 2   TYR 2   2   2   TYR TYR F . n 
E 4 3   THR 3   3   3   THR THR F . n 
E 4 4   PHE 4   4   4   PHE PHE F . n 
E 4 5   VAL 5   5   5   VAL VAL F . n 
E 4 6   VAL 6   6   6   VAL VAL F . n 
E 4 7   ARG 7   7   7   ARG ARG F . n 
E 4 8   ASP 8   8   8   ASP ASP F . n 
E 4 9   GLU 9   9   9   GLU GLU F . n 
E 4 10  ASN 10  10  10  ASN ASN F . n 
E 4 11  SER 11  11  11  SER SER F . n 
E 4 12  SER 12  12  12  SER SER F . n 
E 4 13  VAL 13  13  13  VAL VAL F . n 
E 4 14  TYR 14  14  14  TYR TYR F . n 
E 4 15  ALA 15  15  15  ALA ALA F . n 
E 4 16  GLU 16  16  16  GLU GLU F . n 
E 4 17  VAL 17  17  17  VAL VAL F . n 
E 4 18  SER 18  18  18  SER SER F . n 
E 4 19  ARG 19  19  19  ARG ARG F . n 
E 4 20  LEU 20  20  20  LEU LEU F . n 
E 4 21  LEU 21  21  21  LEU LEU F . n 
E 4 22  LEU 22  22  22  LEU LEU F . n 
E 4 23  ALA 23  23  23  ALA ALA F . n 
E 4 24  THR 24  24  24  THR THR F . n 
E 4 25  GLY 25  25  25  GLY GLY F . n 
E 4 26  GLN 26  26  26  GLN GLN F . n 
E 4 27  TRP 27  27  27  TRP TRP F . n 
E 4 28  LYS 28  28  28  LYS LYS F . n 
E 4 29  ARG 29  29  29  ARG ARG F . n 
E 4 30  LEU 30  30  30  LEU LEU F . n 
E 4 31  ARG 31  31  31  ARG ARG F . n 
E 4 32  LYS 32  32  32  LYS LYS F . n 
E 4 33  ASP 33  33  33  ASP ASP F . n 
E 4 34  ASN 34  34  34  ASN ASN F . n 
E 4 35  PRO 35  35  35  PRO PRO F . n 
E 4 36  ARG 36  36  36  ARG ARG F . n 
E 4 37  PHE 37  37  37  PHE PHE F . n 
E 4 38  ASN 38  38  38  ASN ASN F . n 
E 4 39  LEU 39  39  39  LEU LEU F . n 
E 4 40  MET 40  40  40  MET MET F . n 
E 4 41  LEU 41  41  41  LEU LEU F . n 
E 4 42  GLY 42  42  42  GLY GLY F . n 
E 4 43  GLU 43  43  43  GLU GLU F . n 
E 4 44  ARG 44  44  44  ARG ARG F . n 
E 4 45  ASN 45  45  45  ASN ASN F . n 
E 4 46  ARG 46  46  46  ARG ARG F . n 
E 4 47  LEU 47  47  47  LEU LEU F . n 
E 4 48  PRO 48  48  48  PRO PRO F . n 
E 4 49  PHE 49  49  49  PHE PHE F . n 
E 4 50  GLY 50  50  50  GLY GLY F . n 
E 4 51  ARG 51  51  51  ARG ARG F . n 
E 4 52  LEU 52  52  52  LEU LEU F . n 
E 4 53  GLY 53  53  53  GLY GLY F . n 
E 4 54  HIS 54  54  54  HIS HIS F . n 
E 4 55  GLU 55  55  55  GLU GLU F . n 
E 4 56  PRO 56  56  56  PRO PRO F . n 
E 4 57  GLY 57  57  57  GLY GLY F . n 
E 4 58  LEU 58  58  58  LEU LEU F . n 
E 4 59  VAL 59  59  59  VAL VAL F . n 
E 4 60  GLN 60  60  60  GLN GLN F . n 
E 4 61  LEU 61  61  61  LEU LEU F . n 
E 4 62  VAL 62  62  62  VAL VAL F . n 
E 4 63  ASN 63  63  63  ASN ASN F . n 
E 4 64  TYR 64  64  64  TYR TYR F . n 
E 4 65  TYR 65  65  65  TYR TYR F . n 
E 4 66  ARG 66  66  66  ARG ARG F . n 
E 4 67  GLY 67  67  67  GLY GLY F . n 
E 4 68  ALA 68  68  68  ALA ALA F . n 
E 4 69  ASP 69  69  69  ASP ASP F . n 
E 4 70  LYS 70  70  70  LYS LYS F . n 
E 4 71  LEU 71  71  71  LEU LEU F . n 
E 4 72  CYS 72  72  72  CYS CYS F . n 
E 4 73  ARG 73  73  73  ARG ARG F . n 
E 4 74  LYS 74  74  74  LYS LYS F . n 
E 4 75  ALA 75  75  75  ALA ALA F . n 
E 4 76  SER 76  76  76  SER SER F . n 
E 4 77  LEU 77  77  77  LEU LEU F . n 
E 4 78  VAL 78  78  78  VAL VAL F . n 
E 4 79  LYS 79  79  79  LYS LYS F . n 
E 4 80  LEU 80  80  80  LEU LEU F . n 
E 4 81  ILE 81  81  81  ILE ILE F . n 
E 4 82  LYS 82  82  82  LYS LYS F . n 
E 4 83  THR 83  83  83  THR THR F . n 
E 4 84  SER 84  84  84  SER SER F . n 
E 4 85  PRO 85  85  85  PRO PRO F . n 
E 4 86  GLU 86  86  86  GLU GLU F . n 
E 4 87  LEU 87  87  87  LEU LEU F . n 
E 4 88  SER 88  88  88  SER SER F . n 
E 4 89  GLU 89  89  89  GLU GLU F . n 
E 4 90  SER 90  90  90  SER SER F . n 
E 4 91  CYS 91  91  91  CYS CYS F . n 
E 4 92  THR 92  92  92  THR THR F . n 
E 4 93  TRP 93  93  93  TRP TRP F . n 
E 4 94  PHE 94  94  94  PHE PHE F . n 
E 4 95  PRO 95  95  95  PRO PRO F . n 
E 4 96  GLU 96  96  96  GLU GLU F . n 
E 4 97  SER 97  97  97  SER SER F . n 
E 4 98  TYR 98  98  98  TYR TYR F . n 
E 4 99  VAL 99  99  99  VAL VAL F . n 
E 4 100 ILE 100 100 100 ILE ILE F . n 
E 4 101 TYR 101 101 101 TYR TYR F . n 
E 4 102 PRO 102 102 102 PRO PRO F . n 
E 4 103 THR 103 103 103 THR THR F . n 
E 4 104 ASN 104 104 ?   ?   ?   F . n 
E 4 105 LEU 105 105 ?   ?   ?   F . n 
E 4 106 LYS 106 106 ?   ?   ?   F . n 
E 4 107 THR 107 107 ?   ?   ?   F . n 
E 4 108 PRO 108 108 ?   ?   ?   F . n 
E 4 109 VAL 109 109 ?   ?   ?   F . n 
E 4 110 ALA 110 110 ?   ?   ?   F . n 
E 4 111 PRO 111 111 ?   ?   ?   F . n 
E 4 112 ALA 112 112 ?   ?   ?   F . n 
E 4 113 GLN 113 113 ?   ?   ?   F . n 
E 4 114 ASN 114 114 ?   ?   ?   F . n 
E 4 115 GLY 115 115 ?   ?   ?   F . n 
E 4 116 ILE 116 116 ?   ?   ?   F . n 
E 4 117 ARG 117 117 ?   ?   ?   F . n 
E 4 118 HIS 118 118 ?   ?   ?   F . n 
E 4 119 LEU 119 119 ?   ?   ?   F . n 
E 4 120 ILE 120 120 ?   ?   ?   F . n 
E 4 121 ASN 121 121 ?   ?   ?   F . n 
E 4 122 ASN 122 122 ?   ?   ?   F . n 
E 4 123 THR 123 123 ?   ?   ?   F . n 
E 4 124 ARG 124 124 ?   ?   ?   F . n 
E 4 125 THR 125 125 125 THR THR F . n 
E 4 126 ASP 126 126 126 ASP ASP F . n 
E 4 127 GLU 127 127 127 GLU GLU F . n 
E 4 128 ARG 128 128 128 ARG ARG F . n 
E 4 129 GLU 129 129 129 GLU GLU F . n 
E 4 130 VAL 130 130 130 VAL VAL F . n 
E 4 131 PHE 131 131 131 PHE PHE F . n 
E 4 132 LEU 132 132 132 LEU LEU F . n 
E 4 133 ALA 133 133 133 ALA ALA F . n 
E 4 134 ALA 134 134 134 ALA ALA F . n 
E 4 135 TYR 135 135 135 TYR TYR F . n 
E 4 136 ASN 136 136 136 ASN ASN F . n 
E 4 137 ARG 137 137 137 ARG ARG F . n 
E 4 138 ARG 138 138 ?   ?   ?   F . n 
E 4 139 ARG 139 139 ?   ?   ?   F . n 
E 4 140 GLU 140 140 ?   ?   ?   F . n 
E 4 141 GLY 141 141 ?   ?   ?   F . n 
E 4 142 ARG 142 142 ?   ?   ?   F . n 
E 4 143 GLU 143 143 ?   ?   ?   F . n 
E 4 144 GLY 144 144 144 GLY GLY F . n 
E 4 145 ASN 145 145 145 ASN ASN F . n 
E 4 146 VAL 146 146 146 VAL VAL F . n 
E 4 147 TRP 147 147 147 TRP TRP F . n 
E 4 148 ILE 148 148 148 ILE ILE F . n 
E 4 149 ALA 149 149 149 ALA ALA F . n 
E 4 150 LYS 150 150 ?   ?   ?   F . n 
E 4 151 SER 151 151 ?   ?   ?   F . n 
E 4 152 SER 152 152 ?   ?   ?   F . n 
E 4 153 ALA 153 153 ?   ?   ?   F . n 
E 4 154 GLY 154 154 ?   ?   ?   F . n 
E 4 155 ALA 155 155 ?   ?   ?   F . n 
E 4 156 LYS 156 156 ?   ?   ?   F . n 
E 4 157 GLY 157 157 ?   ?   ?   F . n 
E 4 158 GLU 158 158 ?   ?   ?   F . n 
E 4 159 GLY 159 159 159 GLY GLY F . n 
E 4 160 ILE 160 160 160 ILE ILE F . n 
E 4 161 LEU 161 161 161 LEU LEU F . n 
E 4 162 ILE 162 162 162 ILE ILE F . n 
E 4 163 SER 163 163 163 SER SER F . n 
E 4 164 SER 164 164 164 SER SER F . n 
E 4 165 GLU 165 165 165 GLU GLU F . n 
E 4 166 ALA 166 166 166 ALA ALA F . n 
E 4 167 SER 167 167 167 SER SER F . n 
E 4 168 GLU 168 168 168 GLU GLU F . n 
E 4 169 LEU 169 169 169 LEU LEU F . n 
E 4 170 LEU 170 170 170 LEU LEU F . n 
E 4 171 ASP 171 171 171 ASP ASP F . n 
E 4 172 PHE 172 172 172 PHE PHE F . n 
E 4 173 ILE 173 173 173 ILE ILE F . n 
E 4 174 ASP 174 174 174 ASP ASP F . n 
E 4 175 GLU 175 175 175 GLU GLU F . n 
E 4 176 GLN 176 176 176 GLN GLN F . n 
E 4 177 GLY 177 177 177 GLY GLY F . n 
E 4 178 GLN 178 178 178 GLN GLN F . n 
E 4 179 VAL 179 179 179 VAL VAL F . n 
E 4 180 HIS 180 180 180 HIS HIS F . n 
E 4 181 VAL 181 181 181 VAL VAL F . n 
E 4 182 ILE 182 182 182 ILE ILE F . n 
E 4 183 GLN 183 183 183 GLN GLN F . n 
E 4 184 LYS 184 184 184 LYS LYS F . n 
E 4 185 TYR 185 185 185 TYR TYR F . n 
E 4 186 LEU 186 186 186 LEU LEU F . n 
E 4 187 GLU 187 187 187 GLU GLU F . n 
E 4 188 LYS 188 188 188 LYS LYS F . n 
E 4 189 PRO 189 189 189 PRO PRO F . n 
E 4 190 LEU 190 190 190 LEU LEU F . n 
E 4 191 LEU 191 191 191 LEU LEU F . n 
E 4 192 LEU 192 192 192 LEU LEU F . n 
E 4 193 GLU 193 193 193 GLU GLU F . n 
E 4 194 PRO 194 194 194 PRO PRO F . n 
E 4 195 GLY 195 195 195 GLY GLY F . n 
E 4 196 HIS 196 196 196 HIS HIS F . n 
E 4 197 ARG 197 197 197 ARG ARG F . n 
E 4 198 LYS 198 198 198 LYS LYS F . n 
E 4 199 PHE 199 199 199 PHE PHE F . n 
E 4 200 ASP 200 200 200 ASP ASP F . n 
E 4 201 ILE 201 201 201 ILE ILE F . n 
E 4 202 ARG 202 202 202 ARG ARG F . n 
E 4 203 SER 203 203 203 SER SER F . n 
E 4 204 TRP 204 204 204 TRP TRP F . n 
E 4 205 VAL 205 205 205 VAL VAL F . n 
E 4 206 LEU 206 206 206 LEU LEU F . n 
E 4 207 VAL 207 207 207 VAL VAL F . n 
E 4 208 ASP 208 208 208 ASP ASP F . n 
E 4 209 HIS 209 209 209 HIS HIS F . n 
E 4 210 LEU 210 210 210 LEU LEU F . n 
E 4 211 TYR 211 211 211 TYR TYR F . n 
E 4 212 ASN 212 212 212 ASN ASN F . n 
E 4 213 ILE 213 213 213 ILE ILE F . n 
E 4 214 TYR 214 214 214 TYR TYR F . n 
E 4 215 LEU 215 215 215 LEU LEU F . n 
E 4 216 TYR 216 216 216 TYR TYR F . n 
E 4 217 ARG 217 217 217 ARG ARG F . n 
E 4 218 GLU 218 218 218 GLU GLU F . n 
E 4 219 GLY 219 219 219 GLY GLY F . n 
E 4 220 VAL 220 220 220 VAL VAL F . n 
E 4 221 LEU 221 221 221 LEU LEU F . n 
E 4 222 ARG 222 222 222 ARG ARG F . n 
E 4 223 THR 223 223 223 THR THR F . n 
E 4 224 SER 224 224 224 SER SER F . n 
E 4 225 SER 225 225 225 SER SER F . n 
E 4 226 GLU 226 226 226 GLU GLU F . n 
E 4 227 PRO 227 227 227 PRO PRO F . n 
E 4 228 TYR 228 228 228 TYR TYR F . n 
E 4 229 ASN 229 229 229 ASN ASN F . n 
E 4 230 SER 230 230 230 SER SER F . n 
E 4 231 ALA 231 231 231 ALA ALA F . n 
E 4 232 ASN 232 232 232 ASN ASN F . n 
E 4 233 PHE 233 233 233 PHE PHE F . n 
E 4 234 GLN 234 234 234 GLN GLN F . n 
E 4 235 ASP 235 235 235 ASP ASP F . n 
E 4 236 LYS 236 236 236 LYS LYS F . n 
E 4 237 THR 237 237 237 THR THR F . n 
E 4 238 CYS 238 238 238 CYS CYS F . n 
E 4 239 HIS 239 239 239 HIS HIS F . n 
E 4 240 LEU 240 240 240 LEU LEU F . n 
E 4 241 THR 241 241 241 THR THR F . n 
E 4 242 ASN 242 242 242 ASN ASN F . n 
E 4 243 HIS 243 243 243 HIS HIS F . n 
E 4 244 CYS 244 244 244 CYS CYS F . n 
E 4 245 ILE 245 245 245 ILE ILE F . n 
E 4 246 GLN 246 246 246 GLN GLN F . n 
E 4 247 LYS 247 247 247 LYS LYS F . n 
E 4 248 GLU 248 248 248 GLU GLU F . n 
E 4 249 TYR 249 249 249 TYR TYR F . n 
E 4 250 SER 250 250 250 SER SER F . n 
E 4 251 LYS 251 251 ?   ?   ?   F . n 
E 4 252 ASN 252 252 ?   ?   ?   F . n 
E 4 253 TYR 253 253 ?   ?   ?   F . n 
E 4 254 GLY 254 254 ?   ?   ?   F . n 
E 4 255 ARG 255 255 255 ARG ARG F . n 
E 4 256 TYR 256 256 256 TYR TYR F . n 
E 4 257 GLU 257 257 257 GLU GLU F . n 
E 4 258 GLU 258 258 258 GLU GLU F . n 
E 4 259 GLY 259 259 259 GLY GLY F . n 
E 4 260 ASN 260 260 260 ASN ASN F . n 
E 4 261 GLU 261 261 261 GLU GLU F . n 
E 4 262 MET 262 262 262 MET MET F . n 
E 4 263 PHE 263 263 263 PHE PHE F . n 
E 4 264 PHE 264 264 264 PHE PHE F . n 
E 4 265 GLU 265 265 265 GLU GLU F . n 
E 4 266 GLU 266 266 266 GLU GLU F . n 
E 4 267 PHE 267 267 267 PHE PHE F . n 
E 4 268 ASN 268 268 268 ASN ASN F . n 
E 4 269 GLN 269 269 269 GLN GLN F . n 
E 4 270 TYR 270 270 270 TYR TYR F . n 
E 4 271 LEU 271 271 271 LEU LEU F . n 
E 4 272 MET 272 272 272 MET MET F . n 
E 4 273 ASP 273 273 273 ASP ASP F . n 
E 4 274 ALA 274 274 274 ALA ALA F . n 
E 4 275 LEU 275 275 275 LEU LEU F . n 
E 4 276 ASN 276 276 276 ASN ASN F . n 
E 4 277 THR 277 277 277 THR THR F . n 
E 4 278 THR 278 278 278 THR THR F . n 
E 4 279 LEU 279 279 279 LEU LEU F . n 
E 4 280 GLU 280 280 280 GLU GLU F . n 
E 4 281 ASN 281 281 281 ASN ASN F . n 
E 4 282 SER 282 282 282 SER SER F . n 
E 4 283 ILE 283 283 283 ILE ILE F . n 
E 4 284 LEU 284 284 284 LEU LEU F . n 
E 4 285 LEU 285 285 285 LEU LEU F . n 
E 4 286 GLN 286 286 286 GLN GLN F . n 
E 4 287 ILE 287 287 287 ILE ILE F . n 
E 4 288 LYS 288 288 288 LYS LYS F . n 
E 4 289 HIS 289 289 289 HIS HIS F . n 
E 4 290 ILE 290 290 290 ILE ILE F . n 
E 4 291 ILE 291 291 291 ILE ILE F . n 
E 4 292 ARG 292 292 292 ARG ARG F . n 
E 4 293 SER 293 293 293 SER SER F . n 
E 4 294 CYS 294 294 294 CYS CYS F . n 
E 4 295 LEU 295 295 295 LEU LEU F . n 
E 4 296 MET 296 296 296 MET MET F . n 
E 4 297 CYS 297 297 297 CYS CYS F . n 
E 4 298 ILE 298 298 298 ILE ILE F . n 
E 4 299 GLU 299 299 299 GLU GLU F . n 
E 4 300 PRO 300 300 300 PRO PRO F . n 
E 4 301 ALA 301 301 301 ALA ALA F . n 
E 4 302 ILE 302 302 302 ILE ILE F . n 
E 4 303 SER 303 303 303 SER SER F . n 
E 4 304 THR 304 304 304 THR THR F . n 
E 4 305 LYS 305 305 305 LYS LYS F . n 
E 4 306 HIS 306 306 306 HIS HIS F . n 
E 4 307 LEU 307 307 307 LEU LEU F . n 
E 4 308 HIS 308 308 308 HIS HIS F . n 
E 4 309 TYR 309 309 309 TYR TYR F . n 
E 4 310 GLN 310 310 310 GLN GLN F . n 
E 4 311 SER 311 311 311 SER SER F . n 
E 4 312 PHE 312 312 312 PHE PHE F . n 
E 4 313 GLN 313 313 313 GLN GLN F . n 
E 4 314 LEU 314 314 314 LEU LEU F . n 
E 4 315 PHE 315 315 315 PHE PHE F . n 
E 4 316 GLY 316 316 316 GLY GLY F . n 
E 4 317 PHE 317 317 317 PHE PHE F . n 
E 4 318 ASP 318 318 318 ASP ASP F . n 
E 4 319 PHE 319 319 319 PHE PHE F . n 
E 4 320 MET 320 320 320 MET MET F . n 
E 4 321 VAL 321 321 321 VAL VAL F . n 
E 4 322 ASP 322 322 322 ASP ASP F . n 
E 4 323 GLU 323 323 323 GLU GLU F . n 
E 4 324 GLU 324 324 324 GLU GLU F . n 
E 4 325 LEU 325 325 325 LEU LEU F . n 
E 4 326 LYS 326 326 326 LYS LYS F . n 
E 4 327 VAL 327 327 327 VAL VAL F . n 
E 4 328 TRP 328 328 328 TRP TRP F . n 
E 4 329 LEU 329 329 329 LEU LEU F . n 
E 4 330 ILE 330 330 330 ILE ILE F . n 
E 4 331 GLU 331 331 331 GLU GLU F . n 
E 4 332 VAL 332 332 332 VAL VAL F . n 
E 4 333 ASN 333 333 333 ASN ASN F . n 
E 4 334 GLY 334 334 334 GLY GLY F . n 
E 4 335 ALA 335 335 335 ALA ALA F . n 
E 4 336 PRO 336 336 336 PRO PRO F . n 
E 4 337 ALA 337 337 337 ALA ALA F . n 
E 4 338 CYS 338 338 338 CYS CYS F . n 
E 4 339 ALA 339 339 339 ALA ALA F . n 
E 4 340 GLN 340 340 340 GLN GLN F . n 
E 4 341 LYS 341 341 341 LYS LYS F . n 
E 4 342 LEU 342 342 342 LEU LEU F . n 
E 4 343 TYR 343 343 343 TYR TYR F . n 
E 4 344 ALA 344 344 344 ALA ALA F . n 
E 4 345 GLU 345 345 345 GLU GLU F . n 
E 4 346 LEU 346 346 346 LEU LEU F . n 
E 4 347 CYS 347 347 347 CYS CYS F . n 
E 4 348 GLN 348 348 348 GLN GLN F . n 
E 4 349 GLY 349 349 349 GLY GLY F . n 
E 4 350 ILE 350 350 350 ILE ILE F . n 
E 4 351 VAL 351 351 351 VAL VAL F . n 
E 4 352 ASP 352 352 352 ASP ASP F . n 
E 4 353 VAL 353 353 353 VAL VAL F . n 
E 4 354 ALA 354 354 354 ALA ALA F . n 
E 4 355 ILE 355 355 355 ILE ILE F . n 
E 4 356 SER 356 356 356 SER SER F . n 
E 4 357 SER 357 357 357 SER SER F . n 
E 4 358 VAL 358 358 358 VAL VAL F . n 
E 4 359 PHE 359 359 359 PHE PHE F . n 
E 4 360 PRO 360 360 360 PRO PRO F . n 
E 4 361 LEU 361 361 361 LEU LEU F . n 
E 4 362 ALA 362 362 362 ALA ALA F . n 
E 4 363 ASP 363 363 ?   ?   ?   F . n 
E 4 364 THR 364 364 ?   ?   ?   F . n 
E 4 365 GLY 365 365 ?   ?   ?   F . n 
E 4 366 GLN 366 366 ?   ?   ?   F . n 
E 4 367 LYS 367 367 ?   ?   ?   F . n 
E 4 368 THR 368 368 ?   ?   ?   F . n 
E 4 369 SER 369 369 ?   ?   ?   F . n 
E 4 370 GLN 370 370 ?   ?   ?   F . n 
E 4 371 PRO 371 371 ?   ?   ?   F . n 
E 4 372 THR 372 372 372 THR THR F . n 
E 4 373 SER 373 373 373 SER SER F . n 
E 4 374 ILE 374 374 374 ILE ILE F . n 
E 4 375 PHE 375 375 375 PHE PHE F . n 
E 4 376 ILE 376 376 376 ILE ILE F . n 
E 4 377 LYS 377 377 377 LYS LYS F . n 
E 4 378 LEU 378 378 378 LEU LEU F . n 
E 4 379 HIS 379 379 379 HIS HIS F . n 
E 4 380 HIS 380 380 380 HIS HIS F . n 
E 4 381 HIS 381 381 ?   ?   ?   F . n 
E 4 382 HIS 382 382 ?   ?   ?   F . n 
E 4 383 HIS 383 383 ?   ?   ?   F . n 
E 4 384 HIS 384 384 ?   ?   ?   F . n 
F 2 1   MET 1   1   1   MET MET B . n 
F 2 2   ARG 2   2   2   ARG ARG B . n 
F 2 3   GLU 3   3   3   GLU GLU B . n 
F 2 4   ILE 4   4   4   ILE ILE B . n 
F 2 5   VAL 5   5   5   VAL VAL B . n 
F 2 6   HIS 6   6   6   HIS HIS B . n 
F 2 7   ILE 7   7   7   ILE ILE B . n 
F 2 8   GLN 8   8   8   GLN GLN B . n 
F 2 9   ALA 9   9   9   ALA ALA B . n 
F 2 10  GLY 10  10  10  GLY GLY B . n 
F 2 11  GLN 11  11  11  GLN GLN B . n 
F 2 12  CYS 12  12  12  CYS CYS B . n 
F 2 13  GLY 13  13  13  GLY GLY B . n 
F 2 14  ASN 14  14  14  ASN ASN B . n 
F 2 15  GLN 15  15  15  GLN GLN B . n 
F 2 16  ILE 16  16  16  ILE ILE B . n 
F 2 17  GLY 17  17  17  GLY GLY B . n 
F 2 18  ALA 18  18  18  ALA ALA B . n 
F 2 19  LYS 19  19  19  LYS LYS B . n 
F 2 20  PHE 20  20  20  PHE PHE B . n 
F 2 21  TRP 21  21  21  TRP TRP B . n 
F 2 22  GLU 22  22  22  GLU GLU B . n 
F 2 23  VAL 23  23  23  VAL VAL B . n 
F 2 24  ILE 24  24  24  ILE ILE B . n 
F 2 25  SER 25  25  25  SER SER B . n 
F 2 26  ASP 26  26  26  ASP ASP B . n 
F 2 27  GLU 27  27  27  GLU GLU B . n 
F 2 28  HIS 28  28  28  HIS HIS B . n 
F 2 29  GLY 29  29  29  GLY GLY B . n 
F 2 30  ILE 30  30  30  ILE ILE B . n 
F 2 31  ASP 31  31  31  ASP ASP B . n 
F 2 32  PRO 32  32  32  PRO PRO B . n 
F 2 33  THR 33  33  33  THR THR B . n 
F 2 34  GLY 34  34  34  GLY GLY B . n 
F 2 35  SER 35  35  35  SER SER B . n 
F 2 36  TYR 36  36  36  TYR TYR B . n 
F 2 37  HIS 37  37  37  HIS HIS B . n 
F 2 38  GLY 38  38  38  GLY GLY B . n 
F 2 39  ASP 39  39  39  ASP ASP B . n 
F 2 40  SER 40  40  40  SER SER B . n 
F 2 41  ASP 41  41  41  ASP ASP B . n 
F 2 42  LEU 42  42  42  LEU LEU B . n 
F 2 43  GLN 43  45  45  GLN GLN B . n 
F 2 44  LEU 44  46  46  LEU LEU B . n 
F 2 45  GLU 45  47  47  GLU GLU B . n 
F 2 46  ARG 46  48  48  ARG ARG B . n 
F 2 47  ILE 47  49  49  ILE ILE B . n 
F 2 48  ASN 48  50  50  ASN ASN B . n 
F 2 49  VAL 49  51  51  VAL VAL B . n 
F 2 50  TYR 50  52  52  TYR TYR B . n 
F 2 51  TYR 51  53  53  TYR TYR B . n 
F 2 52  ASN 52  54  54  ASN ASN B . n 
F 2 53  GLU 53  55  55  GLU GLU B . n 
F 2 54  ALA 54  56  56  ALA ALA B . n 
F 2 55  THR 55  57  57  THR THR B . n 
F 2 56  GLY 56  58  58  GLY GLY B . n 
F 2 57  ASN 57  59  59  ASN ASN B . n 
F 2 58  LYS 58  60  60  LYS LYS B . n 
F 2 59  TYR 59  61  61  TYR TYR B . n 
F 2 60  VAL 60  62  62  VAL VAL B . n 
F 2 61  PRO 61  63  63  PRO PRO B . n 
F 2 62  ARG 62  64  64  ARG ARG B . n 
F 2 63  ALA 63  65  65  ALA ALA B . n 
F 2 64  ILE 64  66  66  ILE ILE B . n 
F 2 65  LEU 65  67  67  LEU LEU B . n 
F 2 66  VAL 66  68  68  VAL VAL B . n 
F 2 67  ASP 67  69  69  ASP ASP B . n 
F 2 68  LEU 68  70  70  LEU LEU B . n 
F 2 69  GLU 69  71  71  GLU GLU B . n 
F 2 70  PRO 70  72  72  PRO PRO B . n 
F 2 71  GLY 71  73  73  GLY GLY B . n 
F 2 72  THR 72  74  74  THR THR B . n 
F 2 73  MET 73  75  75  MET MET B . n 
F 2 74  ASP 74  76  76  ASP ASP B . n 
F 2 75  SER 75  77  77  SER SER B . n 
F 2 76  VAL 76  78  78  VAL VAL B . n 
F 2 77  ARG 77  79  79  ARG ARG B . n 
F 2 78  SER 78  80  80  SER SER B . n 
F 2 79  GLY 79  81  81  GLY GLY B . n 
F 2 80  PRO 80  82  82  PRO PRO B . n 
F 2 81  PHE 81  83  83  PHE PHE B . n 
F 2 82  GLY 82  84  84  GLY GLY B . n 
F 2 83  GLN 83  85  85  GLN GLN B . n 
F 2 84  ILE 84  86  86  ILE ILE B . n 
F 2 85  PHE 85  87  87  PHE PHE B . n 
F 2 86  ARG 86  88  88  ARG ARG B . n 
F 2 87  PRO 87  89  89  PRO PRO B . n 
F 2 88  ASP 88  90  90  ASP ASP B . n 
F 2 89  ASN 89  91  91  ASN ASN B . n 
F 2 90  PHE 90  92  92  PHE PHE B . n 
F 2 91  VAL 91  93  93  VAL VAL B . n 
F 2 92  PHE 92  94  94  PHE PHE B . n 
F 2 93  GLY 93  95  95  GLY GLY B . n 
F 2 94  GLN 94  96  96  GLN GLN B . n 
F 2 95  SER 95  97  97  SER SER B . n 
F 2 96  GLY 96  98  98  GLY GLY B . n 
F 2 97  ALA 97  99  99  ALA ALA B . n 
F 2 98  GLY 98  100 100 GLY GLY B . n 
F 2 99  ASN 99  101 101 ASN ASN B . n 
F 2 100 ASN 100 102 102 ASN ASN B . n 
F 2 101 TRP 101 103 103 TRP TRP B . n 
F 2 102 ALA 102 104 104 ALA ALA B . n 
F 2 103 LYS 103 105 105 LYS LYS B . n 
F 2 104 GLY 104 106 106 GLY GLY B . n 
F 2 105 HIS 105 107 107 HIS HIS B . n 
F 2 106 TYR 106 108 108 TYR TYR B . n 
F 2 107 THR 107 109 109 THR THR B . n 
F 2 108 GLU 108 110 110 GLU GLU B . n 
F 2 109 GLY 109 111 111 GLY GLY B . n 
F 2 110 ALA 110 112 112 ALA ALA B . n 
F 2 111 GLU 111 113 113 GLU GLU B . n 
F 2 112 LEU 112 114 114 LEU LEU B . n 
F 2 113 VAL 113 115 115 VAL VAL B . n 
F 2 114 ASP 114 116 116 ASP ASP B . n 
F 2 115 SER 115 117 117 SER SER B . n 
F 2 116 VAL 116 118 118 VAL VAL B . n 
F 2 117 LEU 117 119 119 LEU LEU B . n 
F 2 118 ASP 118 120 120 ASP ASP B . n 
F 2 119 VAL 119 121 121 VAL VAL B . n 
F 2 120 VAL 120 122 122 VAL VAL B . n 
F 2 121 ARG 121 123 123 ARG ARG B . n 
F 2 122 LYS 122 124 124 LYS LYS B . n 
F 2 123 GLU 123 125 125 GLU GLU B . n 
F 2 124 SER 124 126 126 SER SER B . n 
F 2 125 GLU 125 127 127 GLU GLU B . n 
F 2 126 SER 126 128 128 SER SER B . n 
F 2 127 CYS 127 129 129 CYS CYS B . n 
F 2 128 ASP 128 130 130 ASP ASP B . n 
F 2 129 CYS 129 131 131 CYS CYS B . n 
F 2 130 LEU 130 132 132 LEU LEU B . n 
F 2 131 GLN 131 133 133 GLN GLN B . n 
F 2 132 GLY 132 134 134 GLY GLY B . n 
F 2 133 PHE 133 135 135 PHE PHE B . n 
F 2 134 GLN 134 136 136 GLN GLN B . n 
F 2 135 LEU 135 137 137 LEU LEU B . n 
F 2 136 THR 136 138 138 THR THR B . n 
F 2 137 HIS 137 139 139 HIS HIS B . n 
F 2 138 SER 138 140 140 SER SER B . n 
F 2 139 LEU 139 141 141 LEU LEU B . n 
F 2 140 GLY 140 142 142 GLY GLY B . n 
F 2 141 GLY 141 143 143 GLY GLY B . n 
F 2 142 GLY 142 144 144 GLY GLY B . n 
F 2 143 THR 143 145 145 THR THR B . n 
F 2 144 GLY 144 146 146 GLY GLY B . n 
F 2 145 SER 145 147 147 SER SER B . n 
F 2 146 GLY 146 148 148 GLY GLY B . n 
F 2 147 MET 147 149 149 MET MET B . n 
F 2 148 GLY 148 150 150 GLY GLY B . n 
F 2 149 THR 149 151 151 THR THR B . n 
F 2 150 LEU 150 152 152 LEU LEU B . n 
F 2 151 LEU 151 153 153 LEU LEU B . n 
F 2 152 ILE 152 154 154 ILE ILE B . n 
F 2 153 SER 153 155 155 SER SER B . n 
F 2 154 LYS 154 156 156 LYS LYS B . n 
F 2 155 ILE 155 157 157 ILE ILE B . n 
F 2 156 ARG 156 158 158 ARG ARG B . n 
F 2 157 GLU 157 159 159 GLU GLU B . n 
F 2 158 GLU 158 160 160 GLU GLU B . n 
F 2 159 TYR 159 161 161 TYR TYR B . n 
F 2 160 PRO 160 162 162 PRO PRO B . n 
F 2 161 ASP 161 163 163 ASP ASP B . n 
F 2 162 ARG 162 164 164 ARG ARG B . n 
F 2 163 ILE 163 165 165 ILE ILE B . n 
F 2 164 MET 164 166 166 MET MET B . n 
F 2 165 ASN 165 167 167 ASN ASN B . n 
F 2 166 THR 166 168 168 THR THR B . n 
F 2 167 PHE 167 169 169 PHE PHE B . n 
F 2 168 SER 168 170 170 SER SER B . n 
F 2 169 VAL 169 171 171 VAL VAL B . n 
F 2 170 MET 170 172 172 MET MET B . n 
F 2 171 PRO 171 173 173 PRO PRO B . n 
F 2 172 SER 172 174 174 SER SER B . n 
F 2 173 PRO 173 175 175 PRO PRO B . n 
F 2 174 LYS 174 176 176 LYS LYS B . n 
F 2 175 VAL 175 177 177 VAL VAL B . n 
F 2 176 SER 176 178 178 SER SER B . n 
F 2 177 ASP 177 179 179 ASP ASP B . n 
F 2 178 THR 178 180 180 THR THR B . n 
F 2 179 VAL 179 181 181 VAL VAL B . n 
F 2 180 VAL 180 182 182 VAL VAL B . n 
F 2 181 GLU 181 183 183 GLU GLU B . n 
F 2 182 PRO 182 184 184 PRO PRO B . n 
F 2 183 TYR 183 185 185 TYR TYR B . n 
F 2 184 ASN 184 186 186 ASN ASN B . n 
F 2 185 ALA 185 187 187 ALA ALA B . n 
F 2 186 THR 186 188 188 THR THR B . n 
F 2 187 LEU 187 189 189 LEU LEU B . n 
F 2 188 SER 188 190 190 SER SER B . n 
F 2 189 VAL 189 191 191 VAL VAL B . n 
F 2 190 HIS 190 192 192 HIS HIS B . n 
F 2 191 GLN 191 193 193 GLN GLN B . n 
F 2 192 LEU 192 194 194 LEU LEU B . n 
F 2 193 VAL 193 195 195 VAL VAL B . n 
F 2 194 GLU 194 196 196 GLU GLU B . n 
F 2 195 ASN 195 197 197 ASN ASN B . n 
F 2 196 THR 196 198 198 THR THR B . n 
F 2 197 ASP 197 199 199 ASP ASP B . n 
F 2 198 GLU 198 200 200 GLU GLU B . n 
F 2 199 THR 199 201 201 THR THR B . n 
F 2 200 TYR 200 202 202 TYR TYR B . n 
F 2 201 CYS 201 203 203 CYS CYS B . n 
F 2 202 ILE 202 204 204 ILE ILE B . n 
F 2 203 ASP 203 205 205 ASP ASP B . n 
F 2 204 ASN 204 206 206 ASN ASN B . n 
F 2 205 GLU 205 207 207 GLU GLU B . n 
F 2 206 ALA 206 208 208 ALA ALA B . n 
F 2 207 LEU 207 209 209 LEU LEU B . n 
F 2 208 TYR 208 210 210 TYR TYR B . n 
F 2 209 ASP 209 211 211 ASP ASP B . n 
F 2 210 ILE 210 212 212 ILE ILE B . n 
F 2 211 CYS 211 213 213 CYS CYS B . n 
F 2 212 PHE 212 214 214 PHE PHE B . n 
F 2 213 ARG 213 215 215 ARG ARG B . n 
F 2 214 THR 214 216 216 THR THR B . n 
F 2 215 LEU 215 217 217 LEU LEU B . n 
F 2 216 LYS 216 218 218 LYS LYS B . n 
F 2 217 LEU 217 219 219 LEU LEU B . n 
F 2 218 THR 218 220 220 THR THR B . n 
F 2 219 THR 219 221 221 THR THR B . n 
F 2 220 PRO 220 222 222 PRO PRO B . n 
F 2 221 THR 221 223 223 THR THR B . n 
F 2 222 TYR 222 224 224 TYR TYR B . n 
F 2 223 GLY 223 225 225 GLY GLY B . n 
F 2 224 ASP 224 226 226 ASP ASP B . n 
F 2 225 LEU 225 227 227 LEU LEU B . n 
F 2 226 ASN 226 228 228 ASN ASN B . n 
F 2 227 HIS 227 229 229 HIS HIS B . n 
F 2 228 LEU 228 230 230 LEU LEU B . n 
F 2 229 VAL 229 231 231 VAL VAL B . n 
F 2 230 SER 230 232 232 SER SER B . n 
F 2 231 ALA 231 233 233 ALA ALA B . n 
F 2 232 THR 232 234 234 THR THR B . n 
F 2 233 MET 233 235 235 MET MET B . n 
F 2 234 SER 234 236 236 SER SER B . n 
F 2 235 GLY 235 237 237 GLY GLY B . n 
F 2 236 VAL 236 238 238 VAL VAL B . n 
F 2 237 THR 237 239 239 THR THR B . n 
F 2 238 THR 238 240 240 THR THR B . n 
F 2 239 CYS 239 241 241 CYS CYS B . n 
F 2 240 LEU 240 242 242 LEU LEU B . n 
F 2 241 ARG 241 243 243 ARG ARG B . n 
F 2 242 PHE 242 244 244 PHE PHE B . n 
F 2 243 PRO 243 245 245 PRO PRO B . n 
F 2 244 GLY 244 246 246 GLY GLY B . n 
F 2 245 GLN 245 247 247 GLN GLN B . n 
F 2 246 LEU 246 248 248 LEU LEU B . n 
F 2 247 ASN 247 249 249 ASN ASN B . n 
F 2 248 ALA 248 250 250 ALA ALA B . n 
F 2 249 ASP 249 251 251 ASP ASP B . n 
F 2 250 LEU 250 252 252 LEU LEU B . n 
F 2 251 ARG 251 253 253 ARG ARG B . n 
F 2 252 LYS 252 254 254 LYS LYS B . n 
F 2 253 LEU 253 255 255 LEU LEU B . n 
F 2 254 ALA 254 256 256 ALA ALA B . n 
F 2 255 VAL 255 257 257 VAL VAL B . n 
F 2 256 ASN 256 258 258 ASN ASN B . n 
F 2 257 MET 257 259 259 MET MET B . n 
F 2 258 VAL 258 260 260 VAL VAL B . n 
F 2 259 PRO 259 261 261 PRO PRO B . n 
F 2 260 PHE 260 262 262 PHE PHE B . n 
F 2 261 PRO 261 263 263 PRO PRO B . n 
F 2 262 ARG 262 264 264 ARG ARG B . n 
F 2 263 LEU 263 265 265 LEU LEU B . n 
F 2 264 HIS 264 266 266 HIS HIS B . n 
F 2 265 PHE 265 267 267 PHE PHE B . n 
F 2 266 PHE 266 268 268 PHE PHE B . n 
F 2 267 MET 267 269 269 MET MET B . n 
F 2 268 PRO 268 270 270 PRO PRO B . n 
F 2 269 GLY 269 271 271 GLY GLY B . n 
F 2 270 PHE 270 272 272 PHE PHE B . n 
F 2 271 ALA 271 273 273 ALA ALA B . n 
F 2 272 PRO 272 274 274 PRO PRO B . n 
F 2 273 LEU 273 275 275 LEU LEU B . n 
F 2 274 THR 274 276 276 THR THR B . n 
F 2 275 SER 275 277 277 SER SER B . n 
F 2 276 ARG 276 278 278 ARG ARG B . n 
F 2 277 GLY 277 279 279 GLY GLY B . n 
F 2 278 SER 278 280 280 SER SER B . n 
F 2 279 GLN 279 281 281 GLN GLN B . n 
F 2 280 GLN 280 282 282 GLN GLN B . n 
F 2 281 TYR 281 283 283 TYR TYR B . n 
F 2 282 ARG 282 284 284 ARG ARG B . n 
F 2 283 ALA 283 285 285 ALA ALA B . n 
F 2 284 LEU 284 286 286 LEU LEU B . n 
F 2 285 THR 285 287 287 THR THR B . n 
F 2 286 VAL 286 288 288 VAL VAL B . n 
F 2 287 PRO 287 289 289 PRO PRO B . n 
F 2 288 GLU 288 290 290 GLU GLU B . n 
F 2 289 LEU 289 291 291 LEU LEU B . n 
F 2 290 THR 290 292 292 THR THR B . n 
F 2 291 GLN 291 293 293 GLN GLN B . n 
F 2 292 GLN 292 294 294 GLN GLN B . n 
F 2 293 MET 293 295 295 MET MET B . n 
F 2 294 PHE 294 296 296 PHE PHE B . n 
F 2 295 ASP 295 297 297 ASP ASP B . n 
F 2 296 SER 296 298 298 SER SER B . n 
F 2 297 LYS 297 299 299 LYS LYS B . n 
F 2 298 ASN 298 300 300 ASN ASN B . n 
F 2 299 MET 299 301 301 MET MET B . n 
F 2 300 MET 300 302 302 MET MET B . n 
F 2 301 ALA 301 303 303 ALA ALA B . n 
F 2 302 ALA 302 304 304 ALA ALA B . n 
F 2 303 CYS 303 305 305 CYS CYS B . n 
F 2 304 ASP 304 306 306 ASP ASP B . n 
F 2 305 PRO 305 307 307 PRO PRO B . n 
F 2 306 ARG 306 308 308 ARG ARG B . n 
F 2 307 HIS 307 309 309 HIS HIS B . n 
F 2 308 GLY 308 310 310 GLY GLY B . n 
F 2 309 ARG 309 311 311 ARG ARG B . n 
F 2 310 TYR 310 312 312 TYR TYR B . n 
F 2 311 LEU 311 313 313 LEU LEU B . n 
F 2 312 THR 312 314 314 THR THR B . n 
F 2 313 VAL 313 315 315 VAL VAL B . n 
F 2 314 ALA 314 316 316 ALA ALA B . n 
F 2 315 ALA 315 317 317 ALA ALA B . n 
F 2 316 ILE 316 318 318 ILE ILE B . n 
F 2 317 PHE 317 319 319 PHE PHE B . n 
F 2 318 ARG 318 320 320 ARG ARG B . n 
F 2 319 GLY 319 321 321 GLY GLY B . n 
F 2 320 ARG 320 322 322 ARG ARG B . n 
F 2 321 MET 321 323 323 MET MET B . n 
F 2 322 SER 322 324 324 SER SER B . n 
F 2 323 MET 323 325 325 MET MET B . n 
F 2 324 LYS 324 326 326 LYS LYS B . n 
F 2 325 GLU 325 327 327 GLU GLU B . n 
F 2 326 VAL 326 328 328 VAL VAL B . n 
F 2 327 ASP 327 329 329 ASP ASP B . n 
F 2 328 GLU 328 330 330 GLU GLU B . n 
F 2 329 GLN 329 331 331 GLN GLN B . n 
F 2 330 MET 330 332 332 MET MET B . n 
F 2 331 LEU 331 333 333 LEU LEU B . n 
F 2 332 ASN 332 334 334 ASN ASN B . n 
F 2 333 VAL 333 335 335 VAL VAL B . n 
F 2 334 GLN 334 336 336 GLN GLN B . n 
F 2 335 ASN 335 337 337 ASN ASN B . n 
F 2 336 LYS 336 338 338 LYS LYS B . n 
F 2 337 ASN 337 339 339 ASN ASN B . n 
F 2 338 SER 338 340 340 SER SER B . n 
F 2 339 SER 339 341 341 SER SER B . n 
F 2 340 TYR 340 342 342 TYR TYR B . n 
F 2 341 PHE 341 343 343 PHE PHE B . n 
F 2 342 VAL 342 344 344 VAL VAL B . n 
F 2 343 GLU 343 345 345 GLU GLU B . n 
F 2 344 TRP 344 346 346 TRP TRP B . n 
F 2 345 ILE 345 347 347 ILE ILE B . n 
F 2 346 PRO 346 348 348 PRO PRO B . n 
F 2 347 ASN 347 349 349 ASN ASN B . n 
F 2 348 ASN 348 350 350 ASN ASN B . n 
F 2 349 VAL 349 351 351 VAL VAL B . n 
F 2 350 LYS 350 352 352 LYS LYS B . n 
F 2 351 THR 351 353 353 THR THR B . n 
F 2 352 ALA 352 354 354 ALA ALA B . n 
F 2 353 VAL 353 355 355 VAL VAL B . n 
F 2 354 CYS 354 356 356 CYS CYS B . n 
F 2 355 ASP 355 357 357 ASP ASP B . n 
F 2 356 ILE 356 358 358 ILE ILE B . n 
F 2 357 PRO 357 359 359 PRO PRO B . n 
F 2 358 PRO 358 360 360 PRO PRO B . n 
F 2 359 ARG 359 369 369 ARG ARG B . n 
F 2 360 GLY 360 370 370 GLY GLY B . n 
F 2 361 LEU 361 371 371 LEU LEU B . n 
F 2 362 LYS 362 372 372 LYS LYS B . n 
F 2 363 MET 363 373 373 MET MET B . n 
F 2 364 SER 364 374 374 SER SER B . n 
F 2 365 ALA 365 375 375 ALA ALA B . n 
F 2 366 THR 366 376 376 THR THR B . n 
F 2 367 PHE 367 377 377 PHE PHE B . n 
F 2 368 ILE 368 378 378 ILE ILE B . n 
F 2 369 GLY 369 379 379 GLY GLY B . n 
F 2 370 ASN 370 380 380 ASN ASN B . n 
F 2 371 SER 371 381 381 SER SER B . n 
F 2 372 THR 372 382 382 THR THR B . n 
F 2 373 ALA 373 383 383 ALA ALA B . n 
F 2 374 ILE 374 384 384 ILE ILE B . n 
F 2 375 GLN 375 385 385 GLN GLN B . n 
F 2 376 GLU 376 386 386 GLU GLU B . n 
F 2 377 LEU 377 387 387 LEU LEU B . n 
F 2 378 PHE 378 388 388 PHE PHE B . n 
F 2 379 LYS 379 389 389 LYS LYS B . n 
F 2 380 ARG 380 390 390 ARG ARG B . n 
F 2 381 ILE 381 391 391 ILE ILE B . n 
F 2 382 SER 382 392 392 SER SER B . n 
F 2 383 GLU 383 393 393 GLU GLU B . n 
F 2 384 GLN 384 394 394 GLN GLN B . n 
F 2 385 PHE 385 395 395 PHE PHE B . n 
F 2 386 THR 386 396 396 THR THR B . n 
F 2 387 ALA 387 397 397 ALA ALA B . n 
F 2 388 MET 388 398 398 MET MET B . n 
F 2 389 PHE 389 399 399 PHE PHE B . n 
F 2 390 ARG 390 400 400 ARG ARG B . n 
F 2 391 ARG 391 401 401 ARG ARG B . n 
F 2 392 LYS 392 402 402 LYS LYS B . n 
F 2 393 ALA 393 403 403 ALA ALA B . n 
F 2 394 PHE 394 404 404 PHE PHE B . n 
F 2 395 LEU 395 405 405 LEU LEU B . n 
F 2 396 HIS 396 406 406 HIS HIS B . n 
F 2 397 TRP 397 407 407 TRP TRP B . n 
F 2 398 TYR 398 408 408 TYR TYR B . n 
F 2 399 THR 399 409 409 THR THR B . n 
F 2 400 GLY 400 410 410 GLY GLY B . n 
F 2 401 GLU 401 411 411 GLU GLU B . n 
F 2 402 GLY 402 412 412 GLY GLY B . n 
F 2 403 MET 403 413 413 MET MET B . n 
F 2 404 ASP 404 414 414 ASP ASP B . n 
F 2 405 GLU 405 415 415 GLU GLU B . n 
F 2 406 MET 406 416 416 MET MET B . n 
F 2 407 GLU 407 417 417 GLU GLU B . n 
F 2 408 PHE 408 418 418 PHE PHE B . n 
F 2 409 THR 409 419 419 THR THR B . n 
F 2 410 GLU 410 420 420 GLU GLU B . n 
F 2 411 ALA 411 421 421 ALA ALA B . n 
F 2 412 GLU 412 422 422 GLU GLU B . n 
F 2 413 SER 413 423 423 SER SER B . n 
F 2 414 ASN 414 424 424 ASN ASN B . n 
F 2 415 MET 415 425 425 MET MET B . n 
F 2 416 ASN 416 426 426 ASN ASN B . n 
F 2 417 ASP 417 427 427 ASP ASP B . n 
F 2 418 LEU 418 428 428 LEU LEU B . n 
F 2 419 VAL 419 429 429 VAL VAL B . n 
F 2 420 SER 420 430 430 SER SER B . n 
F 2 421 GLU 421 431 431 GLU GLU B . n 
F 2 422 TYR 422 432 432 TYR TYR B . n 
F 2 423 GLN 423 433 433 GLN GLN B . n 
F 2 424 GLN 424 434 434 GLN GLN B . n 
F 2 425 TYR 425 435 435 TYR TYR B . n 
F 2 426 GLN 426 436 436 GLN GLN B . n 
F 2 427 ASP 427 437 437 ASP ASP B . n 
F 2 428 ALA 428 438 438 ALA ALA B . n 
F 2 429 THR 429 439 ?   ?   ?   B . n 
F 2 430 ALA 430 440 ?   ?   ?   B . n 
F 2 431 ASP 431 441 ?   ?   ?   B . n 
F 2 432 GLU 432 442 ?   ?   ?   B . n 
F 2 433 GLN 433 443 ?   ?   ?   B . n 
F 2 434 GLY 434 444 ?   ?   ?   B . n 
F 2 435 GLU 435 445 ?   ?   ?   B . n 
F 2 436 PHE 436 446 ?   ?   ?   B . n 
F 2 437 GLU 437 447 ?   ?   ?   B . n 
F 2 438 GLU 438 448 ?   ?   ?   B . n 
F 2 439 GLU 439 449 ?   ?   ?   B . n 
F 2 440 GLU 440 450 ?   ?   ?   B . n 
F 2 441 GLY 441 451 ?   ?   ?   B . n 
F 2 442 GLU 442 452 ?   ?   ?   B . n 
F 2 443 ASP 443 453 ?   ?   ?   B . n 
F 2 444 GLU 444 454 ?   ?   ?   B . n 
F 2 445 ALA 445 455 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EPR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EPR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 5  GTP   1 501 501 GTP   GTP A . 
H 6  MG    1 502 502 MG    MG  A . 
I 7  CA    1 503 503 CA    CA  A . 
J 5  GTP   1 501 502 GTP   GTP C . 
K 6  MG    1 502 503 MG    MG  C . 
L 7  CA    1 503 504 CA    CA  C . 
M 8  A1EPR 1 504 502 A1EPR LIG C . 
N 9  GDP   1 501 501 GDP   GDP D . 
O 9  GDP   1 501 501 GDP   GDP B . 
P 10 HOH   1 601 7   HOH   HOH C . 
P 10 HOH   2 602 15  HOH   HOH C . 
P 10 HOH   3 603 1   HOH   HOH C . 
P 10 HOH   4 604 14  HOH   HOH C . 
P 10 HOH   5 605 8   HOH   HOH C . 
P 10 HOH   6 606 5   HOH   HOH C . 
Q 10 HOH   1 601 4   HOH   HOH B . 
Q 10 HOH   2 602 12  HOH   HOH B . 
Q 10 HOH   3 603 11  HOH   HOH B . 
Q 10 HOH   4 604 10  HOH   HOH B . 
Q 10 HOH   5 605 9   HOH   HOH B . 
Q 10 HOH   6 606 13  HOH   HOH B . 
Q 10 HOH   7 607 3   HOH   HOH B . 
Q 10 HOH   8 608 2   HOH   HOH B . 
Q 10 HOH   9 609 6   HOH   HOH B . 
# 
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 0 A LEU 136 ? CA  B A LEU 136 CA  
2  1 Y 0 A LEU 136 ? CB  B A LEU 136 CB  
3  1 Y 0 A LEU 136 ? CG  B A LEU 136 CG  
4  1 Y 0 A LEU 136 ? CD1 B A LEU 136 CD1 
5  1 Y 0 A LEU 136 ? CD2 B A LEU 136 CD2 
6  1 Y 1 A GLU 284 ? CG  ? A GLU 284 CG  
7  1 Y 1 A GLU 284 ? CD  ? A GLU 284 CD  
8  1 Y 1 A GLU 284 ? OE1 ? A GLU 284 OE1 
9  1 Y 1 A GLU 284 ? OE2 ? A GLU 284 OE2 
10 1 Y 0 C THR 194 ? CA  B B THR 194 CA  
11 1 Y 0 C THR 194 ? CB  B B THR 194 CB  
12 1 Y 0 C THR 194 ? OG1 B B THR 194 OG1 
13 1 Y 0 C THR 194 ? CG2 B B THR 194 CG2 
14 1 Y 0 C VAL 363 ? CA  B B VAL 363 CA  
15 1 Y 0 C VAL 363 ? CB  B B VAL 363 CB  
16 1 Y 0 C VAL 363 ? CG1 B B VAL 363 CG1 
17 1 Y 0 C VAL 363 ? CG2 B B VAL 363 CG2 
18 1 Y 0 D SER 155 ? CA  A C SER 153 CA  
19 1 Y 0 D SER 155 ? CB  A C SER 153 CB  
20 1 Y 0 D SER 155 ? OG  A C SER 153 OG  
21 1 Y 0 D THR 240 ? CA  A C THR 238 CA  
22 1 Y 0 D THR 240 ? CB  A C THR 238 CB  
23 1 Y 0 D THR 240 ? OG1 A C THR 238 OG1 
24 1 Y 0 D THR 240 ? CG2 A C THR 238 CG2 
25 1 Y 0 D ILE 318 ? CD1 ? C ILE 316 CD1 
26 1 Y 0 D ASN 334 ? CG  ? C ASN 332 CG  
27 1 Y 1 D LYS 338 ? CG  ? C LYS 336 CG  
28 1 Y 1 D LYS 338 ? CD  ? C LYS 336 CD  
29 1 Y 1 D LYS 338 ? CE  ? C LYS 336 CE  
30 1 Y 1 D LYS 338 ? NZ  ? C LYS 336 NZ  
31 1 Y 0 D ILE 384 ? CA  B C ILE 374 CA  
32 1 Y 0 D ILE 384 ? CB  B C ILE 374 CB  
33 1 Y 0 D ILE 384 ? CG1 B C ILE 374 CG1 
34 1 Y 0 D ILE 384 ? CG2 B C ILE 374 CG2 
35 1 Y 0 D ILE 384 ? CD1 B C ILE 374 CD1 
36 1 Y 0 F LEU 275 ? CA  B E LEU 275 CA  
37 1 Y 0 F LEU 275 ? CB  B E LEU 275 CB  
38 1 Y 0 F LEU 275 ? CG  B E LEU 275 CG  
39 1 Y 0 F LEU 275 ? CD1 B E LEU 275 CD1 
40 1 Y 0 F LEU 275 ? CD2 B E LEU 275 CD2 
41 1 Y 0 F THR 277 ? CA  B E THR 277 CA  
42 1 Y 0 F THR 277 ? CB  B E THR 277 CB  
43 1 Y 0 F THR 277 ? OG1 B E THR 277 OG1 
44 1 Y 0 F THR 277 ? CG2 B E THR 277 CG2 
45 1 Y 0 B THR 168 ? CA  B F THR 166 CA  
46 1 Y 0 B THR 168 ? CB  B F THR 166 CB  
47 1 Y 0 B THR 168 ? OG1 B F THR 166 OG1 
48 1 Y 0 B THR 168 ? CG2 B F THR 166 CG2 
49 1 Y 1 B SER 277 ? OG  ? F SER 275 OG  
50 1 Y 1 B SER 280 ? OG  ? F SER 278 OG  
51 1 Y 1 B GLN 281 ? CG  ? F GLN 279 CG  
52 1 Y 1 B GLN 281 ? CD  ? F GLN 279 CD  
53 1 Y 1 B GLN 281 ? OE1 ? F GLN 279 OE1 
54 1 Y 1 B GLN 281 ? NE2 ? F GLN 279 NE2 
55 1 Y 0 B ILE 318 ? CD1 ? F ILE 316 CD1 
56 1 Y 0 B ASN 334 ? CG  ? F ASN 332 CG  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .       2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .       3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .       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                     9LNV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     105.211 
_cell.length_a_esd                 ? 
_cell.length_b                     156.467 
_cell.length_b_esd                 ? 
_cell.length_c                     184.705 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9LNV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9LNV 
_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             2.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.89 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '6% PEG, 5% glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-10 
_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   0.97861 
_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                        'NFPSS BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97861 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       NFPSS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LNV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.67 
_reflns.d_resolution_low                               119.39 
_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                                     87167 
_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                           99.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.2 
_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                                   0.959 
_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                                    2.67 
_reflns_shell.d_res_low                                     2.72 
_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                             4276 
_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                                  0.481 
_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                                 9LNV 
_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                            2.67 
_refine.ls_d_res_low                             91.42 
_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                     86972 
_refine.ls_number_reflns_R_free                  4386 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.74 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2214 
_refine.ls_R_factor_R_free                       0.2877 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2179 
_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                          1.34 
_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                 30.69 
_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                            0.44 
_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.pdbx_number_atoms_protein        17256 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         184 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               17455 
_refine_hist.d_res_high                       2.67 
_refine_hist.d_res_low                        91.42 
# 
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' ? 17.288 ? 6653 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 2681 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3161 ? 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' 2.67 2.70  . . 161 2685 99.00  . . . . 0.2867 . . . . . . . . . . . 0.3895 
'X-RAY DIFFRACTION' 2.70 2.73  . . 137 2728 99.00  . . . . 0.2803 . . . . . . . . . . . 0.3848 
'X-RAY DIFFRACTION' 2.73 2.77  . . 150 2697 99.00  . . . . 0.2796 . . . . . . . . . . . 0.3616 
'X-RAY DIFFRACTION' 2.77 2.80  . . 152 2718 100.00 . . . . 0.2717 . . . . . . . . . . . 0.3613 
'X-RAY DIFFRACTION' 2.80 2.84  . . 132 2737 100.00 . . . . 0.2695 . . . . . . . . . . . 0.3172 
'X-RAY DIFFRACTION' 2.84 2.88  . . 140 2704 100.00 . . . . 0.2681 . . . . . . . . . . . 0.4015 
'X-RAY DIFFRACTION' 2.88 2.92  . . 156 2737 100.00 . . . . 0.2695 . . . . . . . . . . . 0.3658 
'X-RAY DIFFRACTION' 2.92 2.96  . . 136 2716 100.00 . . . . 0.2732 . . . . . . . . . . . 0.3677 
'X-RAY DIFFRACTION' 2.96 3.01  . . 147 2737 100.00 . . . . 0.2654 . . . . . . . . . . . 0.3524 
'X-RAY DIFFRACTION' 3.01 3.06  . . 150 2689 100.00 . . . . 0.2665 . . . . . . . . . . . 0.3373 
'X-RAY DIFFRACTION' 3.06 3.11  . . 138 2777 100.00 . . . . 0.2659 . . . . . . . . . . . 0.3612 
'X-RAY DIFFRACTION' 3.11 3.17  . . 149 2702 100.00 . . . . 0.2658 . . . . . . . . . . . 0.3967 
'X-RAY DIFFRACTION' 3.17 3.23  . . 156 2713 100.00 . . . . 0.2545 . . . . . . . . . . . 0.3439 
'X-RAY DIFFRACTION' 3.23 3.29  . . 138 2773 100.00 . . . . 0.2409 . . . . . . . . . . . 0.3185 
'X-RAY DIFFRACTION' 3.29 3.36  . . 124 2752 100.00 . . . . 0.2380 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 3.36 3.44  . . 147 2736 100.00 . . . . 0.2294 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 3.44 3.53  . . 142 2750 100.00 . . . . 0.2294 . . . . . . . . . . . 0.3011 
'X-RAY DIFFRACTION' 3.53 3.62  . . 144 2752 99.00  . . . . 0.2175 . . . . . . . . . . . 0.2757 
'X-RAY DIFFRACTION' 3.62 3.73  . . 141 2749 100.00 . . . . 0.2180 . . . . . . . . . . . 0.3166 
'X-RAY DIFFRACTION' 3.73 3.85  . . 142 2757 100.00 . . . . 0.2123 . . . . . . . . . . . 0.2653 
'X-RAY DIFFRACTION' 3.85 3.99  . . 160 2715 100.00 . . . . 0.1933 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 3.99 4.15  . . 163 2758 100.00 . . . . 0.1878 . . . . . . . . . . . 0.2300 
'X-RAY DIFFRACTION' 4.15 4.34  . . 139 2776 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2316 
'X-RAY DIFFRACTION' 4.34 4.56  . . 140 2786 100.00 . . . . 0.1687 . . . . . . . . . . . 0.2254 
'X-RAY DIFFRACTION' 4.57 4.85  . . 130 2803 100.00 . . . . 0.1644 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 4.85 5.23  . . 160 2754 100.00 . . . . 0.1849 . . . . . . . . . . . 0.2746 
'X-RAY DIFFRACTION' 5.23 5.75  . . 150 2795 100.00 . . . . 0.1940 . . . . . . . . . . . 0.2510 
'X-RAY DIFFRACTION' 5.75 6.58  . . 165 2805 100.00 . . . . 0.2181 . . . . . . . . . . . 0.2747 
'X-RAY DIFFRACTION' 6.58 8.29  . . 135 2852 100.00 . . . . 0.2084 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 8.29 91.42 . . 162 2933 98.00  . . . . 0.2205 . . . . . . . . . . . 0.2361 
# 
_struct.entry_id                     9LNV 
_struct.title                        'Crystal structure of T2R-TTL-YQVB6 Complex' 
_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        9LNV 
_struct_keywords.text            'tubule inhibitor, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 1  ? 
C N N 2  ? 
D N N 3  ? 
E N N 4  ? 
F N N 2  ? 
G N N 5  ? 
H N N 6  ? 
I N N 7  ? 
J N N 5  ? 
K N N 6  ? 
L N N 7  ? 
M N N 8  ? 
N N N 9  ? 
O N N 9  ? 
P N N 10 ? 
Q N N 10 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP TBA1B_PIG        Q2XVP4     ? 1 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
1  
2 UNP A0A8D1UIR5_PIG   A0A8D1UIR5 ? 2 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
1  
3 UNP STMN4_MOUSE      P63042     ? 3 
;DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ
KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
49 
4 UNP A0A8V0Z8P0_CHICK A0A8V0Z8P0 ? 4 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLAEMQQQLLEGDQTLVLASSTHPESVDSD
KNHGFGHEPGLVQLVNYYRGADKLCRKASLVKLIKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDE
REVFLAAYNRRREGREGNVWIAKSSAGAKGEGILISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLV
DHLYNIYLYREGVLRTSSEPYNSANFQDKTCHLTNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQI
KHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQK
TSQPTSIFIKL
;
1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9LNV A 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
2 1 9LNV C 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
3 2 9LNV D 1 ? 445 ? A0A8D1UIR5 1  ? 445 ? 1 455 
4 3 9LNV E 3 ? 143 ? P63042     49 ? 189 ? 5 145 
5 4 9LNV F 1 ? 378 ? A0A8V0Z8P0 1  ? 411 ? 1 378 
6 2 9LNV B 1 ? 445 ? A0A8D1UIR5 1  ? 445 ? 1 455 
# 
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 
4 9LNV MET E 1   ? UNP P63042     ?   ?  'initiating methionine' 3   1  
4 9LNV ALA E 2   ? UNP P63042     ?   ?  'expression tag'        4   2  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ALA 53 deletion                ?   3  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLU 54 deletion                ?   4  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 MET 55 deletion                ?   5  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLN 56 deletion                ?   6  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLN 57 deletion                ?   7  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLN 58 deletion                ?   8  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 LEU 59 deletion                ?   9  
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 LEU 60 deletion                ?   10 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLU 61 deletion                ?   11 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLY 62 deletion                ?   12 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ASP 63 deletion                ?   13 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLN 64 deletion                ?   14 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 THR 65 deletion                ?   15 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 LEU 66 deletion                ?   16 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 VAL 67 deletion                ?   17 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 LEU 68 deletion                ?   18 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ALA 69 deletion                ?   19 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 SER 70 deletion                ?   20 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 SER 71 deletion                ?   21 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 THR 72 deletion                ?   22 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 HIS 73 deletion                ?   23 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 PRO 74 deletion                ?   24 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLU 75 deletion                ?   25 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 SER 76 deletion                ?   26 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 VAL 77 deletion                ?   27 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ASP 78 deletion                ?   28 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 SER 79 deletion                ?   29 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ASP 80 deletion                ?   30 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 LYS 81 deletion                ?   31 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 ASN 82 deletion                ?   32 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 HIS 83 deletion                ?   33 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 GLY 84 deletion                ?   34 
5 9LNV ?   F ?   ? UNP A0A8V0Z8P0 PHE 85 deletion                ?   35 
5 9LNV HIS F 379 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        379 36 
5 9LNV HIS F 380 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        380 37 
5 9LNV HIS F 381 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        381 38 
5 9LNV HIS F 382 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        382 39 
5 9LNV HIS F 383 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        383 40 
5 9LNV HIS F 384 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        384 41 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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 GLY A 10  ? HIS A 28  ? GLY A 10  HIS A 28  1 ? 19 
HELX_P HELX_P2  AA2 ASP A 47  ? THR A 51  ? ASP A 47  THR A 51  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 72  ? GLY A 81  ? PRO A 72  GLY A 81  1 ? 10 
HELX_P HELX_P4  AA4 TYR A 83  ? PHE A 87  ? TYR A 83  PHE A 87  5 ? 5  
HELX_P HELX_P5  AA5 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P7  AA7 TYR A 108 ? GLU A 113 ? TYR A 108 GLU A 113 1 ? 6  
HELX_P HELX_P8  AA8 ILE A 114 ? GLN A 128 ? ILE A 114 GLN A 128 1 ? 15 
HELX_P HELX_P9  AA9 GLY A 143 ? TYR A 161 ? GLY A 143 TYR A 161 1 ? 19 
HELX_P HELX_P10 AB1 VAL A 182 ? LEU A 195 ? VAL A 182 LEU A 195 1 ? 14 
HELX_P HELX_P11 AB2 GLU A 196 ? SER A 198 ? GLU A 196 SER A 198 5 ? 3  
HELX_P HELX_P12 AB3 ASN A 206 ? ASP A 218 ? ASN A 206 ASP A 218 1 ? 13 
HELX_P HELX_P13 AB4 THR A 223 ? PHE A 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P14 AB5 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P15 AB6 SER A 287 ? CYS A 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P16 AB7 PHE A 296 ? GLN A 301 ? PHE A 296 GLN A 301 5 ? 6  
HELX_P HELX_P17 AB8 ASP A 306 ? GLY A 310 ? ASP A 306 GLY A 310 5 ? 5  
HELX_P HELX_P18 AB9 VAL A 324 ? ARG A 339 ? VAL A 324 ARG A 339 1 ? 16 
HELX_P HELX_P19 AC1 ILE A 384 ? ALA A 400 ? ILE A 384 ALA A 400 1 ? 17 
HELX_P HELX_P20 AC2 PHE A 404 ? GLY A 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P21 AC3 GLU A 414 ? GLY A 436 ? GLU A 414 GLY A 436 1 ? 23 
HELX_P HELX_P22 AC4 GLY B 10  ? GLY B 29  ? GLY C 10  GLY C 29  1 ? 20 
HELX_P HELX_P23 AC5 SER B 48  ? THR B 51  ? SER C 48  THR C 51  5 ? 4  
HELX_P HELX_P24 AC6 PRO B 72  ? THR B 80  ? PRO C 72  THR C 80  1 ? 9  
HELX_P HELX_P25 AC7 TYR B 83  ? PHE B 87  ? TYR C 83  PHE C 87  5 ? 5  
HELX_P HELX_P26 AC8 HIS B 88  ? GLU B 90  ? HIS C 88  GLU C 90  5 ? 3  
HELX_P HELX_P27 AC9 ASN B 102 ? TYR B 108 ? ASN C 102 TYR C 108 1 ? 7  
HELX_P HELX_P28 AD1 ILE B 110 ? GLN B 128 ? ILE C 110 GLN C 128 1 ? 19 
HELX_P HELX_P29 AD2 GLY B 143 ? GLY B 162 ? GLY C 143 GLY C 162 1 ? 20 
HELX_P HELX_P30 AD3 VAL B 182 ? LEU B 195 ? VAL C 182 LEU C 195 1 ? 14 
HELX_P HELX_P31 AD4 GLU B 196 ? SER B 198 ? GLU C 196 SER C 198 5 ? 3  
HELX_P HELX_P32 AD5 ASN B 206 ? ASP B 218 ? ASN C 206 ASP C 218 1 ? 13 
HELX_P HELX_P33 AD6 THR B 223 ? PHE B 244 ? THR C 223 PHE C 244 1 ? 22 
HELX_P HELX_P34 AD7 ASP B 251 ? VAL B 260 ? ASP C 251 VAL C 260 1 ? 10 
HELX_P HELX_P35 AD8 SER B 277 ? TYR B 282 ? SER C 277 TYR C 282 1 ? 6  
HELX_P HELX_P36 AD9 SER B 287 ? CYS B 295 ? SER C 287 CYS C 295 1 ? 9  
HELX_P HELX_P37 AE1 PHE B 296 ? GLN B 301 ? PHE C 296 GLN C 301 5 ? 6  
HELX_P HELX_P38 AE2 ASP B 306 ? GLY B 310 ? ASP C 306 GLY C 310 5 ? 5  
HELX_P HELX_P39 AE3 VAL B 324 ? LYS B 338 ? VAL C 324 LYS C 338 1 ? 15 
HELX_P HELX_P40 AE4 ILE B 384 ? ALA B 400 ? ILE C 384 ALA C 400 1 ? 17 
HELX_P HELX_P41 AE5 PHE B 404 ? GLY B 410 ? PHE C 404 GLY C 410 1 ? 7  
HELX_P HELX_P42 AE6 GLU B 414 ? VAL B 437 ? GLU C 414 VAL C 437 1 ? 24 
HELX_P HELX_P43 AE7 GLY C 10  ? GLY C 29  ? GLY D 10  GLY D 29  1 ? 20 
HELX_P HELX_P44 AE8 SER C 40  ? LEU C 44  ? SER D 40  LEU D 46  5 ? 5  
HELX_P HELX_P45 AE9 ARG C 46  ? VAL C 49  ? ARG D 48  VAL D 51  5 ? 4  
HELX_P HELX_P46 AF1 GLY C 71  ? GLY C 79  ? GLY D 73  GLY D 81  1 ? 9  
HELX_P HELX_P47 AF2 ARG C 86  ? ASP C 88  ? ARG D 88  ASP D 90  5 ? 3  
HELX_P HELX_P48 AF3 ASN C 100 ? TYR C 106 ? ASN D 102 TYR D 108 1 ? 7  
HELX_P HELX_P49 AF4 GLY C 109 ? SER C 126 ? GLY D 111 SER D 128 1 ? 18 
HELX_P HELX_P50 AF5 GLY C 142 ? TYR C 159 ? GLY D 144 TYR D 161 1 ? 18 
HELX_P HELX_P51 AF6 VAL C 180 ? THR C 196 ? VAL D 182 THR D 198 1 ? 17 
HELX_P HELX_P52 AF7 ASN C 204 ? ARG C 213 ? ASN D 206 ARG D 215 1 ? 10 
HELX_P HELX_P53 AF8 THR C 221 ? VAL C 236 ? THR D 223 VAL D 238 1 ? 16 
HELX_P HELX_P54 AF9 THR C 237 ? PHE C 242 ? THR D 239 PHE D 244 1 ? 6  
HELX_P HELX_P55 AG1 ASP C 249 ? VAL C 258 ? ASP D 251 VAL D 260 1 ? 10 
HELX_P HELX_P56 AG2 THR C 285 ? MET C 293 ? THR D 287 MET D 295 1 ? 9  
HELX_P HELX_P57 AG3 PHE C 294 ? MET C 299 ? PHE D 296 MET D 301 5 ? 6  
HELX_P HELX_P58 AG4 ASP C 304 ? GLY C 308 ? ASP D 306 GLY D 310 5 ? 5  
HELX_P HELX_P59 AG5 SER C 322 ? ASN C 337 ? SER D 324 ASN D 339 1 ? 16 
HELX_P HELX_P60 AG6 SER C 338 ? PHE C 341 ? SER D 340 PHE D 343 5 ? 4  
HELX_P HELX_P61 AG7 ILE C 374 ? ARG C 390 ? ILE D 384 ARG D 400 1 ? 17 
HELX_P HELX_P62 AG8 LEU C 395 ? GLY C 400 ? LEU D 405 GLY D 410 1 ? 6  
HELX_P HELX_P63 AG9 GLU C 405 ? ALA C 428 ? GLU D 415 ALA D 438 1 ? 24 
HELX_P HELX_P64 AH1 SER D 44  ? LYS D 133 ? SER E 46  LYS E 135 1 ? 90 
HELX_P HELX_P65 AH2 SER E 11  ? ALA E 23  ? SER F 11  ALA F 23  1 ? 13 
HELX_P HELX_P66 AH3 PRO E 48  ? LEU E 52  ? PRO F 48  LEU F 52  5 ? 5  
HELX_P HELX_P67 AH4 GLY E 67  ? CYS E 72  ? GLY F 67  CYS F 72  5 ? 6  
HELX_P HELX_P68 AH5 ARG E 73  ? THR E 83  ? ARG F 73  THR F 83  1 ? 11 
HELX_P HELX_P69 AH6 LEU E 87  ? CYS E 91  ? LEU F 87  CYS F 91  5 ? 5  
HELX_P HELX_P70 AH7 GLU E 127 ? ASN E 136 ? GLU F 127 ASN F 136 1 ? 10 
HELX_P HELX_P71 AH8 SER E 167 ? GLN E 176 ? SER F 167 GLN F 176 1 ? 10 
HELX_P HELX_P72 AH9 HIS E 243 ? LYS E 247 ? HIS F 243 LYS F 247 5 ? 5  
HELX_P HELX_P73 AI1 GLU E 257 ? GLY E 259 ? GLU F 257 GLY F 259 5 ? 3  
HELX_P HELX_P74 AI2 PHE E 263 ? ASN E 276 ? PHE F 263 ASN F 276 1 ? 14 
HELX_P HELX_P75 AI3 THR E 278 ? ILE E 283 ? THR F 278 ILE F 283 1 ? 6  
HELX_P HELX_P76 AI4 ILE E 283 ? SER E 303 ? ILE F 283 SER F 303 1 ? 21 
HELX_P HELX_P77 AI5 ALA E 339 ? LYS E 341 ? ALA F 339 LYS F 341 5 ? 3  
HELX_P HELX_P78 AI6 LEU E 342 ? ALA E 354 ? LEU F 342 ALA F 354 1 ? 13 
HELX_P HELX_P79 AI7 GLY F 10  ? GLY F 29  ? GLY B 10  GLY B 29  1 ? 20 
HELX_P HELX_P80 AI8 ASP F 41  ? ARG F 46  ? ASP B 41  ARG B 48  1 ? 6  
HELX_P HELX_P81 AI9 ILE F 47  ? VAL F 49  ? ILE B 49  VAL B 51  5 ? 3  
HELX_P HELX_P82 AJ1 THR F 72  ? SER F 78  ? THR B 74  SER B 80  1 ? 7  
HELX_P HELX_P83 AJ2 PHE F 81  ? PHE F 85  ? PHE B 83  PHE B 87  5 ? 5  
HELX_P HELX_P84 AJ3 ARG F 86  ? ASP F 88  ? ARG B 88  ASP B 90  5 ? 3  
HELX_P HELX_P85 AJ4 ASN F 100 ? TYR F 106 ? ASN B 102 TYR B 108 1 ? 7  
HELX_P HELX_P86 AJ5 THR F 107 ? GLU F 125 ? THR B 109 GLU B 127 1 ? 19 
HELX_P HELX_P87 AJ6 GLY F 142 ? TYR F 159 ? GLY B 144 TYR B 161 1 ? 18 
HELX_P HELX_P88 AJ7 VAL F 180 ? THR F 196 ? VAL B 182 THR B 198 1 ? 17 
HELX_P HELX_P89 AJ8 ASN F 204 ? ARG F 213 ? ASN B 206 ARG B 215 1 ? 10 
HELX_P HELX_P90 AJ9 THR F 221 ? PHE F 242 ? THR B 223 PHE B 244 1 ? 22 
HELX_P HELX_P91 AK1 ASP F 249 ? VAL F 258 ? ASP B 251 VAL B 260 1 ? 10 
HELX_P HELX_P92 AK2 THR F 285 ? PHE F 294 ? THR B 287 PHE B 296 1 ? 10 
HELX_P HELX_P93 AK3 ASP F 295 ? MET F 299 ? ASP B 297 MET B 301 5 ? 5  
HELX_P HELX_P94 AK4 ASP F 304 ? GLY F 308 ? ASP B 306 GLY B 310 5 ? 5  
HELX_P HELX_P95 AK5 SER F 322 ? ASN F 337 ? SER B 324 ASN B 339 1 ? 16 
HELX_P HELX_P96 AK6 SER F 338 ? PHE F 341 ? SER B 340 PHE B 343 5 ? 4  
HELX_P HELX_P97 AK7 ILE F 374 ? ARG F 390 ? ILE B 384 ARG B 400 1 ? 17 
HELX_P HELX_P98 AK8 LEU F 395 ? GLY F 400 ? LEU B 405 GLY B 410 1 ? 6  
HELX_P HELX_P99 AK9 ASP F 404 ? ALA F 428 ? ASP B 414 ALA B 438 1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 39 OD2 ? ? ? 1_555 I CA . CA ? ? A ASP 39  A CA 503 1_555 ? ? ? ? ? ? ? 2.432 ? ? 
metalc2  metalc ? ? A THR 41 OG1 ? ? ? 1_555 I CA . CA ? ? A THR 41  A CA 503 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc3  metalc ? ? A GLY 44 O   ? ? ? 1_555 I CA . CA ? ? A GLY 44  A CA 503 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc4  metalc ? ? A ASP 47 OD2 ? ? ? 1_555 I CA . CA ? ? A ASP 47  A CA 503 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc5  metalc ? ? A GLU 55 OE2 ? ? ? 1_555 I CA . CA ? ? A GLU 55  A CA 503 1_555 ? ? ? ? ? ? ? 2.534 ? ? 
metalc6  metalc ? ? G GTP .  O3B ? ? ? 1_555 H MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.768 ? ? 
metalc7  metalc ? ? G GTP .  O1B ? ? ? 1_555 H MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc8  metalc ? ? B ASP 39 OD1 ? ? ? 1_555 L CA . CA ? ? C ASP 39  C CA 503 1_555 ? ? ? ? ? ? ? 2.715 ? ? 
metalc9  metalc ? ? B ASP 39 OD2 ? ? ? 1_555 L CA . CA ? ? C ASP 39  C CA 503 1_555 ? ? ? ? ? ? ? 2.490 ? ? 
metalc10 metalc ? ? B THR 41 OG1 ? ? ? 1_555 L CA . CA ? ? C THR 41  C CA 503 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc11 metalc ? ? B ASP 47 OD2 ? ? ? 1_555 L CA . CA ? ? C ASP 47  C CA 503 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc12 metalc ? ? B GLU 55 OE2 ? ? ? 1_555 L CA . CA ? ? C GLU 55  C CA 503 1_555 ? ? ? ? ? ? ? 2.539 ? ? 
metalc13 metalc ? ? J GTP .  O1G ? ? ? 1_555 K MG . MG ? ? C GTP 501 C MG 502 1_555 ? ? ? ? ? ? ? 2.939 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OG1 ? A THR 41 ? A THR 41  ? 1_555 71.8  ? 
2  OD2 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 O   ? A GLY 44 ? A GLY 44  ? 1_555 83.6  ? 
3  OG1 ? A THR 41 ? A THR 41  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 O   ? A GLY 44 ? A GLY 44  ? 1_555 52.9  ? 
4  OD2 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD2 ? A ASP 47 ? A ASP 47  ? 1_555 114.3 ? 
5  OG1 ? A THR 41 ? A THR 41  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD2 ? A ASP 47 ? A ASP 47  ? 1_555 116.3 ? 
6  O   ? A GLY 44 ? A GLY 44  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD2 ? A ASP 47 ? A ASP 47  ? 1_555 156.6 ? 
7  OD2 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 62.8  ? 
8  OG1 ? A THR 41 ? A THR 41  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 100.1 ? 
9  O   ? A GLY 44 ? A GLY 44  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 59.8  ? 
10 OD2 ? A ASP 47 ? A ASP 47  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 141.0 ? 
11 O3B ? G GTP .  ? A GTP 501 ? 1_555 MG ? H MG . ? A MG 502 ? 1_555 O1B ? G GTP .  ? A GTP 501 ? 1_555 61.4  ? 
12 OD1 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OD2 ? B ASP 39 ? C ASP 39  ? 1_555 48.8  ? 
13 OD1 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OG1 ? B THR 41 ? C THR 41  ? 1_555 59.6  ? 
14 OD2 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OG1 ? B THR 41 ? C THR 41  ? 1_555 65.2  ? 
15 OD1 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OD2 ? B ASP 47 ? C ASP 47  ? 1_555 90.8  ? 
16 OD2 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OD2 ? B ASP 47 ? C ASP 47  ? 1_555 137.7 ? 
17 OG1 ? B THR 41 ? C THR 41  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OD2 ? B ASP 47 ? C ASP 47  ? 1_555 108.7 ? 
18 OD1 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OE2 ? B GLU 55 ? C GLU 55  ? 1_555 97.1  ? 
19 OD2 ? B ASP 39 ? C ASP 39  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OE2 ? B GLU 55 ? C GLU 55  ? 1_555 56.9  ? 
20 OG1 ? B THR 41 ? C THR 41  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OE2 ? B GLU 55 ? C GLU 55  ? 1_555 60.4  ? 
21 OD2 ? B ASP 47 ? C ASP 47  ? 1_555 CA ? L CA . ? C CA 503 ? 1_555 OE2 ? B GLU 55 ? C GLU 55  ? 1_555 159.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 273 A . ? ALA 273 A PRO 274 A ? PRO 274 A 1 1.01  
2 ALA 273 B . ? ALA 273 C PRO 274 B ? PRO 274 C 1 -4.29 
3 ALA 271 C . ? ALA 273 D PRO 272 C ? PRO 274 D 1 1.99  
4 GLU 193 E . ? GLU 193 F PRO 194 E ? PRO 194 F 1 5.91  
5 ALA 271 F . ? ALA 273 B PRO 272 F ? PRO 274 B 1 -2.61 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 6  ? 
AA4 ? 6  ? 
AA5 ? 2  ? 
AA6 ? 4  ? 
AA7 ? 10 ? 
AA8 ? 2  ? 
AA9 ? 5  ? 
AB1 ? 2  ? 
AB2 ? 3  ? 
AB3 ? 5  ? 
AB4 ? 5  ? 
AB5 ? 10 ? 
AB6 ? 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  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA2 1 2  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? parallel      
AA3 4 5  ? anti-parallel 
AA3 5 6  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA5 1 2  ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? anti-parallel 
AA7 8 9  ? anti-parallel 
AA7 9 10 ? parallel      
AA8 1 2  ? anti-parallel 
AA9 1 2  ? parallel      
AA9 2 3  ? parallel      
AA9 3 4  ? parallel      
AA9 4 5  ? parallel      
AB1 1 2  ? anti-parallel 
AB2 1 2  ? anti-parallel 
AB2 2 3  ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB4 1 2  ? anti-parallel 
AB4 2 3  ? anti-parallel 
AB4 3 4  ? anti-parallel 
AB4 4 5  ? anti-parallel 
AB5 1 2  ? parallel      
AB5 2 3  ? parallel      
AB5 3 4  ? parallel      
AB5 4 5  ? parallel      
AB5 5 6  ? parallel      
AB5 6 7  ? parallel      
AB5 7 8  ? anti-parallel 
AB5 8 9  ? anti-parallel 
AB5 9 10 ? parallel      
AB6 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  LEU A 92  ? THR A 94  ? LEU A 92  THR A 94  
AA1 2  ALA A 65  ? ASP A 69  ? ALA A 65  ASP A 69  
AA1 3  CYS A 4   ? VAL A 9   ? CYS A 4   VAL A 9   
AA1 4  GLY A 134 ? SER A 140 ? GLY A 134 SER A 140 
AA1 5  SER A 165 ? TYR A 172 ? SER A 165 TYR A 172 
AA1 6  CYS A 200 ? ASP A 205 ? CYS A 200 ASP A 205 
AA2 1  PHE A 53  ? GLU A 55  ? PHE A 53  GLU A 55  
AA2 2  HIS A 61  ? PRO A 63  ? HIS A 61  PRO A 63  
AA3 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA3 2  ARG A 373 ? THR A 381 ? ARG A 373 THR A 381 
AA3 3  TYR A 312 ? GLY A 321 ? TYR A 312 GLY A 321 
AA3 4  GLY A 350 ? ASN A 356 ? GLY A 350 ASN A 356 
AA3 5  GLN D 16  ? ILE D 21  ? GLN E 18  ILE E 23  
AA3 6  GLU D 5   ? LYS D 11  ? GLU E 7   LYS E 13  
AA4 1  LEU B 92  ? THR B 94  ? LEU C 92  THR C 94  
AA4 2  ALA B 65  ? ASP B 69  ? ALA C 65  ASP C 69  
AA4 3  CYS B 4   ? VAL B 9   ? CYS C 4   VAL C 9   
AA4 4  GLY B 134 ? SER B 140 ? GLY C 134 SER C 140 
AA4 5  SER B 165 ? TYR B 172 ? SER C 165 TYR C 172 
AA4 6  CYS B 200 ? ASP B 205 ? CYS C 200 ASP C 205 
AA5 1  PHE B 53  ? GLU B 55  ? PHE C 53  GLU C 55  
AA5 2  HIS B 61  ? PRO B 63  ? HIS C 61  PRO C 63  
AA6 1  LEU B 269 ? ALA B 273 ? LEU C 269 ALA C 273 
AA6 2  ARG B 373 ? THR B 381 ? ARG C 373 THR C 381 
AA6 3  TYR B 312 ? GLY B 321 ? TYR C 312 GLY C 321 
AA6 4  PHE B 351 ? ASN B 356 ? PHE C 351 ASN C 356 
AA7 1  PHE C 90  ? PHE C 92  ? PHE D 92  PHE D 94  
AA7 2  ALA C 63  ? ASP C 67  ? ALA D 65  ASP D 69  
AA7 3  GLU C 3   ? ALA C 9   ? GLU D 3   ALA D 9   
AA7 4  LEU C 130 ? SER C 138 ? LEU D 132 SER D 140 
AA7 5  ILE C 163 ? MET C 170 ? ILE D 165 MET D 172 
AA7 6  GLU C 198 ? ASP C 203 ? GLU D 200 ASP D 205 
AA7 7  PHE C 265 ? ALA C 271 ? PHE D 267 ALA D 273 
AA7 8  MET C 363 ? SER C 371 ? MET D 373 SER D 381 
AA7 9  TYR C 310 ? GLY C 319 ? TYR D 312 GLY D 321 
AA7 10 ALA C 352 ? CYS C 354 ? ALA D 354 CYS D 356 
AA8 1  TYR C 51  ? ASN C 52  ? TYR D 53  ASN D 54  
AA8 2  VAL C 60  ? PRO C 61  ? VAL D 62  PRO D 63  
AA9 1  TRP E 27  ? ARG E 29  ? TRP F 27  ARG F 29  
AA9 2  TYR E 2   ? VAL E 6   ? TYR F 2   VAL F 6   
AA9 3  LEU E 39  ? LEU E 41  ? LEU F 39  LEU F 41  
AA9 4  LEU E 61  ? VAL E 62  ? LEU F 61  VAL F 62  
AA9 5  GLN E 310 ? SER E 311 ? GLN F 310 SER F 311 
AB1 1  VAL E 99  ? ILE E 100 ? VAL F 99  ILE F 100 
AB1 2  HIS E 180 ? VAL E 181 ? HIS F 180 VAL F 181 
AB2 1  ILE E 162 ? SER E 163 ? ILE F 162 SER F 163 
AB2 2  TRP E 147 ? ILE E 148 ? TRP F 147 ILE F 148 
AB2 3  GLN E 183 ? LYS E 184 ? GLN F 183 LYS F 184 
AB3 1  GLU E 261 ? MET E 262 ? GLU F 261 MET F 262 
AB3 2  VAL E 220 ? ARG E 222 ? VAL F 220 ARG F 222 
AB3 3  ASP E 200 ? VAL E 207 ? ASP F 200 VAL F 207 
AB3 4  GLN E 313 ? VAL E 321 ? GLN F 313 VAL F 321 
AB3 5  VAL E 327 ? ASN E 333 ? VAL F 327 ASN F 333 
AB4 1  GLU E 261 ? MET E 262 ? GLU F 261 MET F 262 
AB4 2  VAL E 220 ? ARG E 222 ? VAL F 220 ARG F 222 
AB4 3  ASP E 200 ? VAL E 207 ? ASP F 200 VAL F 207 
AB4 4  ILE E 213 ? TYR E 216 ? ILE F 213 TYR F 216 
AB4 5  PHE E 375 ? LYS E 377 ? PHE F 375 LYS F 377 
AB5 1  PHE F 90  ? PHE F 92  ? PHE B 92  PHE B 94  
AB5 2  ALA F 63  ? ASP F 67  ? ALA B 65  ASP B 69  
AB5 3  GLU F 3   ? ALA F 9   ? GLU B 3   ALA B 9   
AB5 4  LEU F 130 ? SER F 138 ? LEU B 132 SER B 140 
AB5 5  ILE F 163 ? MET F 170 ? ILE B 165 MET B 172 
AB5 6  GLU F 198 ? ASP F 203 ? GLU B 200 ASP B 205 
AB5 7  PHE F 265 ? ALA F 271 ? PHE B 267 ALA B 273 
AB5 8  SER F 364 ? SER F 371 ? SER B 374 SER B 381 
AB5 9  TYR F 310 ? ARG F 318 ? TYR B 312 ARG B 320 
AB5 10 VAL F 349 ? CYS F 354 ? VAL B 351 CYS B 356 
AB6 1  TYR F 51  ? ALA F 54  ? TYR B 53  ALA B 56  
AB6 2  LYS F 58  ? PRO F 61  ? LYS B 60  PRO B 63  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O ILE A 93  ? O ILE A 93  N PHE A 67  ? N PHE A 67  
AA1 2 3  O VAL A 68  ? O VAL A 68  N HIS A 8   ? N HIS A 8   
AA1 3 4  N ILE A 7   ? N ILE A 7   O LEU A 136 ? O LEU A 136 
AA1 4 5  N PHE A 135 ? N PHE A 135 O SER A 165 ? O SER A 165 
AA1 5 6  N TYR A 172 ? N TYR A 172 O VAL A 204 ? O VAL A 204 
AA2 1 2  N SER A 54  ? N SER A 54  O VAL A 62  ? O VAL A 62  
AA3 1 2  N THR A 271 ? N THR A 271 O MET A 377 ? O MET A 377 
AA3 2 3  O CYS A 376 ? O CYS A 376 N LEU A 318 ? N LEU A 318 
AA3 3 4  N TYR A 319 ? N TYR A 319 O GLY A 354 ? O GLY A 354 
AA3 4 5  N ILE A 355 ? N ILE A 355 O GLN D 16  ? O GLN E 18  
AA3 5 6  O SER D 17  ? O SER E 19  N ASN D 10  ? N ASN E 12  
AA4 1 2  O ILE B 93  ? O ILE C 93  N PHE B 67  ? N PHE C 67  
AA4 2 3  O VAL B 68  ? O VAL C 68  N HIS B 8   ? N HIS C 8   
AA4 3 4  N ILE B 7   ? N ILE C 7   O LEU B 136 ? O LEU C 136 
AA4 4 5  N VAL B 137 ? N VAL C 137 O LEU B 167 ? O LEU C 167 
AA4 5 6  N GLU B 168 ? N GLU C 168 O PHE B 202 ? O PHE C 202 
AA5 1 2  N SER B 54  ? N SER C 54  O VAL B 62  ? O VAL C 62  
AA6 1 2  N LEU B 269 ? N LEU C 269 O SER B 379 ? O SER C 379 
AA6 2 3  O LEU B 378 ? O LEU C 378 N CYS B 316 ? N CYS C 316 
AA6 3 4  N TYR B 319 ? N TYR C 319 O GLY B 354 ? O GLY C 354 
AA7 1 2  O VAL C 91  ? O VAL D 93  N LEU C 65  ? N LEU D 67  
AA7 2 3  O ILE C 64  ? O ILE D 66  N HIS C 6   ? N HIS D 6   
AA7 3 4  N GLU C 3   ? N GLU D 3   O GLN C 131 ? O GLN D 133 
AA7 4 5  N PHE C 133 ? N PHE D 135 O ASN C 165 ? O ASN D 167 
AA7 5 6  N MET C 170 ? N MET D 172 O ILE C 202 ? O ILE D 204 
AA7 6 7  N THR C 199 ? N THR D 201 O PHE C 266 ? O PHE D 268 
AA7 7 8  N MET C 267 ? N MET D 269 O GLY C 369 ? O GLY D 379 
AA7 8 9  O ILE C 368 ? O ILE D 378 N ALA C 314 ? N ALA D 316 
AA7 9 10 N PHE C 317 ? N PHE D 319 O ALA C 352 ? O ALA D 354 
AA8 1 2  N ASN C 52  ? N ASN D 54  O VAL C 60  ? O VAL D 62  
AA9 1 2  O LYS E 28  ? O LYS F 28  N TYR E 2   ? N TYR F 2   
AA9 2 3  N VAL E 5   ? N VAL F 5   O LEU E 39  ? O LEU F 39  
AA9 3 4  N MET E 40  ? N MET F 40  O LEU E 61  ? O LEU F 61  
AA9 4 5  N VAL E 62  ? N VAL F 62  O GLN E 310 ? O GLN F 310 
AB1 1 2  N ILE E 100 ? N ILE F 100 O HIS E 180 ? O HIS F 180 
AB2 1 2  O SER E 163 ? O SER F 163 N TRP E 147 ? N TRP F 147 
AB2 2 3  N ILE E 148 ? N ILE F 148 O GLN E 183 ? O GLN F 183 
AB3 1 2  O MET E 262 ? O MET F 262 N LEU E 221 ? N LEU F 221 
AB3 2 3  O VAL E 220 ? O VAL F 220 N ARG E 202 ? N ARG F 202 
AB3 3 4  N SER E 203 ? N SER F 203 O PHE E 317 ? O PHE F 317 
AB3 4 5  N GLY E 316 ? N GLY F 316 O ASN E 333 ? O ASN F 333 
AB4 1 2  O MET E 262 ? O MET F 262 N LEU E 221 ? N LEU F 221 
AB4 2 3  O VAL E 220 ? O VAL F 220 N ARG E 202 ? N ARG F 202 
AB4 3 4  N LEU E 206 ? N LEU F 206 O TYR E 214 ? O TYR F 214 
AB4 4 5  N LEU E 215 ? N LEU F 215 O ILE E 376 ? O ILE F 376 
AB5 1 2  O VAL F 91  ? O VAL B 93  N LEU F 65  ? N LEU B 67  
AB5 2 3  O VAL F 66  ? O VAL B 68  N GLN F 8   ? N GLN B 8   
AB5 3 4  N GLU F 3   ? N GLU B 3   O GLN F 131 ? O GLN B 133 
AB5 4 5  N PHE F 133 ? N PHE B 135 O ILE F 163 ? O ILE B 165 
AB5 5 6  N MET F 170 ? N MET B 172 O ILE F 202 ? O ILE B 204 
AB5 6 7  N THR F 199 ? N THR B 201 O PHE F 266 ? O PHE B 268 
AB5 7 8  N MET F 267 ? N MET B 269 O GLY F 369 ? O GLY B 379 
AB5 8 9  O THR F 366 ? O THR B 376 N ILE F 316 ? N ILE B 318 
AB5 9 10 N PHE F 317 ? N PHE B 319 O CYS F 354 ? O CYS B 356 
AB6 1 2  N ASN F 52  ? N ASN B 54  O VAL F 60  ? O VAL B 62  
# 
_pdbx_entry_details.entry_id                   9LNV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 N   D GLN 11  ? ? O1B D GDP 501 ? ? 1.30 
2  1 O   C THR 349 ? ? O   C HOH 601 ? ? 1.88 
3  1 OG  A SER 140 ? ? O2A A GTP 501 ? ? 1.97 
4  1 OH  D TYR 108 ? ? OE2 D GLU 417 ? ? 2.03 
5  1 NH1 B ARG 278 ? ? O   B HOH 601 ? ? 2.04 
6  1 NE2 C GLN 285 ? ? OE1 C GLN 372 ? ? 2.10 
7  1 O   D ARG 215 ? ? N   D LEU 217 ? ? 2.12 
8  1 O   B GLY 73  ? ? N   B MET 75  ? ? 2.12 
9  1 NH1 B ARG 264 ? ? OE1 B GLU 431 ? ? 2.13 
10 1 NZ  F LYS 74  ? ? OE1 F GLU 331 ? ? 2.13 
11 1 OG1 A THR 41  ? ? O   A GLY 44  ? ? 2.14 
12 1 NZ  A LYS 60  ? ? O   A GLN 85  ? ? 2.15 
13 1 OH  D TYR 52  ? ? OE1 D GLN 136 ? ? 2.17 
14 1 N   A HIS 88  ? ? OE1 A GLN 91  ? ? 2.17 
15 1 OG1 D THR 382 ? ? OE1 D GLN 436 ? ? 2.17 
16 1 N   A GLN 11  ? ? O2B A GTP 501 ? ? 2.19 
17 1 O   F THR 278 ? ? OG  F SER 282 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_1              87 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              88 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              88 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                104.71 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            -16.99 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 PRO A 32  ? ? -57.11  0.72    
2   1 ASP A 47  ? ? -59.52  170.54  
3   1 PRO A 63  ? ? -39.75  144.36  
4   1 LYS A 96  ? ? -85.96  -71.27  
5   1 THR A 109 ? ? -66.88  -76.01  
6   1 ILE A 114 ? ? -153.48 -16.85  
7   1 GLN A 128 ? ? -92.05  36.07   
8   1 LEU A 132 ? ? -29.27  131.16  
9   1 TYR A 161 ? ? -157.53 39.08   
10  1 TYR A 282 ? ? 50.93   143.21  
11  1 ALA A 294 ? ? -39.35  -29.88  
12  1 CYS A 305 ? ? 175.29  170.80  
13  1 HIS A 309 ? ? -101.77 56.75   
14  1 TRP A 346 ? ? -71.59  28.92   
15  1 PHE A 404 ? ? 75.77   -11.47  
16  1 GLU A 415 ? ? -37.73  -36.72  
17  1 ASP A 438 ? ? -31.29  -109.21 
18  1 THR C 41  ? ? -58.86  93.86   
19  1 ASN C 50  ? ? -58.43  -9.18   
20  1 ALA C 58  ? ? -69.89  6.62    
21  1 TYR C 108 ? ? -116.36 -75.78  
22  1 SER C 147 ? ? -95.49  -60.67  
23  1 CYS C 200 ? ? -171.12 133.08  
24  1 HIS C 283 ? ? 54.97   16.15   
25  1 PRO C 298 ? ? -58.91  -6.45   
26  1 ALA C 314 ? ? 174.13  154.57  
27  1 LYS C 338 ? ? -99.03  38.10   
28  1 THR C 349 ? ? 94.30   -73.55  
29  1 PHE C 404 ? ? 69.75   -12.01  
30  1 ARG D 2   ? ? -17.08  112.36  
31  1 PRO D 32  ? ? -67.33  15.98   
32  1 HIS D 37  ? ? -105.57 59.95   
33  1 THR D 57  ? ? -44.63  157.45  
34  1 ASN D 59  ? ? 58.26   18.38   
35  1 ARG D 64  ? ? -65.95  64.06   
36  1 LEU D 70  ? ? -70.93  23.71   
37  1 GLU D 71  ? ? 176.59  103.31  
38  1 PRO D 72  ? ? -59.27  -164.86 
39  1 PHE D 87  ? ? -68.74  -168.01 
40  1 ASP D 90  ? ? -68.23  7.02    
41  1 GLN D 96  ? ? -145.03 -40.20  
42  1 THR D 109 ? ? -122.51 -84.27  
43  1 SER D 128 ? ? -82.07  37.73   
44  1 CYS D 131 ? ? -157.33 84.05   
45  1 THR D 180 ? ? -73.12  44.85   
46  1 VAL D 181 ? ? 52.51   -56.72  
47  1 PHE D 214 ? ? -45.32  -79.76  
48  1 ARG D 215 ? ? -61.08  -145.21 
49  1 THR D 216 ? ? 19.49   -56.46  
50  1 LYS D 218 ? ? 78.14   53.69   
51  1 THR D 221 ? ? 44.20   80.78   
52  1 ASN D 228 ? ? -59.92  -3.07   
53  1 LEU D 265 ? ? -66.84  68.45   
54  1 ALA D 273 ? ? 173.76  143.53  
55  1 ALA D 304 ? ? -58.06  75.36   
56  1 ARG D 308 ? ? -68.88  2.98    
57  1 MET D 373 ? ? -178.38 137.60  
58  1 ASN D 380 ? ? -110.64 77.24   
59  1 ILE D 384 ? ? -58.44  -6.41   
60  1 GLN D 394 ? ? -35.21  -37.87  
61  1 MET D 398 ? ? -140.09 -47.37  
62  1 LYS D 402 ? ? 45.80   19.03   
63  1 PHE D 404 ? ? 55.39   10.09   
64  1 LEU D 405 ? ? -69.01  6.57    
65  1 TRP D 407 ? ? -49.14  -18.74  
66  1 GLU E 10  ? ? 35.52   36.84   
67  1 CYS E 14  ? ? -105.46 -169.35 
68  1 LYS E 25  ? ? 165.76  130.99  
69  1 PRO E 27  ? ? -59.93  -121.07 
70  1 LYS E 135 ? ? -67.27  25.80   
71  1 ASN E 136 ? ? -136.72 -40.46  
72  1 LYS E 137 ? ? -64.56  1.39    
73  1 GLU E 138 ? ? -110.22 58.00   
74  1 ALA F 23  ? ? -68.33  18.30   
75  1 THR F 83  ? ? -91.06  39.85   
76  1 LEU F 87  ? ? -131.57 -69.76  
77  1 SER F 88  ? ? 51.08   -160.95 
78  1 GLU F 89  ? ? -63.57  0.19    
79  1 SER F 90  ? ? -64.14  4.62    
80  1 PRO F 102 ? ? -66.61  94.89   
81  1 ASP F 126 ? ? -106.43 -159.80 
82  1 GLU F 127 ? ? -143.31 27.80   
83  1 ALA F 133 ? ? -43.09  -76.10  
84  1 ASN F 136 ? ? -57.25  92.54   
85  1 ALA F 166 ? ? -52.04  -107.79 
86  1 SER F 167 ? ? 34.10   -78.61  
87  1 GLU F 175 ? ? -59.14  -70.97  
88  1 LYS F 188 ? ? -103.30 76.98   
89  1 SER F 230 ? ? -41.46  -82.10  
90  1 ASN F 232 ? ? 72.89   113.59  
91  1 GLN F 234 ? ? -66.07  49.37   
92  1 LYS F 236 ? ? 83.35   -172.81 
93  1 THR F 237 ? ? 75.92   -53.47  
94  1 ILE F 245 ? ? -73.19  22.31   
95  1 GLU F 248 ? ? -179.57 10.96   
96  1 TYR F 249 ? ? -157.96 -12.00  
97  1 ASN F 276 ? ? 71.11   34.79   
98  1 GLU F 280 ? ? -39.49  -74.99  
99  1 GLN F 313 ? ? -171.92 146.38  
100 1 ILE F 330 ? ? -100.67 -73.97  
101 1 ARG B 2   ? ? 33.95   83.35   
102 1 PRO B 32  ? ? -52.15  -7.98   
103 1 HIS B 37  ? ? -142.20 46.04   
104 1 SER B 40  ? ? -173.08 133.30  
105 1 THR B 74  ? ? 48.57   -61.72  
106 1 GLN B 96  ? ? -132.64 -35.72  
107 1 THR B 109 ? ? -104.91 -82.07  
108 1 GLU B 127 ? ? -62.75  2.15    
109 1 CYS B 131 ? ? -156.87 87.66   
110 1 ARG B 215 ? ? -50.27  -85.80  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    N39 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    C 
_pdbx_validate_chiral.auth_comp_id    A1EPR 
_pdbx_validate_chiral.auth_seq_id     504 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
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 VAL 440 ? A VAL 440 
2   1 Y 1 A GLU 441 ? A GLU 441 
3   1 Y 1 A GLY 442 ? A GLY 442 
4   1 Y 1 A GLU 443 ? A GLU 443 
5   1 Y 1 A GLY 444 ? A GLY 444 
6   1 Y 1 A GLU 445 ? A GLU 445 
7   1 Y 1 A GLU 446 ? A GLU 446 
8   1 Y 1 A GLU 447 ? A GLU 447 
9   1 Y 1 A GLY 448 ? A GLY 448 
10  1 Y 1 A GLU 449 ? A GLU 449 
11  1 Y 1 A GLU 450 ? A GLU 450 
12  1 Y 1 C GLU 441 ? B GLU 441 
13  1 Y 1 C GLY 442 ? B GLY 442 
14  1 Y 1 C GLU 443 ? B GLU 443 
15  1 Y 1 C GLY 444 ? B GLY 444 
16  1 Y 1 C GLU 445 ? B GLU 445 
17  1 Y 1 C GLU 446 ? B GLU 446 
18  1 Y 1 C GLU 447 ? B GLU 447 
19  1 Y 1 C GLY 448 ? B GLY 448 
20  1 Y 1 C GLU 449 ? B GLU 449 
21  1 Y 1 C GLU 450 ? B GLU 450 
22  1 Y 1 D SER 277 ? C SER 275 
23  1 Y 1 D ARG 278 ? C ARG 276 
24  1 Y 1 D GLY 279 ? C GLY 277 
25  1 Y 1 D SER 280 ? C SER 278 
26  1 Y 1 D GLN 281 ? C GLN 279 
27  1 Y 1 D GLN 282 ? C GLN 280 
28  1 Y 1 D TYR 283 ? C TYR 281 
29  1 Y 1 D GLU 442 ? C GLU 432 
30  1 Y 1 D GLN 443 ? C GLN 433 
31  1 Y 1 D GLY 444 ? C GLY 434 
32  1 Y 1 D GLU 445 ? C GLU 435 
33  1 Y 1 D PHE 446 ? C PHE 436 
34  1 Y 1 D GLU 447 ? C GLU 437 
35  1 Y 1 D GLU 448 ? C GLU 438 
36  1 Y 1 D GLU 449 ? C GLU 439 
37  1 Y 1 D GLU 450 ? C GLU 440 
38  1 Y 1 D GLY 451 ? C GLY 441 
39  1 Y 1 D GLU 452 ? C GLU 442 
40  1 Y 1 D ASP 453 ? C ASP 443 
41  1 Y 1 D GLU 454 ? C GLU 444 
42  1 Y 1 D ALA 455 ? C ALA 445 
43  1 Y 1 E MET 3   ? D MET 1   
44  1 Y 1 E ALA 4   ? D ALA 2   
45  1 Y 1 E ASP 5   ? D ASP 3   
46  1 Y 1 E PHE 29  ? D PHE 27  
47  1 Y 1 E ASP 30  ? D ASP 28  
48  1 Y 1 E GLY 31  ? D GLY 29  
49  1 Y 1 E VAL 32  ? D VAL 30  
50  1 Y 1 E PRO 33  ? D PRO 31  
51  1 Y 1 E GLU 34  ? D GLU 32  
52  1 Y 1 E PHE 35  ? D PHE 33  
53  1 Y 1 E ASN 36  ? D ASN 34  
54  1 Y 1 E ALA 37  ? D ALA 35  
55  1 Y 1 E SER 38  ? D SER 36  
56  1 Y 1 E LEU 39  ? D LEU 37  
57  1 Y 1 E PRO 40  ? D PRO 38  
58  1 Y 1 E ARG 41  ? D ARG 39  
59  1 Y 1 E ARG 42  ? D ARG 40  
60  1 Y 1 E ARG 43  ? D ARG 41  
61  1 Y 1 E GLU 141 ? D GLU 139 
62  1 Y 1 E GLU 142 ? D GLU 140 
63  1 Y 1 E ALA 143 ? D ALA 141 
64  1 Y 1 E SER 144 ? D SER 142 
65  1 Y 1 E ARG 145 ? D ARG 143 
66  1 Y 1 F ASN 104 ? E ASN 104 
67  1 Y 1 F LEU 105 ? E LEU 105 
68  1 Y 1 F LYS 106 ? E LYS 106 
69  1 Y 1 F THR 107 ? E THR 107 
70  1 Y 1 F PRO 108 ? E PRO 108 
71  1 Y 1 F VAL 109 ? E VAL 109 
72  1 Y 1 F ALA 110 ? E ALA 110 
73  1 Y 1 F PRO 111 ? E PRO 111 
74  1 Y 1 F ALA 112 ? E ALA 112 
75  1 Y 1 F GLN 113 ? E GLN 113 
76  1 Y 1 F ASN 114 ? E ASN 114 
77  1 Y 1 F GLY 115 ? E GLY 115 
78  1 Y 1 F ILE 116 ? E ILE 116 
79  1 Y 1 F ARG 117 ? E ARG 117 
80  1 Y 1 F HIS 118 ? E HIS 118 
81  1 Y 1 F LEU 119 ? E LEU 119 
82  1 Y 1 F ILE 120 ? E ILE 120 
83  1 Y 1 F ASN 121 ? E ASN 121 
84  1 Y 1 F ASN 122 ? E ASN 122 
85  1 Y 1 F THR 123 ? E THR 123 
86  1 Y 1 F ARG 124 ? E ARG 124 
87  1 Y 1 F ARG 138 ? E ARG 138 
88  1 Y 1 F ARG 139 ? E ARG 139 
89  1 Y 1 F GLU 140 ? E GLU 140 
90  1 Y 1 F GLY 141 ? E GLY 141 
91  1 Y 1 F ARG 142 ? E ARG 142 
92  1 Y 1 F GLU 143 ? E GLU 143 
93  1 Y 1 F LYS 150 ? E LYS 150 
94  1 Y 1 F SER 151 ? E SER 151 
95  1 Y 1 F SER 152 ? E SER 152 
96  1 Y 1 F ALA 153 ? E ALA 153 
97  1 Y 1 F GLY 154 ? E GLY 154 
98  1 Y 1 F ALA 155 ? E ALA 155 
99  1 Y 1 F LYS 156 ? E LYS 156 
100 1 Y 1 F GLY 157 ? E GLY 157 
101 1 Y 1 F GLU 158 ? E GLU 158 
102 1 Y 1 F LYS 251 ? E LYS 251 
103 1 Y 1 F ASN 252 ? E ASN 252 
104 1 Y 1 F TYR 253 ? E TYR 253 
105 1 Y 1 F GLY 254 ? E GLY 254 
106 1 Y 1 F ASP 363 ? E ASP 363 
107 1 Y 1 F THR 364 ? E THR 364 
108 1 Y 1 F GLY 365 ? E GLY 365 
109 1 Y 1 F GLN 366 ? E GLN 366 
110 1 Y 1 F LYS 367 ? E LYS 367 
111 1 Y 1 F THR 368 ? E THR 368 
112 1 Y 1 F SER 369 ? E SER 369 
113 1 Y 1 F GLN 370 ? E GLN 370 
114 1 Y 1 F PRO 371 ? E PRO 371 
115 1 Y 1 F HIS 381 ? E HIS 381 
116 1 Y 1 F HIS 382 ? E HIS 382 
117 1 Y 1 F HIS 383 ? E HIS 383 
118 1 Y 1 F HIS 384 ? E HIS 384 
119 1 Y 1 B THR 439 ? F THR 429 
120 1 Y 1 B ALA 440 ? F ALA 430 
121 1 Y 1 B ASP 441 ? F ASP 431 
122 1 Y 1 B GLU 442 ? F GLU 432 
123 1 Y 1 B GLN 443 ? F GLN 433 
124 1 Y 1 B GLY 444 ? F GLY 434 
125 1 Y 1 B GLU 445 ? F GLU 435 
126 1 Y 1 B PHE 446 ? F PHE 436 
127 1 Y 1 B GLU 447 ? F GLU 437 
128 1 Y 1 B GLU 448 ? F GLU 438 
129 1 Y 1 B GLU 449 ? F GLU 439 
130 1 Y 1 B GLU 450 ? F GLU 440 
131 1 Y 1 B GLY 451 ? F GLY 441 
132 1 Y 1 B GLU 452 ? F GLU 442 
133 1 Y 1 B ASP 453 ? F ASP 443 
134 1 Y 1 B GLU 454 ? F GLU 444 
135 1 Y 1 B ALA 455 ? F ALA 445 
136 1 N 0 A GTP 501 ? G GTP ?   
137 1 N 0 A MG  502 ? H MG  ?   
138 1 N 0 A CA  503 ? I CA  ?   
139 1 N 0 C GTP 501 ? J GTP ?   
140 1 N 0 C MG  502 ? K MG  ?   
141 1 N 0 C CA  503 ? L CA  ?   
142 1 N 0 D GDP 501 ? N GDP ?   
143 1 N 0 B GDP 501 ? O GDP ?   
# 
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 
A1EPR C10    C  N N 1   
A1EPR C13    C  Y N 2   
A1EPR C15    C  Y N 3   
A1EPR C17    C  Y N 4   
A1EPR C20    C  N N 5   
A1EPR C21    C  N N 6   
A1EPR C22    C  N N 7   
A1EPR C26    C  N N 8   
A1EPR C02    C  N R 9   
A1EPR C03    C  N S 10  
A1EPR C04    C  N R 11  
A1EPR C05    C  N R 12  
A1EPR C06    C  N N 13  
A1EPR C07    C  N N 14  
A1EPR C08    C  N N 15  
A1EPR C11    C  N N 16  
A1EPR C12    C  N R 17  
A1EPR C14    C  Y N 18  
A1EPR C16    C  Y N 19  
A1EPR C18    C  Y N 20  
A1EPR C19    C  N R 21  
A1EPR C23    C  N N 22  
A1EPR C29    C  N N 23  
A1EPR C30    C  N N 24  
A1EPR C33    C  N N 25  
A1EPR C34    C  N N 26  
A1EPR C35    C  N R 27  
A1EPR C36    C  N N 28  
A1EPR C37    C  N S 29  
A1EPR C38    C  N N 30  
A1EPR C40    C  N N 31  
A1EPR C41    C  N N 32  
A1EPR C42    C  Y N 33  
A1EPR C43    C  Y N 34  
A1EPR C44    C  Y N 35  
A1EPR C45    C  Y N 36  
A1EPR C46    C  Y N 37  
A1EPR C47    C  Y N 38  
A1EPR C48    C  Y N 39  
A1EPR C50    C  Y N 40  
A1EPR C51    C  N S 41  
A1EPR C52    C  N N 42  
A1EPR C53    C  N N 43  
A1EPR C54    C  N N 44  
A1EPR C56    C  N N 45  
A1EPR C59    C  N N 46  
A1EPR F60    F  N N 47  
A1EPR N01    N  N N 48  
A1EPR N09    N  N N 49  
A1EPR N39    N  N R 50  
A1EPR N49    N  Y N 51  
A1EPR O24    O  N N 52  
A1EPR O25    O  N N 53  
A1EPR O27    O  N N 54  
A1EPR O28    O  N N 55  
A1EPR O31    O  N N 56  
A1EPR O32    O  N N 57  
A1EPR O55    O  N N 58  
A1EPR O57    O  N N 59  
A1EPR O58    O  N N 60  
A1EPR H102   H  N N 61  
A1EPR H101   H  N N 62  
A1EPR H171   H  N N 63  
A1EPR H201   H  N N 64  
A1EPR H202   H  N N 65  
A1EPR H213   H  N N 66  
A1EPR H212   H  N N 67  
A1EPR H211   H  N N 68  
A1EPR H223   H  N N 69  
A1EPR H221   H  N N 70  
A1EPR H222   H  N N 71  
A1EPR H262   H  N N 72  
A1EPR H263   H  N N 73  
A1EPR H261   H  N N 74  
A1EPR H1     H  N N 75  
A1EPR H041   H  N N 76  
A1EPR H061   H  N N 77  
A1EPR H071   H  N N 78  
A1EPR H081   H  N N 79  
A1EPR H112   H  N N 80  
A1EPR H111   H  N N 81  
A1EPR H141   H  N N 82  
A1EPR H191   H  N N 83  
A1EPR H301   H  N N 84  
A1EPR H302   H  N N 85  
A1EPR H303   H  N N 86  
A1EPR H332   H  N N 87  
A1EPR H333   H  N N 88  
A1EPR H331   H  N N 89  
A1EPR H341   H  N N 90  
A1EPR H342   H  N N 91  
A1EPR H351   H  N N 92  
A1EPR H361   H  N N 93  
A1EPR H362   H  N N 94  
A1EPR H382   H  N N 95  
A1EPR H381   H  N N 96  
A1EPR H401   H  N N 97  
A1EPR H402   H  N N 98  
A1EPR H411   H  N N 99  
A1EPR H412   H  N N 100 
A1EPR H441   H  N N 101 
A1EPR H451   H  N N 102 
A1EPR H471   H  N N 103 
A1EPR H522   H  N N 104 
A1EPR H521   H  N N 105 
A1EPR H531   H  N N 106 
A1EPR H532   H  N N 107 
A1EPR H543   H  N N 108 
A1EPR H541   H  N N 109 
A1EPR H542   H  N N 110 
A1EPR H591   H  N N 111 
A1EPR H593   H  N N 112 
A1EPR H592   H  N N 113 
A1EPR H491   H  N N 114 
A1EPR H271   H  N N 115 
A1EPR H551   H  N N 116 
A1EPR H2     H  N N 117 
ALA   N      N  N N 118 
ALA   CA     C  N S 119 
ALA   C      C  N N 120 
ALA   O      O  N N 121 
ALA   CB     C  N N 122 
ALA   OXT    O  N N 123 
ALA   H      H  N N 124 
ALA   H2     H  N N 125 
ALA   HA     H  N N 126 
ALA   HB1    H  N N 127 
ALA   HB2    H  N N 128 
ALA   HB3    H  N N 129 
ALA   HXT    H  N N 130 
ARG   N      N  N N 131 
ARG   CA     C  N S 132 
ARG   C      C  N N 133 
ARG   O      O  N N 134 
ARG   CB     C  N N 135 
ARG   CG     C  N N 136 
ARG   CD     C  N N 137 
ARG   NE     N  N N 138 
ARG   CZ     C  N N 139 
ARG   NH1    N  N N 140 
ARG   NH2    N  N N 141 
ARG   OXT    O  N N 142 
ARG   H      H  N N 143 
ARG   H2     H  N N 144 
ARG   HA     H  N N 145 
ARG   HB2    H  N N 146 
ARG   HB3    H  N N 147 
ARG   HG2    H  N N 148 
ARG   HG3    H  N N 149 
ARG   HD2    H  N N 150 
ARG   HD3    H  N N 151 
ARG   HE     H  N N 152 
ARG   HH11   H  N N 153 
ARG   HH12   H  N N 154 
ARG   HH21   H  N N 155 
ARG   HH22   H  N N 156 
ARG   HXT    H  N N 157 
ASN   N      N  N N 158 
ASN   CA     C  N S 159 
ASN   C      C  N N 160 
ASN   O      O  N N 161 
ASN   CB     C  N N 162 
ASN   CG     C  N N 163 
ASN   OD1    O  N N 164 
ASN   ND2    N  N N 165 
ASN   OXT    O  N N 166 
ASN   H      H  N N 167 
ASN   H2     H  N N 168 
ASN   HA     H  N N 169 
ASN   HB2    H  N N 170 
ASN   HB3    H  N N 171 
ASN   HD21   H  N N 172 
ASN   HD22   H  N N 173 
ASN   HXT    H  N N 174 
ASP   N      N  N N 175 
ASP   CA     C  N S 176 
ASP   C      C  N N 177 
ASP   O      O  N N 178 
ASP   CB     C  N N 179 
ASP   CG     C  N N 180 
ASP   OD1    O  N N 181 
ASP   OD2    O  N N 182 
ASP   OXT    O  N N 183 
ASP   H      H  N N 184 
ASP   H2     H  N N 185 
ASP   HA     H  N N 186 
ASP   HB2    H  N N 187 
ASP   HB3    H  N N 188 
ASP   HD2    H  N N 189 
ASP   HXT    H  N N 190 
CA    CA     CA N N 191 
CYS   N      N  N N 192 
CYS   CA     C  N R 193 
CYS   C      C  N N 194 
CYS   O      O  N N 195 
CYS   CB     C  N N 196 
CYS   SG     S  N N 197 
CYS   OXT    O  N N 198 
CYS   H      H  N N 199 
CYS   H2     H  N N 200 
CYS   HA     H  N N 201 
CYS   HB2    H  N N 202 
CYS   HB3    H  N N 203 
CYS   HG     H  N N 204 
CYS   HXT    H  N N 205 
GDP   PB     P  N N 206 
GDP   O1B    O  N N 207 
GDP   O2B    O  N N 208 
GDP   O3B    O  N N 209 
GDP   O3A    O  N N 210 
GDP   PA     P  N N 211 
GDP   O1A    O  N N 212 
GDP   O2A    O  N N 213 
GDP   "O5'"  O  N N 214 
GDP   "C5'"  C  N N 215 
GDP   "C4'"  C  N R 216 
GDP   "O4'"  O  N N 217 
GDP   "C3'"  C  N S 218 
GDP   "O3'"  O  N N 219 
GDP   "C2'"  C  N R 220 
GDP   "O2'"  O  N N 221 
GDP   "C1'"  C  N R 222 
GDP   N9     N  Y N 223 
GDP   C8     C  Y N 224 
GDP   N7     N  Y N 225 
GDP   C5     C  Y N 226 
GDP   C6     C  N N 227 
GDP   O6     O  N N 228 
GDP   N1     N  N N 229 
GDP   C2     C  N N 230 
GDP   N2     N  N N 231 
GDP   N3     N  N N 232 
GDP   C4     C  Y N 233 
GDP   HOB2   H  N N 234 
GDP   HOB3   H  N N 235 
GDP   HOA2   H  N N 236 
GDP   "H5'"  H  N N 237 
GDP   "H5''" H  N N 238 
GDP   "H4'"  H  N N 239 
GDP   "H3'"  H  N N 240 
GDP   "HO3'" H  N N 241 
GDP   "H2'"  H  N N 242 
GDP   "HO2'" H  N N 243 
GDP   "H1'"  H  N N 244 
GDP   H8     H  N N 245 
GDP   HN1    H  N N 246 
GDP   HN21   H  N N 247 
GDP   HN22   H  N N 248 
GLN   N      N  N N 249 
GLN   CA     C  N S 250 
GLN   C      C  N N 251 
GLN   O      O  N N 252 
GLN   CB     C  N N 253 
GLN   CG     C  N N 254 
GLN   CD     C  N N 255 
GLN   OE1    O  N N 256 
GLN   NE2    N  N N 257 
GLN   OXT    O  N N 258 
GLN   H      H  N N 259 
GLN   H2     H  N N 260 
GLN   HA     H  N N 261 
GLN   HB2    H  N N 262 
GLN   HB3    H  N N 263 
GLN   HG2    H  N N 264 
GLN   HG3    H  N N 265 
GLN   HE21   H  N N 266 
GLN   HE22   H  N N 267 
GLN   HXT    H  N N 268 
GLU   N      N  N N 269 
GLU   CA     C  N S 270 
GLU   C      C  N N 271 
GLU   O      O  N N 272 
GLU   CB     C  N N 273 
GLU   CG     C  N N 274 
GLU   CD     C  N N 275 
GLU   OE1    O  N N 276 
GLU   OE2    O  N N 277 
GLU   OXT    O  N N 278 
GLU   H      H  N N 279 
GLU   H2     H  N N 280 
GLU   HA     H  N N 281 
GLU   HB2    H  N N 282 
GLU   HB3    H  N N 283 
GLU   HG2    H  N N 284 
GLU   HG3    H  N N 285 
GLU   HE2    H  N N 286 
GLU   HXT    H  N N 287 
GLY   N      N  N N 288 
GLY   CA     C  N N 289 
GLY   C      C  N N 290 
GLY   O      O  N N 291 
GLY   OXT    O  N N 292 
GLY   H      H  N N 293 
GLY   H2     H  N N 294 
GLY   HA2    H  N N 295 
GLY   HA3    H  N N 296 
GLY   HXT    H  N N 297 
GTP   PG     P  N N 298 
GTP   O1G    O  N N 299 
GTP   O2G    O  N N 300 
GTP   O3G    O  N N 301 
GTP   O3B    O  N N 302 
GTP   PB     P  N N 303 
GTP   O1B    O  N N 304 
GTP   O2B    O  N N 305 
GTP   O3A    O  N N 306 
GTP   PA     P  N N 307 
GTP   O1A    O  N N 308 
GTP   O2A    O  N N 309 
GTP   "O5'"  O  N N 310 
GTP   "C5'"  C  N N 311 
GTP   "C4'"  C  N R 312 
GTP   "O4'"  O  N N 313 
GTP   "C3'"  C  N S 314 
GTP   "O3'"  O  N N 315 
GTP   "C2'"  C  N R 316 
GTP   "O2'"  O  N N 317 
GTP   "C1'"  C  N R 318 
GTP   N9     N  Y N 319 
GTP   C8     C  Y N 320 
GTP   N7     N  Y N 321 
GTP   C5     C  Y N 322 
GTP   C6     C  N N 323 
GTP   O6     O  N N 324 
GTP   N1     N  N N 325 
GTP   C2     C  N N 326 
GTP   N2     N  N N 327 
GTP   N3     N  N N 328 
GTP   C4     C  Y N 329 
GTP   HOG2   H  N N 330 
GTP   HOG3   H  N N 331 
GTP   HOB2   H  N N 332 
GTP   HOA2   H  N N 333 
GTP   "H5'"  H  N N 334 
GTP   "H5''" H  N N 335 
GTP   "H4'"  H  N N 336 
GTP   "H3'"  H  N N 337 
GTP   "HO3'" H  N N 338 
GTP   "H2'"  H  N N 339 
GTP   "HO2'" H  N N 340 
GTP   "H1'"  H  N N 341 
GTP   H8     H  N N 342 
GTP   HN1    H  N N 343 
GTP   HN21   H  N N 344 
GTP   HN22   H  N N 345 
HIS   N      N  N N 346 
HIS   CA     C  N S 347 
HIS   C      C  N N 348 
HIS   O      O  N N 349 
HIS   CB     C  N N 350 
HIS   CG     C  Y N 351 
HIS   ND1    N  Y N 352 
HIS   CD2    C  Y N 353 
HIS   CE1    C  Y N 354 
HIS   NE2    N  Y N 355 
HIS   OXT    O  N N 356 
HIS   H      H  N N 357 
HIS   H2     H  N N 358 
HIS   HA     H  N N 359 
HIS   HB2    H  N N 360 
HIS   HB3    H  N N 361 
HIS   HD1    H  N N 362 
HIS   HD2    H  N N 363 
HIS   HE1    H  N N 364 
HIS   HE2    H  N N 365 
HIS   HXT    H  N N 366 
HOH   O      O  N N 367 
HOH   H1     H  N N 368 
HOH   H2     H  N N 369 
ILE   N      N  N N 370 
ILE   CA     C  N S 371 
ILE   C      C  N N 372 
ILE   O      O  N N 373 
ILE   CB     C  N S 374 
ILE   CG1    C  N N 375 
ILE   CG2    C  N N 376 
ILE   CD1    C  N N 377 
ILE   OXT    O  N N 378 
ILE   H      H  N N 379 
ILE   H2     H  N N 380 
ILE   HA     H  N N 381 
ILE   HB     H  N N 382 
ILE   HG12   H  N N 383 
ILE   HG13   H  N N 384 
ILE   HG21   H  N N 385 
ILE   HG22   H  N N 386 
ILE   HG23   H  N N 387 
ILE   HD11   H  N N 388 
ILE   HD12   H  N N 389 
ILE   HD13   H  N N 390 
ILE   HXT    H  N N 391 
LEU   N      N  N N 392 
LEU   CA     C  N S 393 
LEU   C      C  N N 394 
LEU   O      O  N N 395 
LEU   CB     C  N N 396 
LEU   CG     C  N N 397 
LEU   CD1    C  N N 398 
LEU   CD2    C  N N 399 
LEU   OXT    O  N N 400 
LEU   H      H  N N 401 
LEU   H2     H  N N 402 
LEU   HA     H  N N 403 
LEU   HB2    H  N N 404 
LEU   HB3    H  N N 405 
LEU   HG     H  N N 406 
LEU   HD11   H  N N 407 
LEU   HD12   H  N N 408 
LEU   HD13   H  N N 409 
LEU   HD21   H  N N 410 
LEU   HD22   H  N N 411 
LEU   HD23   H  N N 412 
LEU   HXT    H  N N 413 
LYS   N      N  N N 414 
LYS   CA     C  N S 415 
LYS   C      C  N N 416 
LYS   O      O  N N 417 
LYS   CB     C  N N 418 
LYS   CG     C  N N 419 
LYS   CD     C  N N 420 
LYS   CE     C  N N 421 
LYS   NZ     N  N N 422 
LYS   OXT    O  N N 423 
LYS   H      H  N N 424 
LYS   H2     H  N N 425 
LYS   HA     H  N N 426 
LYS   HB2    H  N N 427 
LYS   HB3    H  N N 428 
LYS   HG2    H  N N 429 
LYS   HG3    H  N N 430 
LYS   HD2    H  N N 431 
LYS   HD3    H  N N 432 
LYS   HE2    H  N N 433 
LYS   HE3    H  N N 434 
LYS   HZ1    H  N N 435 
LYS   HZ2    H  N N 436 
LYS   HZ3    H  N N 437 
LYS   HXT    H  N N 438 
MET   N      N  N N 439 
MET   CA     C  N S 440 
MET   C      C  N N 441 
MET   O      O  N N 442 
MET   CB     C  N N 443 
MET   CG     C  N N 444 
MET   SD     S  N N 445 
MET   CE     C  N N 446 
MET   OXT    O  N N 447 
MET   H      H  N N 448 
MET   H2     H  N N 449 
MET   HA     H  N N 450 
MET   HB2    H  N N 451 
MET   HB3    H  N N 452 
MET   HG2    H  N N 453 
MET   HG3    H  N N 454 
MET   HE1    H  N N 455 
MET   HE2    H  N N 456 
MET   HE3    H  N N 457 
MET   HXT    H  N N 458 
MG    MG     MG N N 459 
PHE   N      N  N N 460 
PHE   CA     C  N S 461 
PHE   C      C  N N 462 
PHE   O      O  N N 463 
PHE   CB     C  N N 464 
PHE   CG     C  Y N 465 
PHE   CD1    C  Y N 466 
PHE   CD2    C  Y N 467 
PHE   CE1    C  Y N 468 
PHE   CE2    C  Y N 469 
PHE   CZ     C  Y N 470 
PHE   OXT    O  N N 471 
PHE   H      H  N N 472 
PHE   H2     H  N N 473 
PHE   HA     H  N N 474 
PHE   HB2    H  N N 475 
PHE   HB3    H  N N 476 
PHE   HD1    H  N N 477 
PHE   HD2    H  N N 478 
PHE   HE1    H  N N 479 
PHE   HE2    H  N N 480 
PHE   HZ     H  N N 481 
PHE   HXT    H  N N 482 
PRO   N      N  N N 483 
PRO   CA     C  N S 484 
PRO   C      C  N N 485 
PRO   O      O  N N 486 
PRO   CB     C  N N 487 
PRO   CG     C  N N 488 
PRO   CD     C  N N 489 
PRO   OXT    O  N N 490 
PRO   H      H  N N 491 
PRO   HA     H  N N 492 
PRO   HB2    H  N N 493 
PRO   HB3    H  N N 494 
PRO   HG2    H  N N 495 
PRO   HG3    H  N N 496 
PRO   HD2    H  N N 497 
PRO   HD3    H  N N 498 
PRO   HXT    H  N N 499 
SER   N      N  N N 500 
SER   CA     C  N S 501 
SER   C      C  N N 502 
SER   O      O  N N 503 
SER   CB     C  N N 504 
SER   OG     O  N N 505 
SER   OXT    O  N N 506 
SER   H      H  N N 507 
SER   H2     H  N N 508 
SER   HA     H  N N 509 
SER   HB2    H  N N 510 
SER   HB3    H  N N 511 
SER   HG     H  N N 512 
SER   HXT    H  N N 513 
THR   N      N  N N 514 
THR   CA     C  N S 515 
THR   C      C  N N 516 
THR   O      O  N N 517 
THR   CB     C  N R 518 
THR   OG1    O  N N 519 
THR   CG2    C  N N 520 
THR   OXT    O  N N 521 
THR   H      H  N N 522 
THR   H2     H  N N 523 
THR   HA     H  N N 524 
THR   HB     H  N N 525 
THR   HG1    H  N N 526 
THR   HG21   H  N N 527 
THR   HG22   H  N N 528 
THR   HG23   H  N N 529 
THR   HXT    H  N N 530 
TRP   N      N  N N 531 
TRP   CA     C  N S 532 
TRP   C      C  N N 533 
TRP   O      O  N N 534 
TRP   CB     C  N N 535 
TRP   CG     C  Y N 536 
TRP   CD1    C  Y N 537 
TRP   CD2    C  Y N 538 
TRP   NE1    N  Y N 539 
TRP   CE2    C  Y N 540 
TRP   CE3    C  Y N 541 
TRP   CZ2    C  Y N 542 
TRP   CZ3    C  Y N 543 
TRP   CH2    C  Y N 544 
TRP   OXT    O  N N 545 
TRP   H      H  N N 546 
TRP   H2     H  N N 547 
TRP   HA     H  N N 548 
TRP   HB2    H  N N 549 
TRP   HB3    H  N N 550 
TRP   HD1    H  N N 551 
TRP   HE1    H  N N 552 
TRP   HE3    H  N N 553 
TRP   HZ2    H  N N 554 
TRP   HZ3    H  N N 555 
TRP   HH2    H  N N 556 
TRP   HXT    H  N N 557 
TYR   N      N  N N 558 
TYR   CA     C  N S 559 
TYR   C      C  N N 560 
TYR   O      O  N N 561 
TYR   CB     C  N N 562 
TYR   CG     C  Y N 563 
TYR   CD1    C  Y N 564 
TYR   CD2    C  Y N 565 
TYR   CE1    C  Y N 566 
TYR   CE2    C  Y N 567 
TYR   CZ     C  Y N 568 
TYR   OH     O  N N 569 
TYR   OXT    O  N N 570 
TYR   H      H  N N 571 
TYR   H2     H  N N 572 
TYR   HA     H  N N 573 
TYR   HB2    H  N N 574 
TYR   HB3    H  N N 575 
TYR   HD1    H  N N 576 
TYR   HD2    H  N N 577 
TYR   HE1    H  N N 578 
TYR   HE2    H  N N 579 
TYR   HH     H  N N 580 
TYR   HXT    H  N N 581 
VAL   N      N  N N 582 
VAL   CA     C  N S 583 
VAL   C      C  N N 584 
VAL   O      O  N N 585 
VAL   CB     C  N N 586 
VAL   CG1    C  N N 587 
VAL   CG2    C  N N 588 
VAL   OXT    O  N N 589 
VAL   H      H  N N 590 
VAL   H2     H  N N 591 
VAL   HA     H  N N 592 
VAL   HB     H  N N 593 
VAL   HG11   H  N N 594 
VAL   HG12   H  N N 595 
VAL   HG13   H  N N 596 
VAL   HG21   H  N N 597 
VAL   HG22   H  N N 598 
VAL   HG23   H  N N 599 
VAL   HXT    H  N N 600 
# 
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 
A1EPR C10   C11    sing N N 1   
A1EPR C10   N09    sing N N 2   
A1EPR C13   C12    sing N N 3   
A1EPR C13   C14    doub Y N 4   
A1EPR C13   C18    sing Y N 5   
A1EPR C15   C14    sing Y N 6   
A1EPR C15   C16    doub Y N 7   
A1EPR C15   C51    sing N N 8   
A1EPR C17   C16    sing Y N 9   
A1EPR C17   C18    doub Y N 10  
A1EPR C20   C21    sing N N 11  
A1EPR C20   C05    sing N N 12  
A1EPR C22   N01    sing N N 13  
A1EPR C26   O25    sing N N 14  
A1EPR C02   C03    sing N N 15  
A1EPR C02   N01    sing N N 16  
A1EPR C03   C04    sing N N 17  
A1EPR C03   C23    sing N N 18  
A1EPR C03   O27    sing N N 19  
A1EPR C04   C05    sing N N 20  
A1EPR C04   O28    sing N N 21  
A1EPR C05   C06    sing N N 22  
A1EPR C05   C19    sing N N 23  
A1EPR C06   C07    doub N N 24  
A1EPR C07   C08    sing N N 25  
A1EPR C08   N09    sing N N 26  
A1EPR C11   C12    sing N N 27  
A1EPR C12   C19    sing N N 28  
A1EPR C16   O32    sing N N 29  
A1EPR C18   N01    sing N N 30  
A1EPR C19   N09    sing N N 31  
A1EPR C23   O24    doub N N 32  
A1EPR C23   O25    sing N N 33  
A1EPR C29   C30    sing N N 34  
A1EPR C29   O28    sing N N 35  
A1EPR C29   O31    doub N N 36  
A1EPR C33   O32    sing N N 37  
A1EPR C34   C35    sing N N 38  
A1EPR C34   C51    sing N N 39  
A1EPR C35   C36    sing N N 40  
A1EPR C35   C52    sing N N 41  
A1EPR C36   C37    sing N N 42  
A1EPR C37   C38    sing N N 43  
A1EPR C37   C53    sing N N 44  
A1EPR C37   O55    sing N N 45  
A1EPR C38   N39    sing N N 46  
A1EPR C40   C41    sing N N 47  
A1EPR C40   N39    sing N N 48  
A1EPR C41   C42    sing N N 49  
A1EPR C42   C43    sing Y N 50  
A1EPR C42   C50    doub Y N 51  
A1EPR C43   C44    doub Y N 52  
A1EPR C43   C48    sing Y N 53  
A1EPR C44   C45    sing Y N 54  
A1EPR C45   C46    doub Y N 55  
A1EPR C46   C47    sing Y N 56  
A1EPR C46   F60    sing N N 57  
A1EPR C47   C48    doub Y N 58  
A1EPR C48   N49    sing Y N 59  
A1EPR C50   C51    sing N N 60  
A1EPR C50   N49    sing Y N 61  
A1EPR C51   C56    sing N N 62  
A1EPR C52   N39    sing N N 63  
A1EPR C53   C54    sing N N 64  
A1EPR C56   O57    doub N N 65  
A1EPR C56   O58    sing N N 66  
A1EPR C59   O58    sing N N 67  
A1EPR C10   H102   sing N N 68  
A1EPR C10   H101   sing N N 69  
A1EPR C17   H171   sing N N 70  
A1EPR C20   H201   sing N N 71  
A1EPR C20   H202   sing N N 72  
A1EPR C21   H213   sing N N 73  
A1EPR C21   H212   sing N N 74  
A1EPR C21   H211   sing N N 75  
A1EPR C22   H223   sing N N 76  
A1EPR C22   H221   sing N N 77  
A1EPR C22   H222   sing N N 78  
A1EPR C26   H262   sing N N 79  
A1EPR C26   H263   sing N N 80  
A1EPR C26   H261   sing N N 81  
A1EPR C02   H1     sing N N 82  
A1EPR C04   H041   sing N N 83  
A1EPR C06   H061   sing N N 84  
A1EPR C07   H071   sing N N 85  
A1EPR C08   H081   sing N N 86  
A1EPR C11   H112   sing N N 87  
A1EPR C11   H111   sing N N 88  
A1EPR C14   H141   sing N N 89  
A1EPR C19   H191   sing N N 90  
A1EPR C30   H301   sing N N 91  
A1EPR C30   H302   sing N N 92  
A1EPR C30   H303   sing N N 93  
A1EPR C33   H332   sing N N 94  
A1EPR C33   H333   sing N N 95  
A1EPR C33   H331   sing N N 96  
A1EPR C34   H341   sing N N 97  
A1EPR C34   H342   sing N N 98  
A1EPR C35   H351   sing N N 99  
A1EPR C36   H361   sing N N 100 
A1EPR C36   H362   sing N N 101 
A1EPR C38   H382   sing N N 102 
A1EPR C38   H381   sing N N 103 
A1EPR C40   H401   sing N N 104 
A1EPR C40   H402   sing N N 105 
A1EPR C41   H411   sing N N 106 
A1EPR C41   H412   sing N N 107 
A1EPR C44   H441   sing N N 108 
A1EPR C45   H451   sing N N 109 
A1EPR C47   H471   sing N N 110 
A1EPR C52   H522   sing N N 111 
A1EPR C52   H521   sing N N 112 
A1EPR C53   H531   sing N N 113 
A1EPR C53   H532   sing N N 114 
A1EPR C54   H543   sing N N 115 
A1EPR C54   H541   sing N N 116 
A1EPR C54   H542   sing N N 117 
A1EPR C59   H591   sing N N 118 
A1EPR C59   H593   sing N N 119 
A1EPR C59   H592   sing N N 120 
A1EPR N49   H491   sing N N 121 
A1EPR O27   H271   sing N N 122 
A1EPR O55   H551   sing N N 123 
A1EPR C02   C12    sing N N 124 
A1EPR C08   H2     sing N N 125 
ALA   N     CA     sing N N 126 
ALA   N     H      sing N N 127 
ALA   N     H2     sing N N 128 
ALA   CA    C      sing N N 129 
ALA   CA    CB     sing N N 130 
ALA   CA    HA     sing N N 131 
ALA   C     O      doub N N 132 
ALA   C     OXT    sing N N 133 
ALA   CB    HB1    sing N N 134 
ALA   CB    HB2    sing N N 135 
ALA   CB    HB3    sing N N 136 
ALA   OXT   HXT    sing N N 137 
ARG   N     CA     sing N N 138 
ARG   N     H      sing N N 139 
ARG   N     H2     sing N N 140 
ARG   CA    C      sing N N 141 
ARG   CA    CB     sing N N 142 
ARG   CA    HA     sing N N 143 
ARG   C     O      doub N N 144 
ARG   C     OXT    sing N N 145 
ARG   CB    CG     sing N N 146 
ARG   CB    HB2    sing N N 147 
ARG   CB    HB3    sing N N 148 
ARG   CG    CD     sing N N 149 
ARG   CG    HG2    sing N N 150 
ARG   CG    HG3    sing N N 151 
ARG   CD    NE     sing N N 152 
ARG   CD    HD2    sing N N 153 
ARG   CD    HD3    sing N N 154 
ARG   NE    CZ     sing N N 155 
ARG   NE    HE     sing N N 156 
ARG   CZ    NH1    sing N N 157 
ARG   CZ    NH2    doub N N 158 
ARG   NH1   HH11   sing N N 159 
ARG   NH1   HH12   sing N N 160 
ARG   NH2   HH21   sing N N 161 
ARG   NH2   HH22   sing N N 162 
ARG   OXT   HXT    sing N N 163 
ASN   N     CA     sing N N 164 
ASN   N     H      sing N N 165 
ASN   N     H2     sing N N 166 
ASN   CA    C      sing N N 167 
ASN   CA    CB     sing N N 168 
ASN   CA    HA     sing N N 169 
ASN   C     O      doub N N 170 
ASN   C     OXT    sing N N 171 
ASN   CB    CG     sing N N 172 
ASN   CB    HB2    sing N N 173 
ASN   CB    HB3    sing N N 174 
ASN   CG    OD1    doub N N 175 
ASN   CG    ND2    sing N N 176 
ASN   ND2   HD21   sing N N 177 
ASN   ND2   HD22   sing N N 178 
ASN   OXT   HXT    sing N N 179 
ASP   N     CA     sing N N 180 
ASP   N     H      sing N N 181 
ASP   N     H2     sing N N 182 
ASP   CA    C      sing N N 183 
ASP   CA    CB     sing N N 184 
ASP   CA    HA     sing N N 185 
ASP   C     O      doub N N 186 
ASP   C     OXT    sing N N 187 
ASP   CB    CG     sing N N 188 
ASP   CB    HB2    sing N N 189 
ASP   CB    HB3    sing N N 190 
ASP   CG    OD1    doub N N 191 
ASP   CG    OD2    sing N N 192 
ASP   OD2   HD2    sing N N 193 
ASP   OXT   HXT    sing N N 194 
CYS   N     CA     sing N N 195 
CYS   N     H      sing N N 196 
CYS   N     H2     sing N N 197 
CYS   CA    C      sing N N 198 
CYS   CA    CB     sing N N 199 
CYS   CA    HA     sing N N 200 
CYS   C     O      doub N N 201 
CYS   C     OXT    sing N N 202 
CYS   CB    SG     sing N N 203 
CYS   CB    HB2    sing N N 204 
CYS   CB    HB3    sing N N 205 
CYS   SG    HG     sing N N 206 
CYS   OXT   HXT    sing N N 207 
GDP   PB    O1B    doub N N 208 
GDP   PB    O2B    sing N N 209 
GDP   PB    O3B    sing N N 210 
GDP   PB    O3A    sing N N 211 
GDP   O2B   HOB2   sing N N 212 
GDP   O3B   HOB3   sing N N 213 
GDP   O3A   PA     sing N N 214 
GDP   PA    O1A    doub N N 215 
GDP   PA    O2A    sing N N 216 
GDP   PA    "O5'"  sing N N 217 
GDP   O2A   HOA2   sing N N 218 
GDP   "O5'" "C5'"  sing N N 219 
GDP   "C5'" "C4'"  sing N N 220 
GDP   "C5'" "H5'"  sing N N 221 
GDP   "C5'" "H5''" sing N N 222 
GDP   "C4'" "O4'"  sing N N 223 
GDP   "C4'" "C3'"  sing N N 224 
GDP   "C4'" "H4'"  sing N N 225 
GDP   "O4'" "C1'"  sing N N 226 
GDP   "C3'" "O3'"  sing N N 227 
GDP   "C3'" "C2'"  sing N N 228 
GDP   "C3'" "H3'"  sing N N 229 
GDP   "O3'" "HO3'" sing N N 230 
GDP   "C2'" "O2'"  sing N N 231 
GDP   "C2'" "C1'"  sing N N 232 
GDP   "C2'" "H2'"  sing N N 233 
GDP   "O2'" "HO2'" sing N N 234 
GDP   "C1'" N9     sing N N 235 
GDP   "C1'" "H1'"  sing N N 236 
GDP   N9    C8     sing Y N 237 
GDP   N9    C4     sing Y N 238 
GDP   C8    N7     doub Y N 239 
GDP   C8    H8     sing N N 240 
GDP   N7    C5     sing Y N 241 
GDP   C5    C6     sing N N 242 
GDP   C5    C4     doub Y N 243 
GDP   C6    O6     doub N N 244 
GDP   C6    N1     sing N N 245 
GDP   N1    C2     sing N N 246 
GDP   N1    HN1    sing N N 247 
GDP   C2    N2     sing N N 248 
GDP   C2    N3     doub N N 249 
GDP   N2    HN21   sing N N 250 
GDP   N2    HN22   sing N N 251 
GDP   N3    C4     sing N N 252 
GLN   N     CA     sing N N 253 
GLN   N     H      sing N N 254 
GLN   N     H2     sing N N 255 
GLN   CA    C      sing N N 256 
GLN   CA    CB     sing N N 257 
GLN   CA    HA     sing N N 258 
GLN   C     O      doub N N 259 
GLN   C     OXT    sing N N 260 
GLN   CB    CG     sing N N 261 
GLN   CB    HB2    sing N N 262 
GLN   CB    HB3    sing N N 263 
GLN   CG    CD     sing N N 264 
GLN   CG    HG2    sing N N 265 
GLN   CG    HG3    sing N N 266 
GLN   CD    OE1    doub N N 267 
GLN   CD    NE2    sing N N 268 
GLN   NE2   HE21   sing N N 269 
GLN   NE2   HE22   sing N N 270 
GLN   OXT   HXT    sing N N 271 
GLU   N     CA     sing N N 272 
GLU   N     H      sing N N 273 
GLU   N     H2     sing N N 274 
GLU   CA    C      sing N N 275 
GLU   CA    CB     sing N N 276 
GLU   CA    HA     sing N N 277 
GLU   C     O      doub N N 278 
GLU   C     OXT    sing N N 279 
GLU   CB    CG     sing N N 280 
GLU   CB    HB2    sing N N 281 
GLU   CB    HB3    sing N N 282 
GLU   CG    CD     sing N N 283 
GLU   CG    HG2    sing N N 284 
GLU   CG    HG3    sing N N 285 
GLU   CD    OE1    doub N N 286 
GLU   CD    OE2    sing N N 287 
GLU   OE2   HE2    sing N N 288 
GLU   OXT   HXT    sing N N 289 
GLY   N     CA     sing N N 290 
GLY   N     H      sing N N 291 
GLY   N     H2     sing N N 292 
GLY   CA    C      sing N N 293 
GLY   CA    HA2    sing N N 294 
GLY   CA    HA3    sing N N 295 
GLY   C     O      doub N N 296 
GLY   C     OXT    sing N N 297 
GLY   OXT   HXT    sing N N 298 
GTP   PG    O1G    doub N N 299 
GTP   PG    O2G    sing N N 300 
GTP   PG    O3G    sing N N 301 
GTP   PG    O3B    sing N N 302 
GTP   O2G   HOG2   sing N N 303 
GTP   O3G   HOG3   sing N N 304 
GTP   O3B   PB     sing N N 305 
GTP   PB    O1B    doub N N 306 
GTP   PB    O2B    sing N N 307 
GTP   PB    O3A    sing N N 308 
GTP   O2B   HOB2   sing N N 309 
GTP   O3A   PA     sing N N 310 
GTP   PA    O1A    doub N N 311 
GTP   PA    O2A    sing N N 312 
GTP   PA    "O5'"  sing N N 313 
GTP   O2A   HOA2   sing N N 314 
GTP   "O5'" "C5'"  sing N N 315 
GTP   "C5'" "C4'"  sing N N 316 
GTP   "C5'" "H5'"  sing N N 317 
GTP   "C5'" "H5''" sing N N 318 
GTP   "C4'" "O4'"  sing N N 319 
GTP   "C4'" "C3'"  sing N N 320 
GTP   "C4'" "H4'"  sing N N 321 
GTP   "O4'" "C1'"  sing N N 322 
GTP   "C3'" "O3'"  sing N N 323 
GTP   "C3'" "C2'"  sing N N 324 
GTP   "C3'" "H3'"  sing N N 325 
GTP   "O3'" "HO3'" sing N N 326 
GTP   "C2'" "O2'"  sing N N 327 
GTP   "C2'" "C1'"  sing N N 328 
GTP   "C2'" "H2'"  sing N N 329 
GTP   "O2'" "HO2'" sing N N 330 
GTP   "C1'" N9     sing N N 331 
GTP   "C1'" "H1'"  sing N N 332 
GTP   N9    C8     sing Y N 333 
GTP   N9    C4     sing Y N 334 
GTP   C8    N7     doub Y N 335 
GTP   C8    H8     sing N N 336 
GTP   N7    C5     sing Y N 337 
GTP   C5    C6     sing N N 338 
GTP   C5    C4     doub Y N 339 
GTP   C6    O6     doub N N 340 
GTP   C6    N1     sing N N 341 
GTP   N1    C2     sing N N 342 
GTP   N1    HN1    sing N N 343 
GTP   C2    N2     sing N N 344 
GTP   C2    N3     doub N N 345 
GTP   N2    HN21   sing N N 346 
GTP   N2    HN22   sing N N 347 
GTP   N3    C4     sing N N 348 
HIS   N     CA     sing N N 349 
HIS   N     H      sing N N 350 
HIS   N     H2     sing N N 351 
HIS   CA    C      sing N N 352 
HIS   CA    CB     sing N N 353 
HIS   CA    HA     sing N N 354 
HIS   C     O      doub N N 355 
HIS   C     OXT    sing N N 356 
HIS   CB    CG     sing N N 357 
HIS   CB    HB2    sing N N 358 
HIS   CB    HB3    sing N N 359 
HIS   CG    ND1    sing Y N 360 
HIS   CG    CD2    doub Y N 361 
HIS   ND1   CE1    doub Y N 362 
HIS   ND1   HD1    sing N N 363 
HIS   CD2   NE2    sing Y N 364 
HIS   CD2   HD2    sing N N 365 
HIS   CE1   NE2    sing Y N 366 
HIS   CE1   HE1    sing N N 367 
HIS   NE2   HE2    sing N N 368 
HIS   OXT   HXT    sing N N 369 
HOH   O     H1     sing N N 370 
HOH   O     H2     sing N N 371 
ILE   N     CA     sing N N 372 
ILE   N     H      sing N N 373 
ILE   N     H2     sing N N 374 
ILE   CA    C      sing N N 375 
ILE   CA    CB     sing N N 376 
ILE   CA    HA     sing N N 377 
ILE   C     O      doub N N 378 
ILE   C     OXT    sing N N 379 
ILE   CB    CG1    sing N N 380 
ILE   CB    CG2    sing N N 381 
ILE   CB    HB     sing N N 382 
ILE   CG1   CD1    sing N N 383 
ILE   CG1   HG12   sing N N 384 
ILE   CG1   HG13   sing N N 385 
ILE   CG2   HG21   sing N N 386 
ILE   CG2   HG22   sing N N 387 
ILE   CG2   HG23   sing N N 388 
ILE   CD1   HD11   sing N N 389 
ILE   CD1   HD12   sing N N 390 
ILE   CD1   HD13   sing N N 391 
ILE   OXT   HXT    sing N N 392 
LEU   N     CA     sing N N 393 
LEU   N     H      sing N N 394 
LEU   N     H2     sing N N 395 
LEU   CA    C      sing N N 396 
LEU   CA    CB     sing N N 397 
LEU   CA    HA     sing N N 398 
LEU   C     O      doub N N 399 
LEU   C     OXT    sing N N 400 
LEU   CB    CG     sing N N 401 
LEU   CB    HB2    sing N N 402 
LEU   CB    HB3    sing N N 403 
LEU   CG    CD1    sing N N 404 
LEU   CG    CD2    sing N N 405 
LEU   CG    HG     sing N N 406 
LEU   CD1   HD11   sing N N 407 
LEU   CD1   HD12   sing N N 408 
LEU   CD1   HD13   sing N N 409 
LEU   CD2   HD21   sing N N 410 
LEU   CD2   HD22   sing N N 411 
LEU   CD2   HD23   sing N N 412 
LEU   OXT   HXT    sing N N 413 
LYS   N     CA     sing N N 414 
LYS   N     H      sing N N 415 
LYS   N     H2     sing N N 416 
LYS   CA    C      sing N N 417 
LYS   CA    CB     sing N N 418 
LYS   CA    HA     sing N N 419 
LYS   C     O      doub N N 420 
LYS   C     OXT    sing N N 421 
LYS   CB    CG     sing N N 422 
LYS   CB    HB2    sing N N 423 
LYS   CB    HB3    sing N N 424 
LYS   CG    CD     sing N N 425 
LYS   CG    HG2    sing N N 426 
LYS   CG    HG3    sing N N 427 
LYS   CD    CE     sing N N 428 
LYS   CD    HD2    sing N N 429 
LYS   CD    HD3    sing N N 430 
LYS   CE    NZ     sing N N 431 
LYS   CE    HE2    sing N N 432 
LYS   CE    HE3    sing N N 433 
LYS   NZ    HZ1    sing N N 434 
LYS   NZ    HZ2    sing N N 435 
LYS   NZ    HZ3    sing N N 436 
LYS   OXT   HXT    sing N N 437 
MET   N     CA     sing N N 438 
MET   N     H      sing N N 439 
MET   N     H2     sing N N 440 
MET   CA    C      sing N N 441 
MET   CA    CB     sing N N 442 
MET   CA    HA     sing N N 443 
MET   C     O      doub N N 444 
MET   C     OXT    sing N N 445 
MET   CB    CG     sing N N 446 
MET   CB    HB2    sing N N 447 
MET   CB    HB3    sing N N 448 
MET   CG    SD     sing N N 449 
MET   CG    HG2    sing N N 450 
MET   CG    HG3    sing N N 451 
MET   SD    CE     sing N N 452 
MET   CE    HE1    sing N N 453 
MET   CE    HE2    sing N N 454 
MET   CE    HE3    sing N N 455 
MET   OXT   HXT    sing N N 456 
PHE   N     CA     sing N N 457 
PHE   N     H      sing N N 458 
PHE   N     H2     sing N N 459 
PHE   CA    C      sing N N 460 
PHE   CA    CB     sing N N 461 
PHE   CA    HA     sing N N 462 
PHE   C     O      doub N N 463 
PHE   C     OXT    sing N N 464 
PHE   CB    CG     sing N N 465 
PHE   CB    HB2    sing N N 466 
PHE   CB    HB3    sing N N 467 
PHE   CG    CD1    doub Y N 468 
PHE   CG    CD2    sing Y N 469 
PHE   CD1   CE1    sing Y N 470 
PHE   CD1   HD1    sing N N 471 
PHE   CD2   CE2    doub Y N 472 
PHE   CD2   HD2    sing N N 473 
PHE   CE1   CZ     doub Y N 474 
PHE   CE1   HE1    sing N N 475 
PHE   CE2   CZ     sing Y N 476 
PHE   CE2   HE2    sing N N 477 
PHE   CZ    HZ     sing N N 478 
PHE   OXT   HXT    sing N N 479 
PRO   N     CA     sing N N 480 
PRO   N     CD     sing N N 481 
PRO   N     H      sing N N 482 
PRO   CA    C      sing N N 483 
PRO   CA    CB     sing N N 484 
PRO   CA    HA     sing N N 485 
PRO   C     O      doub N N 486 
PRO   C     OXT    sing N N 487 
PRO   CB    CG     sing N N 488 
PRO   CB    HB2    sing N N 489 
PRO   CB    HB3    sing N N 490 
PRO   CG    CD     sing N N 491 
PRO   CG    HG2    sing N N 492 
PRO   CG    HG3    sing N N 493 
PRO   CD    HD2    sing N N 494 
PRO   CD    HD3    sing N N 495 
PRO   OXT   HXT    sing N N 496 
SER   N     CA     sing N N 497 
SER   N     H      sing N N 498 
SER   N     H2     sing N N 499 
SER   CA    C      sing N N 500 
SER   CA    CB     sing N N 501 
SER   CA    HA     sing N N 502 
SER   C     O      doub N N 503 
SER   C     OXT    sing N N 504 
SER   CB    OG     sing N N 505 
SER   CB    HB2    sing N N 506 
SER   CB    HB3    sing N N 507 
SER   OG    HG     sing N N 508 
SER   OXT   HXT    sing N N 509 
THR   N     CA     sing N N 510 
THR   N     H      sing N N 511 
THR   N     H2     sing N N 512 
THR   CA    C      sing N N 513 
THR   CA    CB     sing N N 514 
THR   CA    HA     sing N N 515 
THR   C     O      doub N N 516 
THR   C     OXT    sing N N 517 
THR   CB    OG1    sing N N 518 
THR   CB    CG2    sing N N 519 
THR   CB    HB     sing N N 520 
THR   OG1   HG1    sing N N 521 
THR   CG2   HG21   sing N N 522 
THR   CG2   HG22   sing N N 523 
THR   CG2   HG23   sing N N 524 
THR   OXT   HXT    sing N N 525 
TRP   N     CA     sing N N 526 
TRP   N     H      sing N N 527 
TRP   N     H2     sing N N 528 
TRP   CA    C      sing N N 529 
TRP   CA    CB     sing N N 530 
TRP   CA    HA     sing N N 531 
TRP   C     O      doub N N 532 
TRP   C     OXT    sing N N 533 
TRP   CB    CG     sing N N 534 
TRP   CB    HB2    sing N N 535 
TRP   CB    HB3    sing N N 536 
TRP   CG    CD1    doub Y N 537 
TRP   CG    CD2    sing Y N 538 
TRP   CD1   NE1    sing Y N 539 
TRP   CD1   HD1    sing N N 540 
TRP   CD2   CE2    doub Y N 541 
TRP   CD2   CE3    sing Y N 542 
TRP   NE1   CE2    sing Y N 543 
TRP   NE1   HE1    sing N N 544 
TRP   CE2   CZ2    sing Y N 545 
TRP   CE3   CZ3    doub Y N 546 
TRP   CE3   HE3    sing N N 547 
TRP   CZ2   CH2    doub Y N 548 
TRP   CZ2   HZ2    sing N N 549 
TRP   CZ3   CH2    sing Y N 550 
TRP   CZ3   HZ3    sing N N 551 
TRP   CH2   HH2    sing N N 552 
TRP   OXT   HXT    sing N N 553 
TYR   N     CA     sing N N 554 
TYR   N     H      sing N N 555 
TYR   N     H2     sing N N 556 
TYR   CA    C      sing N N 557 
TYR   CA    CB     sing N N 558 
TYR   CA    HA     sing N N 559 
TYR   C     O      doub N N 560 
TYR   C     OXT    sing N N 561 
TYR   CB    CG     sing N N 562 
TYR   CB    HB2    sing N N 563 
TYR   CB    HB3    sing N N 564 
TYR   CG    CD1    doub Y N 565 
TYR   CG    CD2    sing Y N 566 
TYR   CD1   CE1    sing Y N 567 
TYR   CD1   HD1    sing N N 568 
TYR   CD2   CE2    doub Y N 569 
TYR   CD2   HD2    sing N N 570 
TYR   CE1   CZ     doub Y N 571 
TYR   CE1   HE1    sing N N 572 
TYR   CE2   CZ     sing Y N 573 
TYR   CE2   HE2    sing N N 574 
TYR   CZ    OH     sing N N 575 
TYR   OH    HH     sing N N 576 
TYR   OXT   HXT    sing N N 577 
VAL   N     CA     sing N N 578 
VAL   N     H      sing N N 579 
VAL   N     H2     sing N N 580 
VAL   CA    C      sing N N 581 
VAL   CA    CB     sing N N 582 
VAL   CA    HA     sing N N 583 
VAL   C     O      doub N N 584 
VAL   C     OXT    sing N N 585 
VAL   CB    CG1    sing N N 586 
VAL   CB    CG2    sing N N 587 
VAL   CB    HB     sing N N 588 
VAL   CG1   HG11   sing N N 589 
VAL   CG1   HG12   sing N N 590 
VAL   CG1   HG13   sing N N 591 
VAL   CG2   HG21   sing N N 592 
VAL   CG2   HG22   sing N N 593 
VAL   CG2   HG23   sing N N 594 
VAL   OXT   HXT    sing N N 595 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   8CLE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LNV 
_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]   0.009505 
_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]   0.006391 
_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]   0.005414 
_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  
CA 
F  
H  
MG 
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     . MET   A 1  1   ? 39.892  101.276 67.877  1.00 61.68  ? 1   MET   A N     1 
ATOM   2     C  CA    . MET   A 1  1   ? 38.978  100.454 67.082  1.00 73.56  ? 1   MET   A CA    1 
ATOM   3     C  C     . MET   A 1  1   ? 39.712  99.360  66.287  1.00 74.04  ? 1   MET   A C     1 
ATOM   4     O  O     . MET   A 1  1   ? 40.690  99.629  65.575  1.00 75.90  ? 1   MET   A O     1 
ATOM   5     C  CB    . MET   A 1  1   ? 38.154  101.343 66.138  1.00 60.05  ? 1   MET   A CB    1 
ATOM   6     C  CG    . MET   A 1  1   ? 37.381  100.578 65.083  1.00 56.95  ? 1   MET   A CG    1 
ATOM   7     S  SD    . MET   A 1  1   ? 38.403  100.212 63.636  1.00 65.59  ? 1   MET   A SD    1 
ATOM   8     C  CE    . MET   A 1  1   ? 38.573  101.846 62.918  1.00 53.94  ? 1   MET   A CE    1 
ATOM   9     N  N     . ARG   A 1  2   ? 39.218  98.129  66.401  1.00 67.42  ? 2   ARG   A N     1 
ATOM   10    C  CA    . ARG   A 1  2   ? 39.792  96.968  65.732  1.00 58.89  ? 2   ARG   A CA    1 
ATOM   11    C  C     . ARG   A 1  2   ? 38.816  96.426  64.687  1.00 58.93  ? 2   ARG   A C     1 
ATOM   12    O  O     . ARG   A 1  2   ? 37.641  96.171  64.988  1.00 47.52  ? 2   ARG   A O     1 
ATOM   13    C  CB    . ARG   A 1  2   ? 40.140  95.894  66.758  1.00 57.99  ? 2   ARG   A CB    1 
ATOM   14    C  CG    . ARG   A 1  2   ? 40.365  96.444  68.159  1.00 61.77  ? 2   ARG   A CG    1 
ATOM   15    C  CD    . ARG   A 1  2   ? 40.946  95.367  69.039  1.00 64.72  ? 2   ARG   A CD    1 
ATOM   16    N  NE    . ARG   A 1  2   ? 41.971  94.634  68.306  1.00 63.12  ? 2   ARG   A NE    1 
ATOM   17    C  CZ    . ARG   A 1  2   ? 42.472  93.466  68.683  1.00 64.78  ? 2   ARG   A CZ    1 
ATOM   18    N  NH1   . ARG   A 1  2   ? 42.065  92.867  69.796  1.00 53.60  ? 2   ARG   A NH1   1 
ATOM   19    N  NH2   . ARG   A 1  2   ? 43.405  92.887  67.925  1.00 56.36  ? 2   ARG   A NH2   1 
ATOM   20    N  N     . GLU   A 1  3   ? 39.306  96.246  63.464  1.00 57.59  ? 3   GLU   A N     1 
ATOM   21    C  CA    . GLU   A 1  3   ? 38.441  95.873  62.355  1.00 51.56  ? 3   GLU   A CA    1 
ATOM   22    C  C     . GLU   A 1  3   ? 38.070  94.399  62.411  1.00 50.20  ? 3   GLU   A C     1 
ATOM   23    O  O     . GLU   A 1  3   ? 38.798  93.562  62.957  1.00 48.75  ? 3   GLU   A O     1 
ATOM   24    C  CB    . GLU   A 1  3   ? 39.115  96.178  61.021  1.00 55.58  ? 3   GLU   A CB    1 
ATOM   25    C  CG    . GLU   A 1  3   ? 39.620  97.613  60.892  1.00 62.08  ? 3   GLU   A CG    1 
ATOM   26    C  CD    . GLU   A 1  3   ? 41.041  97.817  61.428  1.00 54.91  ? 3   GLU   A CD    1 
ATOM   27    O  OE1   . GLU   A 1  3   ? 41.675  96.838  61.885  1.00 48.95  ? 3   GLU   A OE1   1 
ATOM   28    O  OE2   . GLU   A 1  3   ? 41.517  98.971  61.376  1.00 52.97  ? 3   GLU   A OE2   1 
ATOM   29    N  N     . CYS   A 1  4   ? 36.913  94.094  61.842  1.00 47.75  ? 4   CYS   A N     1 
ATOM   30    C  CA    . CYS   A 1  4   ? 36.426  92.734  61.697  1.00 48.54  ? 4   CYS   A CA    1 
ATOM   31    C  C     . CYS   A 1  4   ? 36.154  92.476  60.225  1.00 46.47  ? 4   CYS   A C     1 
ATOM   32    O  O     . CYS   A 1  4   ? 35.556  93.313  59.535  1.00 40.50  ? 4   CYS   A O     1 
ATOM   33    C  CB    . CYS   A 1  4   ? 35.141  92.503  62.512  1.00 47.10  ? 4   CYS   A CB    1 
ATOM   34    S  SG    . CYS   A 1  4   ? 35.362  92.331  64.290  1.00 61.86  ? 4   CYS   A SG    1 
ATOM   35    N  N     . ILE   A 1  5   ? 36.591  91.320  59.735  1.00 43.24  ? 5   ILE   A N     1 
ATOM   36    C  CA    . ILE   A 1  5   ? 36.366  90.941  58.344  1.00 45.75  ? 5   ILE   A CA    1 
ATOM   37    C  C     . ILE   A 1  5   ? 35.346  89.811  58.283  1.00 40.14  ? 5   ILE   A C     1 
ATOM   38    O  O     . ILE   A 1  5   ? 35.469  88.804  58.994  1.00 41.89  ? 5   ILE   A O     1 
ATOM   39    C  CB    . ILE   A 1  5   ? 37.675  90.545  57.648  1.00 49.85  ? 5   ILE   A CB    1 
ATOM   40    C  CG1   . ILE   A 1  5   ? 38.453  91.813  57.280  1.00 43.22  ? 5   ILE   A CG1   1 
ATOM   41    C  CG2   . ILE   A 1  5   ? 37.361  89.669  56.437  1.00 44.00  ? 5   ILE   A CG2   1 
ATOM   42    C  CD1   . ILE   A 1  5   ? 39.902  91.575  56.998  1.00 48.80  ? 5   ILE   A CD1   1 
ATOM   43    N  N     . SER   A 1  6   ? 34.330  89.993  57.449  1.00 44.94  ? 6   SER   A N     1 
ATOM   44    C  CA    . SER   A 1  6   ? 33.323  88.975  57.198  1.00 42.19  ? 6   SER   A CA    1 
ATOM   45    C  C     . SER   A 1  6   ? 33.731  88.166  55.975  1.00 40.27  ? 6   SER   A C     1 
ATOM   46    O  O     . SER   A 1  6   ? 34.338  88.697  55.045  1.00 51.83  ? 6   SER   A O     1 
ATOM   47    C  CB    . SER   A 1  6   ? 31.954  89.624  56.976  1.00 46.94  ? 6   SER   A CB    1 
ATOM   48    O  OG    . SER   A 1  6   ? 31.421  90.186  58.173  1.00 39.40  ? 6   SER   A OG    1 
ATOM   49    N  N     . ILE   A 1  7   ? 33.409  86.874  55.984  1.00 35.11  ? 7   ILE   A N     1 
ATOM   50    C  CA    . ILE   A 1  7   ? 33.733  85.979  54.868  1.00 43.45  ? 7   ILE   A CA    1 
ATOM   51    C  C     . ILE   A 1  7   ? 32.511  85.110  54.579  1.00 37.58  ? 7   ILE   A C     1 
ATOM   52    O  O     . ILE   A 1  7   ? 32.173  84.227  55.373  1.00 42.65  ? 7   ILE   A O     1 
ATOM   53    C  CB    . ILE   A 1  7   ? 34.959  85.094  55.152  1.00 46.79  ? 7   ILE   A CB    1 
ATOM   54    C  CG1   . ILE   A 1  7   ? 36.165  85.929  55.577  1.00 43.04  ? 7   ILE   A CG1   1 
ATOM   55    C  CG2   . ILE   A 1  7   ? 35.302  84.216  53.931  1.00 38.55  ? 7   ILE   A CG2   1 
ATOM   56    C  CD1   . ILE   A 1  7   ? 37.376  85.076  55.947  1.00 39.82  ? 7   ILE   A CD1   1 
ATOM   57    N  N     . HIS   A 1  8   ? 31.879  85.324  53.435  1.00 37.90  ? 8   HIS   A N     1 
ATOM   58    C  CA    . HIS   A 1  8   ? 30.625  84.664  53.088  1.00 38.19  ? 8   HIS   A CA    1 
ATOM   59    C  C     . HIS   A 1  8   ? 30.896  83.555  52.082  1.00 37.04  ? 8   HIS   A C     1 
ATOM   60    O  O     . HIS   A 1  8   ? 31.229  83.834  50.929  1.00 36.49  ? 8   HIS   A O     1 
ATOM   61    C  CB    . HIS   A 1  8   ? 29.645  85.691  52.540  1.00 37.81  ? 8   HIS   A CB    1 
ATOM   62    C  CG    . HIS   A 1  8   ? 29.456  86.865  53.452  1.00 47.07  ? 8   HIS   A CG    1 
ATOM   63    N  ND1   . HIS   A 1  8   ? 28.665  86.808  54.580  1.00 48.07  ? 8   HIS   A ND1   1 
ATOM   64    C  CD2   . HIS   A 1  8   ? 29.979  88.115  53.421  1.00 49.33  ? 8   HIS   A CD2   1 
ATOM   65    C  CE1   . HIS   A 1  8   ? 28.693  87.979  55.194  1.00 47.78  ? 8   HIS   A CE1   1 
ATOM   66    N  NE2   . HIS   A 1  8   ? 29.482  88.789  54.512  1.00 43.93  ? 8   HIS   A NE2   1 
ATOM   67    N  N     . VAL   A 1  9   ? 30.728  82.302  52.519  1.00 37.78  ? 9   VAL   A N     1 
ATOM   68    C  CA    . VAL   A 1  9   ? 31.140  81.107  51.779  1.00 28.65  ? 9   VAL   A CA    1 
ATOM   69    C  C     . VAL   A 1  9   ? 29.898  80.330  51.361  1.00 32.57  ? 9   VAL   A C     1 
ATOM   70    O  O     . VAL   A 1  9   ? 29.064  79.979  52.205  1.00 39.85  ? 9   VAL   A O     1 
ATOM   71    C  CB    . VAL   A 1  9   ? 32.063  80.205  52.623  1.00 27.33  ? 9   VAL   A CB    1 
ATOM   72    C  CG1   . VAL   A 1  9   ? 32.558  79.050  51.801  1.00 38.46  ? 9   VAL   A CG1   1 
ATOM   73    C  CG2   . VAL   A 1  9   ? 33.232  80.976  53.194  1.00 30.95  ? 9   VAL   A CG2   1 
ATOM   74    N  N     . GLY   A 1  10  ? 29.787  80.034  50.069  1.00 35.50  ? 10  GLY   A N     1 
ATOM   75    C  CA    . GLY   A 1  10  ? 28.663  79.273  49.559  1.00 34.03  ? 10  GLY   A CA    1 
ATOM   76    C  C     . GLY   A 1  10  ? 27.435  80.126  49.297  1.00 31.75  ? 10  GLY   A C     1 
ATOM   77    O  O     . GLY   A 1  10  ? 27.393  81.318  49.584  1.00 36.58  ? 10  GLY   A O     1 
ATOM   78    N  N     . GLN   A 1  11  ? 26.405  79.486  48.736  1.00 25.22  ? 11  GLN   A N     1 
ATOM   79    C  CA    . GLN   A 1  11  ? 25.171  80.204  48.432  1.00 29.18  ? 11  GLN   A CA    1 
ATOM   80    C  C     . GLN   A 1  11  ? 24.539  80.767  49.698  1.00 39.16  ? 11  GLN   A C     1 
ATOM   81    O  O     . GLN   A 1  11  ? 24.086  81.921  49.717  1.00 32.93  ? 11  GLN   A O     1 
ATOM   82    C  CB    . GLN   A 1  11  ? 24.181  79.285  47.709  1.00 28.44  ? 11  GLN   A CB    1 
ATOM   83    C  CG    . GLN   A 1  11  ? 22.775  79.883  47.529  1.00 29.91  ? 11  GLN   A CG    1 
ATOM   84    C  CD    . GLN   A 1  11  ? 21.875  79.055  46.617  1.00 30.21  ? 11  GLN   A CD    1 
ATOM   85    O  OE1   . GLN   A 1  11  ? 22.192  78.845  45.452  1.00 51.78  ? 11  GLN   A OE1   1 
ATOM   86    N  NE2   . GLN   A 1  11  ? 20.742  78.609  47.134  1.00 20.62  ? 11  GLN   A NE2   1 
ATOM   87    N  N     . ALA   A 1  12  ? 24.501  79.960  50.766  1.00 31.61  ? 12  ALA   A N     1 
ATOM   88    C  CA    . ALA   A 1  12  ? 23.843  80.377  51.995  1.00 24.56  ? 12  ALA   A CA    1 
ATOM   89    C  C     . ALA   A 1  12  ? 24.603  81.514  52.667  1.00 35.79  ? 12  ALA   A C     1 
ATOM   90    O  O     . ALA   A 1  12  ? 24.023  82.564  52.974  1.00 37.94  ? 12  ALA   A O     1 
ATOM   91    C  CB    . ALA   A 1  12  ? 23.690  79.190  52.943  1.00 22.14  ? 12  ALA   A CB    1 
ATOM   92    N  N     . GLY   A 1  13  ? 25.902  81.325  52.910  1.00 32.26  ? 13  GLY   A N     1 
ATOM   93    C  CA    . GLY   A 1  13  ? 26.703  82.421  53.436  1.00 34.16  ? 13  GLY   A CA    1 
ATOM   94    C  C     . GLY   A 1  13  ? 26.571  83.685  52.607  1.00 38.19  ? 13  GLY   A C     1 
ATOM   95    O  O     . GLY   A 1  13  ? 26.442  84.784  53.153  1.00 35.04  ? 13  GLY   A O     1 
ATOM   96    N  N     . VAL   A 1  14  ? 26.578  83.538  51.273  1.00 35.97  ? 14  VAL   A N     1 
ATOM   97    C  CA    . VAL   A 1  14  ? 26.510  84.684  50.369  1.00 35.41  ? 14  VAL   A CA    1 
ATOM   98    C  C     . VAL   A 1  14  ? 25.147  85.358  50.462  1.00 39.00  ? 14  VAL   A C     1 
ATOM   99    O  O     . VAL   A 1  14  ? 25.046  86.583  50.578  1.00 34.45  ? 14  VAL   A O     1 
ATOM   100   C  CB    . VAL   A 1  14  ? 26.815  84.248  48.921  1.00 33.83  ? 14  VAL   A CB    1 
ATOM   101   C  CG1   . VAL   A 1  14  ? 26.450  85.347  47.928  1.00 33.61  ? 14  VAL   A CG1   1 
ATOM   102   C  CG2   . VAL   A 1  14  ? 28.261  83.907  48.768  1.00 34.78  ? 14  VAL   A CG2   1 
ATOM   103   N  N     . GLN   A 1  15  ? 24.075  84.573  50.395  1.00 41.81  ? 15  GLN   A N     1 
ATOM   104   C  CA    . GLN   A 1  15  ? 22.749  85.176  50.451  1.00 41.62  ? 15  GLN   A CA    1 
ATOM   105   C  C     . GLN   A 1  15  ? 22.425  85.690  51.849  1.00 37.74  ? 15  GLN   A C     1 
ATOM   106   O  O     . GLN   A 1  15  ? 21.744  86.716  51.986  1.00 35.40  ? 15  GLN   A O     1 
ATOM   107   C  CB    . GLN   A 1  15  ? 21.699  84.182  49.950  1.00 31.20  ? 15  GLN   A CB    1 
ATOM   108   C  CG    . GLN   A 1  15  ? 21.566  84.275  48.458  1.00 24.81  ? 15  GLN   A CG    1 
ATOM   109   C  CD    . GLN   A 1  15  ? 20.773  83.147  47.802  1.00 36.99  ? 15  GLN   A CD    1 
ATOM   110   O  OE1   . GLN   A 1  15  ? 20.329  82.195  48.451  1.00 27.76  ? 15  GLN   A OE1   1 
ATOM   111   N  NE2   . GLN   A 1  15  ? 20.582  83.272  46.486  1.00 33.63  ? 15  GLN   A NE2   1 
ATOM   112   N  N     . ILE   A 1  16  ? 22.913  85.013  52.891  1.00 34.57  ? 16  ILE   A N     1 
ATOM   113   C  CA    . ILE   A 1  16  ? 22.759  85.540  54.242  1.00 34.45  ? 16  ILE   A CA    1 
ATOM   114   C  C     . ILE   A 1  16  ? 23.596  86.807  54.415  1.00 42.05  ? 16  ILE   A C     1 
ATOM   115   O  O     . ILE   A 1  16  ? 23.074  87.875  54.777  1.00 36.20  ? 16  ILE   A O     1 
ATOM   116   C  CB    . ILE   A 1  16  ? 23.105  84.461  55.277  1.00 30.02  ? 16  ILE   A CB    1 
ATOM   117   C  CG1   . ILE   A 1  16  ? 21.928  83.511  55.389  1.00 26.72  ? 16  ILE   A CG1   1 
ATOM   118   C  CG2   . ILE   A 1  16  ? 23.390  85.067  56.641  1.00 28.97  ? 16  ILE   A CG2   1 
ATOM   119   C  CD1   . ILE   A 1  16  ? 22.294  82.211  56.051  1.00 27.82  ? 16  ILE   A CD1   1 
ATOM   120   N  N     . GLY   A 1  17  ? 24.893  86.719  54.116  1.00 41.66  ? 17  GLY   A N     1 
ATOM   121   C  CA    . GLY   A 1  17  ? 25.723  87.907  53.975  1.00 42.56  ? 17  GLY   A CA    1 
ATOM   122   C  C     . GLY   A 1  17  ? 25.048  89.099  53.310  1.00 42.32  ? 17  GLY   A C     1 
ATOM   123   O  O     . GLY   A 1  17  ? 25.092  90.216  53.838  1.00 50.77  ? 17  GLY   A O     1 
ATOM   124   N  N     . ASN   A 1  18  ? 24.414  88.889  52.157  1.00 35.13  ? 18  ASN   A N     1 
ATOM   125   C  CA    . ASN   A 1  18  ? 23.785  90.006  51.465  1.00 30.81  ? 18  ASN   A CA    1 
ATOM   126   C  C     . ASN   A 1  18  ? 22.727  90.651  52.332  1.00 41.50  ? 18  ASN   A C     1 
ATOM   127   O  O     . ASN   A 1  18  ? 22.615  91.880  52.389  1.00 47.43  ? 18  ASN   A O     1 
ATOM   128   C  CB    . ASN   A 1  18  ? 23.168  89.541  50.155  1.00 38.52  ? 18  ASN   A CB    1 
ATOM   129   C  CG    . ASN   A 1  18  ? 23.917  90.063  48.967  1.00 56.53  ? 18  ASN   A CG    1 
ATOM   130   O  OD1   . ASN   A 1  18  ? 25.049  89.648  48.724  1.00 59.28  ? 18  ASN   A OD1   1 
ATOM   131   N  ND2   . ASN   A 1  18  ? 23.307  91.002  48.220  1.00 51.34  ? 18  ASN   A ND2   1 
ATOM   132   N  N     . ALA   A 1  19  ? 21.933  89.836  53.009  1.00 42.70  ? 19  ALA   A N     1 
ATOM   133   C  CA    . ALA   A 1  19  ? 20.876  90.380  53.836  1.00 33.76  ? 19  ALA   A CA    1 
ATOM   134   C  C     . ALA   A 1  19  ? 21.456  91.105  55.049  1.00 46.52  ? 19  ALA   A C     1 
ATOM   135   O  O     . ALA   A 1  19  ? 20.948  92.158  55.455  1.00 38.88  ? 19  ALA   A O     1 
ATOM   136   C  CB    . ALA   A 1  19  ? 19.939  89.253  54.251  1.00 30.31  ? 19  ALA   A CB    1 
ATOM   137   N  N     . CYS   A 1  20  ? 22.513  90.553  55.653  1.00 33.02  ? 20  CYS   A N     1 
ATOM   138   C  CA    . CYS   A 1  20  ? 23.158  91.245  56.761  1.00 32.67  ? 20  CYS   A CA    1 
ATOM   139   C  C     . CYS   A 1  20  ? 23.679  92.613  56.326  1.00 46.24  ? 20  CYS   A C     1 
ATOM   140   O  O     . CYS   A 1  20  ? 23.453  93.627  57.006  1.00 40.18  ? 20  CYS   A O     1 
ATOM   141   C  CB    . CYS   A 1  20  ? 24.289  90.395  57.320  1.00 28.28  ? 20  CYS   A CB    1 
ATOM   142   S  SG    . CYS   A 1  20  ? 23.681  89.033  58.248  1.00 43.85  ? 20  CYS   A SG    1 
ATOM   143   N  N     . TRP   A 1  21  ? 24.386  92.661  55.190  1.00 37.72  ? 21  TRP   A N     1 
ATOM   144   C  CA    . TRP   A 1  21  ? 24.963  93.928  54.763  1.00 33.86  ? 21  TRP   A CA    1 
ATOM   145   C  C     . TRP   A 1  21  ? 23.887  94.922  54.382  1.00 36.75  ? 21  TRP   A C     1 
ATOM   146   O  O     . TRP   A 1  21  ? 24.096  96.126  54.504  1.00 45.41  ? 21  TRP   A O     1 
ATOM   147   C  CB    . TRP   A 1  21  ? 25.951  93.693  53.625  1.00 38.49  ? 21  TRP   A CB    1 
ATOM   148   C  CG    . TRP   A 1  21  ? 27.172  93.059  54.172  1.00 45.80  ? 21  TRP   A CG    1 
ATOM   149   C  CD1   . TRP   A 1  21  ? 27.529  91.748  54.089  1.00 36.04  ? 21  TRP   A CD1   1 
ATOM   150   C  CD2   . TRP   A 1  21  ? 28.173  93.702  54.975  1.00 39.88  ? 21  TRP   A CD2   1 
ATOM   151   N  NE1   . TRP   A 1  21  ? 28.708  91.537  54.769  1.00 36.17  ? 21  TRP   A NE1   1 
ATOM   152   C  CE2   . TRP   A 1  21  ? 29.122  92.719  55.324  1.00 38.56  ? 21  TRP   A CE2   1 
ATOM   153   C  CE3   . TRP   A 1  21  ? 28.359  95.012  55.425  1.00 33.20  ? 21  TRP   A CE3   1 
ATOM   154   C  CZ2   . TRP   A 1  21  ? 30.250  93.009  56.092  1.00 38.30  ? 21  TRP   A CZ2   1 
ATOM   155   C  CZ3   . TRP   A 1  21  ? 29.472  95.296  56.196  1.00 38.16  ? 21  TRP   A CZ3   1 
ATOM   156   C  CH2   . TRP   A 1  21  ? 30.407  94.298  56.516  1.00 33.57  ? 21  TRP   A CH2   1 
ATOM   157   N  N     . GLU   A 1  22  ? 22.720  94.449  53.957  1.00 37.87  ? 22  GLU   A N     1 
ATOM   158   C  CA    . GLU   A 1  22  ? 21.624  95.377  53.741  1.00 40.37  ? 22  GLU   A CA    1 
ATOM   159   C  C     . GLU   A 1  22  ? 21.075  95.885  55.063  1.00 43.15  ? 22  GLU   A C     1 
ATOM   160   O  O     . GLU   A 1  22  ? 20.808  97.081  55.206  1.00 51.90  ? 22  GLU   A O     1 
ATOM   161   C  CB    . GLU   A 1  22  ? 20.508  94.725  52.939  1.00 47.19  ? 22  GLU   A CB    1 
ATOM   162   C  CG    . GLU   A 1  22  ? 19.260  95.564  52.995  1.00 47.23  ? 22  GLU   A CG    1 
ATOM   163   C  CD    . GLU   A 1  22  ? 18.140  95.023  52.159  1.00 53.14  ? 22  GLU   A CD    1 
ATOM   164   O  OE1   . GLU   A 1  22  ? 17.922  93.790  52.179  1.00 48.61  ? 22  GLU   A OE1   1 
ATOM   165   O  OE2   . GLU   A 1  22  ? 17.475  95.847  51.488  1.00 58.96  ? 22  GLU   A OE2   1 
ATOM   166   N  N     . LEU   A 1  23  ? 20.883  94.993  56.036  1.00 35.76  ? 23  LEU   A N     1 
ATOM   167   C  CA    . LEU   A 1  23  ? 20.447  95.433  57.355  1.00 41.14  ? 23  LEU   A CA    1 
ATOM   168   C  C     . LEU   A 1  23  ? 21.469  96.383  57.978  1.00 42.85  ? 23  LEU   A C     1 
ATOM   169   O  O     . LEU   A 1  23  ? 21.121  97.494  58.399  1.00 38.78  ? 23  LEU   A O     1 
ATOM   170   C  CB    . LEU   A 1  23  ? 20.190  94.225  58.255  1.00 35.99  ? 23  LEU   A CB    1 
ATOM   171   C  CG    . LEU   A 1  23  ? 19.573  94.553  59.610  1.00 40.89  ? 23  LEU   A CG    1 
ATOM   172   C  CD1   . LEU   A 1  23  ? 18.200  95.196  59.437  1.00 41.68  ? 23  LEU   A CD1   1 
ATOM   173   C  CD2   . LEU   A 1  23  ? 19.506  93.316  60.507  1.00 42.87  ? 23  LEU   A CD2   1 
ATOM   174   N  N     . TYR   A 1  24  ? 22.742  95.972  58.021  1.00 37.42  ? 24  TYR   A N     1 
ATOM   175   C  CA    . TYR   A 1  24  ? 23.825  96.863  58.452  1.00 43.00  ? 24  TYR   A CA    1 
ATOM   176   C  C     . TYR   A 1  24  ? 23.740  98.273  57.851  1.00 51.63  ? 24  TYR   A C     1 
ATOM   177   O  O     . TYR   A 1  24  ? 23.882  99.276  58.565  1.00 45.46  ? 24  TYR   A O     1 
ATOM   178   C  CB    . TYR   A 1  24  ? 25.181  96.264  58.079  1.00 40.27  ? 24  TYR   A CB    1 
ATOM   179   C  CG    . TYR   A 1  24  ? 25.566  95.014  58.805  1.00 40.26  ? 24  TYR   A CG    1 
ATOM   180   C  CD1   . TYR   A 1  24  ? 24.848  94.564  59.897  1.00 40.51  ? 24  TYR   A CD1   1 
ATOM   181   C  CD2   . TYR   A 1  24  ? 26.671  94.283  58.399  1.00 38.96  ? 24  TYR   A CD2   1 
ATOM   182   C  CE1   . TYR   A 1  24  ? 25.221  93.408  60.562  1.00 37.86  ? 24  TYR   A CE1   1 
ATOM   183   C  CE2   . TYR   A 1  24  ? 27.045  93.140  59.054  1.00 42.51  ? 24  TYR   A CE2   1 
ATOM   184   C  CZ    . TYR   A 1  24  ? 26.324  92.708  60.133  1.00 34.03  ? 24  TYR   A CZ    1 
ATOM   185   O  OH    . TYR   A 1  24  ? 26.722  91.567  60.783  1.00 44.50  ? 24  TYR   A OH    1 
ATOM   186   N  N     . CYS   A 1  25  ? 23.563  98.371  56.525  1.00 46.64  ? 25  CYS   A N     1 
ATOM   187   C  CA    . CYS   A 1  25  ? 23.575  99.683  55.881  1.00 42.99  ? 25  CYS   A CA    1 
ATOM   188   C  C     . CYS   A 1  25  ? 22.426  100.541 56.389  1.00 51.76  ? 25  CYS   A C     1 
ATOM   189   O  O     . CYS   A 1  25  ? 22.624  101.695 56.789  1.00 55.36  ? 25  CYS   A O     1 
ATOM   190   C  CB    . CYS   A 1  25  ? 23.519  99.541  54.357  1.00 36.75  ? 25  CYS   A CB    1 
ATOM   191   S  SG    . CYS   A 1  25  ? 25.095  99.067  53.587  1.00 47.68  ? 25  CYS   A SG    1 
ATOM   192   N  N     . LEU   A 1  26  ? 21.212  99.990  56.385  1.00 47.41  ? 26  LEU   A N     1 
ATOM   193   C  CA    . LEU   A 1  26  ? 20.082  100.684 56.984  1.00 43.98  ? 26  LEU   A CA    1 
ATOM   194   C  C     . LEU   A 1  26  ? 20.432  101.230 58.366  1.00 52.49  ? 26  LEU   A C     1 
ATOM   195   O  O     . LEU   A 1  26  ? 20.086  102.367 58.701  1.00 45.09  ? 26  LEU   A O     1 
ATOM   196   C  CB    . LEU   A 1  26  ? 18.893  99.736  57.074  1.00 34.85  ? 26  LEU   A CB    1 
ATOM   197   C  CG    . LEU   A 1  26  ? 17.913  99.818  55.922  1.00 40.03  ? 26  LEU   A CG    1 
ATOM   198   C  CD1   . LEU   A 1  26  ? 18.491  100.657 54.823  1.00 29.11  ? 26  LEU   A CD1   1 
ATOM   199   C  CD2   . LEU   A 1  26  ? 17.579  98.413  55.424  1.00 50.03  ? 26  LEU   A CD2   1 
ATOM   200   N  N     . GLU   A 1  27  ? 21.149  100.437 59.167  1.00 51.18  ? 27  GLU   A N     1 
ATOM   201   C  CA    . GLU   A 1  27  ? 21.340  100.762 60.576  1.00 50.99  ? 27  GLU   A CA    1 
ATOM   202   C  C     . GLU   A 1  27  ? 22.287  101.944 60.770  1.00 44.34  ? 27  GLU   A C     1 
ATOM   203   O  O     . GLU   A 1  27  ? 22.052  102.791 61.639  1.00 46.21  ? 27  GLU   A O     1 
ATOM   204   C  CB    . GLU   A 1  27  ? 21.839  99.519  61.321  1.00 45.98  ? 27  GLU   A CB    1 
ATOM   205   C  CG    . GLU   A 1  27  ? 20.723  98.512  61.597  1.00 45.44  ? 27  GLU   A CG    1 
ATOM   206   C  CD    . GLU   A 1  27  ? 21.202  97.215  62.257  1.00 47.39  ? 27  GLU   A CD    1 
ATOM   207   O  OE1   . GLU   A 1  27  ? 22.416  97.095  62.562  1.00 42.65  ? 27  GLU   A OE1   1 
ATOM   208   O  OE2   . GLU   A 1  27  ? 20.351  96.315  62.464  1.00 42.38  ? 27  GLU   A OE2   1 
ATOM   209   N  N     . HIS   A 1  28  ? 23.370  102.004 59.998  1.00 42.28  ? 28  HIS   A N     1 
ATOM   210   C  CA    . HIS   A 1  28  ? 24.336  103.092 60.082  1.00 45.34  ? 28  HIS   A CA    1 
ATOM   211   C  C     . HIS   A 1  28  ? 24.061  104.210 59.081  1.00 49.70  ? 28  HIS   A C     1 
ATOM   212   O  O     . HIS   A 1  28  ? 24.936  105.053 58.857  1.00 48.87  ? 28  HIS   A O     1 
ATOM   213   C  CB    . HIS   A 1  28  ? 25.763  102.593 59.843  1.00 36.99  ? 28  HIS   A CB    1 
ATOM   214   C  CG    . HIS   A 1  28  ? 26.181  101.447 60.706  1.00 41.97  ? 28  HIS   A CG    1 
ATOM   215   N  ND1   . HIS   A 1  28  ? 26.694  101.618 61.969  1.00 38.08  ? 28  HIS   A ND1   1 
ATOM   216   C  CD2   . HIS   A 1  28  ? 26.225  100.116 60.461  1.00 48.33  ? 28  HIS   A CD2   1 
ATOM   217   C  CE1   . HIS   A 1  28  ? 27.007  100.442 62.481  1.00 36.48  ? 28  HIS   A CE1   1 
ATOM   218   N  NE2   . HIS   A 1  28  ? 26.733  99.514  61.586  1.00 42.85  ? 28  HIS   A NE2   1 
ATOM   219   N  N     . GLY   A 1  29  ? 22.891  104.226 58.454  1.00 48.92  ? 29  GLY   A N     1 
ATOM   220   C  CA    . GLY   A 1  29  ? 22.614  105.232 57.451  1.00 46.01  ? 29  GLY   A CA    1 
ATOM   221   C  C     . GLY   A 1  29  ? 23.666  105.310 56.361  1.00 58.46  ? 29  GLY   A C     1 
ATOM   222   O  O     . GLY   A 1  29  ? 24.232  106.383 56.114  1.00 59.03  ? 29  GLY   A O     1 
ATOM   223   N  N     . ILE   A 1  30  ? 23.948  104.177 55.716  1.00 50.30  ? 30  ILE   A N     1 
ATOM   224   C  CA    . ILE   A 1  30  ? 24.814  104.115 54.545  1.00 51.55  ? 30  ILE   A CA    1 
ATOM   225   C  C     . ILE   A 1  30  ? 23.946  103.781 53.339  1.00 55.73  ? 30  ILE   A C     1 
ATOM   226   O  O     . ILE   A 1  30  ? 23.179  102.815 53.375  1.00 60.23  ? 30  ILE   A O     1 
ATOM   227   C  CB    . ILE   A 1  30  ? 25.935  103.081 54.725  1.00 49.39  ? 30  ILE   A CB    1 
ATOM   228   C  CG1   . ILE   A 1  30  ? 26.698  103.355 56.015  1.00 51.27  ? 30  ILE   A CG1   1 
ATOM   229   C  CG2   . ILE   A 1  30  ? 26.892  103.108 53.535  1.00 58.09  ? 30  ILE   A CG2   1 
ATOM   230   C  CD1   . ILE   A 1  30  ? 27.917  102.475 56.200  1.00 47.11  ? 30  ILE   A CD1   1 
ATOM   231   N  N     . GLN   A 1  31  ? 24.063  104.571 52.275  1.00 65.14  ? 31  GLN   A N     1 
ATOM   232   C  CA    . GLN   A 1  31  ? 23.215  104.392 51.100  1.00 75.12  ? 31  GLN   A CA    1 
ATOM   233   C  C     . GLN   A 1  31  ? 23.752  103.282 50.200  1.00 74.56  ? 31  GLN   A C     1 
ATOM   234   O  O     . GLN   A 1  31  ? 24.889  102.821 50.358  1.00 69.53  ? 31  GLN   A O     1 
ATOM   235   C  CB    . GLN   A 1  31  ? 23.102  105.705 50.329  1.00 75.07  ? 31  GLN   A CB    1 
ATOM   236   C  CG    . GLN   A 1  31  ? 22.214  106.759 50.987  1.00 83.44  ? 31  GLN   A CG    1 
ATOM   237   C  CD    . GLN   A 1  31  ? 22.930  108.101 51.172  1.00 91.17  ? 31  GLN   A CD    1 
ATOM   238   O  OE1   . GLN   A 1  31  ? 23.974  108.356 50.556  1.00 76.40  ? 31  GLN   A OE1   1 
ATOM   239   N  NE2   . GLN   A 1  31  ? 22.375  108.959 52.034  1.00 85.65  ? 31  GLN   A NE2   1 
ATOM   240   N  N     . PRO   A 1  32  ? 22.933  102.834 49.219  1.00 73.70  ? 32  PRO   A N     1 
ATOM   241   C  CA    . PRO   A 1  32  ? 23.358  101.753 48.309  1.00 74.28  ? 32  PRO   A CA    1 
ATOM   242   C  C     . PRO   A 1  32  ? 24.644  102.019 47.535  1.00 73.09  ? 32  PRO   A C     1 
ATOM   243   O  O     . PRO   A 1  32  ? 25.065  101.175 46.735  1.00 66.44  ? 32  PRO   A O     1 
ATOM   244   C  CB    . PRO   A 1  32  ? 22.166  101.626 47.351  1.00 56.04  ? 32  PRO   A CB    1 
ATOM   245   C  CG    . PRO   A 1  32  ? 20.997  102.078 48.159  1.00 53.20  ? 32  PRO   A CG    1 
ATOM   246   C  CD    . PRO   A 1  32  ? 21.511  103.182 49.041  1.00 62.90  ? 32  PRO   A CD    1 
ATOM   247   N  N     . ASP   A 1  33  ? 25.281  103.172 47.743  1.00 67.67  ? 33  ASP   A N     1 
ATOM   248   C  CA    . ASP   A 1  33  ? 26.521  103.496 47.048  1.00 61.97  ? 33  ASP   A CA    1 
ATOM   249   C  C     . ASP   A 1  33  ? 27.648  103.838 48.006  1.00 70.12  ? 33  ASP   A C     1 
ATOM   250   O  O     . ASP   A 1  33  ? 28.573  104.555 47.618  1.00 67.95  ? 33  ASP   A O     1 
ATOM   251   C  CB    . ASP   A 1  33  ? 26.312  104.650 46.068  1.00 64.20  ? 33  ASP   A CB    1 
ATOM   252   C  CG    . ASP   A 1  33  ? 25.814  105.899 46.746  1.00 64.05  ? 33  ASP   A CG    1 
ATOM   253   O  OD1   . ASP   A 1  33  ? 25.030  105.748 47.700  1.00 80.23  ? 33  ASP   A OD1   1 
ATOM   254   O  OD2   . ASP   A 1  33  ? 26.198  107.019 46.343  1.00 48.99  ? 33  ASP   A OD2   1 
ATOM   255   N  N     . GLY   A 1  34  ? 27.587  103.350 49.250  1.00 66.82  ? 34  GLY   A N     1 
ATOM   256   C  CA    . GLY   A 1  34  ? 28.648  103.554 50.217  1.00 68.10  ? 34  GLY   A CA    1 
ATOM   257   C  C     . GLY   A 1  34  ? 28.700  104.929 50.850  1.00 67.61  ? 34  GLY   A C     1 
ATOM   258   O  O     . GLY   A 1  34  ? 29.491  105.134 51.788  1.00 55.69  ? 34  GLY   A O     1 
ATOM   259   N  N     . GLN   A 1  35  ? 27.893  105.875 50.365  1.00 68.87  ? 35  GLN   A N     1 
ATOM   260   C  CA    . GLN   A 1  35  ? 27.830  107.217 50.927  1.00 77.05  ? 35  GLN   A CA    1 
ATOM   261   C  C     . GLN   A 1  35  ? 27.033  107.214 52.228  1.00 78.14  ? 35  GLN   A C     1 
ATOM   262   O  O     . GLN   A 1  35  ? 26.002  106.540 52.341  1.00 70.70  ? 35  GLN   A O     1 
ATOM   263   C  CB    . GLN   A 1  35  ? 27.198  108.188 49.924  1.00 59.19  ? 35  GLN   A CB    1 
ATOM   264   C  CG    . GLN   A 1  35  ? 28.106  108.580 48.788  1.00 59.64  ? 35  GLN   A CG    1 
ATOM   265   C  CD    . GLN   A 1  35  ? 29.395  109.236 49.266  1.00 68.01  ? 35  GLN   A CD    1 
ATOM   266   O  OE1   . GLN   A 1  35  ? 30.471  108.963 48.738  1.00 67.68  ? 35  GLN   A OE1   1 
ATOM   267   N  NE2   . GLN   A 1  35  ? 29.289  110.107 50.265  1.00 71.87  ? 35  GLN   A NE2   1 
ATOM   268   N  N     . MET   A 1  36  ? 27.515  107.985 53.206  1.00 67.12  ? 36  MET   A N     1 
ATOM   269   C  CA    . MET   A 1  36  ? 26.976  107.980 54.568  1.00 64.04  ? 36  MET   A CA    1 
ATOM   270   C  C     . MET   A 1  36  ? 26.968  109.411 55.083  1.00 63.28  ? 36  MET   A C     1 
ATOM   271   O  O     . MET   A 1  36  ? 27.891  109.842 55.783  1.00 57.55  ? 36  MET   A O     1 
ATOM   272   C  CB    . MET   A 1  36  ? 27.810  107.066 55.472  1.00 63.25  ? 36  MET   A CB    1 
ATOM   273   C  CG    . MET   A 1  36  ? 27.378  106.940 56.934  1.00 58.48  ? 36  MET   A CG    1 
ATOM   274   S  SD    . MET   A 1  36  ? 28.674  106.093 57.899  1.00 62.75  ? 36  MET   A SD    1 
ATOM   275   C  CE    . MET   A 1  36  ? 27.848  105.923 59.479  1.00 60.62  ? 36  MET   A CE    1 
ATOM   276   N  N     . PRO   A 1  37  ? 25.934  110.187 54.747  1.00 58.91  ? 37  PRO   A N     1 
ATOM   277   C  CA    . PRO   A 1  37  ? 25.901  111.596 55.167  1.00 65.76  ? 37  PRO   A CA    1 
ATOM   278   C  C     . PRO   A 1  37  ? 26.339  111.807 56.609  1.00 66.31  ? 37  PRO   A C     1 
ATOM   279   O  O     . PRO   A 1  37  ? 27.099  112.736 56.900  1.00 69.59  ? 37  PRO   A O     1 
ATOM   280   C  CB    . PRO   A 1  37  ? 24.431  111.987 54.967  1.00 64.65  ? 37  PRO   A CB    1 
ATOM   281   C  CG    . PRO   A 1  37  ? 23.966  111.103 53.863  1.00 70.07  ? 37  PRO   A CG    1 
ATOM   282   C  CD    . PRO   A 1  37  ? 24.730  109.801 53.992  1.00 65.53  ? 37  PRO   A CD    1 
ATOM   283   N  N     . SER   A 1  38  ? 25.899  110.922 57.510  1.00 65.86  ? 38  SER   A N     1 
ATOM   284   C  CA    . SER   A 1  38  ? 26.107  111.129 58.939  1.00 64.02  ? 38  SER   A CA    1 
ATOM   285   C  C     . SER   A 1  38  ? 27.566  110.992 59.377  1.00 57.35  ? 38  SER   A C     1 
ATOM   286   O  O     . SER   A 1  38  ? 27.906  111.493 60.455  1.00 60.20  ? 38  SER   A O     1 
ATOM   287   C  CB    . SER   A 1  38  ? 25.219  110.177 59.745  1.00 56.27  ? 38  SER   A CB    1 
ATOM   288   O  OG    . SER   A 1  38  ? 25.334  108.842 59.297  1.00 67.77  ? 38  SER   A OG    1 
ATOM   289   N  N     . ASP   A 1  39  ? 28.441  110.351 58.591  1.00 55.75  ? 39  ASP   A N     1 
ATOM   290   C  CA    . ASP   A 1  39  ? 29.872  110.401 58.899  1.00 60.18  ? 39  ASP   A CA    1 
ATOM   291   C  C     . ASP   A 1  39  ? 30.401  111.763 58.483  1.00 69.88  ? 39  ASP   A C     1 
ATOM   292   O  O     . ASP   A 1  39  ? 30.240  112.172 57.328  1.00 73.83  ? 39  ASP   A O     1 
ATOM   293   C  CB    . ASP   A 1  39  ? 30.695  109.305 58.213  1.00 57.11  ? 39  ASP   A CB    1 
ATOM   294   C  CG    . ASP   A 1  39  ? 32.180  109.321 58.672  1.00 65.43  ? 39  ASP   A CG    1 
ATOM   295   O  OD1   . ASP   A 1  39  ? 32.535  110.230 59.442  1.00 70.11  ? 39  ASP   A OD1   1 
ATOM   296   O  OD2   . ASP   A 1  39  ? 33.000  108.449 58.301  1.00 52.36  ? 39  ASP   A OD2   1 
ATOM   297   N  N     . LYS   A 1  40  ? 31.022  112.469 59.424  1.00 72.85  ? 40  LYS   A N     1 
ATOM   298   C  CA    . LYS   A 1  40  ? 31.639  113.752 59.134  1.00 66.30  ? 40  LYS   A CA    1 
ATOM   299   C  C     . LYS   A 1  40  ? 33.148  113.648 58.957  1.00 68.28  ? 40  LYS   A C     1 
ATOM   300   O  O     . LYS   A 1  40  ? 33.777  114.637 58.566  1.00 81.65  ? 40  LYS   A O     1 
ATOM   301   C  CB    . LYS   A 1  40  ? 31.302  114.766 60.236  1.00 62.74  ? 40  LYS   A CB    1 
ATOM   302   C  CG    . LYS   A 1  40  ? 29.809  114.977 60.449  1.00 62.04  ? 40  LYS   A CG    1 
ATOM   303   C  CD    . LYS   A 1  40  ? 29.120  115.429 59.170  1.00 61.76  ? 40  LYS   A CD    1 
ATOM   304   C  CE    . LYS   A 1  40  ? 27.598  115.529 59.346  1.00 67.56  ? 40  LYS   A CE    1 
ATOM   305   N  NZ    . LYS   A 1  40  ? 26.894  115.882 58.063  1.00 55.69  ? 40  LYS   A NZ    1 
ATOM   306   N  N     . THR   A 1  41  ? 33.736  112.481 59.224  1.00 59.32  ? 41  THR   A N     1 
ATOM   307   C  CA    . THR   A 1  41  ? 35.128  112.179 58.878  1.00 61.44  ? 41  THR   A CA    1 
ATOM   308   C  C     . THR   A 1  41  ? 35.155  111.676 57.435  1.00 68.72  ? 41  THR   A C     1 
ATOM   309   O  O     . THR   A 1  41  ? 35.069  110.473 57.177  1.00 74.04  ? 41  THR   A O     1 
ATOM   310   C  CB    . THR   A 1  41  ? 35.694  111.130 59.827  1.00 72.54  ? 41  THR   A CB    1 
ATOM   311   O  OG1   . THR   A 1  41  ? 35.114  109.844 59.524  1.00 77.53  ? 41  THR   A OG1   1 
ATOM   312   C  CG2   . THR   A 1  41  ? 35.362  111.489 61.256  1.00 61.72  ? 41  THR   A CG2   1 
ATOM   313   N  N     . ILE   A 1  42  ? 35.263  112.599 56.479  1.00 62.96  ? 42  ILE   A N     1 
ATOM   314   C  CA    . ILE   A 1  42  ? 35.222  112.240 55.063  1.00 54.57  ? 42  ILE   A CA    1 
ATOM   315   C  C     . ILE   A 1  42  ? 36.588  111.697 54.663  1.00 51.22  ? 42  ILE   A C     1 
ATOM   316   O  O     . ILE   A 1  42  ? 37.601  112.393 54.775  1.00 60.85  ? 42  ILE   A O     1 
ATOM   317   C  CB    . ILE   A 1  42  ? 34.817  113.439 54.191  1.00 57.02  ? 42  ILE   A CB    1 
ATOM   318   C  CG1   . ILE   A 1  42  ? 33.586  114.158 54.773  1.00 64.46  ? 42  ILE   A CG1   1 
ATOM   319   C  CG2   . ILE   A 1  42  ? 34.542  112.995 52.756  1.00 46.52  ? 42  ILE   A CG2   1 
ATOM   320   C  CD1   . ILE   A 1  42  ? 32.234  113.504 54.479  1.00 47.78  ? 42  ILE   A CD1   1 
ATOM   321   N  N     . GLY   A 1  43  ? 36.623  110.446 54.215  1.00 47.27  ? 43  GLY   A N     1 
ATOM   322   C  CA    . GLY   A 1  43  ? 37.867  109.769 53.923  1.00 59.19  ? 43  GLY   A CA    1 
ATOM   323   C  C     . GLY   A 1  43  ? 38.296  108.733 54.946  1.00 67.50  ? 43  GLY   A C     1 
ATOM   324   O  O     . GLY   A 1  43  ? 39.222  107.956 54.662  1.00 62.82  ? 43  GLY   A O     1 
ATOM   325   N  N     . GLY   A 1  44  ? 37.655  108.692 56.119  1.00 73.64  ? 44  GLY   A N     1 
ATOM   326   C  CA    . GLY   A 1  44  ? 37.983  107.694 57.126  1.00 76.54  ? 44  GLY   A CA    1 
ATOM   327   C  C     . GLY   A 1  44  ? 37.397  107.894 58.514  1.00 66.14  ? 44  GLY   A C     1 
ATOM   328   O  O     . GLY   A 1  44  ? 36.213  108.221 58.676  1.00 59.48  ? 44  GLY   A O     1 
ATOM   329   N  N     . GLY   A 1  45  ? 38.229  107.679 59.524  1.00 58.26  ? 45  GLY   A N     1 
ATOM   330   C  CA    . GLY   A 1  45  ? 37.821  107.750 60.912  1.00 73.91  ? 45  GLY   A CA    1 
ATOM   331   C  C     . GLY   A 1  45  ? 38.092  106.453 61.654  1.00 71.58  ? 45  GLY   A C     1 
ATOM   332   O  O     . GLY   A 1  45  ? 38.570  105.466 61.096  1.00 71.78  ? 45  GLY   A O     1 
ATOM   333   N  N     . ASP   A 1  46  ? 37.790  106.479 62.951  1.00 71.97  ? 46  ASP   A N     1 
ATOM   334   C  CA    . ASP   A 1  46  ? 37.870  105.270 63.763  1.00 65.98  ? 46  ASP   A CA    1 
ATOM   335   C  C     . ASP   A 1  46  ? 36.639  105.137 64.650  1.00 64.56  ? 46  ASP   A C     1 
ATOM   336   O  O     . ASP   A 1  46  ? 36.723  104.617 65.767  1.00 74.41  ? 46  ASP   A O     1 
ATOM   337   C  CB    . ASP   A 1  46  ? 39.154  105.230 64.599  1.00 60.11  ? 46  ASP   A CB    1 
ATOM   338   C  CG    . ASP   A 1  46  ? 39.294  106.425 65.529  1.00 79.08  ? 46  ASP   A CG    1 
ATOM   339   O  OD1   . ASP   A 1  46  ? 38.536  107.410 65.360  1.00 79.85  ? 46  ASP   A OD1   1 
ATOM   340   O  OD2   . ASP   A 1  46  ? 40.164  106.374 66.433  1.00 77.06  ? 46  ASP   A OD2   1 
ATOM   341   N  N     . ASP   A 1  47  ? 35.490  105.593 64.159  1.00 53.27  ? 47  ASP   A N     1 
ATOM   342   C  CA    . ASP   A 1  47  ? 34.237  105.413 64.871  1.00 62.88  ? 47  ASP   A CA    1 
ATOM   343   C  C     . ASP   A 1  47  ? 33.963  103.917 65.076  1.00 66.34  ? 47  ASP   A C     1 
ATOM   344   O  O     . ASP   A 1  47  ? 34.650  103.051 64.530  1.00 59.91  ? 47  ASP   A O     1 
ATOM   345   C  CB    . ASP   A 1  47  ? 33.108  106.091 64.101  1.00 54.27  ? 47  ASP   A CB    1 
ATOM   346   C  CG    . ASP   A 1  47  ? 33.575  107.356 63.401  1.00 74.56  ? 47  ASP   A CG    1 
ATOM   347   O  OD1   . ASP   A 1  47  ? 34.337  108.128 64.018  1.00 81.58  ? 47  ASP   A OD1   1 
ATOM   348   O  OD2   . ASP   A 1  47  ? 33.211  107.572 62.224  1.00 70.91  ? 47  ASP   A OD2   1 
ATOM   349   N  N     . SER   A 1  48  ? 32.943  103.611 65.888  1.00 64.58  ? 48  SER   A N     1 
ATOM   350   C  CA    . SER   A 1  48  ? 32.651  102.209 66.187  1.00 60.68  ? 48  SER   A CA    1 
ATOM   351   C  C     . SER   A 1  48  ? 32.196  101.438 64.945  1.00 62.60  ? 48  SER   A C     1 
ATOM   352   O  O     . SER   A 1  48  ? 32.419  100.223 64.853  1.00 54.28  ? 48  SER   A O     1 
ATOM   353   C  CB    . SER   A 1  48  ? 31.603  102.110 67.300  1.00 51.80  ? 48  SER   A CB    1 
ATOM   354   O  OG    . SER   A 1  48  ? 32.170  102.375 68.586  1.00 65.11  ? 48  SER   A OG    1 
ATOM   355   N  N     . PHE   A 1  49  ? 31.576  102.112 63.979  1.00 54.52  ? 49  PHE   A N     1 
ATOM   356   C  CA    . PHE   A 1  49  ? 31.122  101.402 62.798  1.00 49.37  ? 49  PHE   A CA    1 
ATOM   357   C  C     . PHE   A 1  49  ? 32.230  101.148 61.796  1.00 55.15  ? 49  PHE   A C     1 
ATOM   358   O  O     . PHE   A 1  49  ? 31.970  100.537 60.757  1.00 50.67  ? 49  PHE   A O     1 
ATOM   359   C  CB    . PHE   A 1  49  ? 29.977  102.148 62.116  1.00 55.54  ? 49  PHE   A CB    1 
ATOM   360   C  CG    . PHE   A 1  49  ? 30.345  103.495 61.575  1.00 59.31  ? 49  PHE   A CG    1 
ATOM   361   C  CD1   . PHE   A 1  49  ? 31.104  103.613 60.417  1.00 64.62  ? 49  PHE   A CD1   1 
ATOM   362   C  CD2   . PHE   A 1  49  ? 29.878  104.647 62.189  1.00 56.70  ? 49  PHE   A CD2   1 
ATOM   363   C  CE1   . PHE   A 1  49  ? 31.424  104.859 59.902  1.00 67.18  ? 49  PHE   A CE1   1 
ATOM   364   C  CE2   . PHE   A 1  49  ? 30.190  105.893 61.683  1.00 65.35  ? 49  PHE   A CE2   1 
ATOM   365   C  CZ    . PHE   A 1  49  ? 30.969  106.001 60.535  1.00 70.01  ? 49  PHE   A CZ    1 
ATOM   366   N  N     . ASN   A 1  50  ? 33.449  101.586 62.070  1.00 59.36  ? 50  ASN   A N     1 
ATOM   367   C  CA    . ASN   A 1  50  ? 34.538  101.267 61.160  1.00 54.35  ? 50  ASN   A CA    1 
ATOM   368   C  C     . ASN   A 1  50  ? 35.101  99.878  61.382  1.00 53.68  ? 50  ASN   A C     1 
ATOM   369   O  O     . ASN   A 1  50  ? 36.009  99.480  60.647  1.00 63.15  ? 50  ASN   A O     1 
ATOM   370   C  CB    . ASN   A 1  50  ? 35.652  102.299 61.273  1.00 53.91  ? 50  ASN   A CB    1 
ATOM   371   C  CG    . ASN   A 1  50  ? 35.303  103.573 60.584  1.00 52.48  ? 50  ASN   A CG    1 
ATOM   372   O  OD1   . ASN   A 1  50  ? 35.406  104.655 61.156  1.00 63.05  ? 50  ASN   A OD1   1 
ATOM   373   N  ND2   . ASN   A 1  50  ? 34.856  103.459 59.346  1.00 61.87  ? 50  ASN   A ND2   1 
ATOM   374   N  N     . THR   A 1  51  ? 34.608  99.136  62.377  1.00 48.40  ? 51  THR   A N     1 
ATOM   375   C  CA    A THR   A 1  51  ? 35.014  97.741  62.491  0.61 53.98  ? 51  THR   A CA    1 
ATOM   376   C  CA    B THR   A 1  51  ? 34.997  97.735  62.500  0.39 53.90  ? 51  THR   A CA    1 
ATOM   377   C  C     . THR   A 1  51  ? 34.480  96.918  61.320  1.00 57.16  ? 51  THR   A C     1 
ATOM   378   O  O     . THR   A 1  51  ? 35.110  95.929  60.918  1.00 53.07  ? 51  THR   A O     1 
ATOM   379   C  CB    A THR   A 1  51  ? 34.554  97.155  63.830  0.61 50.55  ? 51  THR   A CB    1 
ATOM   380   C  CB    B THR   A 1  51  ? 34.479  97.162  63.821  0.39 50.54  ? 51  THR   A CB    1 
ATOM   381   O  OG1   A THR   A 1  51  ? 33.152  96.863  63.781  0.61 44.14  ? 51  THR   A OG1   1 
ATOM   382   O  OG1   B THR   A 1  51  ? 34.893  98.006  64.900  0.39 50.60  ? 51  THR   A OG1   1 
ATOM   383   C  CG2   A THR   A 1  51  ? 34.814  98.142  64.949  0.61 50.69  ? 51  THR   A CG2   1 
ATOM   384   C  CG2   B THR   A 1  51  ? 35.024  95.761  64.051  0.39 48.63  ? 51  THR   A CG2   1 
ATOM   385   N  N     . PHE   A 1  52  ? 33.350  97.327  60.740  1.00 50.50  ? 52  PHE   A N     1 
ATOM   386   C  CA    . PHE   A 1  52  ? 32.736  96.620  59.630  1.00 48.11  ? 52  PHE   A CA    1 
ATOM   387   C  C     . PHE   A 1  52  ? 32.813  97.347  58.300  1.00 51.02  ? 52  PHE   A C     1 
ATOM   388   O  O     . PHE   A 1  52  ? 32.520  96.732  57.275  1.00 49.71  ? 52  PHE   A O     1 
ATOM   389   C  CB    . PHE   A 1  52  ? 31.267  96.328  59.950  1.00 34.30  ? 52  PHE   A CB    1 
ATOM   390   C  CG    . PHE   A 1  52  ? 31.088  95.117  60.810  1.00 50.25  ? 52  PHE   A CG    1 
ATOM   391   C  CD1   . PHE   A 1  52  ? 31.870  94.941  61.937  1.00 46.24  ? 52  PHE   A CD1   1 
ATOM   392   C  CD2   . PHE   A 1  52  ? 30.157  94.144  60.484  1.00 46.34  ? 52  PHE   A CD2   1 
ATOM   393   C  CE1   . PHE   A 1  52  ? 31.719  93.836  62.723  1.00 45.45  ? 52  PHE   A CE1   1 
ATOM   394   C  CE2   . PHE   A 1  52  ? 30.001  93.040  61.264  1.00 39.39  ? 52  PHE   A CE2   1 
ATOM   395   C  CZ    . PHE   A 1  52  ? 30.789  92.877  62.386  1.00 43.00  ? 52  PHE   A CZ    1 
ATOM   396   N  N     . PHE   A 1  53  ? 33.170  98.630  58.282  1.00 51.39  ? 53  PHE   A N     1 
ATOM   397   C  CA    . PHE   A 1  53  ? 33.331  99.375  57.044  1.00 45.52  ? 53  PHE   A CA    1 
ATOM   398   C  C     . PHE   A 1  53  ? 34.666  100.105 57.060  1.00 59.35  ? 53  PHE   A C     1 
ATOM   399   O  O     . PHE   A 1  53  ? 35.119  100.566 58.113  1.00 54.14  ? 53  PHE   A O     1 
ATOM   400   C  CB    . PHE   A 1  53  ? 32.234  100.402 56.829  1.00 39.94  ? 53  PHE   A CB    1 
ATOM   401   C  CG    . PHE   A 1  53  ? 30.857  99.834  56.749  1.00 48.78  ? 53  PHE   A CG    1 
ATOM   402   C  CD1   . PHE   A 1  53  ? 30.268  99.233  57.856  1.00 43.44  ? 53  PHE   A CD1   1 
ATOM   403   C  CD2   . PHE   A 1  53  ? 30.115  99.958  55.578  1.00 47.48  ? 53  PHE   A CD2   1 
ATOM   404   C  CE1   . PHE   A 1  53  ? 28.969  98.734  57.793  1.00 38.52  ? 53  PHE   A CE1   1 
ATOM   405   C  CE2   . PHE   A 1  53  ? 28.815  99.465  55.500  1.00 45.62  ? 53  PHE   A CE2   1 
ATOM   406   C  CZ    . PHE   A 1  53  ? 28.239  98.847  56.614  1.00 48.82  ? 53  PHE   A CZ    1 
ATOM   407   N  N     . SER   A 1  54  ? 35.287  100.195 55.883  1.00 61.71  ? 54  SER   A N     1 
ATOM   408   C  CA    . SER   A 1  54  ? 36.446  101.028 55.598  1.00 49.43  ? 54  SER   A CA    1 
ATOM   409   C  C     . SER   A 1  54  ? 36.009  102.165 54.678  1.00 56.94  ? 54  SER   A C     1 
ATOM   410   O  O     . SER   A 1  54  ? 34.880  102.186 54.181  1.00 51.18  ? 54  SER   A O     1 
ATOM   411   C  CB    . SER   A 1  54  ? 37.567  100.204 54.967  1.00 44.65  ? 54  SER   A CB    1 
ATOM   412   O  OG    . SER   A 1  54  ? 37.243  99.863  53.632  1.00 52.45  ? 54  SER   A OG    1 
ATOM   413   N  N     . GLU   A 1  55  ? 36.896  103.138 54.460  1.00 57.29  ? 55  GLU   A N     1 
ATOM   414   C  CA    . GLU   A 1  55  ? 36.449  104.411 53.907  1.00 64.77  ? 55  GLU   A CA    1 
ATOM   415   C  C     . GLU   A 1  55  ? 37.272  104.851 52.704  1.00 60.76  ? 55  GLU   A C     1 
ATOM   416   O  O     . GLU   A 1  55  ? 38.490  104.653 52.647  1.00 54.27  ? 55  GLU   A O     1 
ATOM   417   C  CB    . GLU   A 1  55  ? 36.461  105.510 54.979  1.00 65.82  ? 55  GLU   A CB    1 
ATOM   418   C  CG    . GLU   A 1  55  ? 35.447  105.264 56.100  1.00 71.96  ? 55  GLU   A CG    1 
ATOM   419   C  CD    . GLU   A 1  55  ? 35.033  106.535 56.800  1.00 72.10  ? 55  GLU   A CD    1 
ATOM   420   O  OE1   . GLU   A 1  55  ? 35.129  107.612 56.168  1.00 67.49  ? 55  GLU   A OE1   1 
ATOM   421   O  OE2   . GLU   A 1  55  ? 34.621  106.458 57.976  1.00 65.60  ? 55  GLU   A OE2   1 
ATOM   422   N  N     . THR   A 1  56  ? 36.582  105.477 51.757  1.00 62.87  ? 56  THR   A N     1 
ATOM   423   C  CA    . THR   A 1  56  ? 37.144  105.886 50.482  1.00 67.18  ? 56  THR   A CA    1 
ATOM   424   C  C     . THR   A 1  56  ? 37.227  107.405 50.402  1.00 70.75  ? 56  THR   A C     1 
ATOM   425   O  O     . THR   A 1  56  ? 36.315  108.112 50.849  1.00 62.72  ? 56  THR   A O     1 
ATOM   426   C  CB    . THR   A 1  56  ? 36.299  105.322 49.339  1.00 53.32  ? 56  THR   A CB    1 
ATOM   427   O  OG1   . THR   A 1  56  ? 36.828  104.046 48.978  1.00 45.87  ? 56  THR   A OG1   1 
ATOM   428   C  CG2   . THR   A 1  56  ? 36.291  106.239 48.126  1.00 62.92  ? 56  THR   A CG2   1 
ATOM   429   N  N     . GLY   A 1  57  ? 38.337  107.896 49.842  1.00 68.19  ? 57  GLY   A N     1 
ATOM   430   C  CA    . GLY   A 1  57  ? 38.504  109.334 49.678  1.00 64.20  ? 57  GLY   A CA    1 
ATOM   431   C  C     . GLY   A 1  57  ? 37.289  110.007 49.070  1.00 65.94  ? 57  GLY   A C     1 
ATOM   432   O  O     . GLY   A 1  57  ? 36.847  111.059 49.534  1.00 72.07  ? 57  GLY   A O     1 
ATOM   433   N  N     . ALA   A 1  58  ? 36.728  109.412 48.017  1.00 71.07  ? 58  ALA   A N     1 
ATOM   434   C  CA    . ALA   A 1  58  ? 35.536  109.994 47.407  1.00 72.59  ? 58  ALA   A CA    1 
ATOM   435   C  C     . ALA   A 1  58  ? 34.305  109.887 48.299  1.00 67.80  ? 58  ALA   A C     1 
ATOM   436   O  O     . ALA   A 1  58  ? 33.237  110.373 47.898  1.00 57.37  ? 58  ALA   A O     1 
ATOM   437   C  CB    . ALA   A 1  58  ? 35.261  109.343 46.045  1.00 66.80  ? 58  ALA   A CB    1 
ATOM   438   N  N     . GLY   A 1  59  ? 34.429  109.270 49.478  1.00 63.44  ? 59  GLY   A N     1 
ATOM   439   C  CA    . GLY   A 1  59  ? 33.357  109.203 50.456  1.00 63.92  ? 59  GLY   A CA    1 
ATOM   440   C  C     . GLY   A 1  59  ? 32.692  107.848 50.634  1.00 69.41  ? 59  GLY   A C     1 
ATOM   441   O  O     . GLY   A 1  59  ? 31.637  107.777 51.276  1.00 65.31  ? 59  GLY   A O     1 
ATOM   442   N  N     . LYS   A 1  60  ? 33.267  106.777 50.102  1.00 73.59  ? 60  LYS   A N     1 
ATOM   443   C  CA    . LYS   A 1  60  ? 32.610  105.477 50.090  1.00 70.24  ? 60  LYS   A CA    1 
ATOM   444   C  C     . LYS   A 1  60  ? 32.921  104.722 51.379  1.00 64.93  ? 60  LYS   A C     1 
ATOM   445   O  O     . LYS   A 1  60  ? 34.080  104.678 51.814  1.00 54.44  ? 60  LYS   A O     1 
ATOM   446   C  CB    . LYS   A 1  60  ? 33.061  104.667 48.867  1.00 69.79  ? 60  LYS   A CB    1 
ATOM   447   C  CG    . LYS   A 1  60  ? 32.322  103.334 48.654  1.00 74.64  ? 60  LYS   A CG    1 
ATOM   448   C  CD    . LYS   A 1  60  ? 31.191  103.454 47.627  1.00 70.23  ? 60  LYS   A CD    1 
ATOM   449   C  CE    . LYS   A 1  60  ? 31.634  103.036 46.225  1.00 66.08  ? 60  LYS   A CE    1 
ATOM   450   N  NZ    . LYS   A 1  60  ? 31.882  101.565 46.121  1.00 67.72  ? 60  LYS   A NZ    1 
ATOM   451   N  N     . HIS   A 1  61  ? 31.876  104.145 51.993  1.00 58.25  ? 61  HIS   A N     1 
ATOM   452   C  CA    . HIS   A 1  61  ? 32.019  103.175 53.079  1.00 62.45  ? 61  HIS   A CA    1 
ATOM   453   C  C     . HIS   A 1  61  ? 31.747  101.791 52.504  1.00 55.57  ? 61  HIS   A C     1 
ATOM   454   O  O     . HIS   A 1  61  ? 30.619  101.494 52.104  1.00 56.69  ? 61  HIS   A O     1 
ATOM   455   C  CB    . HIS   A 1  61  ? 31.064  103.478 54.231  1.00 69.59  ? 61  HIS   A CB    1 
ATOM   456   C  CG    . HIS   A 1  61  ? 31.315  104.796 54.890  1.00 66.52  ? 61  HIS   A CG    1 
ATOM   457   N  ND1   . HIS   A 1  61  ? 30.630  105.941 54.547  1.00 54.38  ? 61  HIS   A ND1   1 
ATOM   458   C  CD2   . HIS   A 1  61  ? 32.190  105.153 55.859  1.00 64.62  ? 61  HIS   A CD2   1 
ATOM   459   C  CE1   . HIS   A 1  61  ? 31.065  106.945 55.285  1.00 66.16  ? 61  HIS   A CE1   1 
ATOM   460   N  NE2   . HIS   A 1  61  ? 32.011  106.494 56.089  1.00 68.24  ? 61  HIS   A NE2   1 
ATOM   461   N  N     . VAL   A 1  62  ? 32.768  100.946 52.468  1.00 48.44  ? 62  VAL   A N     1 
ATOM   462   C  CA    . VAL   A 1  62  ? 32.714  99.684  51.747  1.00 58.86  ? 62  VAL   A CA    1 
ATOM   463   C  C     . VAL   A 1  62  ? 32.910  98.557  52.749  1.00 52.86  ? 62  VAL   A C     1 
ATOM   464   O  O     . VAL   A 1  62  ? 33.902  98.550  53.480  1.00 45.50  ? 62  VAL   A O     1 
ATOM   465   C  CB    . VAL   A 1  62  ? 33.763  99.593  50.624  1.00 61.48  ? 62  VAL   A CB    1 
ATOM   466   C  CG1   . VAL   A 1  62  ? 34.881  100.586 50.846  1.00 55.30  ? 62  VAL   A CG1   1 
ATOM   467   C  CG2   . VAL   A 1  62  ? 34.315  98.167  50.541  1.00 47.82  ? 62  VAL   A CG2   1 
ATOM   468   N  N     . PRO   A 1  63  ? 31.987  97.590  52.813  1.00 55.01  ? 63  PRO   A N     1 
ATOM   469   C  CA    . PRO   A 1  63  ? 32.157  96.436  53.699  1.00 42.22  ? 63  PRO   A CA    1 
ATOM   470   C  C     . PRO   A 1  63  ? 33.575  95.898  53.758  1.00 45.30  ? 63  PRO   A C     1 
ATOM   471   O  O     . PRO   A 1  63  ? 34.301  95.929  52.761  1.00 54.64  ? 63  PRO   A O     1 
ATOM   472   C  CB    . PRO   A 1  63  ? 31.196  95.418  53.085  1.00 40.06  ? 63  PRO   A CB    1 
ATOM   473   C  CG    . PRO   A 1  63  ? 30.061  96.278  52.609  1.00 38.66  ? 63  PRO   A CG    1 
ATOM   474   C  CD    . PRO   A 1  63  ? 30.674  97.569  52.138  1.00 45.51  ? 63  PRO   A CD    1 
ATOM   475   N  N     . ARG   A 1  64  ? 33.989  95.432  54.932  1.00 33.65  ? 64  ARG   A N     1 
ATOM   476   C  CA    . ARG   A 1  64  ? 35.218  94.656  55.057  1.00 44.07  ? 64  ARG   A CA    1 
ATOM   477   C  C     . ARG   A 1  64  ? 34.870  93.185  54.844  1.00 50.49  ? 64  ARG   A C     1 
ATOM   478   O  O     . ARG   A 1  64  ? 35.092  92.302  55.680  1.00 45.76  ? 64  ARG   A O     1 
ATOM   479   C  CB    . ARG   A 1  64  ? 35.883  94.904  56.406  1.00 49.47  ? 64  ARG   A CB    1 
ATOM   480   C  CG    . ARG   A 1  64  ? 35.837  96.364  56.842  1.00 56.27  ? 64  ARG   A CG    1 
ATOM   481   C  CD    . ARG   A 1  64  ? 36.355  96.562  58.269  1.00 62.22  ? 64  ARG   A CD    1 
ATOM   482   N  NE    . ARG   A 1  64  ? 37.782  96.850  58.266  1.00 61.68  ? 64  ARG   A NE    1 
ATOM   483   C  CZ    . ARG   A 1  64  ? 38.298  98.057  58.085  1.00 60.41  ? 64  ARG   A CZ    1 
ATOM   484   N  NH1   . ARG   A 1  64  ? 37.532  99.133  58.021  1.00 54.81  ? 64  ARG   A NH1   1 
ATOM   485   N  NH2   . ARG   A 1  64  ? 39.615  98.182  57.936  1.00 59.37  ? 64  ARG   A NH2   1 
ATOM   486   N  N     . ALA   A 1  65  ? 34.274  92.957  53.682  1.00 58.49  ? 65  ALA   A N     1 
ATOM   487   C  CA    . ALA   A 1  65  ? 33.623  91.703  53.361  1.00 51.54  ? 65  ALA   A CA    1 
ATOM   488   C  C     . ALA   A 1  65  ? 34.283  91.057  52.151  1.00 53.40  ? 65  ALA   A C     1 
ATOM   489   O  O     . ALA   A 1  65  ? 34.784  91.736  51.245  1.00 48.03  ? 65  ALA   A O     1 
ATOM   490   C  CB    . ALA   A 1  65  ? 32.130  91.929  53.093  1.00 40.75  ? 65  ALA   A CB    1 
ATOM   491   N  N     . VAL   A 1  66  ? 34.290  89.729  52.163  1.00 52.51  ? 66  VAL   A N     1 
ATOM   492   C  CA    A VAL   A 1  66  ? 34.725  88.930  51.028  0.66 52.15  ? 66  VAL   A CA    1 
ATOM   493   C  CA    B VAL   A 1  66  ? 34.738  88.916  51.039  0.34 52.10  ? 66  VAL   A CA    1 
ATOM   494   C  C     . VAL   A 1  66  ? 33.702  87.821  50.819  1.00 52.67  ? 66  VAL   A C     1 
ATOM   495   O  O     . VAL   A 1  66  ? 33.381  87.074  51.751  1.00 51.56  ? 66  VAL   A O     1 
ATOM   496   C  CB    A VAL   A 1  66  ? 36.141  88.353  51.232  0.66 49.18  ? 66  VAL   A CB    1 
ATOM   497   C  CB    B VAL   A 1  66  ? 36.128  88.307  51.287  0.34 49.18  ? 66  VAL   A CB    1 
ATOM   498   C  CG1   A VAL   A 1  66  ? 36.140  87.279  52.287  0.66 42.89  ? 66  VAL   A CG1   1 
ATOM   499   C  CG1   B VAL   A 1  66  ? 36.452  87.288  50.213  0.34 50.43  ? 66  VAL   A CG1   1 
ATOM   500   C  CG2   A VAL   A 1  66  ? 36.682  87.818  49.920  0.66 51.22  ? 66  VAL   A CG2   1 
ATOM   501   C  CG2   B VAL   A 1  66  ? 37.186  89.401  51.325  0.34 49.73  ? 66  VAL   A CG2   1 
ATOM   502   N  N     . PHE   A 1  67  ? 33.167  87.735  49.605  1.00 49.93  ? 67  PHE   A N     1 
ATOM   503   C  CA    . PHE   A 1  67  ? 32.216  86.698  49.227  1.00 46.63  ? 67  PHE   A CA    1 
ATOM   504   C  C     . PHE   A 1  67  ? 32.903  85.697  48.309  1.00 47.29  ? 67  PHE   A C     1 
ATOM   505   O  O     . PHE   A 1  67  ? 33.647  86.086  47.404  1.00 47.73  ? 67  PHE   A O     1 
ATOM   506   C  CB    . PHE   A 1  67  ? 31.012  87.280  48.492  1.00 44.00  ? 67  PHE   A CB    1 
ATOM   507   C  CG    . PHE   A 1  67  ? 30.159  88.179  49.318  1.00 47.21  ? 67  PHE   A CG    1 
ATOM   508   C  CD1   . PHE   A 1  67  ? 30.693  89.297  49.934  1.00 55.55  ? 67  PHE   A CD1   1 
ATOM   509   C  CD2   . PHE   A 1  67  ? 28.803  87.933  49.436  1.00 37.88  ? 67  PHE   A CD2   1 
ATOM   510   C  CE1   . PHE   A 1  67  ? 29.893  90.135  50.681  1.00 52.68  ? 67  PHE   A CE1   1 
ATOM   511   C  CE2   . PHE   A 1  67  ? 28.003  88.768  50.163  1.00 39.49  ? 67  PHE   A CE2   1 
ATOM   512   C  CZ    . PHE   A 1  67  ? 28.542  89.867  50.792  1.00 46.61  ? 67  PHE   A CZ    1 
ATOM   513   N  N     . VAL   A 1  68  ? 32.623  84.412  48.513  1.00 43.79  ? 68  VAL   A N     1 
ATOM   514   C  CA    A VAL   A 1  68  ? 33.270  83.359  47.741  0.58 37.38  ? 68  VAL   A CA    1 
ATOM   515   C  CA    B VAL   A 1  68  ? 33.274  83.354  47.744  0.42 37.46  ? 68  VAL   A CA    1 
ATOM   516   C  C     . VAL   A 1  68  ? 32.332  82.177  47.533  1.00 41.47  ? 68  VAL   A C     1 
ATOM   517   O  O     . VAL   A 1  68  ? 32.095  81.377  48.451  1.00 40.16  ? 68  VAL   A O     1 
ATOM   518   C  CB    A VAL   A 1  68  ? 34.571  82.920  48.428  0.58 38.17  ? 68  VAL   A CB    1 
ATOM   519   C  CB    B VAL   A 1  68  ? 34.571  82.879  48.424  0.42 38.22  ? 68  VAL   A CB    1 
ATOM   520   C  CG1   A VAL   A 1  68  ? 34.935  81.500  48.030  0.58 40.91  ? 68  VAL   A CG1   1 
ATOM   521   C  CG1   B VAL   A 1  68  ? 34.306  82.435  49.853  0.42 36.94  ? 68  VAL   A CG1   1 
ATOM   522   C  CG2   A VAL   A 1  68  ? 35.689  83.897  48.079  0.58 43.36  ? 68  VAL   A CG2   1 
ATOM   523   C  CG2   B VAL   A 1  68  ? 35.180  81.736  47.637  0.42 41.62  ? 68  VAL   A CG2   1 
ATOM   524   N  N     . ASP   A 1  69  ? 31.803  82.053  46.324  1.00 37.82  ? 69  ASP   A N     1 
ATOM   525   C  CA    . ASP   A 1  69  ? 31.053  80.877  45.907  1.00 42.59  ? 69  ASP   A CA    1 
ATOM   526   C  C     . ASP   A 1  69  ? 31.838  80.169  44.804  1.00 43.37  ? 69  ASP   A C     1 
ATOM   527   O  O     . ASP   A 1  69  ? 32.502  80.824  43.996  1.00 40.28  ? 69  ASP   A O     1 
ATOM   528   C  CB    . ASP   A 1  69  ? 29.655  81.279  45.420  1.00 47.38  ? 69  ASP   A CB    1 
ATOM   529   C  CG    . ASP   A 1  69  ? 28.680  80.130  45.443  1.00 41.33  ? 69  ASP   A CG    1 
ATOM   530   O  OD1   . ASP   A 1  69  ? 29.111  79.041  45.862  1.00 44.06  ? 69  ASP   A OD1   1 
ATOM   531   O  OD2   . ASP   A 1  69  ? 27.499  80.312  45.043  1.00 43.14  ? 69  ASP   A OD2   1 
ATOM   532   N  N     . LEU   A 1  70  ? 31.790  78.830  44.784  1.00 42.43  ? 70  LEU   A N     1 
ATOM   533   C  CA    . LEU   A 1  70  ? 32.479  78.055  43.751  1.00 37.61  ? 70  LEU   A CA    1 
ATOM   534   C  C     . LEU   A 1  70  ? 31.763  78.058  42.406  1.00 45.02  ? 70  LEU   A C     1 
ATOM   535   O  O     . LEU   A 1  70  ? 32.220  77.372  41.484  1.00 45.30  ? 70  LEU   A O     1 
ATOM   536   C  CB    . LEU   A 1  70  ? 32.676  76.613  44.191  1.00 27.27  ? 70  LEU   A CB    1 
ATOM   537   C  CG    . LEU   A 1  70  ? 33.715  76.483  45.278  1.00 44.34  ? 70  LEU   A CG    1 
ATOM   538   C  CD1   . LEU   A 1  70  ? 34.027  75.004  45.551  1.00 39.06  ? 70  LEU   A CD1   1 
ATOM   539   C  CD2   . LEU   A 1  70  ? 34.945  77.282  44.853  1.00 38.98  ? 70  LEU   A CD2   1 
ATOM   540   N  N     . GLU   A 1  71  ? 30.660  78.790  42.268  1.00 41.67  ? 71  GLU   A N     1 
ATOM   541   C  CA    . GLU   A 1  71  ? 30.077  79.026  40.953  1.00 43.67  ? 71  GLU   A CA    1 
ATOM   542   C  C     . GLU   A 1  71  ? 29.521  80.446  40.918  1.00 46.26  ? 71  GLU   A C     1 
ATOM   543   O  O     . GLU   A 1  71  ? 29.408  81.091  41.965  1.00 60.60  ? 71  GLU   A O     1 
ATOM   544   C  CB    . GLU   A 1  71  ? 29.005  77.974  40.622  1.00 50.01  ? 71  GLU   A CB    1 
ATOM   545   C  CG    . GLU   A 1  71  ? 27.881  77.812  41.643  1.00 40.85  ? 71  GLU   A CG    1 
ATOM   546   C  CD    . GLU   A 1  71  ? 26.621  78.581  41.263  1.00 38.08  ? 71  GLU   A CD    1 
ATOM   547   O  OE1   . GLU   A 1  71  ? 26.724  79.600  40.557  1.00 41.45  ? 71  GLU   A OE1   1 
ATOM   548   O  OE2   . GLU   A 1  71  ? 25.519  78.166  41.672  1.00 52.24  ? 71  GLU   A OE2   1 
ATOM   549   N  N     . PRO   A 1  72  ? 29.198  80.989  39.744  1.00 42.53  ? 72  PRO   A N     1 
ATOM   550   C  CA    . PRO   A 1  72  ? 28.921  82.425  39.655  1.00 43.37  ? 72  PRO   A CA    1 
ATOM   551   C  C     . PRO   A 1  72  ? 27.478  82.848  39.861  1.00 50.69  ? 72  PRO   A C     1 
ATOM   552   O  O     . PRO   A 1  72  ? 27.238  84.055  40.003  1.00 52.16  ? 72  PRO   A O     1 
ATOM   553   C  CB    . PRO   A 1  72  ? 29.364  82.759  38.222  1.00 51.27  ? 72  PRO   A CB    1 
ATOM   554   C  CG    . PRO   A 1  72  ? 29.125  81.483  37.455  1.00 41.50  ? 72  PRO   A CG    1 
ATOM   555   C  CD    . PRO   A 1  72  ? 29.430  80.371  38.421  1.00 44.80  ? 72  PRO   A CD    1 
ATOM   556   N  N     . THR   A 1  73  ? 26.518  81.923  39.869  1.00 49.29  ? 73  THR   A N     1 
ATOM   557   C  CA    . THR   A 1  73  ? 25.112  82.324  39.811  1.00 54.32  ? 73  THR   A CA    1 
ATOM   558   C  C     . THR   A 1  73  ? 24.769  83.308  40.926  1.00 56.49  ? 73  THR   A C     1 
ATOM   559   O  O     . THR   A 1  73  ? 24.122  84.336  40.690  1.00 56.80  ? 73  THR   A O     1 
ATOM   560   C  CB    . THR   A 1  73  ? 24.188  81.100  39.902  1.00 58.10  ? 73  THR   A CB    1 
ATOM   561   O  OG1   . THR   A 1  73  ? 24.847  79.932  39.398  1.00 49.34  ? 73  THR   A OG1   1 
ATOM   562   C  CG2   . THR   A 1  73  ? 22.906  81.340  39.112  1.00 58.64  ? 73  THR   A CG2   1 
ATOM   563   N  N     . VAL   A 1  74  ? 25.193  83.001  42.155  1.00 56.86  ? 74  VAL   A N     1 
ATOM   564   C  CA    . VAL   A 1  74  ? 24.703  83.739  43.315  1.00 55.00  ? 74  VAL   A CA    1 
ATOM   565   C  C     . VAL   A 1  74  ? 25.447  85.062  43.473  1.00 48.50  ? 74  VAL   A C     1 
ATOM   566   O  O     . VAL   A 1  74  ? 24.832  86.128  43.599  1.00 52.44  ? 74  VAL   A O     1 
ATOM   567   C  CB    . VAL   A 1  74  ? 24.808  82.872  44.584  1.00 46.86  ? 74  VAL   A CB    1 
ATOM   568   C  CG1   . VAL   A 1  74  ? 23.645  83.166  45.490  1.00 42.47  ? 74  VAL   A CG1   1 
ATOM   569   C  CG2   . VAL   A 1  74  ? 24.840  81.395  44.229  1.00 46.57  ? 74  VAL   A CG2   1 
ATOM   570   N  N     . ILE   A 1  75  ? 26.778  85.020  43.474  1.00 35.89  ? 75  ILE   A N     1 
ATOM   571   C  CA    . ILE   A 1  75  ? 27.547  86.253  43.604  1.00 42.16  ? 75  ILE   A CA    1 
ATOM   572   C  C     . ILE   A 1  75  ? 27.330  87.192  42.413  1.00 44.57  ? 75  ILE   A C     1 
ATOM   573   O  O     . ILE   A 1  75  ? 27.443  88.413  42.557  1.00 45.43  ? 75  ILE   A O     1 
ATOM   574   C  CB    . ILE   A 1  75  ? 29.032  85.915  43.816  1.00 36.62  ? 75  ILE   A CB    1 
ATOM   575   C  CG1   . ILE   A 1  75  ? 29.209  85.214  45.178  1.00 35.49  ? 75  ILE   A CG1   1 
ATOM   576   C  CG2   . ILE   A 1  75  ? 29.881  87.165  43.645  1.00 38.69  ? 75  ILE   A CG2   1 
ATOM   577   C  CD1   . ILE   A 1  75  ? 30.632  84.758  45.492  1.00 36.64  ? 75  ILE   A CD1   1 
ATOM   578   N  N     . ASP   A 1  76  ? 27.017  86.653  41.229  1.00 47.13  ? 76  ASP   A N     1 
ATOM   579   C  CA    . ASP   A 1  76  ? 26.571  87.505  40.125  1.00 51.78  ? 76  ASP   A CA    1 
ATOM   580   C  C     . ASP   A 1  76  ? 25.421  88.394  40.559  1.00 56.45  ? 76  ASP   A C     1 
ATOM   581   O  O     . ASP   A 1  76  ? 25.388  89.589  40.237  1.00 56.89  ? 76  ASP   A O     1 
ATOM   582   C  CB    . ASP   A 1  76  ? 26.137  86.662  38.920  1.00 47.82  ? 76  ASP   A CB    1 
ATOM   583   C  CG    . ASP   A 1  76  ? 27.291  86.342  37.973  1.00 50.91  ? 76  ASP   A CG    1 
ATOM   584   O  OD1   . ASP   A 1  76  ? 28.396  86.893  38.169  1.00 47.01  ? 76  ASP   A OD1   1 
ATOM   585   O  OD2   . ASP   A 1  76  ? 27.092  85.527  37.042  1.00 47.50  ? 76  ASP   A OD2   1 
ATOM   586   N  N     . GLU   A 1  77  ? 24.456  87.819  41.280  1.00 58.62  ? 77  GLU   A N     1 
ATOM   587   C  CA    . GLU   A 1  77  ? 23.358  88.614  41.809  1.00 63.48  ? 77  GLU   A CA    1 
ATOM   588   C  C     . GLU   A 1  77  ? 23.886  89.808  42.591  1.00 60.66  ? 77  GLU   A C     1 
ATOM   589   O  O     . GLU   A 1  77  ? 23.376  90.922  42.446  1.00 62.41  ? 77  GLU   A O     1 
ATOM   590   C  CB    . GLU   A 1  77  ? 22.444  87.739  42.675  1.00 68.39  ? 77  GLU   A CB    1 
ATOM   591   C  CG    . GLU   A 1  77  ? 21.451  86.865  41.875  1.00 67.07  ? 77  GLU   A CG    1 
ATOM   592   C  CD    . GLU   A 1  77  ? 20.297  87.676  41.277  1.00 92.51  ? 77  GLU   A CD    1 
ATOM   593   O  OE1   . GLU   A 1  77  ? 19.606  88.389  42.044  1.00 89.90  ? 77  GLU   A OE1   1 
ATOM   594   O  OE2   . GLU   A 1  77  ? 20.089  87.615  40.041  1.00 83.89  ? 77  GLU   A OE2   1 
ATOM   595   N  N     . VAL   A 1  78  ? 24.939  89.600  43.391  1.00 60.11  ? 78  VAL   A N     1 
ATOM   596   C  CA    . VAL   A 1  78  ? 25.549  90.692  44.146  1.00 52.91  ? 78  VAL   A CA    1 
ATOM   597   C  C     . VAL   A 1  78  ? 26.290  91.648  43.219  1.00 51.85  ? 78  VAL   A C     1 
ATOM   598   O  O     . VAL   A 1  78  ? 26.223  92.869  43.395  1.00 59.74  ? 78  VAL   A O     1 
ATOM   599   C  CB    . VAL   A 1  78  ? 26.489  90.146  45.234  1.00 52.45  ? 78  VAL   A CB    1 
ATOM   600   C  CG1   . VAL   A 1  78  ? 26.896  91.266  46.181  1.00 42.73  ? 78  VAL   A CG1   1 
ATOM   601   C  CG2   . VAL   A 1  78  ? 25.838  89.024  45.979  1.00 34.65  ? 78  VAL   A CG2   1 
ATOM   602   N  N     . ARG   A 1  79  ? 27.020  91.120  42.231  1.00 56.40  ? 79  ARG   A N     1 
ATOM   603   C  CA    . ARG   A 1  79  ? 27.694  91.991  41.264  1.00 59.60  ? 79  ARG   A CA    1 
ATOM   604   C  C     . ARG   A 1  79  ? 26.713  92.872  40.500  1.00 61.93  ? 79  ARG   A C     1 
ATOM   605   O  O     . ARG   A 1  79  ? 27.075  93.980  40.086  1.00 64.67  ? 79  ARG   A O     1 
ATOM   606   C  CB    . ARG   A 1  79  ? 28.515  91.170  40.271  1.00 46.90  ? 79  ARG   A CB    1 
ATOM   607   C  CG    . ARG   A 1  79  ? 29.760  90.552  40.860  1.00 46.50  ? 79  ARG   A CG    1 
ATOM   608   C  CD    . ARG   A 1  79  ? 30.213  89.416  39.982  1.00 48.44  ? 79  ARG   A CD    1 
ATOM   609   N  NE    . ARG   A 1  79  ? 31.440  88.791  40.463  1.00 51.38  ? 79  ARG   A NE    1 
ATOM   610   C  CZ    . ARG   A 1  79  ? 31.760  87.524  40.236  1.00 56.13  ? 79  ARG   A CZ    1 
ATOM   611   N  NH1   . ARG   A 1  79  ? 30.961  86.718  39.543  1.00 54.50  ? 79  ARG   A NH1   1 
ATOM   612   N  NH2   . ARG   A 1  79  ? 32.902  87.046  40.727  1.00 47.83  ? 79  ARG   A NH2   1 
ATOM   613   N  N     . THR   A 1  80  ? 25.478  92.405  40.297  1.00 59.91  ? 80  THR   A N     1 
ATOM   614   C  CA    . THR   A 1  80  ? 24.468  93.143  39.546  1.00 65.46  ? 80  THR   A CA    1 
ATOM   615   C  C     . THR   A 1  80  ? 23.359  93.738  40.404  1.00 70.15  ? 80  THR   A C     1 
ATOM   616   O  O     . THR   A 1  80  ? 22.783  94.756  40.016  1.00 79.24  ? 80  THR   A O     1 
ATOM   617   C  CB    . THR   A 1  80  ? 23.820  92.235  38.494  1.00 68.09  ? 80  THR   A CB    1 
ATOM   618   O  OG1   . THR   A 1  80  ? 23.058  91.219  39.160  1.00 70.86  ? 80  THR   A OG1   1 
ATOM   619   C  CG2   . THR   A 1  80  ? 24.883  91.580  37.615  1.00 55.68  ? 80  THR   A CG2   1 
ATOM   620   N  N     . GLY   A 1  81  ? 23.034  93.128  41.545  1.00 68.54  ? 81  GLY   A N     1 
ATOM   621   C  CA    . GLY   A 1  81  ? 21.926  93.560  42.386  1.00 68.81  ? 81  GLY   A CA    1 
ATOM   622   C  C     . GLY   A 1  81  ? 21.979  95.002  42.851  1.00 64.26  ? 81  GLY   A C     1 
ATOM   623   O  O     . GLY   A 1  81  ? 22.726  95.808  42.290  1.00 72.38  ? 81  GLY   A O     1 
ATOM   624   N  N     . THR   A 1  82  ? 21.203  95.346  43.882  1.00 54.88  ? 82  THR   A N     1 
ATOM   625   C  CA    . THR   A 1  82  ? 21.033  96.760  44.190  1.00 59.86  ? 82  THR   A CA    1 
ATOM   626   C  C     . THR   A 1  82  ? 22.239  97.348  44.909  1.00 51.62  ? 82  THR   A C     1 
ATOM   627   O  O     . THR   A 1  82  ? 22.481  98.556  44.817  1.00 57.53  ? 82  THR   A O     1 
ATOM   628   C  CB    . THR   A 1  82  ? 19.758  96.989  45.010  1.00 50.90  ? 82  THR   A CB    1 
ATOM   629   O  OG1   . THR   A 1  82  ? 20.058  96.934  46.404  1.00 66.45  ? 82  THR   A OG1   1 
ATOM   630   C  CG2   . THR   A 1  82  ? 18.723  95.941  44.699  1.00 46.40  ? 82  THR   A CG2   1 
ATOM   631   N  N     . TYR   A 1  83  ? 23.017  96.526  45.606  1.00 54.61  ? 83  TYR   A N     1 
ATOM   632   C  CA    . TYR   A 1  83  ? 24.151  97.017  46.382  1.00 64.65  ? 83  TYR   A CA    1 
ATOM   633   C  C     . TYR   A 1  83  ? 25.480  96.761  45.680  1.00 66.07  ? 83  TYR   A C     1 
ATOM   634   O  O     . TYR   A 1  83  ? 26.495  96.526  46.341  1.00 70.92  ? 83  TYR   A O     1 
ATOM   635   C  CB    . TYR   A 1  83  ? 24.150  96.397  47.784  1.00 58.30  ? 83  TYR   A CB    1 
ATOM   636   C  CG    . TYR   A 1  83  ? 23.173  97.050  48.751  1.00 62.40  ? 83  TYR   A CG    1 
ATOM   637   C  CD1   . TYR   A 1  83  ? 23.512  98.219  49.434  1.00 61.24  ? 83  TYR   A CD1   1 
ATOM   638   C  CD2   . TYR   A 1  83  ? 21.913  96.498  48.984  1.00 59.60  ? 83  TYR   A CD2   1 
ATOM   639   C  CE1   . TYR   A 1  83  ? 22.625  98.818  50.317  1.00 60.58  ? 83  TYR   A CE1   1 
ATOM   640   C  CE2   . TYR   A 1  83  ? 21.011  97.094  49.861  1.00 50.93  ? 83  TYR   A CE2   1 
ATOM   641   C  CZ    . TYR   A 1  83  ? 21.373  98.253  50.529  1.00 65.29  ? 83  TYR   A CZ    1 
ATOM   642   O  OH    . TYR   A 1  83  ? 20.488  98.851  51.412  1.00 62.69  ? 83  TYR   A OH    1 
ATOM   643   N  N     . ARG   A 1  84  ? 25.498  96.832  44.345  1.00 70.72  ? 84  ARG   A N     1 
ATOM   644   C  CA    . ARG   A 1  84  ? 26.691  96.442  43.596  1.00 66.42  ? 84  ARG   A CA    1 
ATOM   645   C  C     . ARG   A 1  84  ? 27.832  97.438  43.760  1.00 62.72  ? 84  ARG   A C     1 
ATOM   646   O  O     . ARG   A 1  84  ? 28.999  97.031  43.732  1.00 58.27  ? 84  ARG   A O     1 
ATOM   647   C  CB    . ARG   A 1  84  ? 26.349  96.260  42.116  1.00 68.75  ? 84  ARG   A CB    1 
ATOM   648   C  CG    . ARG   A 1  84  ? 25.802  97.486  41.442  1.00 65.76  ? 84  ARG   A CG    1 
ATOM   649   C  CD    . ARG   A 1  84  ? 24.906  97.112  40.291  1.00 67.03  ? 84  ARG   A CD    1 
ATOM   650   N  NE    . ARG   A 1  84  ? 24.609  98.267  39.452  1.00 87.95  ? 84  ARG   A NE    1 
ATOM   651   C  CZ    . ARG   A 1  84  ? 23.584  99.091  39.629  1.00 88.41  ? 84  ARG   A CZ    1 
ATOM   652   N  NH1   . ARG   A 1  84  ? 22.717  98.916  40.615  1.00 83.88  ? 84  ARG   A NH1   1 
ATOM   653   N  NH2   . ARG   A 1  84  ? 23.425  100.116 38.795  1.00 92.59  ? 84  ARG   A NH2   1 
ATOM   654   N  N     . GLN   A 1  85  ? 27.529  98.734  43.937  1.00 62.60  ? 85  GLN   A N     1 
ATOM   655   C  CA    . GLN   A 1  85  ? 28.584  99.726  44.169  1.00 67.98  ? 85  GLN   A CA    1 
ATOM   656   C  C     . GLN   A 1  85  ? 29.240  99.580  45.538  1.00 66.52  ? 85  GLN   A C     1 
ATOM   657   O  O     . GLN   A 1  85  ? 30.330  100.121 45.757  1.00 61.42  ? 85  GLN   A O     1 
ATOM   658   C  CB    . GLN   A 1  85  ? 28.042  101.153 44.049  1.00 61.43  ? 85  GLN   A CB    1 
ATOM   659   C  CG    . GLN   A 1  85  ? 27.154  101.412 42.864  1.00 56.22  ? 85  GLN   A CG    1 
ATOM   660   C  CD    . GLN   A 1  85  ? 25.711  101.643 43.280  1.00 73.71  ? 85  GLN   A CD    1 
ATOM   661   O  OE1   . GLN   A 1  85  ? 25.035  100.736 43.797  1.00 69.87  ? 85  GLN   A OE1   1 
ATOM   662   N  NE2   . GLN   A 1  85  ? 25.233  102.867 43.074  1.00 65.08  ? 85  GLN   A NE2   1 
ATOM   663   N  N     . LEU   A 1  86  ? 28.602  98.864  46.459  1.00 66.81  ? 86  LEU   A N     1 
ATOM   664   C  CA    . LEU   A 1  86  ? 29.090  98.808  47.826  1.00 62.42  ? 86  LEU   A CA    1 
ATOM   665   C  C     . LEU   A 1  86  ? 30.349  97.954  47.952  1.00 60.31  ? 86  LEU   A C     1 
ATOM   666   O  O     . LEU   A 1  86  ? 31.168  98.209  48.836  1.00 63.39  ? 86  LEU   A O     1 
ATOM   667   C  CB    . LEU   A 1  86  ? 27.971  98.284  48.728  1.00 71.03  ? 86  LEU   A CB    1 
ATOM   668   C  CG    . LEU   A 1  86  ? 27.954  98.522  50.238  1.00 61.13  ? 86  LEU   A CG    1 
ATOM   669   C  CD1   . LEU   A 1  86  ? 27.866  99.996  50.547  1.00 57.86  ? 86  LEU   A CD1   1 
ATOM   670   C  CD2   . LEU   A 1  86  ? 26.773  97.782  50.826  1.00 55.41  ? 86  LEU   A CD2   1 
ATOM   671   N  N     . PHE   A 1  87  ? 30.531  96.951  47.090  1.00 70.02  ? 87  PHE   A N     1 
ATOM   672   C  CA    . PHE   A 1  87  ? 31.671  96.039  47.163  1.00 60.50  ? 87  PHE   A CA    1 
ATOM   673   C  C     . PHE   A 1  87  ? 32.634  96.287  46.009  1.00 66.09  ? 87  PHE   A C     1 
ATOM   674   O  O     . PHE   A 1  87  ? 32.211  96.553  44.876  1.00 67.23  ? 87  PHE   A O     1 
ATOM   675   C  CB    . PHE   A 1  87  ? 31.238  94.573  47.108  1.00 53.44  ? 87  PHE   A CB    1 
ATOM   676   C  CG    . PHE   A 1  87  ? 30.110  94.234  48.018  1.00 55.30  ? 87  PHE   A CG    1 
ATOM   677   C  CD1   . PHE   A 1  87  ? 28.794  94.419  47.603  1.00 47.79  ? 87  PHE   A CD1   1 
ATOM   678   C  CD2   . PHE   A 1  87  ? 30.355  93.711  49.282  1.00 48.88  ? 87  PHE   A CD2   1 
ATOM   679   C  CE1   . PHE   A 1  87  ? 27.734  94.109  48.444  1.00 44.36  ? 87  PHE   A CE1   1 
ATOM   680   C  CE2   . PHE   A 1  87  ? 29.303  93.393  50.128  1.00 48.24  ? 87  PHE   A CE2   1 
ATOM   681   C  CZ    . PHE   A 1  87  ? 27.989  93.591  49.709  1.00 50.11  ? 87  PHE   A CZ    1 
ATOM   682   N  N     . HIS   A 1  88  ? 33.920  96.170  46.285  1.00 63.13  ? 88  HIS   A N     1 
ATOM   683   C  CA    . HIS   A 1  88  ? 34.586  96.299  45.001  1.00 67.26  ? 88  HIS   A CA    1 
ATOM   684   C  C     . HIS   A 1  88  ? 34.874  94.920  44.414  1.00 68.77  ? 88  HIS   A C     1 
ATOM   685   O  O     . HIS   A 1  88  ? 34.983  93.931  45.148  1.00 64.25  ? 88  HIS   A O     1 
ATOM   686   C  CB    . HIS   A 1  88  ? 35.887  97.109  45.121  1.00 74.70  ? 88  HIS   A CB    1 
ATOM   687   C  CG    . HIS   A 1  88  ? 36.929  96.482  45.999  1.00 79.51  ? 88  HIS   A CG    1 
ATOM   688   N  ND1   . HIS   A 1  88  ? 38.149  96.048  45.519  1.00 86.18  ? 88  HIS   A ND1   1 
ATOM   689   C  CD2   . HIS   A 1  88  ? 36.945  96.240  47.333  1.00 90.29  ? 88  HIS   A CD2   1 
ATOM   690   C  CE1   . HIS   A 1  88  ? 38.863  95.550  46.515  1.00 84.25  ? 88  HIS   A CE1   1 
ATOM   691   N  NE2   . HIS   A 1  88  ? 38.155  95.654  47.627  1.00 93.87  ? 88  HIS   A NE2   1 
ATOM   692   N  N     . PRO   A 1  89  ? 34.972  94.827  43.094  1.00 66.24  ? 89  PRO   A N     1 
ATOM   693   C  CA    . PRO   A 1  89  ? 35.148  93.521  42.444  1.00 61.73  ? 89  PRO   A CA    1 
ATOM   694   C  C     . PRO   A 1  89  ? 36.109  92.557  43.132  1.00 58.04  ? 89  PRO   A C     1 
ATOM   695   O  O     . PRO   A 1  89  ? 35.800  91.369  43.237  1.00 60.72  ? 89  PRO   A O     1 
ATOM   696   C  CB    . PRO   A 1  89  ? 35.655  93.915  41.055  1.00 68.49  ? 89  PRO   A CB    1 
ATOM   697   C  CG    . PRO   A 1  89  ? 34.909  95.203  40.777  1.00 69.88  ? 89  PRO   A CG    1 
ATOM   698   C  CD    . PRO   A 1  89  ? 34.767  95.909  42.113  1.00 59.65  ? 89  PRO   A CD    1 
ATOM   699   N  N     . GLU   A 1  90  ? 37.269  93.026  43.596  1.00 57.28  ? 90  GLU   A N     1 
ATOM   700   C  CA    . GLU   A 1  90  ? 38.258  92.101  44.145  1.00 57.85  ? 90  GLU   A CA    1 
ATOM   701   C  C     . GLU   A 1  90  ? 37.708  91.241  45.271  1.00 62.82  ? 90  GLU   A C     1 
ATOM   702   O  O     . GLU   A 1  90  ? 38.347  90.250  45.642  1.00 58.75  ? 90  GLU   A O     1 
ATOM   703   C  CB    . GLU   A 1  90  ? 39.485  92.847  44.671  1.00 65.01  ? 90  GLU   A CB    1 
ATOM   704   C  CG    . GLU   A 1  90  ? 40.573  93.069  43.647  1.00 85.06  ? 90  GLU   A CG    1 
ATOM   705   C  CD    . GLU   A 1  90  ? 40.249  94.216  42.713  1.00 90.16  ? 90  GLU   A CD    1 
ATOM   706   O  OE1   . GLU   A 1  90  ? 39.358  95.028  43.067  1.00 83.28  ? 90  GLU   A OE1   1 
ATOM   707   O  OE2   . GLU   A 1  90  ? 40.881  94.299  41.632  1.00 91.06  ? 90  GLU   A OE2   1 
ATOM   708   N  N     . GLN   A 1  91  ? 36.570  91.601  45.854  1.00 58.28  ? 91  GLN   A N     1 
ATOM   709   C  CA    . GLN   A 1  91  ? 36.077  90.883  47.017  1.00 53.93  ? 91  GLN   A CA    1 
ATOM   710   C  C     . GLN   A 1  91  ? 34.884  89.987  46.704  1.00 52.28  ? 91  GLN   A C     1 
ATOM   711   O  O     . GLN   A 1  91  ? 34.398  89.288  47.601  1.00 56.68  ? 91  GLN   A O     1 
ATOM   712   C  CB    . GLN   A 1  91  ? 35.742  91.872  48.140  1.00 61.73  ? 91  GLN   A CB    1 
ATOM   713   C  CG    . GLN   A 1  91  ? 34.743  92.946  47.751  1.00 70.87  ? 91  GLN   A CG    1 
ATOM   714   C  CD    . GLN   A 1  91  ? 34.902  94.222  48.563  1.00 67.39  ? 91  GLN   A CD    1 
ATOM   715   O  OE1   . GLN   A 1  91  ? 34.342  95.264  48.214  1.00 69.65  ? 91  GLN   A OE1   1 
ATOM   716   N  NE2   . GLN   A 1  91  ? 35.674  94.150  49.643  1.00 52.51  ? 91  GLN   A NE2   1 
ATOM   717   N  N     . LEU   A 1  92  ? 34.424  89.955  45.457  1.00 50.34  ? 92  LEU   A N     1 
ATOM   718   C  CA    . LEU   A 1  92  ? 33.414  89.004  45.003  1.00 42.60  ? 92  LEU   A CA    1 
ATOM   719   C  C     . LEU   A 1  92  ? 34.119  87.959  44.138  1.00 42.99  ? 92  LEU   A C     1 
ATOM   720   O  O     . LEU   A 1  92  ? 34.366  88.185  42.953  1.00 52.67  ? 92  LEU   A O     1 
ATOM   721   C  CB    . LEU   A 1  92  ? 32.308  89.727  44.250  1.00 41.53  ? 92  LEU   A CB    1 
ATOM   722   C  CG    . LEU   A 1  92  ? 31.796  91.019  44.893  1.00 37.71  ? 92  LEU   A CG    1 
ATOM   723   C  CD1   . LEU   A 1  92  ? 30.373  91.323  44.448  1.00 45.91  ? 92  LEU   A CD1   1 
ATOM   724   C  CD2   . LEU   A 1  92  ? 31.842  90.909  46.377  1.00 49.43  ? 92  LEU   A CD2   1 
ATOM   725   N  N     . ILE   A 1  93  ? 34.452  86.820  44.737  1.00 42.89  ? 93  ILE   A N     1 
ATOM   726   C  CA    . ILE   A 1  93  ? 35.284  85.792  44.122  1.00 38.35  ? 93  ILE   A CA    1 
ATOM   727   C  C     . ILE   A 1  93  ? 34.409  84.600  43.754  1.00 44.94  ? 93  ILE   A C     1 
ATOM   728   O  O     . ILE   A 1  93  ? 33.897  83.908  44.640  1.00 49.93  ? 93  ILE   A O     1 
ATOM   729   C  CB    . ILE   A 1  93  ? 36.407  85.341  45.063  1.00 36.22  ? 93  ILE   A CB    1 
ATOM   730   C  CG1   . ILE   A 1  93  ? 37.131  86.543  45.680  1.00 47.00  ? 93  ILE   A CG1   1 
ATOM   731   C  CG2   . ILE   A 1  93  ? 37.371  84.440  44.318  1.00 38.49  ? 93  ILE   A CG2   1 
ATOM   732   C  CD1   . ILE   A 1  93  ? 38.020  86.187  46.887  1.00 29.55  ? 93  ILE   A CD1   1 
ATOM   733   N  N     . THR   A 1  94  ? 34.289  84.312  42.460  1.00 52.36  ? 94  THR   A N     1 
ATOM   734   C  CA    . THR   A 1  94  ? 33.477  83.198  41.984  1.00 51.71  ? 94  THR   A CA    1 
ATOM   735   C  C     . THR   A 1  94  ? 34.281  82.234  41.116  1.00 50.75  ? 94  THR   A C     1 
ATOM   736   O  O     . THR   A 1  94  ? 35.228  82.625  40.427  1.00 50.45  ? 94  THR   A O     1 
ATOM   737   C  CB    . THR   A 1  94  ? 32.262  83.705  41.203  1.00 58.73  ? 94  THR   A CB    1 
ATOM   738   O  OG1   . THR   A 1  94  ? 32.686  84.538  40.113  1.00 53.40  ? 94  THR   A OG1   1 
ATOM   739   C  CG2   . THR   A 1  94  ? 31.362  84.507  42.137  1.00 53.72  ? 94  THR   A CG2   1 
ATOM   740   N  N     . GLY   A 1  95  ? 33.878  80.961  41.153  1.00 65.55  ? 95  GLY   A N     1 
ATOM   741   C  CA    . GLY   A 1  95  ? 34.525  79.901  40.418  1.00 54.78  ? 95  GLY   A CA    1 
ATOM   742   C  C     . GLY   A 1  95  ? 33.687  79.367  39.266  1.00 48.12  ? 95  GLY   A C     1 
ATOM   743   O  O     . GLY   A 1  95  ? 32.632  79.898  38.913  1.00 43.81  ? 95  GLY   A O     1 
ATOM   744   N  N     . LYS   A 1  96  ? 34.179  78.276  38.683  1.00 60.36  ? 96  LYS   A N     1 
ATOM   745   C  CA    . LYS   A 1  96  ? 33.659  77.756  37.408  1.00 59.54  ? 96  LYS   A CA    1 
ATOM   746   C  C     . LYS   A 1  96  ? 32.462  76.837  37.646  1.00 49.35  ? 96  LYS   A C     1 
ATOM   747   O  O     . LYS   A 1  96  ? 31.323  77.178  37.316  1.00 45.95  ? 96  LYS   A O     1 
ATOM   748   C  CB    . LYS   A 1  96  ? 34.778  77.032  36.646  1.00 61.33  ? 96  LYS   A CB    1 
ATOM   749   C  CG    . LYS   A 1  96  ? 36.221  77.526  36.937  1.00 78.31  ? 96  LYS   A CG    1 
ATOM   750   C  CD    . LYS   A 1  96  ? 36.770  77.084  38.324  1.00 73.87  ? 96  LYS   A CD    1 
ATOM   751   C  CE    . LYS   A 1  96  ? 38.059  77.851  38.699  1.00 79.80  ? 96  LYS   A CE    1 
ATOM   752   N  NZ    . LYS   A 1  96  ? 38.458  77.753  40.151  1.00 58.59  ? 96  LYS   A NZ    1 
ATOM   753   N  N     . GLU   A 1  97  ? 32.717  75.657  38.190  1.00 48.78  ? 97  GLU   A N     1 
ATOM   754   C  CA    . GLU   A 1  97  ? 31.675  74.721  38.560  1.00 50.24  ? 97  GLU   A CA    1 
ATOM   755   C  C     . GLU   A 1  97  ? 31.750  74.500  40.066  1.00 45.47  ? 97  GLU   A C     1 
ATOM   756   O  O     . GLU   A 1  97  ? 32.738  74.848  40.711  1.00 46.48  ? 97  GLU   A O     1 
ATOM   757   C  CB    . GLU   A 1  97  ? 31.794  73.400  37.757  1.00 53.78  ? 97  GLU   A CB    1 
ATOM   758   C  CG    . GLU   A 1  97  ? 32.877  72.396  38.159  1.00 52.55  ? 97  GLU   A CG    1 
ATOM   759   C  CD    . GLU   A 1  97  ? 33.149  71.336  37.062  1.00 66.56  ? 97  GLU   A CD    1 
ATOM   760   O  OE1   . GLU   A 1  97  ? 33.740  71.683  36.009  1.00 73.37  ? 97  GLU   A OE1   1 
ATOM   761   O  OE2   . GLU   A 1  97  ? 32.774  70.156  37.247  1.00 53.44  ? 97  GLU   A OE2   1 
ATOM   762   N  N     . ASP   A 1  98  ? 30.682  73.953  40.637  1.00 52.93  ? 98  ASP   A N     1 
ATOM   763   C  CA    . ASP   A 1  98  ? 30.555  73.933  42.084  1.00 36.57  ? 98  ASP   A CA    1 
ATOM   764   C  C     . ASP   A 1  98  ? 30.866  72.558  42.640  1.00 35.09  ? 98  ASP   A C     1 
ATOM   765   O  O     . ASP   A 1  98  ? 31.286  71.641  41.922  1.00 54.17  ? 98  ASP   A O     1 
ATOM   766   C  CB    . ASP   A 1  98  ? 29.166  74.396  42.506  1.00 32.58  ? 98  ASP   A CB    1 
ATOM   767   C  CG    . ASP   A 1  98  ? 28.093  73.413  42.161  1.00 26.88  ? 98  ASP   A CG    1 
ATOM   768   O  OD1   . ASP   A 1  98  ? 28.193  72.256  42.590  1.00 29.30  ? 98  ASP   A OD1   1 
ATOM   769   O  OD2   . ASP   A 1  98  ? 27.128  73.804  41.489  1.00 36.50  ? 98  ASP   A OD2   1 
ATOM   770   N  N     . ALA   A 1  99  ? 30.640  72.403  43.936  1.00 26.43  ? 99  ALA   A N     1 
ATOM   771   C  CA    . ALA   A 1  99  ? 31.090  71.230  44.675  1.00 33.64  ? 99  ALA   A CA    1 
ATOM   772   C  C     . ALA   A 1  99  ? 30.038  70.126  44.738  1.00 30.01  ? 99  ALA   A C     1 
ATOM   773   O  O     . ALA   A 1  99  ? 30.221  69.154  45.492  1.00 27.63  ? 99  ALA   A O     1 
ATOM   774   C  CB    . ALA   A 1  99  ? 31.527  71.636  46.091  1.00 25.25  ? 99  ALA   A CB    1 
ATOM   775   N  N     . ALA   A 1  100 ? 28.942  70.271  43.986  1.00 18.88  ? 100 ALA   A N     1 
ATOM   776   C  CA    . ALA   A 1  100 ? 27.931  69.226  43.816  1.00 28.74  ? 100 ALA   A CA    1 
ATOM   777   C  C     . ALA   A 1  100 ? 27.507  68.587  45.143  1.00 29.09  ? 100 ALA   A C     1 
ATOM   778   O  O     . ALA   A 1  100 ? 27.490  67.369  45.284  1.00 34.82  ? 100 ALA   A O     1 
ATOM   779   C  CB    . ALA   A 1  100 ? 28.437  68.154  42.844  1.00 27.71  ? 100 ALA   A CB    1 
ATOM   780   N  N     . ASN   A 1  101 ? 27.151  69.416  46.121  1.00 30.62  ? 101 ASN   A N     1 
ATOM   781   C  CA    . ASN   A 1  101 ? 26.762  68.946  47.454  1.00 29.42  ? 101 ASN   A CA    1 
ATOM   782   C  C     . ASN   A 1  101 ? 27.667  67.849  47.997  1.00 32.37  ? 101 ASN   A C     1 
ATOM   783   O  O     . ASN   A 1  101 ? 27.237  66.999  48.790  1.00 30.59  ? 101 ASN   A O     1 
ATOM   784   C  CB    . ASN   A 1  101 ? 25.325  68.448  47.457  1.00 23.89  ? 101 ASN   A CB    1 
ATOM   785   C  CG    . ASN   A 1  101 ? 24.358  69.516  47.086  1.00 27.85  ? 101 ASN   A CG    1 
ATOM   786   O  OD1   . ASN   A 1  101 ? 23.585  69.362  46.146  1.00 29.41  ? 101 ASN   A OD1   1 
ATOM   787   N  ND2   . ASN   A 1  101 ? 24.403  70.639  47.817  1.00 36.82  ? 101 ASN   A ND2   1 
ATOM   788   N  N     . ASN   A 1  102 ? 28.931  67.886  47.598  1.00 29.57  ? 102 ASN   A N     1 
ATOM   789   C  CA    . ASN   A 1  102 ? 29.921  66.898  47.999  1.00 33.85  ? 102 ASN   A CA    1 
ATOM   790   C  C     . ASN   A 1  102 ? 30.996  67.597  48.840  1.00 37.02  ? 102 ASN   A C     1 
ATOM   791   O  O     . ASN   A 1  102 ? 31.781  68.403  48.320  1.00 35.59  ? 102 ASN   A O     1 
ATOM   792   C  CB    . ASN   A 1  102 ? 30.495  66.244  46.742  1.00 28.24  ? 102 ASN   A CB    1 
ATOM   793   C  CG    . ASN   A 1  102 ? 31.496  65.172  47.045  1.00 31.07  ? 102 ASN   A CG    1 
ATOM   794   O  OD1   . ASN   A 1  102 ? 32.078  65.134  48.129  1.00 41.18  ? 102 ASN   A OD1   1 
ATOM   795   N  ND2   . ASN   A 1  102 ? 31.698  64.274  46.091  1.00 34.02  ? 102 ASN   A ND2   1 
ATOM   796   N  N     . TYR   A 1  103 ? 31.039  67.302  50.141  1.00 29.22  ? 103 TYR   A N     1 
ATOM   797   C  CA    . TYR   A 1  103 ? 32.069  67.921  50.979  1.00 37.38  ? 103 TYR   A CA    1 
ATOM   798   C  C     . TYR   A 1  103 ? 33.463  67.697  50.390  1.00 32.94  ? 103 TYR   A C     1 
ATOM   799   O  O     . TYR   A 1  103 ? 34.255  68.633  50.262  1.00 32.76  ? 103 TYR   A O     1 
ATOM   800   C  CB    . TYR   A 1  103 ? 31.997  67.388  52.422  1.00 26.57  ? 103 TYR   A CB    1 
ATOM   801   C  CG    . TYR   A 1  103 ? 33.205  67.755  53.259  1.00 33.68  ? 103 TYR   A CG    1 
ATOM   802   C  CD1   . TYR   A 1  103 ? 34.342  66.958  53.270  1.00 34.69  ? 103 TYR   A CD1   1 
ATOM   803   C  CD2   . TYR   A 1  103 ? 33.218  68.912  54.028  1.00 37.27  ? 103 TYR   A CD2   1 
ATOM   804   C  CE1   . TYR   A 1  103 ? 35.449  67.295  54.036  1.00 35.70  ? 103 TYR   A CE1   1 
ATOM   805   C  CE2   . TYR   A 1  103 ? 34.315  69.260  54.804  1.00 30.08  ? 103 TYR   A CE2   1 
ATOM   806   C  CZ    . TYR   A 1  103 ? 35.434  68.454  54.807  1.00 40.41  ? 103 TYR   A CZ    1 
ATOM   807   O  OH    . TYR   A 1  103 ? 36.541  68.808  55.574  1.00 35.50  ? 103 TYR   A OH    1 
ATOM   808   N  N     . ALA   A 1  104 ? 33.772  66.449  50.019  1.00 39.43  ? 104 ALA   A N     1 
ATOM   809   C  CA    . ALA   A 1  104 ? 35.125  66.091  49.597  1.00 36.09  ? 104 ALA   A CA    1 
ATOM   810   C  C     . ALA   A 1  104 ? 35.542  66.859  48.351  1.00 33.19  ? 104 ALA   A C     1 
ATOM   811   O  O     . ALA   A 1  104 ? 36.713  67.199  48.190  1.00 37.38  ? 104 ALA   A O     1 
ATOM   812   C  CB    . ALA   A 1  104 ? 35.213  64.582  49.363  1.00 32.24  ? 104 ALA   A CB    1 
ATOM   813   N  N     . ARG   A 1  105 ? 34.589  67.178  47.486  1.00 37.36  ? 105 ARG   A N     1 
ATOM   814   C  CA    . ARG   A 1  105 ? 34.858  67.939  46.279  1.00 28.40  ? 105 ARG   A CA    1 
ATOM   815   C  C     . ARG   A 1  105 ? 35.100  69.418  46.556  1.00 38.18  ? 105 ARG   A C     1 
ATOM   816   O  O     . ARG   A 1  105 ? 35.760  70.091  45.752  1.00 41.13  ? 105 ARG   A O     1 
ATOM   817   C  CB    . ARG   A 1  105 ? 33.680  67.730  45.341  1.00 29.07  ? 105 ARG   A CB    1 
ATOM   818   C  CG    . ARG   A 1  105 ? 33.736  68.395  44.021  1.00 29.84  ? 105 ARG   A CG    1 
ATOM   819   C  CD    . ARG   A 1  105 ? 32.522  67.975  43.225  1.00 28.33  ? 105 ARG   A CD    1 
ATOM   820   N  NE    . ARG   A 1  105 ? 32.516  68.630  41.928  1.00 41.22  ? 105 ARG   A NE    1 
ATOM   821   C  CZ    . ARG   A 1  105 ? 33.120  68.133  40.857  1.00 41.34  ? 105 ARG   A CZ    1 
ATOM   822   N  NH1   . ARG   A 1  105 ? 33.731  66.957  40.895  1.00 20.63  ? 105 ARG   A NH1   1 
ATOM   823   N  NH2   . ARG   A 1  105 ? 33.117  68.838  39.728  1.00 54.29  ? 105 ARG   A NH2   1 
ATOM   824   N  N     . GLY   A 1  106 ? 34.568  69.945  47.655  1.00 36.77  ? 106 GLY   A N     1 
ATOM   825   C  CA    . GLY   A 1  106 ? 34.819  71.326  48.019  1.00 33.92  ? 106 GLY   A CA    1 
ATOM   826   C  C     . GLY   A 1  106 ? 36.100  71.494  48.813  1.00 36.93  ? 106 GLY   A C     1 
ATOM   827   O  O     . GLY   A 1  106 ? 36.842  72.463  48.632  1.00 40.54  ? 106 GLY   A O     1 
ATOM   828   N  N     . HIS   A 1  107 ? 36.375  70.546  49.702  1.00 30.75  ? 107 HIS   A N     1 
ATOM   829   C  CA    . HIS   A 1  107 ? 37.631  70.568  50.437  1.00 40.38  ? 107 HIS   A CA    1 
ATOM   830   C  C     . HIS   A 1  107 ? 38.816  70.208  49.539  1.00 46.62  ? 107 HIS   A C     1 
ATOM   831   O  O     . HIS   A 1  107 ? 39.728  71.018  49.328  1.00 49.00  ? 107 HIS   A O     1 
ATOM   832   C  CB    . HIS   A 1  107 ? 37.560  69.605  51.617  1.00 34.01  ? 107 HIS   A CB    1 
ATOM   833   C  CG    . HIS   A 1  107 ? 38.646  69.827  52.614  1.00 39.57  ? 107 HIS   A CG    1 
ATOM   834   N  ND1   . HIS   A 1  107 ? 38.671  70.929  53.443  1.00 43.29  ? 107 HIS   A ND1   1 
ATOM   835   C  CD2   . HIS   A 1  107 ? 39.764  69.118  52.889  1.00 38.87  ? 107 HIS   A CD2   1 
ATOM   836   C  CE1   . HIS   A 1  107 ? 39.749  70.877  54.203  1.00 54.00  ? 107 HIS   A CE1   1 
ATOM   837   N  NE2   . HIS   A 1  107 ? 40.427  69.785  53.890  1.00 54.07  ? 107 HIS   A NE2   1 
ATOM   838   N  N     . TYR   A 1  108 ? 38.823  68.985  49.008  1.00 40.34  ? 108 TYR   A N     1 
ATOM   839   C  CA    . TYR   A 1  108 ? 40.004  68.426  48.368  1.00 32.59  ? 108 TYR   A CA    1 
ATOM   840   C  C     . TYR   A 1  108 ? 40.093  68.796  46.886  1.00 42.92  ? 108 TYR   A C     1 
ATOM   841   O  O     . TYR   A 1  108 ? 41.056  69.437  46.452  1.00 41.48  ? 108 TYR   A O     1 
ATOM   842   C  CB    . TYR   A 1  108 ? 40.015  66.910  48.568  1.00 21.50  ? 108 TYR   A CB    1 
ATOM   843   C  CG    . TYR   A 1  108 ? 40.117  66.467  50.015  1.00 28.06  ? 108 TYR   A CG    1 
ATOM   844   C  CD1   . TYR   A 1  108 ? 41.350  66.382  50.658  1.00 40.13  ? 108 TYR   A CD1   1 
ATOM   845   C  CD2   . TYR   A 1  108 ? 38.981  66.121  50.739  1.00 28.66  ? 108 TYR   A CD2   1 
ATOM   846   C  CE1   . TYR   A 1  108 ? 41.452  65.968  51.989  1.00 33.89  ? 108 TYR   A CE1   1 
ATOM   847   C  CE2   . TYR   A 1  108 ? 39.064  65.699  52.048  1.00 37.31  ? 108 TYR   A CE2   1 
ATOM   848   C  CZ    . TYR   A 1  108 ? 40.307  65.629  52.671  1.00 48.55  ? 108 TYR   A CZ    1 
ATOM   849   O  OH    . TYR   A 1  108 ? 40.391  65.215  53.980  1.00 44.41  ? 108 TYR   A OH    1 
ATOM   850   N  N     . THR   A 1  109 ? 39.107  68.402  46.094  1.00 43.75  ? 109 THR   A N     1 
ATOM   851   C  CA    . THR   A 1  109 ? 39.248  68.581  44.659  1.00 36.83  ? 109 THR   A CA    1 
ATOM   852   C  C     . THR   A 1  109 ? 39.260  70.047  44.260  1.00 43.75  ? 109 THR   A C     1 
ATOM   853   O  O     . THR   A 1  109 ? 40.317  70.585  43.932  1.00 54.50  ? 109 THR   A O     1 
ATOM   854   C  CB    . THR   A 1  109 ? 38.140  67.865  43.912  1.00 40.03  ? 109 THR   A CB    1 
ATOM   855   O  OG1   . THR   A 1  109 ? 38.196  66.464  44.219  1.00 48.82  ? 109 THR   A OG1   1 
ATOM   856   C  CG2   . THR   A 1  109 ? 38.313  68.096  42.427  1.00 26.87  ? 109 THR   A CG2   1 
ATOM   857   N  N     . ILE   A 1  110 ? 38.095  70.700  44.256  1.00 57.32  ? 110 ILE   A N     1 
ATOM   858   C  CA    . ILE   A 1  110 ? 38.017  72.057  43.716  1.00 57.53  ? 110 ILE   A CA    1 
ATOM   859   C  C     . ILE   A 1  110 ? 38.562  73.112  44.672  1.00 55.05  ? 110 ILE   A C     1 
ATOM   860   O  O     . ILE   A 1  110 ? 38.904  74.217  44.230  1.00 54.69  ? 110 ILE   A O     1 
ATOM   861   C  CB    . ILE   A 1  110 ? 36.576  72.433  43.340  1.00 46.10  ? 110 ILE   A CB    1 
ATOM   862   C  CG1   . ILE   A 1  110 ? 36.018  71.442  42.314  1.00 48.51  ? 110 ILE   A CG1   1 
ATOM   863   C  CG2   . ILE   A 1  110 ? 36.548  73.854  42.795  1.00 45.16  ? 110 ILE   A CG2   1 
ATOM   864   C  CD1   . ILE   A 1  110 ? 34.653  71.823  41.757  1.00 47.53  ? 110 ILE   A CD1   1 
ATOM   865   N  N     . GLY   A 1  111 ? 38.651  72.809  45.965  1.00 51.83  ? 111 GLY   A N     1 
ATOM   866   C  CA    . GLY   A 1  111 ? 39.091  73.785  46.939  1.00 50.75  ? 111 GLY   A CA    1 
ATOM   867   C  C     . GLY   A 1  111 ? 40.513  74.203  46.670  1.00 58.42  ? 111 GLY   A C     1 
ATOM   868   O  O     . GLY   A 1  111 ? 40.789  75.382  46.424  1.00 58.84  ? 111 GLY   A O     1 
ATOM   869   N  N     . LYS   A 1  112 ? 41.416  73.219  46.706  1.00 61.65  ? 112 LYS   A N     1 
ATOM   870   C  CA    . LYS   A 1  112 ? 42.822  73.379  46.356  1.00 54.20  ? 112 LYS   A CA    1 
ATOM   871   C  C     . LYS   A 1  112 ? 43.028  74.351  45.196  1.00 52.98  ? 112 LYS   A C     1 
ATOM   872   O  O     . LYS   A 1  112 ? 43.947  75.174  45.230  1.00 60.93  ? 112 LYS   A O     1 
ATOM   873   C  CB    . LYS   A 1  112 ? 43.413  72.008  46.030  1.00 50.55  ? 112 LYS   A CB    1 
ATOM   874   C  CG    . LYS   A 1  112 ? 44.898  71.987  45.723  1.00 53.27  ? 112 LYS   A CG    1 
ATOM   875   C  CD    . LYS   A 1  112 ? 45.433  70.557  45.730  1.00 49.48  ? 112 LYS   A CD    1 
ATOM   876   C  CE    . LYS   A 1  112 ? 46.783  70.461  45.023  1.00 62.98  ? 112 LYS   A CE    1 
ATOM   877   N  NZ    . LYS   A 1  112 ? 46.750  71.063  43.657  1.00 47.56  ? 112 LYS   A NZ    1 
ATOM   878   N  N     . GLU   A 1  113 ? 42.173  74.299  44.181  1.00 53.89  ? 113 GLU   A N     1 
ATOM   879   C  CA    . GLU   A 1  113 ? 42.355  75.163  43.021  1.00 51.74  ? 113 GLU   A CA    1 
ATOM   880   C  C     . GLU   A 1  113 ? 41.886  76.593  43.264  1.00 53.95  ? 113 GLU   A C     1 
ATOM   881   O  O     . GLU   A 1  113 ? 41.736  77.350  42.299  1.00 66.65  ? 113 GLU   A O     1 
ATOM   882   C  CB    . GLU   A 1  113 ? 41.646  74.553  41.791  1.00 50.04  ? 113 GLU   A CB    1 
ATOM   883   C  CG    . GLU   A 1  113 ? 40.342  75.233  41.334  1.00 62.40  ? 113 GLU   A CG    1 
ATOM   884   C  CD    . GLU   A 1  113 ? 39.658  74.518  40.144  1.00 74.80  ? 113 GLU   A CD    1 
ATOM   885   O  OE1   . GLU   A 1  113 ? 39.792  73.272  40.015  1.00 62.11  ? 113 GLU   A OE1   1 
ATOM   886   O  OE2   . GLU   A 1  113 ? 38.975  75.204  39.340  1.00 60.90  ? 113 GLU   A OE2   1 
ATOM   887   N  N     . ILE   A 1  114 ? 41.665  77.000  44.513  1.00 52.61  ? 114 ILE   A N     1 
ATOM   888   C  CA    . ILE   A 1  114 ? 41.120  78.339  44.744  1.00 56.26  ? 114 ILE   A CA    1 
ATOM   889   C  C     . ILE   A 1  114 ? 41.516  78.892  46.111  1.00 51.35  ? 114 ILE   A C     1 
ATOM   890   O  O     . ILE   A 1  114 ? 41.436  80.105  46.341  1.00 46.97  ? 114 ILE   A O     1 
ATOM   891   C  CB    . ILE   A 1  114 ? 39.590  78.339  44.575  1.00 54.86  ? 114 ILE   A CB    1 
ATOM   892   C  CG1   . ILE   A 1  114 ? 39.085  79.736  44.212  1.00 42.61  ? 114 ILE   A CG1   1 
ATOM   893   C  CG2   . ILE   A 1  114 ? 38.900  77.798  45.838  1.00 52.72  ? 114 ILE   A CG2   1 
ATOM   894   C  CD1   . ILE   A 1  114 ? 37.593  79.771  43.967  1.00 31.69  ? 114 ILE   A CD1   1 
ATOM   895   N  N     . ILE   A 1  115 ? 41.968  78.016  47.015  1.00 50.14  ? 115 ILE   A N     1 
ATOM   896   C  CA    . ILE   A 1  115 ? 42.344  78.448  48.362  1.00 55.41  ? 115 ILE   A CA    1 
ATOM   897   C  C     . ILE   A 1  115 ? 43.292  79.646  48.305  1.00 58.19  ? 115 ILE   A C     1 
ATOM   898   O  O     . ILE   A 1  115 ? 43.089  80.651  48.997  1.00 61.60  ? 115 ILE   A O     1 
ATOM   899   C  CB    . ILE   A 1  115 ? 42.958  77.280  49.153  1.00 47.79  ? 115 ILE   A CB    1 
ATOM   900   C  CG1   . ILE   A 1  115 ? 43.068  77.639  50.635  1.00 50.01  ? 115 ILE   A CG1   1 
ATOM   901   C  CG2   . ILE   A 1  115 ? 44.319  76.961  48.628  1.00 49.10  ? 115 ILE   A CG2   1 
ATOM   902   C  CD1   . ILE   A 1  115 ? 41.788  78.149  51.246  1.00 43.42  ? 115 ILE   A CD1   1 
ATOM   903   N  N     . ASP   A 1  116 ? 44.332  79.569  47.470  1.00 58.98  ? 116 ASP   A N     1 
ATOM   904   C  CA    . ASP   A 1  116 ? 45.320  80.646  47.448  1.00 54.01  ? 116 ASP   A CA    1 
ATOM   905   C  C     . ASP   A 1  116 ? 44.713  81.957  46.946  1.00 52.74  ? 116 ASP   A C     1 
ATOM   906   O  O     . ASP   A 1  116 ? 44.933  83.019  47.543  1.00 49.83  ? 116 ASP   A O     1 
ATOM   907   C  CB    . ASP   A 1  116 ? 46.532  80.248  46.604  1.00 52.70  ? 116 ASP   A CB    1 
ATOM   908   C  CG    . ASP   A 1  116 ? 47.318  79.096  47.205  1.00 50.10  ? 116 ASP   A CG    1 
ATOM   909   O  OD1   . ASP   A 1  116 ? 47.389  78.995  48.446  1.00 59.84  ? 116 ASP   A OD1   1 
ATOM   910   O  OD2   . ASP   A 1  116 ? 47.877  78.289  46.432  1.00 60.80  ? 116 ASP   A OD2   1 
ATOM   911   N  N     . LEU   A 1  117 ? 43.948  81.920  45.852  1.00 47.45  ? 117 LEU   A N     1 
ATOM   912   C  CA    . LEU   A 1  117 ? 43.383  83.179  45.373  1.00 43.62  ? 117 LEU   A CA    1 
ATOM   913   C  C     . LEU   A 1  117 ? 42.503  83.825  46.439  1.00 62.91  ? 117 LEU   A C     1 
ATOM   914   O  O     . LEU   A 1  117 ? 42.423  85.062  46.513  1.00 58.35  ? 117 LEU   A O     1 
ATOM   915   C  CB    . LEU   A 1  117 ? 42.598  82.963  44.082  1.00 29.56  ? 117 LEU   A CB    1 
ATOM   916   C  CG    . LEU   A 1  117 ? 41.732  84.147  43.625  1.00 46.99  ? 117 LEU   A CG    1 
ATOM   917   C  CD1   . LEU   A 1  117 ? 42.364  84.978  42.524  1.00 53.52  ? 117 LEU   A CD1   1 
ATOM   918   C  CD2   . LEU   A 1  117 ? 40.377  83.669  43.183  1.00 51.81  ? 117 LEU   A CD2   1 
ATOM   919   N  N     . VAL   A 1  118 ? 41.857  83.003  47.282  1.00 60.80  ? 118 VAL   A N     1 
ATOM   920   C  CA    . VAL   A 1  118 ? 40.948  83.511  48.310  1.00 53.03  ? 118 VAL   A CA    1 
ATOM   921   C  C     . VAL   A 1  118 ? 41.734  84.082  49.476  1.00 45.34  ? 118 VAL   A C     1 
ATOM   922   O  O     . VAL   A 1  118 ? 41.441  85.182  49.953  1.00 44.40  ? 118 VAL   A O     1 
ATOM   923   C  CB    . VAL   A 1  118 ? 39.959  82.409  48.762  1.00 48.83  ? 118 VAL   A CB    1 
ATOM   924   C  CG1   . VAL   A 1  118 ? 39.903  82.273  50.289  1.00 47.73  ? 118 VAL   A CG1   1 
ATOM   925   C  CG2   . VAL   A 1  118 ? 38.564  82.701  48.228  1.00 39.92  ? 118 VAL   A CG2   1 
ATOM   926   N  N     . LEU   A 1  119 ? 42.741  83.342  49.948  1.00 51.60  ? 119 LEU   A N     1 
ATOM   927   C  CA    . LEU   A 1  119 ? 43.645  83.865  50.969  1.00 49.15  ? 119 LEU   A CA    1 
ATOM   928   C  C     . LEU   A 1  119 ? 44.287  85.177  50.526  1.00 57.78  ? 119 LEU   A C     1 
ATOM   929   O  O     . LEU   A 1  119 ? 44.456  86.102  51.332  1.00 59.39  ? 119 LEU   A O     1 
ATOM   930   C  CB    . LEU   A 1  119 ? 44.714  82.828  51.284  1.00 42.20  ? 119 LEU   A CB    1 
ATOM   931   C  CG    . LEU   A 1  119 ? 44.226  81.632  52.081  1.00 44.66  ? 119 LEU   A CG    1 
ATOM   932   C  CD1   . LEU   A 1  119 ? 45.378  80.702  52.349  1.00 50.60  ? 119 LEU   A CD1   1 
ATOM   933   C  CD2   . LEU   A 1  119 ? 43.614  82.114  53.374  1.00 37.62  ? 119 LEU   A CD2   1 
ATOM   934   N  N     . ASP   A 1  120 ? 44.662  85.270  49.249  1.00 58.71  ? 120 ASP   A N     1 
ATOM   935   C  CA    . ASP   A 1  120 ? 45.166  86.512  48.684  1.00 53.34  ? 120 ASP   A CA    1 
ATOM   936   C  C     . ASP   A 1  120 ? 44.159  87.617  48.940  1.00 58.51  ? 120 ASP   A C     1 
ATOM   937   O  O     . ASP   A 1  120 ? 44.434  88.547  49.701  1.00 70.28  ? 120 ASP   A O     1 
ATOM   938   C  CB    . ASP   A 1  120 ? 45.417  86.360  47.183  1.00 70.72  ? 120 ASP   A CB    1 
ATOM   939   C  CG    . ASP   A 1  120 ? 46.738  86.973  46.736  1.00 86.58  ? 120 ASP   A CG    1 
ATOM   940   O  OD1   . ASP   A 1  120 ? 47.794  86.565  47.283  1.00 90.56  ? 120 ASP   A OD1   1 
ATOM   941   O  OD2   . ASP   A 1  120 ? 46.714  87.842  45.825  1.00 82.31  ? 120 ASP   A OD2   1 
ATOM   942   N  N     . ARG   A 1  121 ? 42.980  87.506  48.321  1.00 60.15  ? 121 ARG   A N     1 
ATOM   943   C  CA    . ARG   A 1  121 ? 41.962  88.549  48.433  1.00 54.71  ? 121 ARG   A CA    1 
ATOM   944   C  C     . ARG   A 1  121 ? 41.625  88.885  49.882  1.00 55.10  ? 121 ARG   A C     1 
ATOM   945   O  O     . ARG   A 1  121 ? 41.195  90.006  50.181  1.00 52.24  ? 121 ARG   A O     1 
ATOM   946   C  CB    . ARG   A 1  121 ? 40.726  88.105  47.672  1.00 51.84  ? 121 ARG   A CB    1 
ATOM   947   C  CG    . ARG   A 1  121 ? 41.025  87.812  46.205  1.00 61.13  ? 121 ARG   A CG    1 
ATOM   948   C  CD    . ARG   A 1  121 ? 40.876  89.072  45.352  1.00 67.25  ? 121 ARG   A CD    1 
ATOM   949   N  NE    . ARG   A 1  121 ? 41.562  88.971  44.070  1.00 72.95  ? 121 ARG   A NE    1 
ATOM   950   C  CZ    . ARG   A 1  121 ? 40.962  88.753  42.907  1.00 81.87  ? 121 ARG   A CZ    1 
ATOM   951   N  NH1   . ARG   A 1  121 ? 39.648  88.601  42.823  1.00 77.78  ? 121 ARG   A NH1   1 
ATOM   952   N  NH2   . ARG   A 1  121 ? 41.698  88.690  41.801  1.00 85.24  ? 121 ARG   A NH2   1 
ATOM   953   N  N     . ILE   A 1  122 ? 41.833  87.939  50.796  1.00 52.57  ? 122 ILE   A N     1 
ATOM   954   C  CA    . ILE   A 1  122 ? 41.612  88.198  52.215  1.00 56.05  ? 122 ILE   A CA    1 
ATOM   955   C  C     . ILE   A 1  122 ? 42.735  89.065  52.782  1.00 61.93  ? 122 ILE   A C     1 
ATOM   956   O  O     . ILE   A 1  122 ? 42.486  90.049  53.493  1.00 53.37  ? 122 ILE   A O     1 
ATOM   957   C  CB    . ILE   A 1  122 ? 41.488  86.866  52.981  1.00 56.28  ? 122 ILE   A CB    1 
ATOM   958   C  CG1   . ILE   A 1  122 ? 40.105  86.229  52.773  1.00 47.36  ? 122 ILE   A CG1   1 
ATOM   959   C  CG2   . ILE   A 1  122 ? 41.860  87.050  54.461  1.00 37.67  ? 122 ILE   A CG2   1 
ATOM   960   C  CD1   . ILE   A 1  122 ? 39.992  84.822  53.377  1.00 41.96  ? 122 ILE   A CD1   1 
ATOM   961   N  N     . ARG   A 1  123 ? 43.993  88.700  52.497  1.00 62.50  ? 123 ARG   A N     1 
ATOM   962   C  CA    . ARG   A 1  123 ? 45.112  89.485  53.014  1.00 61.36  ? 123 ARG   A CA    1 
ATOM   963   C  C     . ARG   A 1  123 ? 45.097  90.910  52.484  1.00 56.85  ? 123 ARG   A C     1 
ATOM   964   O  O     . ARG   A 1  123 ? 45.545  91.830  53.173  1.00 59.89  ? 123 ARG   A O     1 
ATOM   965   C  CB    . ARG   A 1  123 ? 46.443  88.833  52.676  1.00 59.26  ? 123 ARG   A CB    1 
ATOM   966   C  CG    . ARG   A 1  123 ? 47.597  89.695  53.104  1.00 53.96  ? 123 ARG   A CG    1 
ATOM   967   C  CD    . ARG   A 1  123 ? 48.846  88.889  53.265  1.00 65.62  ? 123 ARG   A CD    1 
ATOM   968   N  NE    . ARG   A 1  123 ? 48.708  87.851  54.281  1.00 66.26  ? 123 ARG   A NE    1 
ATOM   969   C  CZ    . ARG   A 1  123 ? 48.565  88.089  55.577  1.00 65.86  ? 123 ARG   A CZ    1 
ATOM   970   N  NH1   . ARG   A 1  123 ? 48.455  89.323  56.044  1.00 73.44  ? 123 ARG   A NH1   1 
ATOM   971   N  NH2   . ARG   A 1  123 ? 48.525  87.062  56.427  1.00 56.58  ? 123 ARG   A NH2   1 
ATOM   972   N  N     . LYS   A 1  124 ? 44.595  91.117  51.269  1.00 53.54  ? 124 LYS   A N     1 
ATOM   973   C  CA    . LYS   A 1  124 ? 44.396  92.476  50.789  1.00 50.81  ? 124 LYS   A CA    1 
ATOM   974   C  C     . LYS   A 1  124 ? 43.546  93.285  51.771  1.00 59.08  ? 124 LYS   A C     1 
ATOM   975   O  O     . LYS   A 1  124 ? 43.781  94.483  51.968  1.00 61.78  ? 124 LYS   A O     1 
ATOM   976   C  CB    . LYS   A 1  124 ? 43.764  92.442  49.395  1.00 50.81  ? 124 LYS   A CB    1 
ATOM   977   C  CG    . LYS   A 1  124 ? 43.578  93.809  48.756  1.00 65.07  ? 124 LYS   A CG    1 
ATOM   978   C  CD    . LYS   A 1  124 ? 42.588  93.757  47.596  1.00 76.60  ? 124 LYS   A CD    1 
ATOM   979   C  CE    . LYS   A 1  124 ? 42.389  95.125  46.960  1.00 73.65  ? 124 LYS   A CE    1 
ATOM   980   N  NZ    . LYS   A 1  124 ? 41.643  95.002  45.687  1.00 63.98  ? 124 LYS   A NZ    1 
ATOM   981   N  N     . LEU   A 1  125 ? 42.559  92.644  52.411  1.00 64.69  ? 125 LEU   A N     1 
ATOM   982   C  CA    . LEU   A 1  125 ? 41.717  93.349  53.376  1.00 56.79  ? 125 LEU   A CA    1 
ATOM   983   C  C     . LEU   A 1  125 ? 42.440  93.556  54.699  1.00 54.43  ? 125 LEU   A C     1 
ATOM   984   O  O     . LEU   A 1  125 ? 42.284  94.603  55.338  1.00 57.31  ? 125 LEU   A O     1 
ATOM   985   C  CB    . LEU   A 1  125 ? 40.404  92.594  53.617  1.00 50.13  ? 125 LEU   A CB    1 
ATOM   986   C  CG    . LEU   A 1  125 ? 39.246  92.747  52.622  1.00 52.11  ? 125 LEU   A CG    1 
ATOM   987   C  CD1   . LEU   A 1  125 ? 37.987  92.120  53.196  1.00 51.27  ? 125 LEU   A CD1   1 
ATOM   988   C  CD2   . LEU   A 1  125 ? 38.987  94.191  52.254  1.00 48.26  ? 125 LEU   A CD2   1 
ATOM   989   N  N     . ALA   A 1  126 ? 43.215  92.568  55.140  1.00 45.91  ? 126 ALA   A N     1 
ATOM   990   C  CA    . ALA   A 1  126 ? 43.954  92.734  56.383  1.00 48.36  ? 126 ALA   A CA    1 
ATOM   991   C  C     . ALA   A 1  126 ? 44.936  93.901  56.288  1.00 62.00  ? 126 ALA   A C     1 
ATOM   992   O  O     . ALA   A 1  126 ? 45.095  94.673  57.243  1.00 57.94  ? 126 ALA   A O     1 
ATOM   993   C  CB    . ALA   A 1  126 ? 44.675  91.433  56.729  1.00 45.89  ? 126 ALA   A CB    1 
ATOM   994   N  N     . ASP   A 1  127 ? 45.581  94.062  55.126  1.00 63.74  ? 127 ASP   A N     1 
ATOM   995   C  CA    . ASP   A 1  127 ? 46.596  95.096  54.953  1.00 57.66  ? 127 ASP   A CA    1 
ATOM   996   C  C     . ASP   A 1  127 ? 46.049  96.497  55.189  1.00 61.68  ? 127 ASP   A C     1 
ATOM   997   O  O     . ASP   A 1  127 ? 46.782  97.362  55.683  1.00 70.40  ? 127 ASP   A O     1 
ATOM   998   C  CB    . ASP   A 1  127 ? 47.199  95.005  53.558  1.00 54.27  ? 127 ASP   A CB    1 
ATOM   999   C  CG    . ASP   A 1  127 ? 48.089  93.806  53.396  1.00 57.53  ? 127 ASP   A CG    1 
ATOM   1000  O  OD1   . ASP   A 1  127 ? 48.303  93.089  54.398  1.00 61.98  ? 127 ASP   A OD1   1 
ATOM   1001  O  OD2   . ASP   A 1  127 ? 48.568  93.575  52.267  1.00 61.03  ? 127 ASP   A OD2   1 
ATOM   1002  N  N     . GLN   A 1  128 ? 44.787  96.755  54.835  1.00 58.70  ? 128 GLN   A N     1 
ATOM   1003  C  CA    . GLN   A 1  128 ? 44.165  98.052  55.120  1.00 58.06  ? 128 GLN   A CA    1 
ATOM   1004  C  C     . GLN   A 1  128 ? 43.425  98.066  56.456  1.00 58.22  ? 128 GLN   A C     1 
ATOM   1005  O  O     . GLN   A 1  128 ? 42.384  98.723  56.595  1.00 55.03  ? 128 GLN   A O     1 
ATOM   1006  C  CB    . GLN   A 1  128 ? 43.243  98.459  53.973  1.00 62.75  ? 128 GLN   A CB    1 
ATOM   1007  C  CG    . GLN   A 1  128 ? 42.187  97.445  53.567  1.00 61.36  ? 128 GLN   A CG    1 
ATOM   1008  C  CD    . GLN   A 1  128 ? 41.034  98.075  52.761  1.00 76.77  ? 128 GLN   A CD    1 
ATOM   1009  O  OE1   . GLN   A 1  128 ? 40.991  99.294  52.543  1.00 68.12  ? 128 GLN   A OE1   1 
ATOM   1010  N  NE2   . GLN   A 1  128 ? 40.090  97.239  52.329  1.00 66.48  ? 128 GLN   A NE2   1 
ATOM   1011  N  N     . CYS   A 1  129 ? 43.969  97.362  57.454  1.00 51.58  ? 129 CYS   A N     1 
ATOM   1012  C  CA    . CYS   A 1  129 ? 43.376  97.212  58.782  1.00 57.70  ? 129 CYS   A CA    1 
ATOM   1013  C  C     . CYS   A 1  129 ? 44.412  97.604  59.827  1.00 64.48  ? 129 CYS   A C     1 
ATOM   1014  O  O     . CYS   A 1  129 ? 45.461  96.954  59.930  1.00 71.15  ? 129 CYS   A O     1 
ATOM   1015  C  CB    . CYS   A 1  129 ? 42.919  95.762  59.033  1.00 59.11  ? 129 CYS   A CB    1 
ATOM   1016  S  SG    . CYS   A 1  129 ? 41.423  95.221  58.165  1.00 61.69  ? 129 CYS   A SG    1 
ATOM   1017  N  N     . THR   A 1  130 ? 44.110  98.634  60.626  1.00 54.41  ? 130 THR   A N     1 
ATOM   1018  C  CA    . THR   A 1  130 ? 45.069  99.086  61.636  1.00 43.01  ? 130 THR   A CA    1 
ATOM   1019  C  C     . THR   A 1  130 ? 45.306  98.011  62.693  1.00 43.92  ? 130 THR   A C     1 
ATOM   1020  O  O     . THR   A 1  130 ? 46.452  97.676  63.003  1.00 50.62  ? 130 THR   A O     1 
ATOM   1021  C  CB    . THR   A 1  130 ? 44.598  100.394 62.284  1.00 42.34  ? 130 THR   A CB    1 
ATOM   1022  O  OG1   . THR   A 1  130 ? 43.515  100.146 63.202  1.00 55.43  ? 130 THR   A OG1   1 
ATOM   1023  C  CG2   . THR   A 1  130 ? 44.129  101.380 61.221  1.00 38.15  ? 130 THR   A CG2   1 
ATOM   1024  N  N     . GLY   A 1  131 ? 44.235  97.454  63.257  1.00 51.89  ? 131 GLY   A N     1 
ATOM   1025  C  CA    . GLY   A 1  131 ? 44.365  96.410  64.258  1.00 43.24  ? 131 GLY   A CA    1 
ATOM   1026  C  C     . GLY   A 1  131 ? 43.327  95.303  64.156  1.00 58.16  ? 131 GLY   A C     1 
ATOM   1027  O  O     . GLY   A 1  131 ? 42.653  94.981  65.149  1.00 52.29  ? 131 GLY   A O     1 
ATOM   1028  N  N     . LEU   A 1  132 ? 43.198  94.718  62.953  1.00 48.41  ? 132 LEU   A N     1 
ATOM   1029  C  CA    . LEU   A 1  132 ? 42.366  93.544  62.684  1.00 48.50  ? 132 LEU   A CA    1 
ATOM   1030  C  C     . LEU   A 1  132 ? 42.209  92.613  63.881  1.00 51.43  ? 132 LEU   A C     1 
ATOM   1031  O  O     . LEU   A 1  132 ? 43.195  92.223  64.512  1.00 56.54  ? 132 LEU   A O     1 
ATOM   1032  C  CB    . LEU   A 1  132 ? 42.954  92.746  61.522  1.00 60.36  ? 132 LEU   A CB    1 
ATOM   1033  C  CG    . LEU   A 1  132 ? 42.268  91.402  61.275  1.00 52.76  ? 132 LEU   A CG    1 
ATOM   1034  C  CD1   . LEU   A 1  132 ? 40.983  91.616  60.473  1.00 46.41  ? 132 LEU   A CD1   1 
ATOM   1035  C  CD2   . LEU   A 1  132 ? 43.210  90.444  60.587  1.00 30.16  ? 132 LEU   A CD2   1 
ATOM   1036  N  N     . GLN   A 1  133 ? 40.981  92.217  64.197  1.00 50.22  ? 133 GLN   A N     1 
ATOM   1037  C  CA    . GLN   A 1  133 ? 40.788  91.361  65.355  1.00 53.98  ? 133 GLN   A CA    1 
ATOM   1038  C  C     . GLN   A 1  133 ? 40.362  89.944  65.023  1.00 49.70  ? 133 GLN   A C     1 
ATOM   1039  O  O     . GLN   A 1  133 ? 40.577  89.048  65.845  1.00 43.29  ? 133 GLN   A O     1 
ATOM   1040  C  CB    . GLN   A 1  133 ? 39.762  91.973  66.316  1.00 56.08  ? 133 GLN   A CB    1 
ATOM   1041  C  CG    . GLN   A 1  133 ? 38.516  92.504  65.667  1.00 51.11  ? 133 GLN   A CG    1 
ATOM   1042  C  CD    . GLN   A 1  133 ? 37.613  93.160  66.688  1.00 53.17  ? 133 GLN   A CD    1 
ATOM   1043  O  OE1   . GLN   A 1  133 ? 37.378  92.612  67.763  1.00 56.59  ? 133 GLN   A OE1   1 
ATOM   1044  N  NE2   . GLN   A 1  133 ? 37.120  94.350  66.369  1.00 55.15  ? 133 GLN   A NE2   1 
ATOM   1045  N  N     . GLY   A 1  134 ? 39.772  89.709  63.862  1.00 55.80  ? 134 GLY   A N     1 
ATOM   1046  C  CA    . GLY   A 1  134 ? 39.336  88.367  63.543  1.00 54.07  ? 134 GLY   A CA    1 
ATOM   1047  C  C     . GLY   A 1  134 ? 38.296  88.346  62.441  1.00 49.15  ? 134 GLY   A C     1 
ATOM   1048  O  O     . GLY   A 1  134 ? 38.016  89.358  61.783  1.00 45.31  ? 134 GLY   A O     1 
ATOM   1049  N  N     . PHE   A 1  135 ? 37.721  87.158  62.269  1.00 45.27  ? 135 PHE   A N     1 
ATOM   1050  C  CA    . PHE   A 1  135 ? 36.898  86.850  61.111  1.00 45.69  ? 135 PHE   A CA    1 
ATOM   1051  C  C     . PHE   A 1  135 ? 35.520  86.378  61.541  1.00 38.57  ? 135 PHE   A C     1 
ATOM   1052  O  O     . PHE   A 1  135 ? 35.369  85.688  62.556  1.00 33.94  ? 135 PHE   A O     1 
ATOM   1053  C  CB    . PHE   A 1  135 ? 37.571  85.780  60.225  1.00 34.09  ? 135 PHE   A CB    1 
ATOM   1054  C  CG    . PHE   A 1  135 ? 38.955  86.149  59.788  1.00 36.00  ? 135 PHE   A CG    1 
ATOM   1055  C  CD1   . PHE   A 1  135 ? 39.155  87.203  58.894  1.00 45.52  ? 135 PHE   A CD1   1 
ATOM   1056  C  CD2   . PHE   A 1  135 ? 40.062  85.472  60.287  1.00 41.16  ? 135 PHE   A CD2   1 
ATOM   1057  C  CE1   . PHE   A 1  135 ? 40.438  87.569  58.494  1.00 43.01  ? 135 PHE   A CE1   1 
ATOM   1058  C  CE2   . PHE   A 1  135 ? 41.351  85.825  59.891  1.00 44.94  ? 135 PHE   A CE2   1 
ATOM   1059  C  CZ    . PHE   A 1  135 ? 41.537  86.874  58.985  1.00 40.22  ? 135 PHE   A CZ    1 
ATOM   1060  N  N     . LEU   A 1  136 ? 34.530  86.776  60.758  1.00 35.24  ? 136 LEU   A N     1 
ATOM   1061  C  CA    A LEU   A 1  136 ? 33.161  86.298  60.880  1.00 37.11  ? 136 LEU   A CA    1 
ATOM   1062  C  CA    B LEU   A 1  136 ? 33.160  86.291  60.886  0.00 37.27  ? 136 LEU   A CA    1 
ATOM   1063  C  C     . LEU   A 1  136 ? 32.850  85.500  59.622  1.00 36.76  ? 136 LEU   A C     1 
ATOM   1064  O  O     . LEU   A 1  136 ? 32.768  86.070  58.530  1.00 42.74  ? 136 LEU   A O     1 
ATOM   1065  C  CB    A LEU   A 1  136 ? 32.195  87.469  61.049  1.00 37.87  ? 136 LEU   A CB    1 
ATOM   1066  C  CB    B LEU   A 1  136 ? 32.176  87.443  61.078  0.00 38.03  ? 136 LEU   A CB    1 
ATOM   1067  C  CG    A LEU   A 1  136 ? 32.179  88.215  62.387  1.00 38.21  ? 136 LEU   A CG    1 
ATOM   1068  C  CG    B LEU   A 1  136 ? 32.275  88.252  62.375  0.00 38.33  ? 136 LEU   A CG    1 
ATOM   1069  C  CD1   A LEU   A 1  136 ? 33.429  89.037  62.595  1.00 37.05  ? 136 LEU   A CD1   1 
ATOM   1070  C  CD1   B LEU   A 1  136 ? 33.568  89.054  62.433  0.00 37.76  ? 136 LEU   A CD1   1 
ATOM   1071  C  CD2   A LEU   A 1  136 ? 30.969  89.120  62.412  1.00 44.39  ? 136 LEU   A CD2   1 
ATOM   1072  C  CD2   B LEU   A 1  136 ? 31.067  89.165  62.530  0.00 43.84  ? 136 LEU   A CD2   1 
ATOM   1073  N  N     . VAL   A 1  137 ? 32.689  84.189  59.762  1.00 39.52  ? 137 VAL   A N     1 
ATOM   1074  C  CA    . VAL   A 1  137 ? 32.557  83.297  58.608  1.00 37.84  ? 137 VAL   A CA    1 
ATOM   1075  C  C     . VAL   A 1  137 ? 31.137  82.748  58.558  1.00 39.85  ? 137 VAL   A C     1 
ATOM   1076  O  O     . VAL   A 1  137 ? 30.698  82.066  59.495  1.00 31.99  ? 137 VAL   A O     1 
ATOM   1077  C  CB    . VAL   A 1  137 ? 33.594  82.167  58.664  1.00 37.62  ? 137 VAL   A CB    1 
ATOM   1078  C  CG1   . VAL   A 1  137 ? 33.427  81.237  57.480  1.00 27.31  ? 137 VAL   A CG1   1 
ATOM   1079  C  CG2   . VAL   A 1  137 ? 34.990  82.774  58.684  1.00 36.36  ? 137 VAL   A CG2   1 
ATOM   1080  N  N     . PHE   A 1  138 ? 30.441  83.040  57.447  1.00 44.21  ? 138 PHE   A N     1 
ATOM   1081  C  CA    . PHE   A 1  138 ? 29.035  82.714  57.190  1.00 34.25  ? 138 PHE   A CA    1 
ATOM   1082  C  C     . PHE   A 1  138 ? 28.947  81.577  56.173  1.00 42.35  ? 138 PHE   A C     1 
ATOM   1083  O  O     . PHE   A 1  138 ? 29.376  81.732  55.020  1.00 39.41  ? 138 PHE   A O     1 
ATOM   1084  C  CB    . PHE   A 1  138 ? 28.284  83.918  56.618  1.00 32.01  ? 138 PHE   A CB    1 
ATOM   1085  C  CG    . PHE   A 1  138 ? 28.118  85.060  57.559  1.00 42.65  ? 138 PHE   A CG    1 
ATOM   1086  C  CD1   . PHE   A 1  138 ? 29.201  85.828  57.947  1.00 40.45  ? 138 PHE   A CD1   1 
ATOM   1087  C  CD2   . PHE   A 1  138 ? 26.856  85.415  58.013  1.00 39.31  ? 138 PHE   A CD2   1 
ATOM   1088  C  CE1   . PHE   A 1  138 ? 29.032  86.902  58.798  1.00 37.79  ? 138 PHE   A CE1   1 
ATOM   1089  C  CE2   . PHE   A 1  138 ? 26.690  86.488  58.874  1.00 41.16  ? 138 PHE   A CE2   1 
ATOM   1090  C  CZ    . PHE   A 1  138 ? 27.777  87.232  59.262  1.00 38.18  ? 138 PHE   A CZ    1 
ATOM   1091  N  N     . HIS   A 1  139 ? 28.329  80.468  56.562  1.00 40.50  ? 139 HIS   A N     1 
ATOM   1092  C  CA    . HIS   A 1  139 ? 28.284  79.316  55.673  1.00 36.37  ? 139 HIS   A CA    1 
ATOM   1093  C  C     . HIS   A 1  139 ? 27.205  78.340  56.127  1.00 34.39  ? 139 HIS   A C     1 
ATOM   1094  O  O     . HIS   A 1  139 ? 26.774  78.343  57.285  1.00 31.39  ? 139 HIS   A O     1 
ATOM   1095  C  CB    . HIS   A 1  139 ? 29.645  78.610  55.629  1.00 32.15  ? 139 HIS   A CB    1 
ATOM   1096  C  CG    . HIS   A 1  139 ? 30.012  77.933  56.914  1.00 28.62  ? 139 HIS   A CG    1 
ATOM   1097  N  ND1   . HIS   A 1  139 ? 29.840  76.583  57.119  1.00 23.60  ? 139 HIS   A ND1   1 
ATOM   1098  C  CD2   . HIS   A 1  139 ? 30.535  78.421  58.064  1.00 30.82  ? 139 HIS   A CD2   1 
ATOM   1099  C  CE1   . HIS   A 1  139 ? 30.256  76.261  58.329  1.00 25.42  ? 139 HIS   A CE1   1 
ATOM   1100  N  NE2   . HIS   A 1  139 ? 30.689  77.359  58.922  1.00 27.22  ? 139 HIS   A NE2   1 
ATOM   1101  N  N     . SER   A 1  140 ? 26.797  77.484  55.193  1.00 31.93  ? 140 SER   A N     1 
ATOM   1102  C  CA    . SER   A 1  140 ? 25.952  76.338  55.492  1.00 33.42  ? 140 SER   A CA    1 
ATOM   1103  C  C     . SER   A 1  140 ? 26.821  75.132  55.826  1.00 26.57  ? 140 SER   A C     1 
ATOM   1104  O  O     . SER   A 1  140 ? 27.965  75.040  55.384  1.00 26.56  ? 140 SER   A O     1 
ATOM   1105  C  CB    . SER   A 1  140 ? 25.053  75.990  54.301  1.00 35.97  ? 140 SER   A CB    1 
ATOM   1106  O  OG    . SER   A 1  140 ? 25.783  75.259  53.320  1.00 27.87  ? 140 SER   A OG    1 
ATOM   1107  N  N     . PHE   A 1  141 ? 26.264  74.218  56.630  1.00 24.86  ? 141 PHE   A N     1 
ATOM   1108  C  CA    . PHE   A 1  141 ? 26.826  72.878  56.791  1.00 25.47  ? 141 PHE   A CA    1 
ATOM   1109  C  C     . PHE   A 1  141 ? 26.603  71.982  55.566  1.00 31.76  ? 141 PHE   A C     1 
ATOM   1110  O  O     . PHE   A 1  141 ? 27.440  71.127  55.284  1.00 26.44  ? 141 PHE   A O     1 
ATOM   1111  C  CB    . PHE   A 1  141 ? 26.190  72.178  57.985  1.00 29.10  ? 141 PHE   A CB    1 
ATOM   1112  C  CG    . PHE   A 1  141 ? 26.684  72.639  59.300  1.00 29.52  ? 141 PHE   A CG    1 
ATOM   1113  C  CD1   . PHE   A 1  141 ? 27.730  73.529  59.396  1.00 36.65  ? 141 PHE   A CD1   1 
ATOM   1114  C  CD2   . PHE   A 1  141 ? 26.103  72.169  60.456  1.00 25.43  ? 141 PHE   A CD2   1 
ATOM   1115  C  CE1   . PHE   A 1  141 ? 28.175  73.936  60.639  1.00 35.57  ? 141 PHE   A CE1   1 
ATOM   1116  C  CE2   . PHE   A 1  141 ? 26.552  72.571  61.700  1.00 24.97  ? 141 PHE   A CE2   1 
ATOM   1117  C  CZ    . PHE   A 1  141 ? 27.581  73.438  61.792  1.00 28.52  ? 141 PHE   A CZ    1 
ATOM   1118  N  N     . GLY   A 1  142 ? 25.478  72.135  54.848  1.00 35.88  ? 142 GLY   A N     1 
ATOM   1119  C  CA    . GLY   A 1  142 ? 24.978  71.092  53.949  1.00 32.98  ? 142 GLY   A CA    1 
ATOM   1120  C  C     . GLY   A 1  142 ? 25.446  71.013  52.501  1.00 33.75  ? 142 GLY   A C     1 
ATOM   1121  O  O     . GLY   A 1  142 ? 25.418  69.933  51.911  1.00 34.92  ? 142 GLY   A O     1 
ATOM   1122  N  N     . GLY   A 1  143 ? 25.850  72.126  51.898  1.00 32.30  ? 143 GLY   A N     1 
ATOM   1123  C  CA    . GLY   A 1  143 ? 26.399  72.104  50.559  1.00 30.44  ? 143 GLY   A CA    1 
ATOM   1124  C  C     . GLY   A 1  143 ? 27.876  71.713  50.510  1.00 37.74  ? 143 GLY   A C     1 
ATOM   1125  O  O     . GLY   A 1  143 ? 28.529  71.451  51.523  1.00 41.82  ? 143 GLY   A O     1 
ATOM   1126  N  N     . GLY   A 1  144 ? 28.408  71.670  49.286  1.00 34.56  ? 144 GLY   A N     1 
ATOM   1127  C  CA    . GLY   A 1  144 ? 29.785  71.250  49.090  1.00 32.02  ? 144 GLY   A CA    1 
ATOM   1128  C  C     . GLY   A 1  144 ? 30.776  72.345  49.430  1.00 38.36  ? 144 GLY   A C     1 
ATOM   1129  O  O     . GLY   A 1  144 ? 31.761  72.111  50.147  1.00 30.62  ? 144 GLY   A O     1 
ATOM   1130  N  N     . THR   A 1  145 ? 30.520  73.553  48.910  1.00 30.64  ? 145 THR   A N     1 
ATOM   1131  C  CA    . THR   A 1  145 ? 31.355  74.699  49.238  1.00 29.87  ? 145 THR   A CA    1 
ATOM   1132  C  C     . THR   A 1  145 ? 31.234  75.054  50.713  1.00 37.78  ? 145 THR   A C     1 
ATOM   1133  O  O     . THR   A 1  145 ? 32.226  75.059  51.451  1.00 43.30  ? 145 THR   A O     1 
ATOM   1134  C  CB    . THR   A 1  145 ? 30.975  75.910  48.392  1.00 32.27  ? 145 THR   A CB    1 
ATOM   1135  O  OG1   . THR   A 1  145 ? 30.794  75.533  47.022  1.00 27.46  ? 145 THR   A OG1   1 
ATOM   1136  C  CG2   . THR   A 1  145 ? 32.078  76.952  48.492  1.00 43.50  ? 145 THR   A CG2   1 
ATOM   1137  N  N     . GLY   A 1  146 ? 30.025  75.370  51.154  1.00 32.57  ? 146 GLY   A N     1 
ATOM   1138  C  CA    . GLY   A 1  146 ? 29.814  75.836  52.505  1.00 30.35  ? 146 GLY   A CA    1 
ATOM   1139  C  C     . GLY   A 1  146 ? 30.357  74.930  53.589  1.00 30.59  ? 146 GLY   A C     1 
ATOM   1140  O  O     . GLY   A 1  146 ? 30.621  75.393  54.696  1.00 36.55  ? 146 GLY   A O     1 
ATOM   1141  N  N     . SER   A 1  147 ? 30.520  73.645  53.308  1.00 32.41  ? 147 SER   A N     1 
ATOM   1142  C  CA    . SER   A 1  147 ? 31.095  72.732  54.288  1.00 31.44  ? 147 SER   A CA    1 
ATOM   1143  C  C     . SER   A 1  147 ? 32.569  72.452  54.051  1.00 29.86  ? 147 SER   A C     1 
ATOM   1144  O  O     . SER   A 1  147 ? 33.354  72.434  55.001  1.00 25.80  ? 147 SER   A O     1 
ATOM   1145  C  CB    . SER   A 1  147 ? 30.338  71.402  54.288  1.00 31.91  ? 147 SER   A CB    1 
ATOM   1146  O  OG    . SER   A 1  147 ? 30.148  70.929  52.964  1.00 32.35  ? 147 SER   A OG    1 
ATOM   1147  N  N     . GLY   A 1  148 ? 32.951  72.206  52.806  1.00 28.50  ? 148 GLY   A N     1 
ATOM   1148  C  CA    . GLY   A 1  148 ? 34.246  71.646  52.509  1.00 26.68  ? 148 GLY   A CA    1 
ATOM   1149  C  C     . GLY   A 1  148 ? 35.271  72.690  52.145  1.00 32.88  ? 148 GLY   A C     1 
ATOM   1150  O  O     . GLY   A 1  148 ? 36.431  72.553  52.534  1.00 42.17  ? 148 GLY   A O     1 
ATOM   1151  N  N     . PHE   A 1  149 ? 34.887  73.718  51.382  1.00 22.65  ? 149 PHE   A N     1 
ATOM   1152  C  CA    . PHE   A 1  149 ? 35.793  74.844  51.237  1.00 28.45  ? 149 PHE   A CA    1 
ATOM   1153  C  C     . PHE   A 1  149 ? 35.956  75.598  52.556  1.00 46.32  ? 149 PHE   A C     1 
ATOM   1154  O  O     . PHE   A 1  149 ? 37.083  75.929  52.953  1.00 46.00  ? 149 PHE   A O     1 
ATOM   1155  C  CB    . PHE   A 1  149 ? 35.336  75.798  50.154  1.00 35.35  ? 149 PHE   A CB    1 
ATOM   1156  C  CG    . PHE   A 1  149 ? 36.356  76.844  49.862  1.00 41.63  ? 149 PHE   A CG    1 
ATOM   1157  C  CD1   . PHE   A 1  149 ? 37.624  76.474  49.443  1.00 43.01  ? 149 PHE   A CD1   1 
ATOM   1158  C  CD2   . PHE   A 1  149 ? 36.086  78.179  50.056  1.00 43.26  ? 149 PHE   A CD2   1 
ATOM   1159  C  CE1   . PHE   A 1  149 ? 38.593  77.423  49.187  1.00 50.30  ? 149 PHE   A CE1   1 
ATOM   1160  C  CE2   . PHE   A 1  149 ? 37.054  79.138  49.802  1.00 48.55  ? 149 PHE   A CE2   1 
ATOM   1161  C  CZ    . PHE   A 1  149 ? 38.311  78.758  49.368  1.00 49.55  ? 149 PHE   A CZ    1 
ATOM   1162  N  N     . THR   A 1  150 ? 34.836  75.870  53.251  1.00 49.55  ? 150 THR   A N     1 
ATOM   1163  C  CA    . THR   A 1  150 ? 34.868  76.586  54.530  1.00 38.30  ? 150 THR   A CA    1 
ATOM   1164  C  C     . THR   A 1  150 ? 35.824  75.945  55.533  1.00 30.94  ? 150 THR   A C     1 
ATOM   1165  O  O     . THR   A 1  150 ? 36.542  76.653  56.239  1.00 38.60  ? 150 THR   A O     1 
ATOM   1166  C  CB    . THR   A 1  150 ? 33.459  76.673  55.128  1.00 30.79  ? 150 THR   A CB    1 
ATOM   1167  O  OG1   . THR   A 1  150 ? 32.801  77.855  54.657  1.00 35.47  ? 150 THR   A OG1   1 
ATOM   1168  C  CG2   . THR   A 1  150 ? 33.524  76.717  56.629  1.00 26.35  ? 150 THR   A CG2   1 
ATOM   1169  N  N     . SER   A 1  151 ? 35.849  74.612  55.616  1.00 30.60  ? 151 SER   A N     1 
ATOM   1170  C  CA    . SER   A 1  151 ? 36.771  73.947  56.550  1.00 37.59  ? 151 SER   A CA    1 
ATOM   1171  C  C     . SER   A 1  151 ? 38.219  74.057  56.083  1.00 49.90  ? 151 SER   A C     1 
ATOM   1172  O  O     . SER   A 1  151 ? 39.147  74.003  56.903  1.00 38.42  ? 151 SER   A O     1 
ATOM   1173  C  CB    . SER   A 1  151 ? 36.408  72.462  56.732  1.00 32.82  ? 151 SER   A CB    1 
ATOM   1174  O  OG    . SER   A 1  151 ? 36.853  71.648  55.643  1.00 29.38  ? 151 SER   A OG    1 
ATOM   1175  N  N     . LEU   A 1  152 ? 38.427  74.169  54.769  1.00 47.66  ? 152 LEU   A N     1 
ATOM   1176  C  CA    . LEU   A 1  152 ? 39.767  74.377  54.245  1.00 43.69  ? 152 LEU   A CA    1 
ATOM   1177  C  C     . LEU   A 1  152 ? 40.228  75.795  54.533  1.00 46.42  ? 152 LEU   A C     1 
ATOM   1178  O  O     . LEU   A 1  152 ? 41.344  76.011  55.023  1.00 48.40  ? 152 LEU   A O     1 
ATOM   1179  C  CB    . LEU   A 1  152 ? 39.790  74.089  52.744  1.00 48.08  ? 152 LEU   A CB    1 
ATOM   1180  C  CG    . LEU   A 1  152 ? 41.083  74.429  52.006  1.00 47.46  ? 152 LEU   A CG    1 
ATOM   1181  C  CD1   . LEU   A 1  152 ? 42.094  73.329  52.229  1.00 35.42  ? 152 LEU   A CD1   1 
ATOM   1182  C  CD2   . LEU   A 1  152 ? 40.822  74.683  50.516  1.00 43.58  ? 152 LEU   A CD2   1 
ATOM   1183  N  N     . LEU   A 1  153 ? 39.367  76.777  54.255  1.00 44.99  ? 153 LEU   A N     1 
ATOM   1184  C  CA    . LEU   A 1  153 ? 39.728  78.163  54.530  1.00 44.59  ? 153 LEU   A CA    1 
ATOM   1185  C  C     . LEU   A 1  153 ? 40.033  78.357  56.009  1.00 43.18  ? 153 LEU   A C     1 
ATOM   1186  O  O     . LEU   A 1  153 ? 41.002  79.039  56.363  1.00 45.80  ? 153 LEU   A O     1 
ATOM   1187  C  CB    . LEU   A 1  153 ? 38.619  79.108  54.066  1.00 30.52  ? 153 LEU   A CB    1 
ATOM   1188  C  CG    . LEU   A 1  153 ? 38.902  80.608  54.126  1.00 42.28  ? 153 LEU   A CG    1 
ATOM   1189  C  CD1   . LEU   A 1  153 ? 40.376  80.909  53.891  1.00 44.78  ? 153 LEU   A CD1   1 
ATOM   1190  C  CD2   . LEU   A 1  153 ? 38.064  81.372  53.105  1.00 48.47  ? 153 LEU   A CD2   1 
ATOM   1191  N  N     . MET   A 1  154 ? 39.236  77.740  56.885  1.00 36.24  ? 154 MET   A N     1 
ATOM   1192  C  CA    . MET   A 1  154 ? 39.479  77.854  58.319  1.00 38.97  ? 154 MET   A CA    1 
ATOM   1193  C  C     . MET   A 1  154 ? 40.900  77.425  58.673  1.00 44.97  ? 154 MET   A C     1 
ATOM   1194  O  O     . MET   A 1  154 ? 41.658  78.184  59.290  1.00 36.03  ? 154 MET   A O     1 
ATOM   1195  C  CB    . MET   A 1  154 ? 38.451  77.030  59.095  1.00 32.25  ? 154 MET   A CB    1 
ATOM   1196  C  CG    . MET   A 1  154 ? 37.048  77.652  59.181  1.00 44.47  ? 154 MET   A CG    1 
ATOM   1197  S  SD    . MET   A 1  154 ? 36.822  78.979  60.424  1.00 46.20  ? 154 MET   A SD    1 
ATOM   1198  C  CE    . MET   A 1  154 ? 36.500  80.341  59.327  1.00 33.01  ? 154 MET   A CE    1 
ATOM   1199  N  N     . GLU   A 1  155 ? 41.288  76.210  58.277  1.00 51.52  ? 155 GLU   A N     1 
ATOM   1200  C  CA    . GLU   A 1  155 ? 42.626  75.725  58.610  1.00 51.56  ? 155 GLU   A CA    1 
ATOM   1201  C  C     . GLU   A 1  155 ? 43.715  76.658  58.078  1.00 56.44  ? 155 GLU   A C     1 
ATOM   1202  O  O     . GLU   A 1  155 ? 44.720  76.896  58.755  1.00 51.87  ? 155 GLU   A O     1 
ATOM   1203  C  CB    . GLU   A 1  155 ? 42.810  74.315  58.077  1.00 44.20  ? 155 GLU   A CB    1 
ATOM   1204  C  CG    . GLU   A 1  155 ? 42.034  73.304  58.856  1.00 59.14  ? 155 GLU   A CG    1 
ATOM   1205  C  CD    . GLU   A 1  155 ? 42.273  71.908  58.350  1.00 67.26  ? 155 GLU   A CD    1 
ATOM   1206  O  OE1   . GLU   A 1  155 ? 42.520  71.780  57.125  1.00 59.86  ? 155 GLU   A OE1   1 
ATOM   1207  O  OE2   . GLU   A 1  155 ? 42.230  70.962  59.177  1.00 58.38  ? 155 GLU   A OE2   1 
ATOM   1208  N  N     . ARG   A 1  156 ? 43.537  77.199  56.872  1.00 48.07  ? 156 ARG   A N     1 
ATOM   1209  C  CA    . ARG   A 1  156 ? 44.502  78.169  56.374  1.00 52.95  ? 156 ARG   A CA    1 
ATOM   1210  C  C     . ARG   A 1  156 ? 44.492  79.451  57.205  1.00 57.85  ? 156 ARG   A C     1 
ATOM   1211  O  O     . ARG   A 1  156 ? 45.558  80.005  57.502  1.00 59.25  ? 156 ARG   A O     1 
ATOM   1212  C  CB    . ARG   A 1  156 ? 44.238  78.473  54.897  1.00 49.16  ? 156 ARG   A CB    1 
ATOM   1213  C  CG    . ARG   A 1  156 ? 44.800  77.406  53.969  1.00 59.66  ? 156 ARG   A CG    1 
ATOM   1214  C  CD    . ARG   A 1  156 ? 46.330  77.302  54.044  1.00 52.20  ? 156 ARG   A CD    1 
ATOM   1215  N  NE    . ARG   A 1  156 ? 46.935  78.007  52.922  1.00 64.00  ? 156 ARG   A NE    1 
ATOM   1216  C  CZ    . ARG   A 1  156 ? 47.194  77.450  51.746  1.00 70.69  ? 156 ARG   A CZ    1 
ATOM   1217  N  NH1   . ARG   A 1  156 ? 47.042  76.146  51.550  1.00 69.52  ? 156 ARG   A NH1   1 
ATOM   1218  N  NH2   . ARG   A 1  156 ? 47.604  78.221  50.738  1.00 58.84  ? 156 ARG   A NH2   1 
ATOM   1219  N  N     . LEU   A 1  157 ? 43.308  79.946  57.583  1.00 52.37  ? 157 LEU   A N     1 
ATOM   1220  C  CA    . LEU   A 1  157 ? 43.255  81.188  58.352  1.00 51.57  ? 157 LEU   A CA    1 
ATOM   1221  C  C     . LEU   A 1  157 ? 43.955  81.031  59.700  1.00 49.42  ? 157 LEU   A C     1 
ATOM   1222  O  O     . LEU   A 1  157 ? 44.657  81.943  60.150  1.00 51.70  ? 157 LEU   A O     1 
ATOM   1223  C  CB    . LEU   A 1  157 ? 41.807  81.642  58.541  1.00 45.18  ? 157 LEU   A CB    1 
ATOM   1224  C  CG    . LEU   A 1  157 ? 41.087  82.142  57.292  1.00 42.03  ? 157 LEU   A CG    1 
ATOM   1225  C  CD1   . LEU   A 1  157 ? 39.664  82.609  57.614  1.00 41.93  ? 157 LEU   A CD1   1 
ATOM   1226  C  CD2   . LEU   A 1  157 ? 41.886  83.258  56.650  1.00 44.76  ? 157 LEU   A CD2   1 
ATOM   1227  N  N     . SER   A 1  158 ? 43.792  79.876  60.348  1.00 44.01  ? 158 SER   A N     1 
ATOM   1228  C  CA    . SER   A 1  158 ? 44.493  79.629  61.601  1.00 41.09  ? 158 SER   A CA    1 
ATOM   1229  C  C     . SER   A 1  158 ? 46.006  79.644  61.411  1.00 54.47  ? 158 SER   A C     1 
ATOM   1230  O  O     . SER   A 1  158 ? 46.737  80.215  62.229  1.00 64.19  ? 158 SER   A O     1 
ATOM   1231  C  CB    . SER   A 1  158 ? 44.040  78.304  62.197  1.00 40.84  ? 158 SER   A CB    1 
ATOM   1232  O  OG    . SER   A 1  158 ? 42.658  78.360  62.497  1.00 52.76  ? 158 SER   A OG    1 
ATOM   1233  N  N     . VAL   A 1  159 ? 46.501  79.015  60.349  1.00 54.79  ? 159 VAL   A N     1 
ATOM   1234  C  CA    . VAL   A 1  159 ? 47.931  79.071  60.059  1.00 51.38  ? 159 VAL   A CA    1 
ATOM   1235  C  C     . VAL   A 1  159 ? 48.359  80.504  59.743  1.00 57.67  ? 159 VAL   A C     1 
ATOM   1236  O  O     . VAL   A 1  159 ? 49.375  80.993  60.249  1.00 60.59  ? 159 VAL   A O     1 
ATOM   1237  C  CB    . VAL   A 1  159 ? 48.278  78.110  58.909  1.00 55.57  ? 159 VAL   A CB    1 
ATOM   1238  C  CG1   . VAL   A 1  159 ? 49.665  78.413  58.392  1.00 63.45  ? 159 VAL   A CG1   1 
ATOM   1239  C  CG2   . VAL   A 1  159 ? 48.163  76.651  59.369  1.00 51.94  ? 159 VAL   A CG2   1 
ATOM   1240  N  N     . ASP   A 1  160 ? 47.583  81.202  58.913  1.00 54.85  ? 160 ASP   A N     1 
ATOM   1241  C  CA    . ASP   A 1  160 ? 47.929  82.533  58.425  1.00 46.59  ? 160 ASP   A CA    1 
ATOM   1242  C  C     . ASP   A 1  160 ? 47.588  83.664  59.392  1.00 59.71  ? 160 ASP   A C     1 
ATOM   1243  O  O     . ASP   A 1  160 ? 47.877  84.826  59.064  1.00 51.25  ? 160 ASP   A O     1 
ATOM   1244  C  CB    . ASP   A 1  160 ? 47.215  82.819  57.100  1.00 52.39  ? 160 ASP   A CB    1 
ATOM   1245  C  CG    . ASP   A 1  160 ? 47.960  82.275  55.904  1.00 61.93  ? 160 ASP   A CG    1 
ATOM   1246  O  OD1   . ASP   A 1  160 ? 48.790  81.354  56.099  1.00 57.91  ? 160 ASP   A OD1   1 
ATOM   1247  O  OD2   . ASP   A 1  160 ? 47.716  82.780  54.776  1.00 56.84  ? 160 ASP   A OD2   1 
ATOM   1248  N  N     . TYR   A 1  161 ? 46.955  83.383  60.539  1.00 53.27  ? 161 TYR   A N     1 
ATOM   1249  C  CA    . TYR   A 1  161 ? 46.513  84.464  61.415  1.00 41.00  ? 161 TYR   A CA    1 
ATOM   1250  C  C     . TYR   A 1  161 ? 46.325  84.015  62.856  1.00 54.60  ? 161 TYR   A C     1 
ATOM   1251  O  O     . TYR   A 1  161 ? 45.373  84.457  63.508  1.00 64.51  ? 161 TYR   A O     1 
ATOM   1252  C  CB    . TYR   A 1  161 ? 45.184  85.056  60.945  1.00 38.17  ? 161 TYR   A CB    1 
ATOM   1253  C  CG    . TYR   A 1  161 ? 45.152  85.776  59.619  1.00 41.71  ? 161 TYR   A CG    1 
ATOM   1254  C  CD1   . TYR   A 1  161 ? 44.967  85.077  58.429  1.00 47.48  ? 161 TYR   A CD1   1 
ATOM   1255  C  CD2   . TYR   A 1  161 ? 45.226  87.159  59.556  1.00 36.50  ? 161 TYR   A CD2   1 
ATOM   1256  C  CE1   . TYR   A 1  161 ? 44.902  85.727  57.209  1.00 41.90  ? 161 TYR   A CE1   1 
ATOM   1257  C  CE2   . TYR   A 1  161 ? 45.156  87.832  58.330  1.00 48.63  ? 161 TYR   A CE2   1 
ATOM   1258  C  CZ    . TYR   A 1  161 ? 44.994  87.105  57.156  1.00 52.92  ? 161 TYR   A CZ    1 
ATOM   1259  O  OH    . TYR   A 1  161 ? 44.923  87.751  55.931  1.00 48.77  ? 161 TYR   A OH    1 
ATOM   1260  N  N     . GLY   A 1  162 ? 47.203  83.156  63.367  1.00 48.68  ? 162 GLY   A N     1 
ATOM   1261  C  CA    . GLY   A 1  162 ? 47.061  82.626  64.718  1.00 55.79  ? 162 GLY   A CA    1 
ATOM   1262  C  C     . GLY   A 1  162 ? 46.477  83.550  65.777  1.00 57.92  ? 162 GLY   A C     1 
ATOM   1263  O  O     . GLY   A 1  162 ? 45.559  83.169  66.511  1.00 54.97  ? 162 GLY   A O     1 
ATOM   1264  N  N     . LYS   A 1  163 ? 47.005  84.774  65.865  1.00 65.59  ? 163 LYS   A N     1 
ATOM   1265  C  CA    . LYS   A 1  163 ? 46.570  85.723  66.889  1.00 76.88  ? 163 LYS   A CA    1 
ATOM   1266  C  C     . LYS   A 1  163 ? 45.076  86.052  66.805  1.00 79.41  ? 163 LYS   A C     1 
ATOM   1267  O  O     . LYS   A 1  163 ? 44.496  86.498  67.808  1.00 73.57  ? 163 LYS   A O     1 
ATOM   1268  C  CB    . LYS   A 1  163 ? 47.392  87.024  66.777  1.00 74.81  ? 163 LYS   A CB    1 
ATOM   1269  C  CG    . LYS   A 1  163 ? 48.699  87.082  67.582  1.00 58.86  ? 163 LYS   A CG    1 
ATOM   1270  C  CD    . LYS   A 1  163 ? 49.661  85.962  67.222  1.00 74.23  ? 163 LYS   A CD    1 
ATOM   1271  C  CE    . LYS   A 1  163 ? 49.288  84.640  67.892  1.00 70.87  ? 163 LYS   A CE    1 
ATOM   1272  N  NZ    . LYS   A 1  163 ? 49.957  83.495  67.214  1.00 66.24  ? 163 LYS   A NZ    1 
ATOM   1273  N  N     . LYS   A 1  164 ? 44.447  85.840  65.643  1.00 65.25  ? 164 LYS   A N     1 
ATOM   1274  C  CA    . LYS   A 1  164 ? 43.112  86.342  65.337  1.00 57.26  ? 164 LYS   A CA    1 
ATOM   1275  C  C     . LYS   A 1  164 ? 42.016  85.401  65.836  1.00 51.26  ? 164 LYS   A C     1 
ATOM   1276  O  O     . LYS   A 1  164 ? 42.240  84.211  66.075  1.00 39.36  ? 164 LYS   A O     1 
ATOM   1277  C  CB    . LYS   A 1  164 ? 42.957  86.557  63.833  1.00 43.42  ? 164 LYS   A CB    1 
ATOM   1278  C  CG    . LYS   A 1  164 ? 43.402  87.924  63.339  1.00 59.61  ? 164 LYS   A CG    1 
ATOM   1279  C  CD    . LYS   A 1  164 ? 44.656  88.418  64.046  1.00 65.25  ? 164 LYS   A CD    1 
ATOM   1280  C  CE    . LYS   A 1  164 ? 44.773  89.936  63.915  1.00 67.23  ? 164 LYS   A CE    1 
ATOM   1281  N  NZ    . LYS   A 1  164 ? 45.679  90.554  64.930  1.00 72.26  ? 164 LYS   A NZ    1 
ATOM   1282  N  N     . SER   A 1  165 ? 40.821  85.970  66.004  1.00 46.79  ? 165 SER   A N     1 
ATOM   1283  C  CA    . SER   A 1  165 ? 39.617  85.241  66.389  1.00 50.07  ? 165 SER   A CA    1 
ATOM   1284  C  C     . SER   A 1  165 ? 38.815  84.844  65.151  1.00 40.82  ? 165 SER   A C     1 
ATOM   1285  O  O     . SER   A 1  165 ? 38.869  85.501  64.107  1.00 40.68  ? 165 SER   A O     1 
ATOM   1286  C  CB    . SER   A 1  165 ? 38.729  86.096  67.309  1.00 51.63  ? 165 SER   A CB    1 
ATOM   1287  O  OG    . SER   A 1  165 ? 39.023  85.918  68.681  1.00 37.99  ? 165 SER   A OG    1 
ATOM   1288  N  N     . LYS   A 1  166 ? 38.036  83.781  65.280  1.00 39.49  ? 166 LYS   A N     1 
ATOM   1289  C  CA    . LYS   A 1  166 ? 37.140  83.387  64.192  1.00 45.19  ? 166 LYS   A CA    1 
ATOM   1290  C  C     . LYS   A 1  166 ? 35.829  82.904  64.798  1.00 40.35  ? 166 LYS   A C     1 
ATOM   1291  O  O     . LYS   A 1  166 ? 35.804  81.903  65.520  1.00 39.71  ? 166 LYS   A O     1 
ATOM   1292  C  CB    . LYS   A 1  166 ? 37.783  82.312  63.310  1.00 41.93  ? 166 LYS   A CB    1 
ATOM   1293  C  CG    . LYS   A 1  166 ? 39.110  82.750  62.637  1.00 47.72  ? 166 LYS   A CG    1 
ATOM   1294  C  CD    . LYS   A 1  166 ? 39.575  81.788  61.520  1.00 43.69  ? 166 LYS   A CD    1 
ATOM   1295  C  CE    . LYS   A 1  166 ? 39.841  80.340  62.014  1.00 41.73  ? 166 LYS   A CE    1 
ATOM   1296  N  NZ    . LYS   A 1  166 ? 41.085  80.115  62.821  1.00 32.01  ? 166 LYS   A NZ    1 
ATOM   1297  N  N     . LEU   A 1  167 ? 34.758  83.640  64.534  1.00 36.73  ? 167 LEU   A N     1 
ATOM   1298  C  CA    . LEU   A 1  167 ? 33.389  83.240  64.845  1.00 41.21  ? 167 LEU   A CA    1 
ATOM   1299  C  C     . LEU   A 1  167 ? 32.710  82.697  63.588  1.00 37.64  ? 167 LEU   A C     1 
ATOM   1300  O  O     . LEU   A 1  167 ? 33.007  83.122  62.464  1.00 39.01  ? 167 LEU   A O     1 
ATOM   1301  C  CB    . LEU   A 1  167 ? 32.572  84.426  65.396  1.00 30.71  ? 167 LEU   A CB    1 
ATOM   1302  C  CG    . LEU   A 1  167 ? 32.714  84.892  66.856  1.00 39.96  ? 167 LEU   A CG    1 
ATOM   1303  C  CD1   . LEU   A 1  167 ? 34.168  85.012  67.287  1.00 36.79  ? 167 LEU   A CD1   1 
ATOM   1304  C  CD2   . LEU   A 1  167 ? 31.991  86.211  67.067  1.00 30.92  ? 167 LEU   A CD2   1 
ATOM   1305  N  N     . GLU   A 1  168 ? 31.778  81.767  63.782  1.00 36.73  ? 168 GLU   A N     1 
ATOM   1306  C  CA    . GLU   A 1  168 ? 30.975  81.257  62.681  1.00 34.35  ? 168 GLU   A CA    1 
ATOM   1307  C  C     . GLU   A 1  168 ? 29.507  81.608  62.863  1.00 38.65  ? 168 GLU   A C     1 
ATOM   1308  O  O     . GLU   A 1  168 ? 28.989  81.664  63.988  1.00 37.15  ? 168 GLU   A O     1 
ATOM   1309  C  CB    . GLU   A 1  168 ? 31.061  79.748  62.546  1.00 29.86  ? 168 GLU   A CB    1 
ATOM   1310  C  CG    . GLU   A 1  168 ? 32.416  79.157  62.634  1.00 28.78  ? 168 GLU   A CG    1 
ATOM   1311  C  CD    . GLU   A 1  168 ? 32.400  77.721  62.193  1.00 32.82  ? 168 GLU   A CD    1 
ATOM   1312  O  OE1   . GLU   A 1  168 ? 32.045  77.497  61.020  1.00 28.66  ? 168 GLU   A OE1   1 
ATOM   1313  O  OE2   . GLU   A 1  168 ? 32.709  76.820  63.013  1.00 34.01  ? 168 GLU   A OE2   1 
ATOM   1314  N  N     . PHE   A 1  169 ? 28.842  81.807  61.726  1.00 39.59  ? 169 PHE   A N     1 
ATOM   1315  C  CA    . PHE   A 1  169 ? 27.390  81.754  61.608  1.00 34.90  ? 169 PHE   A CA    1 
ATOM   1316  C  C     . PHE   A 1  169 ? 27.067  80.584  60.684  1.00 36.81  ? 169 PHE   A C     1 
ATOM   1317  O  O     . PHE   A 1  169 ? 27.321  80.654  59.479  1.00 33.88  ? 169 PHE   A O     1 
ATOM   1318  C  CB    . PHE   A 1  169 ? 26.848  83.089  61.099  1.00 33.47  ? 169 PHE   A CB    1 
ATOM   1319  C  CG    . PHE   A 1  169 ? 26.992  84.204  62.106  1.00 40.97  ? 169 PHE   A CG    1 
ATOM   1320  C  CD1   . PHE   A 1  169 ? 26.084  84.330  63.150  1.00 36.22  ? 169 PHE   A CD1   1 
ATOM   1321  C  CD2   . PHE   A 1  169 ? 28.061  85.083  62.043  1.00 42.25  ? 169 PHE   A CD2   1 
ATOM   1322  C  CE1   . PHE   A 1  169 ? 26.220  85.316  64.088  1.00 40.68  ? 169 PHE   A CE1   1 
ATOM   1323  C  CE2   . PHE   A 1  169 ? 28.214  86.080  62.988  1.00 43.72  ? 169 PHE   A CE2   1 
ATOM   1324  C  CZ    . PHE   A 1  169 ? 27.293  86.198  64.011  1.00 47.07  ? 169 PHE   A CZ    1 
ATOM   1325  N  N     . SER   A 1  170 ? 26.544  79.495  61.249  1.00 35.02  ? 170 SER   A N     1 
ATOM   1326  C  CA    . SER   A 1  170 ? 26.464  78.209  60.560  1.00 32.70  ? 170 SER   A CA    1 
ATOM   1327  C  C     . SER   A 1  170 ? 25.016  77.764  60.424  1.00 33.62  ? 170 SER   A C     1 
ATOM   1328  O  O     . SER   A 1  170 ? 24.345  77.505  61.430  1.00 28.76  ? 170 SER   A O     1 
ATOM   1329  C  CB    . SER   A 1  170 ? 27.263  77.133  61.297  1.00 27.78  ? 170 SER   A CB    1 
ATOM   1330  O  OG    . SER   A 1  170 ? 28.595  77.552  61.531  1.00 34.74  ? 170 SER   A OG    1 
ATOM   1331  N  N     . ILE   A 1  171 ? 24.574  77.609  59.177  1.00 32.61  ? 171 ILE   A N     1 
ATOM   1332  C  CA    . ILE   A 1  171 ? 23.218  77.189  58.825  1.00 25.60  ? 171 ILE   A CA    1 
ATOM   1333  C  C     . ILE   A 1  171 ? 23.110  75.663  58.905  1.00 21.66  ? 171 ILE   A C     1 
ATOM   1334  O  O     . ILE   A 1  171 ? 23.695  74.942  58.095  1.00 29.97  ? 171 ILE   A O     1 
ATOM   1335  C  CB    . ILE   A 1  171 ? 22.864  77.707  57.427  1.00 32.01  ? 171 ILE   A CB    1 
ATOM   1336  C  CG1   . ILE   A 1  171 ? 22.877  79.243  57.468  1.00 18.59  ? 171 ILE   A CG1   1 
ATOM   1337  C  CG2   . ILE   A 1  171 ? 21.541  77.095  56.893  1.00 19.66  ? 171 ILE   A CG2   1 
ATOM   1338  C  CD1   . ILE   A 1  171 ? 21.744  79.835  58.267  1.00 20.53  ? 171 ILE   A CD1   1 
ATOM   1339  N  N     . TYR   A 1  172 ? 22.363  75.171  59.866  1.00 19.77  ? 172 TYR   A N     1 
ATOM   1340  C  CA    . TYR   A 1  172 ? 22.231  73.732  60.115  1.00 17.77  ? 172 TYR   A CA    1 
ATOM   1341  C  C     . TYR   A 1  172 ? 21.148  73.138  59.210  1.00 16.89  ? 172 TYR   A C     1 
ATOM   1342  O  O     . TYR   A 1  172 ? 20.140  73.790  58.951  1.00 20.37  ? 172 TYR   A O     1 
ATOM   1343  C  CB    . TYR   A 1  172 ? 21.906  73.520  61.589  1.00 22.30  ? 172 TYR   A CB    1 
ATOM   1344  C  CG    . TYR   A 1  172 ? 21.602  72.122  62.101  1.00 25.69  ? 172 TYR   A CG    1 
ATOM   1345  C  CD1   . TYR   A 1  172 ? 20.411  71.473  61.776  1.00 17.96  ? 172 TYR   A CD1   1 
ATOM   1346  C  CD2   . TYR   A 1  172 ? 22.469  71.495  62.993  1.00 19.59  ? 172 TYR   A CD2   1 
ATOM   1347  C  CE1   . TYR   A 1  172 ? 20.132  70.222  62.284  1.00 21.01  ? 172 TYR   A CE1   1 
ATOM   1348  C  CE2   . TYR   A 1  172 ? 22.190  70.243  63.513  1.00 20.14  ? 172 TYR   A CE2   1 
ATOM   1349  C  CZ    . TYR   A 1  172 ? 21.023  69.607  63.152  1.00 25.43  ? 172 TYR   A CZ    1 
ATOM   1350  O  OH    . TYR   A 1  172 ? 20.738  68.362  63.662  1.00 29.90  ? 172 TYR   A OH    1 
ATOM   1351  N  N     . PRO   A 1  173 ? 21.324  71.912  58.705  1.00 23.24  ? 173 PRO   A N     1 
ATOM   1352  C  CA    . PRO   A 1  173 ? 20.487  71.448  57.584  1.00 17.85  ? 173 PRO   A CA    1 
ATOM   1353  C  C     . PRO   A 1  173 ? 19.111  70.973  58.039  1.00 18.52  ? 173 PRO   A C     1 
ATOM   1354  O  O     . PRO   A 1  173 ? 18.982  70.261  59.037  1.00 21.46  ? 173 PRO   A O     1 
ATOM   1355  C  CB    . PRO   A 1  173 ? 21.312  70.297  56.999  1.00 10.61  ? 173 PRO   A CB    1 
ATOM   1356  C  CG    . PRO   A 1  173 ? 21.892  69.688  58.211  1.00 22.30  ? 173 PRO   A CG    1 
ATOM   1357  C  CD    . PRO   A 1  173 ? 22.192  70.825  59.191  1.00 26.57  ? 173 PRO   A CD    1 
ATOM   1358  N  N     . ALA   A 1  174 ? 18.076  71.369  57.283  1.00 21.51  ? 174 ALA   A N     1 
ATOM   1359  C  CA    . ALA   A 1  174 ? 16.688  71.036  57.595  1.00 15.95  ? 174 ALA   A CA    1 
ATOM   1360  C  C     . ALA   A 1  174 ? 15.971  70.501  56.358  1.00 23.30  ? 174 ALA   A C     1 
ATOM   1361  O  O     . ALA   A 1  174 ? 15.962  71.160  55.309  1.00 25.59  ? 174 ALA   A O     1 
ATOM   1362  C  CB    . ALA   A 1  174 ? 15.947  72.257  58.147  1.00 24.05  ? 174 ALA   A CB    1 
ATOM   1363  N  N     . PRO   A 1  175 ? 15.350  69.321  56.442  1.00 40.26  ? 175 PRO   A N     1 
ATOM   1364  C  CA    . PRO   A 1  175 ? 14.654  68.750  55.264  1.00 25.10  ? 175 PRO   A CA    1 
ATOM   1365  C  C     . PRO   A 1  175 ? 13.701  69.694  54.551  1.00 33.76  ? 175 PRO   A C     1 
ATOM   1366  O  O     . PRO   A 1  175 ? 13.653  69.668  53.318  1.00 45.38  ? 175 PRO   A O     1 
ATOM   1367  C  CB    . PRO   A 1  175 ? 13.898  67.562  55.872  1.00 27.82  ? 175 PRO   A CB    1 
ATOM   1368  C  CG    . PRO   A 1  175 ? 14.746  67.124  56.996  1.00 25.64  ? 175 PRO   A CG    1 
ATOM   1369  C  CD    . PRO   A 1  175 ? 15.374  68.384  57.584  1.00 16.72  ? 175 PRO   A CD    1 
ATOM   1370  N  N     . GLN   A 1  176 ? 12.939  70.527  55.274  1.00 38.08  ? 176 GLN   A N     1 
ATOM   1371  C  CA    . GLN   A 1  176 ? 11.960  71.394  54.614  1.00 32.74  ? 176 GLN   A CA    1 
ATOM   1372  C  C     . GLN   A 1  176 ? 12.555  72.254  53.510  1.00 27.15  ? 176 GLN   A C     1 
ATOM   1373  O  O     . GLN   A 1  176 ? 11.804  72.765  52.683  1.00 37.76  ? 176 GLN   A O     1 
ATOM   1374  C  CB    . GLN   A 1  176 ? 11.268  72.316  55.628  1.00 29.42  ? 176 GLN   A CB    1 
ATOM   1375  C  CG    . GLN   A 1  176 ? 9.850   71.925  55.965  1.00 32.97  ? 176 GLN   A CG    1 
ATOM   1376  C  CD    . GLN   A 1  176 ? 9.575   71.906  57.465  1.00 43.04  ? 176 GLN   A CD    1 
ATOM   1377  O  OE1   . GLN   A 1  176 ? 10.502  71.925  58.271  1.00 47.56  ? 176 GLN   A OE1   1 
ATOM   1378  N  NE2   . GLN   A 1  176 ? 8.290   71.867  57.845  1.00 41.53  ? 176 GLN   A NE2   1 
ATOM   1379  N  N     . VAL   A 1  177 ? 13.870  72.465  53.478  1.00 30.00  ? 177 VAL   A N     1 
ATOM   1380  C  CA    . VAL   A 1  177 ? 14.435  73.306  52.427  1.00 34.16  ? 177 VAL   A CA    1 
ATOM   1381  C  C     . VAL   A 1  177 ? 15.789  72.828  51.913  1.00 35.41  ? 177 VAL   A C     1 
ATOM   1382  O  O     . VAL   A 1  177 ? 16.407  73.507  51.088  1.00 34.99  ? 177 VAL   A O     1 
ATOM   1383  C  CB    . VAL   A 1  177 ? 14.527  74.771  52.889  1.00 30.57  ? 177 VAL   A CB    1 
ATOM   1384  C  CG1   . VAL   A 1  177 ? 13.140  75.355  52.960  1.00 38.70  ? 177 VAL   A CG1   1 
ATOM   1385  C  CG2   . VAL   A 1  177 ? 15.250  74.878  54.227  1.00 25.80  ? 177 VAL   A CG2   1 
ATOM   1386  N  N     . SER   A 1  178 ? 16.236  71.648  52.345  1.00 41.68  ? 178 SER   A N     1 
ATOM   1387  C  CA    . SER   A 1  178 ? 17.480  71.063  51.843  1.00 43.39  ? 178 SER   A CA    1 
ATOM   1388  C  C     . SER   A 1  178 ? 17.344  70.573  50.397  1.00 49.59  ? 178 SER   A C     1 
ATOM   1389  O  O     . SER   A 1  178 ? 16.273  70.143  49.958  1.00 44.75  ? 178 SER   A O     1 
ATOM   1390  C  CB    . SER   A 1  178 ? 17.912  69.886  52.719  1.00 41.33  ? 178 SER   A CB    1 
ATOM   1391  O  OG    . SER   A 1  178 ? 17.299  68.689  52.253  1.00 60.07  ? 178 SER   A OG    1 
ATOM   1392  N  N     . THR   A 1  179 ? 18.467  70.600  49.667  1.00 50.65  ? 179 THR   A N     1 
ATOM   1393  C  CA    . THR   A 1  179 ? 18.540  70.103  48.291  1.00 44.75  ? 179 THR   A CA    1 
ATOM   1394  C  C     . THR   A 1  179 ? 19.548  68.961  48.130  1.00 44.84  ? 179 THR   A C     1 
ATOM   1395  O  O     . THR   A 1  179 ? 20.114  68.792  47.048  1.00 47.67  ? 179 THR   A O     1 
ATOM   1396  C  CB    . THR   A 1  179 ? 18.900  71.226  47.315  1.00 36.21  ? 179 THR   A CB    1 
ATOM   1397  O  OG1   . THR   A 1  179 ? 19.838  72.120  47.929  1.00 43.43  ? 179 THR   A OG1   1 
ATOM   1398  C  CG2   . THR   A 1  179 ? 17.669  71.987  46.871  1.00 46.68  ? 179 THR   A CG2   1 
ATOM   1399  N  N     . ALA   A 1  180 ? 19.798  68.174  49.185  1.00 40.45  ? 180 ALA   A N     1 
ATOM   1400  C  CA    . ALA   A 1  180 ? 20.685  67.016  49.060  1.00 38.47  ? 180 ALA   A CA    1 
ATOM   1401  C  C     . ALA   A 1  180 ? 20.563  66.086  50.260  1.00 35.86  ? 180 ALA   A C     1 
ATOM   1402  O  O     . ALA   A 1  180 ? 20.573  66.554  51.405  1.00 40.35  ? 180 ALA   A O     1 
ATOM   1403  C  CB    . ALA   A 1  180 ? 22.146  67.451  48.887  1.00 28.88  ? 180 ALA   A CB    1 
ATOM   1404  N  N     . VAL   A 1  181 ? 20.453  64.773  50.015  1.00 21.06  ? 181 VAL   A N     1 
ATOM   1405  C  CA    . VAL   A 1  181 ? 20.334  63.817  51.113  1.00 26.75  ? 181 VAL   A CA    1 
ATOM   1406  C  C     . VAL   A 1  181 ? 21.674  63.523  51.781  1.00 26.07  ? 181 VAL   A C     1 
ATOM   1407  O  O     . VAL   A 1  181 ? 21.712  62.809  52.793  1.00 28.25  ? 181 VAL   A O     1 
ATOM   1408  C  CB    . VAL   A 1  181 ? 19.608  62.522  50.643  1.00 28.98  ? 181 VAL   A CB    1 
ATOM   1409  C  CG1   . VAL   A 1  181 ? 18.914  62.699  49.318  1.00 28.52  ? 181 VAL   A CG1   1 
ATOM   1410  C  CG2   . VAL   A 1  181 ? 20.488  61.338  50.573  1.00 24.58  ? 181 VAL   A CG2   1 
ATOM   1411  N  N     . VAL   A 1  182 ? 22.785  64.065  51.273  1.00 23.60  ? 182 VAL   A N     1 
ATOM   1412  C  CA    . VAL   A 1  182 ? 24.076  63.797  51.903  1.00 29.86  ? 182 VAL   A CA    1 
ATOM   1413  C  C     . VAL   A 1  182 ? 24.450  64.852  52.937  1.00 39.83  ? 182 VAL   A C     1 
ATOM   1414  O  O     . VAL   A 1  182 ? 25.523  64.735  53.557  1.00 26.62  ? 182 VAL   A O     1 
ATOM   1415  C  CB    . VAL   A 1  182 ? 25.244  63.684  50.900  1.00 19.43  ? 182 VAL   A CB    1 
ATOM   1416  C  CG1   . VAL   A 1  182 ? 25.154  62.392  50.136  1.00 30.88  ? 182 VAL   A CG1   1 
ATOM   1417  C  CG2   . VAL   A 1  182 ? 25.304  64.894  49.972  1.00 26.00  ? 182 VAL   A CG2   1 
ATOM   1418  N  N     . GLU   A 1  183 ? 23.592  65.860  53.153  1.00 31.00  ? 183 GLU   A N     1 
ATOM   1419  C  CA    . GLU   A 1  183 ? 23.921  66.965  54.049  1.00 29.70  ? 183 GLU   A CA    1 
ATOM   1420  C  C     . GLU   A 1  183 ? 24.398  66.505  55.425  1.00 28.20  ? 183 GLU   A C     1 
ATOM   1421  O  O     . GLU   A 1  183 ? 25.369  67.093  55.930  1.00 33.67  ? 183 GLU   A O     1 
ATOM   1422  C  CB    . GLU   A 1  183 ? 22.719  67.916  54.155  1.00 27.29  ? 183 GLU   A CB    1 
ATOM   1423  C  CG    . GLU   A 1  183 ? 22.183  68.322  52.788  1.00 34.33  ? 183 GLU   A CG    1 
ATOM   1424  C  CD    . GLU   A 1  183 ? 21.583  69.712  52.761  1.00 43.35  ? 183 GLU   A CD    1 
ATOM   1425  O  OE1   . GLU   A 1  183 ? 21.812  70.469  53.718  1.00 39.13  ? 183 GLU   A OE1   1 
ATOM   1426  O  OE2   . GLU   A 1  183 ? 20.874  70.052  51.785  1.00 47.56  ? 183 GLU   A OE2   1 
ATOM   1427  N  N     . PRO   A 1  184 ? 23.832  65.469  56.056  1.00 24.65  ? 184 PRO   A N     1 
ATOM   1428  C  CA    . PRO   A 1  184 ? 24.428  64.994  57.324  1.00 20.35  ? 184 PRO   A CA    1 
ATOM   1429  C  C     . PRO   A 1  184 ? 25.882  64.579  57.195  1.00 23.03  ? 184 PRO   A C     1 
ATOM   1430  O  O     . PRO   A 1  184 ? 26.653  64.762  58.139  1.00 31.29  ? 184 PRO   A O     1 
ATOM   1431  C  CB    . PRO   A 1  184 ? 23.543  63.807  57.722  1.00 17.04  ? 184 PRO   A CB    1 
ATOM   1432  C  CG    . PRO   A 1  184 ? 22.313  63.941  56.927  1.00 16.23  ? 184 PRO   A CG    1 
ATOM   1433  C  CD    . PRO   A 1  184 ? 22.651  64.685  55.660  1.00 17.10  ? 184 PRO   A CD    1 
ATOM   1434  N  N     . TYR   A 1  185 ? 26.273  63.996  56.063  1.00 25.09  ? 185 TYR   A N     1 
ATOM   1435  C  CA    . TYR   A 1  185 ? 27.671  63.665  55.813  1.00 26.50  ? 185 TYR   A CA    1 
ATOM   1436  C  C     . TYR   A 1  185 ? 28.538  64.921  55.801  1.00 29.95  ? 185 TYR   A C     1 
ATOM   1437  O  O     . TYR   A 1  185 ? 29.512  65.029  56.546  1.00 35.11  ? 185 TYR   A O     1 
ATOM   1438  C  CB    . TYR   A 1  185 ? 27.801  62.937  54.473  1.00 32.87  ? 185 TYR   A CB    1 
ATOM   1439  C  CG    . TYR   A 1  185 ? 27.487  61.462  54.496  1.00 33.71  ? 185 TYR   A CG    1 
ATOM   1440  C  CD1   . TYR   A 1  185 ? 27.241  60.804  55.692  1.00 24.01  ? 185 TYR   A CD1   1 
ATOM   1441  C  CD2   . TYR   A 1  185 ? 27.448  60.726  53.312  1.00 25.71  ? 185 TYR   A CD2   1 
ATOM   1442  C  CE1   . TYR   A 1  185 ? 26.969  59.447  55.713  1.00 32.01  ? 185 TYR   A CE1   1 
ATOM   1443  C  CE2   . TYR   A 1  185 ? 27.198  59.367  53.326  1.00 22.87  ? 185 TYR   A CE2   1 
ATOM   1444  C  CZ    . TYR   A 1  185 ? 26.943  58.724  54.522  1.00 32.89  ? 185 TYR   A CZ    1 
ATOM   1445  O  OH    . TYR   A 1  185 ? 26.664  57.351  54.539  1.00 28.99  ? 185 TYR   A OH    1 
ATOM   1446  N  N     . ASN   A 1  186 ? 28.197  65.881  54.944  1.00 26.03  ? 186 ASN   A N     1 
ATOM   1447  C  CA    . ASN   A 1  186 ? 28.953  67.123  54.868  1.00 33.28  ? 186 ASN   A CA    1 
ATOM   1448  C  C     . ASN   A 1  186 ? 28.958  67.880  56.197  1.00 43.32  ? 186 ASN   A C     1 
ATOM   1449  O  O     . ASN   A 1  186 ? 29.895  68.643  56.477  1.00 43.57  ? 186 ASN   A O     1 
ATOM   1450  C  CB    . ASN   A 1  186 ? 28.383  67.999  53.757  1.00 27.33  ? 186 ASN   A CB    1 
ATOM   1451  C  CG    . ASN   A 1  186 ? 28.406  67.304  52.414  1.00 34.34  ? 186 ASN   A CG    1 
ATOM   1452  O  OD1   . ASN   A 1  186 ? 29.210  66.395  52.189  1.00 29.65  ? 186 ASN   A OD1   1 
ATOM   1453  N  ND2   . ASN   A 1  186 ? 27.521  67.719  51.512  1.00 33.67  ? 186 ASN   A ND2   1 
ATOM   1454  N  N     . SER   A 1  187 ? 27.933  67.688  57.023  1.00 30.76  ? 187 SER   A N     1 
ATOM   1455  C  CA    . SER   A 1  187 ? 27.842  68.444  58.259  1.00 29.14  ? 187 SER   A CA    1 
ATOM   1456  C  C     . SER   A 1  187 ? 28.775  67.883  59.327  1.00 37.85  ? 187 SER   A C     1 
ATOM   1457  O  O     . SER   A 1  187 ? 29.472  68.644  60.003  1.00 42.65  ? 187 SER   A O     1 
ATOM   1458  C  CB    . SER   A 1  187 ? 26.394  68.462  58.755  1.00 29.40  ? 187 SER   A CB    1 
ATOM   1459  O  OG    . SER   A 1  187 ? 25.607  69.291  57.929  1.00 37.20  ? 187 SER   A OG    1 
ATOM   1460  N  N     . ILE   A 1  188 ? 28.767  66.560  59.529  1.00 37.02  ? 188 ILE   A N     1 
ATOM   1461  C  CA    . ILE   A 1  188 ? 29.736  65.945  60.432  1.00 34.10  ? 188 ILE   A CA    1 
ATOM   1462  C  C     . ILE   A 1  188 ? 31.154  66.240  59.947  1.00 41.53  ? 188 ILE   A C     1 
ATOM   1463  O  O     . ILE   A 1  188 ? 32.010  66.693  60.716  1.00 33.66  ? 188 ILE   A O     1 
ATOM   1464  C  CB    . ILE   A 1  188 ? 29.485  64.429  60.559  1.00 32.21  ? 188 ILE   A CB    1 
ATOM   1465  C  CG1   . ILE   A 1  188 ? 28.457  64.109  61.649  1.00 30.53  ? 188 ILE   A CG1   1 
ATOM   1466  C  CG2   . ILE   A 1  188 ? 30.769  63.714  60.926  1.00 29.21  ? 188 ILE   A CG2   1 
ATOM   1467  C  CD1   . ILE   A 1  188 ? 27.278  65.020  61.677  1.00 38.99  ? 188 ILE   A CD1   1 
ATOM   1468  N  N     . LEU   A 1  189 ? 31.411  66.017  58.647  1.00 38.22  ? 189 LEU   A N     1 
ATOM   1469  C  CA    . LEU   A 1  189 ? 32.742  66.239  58.083  1.00 33.24  ? 189 LEU   A CA    1 
ATOM   1470  C  C     . LEU   A 1  189 ? 33.283  67.623  58.434  1.00 41.79  ? 189 LEU   A C     1 
ATOM   1471  O  O     . LEU   A 1  189 ? 34.417  67.758  58.908  1.00 40.43  ? 189 LEU   A O     1 
ATOM   1472  C  CB    . LEU   A 1  189 ? 32.721  66.057  56.565  1.00 27.85  ? 189 LEU   A CB    1 
ATOM   1473  C  CG    . LEU   A 1  189 ? 32.508  64.669  55.934  1.00 30.95  ? 189 LEU   A CG    1 
ATOM   1474  C  CD1   . LEU   A 1  189 ? 32.300  64.852  54.454  1.00 32.79  ? 189 LEU   A CD1   1 
ATOM   1475  C  CD2   . LEU   A 1  189 ? 33.653  63.699  56.192  1.00 22.98  ? 189 LEU   A CD2   1 
ATOM   1476  N  N     . THR   A 1  190 ? 32.491  68.673  58.197  1.00 38.49  ? 190 THR   A N     1 
ATOM   1477  C  CA    . THR   A 1  190 ? 33.037  70.022  58.327  1.00 35.01  ? 190 THR   A CA    1 
ATOM   1478  C  C     . THR   A 1  190 ? 33.047  70.505  59.767  1.00 38.98  ? 190 THR   A C     1 
ATOM   1479  O  O     . THR   A 1  190 ? 33.847  71.382  60.117  1.00 35.92  ? 190 THR   A O     1 
ATOM   1480  C  CB    . THR   A 1  190 ? 32.245  71.002  57.480  1.00 34.30  ? 190 THR   A CB    1 
ATOM   1481  O  OG1   . THR   A 1  190 ? 32.966  72.233  57.397  1.00 27.11  ? 190 THR   A OG1   1 
ATOM   1482  C  CG2   . THR   A 1  190 ? 30.903  71.243  58.129  1.00 30.99  ? 190 THR   A CG2   1 
ATOM   1483  N  N     . THR   A 1  191 ? 32.158  69.965  60.600  1.00 34.97  ? 191 THR   A N     1 
ATOM   1484  C  CA    . THR   A 1  191 ? 32.237  70.244  62.026  1.00 42.43  ? 191 THR   A CA    1 
ATOM   1485  C  C     . THR   A 1  191 ? 33.489  69.620  62.611  1.00 35.57  ? 191 THR   A C     1 
ATOM   1486  O  O     . THR   A 1  191 ? 34.207  70.267  63.378  1.00 48.21  ? 191 THR   A O     1 
ATOM   1487  C  CB    . THR   A 1  191 ? 30.974  69.745  62.756  1.00 38.56  ? 191 THR   A CB    1 
ATOM   1488  O  OG1   . THR   A 1  191 ? 29.854  70.560  62.394  1.00 37.27  ? 191 THR   A OG1   1 
ATOM   1489  C  CG2   . THR   A 1  191 ? 31.141  69.831  64.264  1.00 34.85  ? 191 THR   A CG2   1 
ATOM   1490  N  N     . HIS   A 1  192 ? 33.788  68.378  62.236  1.00 34.77  ? 192 HIS   A N     1 
ATOM   1491  C  CA    . HIS   A 1  192 ? 34.982  67.727  62.759  1.00 39.79  ? 192 HIS   A CA    1 
ATOM   1492  C  C     . HIS   A 1  192 ? 36.240  68.509  62.399  1.00 40.23  ? 192 HIS   A C     1 
ATOM   1493  O  O     . HIS   A 1  192 ? 37.064  68.825  63.259  1.00 48.42  ? 192 HIS   A O     1 
ATOM   1494  C  CB    . HIS   A 1  192 ? 35.087  66.305  62.231  1.00 39.55  ? 192 HIS   A CB    1 
ATOM   1495  C  CG    . HIS   A 1  192 ? 36.471  65.756  62.328  1.00 50.94  ? 192 HIS   A CG    1 
ATOM   1496  N  ND1   . HIS   A 1  192 ? 37.156  65.689  63.523  1.00 43.43  ? 192 HIS   A ND1   1 
ATOM   1497  C  CD2   . HIS   A 1  192 ? 37.318  65.298  61.377  1.00 50.32  ? 192 HIS   A CD2   1 
ATOM   1498  C  CE1   . HIS   A 1  192 ? 38.353  65.177  63.306  1.00 52.05  ? 192 HIS   A CE1   1 
ATOM   1499  N  NE2   . HIS   A 1  192 ? 38.480  64.939  62.012  1.00 52.60  ? 192 HIS   A NE2   1 
ATOM   1500  N  N     . THR   A 1  193 ? 36.400  68.837  61.131  1.00 40.03  ? 193 THR   A N     1 
ATOM   1501  C  CA    . THR   A 1  193 ? 37.603  69.534  60.711  1.00 43.71  ? 193 THR   A CA    1 
ATOM   1502  C  C     . THR   A 1  193 ? 37.691  70.918  61.331  1.00 43.05  ? 193 THR   A C     1 
ATOM   1503  O  O     . THR   A 1  193 ? 38.772  71.335  61.757  1.00 55.19  ? 193 THR   A O     1 
ATOM   1504  C  CB    . THR   A 1  193 ? 37.651  69.607  59.182  1.00 41.97  ? 193 THR   A CB    1 
ATOM   1505  O  OG1   . THR   A 1  193 ? 37.959  68.302  58.671  1.00 36.52  ? 193 THR   A OG1   1 
ATOM   1506  C  CG2   . THR   A 1  193 ? 38.701  70.620  58.709  1.00 50.11  ? 193 THR   A CG2   1 
ATOM   1507  N  N     . THR   A 1  194 ? 36.571  71.632  61.422  1.00 42.86  ? 194 THR   A N     1 
ATOM   1508  C  CA    . THR   A 1  194 ? 36.604  73.024  61.853  1.00 41.37  ? 194 THR   A CA    1 
ATOM   1509  C  C     . THR   A 1  194 ? 36.582  73.207  63.374  1.00 43.24  ? 194 THR   A C     1 
ATOM   1510  O  O     . THR   A 1  194 ? 36.928  74.300  63.848  1.00 36.45  ? 194 THR   A O     1 
ATOM   1511  C  CB    . THR   A 1  194 ? 35.439  73.796  61.225  1.00 32.89  ? 194 THR   A CB    1 
ATOM   1512  O  OG1   . THR   A 1  194 ? 35.470  73.624  59.806  1.00 40.61  ? 194 THR   A OG1   1 
ATOM   1513  C  CG2   . THR   A 1  194 ? 35.554  75.254  61.526  1.00 33.46  ? 194 THR   A CG2   1 
ATOM   1514  N  N     . LEU   A 1  195 ? 36.233  72.169  64.151  1.00 30.92  ? 195 LEU   A N     1 
ATOM   1515  C  CA    . LEU   A 1  195 ? 36.051  72.344  65.593  1.00 31.47  ? 195 LEU   A CA    1 
ATOM   1516  C  C     . LEU   A 1  195 ? 37.205  73.128  66.220  1.00 37.46  ? 195 LEU   A C     1 
ATOM   1517  O  O     . LEU   A 1  195 ? 36.984  74.105  66.943  1.00 47.37  ? 195 LEU   A O     1 
ATOM   1518  C  CB    . LEU   A 1  195 ? 35.877  70.987  66.282  1.00 27.67  ? 195 LEU   A CB    1 
ATOM   1519  C  CG    . LEU   A 1  195 ? 34.919  70.977  67.479  1.00 34.98  ? 195 LEU   A CG    1 
ATOM   1520  C  CD1   . LEU   A 1  195 ? 33.697  71.872  67.241  1.00 32.72  ? 195 LEU   A CD1   1 
ATOM   1521  C  CD2   . LEU   A 1  195 ? 34.447  69.577  67.837  1.00 36.41  ? 195 LEU   A CD2   1 
ATOM   1522  N  N     . GLU   A 1  196 ? 38.443  72.735  65.933  1.00 36.56  ? 196 GLU   A N     1 
ATOM   1523  C  CA    . GLU   A 1  196 ? 39.611  73.341  66.563  1.00 37.31  ? 196 GLU   A CA    1 
ATOM   1524  C  C     . GLU   A 1  196 ? 40.042  74.662  65.925  1.00 39.50  ? 196 GLU   A C     1 
ATOM   1525  O  O     . GLU   A 1  196 ? 40.980  75.286  66.417  1.00 49.41  ? 196 GLU   A O     1 
ATOM   1526  C  CB    . GLU   A 1  196 ? 40.783  72.360  66.545  1.00 41.50  ? 196 GLU   A CB    1 
ATOM   1527  C  CG    . GLU   A 1  196 ? 41.847  72.646  67.588  1.00 72.58  ? 196 GLU   A CG    1 
ATOM   1528  C  CD    . GLU   A 1  196 ? 41.460  72.168  68.982  1.00 81.46  ? 196 GLU   A CD    1 
ATOM   1529  O  OE1   . GLU   A 1  196 ? 40.674  71.197  69.079  1.00 77.25  ? 196 GLU   A OE1   1 
ATOM   1530  O  OE2   . GLU   A 1  196 ? 41.950  72.757  69.975  1.00 76.47  ? 196 GLU   A OE2   1 
ATOM   1531  N  N     . HIS   A 1  197 ? 39.383  75.137  64.880  1.00 43.36  ? 197 HIS   A N     1 
ATOM   1532  C  CA    . HIS   A 1  197 ? 39.776  76.398  64.272  1.00 34.45  ? 197 HIS   A CA    1 
ATOM   1533  C  C     . HIS   A 1  197 ? 38.763  77.513  64.483  1.00 38.43  ? 197 HIS   A C     1 
ATOM   1534  O  O     . HIS   A 1  197 ? 39.066  78.663  64.162  1.00 38.04  ? 197 HIS   A O     1 
ATOM   1535  C  CB    . HIS   A 1  197 ? 40.032  76.209  62.770  1.00 43.48  ? 197 HIS   A CB    1 
ATOM   1536  C  CG    . HIS   A 1  197 ? 41.012  75.115  62.455  1.00 57.45  ? 197 HIS   A CG    1 
ATOM   1537  N  ND1   . HIS   A 1  197 ? 40.963  73.870  63.051  1.00 57.50  ? 197 HIS   A ND1   1 
ATOM   1538  C  CD2   . HIS   A 1  197 ? 42.060  75.078  61.601  1.00 56.92  ? 197 HIS   A CD2   1 
ATOM   1539  C  CE1   . HIS   A 1  197 ? 41.941  73.118  62.580  1.00 55.34  ? 197 HIS   A CE1   1 
ATOM   1540  N  NE2   . HIS   A 1  197 ? 42.623  73.827  61.700  1.00 59.70  ? 197 HIS   A NE2   1 
ATOM   1541  N  N     . SER   A 1  198 ? 37.591  77.216  65.036  1.00 43.33  ? 198 SER   A N     1 
ATOM   1542  C  CA    . SER   A 1  198 ? 36.556  78.207  65.295  1.00 41.09  ? 198 SER   A CA    1 
ATOM   1543  C  C     . SER   A 1  198 ? 36.450  78.475  66.798  1.00 42.54  ? 198 SER   A C     1 
ATOM   1544  O  O     . SER   A 1  198 ? 36.353  77.538  67.603  1.00 48.82  ? 198 SER   A O     1 
ATOM   1545  C  CB    . SER   A 1  198 ? 35.210  77.736  64.727  1.00 39.06  ? 198 SER   A CB    1 
ATOM   1546  O  OG    . SER   A 1  198 ? 34.103  78.478  65.236  1.00 38.02  ? 198 SER   A OG    1 
ATOM   1547  N  N     . ASP   A 1  199 ? 36.445  79.756  67.170  1.00 31.04  ? 199 ASP   A N     1 
ATOM   1548  C  CA    . ASP   A 1  199 ? 36.353  80.135  68.575  1.00 38.02  ? 199 ASP   A CA    1 
ATOM   1549  C  C     . ASP   A 1  199 ? 34.921  80.170  69.106  1.00 39.98  ? 199 ASP   A C     1 
ATOM   1550  O  O     . ASP   A 1  199 ? 34.719  80.035  70.316  1.00 35.55  ? 199 ASP   A O     1 
ATOM   1551  C  CB    . ASP   A 1  199 ? 37.014  81.497  68.773  1.00 37.07  ? 199 ASP   A CB    1 
ATOM   1552  C  CG    . ASP   A 1  199 ? 38.463  81.509  68.301  1.00 45.47  ? 199 ASP   A CG    1 
ATOM   1553  O  OD1   . ASP   A 1  199 ? 39.257  80.725  68.882  1.00 32.54  ? 199 ASP   A OD1   1 
ATOM   1554  O  OD2   . ASP   A 1  199 ? 38.782  82.275  67.344  1.00 30.00  ? 199 ASP   A OD2   1 
ATOM   1555  N  N     . CYS   A 1  200 ? 33.924  80.343  68.242  1.00 39.65  ? 200 CYS   A N     1 
ATOM   1556  C  CA    . CYS   A 1  200 ? 32.560  80.516  68.714  1.00 35.80  ? 200 CYS   A CA    1 
ATOM   1557  C  C     . CYS   A 1  200 ? 31.619  80.369  67.531  1.00 39.26  ? 200 CYS   A C     1 
ATOM   1558  O  O     . CYS   A 1  200 ? 31.755  81.097  66.540  1.00 41.34  ? 200 CYS   A O     1 
ATOM   1559  C  CB    . CYS   A 1  200 ? 32.404  81.883  69.391  1.00 32.94  ? 200 CYS   A CB    1 
ATOM   1560  S  SG    . CYS   A 1  200 ? 30.798  82.230  70.129  1.00 34.66  ? 200 CYS   A SG    1 
ATOM   1561  N  N     . ALA   A 1  201 ? 30.674  79.434  67.599  1.00 28.80  ? 201 ALA   A N     1 
ATOM   1562  C  CA    . ALA   A 1  201 ? 29.832  79.134  66.448  1.00 32.12  ? 201 ALA   A CA    1 
ATOM   1563  C  C     . ALA   A 1  201 ? 28.374  79.388  66.786  1.00 29.38  ? 201 ALA   A C     1 
ATOM   1564  O  O     . ALA   A 1  201 ? 27.871  78.902  67.807  1.00 28.82  ? 201 ALA   A O     1 
ATOM   1565  C  CB    . ALA   A 1  201 ? 30.021  77.687  65.993  1.00 35.21  ? 201 ALA   A CB    1 
ATOM   1566  N  N     . PHE   A 1  202 ? 27.692  80.127  65.922  1.00 30.07  ? 202 PHE   A N     1 
ATOM   1567  C  CA    . PHE   A 1  202 ? 26.264  80.396  66.100  1.00 33.86  ? 202 PHE   A CA    1 
ATOM   1568  C  C     . PHE   A 1  202 ? 25.475  79.563  65.089  1.00 32.40  ? 202 PHE   A C     1 
ATOM   1569  O  O     . PHE   A 1  202 ? 25.361  79.926  63.914  1.00 34.07  ? 202 PHE   A O     1 
ATOM   1570  C  CB    . PHE   A 1  202 ? 25.992  81.886  65.977  1.00 31.21  ? 202 PHE   A CB    1 
ATOM   1571  C  CG    . PHE   A 1  202 ? 26.581  82.688  67.102  1.00 34.39  ? 202 PHE   A CG    1 
ATOM   1572  C  CD1   . PHE   A 1  202 ? 26.065  82.578  68.387  1.00 26.82  ? 202 PHE   A CD1   1 
ATOM   1573  C  CD2   . PHE   A 1  202 ? 27.658  83.538  66.880  1.00 28.35  ? 202 PHE   A CD2   1 
ATOM   1574  C  CE1   . PHE   A 1  202 ? 26.611  83.309  69.419  1.00 31.93  ? 202 PHE   A CE1   1 
ATOM   1575  C  CE2   . PHE   A 1  202 ? 28.207  84.266  67.899  1.00 29.77  ? 202 PHE   A CE2   1 
ATOM   1576  C  CZ    . PHE   A 1  202 ? 27.682  84.160  69.174  1.00 32.37  ? 202 PHE   A CZ    1 
ATOM   1577  N  N     . MET   A 1  203 ? 24.961  78.429  65.555  1.00 28.23  ? 203 MET   A N     1 
ATOM   1578  C  CA    . MET   A 1  203 ? 24.249  77.495  64.699  1.00 34.35  ? 203 MET   A CA    1 
ATOM   1579  C  C     . MET   A 1  203 ? 22.795  77.907  64.543  1.00 34.34  ? 203 MET   A C     1 
ATOM   1580  O  O     . MET   A 1  203 ? 22.102  78.169  65.526  1.00 39.80  ? 203 MET   A O     1 
ATOM   1581  C  CB    . MET   A 1  203 ? 24.311  76.079  65.265  1.00 34.52  ? 203 MET   A CB    1 
ATOM   1582  C  CG    . MET   A 1  203 ? 25.374  75.200  64.642  1.00 31.97  ? 203 MET   A CG    1 
ATOM   1583  S  SD    . MET   A 1  203 ? 24.982  73.478  64.997  1.00 43.32  ? 203 MET   A SD    1 
ATOM   1584  C  CE    . MET   A 1  203 ? 24.688  73.551  66.763  1.00 29.12  ? 203 MET   A CE    1 
ATOM   1585  N  N     . VAL   A 1  204 ? 22.325  77.936  63.310  1.00 32.66  ? 204 VAL   A N     1 
ATOM   1586  C  CA    . VAL   A 1  204 ? 20.950  78.280  63.028  1.00 32.68  ? 204 VAL   A CA    1 
ATOM   1587  C  C     . VAL   A 1  204 ? 20.353  77.124  62.228  1.00 31.80  ? 204 VAL   A C     1 
ATOM   1588  O  O     . VAL   A 1  204 ? 20.725  76.883  61.071  1.00 30.80  ? 204 VAL   A O     1 
ATOM   1589  C  CB    . VAL   A 1  204 ? 20.845  79.637  62.312  1.00 33.26  ? 204 VAL   A CB    1 
ATOM   1590  C  CG1   . VAL   A 1  204 ? 19.442  79.887  61.766  1.00 22.31  ? 204 VAL   A CG1   1 
ATOM   1591  C  CG2   . VAL   A 1  204 ? 21.238  80.743  63.302  1.00 19.31  ? 204 VAL   A CG2   1 
ATOM   1592  N  N     . ASP   A 1  205 ? 19.478  76.368  62.881  1.00 29.45  ? 205 ASP   A N     1 
ATOM   1593  C  CA    . ASP   A 1  205 ? 18.694  75.323  62.246  1.00 23.27  ? 205 ASP   A CA    1 
ATOM   1594  C  C     . ASP   A 1  205 ? 17.637  75.964  61.362  1.00 32.52  ? 205 ASP   A C     1 
ATOM   1595  O  O     . ASP   A 1  205 ? 16.676  76.558  61.870  1.00 28.41  ? 205 ASP   A O     1 
ATOM   1596  C  CB    . ASP   A 1  205 ? 18.043  74.462  63.318  1.00 21.17  ? 205 ASP   A CB    1 
ATOM   1597  C  CG    . ASP   A 1  205 ? 17.557  73.130  62.782  1.00 32.35  ? 205 ASP   A CG    1 
ATOM   1598  O  OD1   . ASP   A 1  205 ? 17.263  73.060  61.570  1.00 33.44  ? 205 ASP   A OD1   1 
ATOM   1599  O  OD2   . ASP   A 1  205 ? 17.462  72.160  63.574  1.00 27.93  ? 205 ASP   A OD2   1 
ATOM   1600  N  N     . ASN   A 1  206 ? 17.811  75.848  60.038  1.00 31.63  ? 206 ASN   A N     1 
ATOM   1601  C  CA    . ASN   A 1  206 ? 16.766  76.237  59.093  1.00 26.13  ? 206 ASN   A CA    1 
ATOM   1602  C  C     . ASN   A 1  206 ? 15.396  75.747  59.544  1.00 28.31  ? 206 ASN   A C     1 
ATOM   1603  O  O     . ASN   A 1  206 ? 14.393  76.392  59.249  1.00 25.41  ? 206 ASN   A O     1 
ATOM   1604  C  CB    . ASN   A 1  206 ? 17.058  75.697  57.699  1.00 21.33  ? 206 ASN   A CB    1 
ATOM   1605  C  CG    . ASN   A 1  206 ? 17.814  76.685  56.844  1.00 26.07  ? 206 ASN   A CG    1 
ATOM   1606  O  OD1   . ASN   A 1  206 ? 17.949  77.848  57.213  1.00 29.34  ? 206 ASN   A OD1   1 
ATOM   1607  N  ND2   . ASN   A 1  206 ? 18.309  76.233  55.689  1.00 19.93  ? 206 ASN   A ND2   1 
ATOM   1608  N  N     . GLU   A 1  207 ? 15.323  74.616  60.258  1.00 25.03  ? 207 GLU   A N     1 
ATOM   1609  C  CA    . GLU   A 1  207 ? 14.026  74.180  60.768  1.00 28.87  ? 207 GLU   A CA    1 
ATOM   1610  C  C     . GLU   A 1  207 ? 13.417  75.240  61.690  1.00 34.28  ? 207 GLU   A C     1 
ATOM   1611  O  O     . GLU   A 1  207 ? 12.249  75.627  61.536  1.00 33.73  ? 207 GLU   A O     1 
ATOM   1612  C  CB    . GLU   A 1  207 ? 14.158  72.839  61.489  1.00 30.52  ? 207 GLU   A CB    1 
ATOM   1613  C  CG    . GLU   A 1  207 ? 12.868  72.391  62.156  1.00 32.91  ? 207 GLU   A CG    1 
ATOM   1614  C  CD    . GLU   A 1  207 ? 12.975  71.054  62.912  1.00 42.23  ? 207 GLU   A CD    1 
ATOM   1615  O  OE1   . GLU   A 1  207 ? 13.420  71.050  64.076  1.00 32.66  ? 207 GLU   A OE1   1 
ATOM   1616  O  OE2   . GLU   A 1  207 ? 12.580  70.004  62.351  1.00 53.37  ? 207 GLU   A OE2   1 
ATOM   1617  N  N     . ALA   A 1  208 ? 14.207  75.748  62.639  1.00 28.20  ? 208 ALA   A N     1 
ATOM   1618  C  CA    . ALA   A 1  208 ? 13.665  76.712  63.583  1.00 23.81  ? 208 ALA   A CA    1 
ATOM   1619  C  C     . ALA   A 1  208 ? 13.246  77.997  62.875  1.00 32.94  ? 208 ALA   A C     1 
ATOM   1620  O  O     . ALA   A 1  208 ? 12.177  78.554  63.159  1.00 28.96  ? 208 ALA   A O     1 
ATOM   1621  C  CB    . ALA   A 1  208 ? 14.685  76.988  64.689  1.00 24.81  ? 208 ALA   A CB    1 
ATOM   1622  N  N     . ILE   A 1  209 ? 14.078  78.493  61.955  1.00 29.07  ? 209 ILE   A N     1 
ATOM   1623  C  CA    . ILE   A 1  209 ? 13.738  79.728  61.269  1.00 20.90  ? 209 ILE   A CA    1 
ATOM   1624  C  C     . ILE   A 1  209 ? 12.442  79.549  60.522  1.00 31.18  ? 209 ILE   A C     1 
ATOM   1625  O  O     . ILE   A 1  209 ? 11.611  80.463  60.444  1.00 33.15  ? 209 ILE   A O     1 
ATOM   1626  C  CB    . ILE   A 1  209 ? 14.858  80.158  60.309  1.00 25.40  ? 209 ILE   A CB    1 
ATOM   1627  C  CG1   . ILE   A 1  209 ? 16.122  80.484  61.070  1.00 28.35  ? 209 ILE   A CG1   1 
ATOM   1628  C  CG2   . ILE   A 1  209 ? 14.424  81.389  59.571  1.00 34.32  ? 209 ILE   A CG2   1 
ATOM   1629  C  CD1   . ILE   A 1  209 ? 15.851  81.014  62.440  1.00 31.97  ? 209 ILE   A CD1   1 
ATOM   1630  N  N     . TYR   A 1  210 ? 12.251  78.357  59.967  1.00 32.66  ? 210 TYR   A N     1 
ATOM   1631  C  CA    . TYR   A 1  210 ? 11.127  78.099  59.080  1.00 33.06  ? 210 TYR   A CA    1 
ATOM   1632  C  C     . TYR   A 1  210 ? 9.806   78.189  59.829  1.00 34.36  ? 210 TYR   A C     1 
ATOM   1633  O  O     . TYR   A 1  210 ? 8.854   78.816  59.348  1.00 34.46  ? 210 TYR   A O     1 
ATOM   1634  C  CB    . TYR   A 1  210 ? 11.306  76.723  58.454  1.00 28.22  ? 210 TYR   A CB    1 
ATOM   1635  C  CG    . TYR   A 1  210 ? 10.442  76.438  57.269  1.00 30.89  ? 210 TYR   A CG    1 
ATOM   1636  C  CD1   . TYR   A 1  210 ? 10.799  76.880  56.003  1.00 31.44  ? 210 TYR   A CD1   1 
ATOM   1637  C  CD2   . TYR   A 1  210 ? 9.285   75.689  57.408  1.00 34.55  ? 210 TYR   A CD2   1 
ATOM   1638  C  CE1   . TYR   A 1  210 ? 10.015  76.593  54.904  1.00 37.76  ? 210 TYR   A CE1   1 
ATOM   1639  C  CE2   . TYR   A 1  210 ? 8.490   75.403  56.329  1.00 33.71  ? 210 TYR   A CE2   1 
ATOM   1640  C  CZ    . TYR   A 1  210 ? 8.853   75.851  55.075  1.00 38.59  ? 210 TYR   A CZ    1 
ATOM   1641  O  OH    . TYR   A 1  210 ? 8.040   75.547  54.001  1.00 33.84  ? 210 TYR   A OH    1 
ATOM   1642  N  N     . ASP   A 1  211 ? 9.736   77.564  61.012  1.00 27.36  ? 211 ASP   A N     1 
ATOM   1643  C  CA    . ASP   A 1  211 ? 8.503   77.560  61.796  1.00 34.58  ? 211 ASP   A CA    1 
ATOM   1644  C  C     . ASP   A 1  211 ? 8.204   78.925  62.379  1.00 32.97  ? 211 ASP   A C     1 
ATOM   1645  O  O     . ASP   A 1  211 ? 7.037   79.319  62.462  1.00 41.88  ? 211 ASP   A O     1 
ATOM   1646  C  CB    . ASP   A 1  211 ? 8.578   76.532  62.923  1.00 39.86  ? 211 ASP   A CB    1 
ATOM   1647  C  CG    . ASP   A 1  211 ? 8.464   75.119  62.423  1.00 53.03  ? 211 ASP   A CG    1 
ATOM   1648  O  OD1   . ASP   A 1  211 ? 8.216   74.929  61.205  1.00 50.10  ? 211 ASP   A OD1   1 
ATOM   1649  O  OD2   . ASP   A 1  211 ? 8.629   74.201  63.253  1.00 62.91  ? 211 ASP   A OD2   1 
ATOM   1650  N  N     . ILE   A 1  212 ? 9.235   79.641  62.829  1.00 27.30  ? 212 ILE   A N     1 
ATOM   1651  C  CA    . ILE   A 1  212 ? 9.034   81.012  63.283  1.00 30.29  ? 212 ILE   A CA    1 
ATOM   1652  C  C     . ILE   A 1  212 ? 8.356   81.822  62.183  1.00 41.88  ? 212 ILE   A C     1 
ATOM   1653  O  O     . ILE   A 1  212 ? 7.390   82.563  62.432  1.00 43.02  ? 212 ILE   A O     1 
ATOM   1654  C  CB    . ILE   A 1  212 ? 10.379  81.622  63.713  1.00 27.27  ? 212 ILE   A CB    1 
ATOM   1655  C  CG1   . ILE   A 1  212 ? 10.742  81.136  65.108  1.00 27.62  ? 212 ILE   A CG1   1 
ATOM   1656  C  CG2   . ILE   A 1  212 ? 10.339  83.135  63.647  1.00 22.48  ? 212 ILE   A CG2   1 
ATOM   1657  C  CD1   . ILE   A 1  212 ? 12.218  81.048  65.353  1.00 23.00  ? 212 ILE   A CD1   1 
ATOM   1658  N  N     . CYS   A 1  213 ? 8.824   81.643  60.937  1.00 38.57  ? 213 CYS   A N     1 
ATOM   1659  C  CA    . CYS   A 1  213 ? 8.247   82.314  59.775  1.00 32.26  ? 213 CYS   A CA    1 
ATOM   1660  C  C     . CYS   A 1  213 ? 6.802   81.881  59.507  1.00 37.34  ? 213 CYS   A C     1 
ATOM   1661  O  O     . CYS   A 1  213 ? 5.969   82.701  59.104  1.00 36.10  ? 213 CYS   A O     1 
ATOM   1662  C  CB    . CYS   A 1  213 ? 9.117   82.038  58.552  1.00 33.57  ? 213 CYS   A CB    1 
ATOM   1663  S  SG    . CYS   A 1  213 ? 10.685  82.933  58.504  1.00 42.00  ? 213 CYS   A SG    1 
ATOM   1664  N  N     . ARG   A 1  214 ? 6.485   80.599  59.676  1.00 30.10  ? 214 ARG   A N     1 
ATOM   1665  C  CA    . ARG   A 1  214 ? 5.093   80.188  59.505  1.00 39.79  ? 214 ARG   A CA    1 
ATOM   1666  C  C     . ARG   A 1  214 ? 4.253   80.649  60.681  1.00 44.41  ? 214 ARG   A C     1 
ATOM   1667  O  O     . ARG   A 1  214 ? 3.215   81.294  60.501  1.00 49.76  ? 214 ARG   A O     1 
ATOM   1668  C  CB    . ARG   A 1  214 ? 4.967   78.672  59.367  1.00 47.63  ? 214 ARG   A CB    1 
ATOM   1669  C  CG    . ARG   A 1  214 ? 5.364   78.075  58.045  1.00 38.28  ? 214 ARG   A CG    1 
ATOM   1670  C  CD    . ARG   A 1  214 ? 5.995   76.709  58.334  1.00 41.83  ? 214 ARG   A CD    1 
ATOM   1671  N  NE    . ARG   A 1  214 ? 5.143   75.580  57.975  1.00 47.20  ? 214 ARG   A NE    1 
ATOM   1672  C  CZ    . ARG   A 1  214 ? 5.323   74.335  58.402  1.00 50.55  ? 214 ARG   A CZ    1 
ATOM   1673  N  NH1   . ARG   A 1  214 ? 6.299   74.022  59.244  1.00 38.50  ? 214 ARG   A NH1   1 
ATOM   1674  N  NH2   . ARG   A 1  214 ? 4.494   73.383  57.986  1.00 45.90  ? 214 ARG   A NH2   1 
ATOM   1675  N  N     . ARG   A 1  215 ? 4.702   80.338  61.901  1.00 42.37  ? 215 ARG   A N     1 
ATOM   1676  C  CA    . ARG   A 1  215 ? 3.868   80.552  63.076  1.00 41.71  ? 215 ARG   A CA    1 
ATOM   1677  C  C     . ARG   A 1  215 ? 3.681   82.033  63.382  1.00 43.44  ? 215 ARG   A C     1 
ATOM   1678  O  O     . ARG   A 1  215 ? 2.569   82.459  63.709  1.00 56.69  ? 215 ARG   A O     1 
ATOM   1679  C  CB    . ARG   A 1  215 ? 4.461   79.841  64.287  1.00 38.01  ? 215 ARG   A CB    1 
ATOM   1680  C  CG    . ARG   A 1  215 ? 4.272   78.345  64.339  1.00 32.88  ? 215 ARG   A CG    1 
ATOM   1681  C  CD    . ARG   A 1  215 ? 4.753   77.860  65.731  1.00 68.12  ? 215 ARG   A CD    1 
ATOM   1682  N  NE    . ARG   A 1  215 ? 5.761   78.758  66.305  1.00 48.75  ? 215 ARG   A NE    1 
ATOM   1683  C  CZ    . ARG   A 1  215 ? 7.074   78.547  66.259  1.00 48.82  ? 215 ARG   A CZ    1 
ATOM   1684  N  NH1   . ARG   A 1  215 ? 7.584   77.417  65.787  1.00 47.52  ? 215 ARG   A NH1   1 
ATOM   1685  N  NH2   . ARG   A 1  215 ? 7.900   79.502  66.675  1.00 47.29  ? 215 ARG   A NH2   1 
ATOM   1686  N  N     . ASN   A 1  216 ? 4.740   82.833  63.312  1.00 33.67  ? 216 ASN   A N     1 
ATOM   1687  C  CA    . ASN   A 1  216 ? 4.640   84.203  63.789  1.00 32.89  ? 216 ASN   A CA    1 
ATOM   1688  C  C     . ASN   A 1  216 ? 4.613   85.231  62.679  1.00 42.48  ? 216 ASN   A C     1 
ATOM   1689  O  O     . ASN   A 1  216 ? 4.288   86.389  62.949  1.00 37.76  ? 216 ASN   A O     1 
ATOM   1690  C  CB    . ASN   A 1  216 ? 5.789   84.518  64.749  1.00 34.68  ? 216 ASN   A CB    1 
ATOM   1691  C  CG    . ASN   A 1  216 ? 5.839   83.546  65.900  1.00 31.83  ? 216 ASN   A CG    1 
ATOM   1692  O  OD1   . ASN   A 1  216 ? 4.808   83.121  66.394  1.00 44.72  ? 216 ASN   A OD1   1 
ATOM   1693  N  ND2   . ASN   A 1  216 ? 7.028   83.162  66.307  1.00 34.75  ? 216 ASN   A ND2   1 
ATOM   1694  N  N     . LEU   A 1  217 ? 4.930   84.844  61.447  1.00 45.35  ? 217 LEU   A N     1 
ATOM   1695  C  CA    . LEU   A 1  217 ? 4.843   85.739  60.303  1.00 42.69  ? 217 LEU   A CA    1 
ATOM   1696  C  C     . LEU   A 1  217 ? 3.758   85.326  59.318  1.00 41.87  ? 217 LEU   A C     1 
ATOM   1697  O  O     . LEU   A 1  217 ? 3.584   85.988  58.292  1.00 38.86  ? 217 LEU   A O     1 
ATOM   1698  C  CB    . LEU   A 1  217 ? 6.198   85.818  59.591  1.00 38.62  ? 217 LEU   A CB    1 
ATOM   1699  C  CG    . LEU   A 1  217 ? 7.265   86.413  60.500  1.00 46.46  ? 217 LEU   A CG    1 
ATOM   1700  C  CD1   . LEU   A 1  217 ? 8.599   86.602  59.791  1.00 38.32  ? 217 LEU   A CD1   1 
ATOM   1701  C  CD2   . LEU   A 1  217 ? 6.744   87.723  61.040  1.00 36.54  ? 217 LEU   A CD2   1 
ATOM   1702  N  N     . ASP   A 1  218 ? 3.021   84.255  59.608  1.00 45.54  ? 218 ASP   A N     1 
ATOM   1703  C  CA    . ASP   A 1  218 ? 1.925   83.792  58.750  1.00 48.96  ? 218 ASP   A CA    1 
ATOM   1704  C  C     . ASP   A 1  218 ? 2.376   83.599  57.302  1.00 35.21  ? 218 ASP   A C     1 
ATOM   1705  O  O     . ASP   A 1  218 ? 1.647   83.907  56.361  1.00 46.67  ? 218 ASP   A O     1 
ATOM   1706  C  CB    . ASP   A 1  218 ? 0.727   84.749  58.819  1.00 43.67  ? 218 ASP   A CB    1 
ATOM   1707  C  CG    . ASP   A 1  218 ? 0.404   85.194  60.247  1.00 52.46  ? 218 ASP   A CG    1 
ATOM   1708  O  OD1   . ASP   A 1  218 ? 0.346   84.329  61.158  1.00 47.16  ? 218 ASP   A OD1   1 
ATOM   1709  O  OD2   . ASP   A 1  218 ? 0.218   86.423  60.451  1.00 50.03  ? 218 ASP   A OD2   1 
ATOM   1710  N  N     . ILE   A 1  219 ? 3.583   83.084  57.113  1.00 33.82  ? 219 ILE   A N     1 
ATOM   1711  C  CA    . ILE   A 1  219 ? 4.114   82.797  55.781  1.00 44.88  ? 219 ILE   A CA    1 
ATOM   1712  C  C     . ILE   A 1  219 ? 3.849   81.324  55.469  1.00 36.81  ? 219 ILE   A C     1 
ATOM   1713  O  O     . ILE   A 1  219 ? 4.398   80.431  56.125  1.00 37.86  ? 219 ILE   A O     1 
ATOM   1714  C  CB    . ILE   A 1  219 ? 5.612   83.122  55.675  1.00 48.88  ? 219 ILE   A CB    1 
ATOM   1715  C  CG1   . ILE   A 1  219 ? 5.935   84.452  56.351  1.00 43.50  ? 219 ILE   A CG1   1 
ATOM   1716  C  CG2   . ILE   A 1  219 ? 6.036   83.204  54.210  1.00 38.87  ? 219 ILE   A CG2   1 
ATOM   1717  C  CD1   . ILE   A 1  219 ? 5.898   85.606  55.404  1.00 35.33  ? 219 ILE   A CD1   1 
ATOM   1718  N  N     . GLU   A 1  220 ? 2.995   81.078  54.467  1.00 45.11  ? 220 GLU   A N     1 
ATOM   1719  C  CA    . GLU   A 1  220 ? 2.638   79.745  53.977  1.00 45.45  ? 220 GLU   A CA    1 
ATOM   1720  C  C     . GLU   A 1  220 ? 3.852   78.836  53.806  1.00 47.59  ? 220 GLU   A C     1 
ATOM   1721  O  O     . GLU   A 1  220 ? 4.009   77.841  54.524  1.00 41.87  ? 220 GLU   A O     1 
ATOM   1722  C  CB    . GLU   A 1  220 ? 1.913   79.860  52.633  1.00 54.69  ? 220 GLU   A CB    1 
ATOM   1723  C  CG    . GLU   A 1  220 ? 0.564   80.553  52.681  1.00 52.62  ? 220 GLU   A CG    1 
ATOM   1724  C  CD    . GLU   A 1  220 ? -0.544  79.601  53.071  1.00 63.13  ? 220 GLU   A CD    1 
ATOM   1725  O  OE1   . GLU   A 1  220 ? -0.858  78.711  52.259  1.00 63.90  ? 220 GLU   A OE1   1 
ATOM   1726  O  OE2   . GLU   A 1  220 ? -1.093  79.728  54.190  1.00 70.10  ? 220 GLU   A OE2   1 
ATOM   1727  N  N     . ARG   A 1  221 ? 4.710   79.164  52.842  1.00 43.02  ? 221 ARG   A N     1 
ATOM   1728  C  CA    . ARG   A 1  221 ? 5.896   78.367  52.548  1.00 37.34  ? 221 ARG   A CA    1 
ATOM   1729  C  C     . ARG   A 1  221 ? 7.085   79.316  52.522  1.00 34.75  ? 221 ARG   A C     1 
ATOM   1730  O  O     . ARG   A 1  221 ? 7.467   79.828  51.463  1.00 39.15  ? 221 ARG   A O     1 
ATOM   1731  C  CB    . ARG   A 1  221 ? 5.716   77.592  51.243  1.00 34.37  ? 221 ARG   A CB    1 
ATOM   1732  C  CG    . ARG   A 1  221 ? 7.012   77.133  50.574  1.00 52.79  ? 221 ARG   A CG    1 
ATOM   1733  C  CD    . ARG   A 1  221 ? 7.571   75.874  51.193  1.00 38.91  ? 221 ARG   A CD    1 
ATOM   1734  N  NE    . ARG   A 1  221 ? 8.691   75.308  50.445  1.00 38.12  ? 221 ARG   A NE    1 
ATOM   1735  C  CZ    . ARG   A 1  221 ? 9.951   75.727  50.520  1.00 45.34  ? 221 ARG   A CZ    1 
ATOM   1736  N  NH1   . ARG   A 1  221 ? 10.287  76.810  51.198  1.00 46.36  ? 221 ARG   A NH1   1 
ATOM   1737  N  NH2   . ARG   A 1  221 ? 10.902  75.041  49.896  1.00 47.64  ? 221 ARG   A NH2   1 
ATOM   1738  N  N     . PRO   A 1  222 ? 7.697   79.573  53.676  1.00 40.38  ? 222 PRO   A N     1 
ATOM   1739  C  CA    . PRO   A 1  222 ? 8.827   80.512  53.729  1.00 36.86  ? 222 PRO   A CA    1 
ATOM   1740  C  C     . PRO   A 1  222 ? 9.881   80.192  52.686  1.00 33.35  ? 222 PRO   A C     1 
ATOM   1741  O  O     . PRO   A 1  222 ? 10.215  79.032  52.448  1.00 35.61  ? 222 PRO   A O     1 
ATOM   1742  C  CB    . PRO   A 1  222 ? 9.379   80.326  55.144  1.00 35.23  ? 222 PRO   A CB    1 
ATOM   1743  C  CG    . PRO   A 1  222 ? 8.252   79.748  55.937  1.00 37.47  ? 222 PRO   A CG    1 
ATOM   1744  C  CD    . PRO   A 1  222 ? 7.417   78.950  54.984  1.00 39.73  ? 222 PRO   A CD    1 
ATOM   1745  N  N     . THR   A 1  223 ? 10.410  81.233  52.066  1.00 39.41  ? 223 THR   A N     1 
ATOM   1746  C  CA    . THR   A 1  223 ? 11.497  81.108  51.106  1.00 35.63  ? 223 THR   A CA    1 
ATOM   1747  C  C     . THR   A 1  223 ? 12.821  81.457  51.788  1.00 39.19  ? 223 THR   A C     1 
ATOM   1748  O  O     . THR   A 1  223 ? 12.879  81.760  52.984  1.00 39.68  ? 223 THR   A O     1 
ATOM   1749  C  CB    . THR   A 1  223 ? 11.263  82.029  49.903  1.00 39.16  ? 223 THR   A CB    1 
ATOM   1750  O  OG1   . THR   A 1  223 ? 11.518  83.390  50.292  1.00 42.60  ? 223 THR   A OG1   1 
ATOM   1751  C  CG2   . THR   A 1  223 ? 9.829   81.911  49.405  1.00 28.99  ? 223 THR   A CG2   1 
ATOM   1752  N  N     . TYR   A 1  224 ? 13.897  81.445  51.002  1.00 28.94  ? 224 TYR   A N     1 
ATOM   1753  C  CA    . TYR   A 1  224 ? 15.184  81.889  51.519  1.00 26.84  ? 224 TYR   A CA    1 
ATOM   1754  C  C     . TYR   A 1  224 ? 15.181  83.386  51.864  1.00 39.67  ? 224 TYR   A C     1 
ATOM   1755  O  O     . TYR   A 1  224 ? 15.879  83.805  52.795  1.00 40.20  ? 224 TYR   A O     1 
ATOM   1756  C  CB    . TYR   A 1  224 ? 16.287  81.564  50.513  1.00 23.47  ? 224 TYR   A CB    1 
ATOM   1757  C  CG    . TYR   A 1  224 ? 16.694  80.108  50.476  1.00 22.55  ? 224 TYR   A CG    1 
ATOM   1758  C  CD1   . TYR   A 1  224 ? 16.668  79.334  51.626  1.00 23.70  ? 224 TYR   A CD1   1 
ATOM   1759  C  CD2   . TYR   A 1  224 ? 17.128  79.518  49.296  1.00 23.42  ? 224 TYR   A CD2   1 
ATOM   1760  C  CE1   . TYR   A 1  224 ? 17.047  78.007  51.610  1.00 21.22  ? 224 TYR   A CE1   1 
ATOM   1761  C  CE2   . TYR   A 1  224 ? 17.504  78.182  49.251  1.00 24.40  ? 224 TYR   A CE2   1 
ATOM   1762  C  CZ    . TYR   A 1  224 ? 17.463  77.426  50.419  1.00 34.44  ? 224 TYR   A CZ    1 
ATOM   1763  O  OH    . TYR   A 1  224 ? 17.842  76.092  50.406  1.00 33.58  ? 224 TYR   A OH    1 
ATOM   1764  N  N     . THR   A 1  225 ? 14.400  84.216  51.168  1.00 36.13  ? 225 THR   A N     1 
ATOM   1765  C  CA    . THR   A 1  225 ? 14.421  85.628  51.548  1.00 40.02  ? 225 THR   A CA    1 
ATOM   1766  C  C     . THR   A 1  225 ? 13.723  85.855  52.887  1.00 39.96  ? 225 THR   A C     1 
ATOM   1767  O  O     . THR   A 1  225 ? 14.169  86.693  53.677  1.00 40.47  ? 225 THR   A O     1 
ATOM   1768  C  CB    . THR   A 1  225 ? 13.818  86.522  50.457  1.00 39.05  ? 225 THR   A CB    1 
ATOM   1769  O  OG1   . THR   A 1  225 ? 12.440  86.202  50.282  1.00 59.73  ? 225 THR   A OG1   1 
ATOM   1770  C  CG2   . THR   A 1  225 ? 14.558  86.326  49.134  1.00 37.69  ? 225 THR   A CG2   1 
ATOM   1771  N  N     . ASN   A 1  226 ? 12.638  85.130  53.180  1.00 40.00  ? 226 ASN   A N     1 
ATOM   1772  C  CA    . ASN   A 1  226 ? 12.089  85.203  54.536  1.00 28.48  ? 226 ASN   A CA    1 
ATOM   1773  C  C     . ASN   A 1  226 ? 13.128  84.738  55.545  1.00 30.43  ? 226 ASN   A C     1 
ATOM   1774  O  O     . ASN   A 1  226 ? 13.518  85.478  56.453  1.00 33.51  ? 226 ASN   A O     1 
ATOM   1775  C  CB    . ASN   A 1  226 ? 10.815  84.362  54.670  1.00 35.49  ? 226 ASN   A CB    1 
ATOM   1776  C  CG    . ASN   A 1  226 ? 9.811   84.614  53.549  1.00 40.19  ? 226 ASN   A CG    1 
ATOM   1777  O  OD1   . ASN   A 1  226 ? 9.409   83.680  52.823  1.00 33.27  ? 226 ASN   A OD1   1 
ATOM   1778  N  ND2   . ASN   A 1  226 ? 9.397   85.874  53.404  1.00 28.94  ? 226 ASN   A ND2   1 
ATOM   1779  N  N     . LEU   A 1  227 ? 13.620  83.512  55.373  1.00 32.51  ? 227 LEU   A N     1 
ATOM   1780  C  CA    . LEU   A 1  227 ? 14.593  82.967  56.307  1.00 29.03  ? 227 LEU   A CA    1 
ATOM   1781  C  C     . LEU   A 1  227 ? 15.750  83.926  56.532  1.00 36.10  ? 227 LEU   A C     1 
ATOM   1782  O  O     . LEU   A 1  227 ? 16.199  84.101  57.670  1.00 33.11  ? 227 LEU   A O     1 
ATOM   1783  C  CB    . LEU   A 1  227 ? 15.124  81.625  55.801  1.00 29.34  ? 227 LEU   A CB    1 
ATOM   1784  C  CG    . LEU   A 1  227 ? 14.129  80.515  55.489  1.00 29.46  ? 227 LEU   A CG    1 
ATOM   1785  C  CD1   . LEU   A 1  227 ? 14.867  79.198  55.442  1.00 20.32  ? 227 LEU   A CD1   1 
ATOM   1786  C  CD2   . LEU   A 1  227 ? 13.010  80.511  56.521  1.00 27.97  ? 227 LEU   A CD2   1 
ATOM   1787  N  N     . ASN   A 1  228 ? 16.250  84.557  55.455  1.00 34.14  ? 228 ASN   A N     1 
ATOM   1788  C  CA    . ASN   A 1  228 ? 17.485  85.333  55.543  1.00 30.08  ? 228 ASN   A CA    1 
ATOM   1789  C  C     . ASN   A 1  228 ? 17.266  86.696  56.178  1.00 33.78  ? 228 ASN   A C     1 
ATOM   1790  O  O     . ASN   A 1  228 ? 18.160  87.208  56.865  1.00 34.24  ? 228 ASN   A O     1 
ATOM   1791  C  CB    . ASN   A 1  228 ? 18.124  85.503  54.158  1.00 34.31  ? 228 ASN   A CB    1 
ATOM   1792  C  CG    . ASN   A 1  228 ? 18.753  84.210  53.625  1.00 32.26  ? 228 ASN   A CG    1 
ATOM   1793  O  OD1   . ASN   A 1  228 ? 19.055  83.276  54.377  1.00 30.89  ? 228 ASN   A OD1   1 
ATOM   1794  N  ND2   . ASN   A 1  228 ? 18.951  84.161  52.317  1.00 33.68  ? 228 ASN   A ND2   1 
ATOM   1795  N  N     . ARG   A 1  229 ? 16.098  87.299  55.975  1.00 29.81  ? 229 ARG   A N     1 
ATOM   1796  C  CA    . ARG   A 1  229 ? 15.788  88.528  56.697  1.00 30.03  ? 229 ARG   A CA    1 
ATOM   1797  C  C     . ARG   A 1  229 ? 15.751  88.286  58.205  1.00 34.46  ? 229 ARG   A C     1 
ATOM   1798  O  O     . ARG   A 1  229 ? 16.335  89.054  58.975  1.00 40.45  ? 229 ARG   A O     1 
ATOM   1799  C  CB    . ARG   A 1  229 ? 14.471  89.106  56.208  1.00 28.40  ? 229 ARG   A CB    1 
ATOM   1800  C  CG    . ARG   A 1  229 ? 14.553  89.604  54.791  1.00 44.15  ? 229 ARG   A CG    1 
ATOM   1801  C  CD    . ARG   A 1  229 ? 13.589  90.743  54.562  1.00 45.12  ? 229 ARG   A CD    1 
ATOM   1802  N  NE    . ARG   A 1  229 ? 14.063  91.572  53.473  1.00 48.33  ? 229 ARG   A NE    1 
ATOM   1803  C  CZ    . ARG   A 1  229 ? 13.477  91.653  52.293  1.00 50.26  ? 229 ARG   A CZ    1 
ATOM   1804  N  NH1   . ARG   A 1  229 ? 12.334  91.024  52.051  1.00 38.92  ? 229 ARG   A NH1   1 
ATOM   1805  N  NH2   . ARG   A 1  229 ? 14.048  92.394  51.342  1.00 43.40  ? 229 ARG   A NH2   1 
ATOM   1806  N  N     . LEU   A 1  230 ? 15.087  87.212  58.648  1.00 26.79  ? 230 LEU   A N     1 
ATOM   1807  C  CA    . LEU   A 1  230 ? 15.102  86.884  60.072  1.00 27.54  ? 230 LEU   A CA    1 
ATOM   1808  C  C     . LEU   A 1  230 ? 16.513  86.591  60.559  1.00 33.16  ? 230 LEU   A C     1 
ATOM   1809  O  O     . LEU   A 1  230 ? 16.906  87.022  61.652  1.00 29.61  ? 230 LEU   A O     1 
ATOM   1810  C  CB    . LEU   A 1  230 ? 14.189  85.696  60.361  1.00 30.52  ? 230 LEU   A CB    1 
ATOM   1811  C  CG    . LEU   A 1  230 ? 13.807  85.552  61.821  1.00 24.47  ? 230 LEU   A CG    1 
ATOM   1812  C  CD1   . LEU   A 1  230 ? 13.217  86.855  62.331  1.00 20.60  ? 230 LEU   A CD1   1 
ATOM   1813  C  CD2   . LEU   A 1  230 ? 12.838  84.427  61.959  1.00 24.09  ? 230 LEU   A CD2   1 
ATOM   1814  N  N     . ILE   A 1  231 ? 17.296  85.860  59.760  1.00 34.30  ? 231 ILE   A N     1 
ATOM   1815  C  CA    . ILE   A 1  231 ? 18.667  85.578  60.160  1.00 30.50  ? 231 ILE   A CA    1 
ATOM   1816  C  C     . ILE   A 1  231 ? 19.469  86.863  60.224  1.00 34.81  ? 231 ILE   A C     1 
ATOM   1817  O  O     . ILE   A 1  231 ? 20.377  86.998  61.053  1.00 35.91  ? 231 ILE   A O     1 
ATOM   1818  C  CB    . ILE   A 1  231 ? 19.323  84.569  59.208  1.00 36.28  ? 231 ILE   A CB    1 
ATOM   1819  C  CG1   . ILE   A 1  231 ? 18.579  83.230  59.239  1.00 29.17  ? 231 ILE   A CG1   1 
ATOM   1820  C  CG2   . ILE   A 1  231 ? 20.811  84.398  59.571  1.00 24.80  ? 231 ILE   A CG2   1 
ATOM   1821  C  CD1   . ILE   A 1  231 ? 19.331  82.168  58.467  1.00 23.83  ? 231 ILE   A CD1   1 
ATOM   1822  N  N     . SER   A 1  232 ? 19.159  87.819  59.344  1.00 35.68  ? 232 SER   A N     1 
ATOM   1823  C  CA    . SER   A 1  232 ? 19.840  89.109  59.357  1.00 31.22  ? 232 SER   A CA    1 
ATOM   1824  C  C     . SER   A 1  232 ? 19.614  89.856  60.660  1.00 39.07  ? 232 SER   A C     1 
ATOM   1825  O  O     . SER   A 1  232 ? 20.504  90.580  61.119  1.00 39.32  ? 232 SER   A O     1 
ATOM   1826  C  CB    . SER   A 1  232 ? 19.359  89.959  58.189  1.00 44.05  ? 232 SER   A CB    1 
ATOM   1827  O  OG    . SER   A 1  232 ? 20.346  90.033  57.180  1.00 51.15  ? 232 SER   A OG    1 
ATOM   1828  N  N     . GLN   A 1  233 ? 18.437  89.693  61.271  1.00 36.27  ? 233 GLN   A N     1 
ATOM   1829  C  CA    . GLN   A 1  233 ? 18.165  90.345  62.547  1.00 38.24  ? 233 GLN   A CA    1 
ATOM   1830  C  C     . GLN   A 1  233 ? 18.915  89.664  63.690  1.00 36.05  ? 233 GLN   A C     1 
ATOM   1831  O  O     . GLN   A 1  233 ? 19.645  90.314  64.441  1.00 41.02  ? 233 GLN   A O     1 
ATOM   1832  C  CB    . GLN   A 1  233 ? 16.664  90.346  62.825  1.00 40.64  ? 233 GLN   A CB    1 
ATOM   1833  C  CG    . GLN   A 1  233 ? 15.843  91.017  61.787  1.00 34.75  ? 233 GLN   A CG    1 
ATOM   1834  C  CD    . GLN   A 1  233 ? 15.529  92.420  62.169  1.00 47.71  ? 233 GLN   A CD    1 
ATOM   1835  O  OE1   . GLN   A 1  233 ? 14.522  92.683  62.831  1.00 57.04  ? 233 GLN   A OE1   1 
ATOM   1836  N  NE2   . GLN   A 1  233 ? 16.394  93.342  61.776  1.00 45.83  ? 233 GLN   A NE2   1 
ATOM   1837  N  N     . ILE   A 1  234 ? 18.716  88.358  63.871  1.00 32.72  ? 234 ILE   A N     1 
ATOM   1838  C  CA    . ILE   A 1  234 ? 19.479  87.661  64.903  1.00 37.91  ? 234 ILE   A CA    1 
ATOM   1839  C  C     . ILE   A 1  234 ? 20.951  88.046  64.777  1.00 35.13  ? 234 ILE   A C     1 
ATOM   1840  O  O     . ILE   A 1  234 ? 21.562  88.533  65.734  1.00 33.70  ? 234 ILE   A O     1 
ATOM   1841  C  CB    . ILE   A 1  234 ? 19.257  86.130  64.824  1.00 40.04  ? 234 ILE   A CB    1 
ATOM   1842  C  CG1   . ILE   A 1  234 ? 17.828  85.734  65.193  1.00 24.96  ? 234 ILE   A CG1   1 
ATOM   1843  C  CG2   . ILE   A 1  234 ? 20.148  85.364  65.795  1.00 20.56  ? 234 ILE   A CG2   1 
ATOM   1844  C  CD1   . ILE   A 1  234 ? 16.779  86.595  64.606  1.00 27.45  ? 234 ILE   A CD1   1 
ATOM   1845  N  N     . VAL   A 1  235 ? 21.513  87.922  63.562  1.00 37.85  ? 235 VAL   A N     1 
ATOM   1846  C  CA    . VAL   A 1  235 ? 22.944  88.186  63.359  1.00 38.17  ? 235 VAL   A CA    1 
ATOM   1847  C  C     . VAL   A 1  235 ? 23.287  89.629  63.699  1.00 35.36  ? 235 VAL   A C     1 
ATOM   1848  O  O     . VAL   A 1  235 ? 24.297  89.907  64.354  1.00 37.41  ? 235 VAL   A O     1 
ATOM   1849  C  CB    . VAL   A 1  235 ? 23.375  87.852  61.922  1.00 32.40  ? 235 VAL   A CB    1 
ATOM   1850  C  CG1   . VAL   A 1  235 ? 24.812  88.322  61.717  1.00 31.82  ? 235 VAL   A CG1   1 
ATOM   1851  C  CG2   . VAL   A 1  235 ? 23.257  86.369  61.658  1.00 33.51  ? 235 VAL   A CG2   1 
ATOM   1852  N  N     . SER   A 1  236 ? 22.473  90.573  63.229  1.00 39.49  ? 236 SER   A N     1 
ATOM   1853  C  CA    . SER   A 1  236 ? 22.693  91.975  63.581  1.00 38.07  ? 236 SER   A CA    1 
ATOM   1854  C  C     . SER   A 1  236 ? 22.688  92.185  65.098  1.00 41.75  ? 236 SER   A C     1 
ATOM   1855  O  O     . SER   A 1  236 ? 23.449  93.013  65.617  1.00 44.68  ? 236 SER   A O     1 
ATOM   1856  C  CB    . SER   A 1  236 ? 21.635  92.849  62.914  1.00 37.29  ? 236 SER   A CB    1 
ATOM   1857  O  OG    . SER   A 1  236 ? 21.707  94.164  63.421  1.00 49.25  ? 236 SER   A OG    1 
ATOM   1858  N  N     . SER   A 1  237 ? 21.836  91.449  65.827  1.00 33.54  ? 237 SER   A N     1 
ATOM   1859  C  CA    . SER   A 1  237 ? 21.821  91.556  67.285  1.00 37.81  ? 237 SER   A CA    1 
ATOM   1860  C  C     . SER   A 1  237 ? 23.149  91.121  67.895  1.00 37.16  ? 237 SER   A C     1 
ATOM   1861  O  O     . SER   A 1  237 ? 23.671  91.773  68.806  1.00 41.15  ? 237 SER   A O     1 
ATOM   1862  C  CB    . SER   A 1  237 ? 20.683  90.715  67.865  1.00 38.79  ? 237 SER   A CB    1 
ATOM   1863  O  OG    . SER   A 1  237 ? 19.434  91.263  67.516  1.00 42.05  ? 237 SER   A OG    1 
ATOM   1864  N  N     . ILE   A 1  238 ? 23.701  90.011  67.410  1.00 37.32  ? 238 ILE   A N     1 
ATOM   1865  C  CA    . ILE   A 1  238 ? 24.936  89.479  67.960  1.00 31.55  ? 238 ILE   A CA    1 
ATOM   1866  C  C     . ILE   A 1  238 ? 26.143  90.345  67.601  1.00 38.37  ? 238 ILE   A C     1 
ATOM   1867  O  O     . ILE   A 1  238 ? 27.140  90.360  68.336  1.00 46.19  ? 238 ILE   A O     1 
ATOM   1868  C  CB    . ILE   A 1  238 ? 25.083  88.039  67.468  1.00 33.49  ? 238 ILE   A CB    1 
ATOM   1869  C  CG1   . ILE   A 1  238 ? 23.733  87.346  67.648  1.00 38.38  ? 238 ILE   A CG1   1 
ATOM   1870  C  CG2   . ILE   A 1  238 ? 26.187  87.333  68.227  1.00 33.35  ? 238 ILE   A CG2   1 
ATOM   1871  C  CD1   . ILE   A 1  238 ? 23.514  86.088  66.824  1.00 35.39  ? 238 ILE   A CD1   1 
ATOM   1872  N  N     . THR   A 1  239 ? 26.082  91.088  66.496  1.00 29.69  ? 239 THR   A N     1 
ATOM   1873  C  CA    . THR   A 1  239 ? 27.170  91.974  66.095  1.00 43.03  ? 239 THR   A CA    1 
ATOM   1874  C  C     . THR   A 1  239 ? 26.887  93.447  66.369  1.00 48.17  ? 239 THR   A C     1 
ATOM   1875  O  O     . THR   A 1  239 ? 27.708  94.295  66.000  1.00 50.67  ? 239 THR   A O     1 
ATOM   1876  C  CB    . THR   A 1  239 ? 27.495  91.812  64.597  1.00 39.79  ? 239 THR   A CB    1 
ATOM   1877  O  OG1   . THR   A 1  239 ? 26.341  92.132  63.810  1.00 38.14  ? 239 THR   A OG1   1 
ATOM   1878  C  CG2   . THR   A 1  239 ? 27.946  90.396  64.280  1.00 45.87  ? 239 THR   A CG2   1 
ATOM   1879  N  N     . ALA   A 1  240 ? 25.746  93.784  66.974  1.00 42.92  ? 240 ALA   A N     1 
ATOM   1880  C  CA    . ALA   A 1  240 ? 25.486  95.186  67.275  1.00 35.25  ? 240 ALA   A CA    1 
ATOM   1881  C  C     . ALA   A 1  240 ? 26.620  95.784  68.096  1.00 35.20  ? 240 ALA   A C     1 
ATOM   1882  O  O     . ALA   A 1  240 ? 27.016  96.933  67.874  1.00 38.30  ? 240 ALA   A O     1 
ATOM   1883  C  CB    . ALA   A 1  240 ? 24.153  95.335  68.002  1.00 36.76  ? 240 ALA   A CB    1 
ATOM   1884  N  N     . SER   A 1  241 ? 27.186  95.006  69.018  1.00 30.78  ? 241 SER   A N     1 
ATOM   1885  C  CA    . SER   A 1  241 ? 28.149  95.555  69.968  1.00 30.66  ? 241 SER   A CA    1 
ATOM   1886  C  C     . SER   A 1  241 ? 29.476  95.928  69.324  1.00 41.32  ? 241 SER   A C     1 
ATOM   1887  O  O     . SER   A 1  241 ? 30.218  96.724  69.899  1.00 39.87  ? 241 SER   A O     1 
ATOM   1888  C  CB    . SER   A 1  241 ? 28.411  94.572  71.114  1.00 33.44  ? 241 SER   A CB    1 
ATOM   1889  O  OG    . SER   A 1  241 ? 28.604  93.251  70.632  1.00 43.76  ? 241 SER   A OG    1 
ATOM   1890  N  N     . LEU   A 1  242 ? 29.804  95.371  68.163  1.00 50.57  ? 242 LEU   A N     1 
ATOM   1891  C  CA    . LEU   A 1  242 ? 31.055  95.704  67.499  1.00 40.83  ? 242 LEU   A CA    1 
ATOM   1892  C  C     . LEU   A 1  242 ? 30.940  96.919  66.588  1.00 40.67  ? 242 LEU   A C     1 
ATOM   1893  O  O     . LEU   A 1  242 ? 31.966  97.451  66.161  1.00 46.96  ? 242 LEU   A O     1 
ATOM   1894  C  CB    . LEU   A 1  242 ? 31.542  94.498  66.702  1.00 44.02  ? 242 LEU   A CB    1 
ATOM   1895  C  CG    . LEU   A 1  242 ? 31.610  93.169  67.458  1.00 41.86  ? 242 LEU   A CG    1 
ATOM   1896  C  CD1   . LEU   A 1  242 ? 31.149  92.050  66.549  1.00 35.35  ? 242 LEU   A CD1   1 
ATOM   1897  C  CD2   . LEU   A 1  242 ? 33.028  92.908  67.933  1.00 38.53  ? 242 LEU   A CD2   1 
ATOM   1898  N  N     . ARG   A 1  243 ? 29.723  97.369  66.289  1.00 41.82  ? 243 ARG   A N     1 
ATOM   1899  C  CA    . ARG   A 1  243 ? 29.473  98.460  65.350  1.00 46.85  ? 243 ARG   A CA    1 
ATOM   1900  C  C     . ARG   A 1  243 ? 28.937  99.704  66.044  1.00 44.89  ? 243 ARG   A C     1 
ATOM   1901  O  O     . ARG   A 1  243 ? 28.719  100.726 65.382  1.00 39.07  ? 243 ARG   A O     1 
ATOM   1902  C  CB    . ARG   A 1  243 ? 28.481  98.006  64.251  1.00 32.89  ? 243 ARG   A CB    1 
ATOM   1903  C  CG    . ARG   A 1  243 ? 28.897  96.720  63.567  1.00 36.26  ? 243 ARG   A CG    1 
ATOM   1904  C  CD    . ARG   A 1  243 ? 27.891  96.192  62.564  1.00 41.41  ? 243 ARG   A CD    1 
ATOM   1905  N  NE    . ARG   A 1  243 ? 26.731  95.545  63.170  1.00 36.84  ? 243 ARG   A NE    1 
ATOM   1906  C  CZ    . ARG   A 1  243 ? 25.503  96.042  63.117  1.00 38.58  ? 243 ARG   A CZ    1 
ATOM   1907  N  NH1   . ARG   A 1  243 ? 25.253  97.194  62.523  1.00 35.28  ? 243 ARG   A NH1   1 
ATOM   1908  N  NH2   . ARG   A 1  243 ? 24.501  95.365  63.668  1.00 37.84  ? 243 ARG   A NH2   1 
ATOM   1909  N  N     . PHE   A 1  244 ? 28.707  99.638  67.355  1.00 36.52  ? 244 PHE   A N     1 
ATOM   1910  C  CA    . PHE   A 1  244 ? 28.106  100.738 68.092  1.00 45.19  ? 244 PHE   A CA    1 
ATOM   1911  C  C     . PHE   A 1  244 ? 28.841  100.945 69.406  1.00 44.23  ? 244 PHE   A C     1 
ATOM   1912  O  O     . PHE   A 1  244 ? 29.509  100.049 69.929  1.00 39.08  ? 244 PHE   A O     1 
ATOM   1913  C  CB    . PHE   A 1  244 ? 26.613  100.497 68.367  1.00 45.97  ? 244 PHE   A CB    1 
ATOM   1914  C  CG    . PHE   A 1  244 ? 25.763  100.393 67.117  1.00 43.10  ? 244 PHE   A CG    1 
ATOM   1915  C  CD1   . PHE   A 1  244 ? 25.384  101.526 66.425  1.00 32.42  ? 244 PHE   A CD1   1 
ATOM   1916  C  CD2   . PHE   A 1  244 ? 25.341  99.162  66.648  1.00 35.34  ? 244 PHE   A CD2   1 
ATOM   1917  C  CE1   . PHE   A 1  244 ? 24.610  101.428 65.293  1.00 42.14  ? 244 PHE   A CE1   1 
ATOM   1918  C  CE2   . PHE   A 1  244 ? 24.566  99.064  65.516  1.00 31.71  ? 244 PHE   A CE2   1 
ATOM   1919  C  CZ    . PHE   A 1  244 ? 24.198  100.188 64.837  1.00 35.63  ? 244 PHE   A CZ    1 
ATOM   1920  N  N     . ASP   A 1  245 ? 28.717  102.158 69.931  1.00 57.14  ? 245 ASP   A N     1 
ATOM   1921  C  CA    . ASP   A 1  245 ? 29.282  102.460 71.237  1.00 52.26  ? 245 ASP   A CA    1 
ATOM   1922  C  C     . ASP   A 1  245 ? 28.666  101.551 72.295  1.00 55.79  ? 245 ASP   A C     1 
ATOM   1923  O  O     . ASP   A 1  245 ? 27.437  101.429 72.388  1.00 47.76  ? 245 ASP   A O     1 
ATOM   1924  C  CB    . ASP   A 1  245 ? 29.034  103.924 71.581  1.00 52.69  ? 245 ASP   A CB    1 
ATOM   1925  C  CG    . ASP   A 1  245 ? 29.844  104.385 72.755  1.00 48.18  ? 245 ASP   A CG    1 
ATOM   1926  O  OD1   . ASP   A 1  245 ? 30.875  103.731 73.027  1.00 42.56  ? 245 ASP   A OD1   1 
ATOM   1927  O  OD2   . ASP   A 1  245 ? 29.444  105.393 73.399  1.00 49.59  ? 245 ASP   A OD2   1 
ATOM   1928  N  N     . GLY   A 1  246 ? 29.525  100.900 73.076  1.00 52.36  ? 246 GLY   A N     1 
ATOM   1929  C  CA    . GLY   A 1  246 ? 29.086  100.098 74.205  1.00 44.90  ? 246 GLY   A CA    1 
ATOM   1930  C  C     . GLY   A 1  246 ? 30.281  99.592  74.985  1.00 49.89  ? 246 GLY   A C     1 
ATOM   1931  O  O     . GLY   A 1  246 ? 31.434  99.895  74.669  1.00 45.39  ? 246 GLY   A O     1 
ATOM   1932  N  N     . ALA   A 1  247 ? 29.989  98.805  76.022  1.00 48.80  ? 247 ALA   A N     1 
ATOM   1933  C  CA    . ALA   A 1  247 ? 31.035  98.220  76.850  1.00 48.08  ? 247 ALA   A CA    1 
ATOM   1934  C  C     . ALA   A 1  247 ? 30.863  96.713  77.051  1.00 57.12  ? 247 ALA   A C     1 
ATOM   1935  O  O     . ALA   A 1  247 ? 31.631  96.113  77.822  1.00 53.69  ? 247 ALA   A O     1 
ATOM   1936  C  CB    . ALA   A 1  247 ? 31.102  98.930  78.210  1.00 45.74  ? 247 ALA   A CB    1 
ATOM   1937  N  N     . LEU   A 1  248 ? 29.895  96.085  76.377  1.00 41.71  ? 248 LEU   A N     1 
ATOM   1938  C  CA    . LEU   A 1  248 ? 29.703  94.639  76.413  1.00 43.93  ? 248 LEU   A CA    1 
ATOM   1939  C  C     . LEU   A 1  248 ? 29.979  94.040  75.035  1.00 42.16  ? 248 LEU   A C     1 
ATOM   1940  O  O     . LEU   A 1  248 ? 29.460  94.533  74.021  1.00 38.50  ? 248 LEU   A O     1 
ATOM   1941  C  CB    . LEU   A 1  248 ? 28.281  94.296  76.875  1.00 42.76  ? 248 LEU   A CB    1 
ATOM   1942  C  CG    . LEU   A 1  248 ? 27.867  92.820  76.872  1.00 28.52  ? 248 LEU   A CG    1 
ATOM   1943  C  CD1   . LEU   A 1  248 ? 28.911  92.018  77.586  1.00 29.45  ? 248 LEU   A CD1   1 
ATOM   1944  C  CD2   . LEU   A 1  248 ? 26.508  92.632  77.511  1.00 25.50  ? 248 LEU   A CD2   1 
ATOM   1945  N  N     . ASN   A 1  249 ? 30.777  92.970  75.001  1.00 36.75  ? 249 ASN   A N     1 
ATOM   1946  C  CA    . ASN   A 1  249 ? 31.145  92.288  73.755  1.00 43.78  ? 249 ASN   A CA    1 
ATOM   1947  C  C     . ASN   A 1  249 ? 31.736  93.267  72.739  1.00 45.71  ? 249 ASN   A C     1 
ATOM   1948  O  O     . ASN   A 1  249 ? 31.217  93.440  71.631  1.00 40.18  ? 249 ASN   A O     1 
ATOM   1949  C  CB    . ASN   A 1  249 ? 29.939  91.578  73.125  1.00 38.87  ? 249 ASN   A CB    1 
ATOM   1950  C  CG    . ASN   A 1  249 ? 29.418  90.450  73.955  1.00 32.84  ? 249 ASN   A CG    1 
ATOM   1951  O  OD1   . ASN   A 1  249 ? 30.125  89.887  74.791  1.00 32.67  ? 249 ASN   A OD1   1 
ATOM   1952  N  ND2   . ASN   A 1  249 ? 28.162  90.100  73.725  1.00 32.10  ? 249 ASN   A ND2   1 
ATOM   1953  N  N     . VAL   A 1  250 ? 32.822  93.942  73.131  1.00 46.11  ? 250 VAL   A N     1 
ATOM   1954  C  CA    . VAL   A 1  250 ? 33.350  95.013  72.287  1.00 47.85  ? 250 VAL   A CA    1 
ATOM   1955  C  C     . VAL   A 1  250 ? 34.421  94.523  71.333  1.00 43.78  ? 250 VAL   A C     1 
ATOM   1956  O  O     . VAL   A 1  250 ? 34.910  95.306  70.510  1.00 51.78  ? 250 VAL   A O     1 
ATOM   1957  C  CB    . VAL   A 1  250 ? 33.909  96.193  73.111  1.00 50.31  ? 250 VAL   A CB    1 
ATOM   1958  C  CG1   . VAL   A 1  250 ? 32.791  97.107  73.516  1.00 46.69  ? 250 VAL   A CG1   1 
ATOM   1959  C  CG2   . VAL   A 1  250 ? 34.663  95.692  74.338  1.00 51.46  ? 250 VAL   A CG2   1 
ATOM   1960  N  N     . ASP   A 1  251 ? 34.807  93.259  71.419  1.00 41.93  ? 251 ASP   A N     1 
ATOM   1961  C  CA    . ASP   A 1  251 ? 35.703  92.688  70.431  1.00 48.51  ? 251 ASP   A CA    1 
ATOM   1962  C  C     . ASP   A 1  251 ? 35.530  91.179  70.473  1.00 49.64  ? 251 ASP   A C     1 
ATOM   1963  O  O     . ASP   A 1  251 ? 35.057  90.619  71.468  1.00 45.68  ? 251 ASP   A O     1 
ATOM   1964  C  CB    . ASP   A 1  251 ? 37.160  93.106  70.677  1.00 52.86  ? 251 ASP   A CB    1 
ATOM   1965  C  CG    . ASP   A 1  251 ? 37.911  92.121  71.550  1.00 61.29  ? 251 ASP   A CG    1 
ATOM   1966  O  OD1   . ASP   A 1  251 ? 37.454  91.859  72.691  1.00 52.48  ? 251 ASP   A OD1   1 
ATOM   1967  O  OD2   . ASP   A 1  251 ? 38.949  91.593  71.076  1.00 65.12  ? 251 ASP   A OD2   1 
ATOM   1968  N  N     . LEU   A 1  252 ? 35.939  90.529  69.375  1.00 49.38  ? 252 LEU   A N     1 
ATOM   1969  C  CA    . LEU   A 1  252 ? 35.613  89.118  69.161  1.00 51.96  ? 252 LEU   A CA    1 
ATOM   1970  C  C     . LEU   A 1  252 ? 36.074  88.241  70.322  1.00 45.08  ? 252 LEU   A C     1 
ATOM   1971  O  O     . LEU   A 1  252 ? 35.391  87.277  70.683  1.00 41.76  ? 252 LEU   A O     1 
ATOM   1972  C  CB    . LEU   A 1  252 ? 36.226  88.636  67.843  1.00 46.79  ? 252 LEU   A CB    1 
ATOM   1973  C  CG    . LEU   A 1  252 ? 35.818  89.478  66.638  1.00 42.71  ? 252 LEU   A CG    1 
ATOM   1974  C  CD1   . LEU   A 1  252 ? 36.434  88.925  65.347  1.00 40.10  ? 252 LEU   A CD1   1 
ATOM   1975  C  CD2   . LEU   A 1  252 ? 34.292  89.567  66.572  1.00 33.67  ? 252 LEU   A CD2   1 
ATOM   1976  N  N     . THR   A 1  253 ? 37.234  88.554  70.908  1.00 34.93  ? 253 THR   A N     1 
ATOM   1977  C  CA    . THR   A 1  253 ? 37.729  87.813  72.060  1.00 44.49  ? 253 THR   A CA    1 
ATOM   1978  C  C     . THR   A 1  253 ? 36.728  87.809  73.210  1.00 55.55  ? 253 THR   A C     1 
ATOM   1979  O  O     . THR   A 1  253 ? 36.785  86.923  74.074  1.00 50.19  ? 253 THR   A O     1 
ATOM   1980  C  CB    . THR   A 1  253 ? 39.059  88.415  72.536  1.00 47.49  ? 253 THR   A CB    1 
ATOM   1981  O  OG1   . THR   A 1  253 ? 39.564  89.294  71.526  1.00 60.32  ? 253 THR   A OG1   1 
ATOM   1982  C  CG2   . THR   A 1  253 ? 40.105  87.323  72.848  1.00 43.89  ? 253 THR   A CG2   1 
ATOM   1983  N  N     . GLU   A 1  254 ? 35.811  88.777  73.252  1.00 48.55  ? 254 GLU   A N     1 
ATOM   1984  C  CA    . GLU   A 1  254 ? 34.870  88.791  74.361  1.00 49.80  ? 254 GLU   A CA    1 
ATOM   1985  C  C     . GLU   A 1  254 ? 33.721  87.803  74.162  1.00 50.26  ? 254 GLU   A C     1 
ATOM   1986  O  O     . GLU   A 1  254 ? 33.196  87.270  75.148  1.00 45.08  ? 254 GLU   A O     1 
ATOM   1987  C  CB    . GLU   A 1  254 ? 34.346  90.204  74.584  1.00 47.51  ? 254 GLU   A CB    1 
ATOM   1988  C  CG    . GLU   A 1  254 ? 34.518  90.660  76.019  1.00 44.95  ? 254 GLU   A CG    1 
ATOM   1989  C  CD    . GLU   A 1  254 ? 33.924  92.024  76.245  1.00 58.75  ? 254 GLU   A CD    1 
ATOM   1990  O  OE1   . GLU   A 1  254 ? 34.469  92.991  75.667  1.00 62.83  ? 254 GLU   A OE1   1 
ATOM   1991  O  OE2   . GLU   A 1  254 ? 32.903  92.122  76.976  1.00 54.58  ? 254 GLU   A OE2   1 
ATOM   1992  N  N     . PHE   A 1  255 ? 33.310  87.549  72.916  1.00 44.33  ? 255 PHE   A N     1 
ATOM   1993  C  CA    . PHE   A 1  255 ? 32.350  86.472  72.681  1.00 50.06  ? 255 PHE   A CA    1 
ATOM   1994  C  C     . PHE   A 1  255 ? 32.887  85.154  73.227  1.00 46.78  ? 255 PHE   A C     1 
ATOM   1995  O  O     . PHE   A 1  255 ? 32.161  84.390  73.881  1.00 42.42  ? 255 PHE   A O     1 
ATOM   1996  C  CB    . PHE   A 1  255 ? 32.033  86.355  71.184  1.00 41.42  ? 255 PHE   A CB    1 
ATOM   1997  C  CG    . PHE   A 1  255 ? 31.279  87.531  70.628  1.00 42.86  ? 255 PHE   A CG    1 
ATOM   1998  C  CD1   . PHE   A 1  255 ? 31.944  88.684  70.251  1.00 42.80  ? 255 PHE   A CD1   1 
ATOM   1999  C  CD2   . PHE   A 1  255 ? 29.902  87.478  70.474  1.00 38.42  ? 255 PHE   A CD2   1 
ATOM   2000  C  CE1   . PHE   A 1  255 ? 31.249  89.759  69.737  1.00 36.94  ? 255 PHE   A CE1   1 
ATOM   2001  C  CE2   . PHE   A 1  255 ? 29.203  88.551  69.958  1.00 34.03  ? 255 PHE   A CE2   1 
ATOM   2002  C  CZ    . PHE   A 1  255 ? 29.875  89.690  69.591  1.00 34.07  ? 255 PHE   A CZ    1 
ATOM   2003  N  N     . GLN   A 1  256 ? 34.163  84.877  72.953  1.00 40.72  ? 256 GLN   A N     1 
ATOM   2004  C  CA    . GLN   A 1  256 ? 34.880  83.778  73.581  1.00 44.90  ? 256 GLN   A CA    1 
ATOM   2005  C  C     . GLN   A 1  256 ? 34.696  83.807  75.086  1.00 44.97  ? 256 GLN   A C     1 
ATOM   2006  O  O     . GLN   A 1  256 ? 34.095  82.905  75.679  1.00 37.68  ? 256 GLN   A O     1 
ATOM   2007  C  CB    . GLN   A 1  256 ? 36.356  83.922  73.240  1.00 56.12  ? 256 GLN   A CB    1 
ATOM   2008  C  CG    . GLN   A 1  256 ? 37.141  82.689  72.914  1.00 51.28  ? 256 GLN   A CG    1 
ATOM   2009  C  CD    . GLN   A 1  256 ? 38.396  83.087  72.146  1.00 56.67  ? 256 GLN   A CD    1 
ATOM   2010  O  OE1   . GLN   A 1  256 ? 38.356  84.013  71.327  1.00 50.79  ? 256 GLN   A OE1   1 
ATOM   2011  N  NE2   . GLN   A 1  256 ? 39.519  82.428  72.432  1.00 59.46  ? 256 GLN   A NE2   1 
ATOM   2012  N  N     . THR   A 1  257 ? 35.190  84.885  75.706  1.00 48.18  ? 257 THR   A N     1 
ATOM   2013  C  CA    . THR   A 1  257 ? 35.294  84.966  77.158  1.00 46.19  ? 257 THR   A CA    1 
ATOM   2014  C  C     . THR   A 1  257 ? 33.929  84.931  77.834  1.00 47.48  ? 257 THR   A C     1 
ATOM   2015  O  O     . THR   A 1  257 ? 33.764  84.289  78.879  1.00 48.78  ? 257 THR   A O     1 
ATOM   2016  C  CB    . THR   A 1  257 ? 36.050  86.235  77.542  1.00 41.00  ? 257 THR   A CB    1 
ATOM   2017  O  OG1   . THR   A 1  257 ? 37.446  85.936  77.650  1.00 38.43  ? 257 THR   A OG1   1 
ATOM   2018  C  CG2   . THR   A 1  257 ? 35.548  86.756  78.855  1.00 35.26  ? 257 THR   A CG2   1 
ATOM   2019  N  N     . ASN   A 1  258 ? 32.944  85.627  77.268  1.00 41.51  ? 258 ASN   A N     1 
ATOM   2020  C  CA    . ASN   A 1  258 ? 31.633  85.686  77.899  1.00 38.98  ? 258 ASN   A CA    1 
ATOM   2021  C  C     . ASN   A 1  258 ? 30.847  84.402  77.693  1.00 40.83  ? 258 ASN   A C     1 
ATOM   2022  O  O     . ASN   A 1  258 ? 30.168  83.935  78.617  1.00 44.09  ? 258 ASN   A O     1 
ATOM   2023  C  CB    . ASN   A 1  258 ? 30.848  86.880  77.363  1.00 52.38  ? 258 ASN   A CB    1 
ATOM   2024  C  CG    . ASN   A 1  258 ? 31.343  88.194  77.921  1.00 44.98  ? 258 ASN   A CG    1 
ATOM   2025  O  OD1   . ASN   A 1  258 ? 31.761  88.256  79.067  1.00 46.47  ? 258 ASN   A OD1   1 
ATOM   2026  N  ND2   . ASN   A 1  258 ? 31.305  89.247  77.113  1.00 36.87  ? 258 ASN   A ND2   1 
ATOM   2027  N  N     . LEU   A 1  259 ? 30.954  83.796  76.511  1.00 41.70  ? 259 LEU   A N     1 
ATOM   2028  C  CA    . LEU   A 1  259 ? 30.072  82.697  76.140  1.00 41.51  ? 259 LEU   A CA    1 
ATOM   2029  C  C     . LEU   A 1  259 ? 30.703  81.309  76.212  1.00 38.59  ? 259 LEU   A C     1 
ATOM   2030  O  O     . LEU   A 1  259 ? 29.962  80.330  76.317  1.00 40.22  ? 259 LEU   A O     1 
ATOM   2031  C  CB    . LEU   A 1  259 ? 29.531  82.925  74.722  1.00 46.94  ? 259 LEU   A CB    1 
ATOM   2032  C  CG    . LEU   A 1  259 ? 28.310  83.850  74.589  1.00 38.25  ? 259 LEU   A CG    1 
ATOM   2033  C  CD1   . LEU   A 1  259 ? 28.218  84.798  75.755  1.00 33.27  ? 259 LEU   A CD1   1 
ATOM   2034  C  CD2   . LEU   A 1  259 ? 28.396  84.624  73.294  1.00 30.02  ? 259 LEU   A CD2   1 
ATOM   2035  N  N     . VAL   A 1  260 ? 32.027  81.184  76.177  1.00 45.47  ? 260 VAL   A N     1 
ATOM   2036  C  CA    . VAL   A 1  260 ? 32.644  79.880  75.925  1.00 48.93  ? 260 VAL   A CA    1 
ATOM   2037  C  C     . VAL   A 1  260 ? 33.742  79.542  76.928  1.00 49.10  ? 260 VAL   A C     1 
ATOM   2038  O  O     . VAL   A 1  260 ? 34.929  79.713  76.607  1.00 45.96  ? 260 VAL   A O     1 
ATOM   2039  C  CB    . VAL   A 1  260 ? 33.228  79.814  74.503  1.00 37.41  ? 260 VAL   A CB    1 
ATOM   2040  C  CG1   . VAL   A 1  260 ? 33.630  78.373  74.157  1.00 30.92  ? 260 VAL   A CG1   1 
ATOM   2041  C  CG2   . VAL   A 1  260 ? 32.245  80.371  73.501  1.00 32.89  ? 260 VAL   A CG2   1 
ATOM   2042  N  N     . PRO   A 1  261 ? 33.409  79.021  78.116  1.00 50.15  ? 261 PRO   A N     1 
ATOM   2043  C  CA    . PRO   A 1  261 ? 34.468  78.539  79.029  1.00 50.12  ? 261 PRO   A CA    1 
ATOM   2044  C  C     . PRO   A 1  261 ? 35.252  77.338  78.503  1.00 43.23  ? 261 PRO   A C     1 
ATOM   2045  O  O     . PRO   A 1  261 ? 36.445  77.221  78.806  1.00 50.26  ? 261 PRO   A O     1 
ATOM   2046  C  CB    . PRO   A 1  261 ? 33.698  78.189  80.316  1.00 54.59  ? 261 PRO   A CB    1 
ATOM   2047  C  CG    . PRO   A 1  261 ? 32.284  77.987  79.896  1.00 49.74  ? 261 PRO   A CG    1 
ATOM   2048  C  CD    . PRO   A 1  261 ? 32.068  78.917  78.714  1.00 51.60  ? 261 PRO   A CD    1 
ATOM   2049  N  N     . TYR   A 1  262 ? 34.620  76.433  77.743  1.00 52.61  ? 262 TYR   A N     1 
ATOM   2050  C  CA    . TYR   A 1  262 ? 35.220  75.234  77.161  1.00 44.38  ? 262 TYR   A CA    1 
ATOM   2051  C  C     . TYR   A 1  262 ? 35.426  75.428  75.668  1.00 55.22  ? 262 TYR   A C     1 
ATOM   2052  O  O     . TYR   A 1  262 ? 34.476  75.796  74.966  1.00 54.48  ? 262 TYR   A O     1 
ATOM   2053  C  CB    . TYR   A 1  262 ? 34.323  74.027  77.397  1.00 55.95  ? 262 TYR   A CB    1 
ATOM   2054  C  CG    . TYR   A 1  262 ? 34.484  73.399  78.753  1.00 63.83  ? 262 TYR   A CG    1 
ATOM   2055  C  CD1   . TYR   A 1  262 ? 34.448  74.174  79.909  1.00 67.48  ? 262 TYR   A CD1   1 
ATOM   2056  C  CD2   . TYR   A 1  262 ? 34.669  72.022  78.881  1.00 76.49  ? 262 TYR   A CD2   1 
ATOM   2057  C  CE1   . TYR   A 1  262 ? 34.605  73.595  81.163  1.00 84.64  ? 262 TYR   A CE1   1 
ATOM   2058  C  CE2   . TYR   A 1  262 ? 34.822  71.429  80.128  1.00 92.62  ? 262 TYR   A CE2   1 
ATOM   2059  C  CZ    . TYR   A 1  262 ? 34.786  72.221  81.272  1.00 97.83  ? 262 TYR   A CZ    1 
ATOM   2060  O  OH    . TYR   A 1  262 ? 34.927  71.639  82.519  1.00 90.78  ? 262 TYR   A OH    1 
ATOM   2061  N  N     . PRO   A 1  263 ? 36.623  75.171  75.132  1.00 63.23  ? 263 PRO   A N     1 
ATOM   2062  C  CA    A PRO   A 1  263 ? 36.868  75.543  73.726  0.90 57.53  ? 263 PRO   A CA    1 
ATOM   2063  C  CA    B PRO   A 1  263 ? 36.873  75.533  73.725  0.10 57.22  ? 263 PRO   A CA    1 
ATOM   2064  C  C     . PRO   A 1  263 ? 36.023  74.757  72.734  1.00 46.89  ? 263 PRO   A C     1 
ATOM   2065  O  O     . PRO   A 1  263 ? 35.574  75.330  71.728  1.00 42.49  ? 263 PRO   A O     1 
ATOM   2066  C  CB    A PRO   A 1  263 ? 38.373  75.274  73.548  0.90 58.60  ? 263 PRO   A CB    1 
ATOM   2067  C  CB    B PRO   A 1  263 ? 38.371  75.234  73.549  0.10 58.18  ? 263 PRO   A CB    1 
ATOM   2068  C  CG    A PRO   A 1  263 ? 38.920  75.082  74.946  0.90 52.90  ? 263 PRO   A CG    1 
ATOM   2069  C  CG    B PRO   A 1  263 ? 38.930  75.203  74.941  0.10 53.13  ? 263 PRO   A CG    1 
ATOM   2070  C  CD    A PRO   A 1  263 ? 37.794  74.529  75.749  0.90 56.13  ? 263 PRO   A CD    1 
ATOM   2071  C  CD    B PRO   A 1  263 ? 37.831  74.661  75.798  0.10 56.14  ? 263 PRO   A CD    1 
ATOM   2072  N  N     . ARG   A 1  264 ? 35.789  73.463  72.982  1.00 42.42  ? 264 ARG   A N     1 
ATOM   2073  C  CA    . ARG   A 1  264 ? 35.031  72.646  72.028  1.00 54.57  ? 264 ARG   A CA    1 
ATOM   2074  C  C     . ARG   A 1  264 ? 33.526  72.859  72.143  1.00 51.56  ? 264 ARG   A C     1 
ATOM   2075  O  O     . ARG   A 1  264 ? 32.808  72.809  71.138  1.00 43.64  ? 264 ARG   A O     1 
ATOM   2076  C  CB    . ARG   A 1  264 ? 35.351  71.170  72.217  1.00 47.75  ? 264 ARG   A CB    1 
ATOM   2077  C  CG    . ARG   A 1  264 ? 36.697  70.776  71.637  1.00 45.57  ? 264 ARG   A CG    1 
ATOM   2078  C  CD    . ARG   A 1  264 ? 37.063  69.422  72.127  1.00 35.05  ? 264 ARG   A CD    1 
ATOM   2079  N  NE    . ARG   A 1  264 ? 36.021  68.453  71.805  1.00 46.29  ? 264 ARG   A NE    1 
ATOM   2080  C  CZ    . ARG   A 1  264 ? 35.932  67.850  70.628  1.00 40.72  ? 264 ARG   A CZ    1 
ATOM   2081  N  NH1   . ARG   A 1  264 ? 36.779  68.130  69.643  1.00 38.84  ? 264 ARG   A NH1   1 
ATOM   2082  N  NH2   . ARG   A 1  264 ? 34.988  66.934  70.440  1.00 34.19  ? 264 ARG   A NH2   1 
ATOM   2083  N  N     . ILE   A 1  265 ? 33.034  73.079  73.354  1.00 41.82  ? 265 ILE   A N     1 
ATOM   2084  C  CA    . ILE   A 1  265 ? 31.656  73.484  73.556  1.00 36.00  ? 265 ILE   A CA    1 
ATOM   2085  C  C     . ILE   A 1  265 ? 31.537  74.986  73.304  1.00 33.97  ? 265 ILE   A C     1 
ATOM   2086  O  O     . ILE   A 1  265 ? 31.302  75.777  74.223  1.00 49.07  ? 265 ILE   A O     1 
ATOM   2087  C  CB    . ILE   A 1  265 ? 31.202  73.079  74.967  1.00 47.59  ? 265 ILE   A CB    1 
ATOM   2088  C  CG1   . ILE   A 1  265 ? 31.342  71.560  75.117  1.00 43.26  ? 265 ILE   A CG1   1 
ATOM   2089  C  CG2   . ILE   A 1  265 ? 29.786  73.533  75.232  1.00 40.72  ? 265 ILE   A CG2   1 
ATOM   2090  C  CD1   . ILE   A 1  265 ? 30.904  71.044  76.447  1.00 47.54  ? 265 ILE   A CD1   1 
ATOM   2091  N  N     . HIS   A 1  266 ? 31.690  75.383  72.053  1.00 33.60  ? 266 HIS   A N     1 
ATOM   2092  C  CA    . HIS   A 1  266 ? 31.666  76.774  71.628  1.00 34.38  ? 266 HIS   A CA    1 
ATOM   2093  C  C     . HIS   A 1  266 ? 30.451  77.077  70.748  1.00 38.72  ? 266 HIS   A C     1 
ATOM   2094  O  O     . HIS   A 1  266 ? 30.518  77.876  69.801  1.00 38.57  ? 266 HIS   A O     1 
ATOM   2095  C  CB    . HIS   A 1  266 ? 32.965  77.118  70.899  1.00 39.69  ? 266 HIS   A CB    1 
ATOM   2096  C  CG    . HIS   A 1  266 ? 33.209  76.320  69.644  1.00 46.16  ? 266 HIS   A CG    1 
ATOM   2097  N  ND1   . HIS   A 1  266 ? 34.301  75.492  69.492  1.00 47.03  ? 266 HIS   A ND1   1 
ATOM   2098  C  CD2   . HIS   A 1  266 ? 32.527  76.257  68.470  1.00 40.00  ? 266 HIS   A CD2   1 
ATOM   2099  C  CE1   . HIS   A 1  266 ? 34.276  74.951  68.284  1.00 44.79  ? 266 HIS   A CE1   1 
ATOM   2100  N  NE2   . HIS   A 1  266 ? 33.217  75.407  67.639  1.00 33.91  ? 266 HIS   A NE2   1 
ATOM   2101  N  N     . PHE   A 1  267 ? 29.318  76.443  71.051  1.00 29.57  ? 267 PHE   A N     1 
ATOM   2102  C  CA    . PHE   A 1  267 ? 28.108  76.547  70.238  1.00 30.89  ? 267 PHE   A CA    1 
ATOM   2103  C  C     . PHE   A 1  267 ? 26.993  77.114  71.110  1.00 37.18  ? 267 PHE   A C     1 
ATOM   2104  O  O     . PHE   A 1  267 ? 26.165  76.361  71.648  1.00 42.43  ? 267 PHE   A O     1 
ATOM   2105  C  CB    . PHE   A 1  267 ? 27.722  75.189  69.648  1.00 36.71  ? 267 PHE   A CB    1 
ATOM   2106  C  CG    . PHE   A 1  267 ? 28.721  74.644  68.652  1.00 27.33  ? 267 PHE   A CG    1 
ATOM   2107  C  CD1   . PHE   A 1  267 ? 29.776  73.849  69.069  1.00 30.93  ? 267 PHE   A CD1   1 
ATOM   2108  C  CD2   . PHE   A 1  267 ? 28.604  74.933  67.303  1.00 23.26  ? 267 PHE   A CD2   1 
ATOM   2109  C  CE1   . PHE   A 1  267 ? 30.701  73.342  68.151  1.00 30.49  ? 267 PHE   A CE1   1 
ATOM   2110  C  CE2   . PHE   A 1  267 ? 29.506  74.440  66.391  1.00 28.61  ? 267 PHE   A CE2   1 
ATOM   2111  C  CZ    . PHE   A 1  267 ? 30.558  73.634  66.811  1.00 34.04  ? 267 PHE   A CZ    1 
ATOM   2112  N  N     . PRO   A 1  268 ? 26.951  78.436  71.285  1.00 30.41  ? 268 PRO   A N     1 
ATOM   2113  C  CA    . PRO   A 1  268 ? 25.884  79.055  72.074  1.00 35.63  ? 268 PRO   A CA    1 
ATOM   2114  C  C     . PRO   A 1  268 ? 24.550  79.161  71.339  1.00 27.93  ? 268 PRO   A C     1 
ATOM   2115  O  O     . PRO   A 1  268 ? 24.480  79.496  70.159  1.00 25.63  ? 268 PRO   A O     1 
ATOM   2116  C  CB    . PRO   A 1  268 ? 26.456  80.447  72.379  1.00 32.10  ? 268 PRO   A CB    1 
ATOM   2117  C  CG    . PRO   A 1  268 ? 27.391  80.686  71.304  1.00 26.93  ? 268 PRO   A CG    1 
ATOM   2118  C  CD    . PRO   A 1  268 ? 28.037  79.390  71.038  1.00 27.98  ? 268 PRO   A CD    1 
ATOM   2119  N  N     . LEU   A 1  269 ? 23.483  78.918  72.088  1.00 29.61  ? 269 LEU   A N     1 
ATOM   2120  C  CA    . LEU   A 1  269 ? 22.120  78.974  71.581  1.00 27.96  ? 269 LEU   A CA    1 
ATOM   2121  C  C     . LEU   A 1  269 ? 21.610  80.414  71.517  1.00 22.44  ? 269 LEU   A C     1 
ATOM   2122  O  O     . LEU   A 1  269 ? 21.620  81.136  72.519  1.00 32.04  ? 269 LEU   A O     1 
ATOM   2123  C  CB    . LEU   A 1  269 ? 21.223  78.124  72.487  1.00 24.72  ? 269 LEU   A CB    1 
ATOM   2124  C  CG    . LEU   A 1  269 ? 19.740  78.227  72.207  1.00 22.52  ? 269 LEU   A CG    1 
ATOM   2125  C  CD1   . LEU   A 1  269 ? 19.498  77.664  70.844  1.00 28.76  ? 269 LEU   A CD1   1 
ATOM   2126  C  CD2   . LEU   A 1  269 ? 18.976  77.461  73.242  1.00 26.56  ? 269 LEU   A CD2   1 
ATOM   2127  N  N     . ALA   A 1  270 ? 21.148  80.832  70.350  1.00 23.75  ? 270 ALA   A N     1 
ATOM   2128  C  CA    . ALA   A 1  270 ? 20.565  82.158  70.186  1.00 27.52  ? 270 ALA   A CA    1 
ATOM   2129  C  C     . ALA   A 1  270 ? 19.056  82.059  70.315  1.00 25.33  ? 270 ALA   A C     1 
ATOM   2130  O  O     . ALA   A 1  270 ? 18.457  81.090  69.854  1.00 25.79  ? 270 ALA   A O     1 
ATOM   2131  C  CB    . ALA   A 1  270 ? 20.924  82.783  68.830  1.00 21.77  ? 270 ALA   A CB    1 
ATOM   2132  N  N     . THR   A 1  271 ? 18.451  83.058  70.957  1.00 26.00  ? 271 THR   A N     1 
ATOM   2133  C  CA    . THR   A 1  271 ? 17.002  83.126  71.094  1.00 27.19  ? 271 THR   A CA    1 
ATOM   2134  C  C     . THR   A 1  271 ? 16.548  84.562  70.914  1.00 31.72  ? 271 THR   A C     1 
ATOM   2135  O  O     . THR   A 1  271 ? 17.128  85.480  71.495  1.00 34.04  ? 271 THR   A O     1 
ATOM   2136  C  CB    . THR   A 1  271 ? 16.545  82.599  72.444  1.00 30.67  ? 271 THR   A CB    1 
ATOM   2137  O  OG1   . THR   A 1  271 ? 17.255  81.386  72.730  1.00 32.95  ? 271 THR   A OG1   1 
ATOM   2138  C  CG2   . THR   A 1  271 ? 15.041  82.318  72.409  1.00 30.25  ? 271 THR   A CG2   1 
ATOM   2139  N  N     . TYR   A 1  272 ? 15.513  84.760  70.112  1.00 30.35  ? 272 TYR   A N     1 
ATOM   2140  C  CA    . TYR   A 1  272 ? 15.146  86.099  69.690  1.00 29.91  ? 272 TYR   A CA    1 
ATOM   2141  C  C     . TYR   A 1  272 ? 13.648  86.288  69.823  1.00 31.38  ? 272 TYR   A C     1 
ATOM   2142  O  O     . TYR   A 1  272 ? 12.869  85.374  69.545  1.00 31.35  ? 272 TYR   A O     1 
ATOM   2143  C  CB    . TYR   A 1  272 ? 15.588  86.338  68.243  1.00 28.07  ? 272 TYR   A CB    1 
ATOM   2144  C  CG    . TYR   A 1  272 ? 15.434  87.740  67.774  1.00 22.80  ? 272 TYR   A CG    1 
ATOM   2145  C  CD1   . TYR   A 1  272 ? 16.406  88.704  68.043  1.00 31.60  ? 272 TYR   A CD1   1 
ATOM   2146  C  CD2   . TYR   A 1  272 ? 14.325  88.115  67.047  1.00 24.96  ? 272 TYR   A CD2   1 
ATOM   2147  C  CE1   . TYR   A 1  272 ? 16.254  90.034  67.592  1.00 29.18  ? 272 TYR   A CE1   1 
ATOM   2148  C  CE2   . TYR   A 1  272 ? 14.173  89.425  66.589  1.00 30.61  ? 272 TYR   A CE2   1 
ATOM   2149  C  CZ    . TYR   A 1  272 ? 15.128  90.377  66.873  1.00 24.77  ? 272 TYR   A CZ    1 
ATOM   2150  O  OH    . TYR   A 1  272 ? 14.938  91.656  66.411  1.00 40.03  ? 272 TYR   A OH    1 
ATOM   2151  N  N     . ALA   A 1  273 ? 13.258  87.482  70.250  1.00 32.83  ? 273 ALA   A N     1 
ATOM   2152  C  CA    . ALA   A 1  273 ? 11.859  87.859  70.367  1.00 29.27  ? 273 ALA   A CA    1 
ATOM   2153  C  C     . ALA   A 1  273 ? 11.792  89.369  70.508  1.00 32.55  ? 273 ALA   A C     1 
ATOM   2154  O  O     . ALA   A 1  273 ? 12.736  89.984  71.016  1.00 37.40  ? 273 ALA   A O     1 
ATOM   2155  C  CB    . ALA   A 1  273 ? 11.197  87.167  71.563  1.00 21.59  ? 273 ALA   A CB    1 
ATOM   2156  N  N     . PRO   A 1  274 ? 10.710  89.995  70.072  1.00 39.70  ? 274 PRO   A N     1 
ATOM   2157  C  CA    . PRO   A 1  274 ? 9.511   89.415  69.466  1.00 41.67  ? 274 PRO   A CA    1 
ATOM   2158  C  C     . PRO   A 1  274 ? 9.621   89.380  67.950  1.00 34.14  ? 274 PRO   A C     1 
ATOM   2159  O  O     . PRO   A 1  274 ? 10.225  90.257  67.333  1.00 32.44  ? 274 PRO   A O     1 
ATOM   2160  C  CB    . PRO   A 1  274 ? 8.418   90.384  69.927  1.00 39.51  ? 274 PRO   A CB    1 
ATOM   2161  C  CG    . PRO   A 1  274 ? 9.119   91.724  69.817  1.00 40.79  ? 274 PRO   A CG    1 
ATOM   2162  C  CD    . PRO   A 1  274 ? 10.569  91.457  70.223  1.00 38.54  ? 274 PRO   A CD    1 
ATOM   2163  N  N     . VAL   A 1  275 ? 9.062   88.367  67.314  1.00 27.00  ? 275 VAL   A N     1 
ATOM   2164  C  CA    . VAL   A 1  275 ? 8.925   88.347  65.870  1.00 27.97  ? 275 VAL   A CA    1 
ATOM   2165  C  C     . VAL   A 1  275 ? 7.448   88.568  65.588  1.00 32.08  ? 275 VAL   A C     1 
ATOM   2166  O  O     . VAL   A 1  275 ? 6.616   87.714  65.913  1.00 27.19  ? 275 VAL   A O     1 
ATOM   2167  C  CB    . VAL   A 1  275 ? 9.436   87.037  65.257  1.00 26.44  ? 275 VAL   A CB    1 
ATOM   2168  C  CG1   . VAL   A 1  275 ? 9.240   87.053  63.766  1.00 33.38  ? 275 VAL   A CG1   1 
ATOM   2169  C  CG2   . VAL   A 1  275 ? 10.895  86.837  65.575  1.00 27.74  ? 275 VAL   A CG2   1 
ATOM   2170  N  N     . ILE   A 1  276 ? 7.117   89.722  65.011  1.00 30.04  ? 276 ILE   A N     1 
ATOM   2171  C  CA    . ILE   A 1  276 ? 5.739   90.115  64.752  1.00 30.71  ? 276 ILE   A CA    1 
ATOM   2172  C  C     . ILE   A 1  276 ? 5.567   90.344  63.262  1.00 31.94  ? 276 ILE   A C     1 
ATOM   2173  O  O     . ILE   A 1  276 ? 6.414   90.976  62.620  1.00 44.77  ? 276 ILE   A O     1 
ATOM   2174  C  CB    . ILE   A 1  276 ? 5.345   91.396  65.529  1.00 47.62  ? 276 ILE   A CB    1 
ATOM   2175  C  CG1   . ILE   A 1  276 ? 5.477   91.223  67.057  1.00 28.51  ? 276 ILE   A CG1   1 
ATOM   2176  C  CG2   . ILE   A 1  276 ? 3.954   91.856  65.114  1.00 45.55  ? 276 ILE   A CG2   1 
ATOM   2177  C  CD1   . ILE   A 1  276 ? 4.743   90.038  67.612  1.00 42.17  ? 276 ILE   A CD1   1 
ATOM   2178  N  N     . SER   A 1  277 ? 4.461   89.858  62.717  1.00 34.40  ? 277 SER   A N     1 
ATOM   2179  C  CA    . SER   A 1  277 ? 4.129   90.147  61.325  1.00 40.87  ? 277 SER   A CA    1 
ATOM   2180  C  C     . SER   A 1  277 ? 3.887   91.639  61.133  1.00 43.14  ? 277 SER   A C     1 
ATOM   2181  O  O     . SER   A 1  277 ? 3.138   92.258  61.893  1.00 56.67  ? 277 SER   A O     1 
ATOM   2182  C  CB    . SER   A 1  277 ? 2.887   89.350  60.908  1.00 44.10  ? 277 SER   A CB    1 
ATOM   2183  O  OG    . SER   A 1  277 ? 2.590   89.538  59.535  1.00 52.23  ? 277 SER   A OG    1 
ATOM   2184  N  N     . ALA   A 1  278 ? 4.523   92.228  60.117  1.00 47.48  ? 278 ALA   A N     1 
ATOM   2185  C  CA    . ALA   A 1  278 ? 4.192   93.611  59.784  1.00 44.61  ? 278 ALA   A CA    1 
ATOM   2186  C  C     . ALA   A 1  278 ? 2.788   93.732  59.220  1.00 50.43  ? 278 ALA   A C     1 
ATOM   2187  O  O     . ALA   A 1  278 ? 2.255   94.844  59.159  1.00 51.11  ? 278 ALA   A O     1 
ATOM   2188  C  CB    . ALA   A 1  278 ? 5.196   94.199  58.788  1.00 38.48  ? 278 ALA   A CB    1 
ATOM   2189  N  N     . GLU   A 1  279 ? 2.183   92.615  58.825  1.00 54.26  ? 279 GLU   A N     1 
ATOM   2190  C  CA    . GLU   A 1  279 ? 0.813   92.585  58.338  1.00 65.94  ? 279 GLU   A CA    1 
ATOM   2191  C  C     . GLU   A 1  279 ? -0.215  92.576  59.458  1.00 59.37  ? 279 GLU   A C     1 
ATOM   2192  O  O     . GLU   A 1  279 ? -1.413  92.654  59.172  1.00 70.46  ? 279 GLU   A O     1 
ATOM   2193  C  CB    . GLU   A 1  279 ? 0.597   91.350  57.451  1.00 76.14  ? 279 GLU   A CB    1 
ATOM   2194  C  CG    . GLU   A 1  279 ? 1.310   91.402  56.114  1.00 65.64  ? 279 GLU   A CG    1 
ATOM   2195  C  CD    . GLU   A 1  279 ? 0.679   92.395  55.187  1.00 77.64  ? 279 GLU   A CD    1 
ATOM   2196  O  OE1   . GLU   A 1  279 ? -0.522  92.686  55.382  1.00 88.26  ? 279 GLU   A OE1   1 
ATOM   2197  O  OE2   . GLU   A 1  279 ? 1.374   92.887  54.272  1.00 90.25  ? 279 GLU   A OE2   1 
ATOM   2198  N  N     . LYS   A 1  280 ? 0.210   92.455  60.710  1.00 64.03  ? 280 LYS   A N     1 
ATOM   2199  C  CA    . LYS   A 1  280 ? -0.733  92.452  61.822  1.00 72.96  ? 280 LYS   A CA    1 
ATOM   2200  C  C     . LYS   A 1  280 ? -1.360  93.832  61.954  1.00 74.07  ? 280 LYS   A C     1 
ATOM   2201  O  O     . LYS   A 1  280 ? -0.649  94.845  61.981  1.00 65.90  ? 280 LYS   A O     1 
ATOM   2202  C  CB    . LYS   A 1  280 ? -0.028  92.047  63.122  1.00 63.42  ? 280 LYS   A CB    1 
ATOM   2203  C  CG    . LYS   A 1  280 ? -0.961  91.629  64.244  1.00 75.57  ? 280 LYS   A CG    1 
ATOM   2204  C  CD    . LYS   A 1  280 ? -0.286  90.691  65.252  1.00 71.80  ? 280 LYS   A CD    1 
ATOM   2205  C  CE    . LYS   A 1  280 ? -0.723  89.235  65.047  1.00 84.44  ? 280 LYS   A CE    1 
ATOM   2206  N  NZ    . LYS   A 1  280 ? -0.438  88.669  63.674  1.00 61.25  ? 280 LYS   A NZ    1 
ATOM   2207  N  N     . ALA   A 1  281 ? -2.693  93.873  62.003  1.00 75.65  ? 281 ALA   A N     1 
ATOM   2208  C  CA    . ALA   A 1  281 ? -3.430  95.129  62.143  1.00 79.34  ? 281 ALA   A CA    1 
ATOM   2209  C  C     . ALA   A 1  281 ? -3.323  95.579  63.594  1.00 94.20  ? 281 ALA   A C     1 
ATOM   2210  O  O     . ALA   A 1  281 ? -4.024  95.066  64.470  1.00 104.72 ? 281 ALA   A O     1 
ATOM   2211  C  CB    . ALA   A 1  281 ? -4.884  94.958  61.718  1.00 69.67  ? 281 ALA   A CB    1 
ATOM   2212  N  N     . TYR   A 1  282 ? -2.443  96.548  63.851  1.00 94.67  ? 282 TYR   A N     1 
ATOM   2213  C  CA    . TYR   A 1  282 ? -2.085  96.947  65.210  1.00 99.16  ? 282 TYR   A CA    1 
ATOM   2214  C  C     . TYR   A 1  282 ? -1.688  95.761  66.085  1.00 96.75  ? 282 TYR   A C     1 
ATOM   2215  O  O     . TYR   A 1  282 ? -2.288  94.677  66.031  1.00 79.75  ? 282 TYR   A O     1 
ATOM   2216  C  CB    . TYR   A 1  282 ? -3.218  97.709  65.903  1.00 97.02  ? 282 TYR   A CB    1 
ATOM   2217  C  CG    . TYR   A 1  282 ? -2.939  97.903  67.378  1.00 88.86  ? 282 TYR   A CG    1 
ATOM   2218  C  CD1   . TYR   A 1  282 ? -2.239  99.016  67.834  1.00 99.42  ? 282 TYR   A CD1   1 
ATOM   2219  C  CD2   . TYR   A 1  282 ? -3.343  96.957  68.316  1.00 89.19  ? 282 TYR   A CD2   1 
ATOM   2220  C  CE1   . TYR   A 1  282 ? -1.962  99.195  69.194  1.00 87.07  ? 282 TYR   A CE1   1 
ATOM   2221  C  CE2   . TYR   A 1  282 ? -3.060  97.119  69.666  1.00 91.85  ? 282 TYR   A CE2   1 
ATOM   2222  C  CZ    . TYR   A 1  282 ? -2.376  98.245  70.104  1.00 83.21  ? 282 TYR   A CZ    1 
ATOM   2223  O  OH    . TYR   A 1  282 ? -2.110  98.416  71.451  1.00 80.51  ? 282 TYR   A OH    1 
ATOM   2224  N  N     . HIS   A 1  283 ? -0.705  95.993  66.946  1.00 98.97  ? 283 HIS   A N     1 
ATOM   2225  C  CA    . HIS   A 1  283 ? -0.142  94.955  67.790  1.00 86.40  ? 283 HIS   A CA    1 
ATOM   2226  C  C     . HIS   A 1  283 ? -0.016  95.481  69.214  1.00 77.81  ? 283 HIS   A C     1 
ATOM   2227  O  O     . HIS   A 1  283 ? 0.526   96.571  69.428  1.00 74.63  ? 283 HIS   A O     1 
ATOM   2228  C  CB    . HIS   A 1  283 ? 1.218   94.524  67.233  1.00 78.03  ? 283 HIS   A CB    1 
ATOM   2229  C  CG    . HIS   A 1  283 ? 1.825   93.373  67.957  1.00 77.63  ? 283 HIS   A CG    1 
ATOM   2230  N  ND1   . HIS   A 1  283 ? 1.254   92.116  67.964  1.00 82.07  ? 283 HIS   A ND1   1 
ATOM   2231  C  CD2   . HIS   A 1  283 ? 2.950   93.284  68.705  1.00 67.59  ? 283 HIS   A CD2   1 
ATOM   2232  C  CE1   . HIS   A 1  283 ? 2.001   91.303  68.689  1.00 80.08  ? 283 HIS   A CE1   1 
ATOM   2233  N  NE2   . HIS   A 1  283 ? 3.035   91.986  69.149  1.00 86.97  ? 283 HIS   A NE2   1 
ATOM   2234  N  N     . GLU   A 1  284 ? -0.534  94.721  70.183  1.00 75.45  ? 284 GLU   A N     1 
ATOM   2235  C  CA    . GLU   A 1  284 ? -0.306  95.041  71.593  1.00 72.32  ? 284 GLU   A CA    1 
ATOM   2236  C  C     . GLU   A 1  284 ? 1.169   94.813  71.907  1.00 71.54  ? 284 GLU   A C     1 
ATOM   2237  O  O     . GLU   A 1  284 ? 1.625   93.666  71.979  1.00 62.69  ? 284 GLU   A O     1 
ATOM   2238  C  CB    . GLU   A 1  284 ? -1.208  94.204  72.502  1.00 50.40  ? 284 GLU   A CB    1 
ATOM   2239  N  N     . GLN   A 1  285 ? 1.912   95.911  72.087  1.00 73.34  ? 285 GLN   A N     1 
ATOM   2240  C  CA    . GLN   A 1  285 ? 3.365   95.857  72.231  1.00 63.42  ? 285 GLN   A CA    1 
ATOM   2241  C  C     . GLN   A 1  285 ? 3.794   95.064  73.471  1.00 60.14  ? 285 GLN   A C     1 
ATOM   2242  O  O     . GLN   A 1  285 ? 3.147   95.103  74.524  1.00 57.98  ? 285 GLN   A O     1 
ATOM   2243  C  CB    . GLN   A 1  285 ? 3.921   97.283  72.288  1.00 62.83  ? 285 GLN   A CB    1 
ATOM   2244  C  CG    . GLN   A 1  285 ? 5.392   97.407  71.927  1.00 63.97  ? 285 GLN   A CG    1 
ATOM   2245  C  CD    . GLN   A 1  285 ? 5.649   97.544  70.414  1.00 71.15  ? 285 GLN   A CD    1 
ATOM   2246  O  OE1   . GLN   A 1  285 ? 6.793   97.753  69.987  1.00 62.12  ? 285 GLN   A OE1   1 
ATOM   2247  N  NE2   . GLN   A 1  285 ? 4.590   97.422  69.606  1.00 58.80  ? 285 GLN   A NE2   1 
ATOM   2248  N  N     . LEU   A 1  286 ? 4.905   94.347  73.342  1.00 59.13  ? 286 LEU   A N     1 
ATOM   2249  C  CA    . LEU   A 1  286 ? 5.386   93.480  74.407  1.00 52.29  ? 286 LEU   A CA    1 
ATOM   2250  C  C     . LEU   A 1  286 ? 6.293   94.234  75.380  1.00 44.00  ? 286 LEU   A C     1 
ATOM   2251  O  O     . LEU   A 1  286 ? 7.020   95.158  75.004  1.00 39.24  ? 286 LEU   A O     1 
ATOM   2252  C  CB    . LEU   A 1  286 ? 6.141   92.283  73.824  1.00 55.10  ? 286 LEU   A CB    1 
ATOM   2253  C  CG    . LEU   A 1  286 ? 5.371   91.175  73.107  1.00 44.88  ? 286 LEU   A CG    1 
ATOM   2254  C  CD1   . LEU   A 1  286 ? 4.204   90.727  73.956  1.00 52.35  ? 286 LEU   A CD1   1 
ATOM   2255  C  CD2   . LEU   A 1  286 ? 4.901   91.658  71.763  1.00 51.57  ? 286 LEU   A CD2   1 
ATOM   2256  N  N     . SER   A 1  287 ? 6.257   93.806  76.637  1.00 40.88  ? 287 SER   A N     1 
ATOM   2257  C  CA    . SER   A 1  287 ? 7.038   94.389  77.720  1.00 43.79  ? 287 SER   A CA    1 
ATOM   2258  C  C     . SER   A 1  287 ? 8.415   93.737  77.826  1.00 40.46  ? 287 SER   A C     1 
ATOM   2259  O  O     . SER   A 1  287 ? 8.668   92.667  77.268  1.00 42.51  ? 287 SER   A O     1 
ATOM   2260  C  CB    . SER   A 1  287 ? 6.308   94.212  79.042  1.00 35.79  ? 287 SER   A CB    1 
ATOM   2261  O  OG    . SER   A 1  287 ? 6.292   92.835  79.376  1.00 44.79  ? 287 SER   A OG    1 
ATOM   2262  N  N     . VAL   A 1  288 ? 9.312   94.399  78.564  1.00 32.64  ? 288 VAL   A N     1 
ATOM   2263  C  CA    . VAL   A 1  288 ? 10.583  93.767  78.913  1.00 34.53  ? 288 VAL   A CA    1 
ATOM   2264  C  C     . VAL   A 1  288 ? 10.332  92.415  79.569  1.00 38.46  ? 288 VAL   A C     1 
ATOM   2265  O  O     . VAL   A 1  288 ? 10.987  91.414  79.245  1.00 33.31  ? 288 VAL   A O     1 
ATOM   2266  C  CB    . VAL   A 1  288 ? 11.413  94.692  79.820  1.00 30.39  ? 288 VAL   A CB    1 
ATOM   2267  C  CG1   . VAL   A 1  288 ? 12.626  93.949  80.392  1.00 21.87  ? 288 VAL   A CG1   1 
ATOM   2268  C  CG2   . VAL   A 1  288 ? 11.811  95.933  79.048  1.00 35.27  ? 288 VAL   A CG2   1 
ATOM   2269  N  N     . ALA   A 1  289 ? 9.372   92.356  80.492  1.00 33.88  ? 289 ALA   A N     1 
ATOM   2270  C  CA    . ALA   A 1  289 ? 9.014   91.062  81.054  1.00 36.80  ? 289 ALA   A CA    1 
ATOM   2271  C  C     . ALA   A 1  289 ? 8.654   90.093  79.940  1.00 41.57  ? 289 ALA   A C     1 
ATOM   2272  O  O     . ALA   A 1  289 ? 9.202   88.987  79.857  1.00 48.60  ? 289 ALA   A O     1 
ATOM   2273  C  CB    . ALA   A 1  289 ? 7.856   91.193  82.047  1.00 16.80  ? 289 ALA   A CB    1 
ATOM   2274  N  N     . GLU   A 1  290 ? 7.755   90.508  79.047  1.00 37.83  ? 290 GLU   A N     1 
ATOM   2275  C  CA    . GLU   A 1  290 ? 7.246   89.586  78.040  1.00 41.03  ? 290 GLU   A CA    1 
ATOM   2276  C  C     . GLU   A 1  290 ? 8.355   89.122  77.085  1.00 38.72  ? 290 GLU   A C     1 
ATOM   2277  O  O     . GLU   A 1  290 ? 8.488   87.922  76.817  1.00 30.59  ? 290 GLU   A O     1 
ATOM   2278  C  CB    . GLU   A 1  290 ? 6.066   90.237  77.312  1.00 35.49  ? 290 GLU   A CB    1 
ATOM   2279  C  CG    . GLU   A 1  290 ? 4.910   90.506  78.294  1.00 39.88  ? 290 GLU   A CG    1 
ATOM   2280  C  CD    . GLU   A 1  290 ? 3.677   91.210  77.693  1.00 57.89  ? 290 GLU   A CD    1 
ATOM   2281  O  OE1   . GLU   A 1  290 ? 3.818   92.238  76.975  1.00 52.37  ? 290 GLU   A OE1   1 
ATOM   2282  O  OE2   . GLU   A 1  290 ? 2.549   90.734  77.972  1.00 53.64  ? 290 GLU   A OE2   1 
ATOM   2283  N  N     . ILE   A 1  291 ? 9.193   90.044  76.598  1.00 40.30  ? 291 ILE   A N     1 
ATOM   2284  C  CA    . ILE   A 1  291 ? 10.216  89.641  75.632  1.00 35.04  ? 291 ILE   A CA    1 
ATOM   2285  C  C     . ILE   A 1  291 ? 11.297  88.812  76.309  1.00 36.34  ? 291 ILE   A C     1 
ATOM   2286  O  O     . ILE   A 1  291 ? 11.781  87.822  75.750  1.00 40.86  ? 291 ILE   A O     1 
ATOM   2287  C  CB    . ILE   A 1  291 ? 10.815  90.858  74.901  1.00 29.86  ? 291 ILE   A CB    1 
ATOM   2288  C  CG1   . ILE   A 1  291 ? 11.776  91.639  75.795  1.00 30.95  ? 291 ILE   A CG1   1 
ATOM   2289  C  CG2   . ILE   A 1  291 ? 9.724   91.744  74.333  1.00 31.59  ? 291 ILE   A CG2   1 
ATOM   2290  C  CD1   . ILE   A 1  291 ? 12.439  92.806  75.073  1.00 27.42  ? 291 ILE   A CD1   1 
ATOM   2291  N  N     . THR   A 1  292 ? 11.678  89.185  77.527  1.00 40.50  ? 292 THR   A N     1 
ATOM   2292  C  CA    . THR   A 1  292 ? 12.700  88.433  78.246  1.00 33.51  ? 292 THR   A CA    1 
ATOM   2293  C  C     . THR   A 1  292 ? 12.217  87.029  78.575  1.00 40.58  ? 292 THR   A C     1 
ATOM   2294  O  O     . THR   A 1  292 ? 12.996  86.067  78.534  1.00 46.45  ? 292 THR   A O     1 
ATOM   2295  C  CB    . THR   A 1  292 ? 13.090  89.186  79.513  1.00 26.83  ? 292 THR   A CB    1 
ATOM   2296  O  OG1   . THR   A 1  292 ? 13.483  90.510  79.146  1.00 35.26  ? 292 THR   A OG1   1 
ATOM   2297  C  CG2   . THR   A 1  292 ? 14.243  88.526  80.194  1.00 21.06  ? 292 THR   A CG2   1 
ATOM   2298  N  N     . ASN   A 1  293 ? 10.931  86.884  78.897  1.00 46.25  ? 293 ASN   A N     1 
ATOM   2299  C  CA    . ASN   A 1  293 ? 10.393  85.552  79.157  1.00 42.74  ? 293 ASN   A CA    1 
ATOM   2300  C  C     . ASN   A 1  293 ? 10.408  84.697  77.893  1.00 43.60  ? 293 ASN   A C     1 
ATOM   2301  O  O     . ASN   A 1  293 ? 10.867  83.547  77.909  1.00 41.48  ? 293 ASN   A O     1 
ATOM   2302  C  CB    . ASN   A 1  293 ? 8.983   85.655  79.710  1.00 35.54  ? 293 ASN   A CB    1 
ATOM   2303  C  CG    . ASN   A 1  293 ? 8.597   84.432  80.460  1.00 42.41  ? 293 ASN   A CG    1 
ATOM   2304  O  OD1   . ASN   A 1  293 ? 9.359   83.960  81.309  1.00 43.04  ? 293 ASN   A OD1   1 
ATOM   2305  N  ND2   . ASN   A 1  293 ? 7.438   83.868  80.129  1.00 30.20  ? 293 ASN   A ND2   1 
ATOM   2306  N  N     . ALA   A 1  294 ? 9.914   85.252  76.789  1.00 34.66  ? 294 ALA   A N     1 
ATOM   2307  C  CA    . ALA   A 1  294 ? 9.974   84.638  75.479  1.00 30.41  ? 294 ALA   A CA    1 
ATOM   2308  C  C     . ALA   A 1  294 ? 11.304  83.932  75.232  1.00 42.74  ? 294 ALA   A C     1 
ATOM   2309  O  O     . ALA   A 1  294 ? 11.358  82.946  74.492  1.00 38.07  ? 294 ALA   A O     1 
ATOM   2310  C  CB    . ALA   A 1  294 ? 9.744   85.707  74.418  1.00 33.62  ? 294 ALA   A CB    1 
ATOM   2311  N  N     . CYS   A 1  295 ? 12.384  84.422  75.845  1.00 39.57  ? 295 CYS   A N     1 
ATOM   2312  C  CA    . CYS   A 1  295 ? 13.707  83.889  75.559  1.00 32.88  ? 295 CYS   A CA    1 
ATOM   2313  C  C     . CYS   A 1  295 ? 13.902  82.471  76.065  1.00 33.91  ? 295 CYS   A C     1 
ATOM   2314  O  O     . CYS   A 1  295 ? 14.892  81.826  75.692  1.00 41.19  ? 295 CYS   A O     1 
ATOM   2315  C  CB    . CYS   A 1  295 ? 14.779  84.809  76.154  1.00 41.44  ? 295 CYS   A CB    1 
ATOM   2316  S  SG    . CYS   A 1  295 ? 15.060  86.332  75.193  1.00 41.17  ? 295 CYS   A SG    1 
ATOM   2317  N  N     . PHE   A 1  296 ? 13.014  81.977  76.921  1.00 36.08  ? 296 PHE   A N     1 
ATOM   2318  C  CA    . PHE   A 1  296 ? 13.129  80.629  77.467  1.00 41.50  ? 296 PHE   A CA    1 
ATOM   2319  C  C     . PHE   A 1  296 ? 12.042  79.715  76.915  1.00 39.36  ? 296 PHE   A C     1 
ATOM   2320  O  O     . PHE   A 1  296 ? 11.757  78.662  77.487  1.00 37.88  ? 296 PHE   A O     1 
ATOM   2321  C  CB    . PHE   A 1  296 ? 13.116  80.669  79.000  1.00 25.47  ? 296 PHE   A CB    1 
ATOM   2322  C  CG    . PHE   A 1  296 ? 14.235  81.482  79.568  1.00 36.57  ? 296 PHE   A CG    1 
ATOM   2323  C  CD1   . PHE   A 1  296 ? 14.163  82.869  79.578  1.00 37.94  ? 296 PHE   A CD1   1 
ATOM   2324  C  CD2   . PHE   A 1  296 ? 15.387  80.873  80.044  1.00 36.32  ? 296 PHE   A CD2   1 
ATOM   2325  C  CE1   . PHE   A 1  296 ? 15.198  83.617  80.065  1.00 28.85  ? 296 PHE   A CE1   1 
ATOM   2326  C  CE2   . PHE   A 1  296 ? 16.429  81.622  80.538  1.00 24.37  ? 296 PHE   A CE2   1 
ATOM   2327  C  CZ    . PHE   A 1  296 ? 16.335  82.987  80.549  1.00 31.75  ? 296 PHE   A CZ    1 
ATOM   2328  N  N     . GLU   A 1  297 ? 11.436  80.109  75.804  1.00 36.44  ? 297 GLU   A N     1 
ATOM   2329  C  CA    . GLU   A 1  297 ? 10.490  79.280  75.096  1.00 36.41  ? 297 GLU   A CA    1 
ATOM   2330  C  C     . GLU   A 1  297 ? 11.195  78.610  73.929  1.00 48.49  ? 297 GLU   A C     1 
ATOM   2331  O  O     . GLU   A 1  297 ? 11.761  79.302  73.060  1.00 36.66  ? 297 GLU   A O     1 
ATOM   2332  C  CB    . GLU   A 1  297 ? 9.324   80.114  74.603  1.00 30.39  ? 297 GLU   A CB    1 
ATOM   2333  C  CG    . GLU   A 1  297 ? 8.408   80.526  75.710  1.00 43.03  ? 297 GLU   A CG    1 
ATOM   2334  C  CD    . GLU   A 1  297 ? 7.675   79.354  76.288  1.00 51.45  ? 297 GLU   A CD    1 
ATOM   2335  O  OE1   . GLU   A 1  297 ? 7.661   78.292  75.638  1.00 61.55  ? 297 GLU   A OE1   1 
ATOM   2336  O  OE2   . GLU   A 1  297 ? 7.111   79.492  77.387  1.00 60.74  ? 297 GLU   A OE2   1 
ATOM   2337  N  N     . PRO   A 1  298 ? 11.205  77.285  73.874  1.00 44.20  ? 298 PRO   A N     1 
ATOM   2338  C  CA    . PRO   A 1  298 ? 11.849  76.613  72.741  1.00 29.71  ? 298 PRO   A CA    1 
ATOM   2339  C  C     . PRO   A 1  298 ? 11.447  77.194  71.391  1.00 33.77  ? 298 PRO   A C     1 
ATOM   2340  O  O     . PRO   A 1  298 ? 12.292  77.270  70.490  1.00 35.31  ? 298 PRO   A O     1 
ATOM   2341  C  CB    . PRO   A 1  298 ? 11.381  75.164  72.906  1.00 34.13  ? 298 PRO   A CB    1 
ATOM   2342  C  CG    . PRO   A 1  298 ? 11.062  75.036  74.368  1.00 46.03  ? 298 PRO   A CG    1 
ATOM   2343  C  CD    . PRO   A 1  298 ? 10.523  76.351  74.786  1.00 37.92  ? 298 PRO   A CD    1 
ATOM   2344  N  N     . ALA   A 1  299 ? 10.185  77.623  71.224  1.00 28.40  ? 299 ALA   A N     1 
ATOM   2345  C  CA    . ALA   A 1  299 ? 9.718   78.056  69.906  1.00 26.65  ? 299 ALA   A CA    1 
ATOM   2346  C  C     . ALA   A 1  299 ? 10.330  79.365  69.452  1.00 27.75  ? 299 ALA   A C     1 
ATOM   2347  O  O     . ALA   A 1  299 ? 10.004  79.832  68.358  1.00 23.56  ? 299 ALA   A O     1 
ATOM   2348  C  CB    . ALA   A 1  299 ? 8.196   78.193  69.875  1.00 24.54  ? 299 ALA   A CB    1 
ATOM   2349  N  N     . ASN   A 1  300 ? 11.202  79.971  70.245  1.00 26.40  ? 300 ASN   A N     1 
ATOM   2350  C  CA    . ASN   A 1  300 ? 11.862  81.201  69.845  1.00 31.11  ? 300 ASN   A CA    1 
ATOM   2351  C  C     . ASN   A 1  300 ? 13.342  81.001  69.549  1.00 26.55  ? 300 ASN   A C     1 
ATOM   2352  O  O     . ASN   A 1  300 ? 13.996  81.919  69.056  1.00 31.07  ? 300 ASN   A O     1 
ATOM   2353  C  CB    . ASN   A 1  300 ? 11.641  82.258  70.926  1.00 25.92  ? 300 ASN   A CB    1 
ATOM   2354  C  CG    . ASN   A 1  300 ? 10.172  82.555  71.121  1.00 33.72  ? 300 ASN   A CG    1 
ATOM   2355  O  OD1   . ASN   A 1  300 ? 9.441   82.719  70.148  1.00 33.15  ? 300 ASN   A OD1   1 
ATOM   2356  N  ND2   . ASN   A 1  300 ? 9.723   82.604  72.369  1.00 37.20  ? 300 ASN   A ND2   1 
ATOM   2357  N  N     . GLN   A 1  301 ? 13.864  79.810  69.788  1.00 24.50  ? 301 GLN   A N     1 
ATOM   2358  C  CA    . GLN   A 1  301 ? 15.281  79.536  69.645  1.00 32.16  ? 301 GLN   A CA    1 
ATOM   2359  C  C     . GLN   A 1  301 ? 15.652  79.311  68.177  1.00 28.09  ? 301 GLN   A C     1 
ATOM   2360  O  O     . GLN   A 1  301 ? 14.828  78.899  67.359  1.00 30.34  ? 301 GLN   A O     1 
ATOM   2361  C  CB    . GLN   A 1  301 ? 15.639  78.324  70.510  1.00 30.89  ? 301 GLN   A CB    1 
ATOM   2362  C  CG    . GLN   A 1  301 ? 14.937  78.372  71.876  1.00 23.33  ? 301 GLN   A CG    1 
ATOM   2363  C  CD    . GLN   A 1  301 ? 15.228  77.181  72.752  1.00 28.44  ? 301 GLN   A CD    1 
ATOM   2364  O  OE1   . GLN   A 1  301 ? 15.237  77.285  73.971  1.00 41.83  ? 301 GLN   A OE1   1 
ATOM   2365  N  NE2   . GLN   A 1  301 ? 15.463  76.040  72.143  1.00 36.35  ? 301 GLN   A NE2   1 
ATOM   2366  N  N     . MET   A 1  302 ? 16.898  79.647  67.837  1.00 27.28  ? 302 MET   A N     1 
ATOM   2367  C  CA    . MET   A 1  302 ? 17.450  79.332  66.525  1.00 24.81  ? 302 MET   A CA    1 
ATOM   2368  C  C     . MET   A 1  302 ? 17.685  77.843  66.358  1.00 24.53  ? 302 MET   A C     1 
ATOM   2369  O  O     . MET   A 1  302 ? 18.026  77.406  65.266  1.00 35.25  ? 302 MET   A O     1 
ATOM   2370  C  CB    . MET   A 1  302 ? 18.761  80.096  66.298  1.00 18.06  ? 302 MET   A CB    1 
ATOM   2371  C  CG    . MET   A 1  302 ? 18.612  81.422  65.541  1.00 29.41  ? 302 MET   A CG    1 
ATOM   2372  S  SD    . MET   A 1  302 ? 17.309  82.529  66.146  1.00 53.23  ? 302 MET   A SD    1 
ATOM   2373  C  CE    . MET   A 1  302 ? 15.893  81.956  65.240  1.00 27.20  ? 302 MET   A CE    1 
ATOM   2374  N  N     . VAL   A 1  303 ? 17.524  77.068  67.419  1.00 27.08  ? 303 VAL   A N     1 
ATOM   2375  C  CA    . VAL   A 1  303 ? 17.642  75.623  67.397  1.00 25.48  ? 303 VAL   A CA    1 
ATOM   2376  C  C     . VAL   A 1  303 ? 16.605  75.085  68.366  1.00 33.63  ? 303 VAL   A C     1 
ATOM   2377  O  O     . VAL   A 1  303 ? 16.630  75.432  69.551  1.00 42.32  ? 303 VAL   A O     1 
ATOM   2378  C  CB    . VAL   A 1  303 ? 19.044  75.146  67.812  1.00 34.78  ? 303 VAL   A CB    1 
ATOM   2379  C  CG1   . VAL   A 1  303 ? 19.089  73.632  67.840  1.00 29.59  ? 303 VAL   A CG1   1 
ATOM   2380  C  CG2   . VAL   A 1  303 ? 20.120  75.745  66.904  1.00 25.83  ? 303 VAL   A CG2   1 
ATOM   2381  N  N     . LYS   A 1  304 ? 15.688  74.260  67.879  1.00 33.07  ? 304 LYS   A N     1 
ATOM   2382  C  CA    . LYS   A 1  304 ? 14.750  73.607  68.778  1.00 26.80  ? 304 LYS   A CA    1 
ATOM   2383  C  C     . LYS   A 1  304 ? 15.503  72.653  69.689  1.00 26.67  ? 304 LYS   A C     1 
ATOM   2384  O  O     . LYS   A 1  304 ? 16.331  71.864  69.232  1.00 48.53  ? 304 LYS   A O     1 
ATOM   2385  C  CB    . LYS   A 1  304 ? 13.676  72.856  67.987  1.00 31.44  ? 304 LYS   A CB    1 
ATOM   2386  C  CG    . LYS   A 1  304 ? 12.775  73.753  67.179  1.00 27.12  ? 304 LYS   A CG    1 
ATOM   2387  C  CD    . LYS   A 1  304 ? 11.481  73.071  66.829  1.00 32.27  ? 304 LYS   A CD    1 
ATOM   2388  C  CE    . LYS   A 1  304 ? 10.636  73.957  65.907  1.00 43.77  ? 304 LYS   A CE    1 
ATOM   2389  N  NZ    . LYS   A 1  304 ? 9.255   73.390  65.727  1.00 52.83  ? 304 LYS   A NZ    1 
ATOM   2390  N  N     . CYS   A 1  305 ? 15.219  72.721  70.978  1.00 33.23  ? 305 CYS   A N     1 
ATOM   2391  C  CA    . CYS   A 1  305 ? 15.857  71.884  71.991  1.00 32.32  ? 305 CYS   A CA    1 
ATOM   2392  C  C     . CYS   A 1  305 ? 15.302  72.403  73.305  1.00 27.19  ? 305 CYS   A C     1 
ATOM   2393  O  O     . CYS   A 1  305 ? 14.653  73.450  73.339  1.00 35.62  ? 305 CYS   A O     1 
ATOM   2394  C  CB    . CYS   A 1  305 ? 17.388  71.946  71.950  1.00 31.36  ? 305 CYS   A CB    1 
ATOM   2395  S  SG    . CYS   A 1  305 ? 18.172  73.594  72.188  1.00 36.62  ? 305 CYS   A SG    1 
ATOM   2396  N  N     . ASP   A 1  306 ? 15.577  71.689  74.390  1.00 31.12  ? 306 ASP   A N     1 
ATOM   2397  C  CA    . ASP   A 1  306 ? 14.927  71.980  75.670  1.00 33.32  ? 306 ASP   A CA    1 
ATOM   2398  C  C     . ASP   A 1  306 ? 15.996  72.301  76.705  1.00 28.18  ? 306 ASP   A C     1 
ATOM   2399  O  O     . ASP   A 1  306 ? 16.518  71.386  77.361  1.00 35.18  ? 306 ASP   A O     1 
ATOM   2400  C  CB    . ASP   A 1  306 ? 14.048  70.800  76.110  1.00 32.23  ? 306 ASP   A CB    1 
ATOM   2401  C  CG    . ASP   A 1  306 ? 13.113  71.140  77.269  1.00 39.28  ? 306 ASP   A CG    1 
ATOM   2402  O  OD1   . ASP   A 1  306 ? 13.388  72.097  78.016  1.00 43.59  ? 306 ASP   A OD1   1 
ATOM   2403  O  OD2   . ASP   A 1  306 ? 12.100  70.435  77.445  1.00 40.29  ? 306 ASP   A OD2   1 
ATOM   2404  N  N     . PRO   A 1  307 ? 16.328  73.582  76.921  1.00 36.05  ? 307 PRO   A N     1 
ATOM   2405  C  CA    . PRO   A 1  307 ? 17.391  73.904  77.899  1.00 41.32  ? 307 PRO   A CA    1 
ATOM   2406  C  C     . PRO   A 1  307 ? 17.037  73.579  79.356  1.00 31.00  ? 307 PRO   A C     1 
ATOM   2407  O  O     . PRO   A 1  307 ? 17.925  73.655  80.209  1.00 41.65  ? 307 PRO   A O     1 
ATOM   2408  C  CB    . PRO   A 1  307 ? 17.637  75.416  77.696  1.00 26.41  ? 307 PRO   A CB    1 
ATOM   2409  C  CG    . PRO   A 1  307 ? 16.866  75.818  76.479  1.00 30.62  ? 307 PRO   A CG    1 
ATOM   2410  C  CD    . PRO   A 1  307 ? 15.761  74.801  76.308  1.00 37.16  ? 307 PRO   A CD    1 
ATOM   2411  N  N     . ARG   A 1  308 ? 15.794  73.202  79.668  1.00 36.27  ? 308 ARG   A N     1 
ATOM   2412  C  CA    . ARG   A 1  308 ? 15.513  72.658  80.995  1.00 39.89  ? 308 ARG   A CA    1 
ATOM   2413  C  C     . ARG   A 1  308 ? 16.304  71.383  81.255  1.00 42.64  ? 308 ARG   A C     1 
ATOM   2414  O  O     . ARG   A 1  308 ? 16.697  71.123  82.397  1.00 54.37  ? 308 ARG   A O     1 
ATOM   2415  C  CB    . ARG   A 1  308 ? 14.021  72.367  81.177  1.00 34.59  ? 308 ARG   A CB    1 
ATOM   2416  C  CG    . ARG   A 1  308 ? 13.105  73.560  81.077  1.00 29.99  ? 308 ARG   A CG    1 
ATOM   2417  C  CD    . ARG   A 1  308 ? 11.647  73.120  81.101  1.00 31.48  ? 308 ARG   A CD    1 
ATOM   2418  N  NE    . ARG   A 1  308 ? 11.369  72.184  80.020  1.00 42.11  ? 308 ARG   A NE    1 
ATOM   2419  C  CZ    . ARG   A 1  308 ? 10.207  71.580  79.811  1.00 37.63  ? 308 ARG   A CZ    1 
ATOM   2420  N  NH1   . ARG   A 1  308 ? 9.161   71.801  80.594  1.00 31.33  ? 308 ARG   A NH1   1 
ATOM   2421  N  NH2   . ARG   A 1  308 ? 10.097  70.722  78.798  1.00 27.36  ? 308 ARG   A NH2   1 
ATOM   2422  N  N     . HIS   A 1  309 ? 16.545  70.573  80.230  1.00 39.78  ? 309 HIS   A N     1 
ATOM   2423  C  CA    . HIS   A 1  309 ? 17.260  69.310  80.415  1.00 33.02  ? 309 HIS   A CA    1 
ATOM   2424  C  C     . HIS   A 1  309 ? 18.713  69.444  79.967  1.00 41.40  ? 309 HIS   A C     1 
ATOM   2425  O  O     . HIS   A 1  309 ? 19.227  68.728  79.109  1.00 56.11  ? 309 HIS   A O     1 
ATOM   2426  C  CB    . HIS   A 1  309 ? 16.533  68.189  79.693  1.00 42.74  ? 309 HIS   A CB    1 
ATOM   2427  C  CG    . HIS   A 1  309 ? 15.181  67.921  80.267  1.00 41.38  ? 309 HIS   A CG    1 
ATOM   2428  N  ND1   . HIS   A 1  309 ? 14.040  68.536  79.798  1.00 37.36  ? 309 HIS   A ND1   1 
ATOM   2429  C  CD2   . HIS   A 1  309 ? 14.797  67.155  81.315  1.00 38.23  ? 309 HIS   A CD2   1 
ATOM   2430  C  CE1   . HIS   A 1  309 ? 13.005  68.138  80.514  1.00 40.13  ? 309 HIS   A CE1   1 
ATOM   2431  N  NE2   . HIS   A 1  309 ? 13.438  67.298  81.441  1.00 43.78  ? 309 HIS   A NE2   1 
ATOM   2432  N  N     . GLY   A 1  310 ? 19.356  70.414  80.593  1.00 42.21  ? 310 GLY   A N     1 
ATOM   2433  C  CA    . GLY   A 1  310 ? 20.783  70.627  80.495  1.00 39.10  ? 310 GLY   A CA    1 
ATOM   2434  C  C     . GLY   A 1  310 ? 21.126  71.756  81.433  1.00 41.02  ? 310 GLY   A C     1 
ATOM   2435  O  O     . GLY   A 1  310 ? 20.250  72.351  82.064  1.00 49.93  ? 310 GLY   A O     1 
ATOM   2436  N  N     . LYS   A 1  311 ? 22.409  72.051  81.530  1.00 38.42  ? 311 LYS   A N     1 
ATOM   2437  C  CA    . LYS   A 1  311 ? 22.853  73.113  82.409  1.00 36.65  ? 311 LYS   A CA    1 
ATOM   2438  C  C     . LYS   A 1  311 ? 23.381  74.249  81.548  1.00 38.45  ? 311 LYS   A C     1 
ATOM   2439  O  O     . LYS   A 1  311 ? 23.604  74.085  80.350  1.00 41.70  ? 311 LYS   A O     1 
ATOM   2440  C  CB    . LYS   A 1  311 ? 23.926  72.624  83.400  1.00 46.86  ? 311 LYS   A CB    1 
ATOM   2441  C  CG    . LYS   A 1  311 ? 23.765  71.193  83.995  1.00 48.77  ? 311 LYS   A CG    1 
ATOM   2442  C  CD    . LYS   A 1  311 ? 22.636  71.011  85.037  1.00 66.33  ? 311 LYS   A CD    1 
ATOM   2443  C  CE    . LYS   A 1  311 ? 21.290  70.473  84.427  1.00 76.27  ? 311 LYS   A CE    1 
ATOM   2444  N  NZ    . LYS   A 1  311 ? 21.238  69.035  83.912  1.00 68.80  ? 311 LYS   A NZ    1 
ATOM   2445  N  N     . TYR   A 1  312 ? 23.525  75.421  82.159  1.00 48.79  ? 312 TYR   A N     1 
ATOM   2446  C  CA    . TYR   A 1  312 ? 24.061  76.609  81.506  1.00 38.50  ? 312 TYR   A CA    1 
ATOM   2447  C  C     . TYR   A 1  312 ? 25.489  76.846  81.954  1.00 41.04  ? 312 TYR   A C     1 
ATOM   2448  O  O     . TYR   A 1  312 ? 25.868  76.523  83.084  1.00 41.56  ? 312 TYR   A O     1 
ATOM   2449  C  CB    . TYR   A 1  312 ? 23.263  77.869  81.841  1.00 33.41  ? 312 TYR   A CB    1 
ATOM   2450  C  CG    . TYR   A 1  312 ? 21.904  77.937  81.238  1.00 35.09  ? 312 TYR   A CG    1 
ATOM   2451  C  CD1   . TYR   A 1  312 ? 20.837  77.284  81.820  1.00 33.76  ? 312 TYR   A CD1   1 
ATOM   2452  C  CD2   . TYR   A 1  312 ? 21.673  78.684  80.088  1.00 42.15  ? 312 TYR   A CD2   1 
ATOM   2453  C  CE1   . TYR   A 1  312 ? 19.567  77.352  81.262  1.00 34.61  ? 312 TYR   A CE1   1 
ATOM   2454  C  CE2   . TYR   A 1  312 ? 20.400  78.764  79.525  1.00 32.13  ? 312 TYR   A CE2   1 
ATOM   2455  C  CZ    . TYR   A 1  312 ? 19.360  78.092  80.123  1.00 27.63  ? 312 TYR   A CZ    1 
ATOM   2456  O  OH    . TYR   A 1  312 ? 18.112  78.165  79.569  1.00 42.65  ? 312 TYR   A OH    1 
ATOM   2457  N  N     . MET   A 1  313 ? 26.265  77.452  81.062  1.00 37.03  ? 313 MET   A N     1 
ATOM   2458  C  CA    . MET   A 1  313 ? 27.599  77.915  81.386  1.00 38.02  ? 313 MET   A CA    1 
ATOM   2459  C  C     . MET   A 1  313 ? 27.750  79.415  81.237  1.00 39.08  ? 313 MET   A C     1 
ATOM   2460  O  O     . MET   A 1  313 ? 28.699  79.977  81.786  1.00 52.44  ? 313 MET   A O     1 
ATOM   2461  C  CB    . MET   A 1  313 ? 28.639  77.208  80.499  1.00 40.24  ? 313 MET   A CB    1 
ATOM   2462  C  CG    . MET   A 1  313 ? 28.605  75.672  80.601  1.00 39.63  ? 313 MET   A CG    1 
ATOM   2463  S  SD    . MET   A 1  313 ? 29.388  74.809  79.201  1.00 42.24  ? 313 MET   A SD    1 
ATOM   2464  C  CE    . MET   A 1  313 ? 28.010  74.757  78.048  1.00 37.77  ? 313 MET   A CE    1 
ATOM   2465  N  N     . ALA   A 1  314 ? 26.844  80.075  80.526  1.00 36.68  ? 314 ALA   A N     1 
ATOM   2466  C  CA    . ALA   A 1  314 ? 26.936  81.501  80.249  1.00 37.15  ? 314 ALA   A CA    1 
ATOM   2467  C  C     . ALA   A 1  314 ? 25.609  81.953  79.655  1.00 40.50  ? 314 ALA   A C     1 
ATOM   2468  O  O     . ALA   A 1  314 ? 24.818  81.139  79.176  1.00 44.81  ? 314 ALA   A O     1 
ATOM   2469  C  CB    . ALA   A 1  314 ? 28.098  81.817  79.305  1.00 34.71  ? 314 ALA   A CB    1 
ATOM   2470  N  N     . CYS   A 1  315 ? 25.376  83.260  79.684  1.00 37.46  ? 315 CYS   A N     1 
ATOM   2471  C  CA    A CYS   A 1  315 ? 24.094  83.796  79.255  0.57 36.03  ? 315 CYS   A CA    1 
ATOM   2472  C  CA    B CYS   A 1  315 ? 24.085  83.807  79.287  0.43 36.07  ? 315 CYS   A CA    1 
ATOM   2473  C  C     . CYS   A 1  315 ? 24.182  85.307  79.066  1.00 41.80  ? 315 CYS   A C     1 
ATOM   2474  O  O     . CYS   A 1  315 ? 24.590  86.039  79.973  1.00 44.27  ? 315 CYS   A O     1 
ATOM   2475  C  CB    A CYS   A 1  315 ? 23.008  83.428  80.272  0.57 37.79  ? 315 CYS   A CB    1 
ATOM   2476  C  CB    B CYS   A 1  315 ? 23.027  83.519  80.351  0.43 37.80  ? 315 CYS   A CB    1 
ATOM   2477  S  SG    A CYS   A 1  315 ? 21.335  83.208  79.595  0.57 34.80  ? 315 CYS   A SG    1 
ATOM   2478  S  SG    B CYS   A 1  315 ? 22.302  81.883  80.293  0.43 31.55  ? 315 CYS   A SG    1 
ATOM   2479  N  N     . CYS   A 1  316 ? 23.801  85.776  77.883  1.00 42.66  ? 316 CYS   A N     1 
ATOM   2480  C  CA    A CYS   A 1  316 ? 23.855  87.188  77.539  0.69 37.09  ? 316 CYS   A CA    1 
ATOM   2481  C  CA    B CYS   A 1  316 ? 23.861  87.187  77.536  0.31 37.17  ? 316 CYS   A CA    1 
ATOM   2482  C  C     . CYS   A 1  316 ? 22.489  87.635  77.053  1.00 42.19  ? 316 CYS   A C     1 
ATOM   2483  O  O     . CYS   A 1  316 ? 21.845  86.940  76.258  1.00 42.02  ? 316 CYS   A O     1 
ATOM   2484  C  CB    A CYS   A 1  316 ? 24.881  87.471  76.442  0.69 37.22  ? 316 CYS   A CB    1 
ATOM   2485  C  CB    B CYS   A 1  316 ? 24.924  87.431  76.457  0.31 37.24  ? 316 CYS   A CB    1 
ATOM   2486  S  SG    A CYS   A 1  316 ? 26.579  87.384  76.961  0.69 37.10  ? 316 CYS   A SG    1 
ATOM   2487  S  SG    B CYS   A 1  316 ? 25.497  89.135  76.287  0.31 38.40  ? 316 CYS   A SG    1 
ATOM   2488  N  N     . LEU   A 1  317 ? 22.047  88.784  77.538  1.00 45.20  ? 317 LEU   A N     1 
ATOM   2489  C  CA    . LEU   A 1  317 ? 20.826  89.420  77.068  1.00 35.03  ? 317 LEU   A CA    1 
ATOM   2490  C  C     . LEU   A 1  317 ? 21.232  90.645  76.268  1.00 30.89  ? 317 LEU   A C     1 
ATOM   2491  O  O     . LEU   A 1  317 ? 21.881  91.550  76.803  1.00 36.19  ? 317 LEU   A O     1 
ATOM   2492  C  CB    . LEU   A 1  317 ? 19.916  89.796  78.237  1.00 33.33  ? 317 LEU   A CB    1 
ATOM   2493  C  CG    . LEU   A 1  317 ? 19.251  88.596  78.912  1.00 41.66  ? 317 LEU   A CG    1 
ATOM   2494  C  CD1   . LEU   A 1  317 ? 18.531  89.022  80.183  1.00 41.79  ? 317 LEU   A CD1   1 
ATOM   2495  C  CD2   . LEU   A 1  317 ? 18.272  87.895  77.943  1.00 35.38  ? 317 LEU   A CD2   1 
ATOM   2496  N  N     . LEU   A 1  318 ? 20.877  90.668  74.993  1.00 25.14  ? 318 LEU   A N     1 
ATOM   2497  C  CA    . LEU   A 1  318 ? 21.174  91.806  74.135  1.00 28.35  ? 318 LEU   A CA    1 
ATOM   2498  C  C     . LEU   A 1  318 ? 19.852  92.461  73.791  1.00 29.51  ? 318 LEU   A C     1 
ATOM   2499  O  O     . LEU   A 1  318 ? 19.018  91.849  73.112  1.00 27.76  ? 318 LEU   A O     1 
ATOM   2500  C  CB    . LEU   A 1  318 ? 21.937  91.384  72.877  1.00 35.77  ? 318 LEU   A CB    1 
ATOM   2501  C  CG    . LEU   A 1  318 ? 23.258  90.664  73.158  1.00 33.86  ? 318 LEU   A CG    1 
ATOM   2502  C  CD1   . LEU   A 1  318 ? 24.044  90.417  71.898  1.00 26.50  ? 318 LEU   A CD1   1 
ATOM   2503  C  CD2   . LEU   A 1  318 ? 24.069  91.457  74.173  1.00 32.54  ? 318 LEU   A CD2   1 
ATOM   2504  N  N     . TYR   A 1  319 ? 19.661  93.696  74.269  1.00 30.92  ? 319 TYR   A N     1 
ATOM   2505  C  CA    . TYR   A 1  319 ? 18.422  94.445  74.091  1.00 27.88  ? 319 TYR   A CA    1 
ATOM   2506  C  C     . TYR   A 1  319 ? 18.594  95.539  73.056  1.00 27.43  ? 319 TYR   A C     1 
ATOM   2507  O  O     . TYR   A 1  319 ? 19.680  96.087  72.874  1.00 33.01  ? 319 TYR   A O     1 
ATOM   2508  C  CB    . TYR   A 1  319 ? 17.946  95.081  75.391  1.00 26.77  ? 319 TYR   A CB    1 
ATOM   2509  C  CG    . TYR   A 1  319 ? 17.414  94.093  76.382  1.00 30.68  ? 319 TYR   A CG    1 
ATOM   2510  C  CD1   . TYR   A 1  319 ? 16.091  93.674  76.332  1.00 24.10  ? 319 TYR   A CD1   1 
ATOM   2511  C  CD2   . TYR   A 1  319 ? 18.240  93.576  77.377  1.00 27.81  ? 319 TYR   A CD2   1 
ATOM   2512  C  CE1   . TYR   A 1  319 ? 15.614  92.759  77.243  1.00 28.27  ? 319 TYR   A CE1   1 
ATOM   2513  C  CE2   . TYR   A 1  319 ? 17.770  92.672  78.299  1.00 25.46  ? 319 TYR   A CE2   1 
ATOM   2514  C  CZ    . TYR   A 1  319 ? 16.461  92.269  78.231  1.00 29.87  ? 319 TYR   A CZ    1 
ATOM   2515  O  OH    . TYR   A 1  319 ? 16.012  91.353  79.146  1.00 29.23  ? 319 TYR   A OH    1 
ATOM   2516  N  N     . ARG   A 1  320 ? 17.496  95.854  72.385  1.00 32.79  ? 320 ARG   A N     1 
ATOM   2517  C  CA    . ARG   A 1  320 ? 17.486  96.868  71.340  1.00 40.18  ? 320 ARG   A CA    1 
ATOM   2518  C  C     . ARG   A 1  320 ? 16.163  97.597  71.424  1.00 39.70  ? 320 ARG   A C     1 
ATOM   2519  O  O     . ARG   A 1  320 ? 15.106  96.987  71.238  1.00 37.76  ? 320 ARG   A O     1 
ATOM   2520  C  CB    . ARG   A 1  320 ? 17.666  96.270  69.941  1.00 33.98  ? 320 ARG   A CB    1 
ATOM   2521  C  CG    . ARG   A 1  320 ? 19.069  95.796  69.629  1.00 26.17  ? 320 ARG   A CG    1 
ATOM   2522  C  CD    . ARG   A 1  320 ? 19.174  95.366  68.155  1.00 39.03  ? 320 ARG   A CD    1 
ATOM   2523  N  NE    . ARG   A 1  320 ? 19.683  96.423  67.284  1.00 31.90  ? 320 ARG   A NE    1 
ATOM   2524  C  CZ    . ARG   A 1  320 ? 20.421  96.201  66.204  1.00 42.67  ? 320 ARG   A CZ    1 
ATOM   2525  N  NH1   . ARG   A 1  320 ? 20.698  94.971  65.800  1.00 38.09  ? 320 ARG   A NH1   1 
ATOM   2526  N  NH2   . ARG   A 1  320 ? 20.910  97.236  65.524  1.00 38.24  ? 320 ARG   A NH2   1 
ATOM   2527  N  N     . GLY   A 1  321 ? 16.234  98.895  71.680  1.00 40.74  ? 321 GLY   A N     1 
ATOM   2528  C  CA    . GLY   A 1  321 ? 15.053  99.717  71.792  1.00 43.57  ? 321 GLY   A CA    1 
ATOM   2529  C  C     . GLY   A 1  321 ? 14.985  100.373 73.151  1.00 46.14  ? 321 GLY   A C     1 
ATOM   2530  O  O     . GLY   A 1  321 ? 15.985  100.906 73.652  1.00 40.55  ? 321 GLY   A O     1 
ATOM   2531  N  N     . ASP   A 1  322 ? 13.816  100.285 73.773  1.00 36.14  ? 322 ASP   A N     1 
ATOM   2532  C  CA    . ASP   A 1  322 ? 13.451  101.089 74.931  1.00 38.09  ? 322 ASP   A CA    1 
ATOM   2533  C  C     . ASP   A 1  322 ? 13.479  100.188 76.166  1.00 39.52  ? 322 ASP   A C     1 
ATOM   2534  O  O     . ASP   A 1  322 ? 12.479  99.561  76.524  1.00 40.70  ? 322 ASP   A O     1 
ATOM   2535  C  CB    . ASP   A 1  322 ? 12.086  101.733 74.668  1.00 44.00  ? 322 ASP   A CB    1 
ATOM   2536  C  CG    . ASP   A 1  322 ? 11.513  102.422 75.873  1.00 51.82  ? 322 ASP   A CG    1 
ATOM   2537  O  OD1   . ASP   A 1  322 ? 12.217  103.278 76.473  1.00 46.75  ? 322 ASP   A OD1   1 
ATOM   2538  O  OD2   . ASP   A 1  322 ? 10.341  102.107 76.192  1.00 44.50  ? 322 ASP   A OD2   1 
ATOM   2539  N  N     . VAL   A 1  323 ? 14.640  100.131 76.814  1.00 28.94  ? 323 VAL   A N     1 
ATOM   2540  C  CA    . VAL   A 1  323 ? 14.885  99.208  77.916  1.00 40.50  ? 323 VAL   A CA    1 
ATOM   2541  C  C     . VAL   A 1  323 ? 15.788  99.884  78.949  1.00 46.52  ? 323 VAL   A C     1 
ATOM   2542  O  O     . VAL   A 1  323 ? 16.798  100.500 78.588  1.00 46.18  ? 323 VAL   A O     1 
ATOM   2543  C  CB    . VAL   A 1  323 ? 15.526  97.903  77.398  1.00 39.95  ? 323 VAL   A CB    1 
ATOM   2544  C  CG1   . VAL   A 1  323 ? 15.765  96.900  78.543  1.00 29.21  ? 323 VAL   A CG1   1 
ATOM   2545  C  CG2   . VAL   A 1  323 ? 14.673  97.307  76.275  1.00 33.27  ? 323 VAL   A CG2   1 
ATOM   2546  N  N     . VAL   A 1  324 ? 15.427  99.774  80.228  1.00 38.61  ? 324 VAL   A N     1 
ATOM   2547  C  CA    . VAL   A 1  324 ? 16.266  100.290 81.315  1.00 47.18  ? 324 VAL   A CA    1 
ATOM   2548  C  C     . VAL   A 1  324 ? 16.530  99.169  82.314  1.00 45.36  ? 324 VAL   A C     1 
ATOM   2549  O  O     . VAL   A 1  324 ? 15.665  98.299  82.514  1.00 41.16  ? 324 VAL   A O     1 
ATOM   2550  C  CB    . VAL   A 1  324 ? 15.645  101.519 82.022  1.00 53.38  ? 324 VAL   A CB    1 
ATOM   2551  C  CG1   . VAL   A 1  324 ? 15.937  102.810 81.247  1.00 38.07  ? 324 VAL   A CG1   1 
ATOM   2552  C  CG2   . VAL   A 1  324 ? 14.131  101.344 82.292  1.00 36.68  ? 324 VAL   A CG2   1 
ATOM   2553  N  N     . PRO   A 1  325 ? 17.700  99.158  82.969  1.00 40.66  ? 325 PRO   A N     1 
ATOM   2554  C  CA    . PRO   A 1  325 ? 18.089  97.977  83.759  1.00 33.87  ? 325 PRO   A CA    1 
ATOM   2555  C  C     . PRO   A 1  325 ? 17.058  97.535  84.783  1.00 38.30  ? 325 PRO   A C     1 
ATOM   2556  O  O     . PRO   A 1  325 ? 16.812  96.328  84.898  1.00 41.55  ? 325 PRO   A O     1 
ATOM   2557  C  CB    . PRO   A 1  325 ? 19.405  98.425  84.402  1.00 34.04  ? 325 PRO   A CB    1 
ATOM   2558  C  CG    . PRO   A 1  325 ? 20.001  99.354  83.369  1.00 33.55  ? 325 PRO   A CG    1 
ATOM   2559  C  CD    . PRO   A 1  325 ? 18.826  100.093 82.782  1.00 37.47  ? 325 PRO   A CD    1 
ATOM   2560  N  N     . LYS   A 1  326 ? 16.444  98.467  85.520  1.00 44.11  ? 326 LYS   A N     1 
ATOM   2561  C  CA    . LYS   A 1  326 ? 15.415  98.108  86.499  1.00 44.94  ? 326 LYS   A CA    1 
ATOM   2562  C  C     . LYS   A 1  326 ? 14.413  97.099  85.930  1.00 46.81  ? 326 LYS   A C     1 
ATOM   2563  O  O     . LYS   A 1  326 ? 14.114  96.071  86.557  1.00 38.90  ? 326 LYS   A O     1 
ATOM   2564  C  CB    . LYS   A 1  326 ? 14.697  99.373  86.972  1.00 41.28  ? 326 LYS   A CB    1 
ATOM   2565  C  CG    . LYS   A 1  326 ? 15.242  100.642 86.328  1.00 55.11  ? 326 LYS   A CG    1 
ATOM   2566  C  CD    . LYS   A 1  326 ? 14.235  101.795 86.378  1.00 63.07  ? 326 LYS   A CD    1 
ATOM   2567  C  CE    . LYS   A 1  326 ? 14.731  102.986 85.556  1.00 65.38  ? 326 LYS   A CE    1 
ATOM   2568  N  NZ    . LYS   A 1  326 ? 13.627  103.868 85.079  1.00 67.62  ? 326 LYS   A NZ    1 
ATOM   2569  N  N     . ASP   A 1  327 ? 13.879  97.383  84.740  1.00 39.66  ? 327 ASP   A N     1 
ATOM   2570  C  CA    . ASP   A 1  327 ? 12.971  96.446  84.090  1.00 36.57  ? 327 ASP   A CA    1 
ATOM   2571  C  C     . ASP   A 1  327 ? 13.631  95.091  83.878  1.00 42.89  ? 327 ASP   A C     1 
ATOM   2572  O  O     . ASP   A 1  327 ? 13.048  94.048  84.202  1.00 39.72  ? 327 ASP   A O     1 
ATOM   2573  C  CB    . ASP   A 1  327 ? 12.506  97.017  82.757  1.00 47.82  ? 327 ASP   A CB    1 
ATOM   2574  C  CG    . ASP   A 1  327 ? 11.779  98.336  82.910  1.00 47.58  ? 327 ASP   A CG    1 
ATOM   2575  O  OD1   . ASP   A 1  327 ? 11.040  98.477  83.905  1.00 48.06  ? 327 ASP   A OD1   1 
ATOM   2576  O  OD2   . ASP   A 1  327 ? 11.959  99.225  82.042  1.00 48.90  ? 327 ASP   A OD2   1 
ATOM   2577  N  N     . VAL   A 1  328 ? 14.858  95.083  83.340  1.00 39.43  ? 328 VAL   A N     1 
ATOM   2578  C  CA    . VAL   A 1  328 ? 15.524  93.815  83.024  1.00 42.16  ? 328 VAL   A CA    1 
ATOM   2579  C  C     . VAL   A 1  328 ? 15.626  92.933  84.266  1.00 43.83  ? 328 VAL   A C     1 
ATOM   2580  O  O     . VAL   A 1  328 ? 15.332  91.733  84.218  1.00 46.11  ? 328 VAL   A O     1 
ATOM   2581  C  CB    . VAL   A 1  328 ? 16.912  94.054  82.396  1.00 34.45  ? 328 VAL   A CB    1 
ATOM   2582  C  CG1   . VAL   A 1  328 ? 17.570  92.721  82.094  1.00 24.58  ? 328 VAL   A CG1   1 
ATOM   2583  C  CG2   . VAL   A 1  328 ? 16.811  94.911  81.121  1.00 29.23  ? 328 VAL   A CG2   1 
ATOM   2584  N  N     . ASN   A 1  329 ? 16.063  93.507  85.392  1.00 40.23  ? 329 ASN   A N     1 
ATOM   2585  C  CA    . ASN   A 1  329 ? 16.227  92.712  86.605  1.00 36.29  ? 329 ASN   A CA    1 
ATOM   2586  C  C     . ASN   A 1  329 ? 14.877  92.348  87.217  1.00 43.60  ? 329 ASN   A C     1 
ATOM   2587  O  O     . ASN   A 1  329 ? 14.669  91.211  87.660  1.00 32.78  ? 329 ASN   A O     1 
ATOM   2588  C  CB    . ASN   A 1  329 ? 17.089  93.474  87.600  1.00 37.18  ? 329 ASN   A CB    1 
ATOM   2589  C  CG    . ASN   A 1  329 ? 18.358  93.995  86.969  1.00 53.44  ? 329 ASN   A CG    1 
ATOM   2590  O  OD1   . ASN   A 1  329 ? 18.418  94.187  85.755  1.00 54.18  ? 329 ASN   A OD1   1 
ATOM   2591  N  ND2   . ASN   A 1  329 ? 19.383  94.231  87.784  1.00 51.87  ? 329 ASN   A ND2   1 
ATOM   2592  N  N     . ALA   A 1  330 ? 13.945  93.297  87.254  1.00 38.92  ? 330 ALA   A N     1 
ATOM   2593  C  CA    . ALA   A 1  330 ? 12.572  92.936  87.562  1.00 41.75  ? 330 ALA   A CA    1 
ATOM   2594  C  C     . ALA   A 1  330 ? 12.154  91.691  86.775  1.00 48.30  ? 330 ALA   A C     1 
ATOM   2595  O  O     . ALA   A 1  330 ? 11.682  90.698  87.349  1.00 39.06  ? 330 ALA   A O     1 
ATOM   2596  C  CB    . ALA   A 1  330 ? 11.663  94.122  87.255  1.00 36.79  ? 330 ALA   A CB    1 
ATOM   2597  N  N     . ALA   A 1  331 ? 12.364  91.722  85.451  1.00 45.46  ? 331 ALA   A N     1 
ATOM   2598  C  CA    . ALA   A 1  331 ? 12.027  90.590  84.586  1.00 41.18  ? 331 ALA   A CA    1 
ATOM   2599  C  C     . ALA   A 1  331 ? 12.796  89.338  84.980  1.00 39.99  ? 331 ALA   A C     1 
ATOM   2600  O  O     . ALA   A 1  331 ? 12.204  88.280  85.218  1.00 42.03  ? 331 ALA   A O     1 
ATOM   2601  C  CB    . ALA   A 1  331 ? 12.307  90.949  83.129  1.00 35.28  ? 331 ALA   A CB    1 
ATOM   2602  N  N     . ILE   A 1  332 ? 14.123  89.437  85.050  1.00 39.02  ? 332 ILE   A N     1 
ATOM   2603  C  CA    . ILE   A 1  332 ? 14.936  88.286  85.428  1.00 40.92  ? 332 ILE   A CA    1 
ATOM   2604  C  C     . ILE   A 1  332 ? 14.487  87.726  86.766  1.00 43.05  ? 332 ILE   A C     1 
ATOM   2605  O  O     . ILE   A 1  332 ? 14.525  86.511  86.980  1.00 51.62  ? 332 ILE   A O     1 
ATOM   2606  C  CB    . ILE   A 1  332 ? 16.426  88.673  85.439  1.00 46.78  ? 332 ILE   A CB    1 
ATOM   2607  C  CG1   . ILE   A 1  332 ? 16.857  89.114  84.034  1.00 30.82  ? 332 ILE   A CG1   1 
ATOM   2608  C  CG2   . ILE   A 1  332 ? 17.289  87.529  86.013  1.00 35.81  ? 332 ILE   A CG2   1 
ATOM   2609  C  CD1   . ILE   A 1  332 ? 18.182  89.843  84.002  1.00 39.68  ? 332 ILE   A CD1   1 
ATOM   2610  N  N     . ALA   A 1  333 ? 14.032  88.589  87.677  1.00 45.54  ? 333 ALA   A N     1 
ATOM   2611  C  CA    . ALA   A 1  333 ? 13.517  88.129  88.964  1.00 45.59  ? 333 ALA   A CA    1 
ATOM   2612  C  C     . ALA   A 1  333 ? 12.356  87.155  88.780  1.00 49.61  ? 333 ALA   A C     1 
ATOM   2613  O  O     . ALA   A 1  333 ? 12.396  86.017  89.258  1.00 56.02  ? 333 ALA   A O     1 
ATOM   2614  C  CB    . ALA   A 1  333 ? 13.084  89.330  89.814  1.00 55.68  ? 333 ALA   A CB    1 
ATOM   2615  N  N     . THR   A 1  334 ? 11.306  87.591  88.088  1.00 52.89  ? 334 THR   A N     1 
ATOM   2616  C  CA    . THR   A 1  334 ? 10.128  86.750  87.914  1.00 54.41  ? 334 THR   A CA    1 
ATOM   2617  C  C     . THR   A 1  334 ? 10.487  85.415  87.276  1.00 63.14  ? 334 THR   A C     1 
ATOM   2618  O  O     . THR   A 1  334 ? 10.202  84.351  87.838  1.00 64.71  ? 334 THR   A O     1 
ATOM   2619  C  CB    . THR   A 1  334 ? 9.082   87.466  87.058  1.00 63.76  ? 334 THR   A CB    1 
ATOM   2620  O  OG1   . THR   A 1  334 ? 9.182   88.885  87.245  1.00 60.17  ? 334 THR   A OG1   1 
ATOM   2621  C  CG2   . THR   A 1  334 ? 7.676   86.984  87.434  1.00 61.59  ? 334 THR   A CG2   1 
ATOM   2622  N  N     . ILE   A 1  335 ? 11.088  85.449  86.077  1.00 60.86  ? 335 ILE   A N     1 
ATOM   2623  C  CA    . ILE   A 1  335 ? 11.337  84.198  85.359  1.00 60.12  ? 335 ILE   A CA    1 
ATOM   2624  C  C     . ILE   A 1  335 ? 12.228  83.285  86.184  1.00 58.00  ? 335 ILE   A C     1 
ATOM   2625  O  O     . ILE   A 1  335 ? 12.089  82.059  86.125  1.00 61.69  ? 335 ILE   A O     1 
ATOM   2626  C  CB    . ILE   A 1  335 ? 11.940  84.434  83.951  1.00 46.12  ? 335 ILE   A CB    1 
ATOM   2627  C  CG1   . ILE   A 1  335 ? 13.414  84.819  84.039  1.00 50.58  ? 335 ILE   A CG1   1 
ATOM   2628  C  CG2   . ILE   A 1  335 ? 11.158  85.476  83.153  1.00 48.69  ? 335 ILE   A CG2   1 
ATOM   2629  C  CD1   . ILE   A 1  335 ? 14.344  83.647  84.183  1.00 55.98  ? 335 ILE   A CD1   1 
ATOM   2630  N  N     . LYS   A 1  336 ? 13.154  83.855  86.965  1.00 51.97  ? 336 LYS   A N     1 
ATOM   2631  C  CA    . LYS   A 1  336 ? 14.051  83.015  87.752  1.00 60.17  ? 336 LYS   A CA    1 
ATOM   2632  C  C     . LYS   A 1  336 ? 13.278  82.043  88.644  1.00 72.10  ? 336 LYS   A C     1 
ATOM   2633  O  O     . LYS   A 1  336 ? 13.778  80.952  88.954  1.00 65.37  ? 336 LYS   A O     1 
ATOM   2634  C  CB    . LYS   A 1  336 ? 14.993  83.885  88.583  1.00 57.12  ? 336 LYS   A CB    1 
ATOM   2635  C  CG    . LYS   A 1  336 ? 15.888  83.093  89.538  1.00 71.69  ? 336 LYS   A CG    1 
ATOM   2636  C  CD    . LYS   A 1  336 ? 16.562  81.910  88.853  1.00 67.35  ? 336 LYS   A CD    1 
ATOM   2637  C  CE    . LYS   A 1  336 ? 17.408  81.108  89.835  1.00 67.05  ? 336 LYS   A CE    1 
ATOM   2638  N  NZ    . LYS   A 1  336 ? 17.951  79.862  89.228  1.00 58.51  ? 336 LYS   A NZ    1 
ATOM   2639  N  N     . THR   A 1  337 ? 12.051  82.406  89.044  1.00 66.19  ? 337 THR   A N     1 
ATOM   2640  C  CA    . THR   A 1  337 ? 11.193  81.518  89.820  1.00 64.04  ? 337 THR   A CA    1 
ATOM   2641  C  C     . THR   A 1  337 ? 10.239  80.684  88.969  1.00 62.83  ? 337 THR   A C     1 
ATOM   2642  O  O     . THR   A 1  337 ? 9.767   79.647  89.444  1.00 67.56  ? 337 THR   A O     1 
ATOM   2643  C  CB    . THR   A 1  337 ? 10.365  82.318  90.835  1.00 61.94  ? 337 THR   A CB    1 
ATOM   2644  O  OG1   . THR   A 1  337 ? 9.329   83.034  90.149  1.00 67.70  ? 337 THR   A OG1   1 
ATOM   2645  C  CG2   . THR   A 1  337 ? 11.250  83.296  91.603  1.00 56.94  ? 337 THR   A CG2   1 
ATOM   2646  N  N     . LYS   A 1  338 ? 9.939   81.100  87.735  1.00 63.01  ? 338 LYS   A N     1 
ATOM   2647  C  CA    . LYS   A 1  338 ? 9.004   80.379  86.875  1.00 50.90  ? 338 LYS   A CA    1 
ATOM   2648  C  C     . LYS   A 1  338 ? 9.667   79.289  86.043  1.00 65.98  ? 338 LYS   A C     1 
ATOM   2649  O  O     . LYS   A 1  338 ? 9.002   78.321  85.664  1.00 68.22  ? 338 LYS   A O     1 
ATOM   2650  C  CB    . LYS   A 1  338 ? 8.299   81.352  85.925  1.00 55.22  ? 338 LYS   A CB    1 
ATOM   2651  C  CG    . LYS   A 1  338 ? 7.138   82.102  86.548  1.00 82.02  ? 338 LYS   A CG    1 
ATOM   2652  C  CD    . LYS   A 1  338 ? 7.556   82.858  87.819  1.00 76.81  ? 338 LYS   A CD    1 
ATOM   2653  C  CE    . LYS   A 1  338 ? 6.375   82.988  88.765  1.00 72.95  ? 338 LYS   A CE    1 
ATOM   2654  N  NZ    . LYS   A 1  338 ? 5.578   81.718  88.792  1.00 60.75  ? 338 LYS   A NZ    1 
ATOM   2655  N  N     . ARG   A 1  339 ? 10.953  79.425  85.748  1.00 58.21  ? 339 ARG   A N     1 
ATOM   2656  C  CA    . ARG   A 1  339 ? 11.638  78.592  84.777  1.00 51.03  ? 339 ARG   A CA    1 
ATOM   2657  C  C     . ARG   A 1  339 ? 12.742  77.784  85.441  1.00 62.12  ? 339 ARG   A C     1 
ATOM   2658  O  O     . ARG   A 1  339 ? 13.168  78.060  86.570  1.00 68.12  ? 339 ARG   A O     1 
ATOM   2659  C  CB    . ARG   A 1  339 ? 12.245  79.446  83.658  1.00 56.61  ? 339 ARG   A CB    1 
ATOM   2660  C  CG    . ARG   A 1  339 ? 11.261  80.305  82.928  1.00 47.13  ? 339 ARG   A CG    1 
ATOM   2661  C  CD    . ARG   A 1  339 ? 10.631  79.525  81.809  1.00 52.35  ? 339 ARG   A CD    1 
ATOM   2662  N  NE    . ARG   A 1  339 ? 9.971   80.420  80.870  1.00 49.89  ? 339 ARG   A NE    1 
ATOM   2663  C  CZ    . ARG   A 1  339 ? 9.152   80.023  79.907  1.00 51.52  ? 339 ARG   A CZ    1 
ATOM   2664  N  NH1   . ARG   A 1  339 ? 8.847   78.741  79.739  1.00 52.05  ? 339 ARG   A NH1   1 
ATOM   2665  N  NH2   . ARG   A 1  339 ? 8.620   80.932  79.094  1.00 48.41  ? 339 ARG   A NH2   1 
ATOM   2666  N  N     . SER   A 1  340 ? 13.235  76.799  84.689  1.00 62.91  ? 340 SER   A N     1 
ATOM   2667  C  CA    . SER   A 1  340 ? 14.278  75.881  85.143  1.00 56.81  ? 340 SER   A CA    1 
ATOM   2668  C  C     . SER   A 1  340 ? 15.588  76.313  84.496  1.00 51.71  ? 340 SER   A C     1 
ATOM   2669  O  O     . SER   A 1  340 ? 15.906  75.923  83.373  1.00 58.15  ? 340 SER   A O     1 
ATOM   2670  C  CB    . SER   A 1  340 ? 13.906  74.447  84.791  1.00 49.28  ? 340 SER   A CB    1 
ATOM   2671  O  OG    . SER   A 1  340 ? 12.626  74.124  85.315  1.00 43.41  ? 340 SER   A OG    1 
ATOM   2672  N  N     . ILE   A 1  341 ? 16.350  77.138  85.210  1.00 52.00  ? 341 ILE   A N     1 
ATOM   2673  C  CA    . ILE   A 1  341 ? 17.543  77.759  84.642  1.00 47.80  ? 341 ILE   A CA    1 
ATOM   2674  C  C     . ILE   A 1  341 ? 18.732  77.428  85.529  1.00 54.42  ? 341 ILE   A C     1 
ATOM   2675  O  O     . ILE   A 1  341 ? 19.264  78.302  86.229  1.00 61.06  ? 341 ILE   A O     1 
ATOM   2676  C  CB    . ILE   A 1  341 ? 17.368  79.285  84.477  1.00 40.54  ? 341 ILE   A CB    1 
ATOM   2677  C  CG1   . ILE   A 1  341 ? 16.116  79.590  83.658  1.00 49.71  ? 341 ILE   A CG1   1 
ATOM   2678  C  CG2   . ILE   A 1  341 ? 18.524  79.881  83.737  1.00 35.76  ? 341 ILE   A CG2   1 
ATOM   2679  C  CD1   . ILE   A 1  341 ? 15.747  81.041  83.648  1.00 49.16  ? 341 ILE   A CD1   1 
ATOM   2680  N  N     . GLN   A 1  342 ? 19.153  76.160  85.499  1.00 48.77  ? 342 GLN   A N     1 
ATOM   2681  C  CA    . GLN   A 1  342 ? 20.265  75.678  86.304  1.00 41.72  ? 342 GLN   A CA    1 
ATOM   2682  C  C     . GLN   A 1  342 ? 21.583  75.793  85.546  1.00 43.25  ? 342 GLN   A C     1 
ATOM   2683  O  O     . GLN   A 1  342 ? 21.719  75.280  84.430  1.00 40.38  ? 342 GLN   A O     1 
ATOM   2684  C  CB    . GLN   A 1  342 ? 20.030  74.231  86.725  1.00 49.48  ? 342 GLN   A CB    1 
ATOM   2685  C  CG    . GLN   A 1  342 ? 21.165  73.660  87.553  1.00 55.02  ? 342 GLN   A CG    1 
ATOM   2686  C  CD    . GLN   A 1  342 ? 20.829  72.300  88.113  1.00 76.68  ? 342 GLN   A CD    1 
ATOM   2687  O  OE1   . GLN   A 1  342 ? 19.691  72.058  88.532  1.00 75.17  ? 342 GLN   A OE1   1 
ATOM   2688  N  NE2   . GLN   A 1  342 ? 21.813  71.393  88.117  1.00 79.48  ? 342 GLN   A NE2   1 
ATOM   2689  N  N     . PHE   A 1  343 ? 22.546  76.466  86.158  1.00 43.82  ? 343 PHE   A N     1 
ATOM   2690  C  CA    . PHE   A 1  343 ? 23.900  76.564  85.644  1.00 41.59  ? 343 PHE   A CA    1 
ATOM   2691  C  C     . PHE   A 1  343 ? 24.740  75.411  86.183  1.00 46.64  ? 343 PHE   A C     1 
ATOM   2692  O  O     . PHE   A 1  343 ? 24.323  74.663  87.069  1.00 52.19  ? 343 PHE   A O     1 
ATOM   2693  C  CB    . PHE   A 1  343 ? 24.531  77.911  86.028  1.00 46.49  ? 343 PHE   A CB    1 
ATOM   2694  C  CG    . PHE   A 1  343 ? 23.993  79.098  85.253  1.00 44.35  ? 343 PHE   A CG    1 
ATOM   2695  C  CD1   . PHE   A 1  343 ? 22.655  79.457  85.333  1.00 41.65  ? 343 PHE   A CD1   1 
ATOM   2696  C  CD2   . PHE   A 1  343 ? 24.839  79.866  84.464  1.00 39.40  ? 343 PHE   A CD2   1 
ATOM   2697  C  CE1   . PHE   A 1  343 ? 22.171  80.544  84.621  1.00 43.81  ? 343 PHE   A CE1   1 
ATOM   2698  C  CE2   . PHE   A 1  343 ? 24.361  80.951  83.761  1.00 36.42  ? 343 PHE   A CE2   1 
ATOM   2699  C  CZ    . PHE   A 1  343 ? 23.027  81.294  83.842  1.00 37.94  ? 343 PHE   A CZ    1 
ATOM   2700  N  N     . VAL   A 1  344 ? 25.939  75.271  85.633  1.00 50.81  ? 344 VAL   A N     1 
ATOM   2701  C  CA    . VAL   A 1  344 ? 26.883  74.253  86.079  1.00 46.53  ? 344 VAL   A CA    1 
ATOM   2702  C  C     . VAL   A 1  344 ? 27.616  74.762  87.307  1.00 57.43  ? 344 VAL   A C     1 
ATOM   2703  O  O     . VAL   A 1  344 ? 28.065  75.915  87.338  1.00 54.52  ? 344 VAL   A O     1 
ATOM   2704  C  CB    . VAL   A 1  344 ? 27.863  73.914  84.950  1.00 47.91  ? 344 VAL   A CB    1 
ATOM   2705  C  CG1   . VAL   A 1  344 ? 27.095  73.388  83.769  1.00 57.40  ? 344 VAL   A CG1   1 
ATOM   2706  C  CG2   . VAL   A 1  344 ? 28.661  75.157  84.555  1.00 47.64  ? 344 VAL   A CG2   1 
ATOM   2707  N  N     . ASP   A 1  345 ? 27.753  73.892  88.318  1.00 62.14  ? 345 ASP   A N     1 
ATOM   2708  C  CA    . ASP   A 1  345 ? 28.307  74.282  89.614  1.00 55.83  ? 345 ASP   A CA    1 
ATOM   2709  C  C     . ASP   A 1  345 ? 29.446  75.285  89.478  1.00 60.33  ? 345 ASP   A C     1 
ATOM   2710  O  O     . ASP   A 1  345 ? 29.432  76.348  90.107  1.00 64.02  ? 345 ASP   A O     1 
ATOM   2711  C  CB    . ASP   A 1  345 ? 28.792  73.044  90.373  1.00 58.92  ? 345 ASP   A CB    1 
ATOM   2712  C  CG    . ASP   A 1  345 ? 27.686  72.040  90.631  1.00 65.27  ? 345 ASP   A CG    1 
ATOM   2713  O  OD1   . ASP   A 1  345 ? 26.508  72.444  90.621  1.00 54.99  ? 345 ASP   A OD1   1 
ATOM   2714  O  OD2   . ASP   A 1  345 ? 27.999  70.847  90.855  1.00 78.37  ? 345 ASP   A OD2   1 
ATOM   2715  N  N     . TRP   A 1  346 ? 30.434  74.969  88.643  1.00 52.40  ? 346 TRP   A N     1 
ATOM   2716  C  CA    . TRP   A 1  346 ? 31.619  75.805  88.495  1.00 56.25  ? 346 TRP   A CA    1 
ATOM   2717  C  C     . TRP   A 1  346 ? 31.347  77.114  87.764  1.00 63.32  ? 346 TRP   A C     1 
ATOM   2718  O  O     . TRP   A 1  346 ? 32.252  77.644  87.107  1.00 58.66  ? 346 TRP   A O     1 
ATOM   2719  C  CB    . TRP   A 1  346 ? 32.717  75.046  87.746  1.00 63.94  ? 346 TRP   A CB    1 
ATOM   2720  C  CG    . TRP   A 1  346 ? 32.284  74.462  86.403  1.00 67.89  ? 346 TRP   A CG    1 
ATOM   2721  C  CD1   . TRP   A 1  346 ? 31.659  73.266  86.197  1.00 74.65  ? 346 TRP   A CD1   1 
ATOM   2722  C  CD2   . TRP   A 1  346 ? 32.465  75.043  85.102  1.00 62.20  ? 346 TRP   A CD2   1 
ATOM   2723  N  NE1   . TRP   A 1  346 ? 31.435  73.068  84.857  1.00 65.09  ? 346 TRP   A NE1   1 
ATOM   2724  C  CE2   . TRP   A 1  346 ? 31.920  74.143  84.163  1.00 69.55  ? 346 TRP   A CE2   1 
ATOM   2725  C  CE3   . TRP   A 1  346 ? 33.034  76.235  84.642  1.00 66.02  ? 346 TRP   A CE3   1 
ATOM   2726  C  CZ2   . TRP   A 1  346 ? 31.925  74.398  82.790  1.00 74.70  ? 346 TRP   A CZ2   1 
ATOM   2727  C  CZ3   . TRP   A 1  346 ? 33.040  76.489  83.280  1.00 72.67  ? 346 TRP   A CZ3   1 
ATOM   2728  C  CH2   . TRP   A 1  346 ? 32.487  75.576  82.369  1.00 78.84  ? 346 TRP   A CH2   1 
ATOM   2729  N  N     . CYS   A 1  347 ? 30.125  77.641  87.863  1.00 59.03  ? 347 CYS   A N     1 
ATOM   2730  C  CA    . CYS   A 1  347 ? 29.750  78.887  87.201  1.00 61.91  ? 347 CYS   A CA    1 
ATOM   2731  C  C     . CYS   A 1  347 ? 28.710  79.596  88.043  1.00 62.40  ? 347 CYS   A C     1 
ATOM   2732  O  O     . CYS   A 1  347 ? 27.927  78.946  88.748  1.00 61.00  ? 347 CYS   A O     1 
ATOM   2733  C  CB    . CYS   A 1  347 ? 29.182  78.678  85.785  1.00 52.74  ? 347 CYS   A CB    1 
ATOM   2734  S  SG    . CYS   A 1  347 ? 30.395  78.362  84.473  1.00 62.35  ? 347 CYS   A SG    1 
ATOM   2735  N  N     . PRO   A 1  348 ? 28.670  80.920  87.991  1.00 51.97  ? 348 PRO   A N     1 
ATOM   2736  C  CA    . PRO   A 1  348 ? 27.646  81.641  88.739  1.00 46.87  ? 348 PRO   A CA    1 
ATOM   2737  C  C     . PRO   A 1  348 ? 26.393  81.791  87.901  1.00 52.78  ? 348 PRO   A C     1 
ATOM   2738  O  O     . PRO   A 1  348 ? 26.441  81.966  86.683  1.00 47.92  ? 348 PRO   A O     1 
ATOM   2739  C  CB    . PRO   A 1  348 ? 28.307  82.998  88.998  1.00 52.70  ? 348 PRO   A CB    1 
ATOM   2740  C  CG    . PRO   A 1  348 ? 29.201  83.184  87.792  1.00 56.44  ? 348 PRO   A CG    1 
ATOM   2741  C  CD    . PRO   A 1  348 ? 29.679  81.819  87.400  1.00 53.76  ? 348 PRO   A CD    1 
ATOM   2742  N  N     . THR   A 1  349 ? 25.255  81.702  88.578  1.00 50.15  ? 349 THR   A N     1 
ATOM   2743  C  CA    . THR   A 1  349 ? 23.991  82.041  87.956  1.00 43.74  ? 349 THR   A CA    1 
ATOM   2744  C  C     . THR   A 1  349 ? 23.902  83.553  87.753  1.00 51.22  ? 349 THR   A C     1 
ATOM   2745  O  O     . THR   A 1  349 ? 23.504  84.289  88.663  1.00 50.70  ? 349 THR   A O     1 
ATOM   2746  C  CB    . THR   A 1  349 ? 22.835  81.540  88.813  1.00 47.15  ? 349 THR   A CB    1 
ATOM   2747  O  OG1   . THR   A 1  349 ? 23.050  80.163  89.147  1.00 54.83  ? 349 THR   A OG1   1 
ATOM   2748  C  CG2   . THR   A 1  349 ? 21.516  81.683  88.065  1.00 48.62  ? 349 THR   A CG2   1 
ATOM   2749  N  N     . GLY   A 1  350 ? 24.273  84.028  86.564  1.00 49.02  ? 350 GLY   A N     1 
ATOM   2750  C  CA    . GLY   A 1  350 ? 24.126  85.431  86.234  1.00 53.58  ? 350 GLY   A CA    1 
ATOM   2751  C  C     . GLY   A 1  350 ? 23.958  85.652  84.745  1.00 46.60  ? 350 GLY   A C     1 
ATOM   2752  O  O     . GLY   A 1  350 ? 24.234  84.772  83.927  1.00 46.85  ? 350 GLY   A O     1 
ATOM   2753  N  N     . PHE   A 1  351 ? 23.514  86.861  84.407  1.00 42.20  ? 351 PHE   A N     1 
ATOM   2754  C  CA    . PHE   A 1  351 ? 23.299  87.290  83.031  1.00 37.03  ? 351 PHE   A CA    1 
ATOM   2755  C  C     . PHE   A 1  351 ? 24.124  88.533  82.744  1.00 35.58  ? 351 PHE   A C     1 
ATOM   2756  O  O     . PHE   A 1  351 ? 24.025  89.523  83.472  1.00 44.63  ? 351 PHE   A O     1 
ATOM   2757  C  CB    . PHE   A 1  351 ? 21.823  87.614  82.786  1.00 42.89  ? 351 PHE   A CB    1 
ATOM   2758  C  CG    . PHE   A 1  351 ? 20.891  86.468  83.035  1.00 49.05  ? 351 PHE   A CG    1 
ATOM   2759  C  CD1   . PHE   A 1  351 ? 20.589  86.068  84.326  1.00 46.24  ? 351 PHE   A CD1   1 
ATOM   2760  C  CD2   . PHE   A 1  351 ? 20.304  85.793  81.976  1.00 45.32  ? 351 PHE   A CD2   1 
ATOM   2761  C  CE1   . PHE   A 1  351 ? 19.733  85.017  84.543  1.00 38.62  ? 351 PHE   A CE1   1 
ATOM   2762  C  CE2   . PHE   A 1  351 ? 19.443  84.729  82.199  1.00 37.58  ? 351 PHE   A CE2   1 
ATOM   2763  C  CZ    . PHE   A 1  351 ? 19.155  84.350  83.473  1.00 32.62  ? 351 PHE   A CZ    1 
ATOM   2764  N  N     . LYS   A 1  352 ? 24.910  88.511  81.675  1.00 32.95  ? 352 LYS   A N     1 
ATOM   2765  C  CA    . LYS   A 1  352 ? 25.429  89.765  81.146  1.00 32.15  ? 352 LYS   A CA    1 
ATOM   2766  C  C     . LYS   A 1  352 ? 24.358  90.424  80.299  1.00 39.37  ? 352 LYS   A C     1 
ATOM   2767  O  O     . LYS   A 1  352 ? 23.615  89.748  79.586  1.00 42.32  ? 352 LYS   A O     1 
ATOM   2768  C  CB    . LYS   A 1  352 ? 26.682  89.541  80.318  1.00 33.15  ? 352 LYS   A CB    1 
ATOM   2769  C  CG    . LYS   A 1  352 ? 27.896  89.373  81.169  1.00 43.09  ? 352 LYS   A CG    1 
ATOM   2770  C  CD    . LYS   A 1  352 ? 29.129  89.070  80.359  1.00 48.35  ? 352 LYS   A CD    1 
ATOM   2771  C  CE    . LYS   A 1  352 ? 30.212  88.788  81.340  1.00 39.69  ? 352 LYS   A CE    1 
ATOM   2772  N  NZ    . LYS   A 1  352 ? 29.489  88.274  82.516  1.00 37.06  ? 352 LYS   A NZ    1 
ATOM   2773  N  N     . VAL   A 1  353 ? 24.264  91.744  80.378  1.00 37.16  ? 353 VAL   A N     1 
ATOM   2774  C  CA    . VAL   A 1  353 ? 23.177  92.450  79.716  1.00 36.79  ? 353 VAL   A CA    1 
ATOM   2775  C  C     . VAL   A 1  353 ? 23.728  93.617  78.914  1.00 37.22  ? 353 VAL   A C     1 
ATOM   2776  O  O     . VAL   A 1  353 ? 24.613  94.347  79.374  1.00 31.43  ? 353 VAL   A O     1 
ATOM   2777  C  CB    . VAL   A 1  353 ? 22.105  92.917  80.722  1.00 36.31  ? 353 VAL   A CB    1 
ATOM   2778  C  CG1   . VAL   A 1  353 ? 21.014  93.723  80.006  1.00 32.55  ? 353 VAL   A CG1   1 
ATOM   2779  C  CG2   . VAL   A 1  353 ? 21.498  91.702  81.398  1.00 36.77  ? 353 VAL   A CG2   1 
ATOM   2780  N  N     . GLY   A 1  354 ? 23.210  93.767  77.693  1.00 36.99  ? 354 GLY   A N     1 
ATOM   2781  C  CA    . GLY   A 1  354 ? 23.561  94.861  76.820  1.00 23.23  ? 354 GLY   A CA    1 
ATOM   2782  C  C     . GLY   A 1  354 ? 22.298  95.510  76.315  1.00 33.33  ? 354 GLY   A C     1 
ATOM   2783  O  O     . GLY   A 1  354 ? 21.377  94.816  75.872  1.00 38.64  ? 354 GLY   A O     1 
ATOM   2784  N  N     . ILE   A 1  355 ? 22.219  96.834  76.402  1.00 34.32  ? 355 ILE   A N     1 
ATOM   2785  C  CA    . ILE   A 1  355 ? 21.081  97.585  75.892  1.00 35.90  ? 355 ILE   A CA    1 
ATOM   2786  C  C     . ILE   A 1  355 ? 21.571  98.612  74.878  1.00 41.79  ? 355 ILE   A C     1 
ATOM   2787  O  O     . ILE   A 1  355 ? 22.520  99.357  75.145  1.00 39.91  ? 355 ILE   A O     1 
ATOM   2788  C  CB    . ILE   A 1  355 ? 20.315  98.287  77.017  1.00 31.14  ? 355 ILE   A CB    1 
ATOM   2789  C  CG1   . ILE   A 1  355 ? 20.044  97.306  78.153  1.00 30.51  ? 355 ILE   A CG1   1 
ATOM   2790  C  CG2   . ILE   A 1  355 ? 19.047  98.922  76.437  1.00 29.57  ? 355 ILE   A CG2   1 
ATOM   2791  C  CD1   . ILE   A 1  355 ? 19.361  97.966  79.369  1.00 34.70  ? 355 ILE   A CD1   1 
ATOM   2792  N  N     . ASN   A 1  356 ? 20.914  98.660  73.724  1.00 38.93  ? 356 ASN   A N     1 
ATOM   2793  C  CA    . ASN   A 1  356 ? 21.157  99.690  72.726  1.00 42.18  ? 356 ASN   A CA    1 
ATOM   2794  C  C     . ASN   A 1  356 ? 19.834  100.389 72.492  1.00 41.08  ? 356 ASN   A C     1 
ATOM   2795  O  O     . ASN   A 1  356 ? 18.873  99.763  72.035  1.00 37.60  ? 356 ASN   A O     1 
ATOM   2796  C  CB    . ASN   A 1  356 ? 21.719  99.110  71.424  1.00 35.57  ? 356 ASN   A CB    1 
ATOM   2797  C  CG    . ASN   A 1  356 ? 22.106  100.190 70.426  1.00 49.28  ? 356 ASN   A CG    1 
ATOM   2798  O  OD1   . ASN   A 1  356 ? 21.313  101.089 70.118  1.00 56.38  ? 356 ASN   A OD1   1 
ATOM   2799  N  ND2   . ASN   A 1  356 ? 23.335  100.116 69.924  1.00 45.37  ? 356 ASN   A ND2   1 
ATOM   2800  N  N     . TYR   A 1  357 ? 19.786  101.679 72.823  1.00 46.40  ? 357 TYR   A N     1 
ATOM   2801  C  CA    . TYR   A 1  357 ? 18.519  102.394 72.856  1.00 50.96  ? 357 TYR   A CA    1 
ATOM   2802  C  C     . TYR   A 1  357 ? 17.827  102.421 71.504  1.00 45.52  ? 357 TYR   A C     1 
ATOM   2803  O  O     . TYR   A 1  357 ? 16.605  102.597 71.458  1.00 51.85  ? 357 TYR   A O     1 
ATOM   2804  C  CB    . TYR   A 1  357 ? 18.742  103.817 73.358  1.00 52.63  ? 357 TYR   A CB    1 
ATOM   2805  C  CG    . TYR   A 1  357 ? 19.185  103.883 74.795  1.00 52.27  ? 357 TYR   A CG    1 
ATOM   2806  C  CD1   . TYR   A 1  357 ? 18.548  103.127 75.769  1.00 50.13  ? 357 TYR   A CD1   1 
ATOM   2807  C  CD2   . TYR   A 1  357 ? 20.234  104.699 75.180  1.00 50.96  ? 357 TYR   A CD2   1 
ATOM   2808  C  CE1   . TYR   A 1  357 ? 18.942  103.178 77.086  1.00 44.07  ? 357 TYR   A CE1   1 
ATOM   2809  C  CE2   . TYR   A 1  357 ? 20.638  104.756 76.498  1.00 59.34  ? 357 TYR   A CE2   1 
ATOM   2810  C  CZ    . TYR   A 1  357 ? 19.989  103.993 77.449  1.00 52.03  ? 357 TYR   A CZ    1 
ATOM   2811  O  OH    . TYR   A 1  357 ? 20.387  104.051 78.766  1.00 48.15  ? 357 TYR   A OH    1 
ATOM   2812  N  N     . GLN   A 1  358 ? 18.566  102.247 70.413  1.00 44.24  ? 358 GLN   A N     1 
ATOM   2813  C  CA    . GLN   A 1  358 ? 17.969  102.344 69.080  1.00 59.17  ? 358 GLN   A CA    1 
ATOM   2814  C  C     . GLN   A 1  358 ? 17.199  101.065 68.765  1.00 51.37  ? 358 GLN   A C     1 
ATOM   2815  O  O     . GLN   A 1  358 ? 17.807  99.989  68.699  1.00 50.04  ? 358 GLN   A O     1 
ATOM   2816  C  CB    . GLN   A 1  358 ? 19.045  102.597 68.033  1.00 54.77  ? 358 GLN   A CB    1 
ATOM   2817  C  CG    . GLN   A 1  358 ? 18.539  103.224 66.749  1.00 63.55  ? 358 GLN   A CG    1 
ATOM   2818  C  CD    . GLN   A 1  358 ? 19.677  103.812 65.899  1.00 93.77  ? 358 GLN   A CD    1 
ATOM   2819  O  OE1   . GLN   A 1  358 ? 20.155  103.192 64.934  1.00 76.94  ? 358 GLN   A OE1   1 
ATOM   2820  N  NE2   . GLN   A 1  358 ? 20.114  105.019 66.262  1.00 101.07 ? 358 GLN   A NE2   1 
ATOM   2821  N  N     . PRO   A 1  359 ? 15.882  101.129 68.590  1.00 47.60  ? 359 PRO   A N     1 
ATOM   2822  C  CA    . PRO   A 1  359 ? 15.081  99.896  68.389  1.00 42.57  ? 359 PRO   A CA    1 
ATOM   2823  C  C     . PRO   A 1  359 ? 15.522  99.132  67.156  1.00 42.74  ? 359 PRO   A C     1 
ATOM   2824  O  O     . PRO   A 1  359 ? 16.311  99.637  66.339  1.00 44.37  ? 359 PRO   A O     1 
ATOM   2825  C  CB    . PRO   A 1  359 ? 13.641  100.418 68.230  1.00 41.32  ? 359 PRO   A CB    1 
ATOM   2826  C  CG    . PRO   A 1  359 ? 13.765  101.920 68.031  1.00 36.58  ? 359 PRO   A CG    1 
ATOM   2827  C  CD    . PRO   A 1  359 ? 15.044  102.335 68.707  1.00 46.46  ? 359 PRO   A CD    1 
ATOM   2828  N  N     . PRO   A 1  360 ? 15.019  97.912  66.979  1.00 48.07  ? 360 PRO   A N     1 
ATOM   2829  C  CA    . PRO   A 1  360 ? 15.416  97.115  65.812  1.00 46.45  ? 360 PRO   A CA    1 
ATOM   2830  C  C     . PRO   A 1  360 ? 15.031  97.810  64.514  1.00 47.19  ? 360 PRO   A C     1 
ATOM   2831  O  O     . PRO   A 1  360 ? 13.917  98.322  64.367  1.00 45.59  ? 360 PRO   A O     1 
ATOM   2832  C  CB    . PRO   A 1  360 ? 14.654  95.797  66.001  1.00 37.60  ? 360 PRO   A CB    1 
ATOM   2833  C  CG    . PRO   A 1  360 ? 14.256  95.768  67.444  1.00 46.79  ? 360 PRO   A CG    1 
ATOM   2834  C  CD    . PRO   A 1  360 ? 14.046  97.203  67.828  1.00 50.86  ? 360 PRO   A CD    1 
ATOM   2835  N  N     . THR   A 1  361 ? 15.978  97.831  63.576  1.00 43.66  ? 361 THR   A N     1 
ATOM   2836  C  CA    . THR   A 1  361 ? 15.746  98.401  62.261  1.00 38.74  ? 361 THR   A CA    1 
ATOM   2837  C  C     . THR   A 1  361 ? 15.046  97.389  61.378  1.00 49.67  ? 361 THR   A C     1 
ATOM   2838  O  O     . THR   A 1  361 ? 15.493  96.246  61.261  1.00 63.67  ? 361 THR   A O     1 
ATOM   2839  C  CB    . THR   A 1  361 ? 17.056  98.806  61.607  1.00 44.24  ? 361 THR   A CB    1 
ATOM   2840  O  OG1   . THR   A 1  361 ? 17.565  99.989  62.236  1.00 45.91  ? 361 THR   A OG1   1 
ATOM   2841  C  CG2   . THR   A 1  361 ? 16.818  99.052  60.134  1.00 45.70  ? 361 THR   A CG2   1 
ATOM   2842  N  N     . VAL   A 1  362 ? 13.968  97.814  60.740  1.00 54.89  ? 362 VAL   A N     1 
ATOM   2843  C  CA    . VAL   A 1  362 ? 13.156  96.940  59.902  1.00 53.91  ? 362 VAL   A CA    1 
ATOM   2844  C  C     . VAL   A 1  362 ? 13.472  97.227  58.439  1.00 60.47  ? 362 VAL   A C     1 
ATOM   2845  O  O     . VAL   A 1  362 ? 13.597  98.393  58.024  1.00 52.43  ? 362 VAL   A O     1 
ATOM   2846  C  CB    . VAL   A 1  362 ? 11.652  97.123  60.210  1.00 57.58  ? 362 VAL   A CB    1 
ATOM   2847  C  CG1   . VAL   A 1  362 ? 10.890  97.701  59.008  1.00 45.67  ? 362 VAL   A CG1   1 
ATOM   2848  C  CG2   . VAL   A 1  362 ? 11.030  95.805  60.689  1.00 55.96  ? 362 VAL   A CG2   1 
ATOM   2849  N  N     . VAL   A 1  363 ? 13.631  96.161  57.661  1.00 56.39  ? 363 VAL   A N     1 
ATOM   2850  C  CA    . VAL   A 1  363 ? 13.827  96.279  56.221  1.00 49.85  ? 363 VAL   A CA    1 
ATOM   2851  C  C     . VAL   A 1  363 ? 12.504  96.713  55.603  1.00 51.98  ? 363 VAL   A C     1 
ATOM   2852  O  O     . VAL   A 1  363 ? 11.498  95.997  55.726  1.00 41.14  ? 363 VAL   A O     1 
ATOM   2853  C  CB    . VAL   A 1  363 ? 14.340  94.963  55.619  1.00 46.82  ? 363 VAL   A CB    1 
ATOM   2854  C  CG1   . VAL   A 1  363 ? 13.510  94.561  54.410  1.00 53.17  ? 363 VAL   A CG1   1 
ATOM   2855  C  CG2   . VAL   A 1  363 ? 15.783  95.121  55.228  1.00 49.69  ? 363 VAL   A CG2   1 
ATOM   2856  N  N     . PRO   A 1  364 ? 12.457  97.873  54.942  1.00 61.27  ? 364 PRO   A N     1 
ATOM   2857  C  CA    . PRO   A 1  364 ? 11.183  98.369  54.400  1.00 56.07  ? 364 PRO   A CA    1 
ATOM   2858  C  C     . PRO   A 1  364 ? 10.569  97.364  53.436  1.00 62.08  ? 364 PRO   A C     1 
ATOM   2859  O  O     . PRO   A 1  364 ? 11.219  96.893  52.496  1.00 47.49  ? 364 PRO   A O     1 
ATOM   2860  C  CB    . PRO   A 1  364 ? 11.578  99.669  53.689  1.00 54.17  ? 364 PRO   A CB    1 
ATOM   2861  C  CG    . PRO   A 1  364 ? 12.874  100.075 54.313  1.00 57.50  ? 364 PRO   A CG    1 
ATOM   2862  C  CD    . PRO   A 1  364 ? 13.577  98.787  54.653  1.00 57.17  ? 364 PRO   A CD    1 
ATOM   2863  N  N     . GLY   A 1  365 ? 9.302   97.034  53.684  1.00 66.38  ? 365 GLY   A N     1 
ATOM   2864  C  CA    . GLY   A 1  365 ? 8.582   96.056  52.906  1.00 53.25  ? 365 GLY   A CA    1 
ATOM   2865  C  C     . GLY   A 1  365 ? 8.667   94.638  53.439  1.00 66.33  ? 365 GLY   A C     1 
ATOM   2866  O  O     . GLY   A 1  365 ? 7.764   93.837  53.174  1.00 77.96  ? 365 GLY   A O     1 
ATOM   2867  N  N     . GLY   A 1  366 ? 9.725   94.307  54.186  1.00 56.70  ? 366 GLY   A N     1 
ATOM   2868  C  CA    . GLY   A 1  366 ? 9.915   92.964  54.700  1.00 47.09  ? 366 GLY   A CA    1 
ATOM   2869  C  C     . GLY   A 1  366 ? 8.716   92.422  55.449  1.00 39.17  ? 366 GLY   A C     1 
ATOM   2870  O  O     . GLY   A 1  366 ? 7.645   93.035  55.458  1.00 42.04  ? 366 GLY   A O     1 
ATOM   2871  N  N     . ASP   A 1  367 ? 8.878   91.275  56.092  1.00 44.79  ? 367 ASP   A N     1 
ATOM   2872  C  CA    . ASP   A 1  367 ? 7.771   90.653  56.812  1.00 54.62  ? 367 ASP   A CA    1 
ATOM   2873  C  C     . ASP   A 1  367 ? 7.725   91.038  58.287  1.00 44.15  ? 367 ASP   A C     1 
ATOM   2874  O  O     . ASP   A 1  367 ? 6.710   90.790  58.944  1.00 44.51  ? 367 ASP   A O     1 
ATOM   2875  C  CB    . ASP   A 1  367 ? 7.847   89.122  56.677  1.00 50.12  ? 367 ASP   A CB    1 
ATOM   2876  C  CG    . ASP   A 1  367 ? 7.951   88.667  55.226  1.00 56.99  ? 367 ASP   A CG    1 
ATOM   2877  O  OD1   . ASP   A 1  367 ? 6.918   88.733  54.516  1.00 48.59  ? 367 ASP   A OD1   1 
ATOM   2878  O  OD2   . ASP   A 1  367 ? 9.070   88.281  54.797  1.00 46.60  ? 367 ASP   A OD2   1 
ATOM   2879  N  N     . LEU   A 1  368 ? 8.778   91.650  58.814  1.00 44.35  ? 368 LEU   A N     1 
ATOM   2880  C  CA    . LEU   A 1  368 ? 8.857   91.959  60.233  1.00 47.45  ? 368 LEU   A CA    1 
ATOM   2881  C  C     . LEU   A 1  368 ? 8.232   93.313  60.514  1.00 42.35  ? 368 LEU   A C     1 
ATOM   2882  O  O     . LEU   A 1  368 ? 8.499   94.290  59.807  1.00 42.23  ? 368 LEU   A O     1 
ATOM   2883  C  CB    . LEU   A 1  368 ? 10.308  91.958  60.716  1.00 48.00  ? 368 LEU   A CB    1 
ATOM   2884  C  CG    . LEU   A 1  368 ? 10.993  90.599  60.789  1.00 47.24  ? 368 LEU   A CG    1 
ATOM   2885  C  CD1   . LEU   A 1  368 ? 11.963  90.567  61.976  1.00 40.29  ? 368 LEU   A CD1   1 
ATOM   2886  C  CD2   . LEU   A 1  368 ? 9.935   89.491  60.883  1.00 48.74  ? 368 LEU   A CD2   1 
ATOM   2887  N  N     . ALA   A 1  369 ? 7.421   93.368  61.559  1.00 38.84  ? 369 ALA   A N     1 
ATOM   2888  C  CA    . ALA   A 1  369 ? 6.912   94.639  62.032  1.00 43.45  ? 369 ALA   A CA    1 
ATOM   2889  C  C     . ALA   A 1  369 ? 7.989   95.369  62.847  1.00 42.61  ? 369 ALA   A C     1 
ATOM   2890  O  O     . ALA   A 1  369 ? 8.994   94.792  63.263  1.00 47.00  ? 369 ALA   A O     1 
ATOM   2891  C  CB    . ALA   A 1  369 ? 5.635   94.416  62.840  1.00 38.93  ? 369 ALA   A CB    1 
ATOM   2892  N  N     . LYS   A 1  370 ? 7.794   96.668  63.022  1.00 46.39  ? 370 LYS   A N     1 
ATOM   2893  C  CA    . LYS   A 1  370 ? 8.722   97.489  63.784  1.00 49.80  ? 370 LYS   A CA    1 
ATOM   2894  C  C     . LYS   A 1  370 ? 8.244   97.551  65.230  1.00 49.26  ? 370 LYS   A C     1 
ATOM   2895  O  O     . LYS   A 1  370 ? 7.168   98.084  65.505  1.00 56.97  ? 370 LYS   A O     1 
ATOM   2896  C  CB    . LYS   A 1  370 ? 8.823   98.891  63.177  1.00 53.24  ? 370 LYS   A CB    1 
ATOM   2897  C  CG    . LYS   A 1  370 ? 9.620   99.891  64.011  1.00 67.73  ? 370 LYS   A CG    1 
ATOM   2898  C  CD    . LYS   A 1  370 ? 9.060   101.324 63.908  1.00 82.14  ? 370 LYS   A CD    1 
ATOM   2899  C  CE    . LYS   A 1  370 ? 7.866   101.563 64.858  1.00 78.26  ? 370 LYS   A CE    1 
ATOM   2900  N  NZ    . LYS   A 1  370 ? 7.452   103.006 64.945  1.00 66.91  ? 370 LYS   A NZ    1 
ATOM   2901  N  N     . VAL   A 1  371 ? 9.031   96.991  66.140  1.00 50.75  ? 371 VAL   A N     1 
ATOM   2902  C  CA    . VAL   A 1  371 ? 8.688   96.895  67.553  1.00 40.38  ? 371 VAL   A CA    1 
ATOM   2903  C  C     . VAL   A 1  371 ? 9.505   97.915  68.329  1.00 47.71  ? 371 VAL   A C     1 
ATOM   2904  O  O     . VAL   A 1  371 ? 10.612  98.293  67.924  1.00 46.84  ? 371 VAL   A O     1 
ATOM   2905  C  CB    . VAL   A 1  371 ? 8.959   95.481  68.097  1.00 36.91  ? 371 VAL   A CB    1 
ATOM   2906  C  CG1   . VAL   A 1  371 ? 8.284   94.425  67.239  1.00 27.33  ? 371 VAL   A CG1   1 
ATOM   2907  C  CG2   . VAL   A 1  371 ? 10.443  95.253  68.162  1.00 34.24  ? 371 VAL   A CG2   1 
ATOM   2908  N  N     . GLN   A 1  372 ? 8.975   98.342  69.474  1.00 50.26  ? 372 GLN   A N     1 
ATOM   2909  C  CA    A GLN   A 1  372 ? 9.648   99.357  70.276  0.52 57.05  ? 372 GLN   A CA    1 
ATOM   2910  C  CA    B GLN   A 1  372 ? 9.670   99.363  70.251  0.48 57.04  ? 372 GLN   A CA    1 
ATOM   2911  C  C     . GLN   A 1  372 ? 10.781  98.796  71.137  1.00 55.65  ? 372 GLN   A C     1 
ATOM   2912  O  O     . GLN   A 1  372 ? 11.575  99.578  71.682  1.00 47.63  ? 372 GLN   A O     1 
ATOM   2913  C  CB    A GLN   A 1  372 ? 8.625   100.090 71.152  0.52 55.84  ? 372 GLN   A CB    1 
ATOM   2914  C  CB    B GLN   A 1  372 ? 8.665   100.177 71.086  0.48 55.83  ? 372 GLN   A CB    1 
ATOM   2915  C  CG    A GLN   A 1  372 ? 7.566   100.842 70.354  0.52 56.05  ? 372 GLN   A CG    1 
ATOM   2916  C  CG    B GLN   A 1  372 ? 7.785   99.391  72.045  0.48 57.46  ? 372 GLN   A CG    1 
ATOM   2917  C  CD    A GLN   A 1  372 ? 8.165   101.715 69.262  0.52 56.93  ? 372 GLN   A CD    1 
ATOM   2918  C  CD    B GLN   A 1  372 ? 6.605   100.211 72.559  0.48 58.49  ? 372 GLN   A CD    1 
ATOM   2919  O  OE1   A GLN   A 1  372 ? 7.768   101.635 68.096  0.52 56.72  ? 372 GLN   A OE1   1 
ATOM   2920  O  OE1   B GLN   A 1  372 ? 5.829   99.753  73.402  0.48 57.89  ? 372 GLN   A OE1   1 
ATOM   2921  N  NE2   A GLN   A 1  372 ? 9.127   102.555 69.637  0.52 54.33  ? 372 GLN   A NE2   1 
ATOM   2922  N  NE2   B GLN   A 1  372 ? 6.464   101.425 72.045  0.48 58.75  ? 372 GLN   A NE2   1 
ATOM   2923  N  N     . ARG   A 1  373 ? 10.885  97.475  71.272  1.00 46.56  ? 373 ARG   A N     1 
ATOM   2924  C  CA    . ARG   A 1  373 ? 11.997  96.886  72.002  1.00 39.12  ? 373 ARG   A CA    1 
ATOM   2925  C  C     . ARG   A 1  373 ? 12.112  95.418  71.608  1.00 38.31  ? 373 ARG   A C     1 
ATOM   2926  O  O     . ARG   A 1  373 ? 11.123  94.779  71.240  1.00 40.11  ? 373 ARG   A O     1 
ATOM   2927  C  CB    . ARG   A 1  373 ? 11.845  97.057  73.525  1.00 41.26  ? 373 ARG   A CB    1 
ATOM   2928  C  CG    . ARG   A 1  373 ? 10.637  96.361  74.202  1.00 37.83  ? 373 ARG   A CG    1 
ATOM   2929  C  CD    . ARG   A 1  373 ? 10.329  96.962  75.624  1.00 44.88  ? 373 ARG   A CD    1 
ATOM   2930  N  NE    . ARG   A 1  373 ? 9.880   98.354  75.561  1.00 42.99  ? 373 ARG   A NE    1 
ATOM   2931  C  CZ    . ARG   A 1  373 ? 8.652   98.730  75.214  1.00 50.45  ? 373 ARG   A CZ    1 
ATOM   2932  N  NH1   . ARG   A 1  373 ? 7.696   97.844  74.993  1.00 45.42  ? 373 ARG   A NH1   1 
ATOM   2933  N  NH2   . ARG   A 1  373 ? 8.382   100.026 75.062  1.00 52.26  ? 373 ARG   A NH2   1 
ATOM   2934  N  N     . ALA   A 1  374 ? 13.335  94.900  71.669  1.00 38.13  ? 374 ALA   A N     1 
ATOM   2935  C  CA    . ALA   A 1  374 ? 13.635  93.561  71.187  1.00 33.71  ? 374 ALA   A CA    1 
ATOM   2936  C  C     . ALA   A 1  374 ? 14.811  93.022  71.977  1.00 31.29  ? 374 ALA   A C     1 
ATOM   2937  O  O     . ALA   A 1  374 ? 15.516  93.767  72.660  1.00 33.29  ? 374 ALA   A O     1 
ATOM   2938  C  CB    . ALA   A 1  374 ? 13.935  93.563  69.685  1.00 35.29  ? 374 ALA   A CB    1 
ATOM   2939  N  N     . VAL   A 1  375 ? 15.032  91.715  71.876  1.00 27.20  ? 375 VAL   A N     1 
ATOM   2940  C  CA    . VAL   A 1  375 ? 16.084  91.103  72.679  1.00 31.18  ? 375 VAL   A CA    1 
ATOM   2941  C  C     . VAL   A 1  375 ? 16.553  89.818  72.014  1.00 32.29  ? 375 VAL   A C     1 
ATOM   2942  O  O     . VAL   A 1  375 ? 15.751  89.006  71.542  1.00 36.90  ? 375 VAL   A O     1 
ATOM   2943  C  CB    . VAL   A 1  375 ? 15.602  90.836  74.120  1.00 25.15  ? 375 VAL   A CB    1 
ATOM   2944  C  CG1   . VAL   A 1  375 ? 14.513  89.779  74.094  1.00 28.34  ? 375 VAL   A CG1   1 
ATOM   2945  C  CG2   . VAL   A 1  375 ? 16.766  90.407  74.992  1.00 25.95  ? 375 VAL   A CG2   1 
ATOM   2946  N  N     . CYS   A 1  376 ? 17.865  89.631  72.002  1.00 33.23  ? 376 CYS   A N     1 
ATOM   2947  C  CA    . CYS   A 1  376 ? 18.473  88.368  71.622  1.00 32.40  ? 376 CYS   A CA    1 
ATOM   2948  C  C     . CYS   A 1  376 ? 19.221  87.836  72.838  1.00 31.26  ? 376 CYS   A C     1 
ATOM   2949  O  O     . CYS   A 1  376 ? 20.078  88.530  73.387  1.00 36.24  ? 376 CYS   A O     1 
ATOM   2950  C  CB    . CYS   A 1  376 ? 19.404  88.550  70.421  1.00 27.91  ? 376 CYS   A CB    1 
ATOM   2951  S  SG    . CYS   A 1  376 ? 20.076  86.999  69.788  1.00 33.55  ? 376 CYS   A SG    1 
ATOM   2952  N  N     . MET   A 1  377 ? 18.863  86.638  73.290  1.00 26.02  ? 377 MET   A N     1 
ATOM   2953  C  CA    . MET   A 1  377 ? 19.634  85.945  74.311  1.00 30.95  ? 377 MET   A CA    1 
ATOM   2954  C  C     . MET   A 1  377 ? 20.686  85.066  73.647  1.00 31.99  ? 377 MET   A C     1 
ATOM   2955  O  O     . MET   A 1  377 ? 20.410  84.399  72.645  1.00 31.12  ? 377 MET   A O     1 
ATOM   2956  C  CB    . MET   A 1  377 ? 18.722  85.105  75.211  1.00 26.62  ? 377 MET   A CB    1 
ATOM   2957  C  CG    . MET   A 1  377 ? 19.447  84.383  76.348  1.00 32.92  ? 377 MET   A CG    1 
ATOM   2958  S  SD    . MET   A 1  377 ? 18.326  83.529  77.504  1.00 38.89  ? 377 MET   A SD    1 
ATOM   2959  C  CE    . MET   A 1  377 ? 17.786  84.957  78.407  1.00 35.41  ? 377 MET   A CE    1 
ATOM   2960  N  N     . LEU   A 1  378 ? 21.902  85.096  74.192  1.00 34.77  ? 378 LEU   A N     1 
ATOM   2961  C  CA    . LEU   A 1  378 ? 22.990  84.190  73.803  1.00 34.98  ? 378 LEU   A CA    1 
ATOM   2962  C  C     . LEU   A 1  378 ? 23.322  83.368  75.037  1.00 32.78  ? 378 LEU   A C     1 
ATOM   2963  O  O     . LEU   A 1  378 ? 24.110  83.787  75.883  1.00 40.16  ? 378 LEU   A O     1 
ATOM   2964  C  CB    . LEU   A 1  378 ? 24.252  84.918  73.287  1.00 29.37  ? 378 LEU   A CB    1 
ATOM   2965  C  CG    . LEU   A 1  378 ? 24.109  85.881  72.110  1.00 36.83  ? 378 LEU   A CG    1 
ATOM   2966  C  CD1   . LEU   A 1  378 ? 25.482  86.322  71.635  1.00 29.68  ? 378 LEU   A CD1   1 
ATOM   2967  C  CD2   . LEU   A 1  378 ? 23.290  85.282  70.987  1.00 20.34  ? 378 LEU   A CD2   1 
ATOM   2968  N  N     . SER   A 1  379 ? 22.712  82.204  75.147  1.00 32.46  ? 379 SER   A N     1 
ATOM   2969  C  CA    . SER   A 1  379 ? 22.975  81.283  76.239  1.00 32.59  ? 379 SER   A CA    1 
ATOM   2970  C  C     . SER   A 1  379 ? 23.822  80.135  75.715  1.00 34.62  ? 379 SER   A C     1 
ATOM   2971  O  O     . SER   A 1  379 ? 23.525  79.584  74.654  1.00 34.83  ? 379 SER   A O     1 
ATOM   2972  C  CB    . SER   A 1  379 ? 21.667  80.752  76.826  1.00 33.28  ? 379 SER   A CB    1 
ATOM   2973  O  OG    . SER   A 1  379 ? 20.813  80.260  75.806  1.00 42.66  ? 379 SER   A OG    1 
ATOM   2974  N  N     . ASN   A 1  380 ? 24.885  79.791  76.440  1.00 34.80  ? 380 ASN   A N     1 
ATOM   2975  C  CA    . ASN   A 1  380 ? 25.618  78.554  76.176  1.00 28.01  ? 380 ASN   A CA    1 
ATOM   2976  C  C     . ASN   A 1  380 ? 25.004  77.455  77.035  1.00 32.36  ? 380 ASN   A C     1 
ATOM   2977  O  O     . ASN   A 1  380 ? 25.433  77.202  78.162  1.00 40.68  ? 380 ASN   A O     1 
ATOM   2978  C  CB    . ASN   A 1  380 ? 27.101  78.727  76.455  1.00 31.70  ? 380 ASN   A CB    1 
ATOM   2979  C  CG    . ASN   A 1  380 ? 27.912  77.549  75.976  1.00 27.72  ? 380 ASN   A CG    1 
ATOM   2980  O  OD1   . ASN   A 1  380 ? 27.416  76.436  75.935  1.00 28.62  ? 380 ASN   A OD1   1 
ATOM   2981  N  ND2   . ASN   A 1  380 ? 29.165  77.788  75.618  1.00 29.86  ? 380 ASN   A ND2   1 
ATOM   2982  N  N     . THR   A 1  381 ? 23.973  76.803  76.507  1.00 35.66  ? 381 THR   A N     1 
ATOM   2983  C  CA    . THR   A 1  381 ? 23.342  75.669  77.172  1.00 40.17  ? 381 THR   A CA    1 
ATOM   2984  C  C     . THR   A 1  381 ? 23.773  74.349  76.536  1.00 35.60  ? 381 THR   A C     1 
ATOM   2985  O  O     . THR   A 1  381 ? 24.130  74.291  75.354  1.00 32.93  ? 381 THR   A O     1 
ATOM   2986  C  CB    . THR   A 1  381 ? 21.816  75.783  77.125  1.00 30.08  ? 381 THR   A CB    1 
ATOM   2987  O  OG1   . THR   A 1  381 ? 21.216  74.612  77.711  1.00 36.68  ? 381 THR   A OG1   1 
ATOM   2988  C  CG2   . THR   A 1  381 ? 21.349  75.966  75.704  1.00 25.89  ? 381 THR   A CG2   1 
ATOM   2989  N  N     . THR   A 1  382 ? 23.742  73.287  77.342  1.00 30.65  ? 382 THR   A N     1 
ATOM   2990  C  CA    . THR   A 1  382 ? 24.071  71.957  76.845  1.00 29.86  ? 382 THR   A CA    1 
ATOM   2991  C  C     . THR   A 1  382 ? 22.918  71.337  76.071  1.00 33.14  ? 382 THR   A C     1 
ATOM   2992  O  O     . THR   A 1  382 ? 23.133  70.365  75.346  1.00 36.56  ? 382 THR   A O     1 
ATOM   2993  C  CB    . THR   A 1  382 ? 24.493  71.013  77.996  1.00 39.40  ? 382 THR   A CB    1 
ATOM   2994  O  OG1   . THR   A 1  382 ? 23.447  70.912  78.971  1.00 38.75  ? 382 THR   A OG1   1 
ATOM   2995  C  CG2   . THR   A 1  382 ? 25.795  71.483  78.686  1.00 30.19  ? 382 THR   A CG2   1 
ATOM   2996  N  N     . ALA   A 1  383 ? 21.710  71.888  76.177  1.00 29.35  ? 383 ALA   A N     1 
ATOM   2997  C  CA    . ALA   A 1  383 ? 20.600  71.342  75.410  1.00 33.06  ? 383 ALA   A CA    1 
ATOM   2998  C  C     . ALA   A 1  383 ? 20.849  71.414  73.902  1.00 31.59  ? 383 ALA   A C     1 
ATOM   2999  O  O     . ALA   A 1  383 ? 20.194  70.697  73.136  1.00 24.61  ? 383 ALA   A O     1 
ATOM   3000  C  CB    . ALA   A 1  383 ? 19.300  72.071  75.787  1.00 30.80  ? 383 ALA   A CB    1 
ATOM   3001  N  N     . ILE   A 1  384 ? 21.775  72.261  73.450  1.00 34.78  ? 384 ILE   A N     1 
ATOM   3002  C  CA    . ILE   A 1  384 ? 22.041  72.339  72.016  1.00 33.19  ? 384 ILE   A CA    1 
ATOM   3003  C  C     . ILE   A 1  384 ? 22.647  71.053  71.470  1.00 33.55  ? 384 ILE   A C     1 
ATOM   3004  O  O     . ILE   A 1  384 ? 22.662  70.858  70.244  1.00 29.88  ? 384 ILE   A O     1 
ATOM   3005  C  CB    . ILE   A 1  384 ? 22.938  73.551  71.680  1.00 22.88  ? 384 ILE   A CB    1 
ATOM   3006  C  CG1   . ILE   A 1  384 ? 22.587  74.090  70.301  1.00 21.35  ? 384 ILE   A CG1   1 
ATOM   3007  C  CG2   . ILE   A 1  384 ? 24.412  73.210  71.763  1.00 17.48  ? 384 ILE   A CG2   1 
ATOM   3008  C  CD1   . ILE   A 1  384 ? 23.372  75.302  69.919  1.00 22.01  ? 384 ILE   A CD1   1 
ATOM   3009  N  N     . ALA   A 1  385 ? 23.126  70.156  72.343  1.00 29.44  ? 385 ALA   A N     1 
ATOM   3010  C  CA    . ALA   A 1  385 ? 23.653  68.886  71.850  1.00 30.81  ? 385 ALA   A CA    1 
ATOM   3011  C  C     . ALA   A 1  385 ? 22.562  67.982  71.323  1.00 28.94  ? 385 ALA   A C     1 
ATOM   3012  O  O     . ALA   A 1  385 ? 22.871  66.995  70.653  1.00 38.92  ? 385 ALA   A O     1 
ATOM   3013  C  CB    . ALA   A 1  385 ? 24.445  68.154  72.930  1.00 28.60  ? 385 ALA   A CB    1 
ATOM   3014  N  N     . GLU   A 1  386 ? 21.299  68.279  71.619  1.00 32.22  ? 386 GLU   A N     1 
ATOM   3015  C  CA    . GLU   A 1  386 ? 20.220  67.607  70.908  1.00 34.21  ? 386 GLU   A CA    1 
ATOM   3016  C  C     . GLU   A 1  386 ? 20.455  67.679  69.407  1.00 34.51  ? 386 GLU   A C     1 
ATOM   3017  O  O     . GLU   A 1  386 ? 20.294  66.685  68.694  1.00 34.98  ? 386 GLU   A O     1 
ATOM   3018  C  CB    . GLU   A 1  386 ? 18.875  68.243  71.261  1.00 34.18  ? 386 GLU   A CB    1 
ATOM   3019  C  CG    . GLU   A 1  386 ? 18.412  68.037  72.699  1.00 32.96  ? 386 GLU   A CG    1 
ATOM   3020  C  CD    . GLU   A 1  386 ? 17.026  68.622  72.940  1.00 38.91  ? 386 GLU   A CD    1 
ATOM   3021  O  OE1   . GLU   A 1  386 ? 16.122  68.371  72.115  1.00 38.47  ? 386 GLU   A OE1   1 
ATOM   3022  O  OE2   . GLU   A 1  386 ? 16.849  69.357  73.935  1.00 43.62  ? 386 GLU   A OE2   1 
ATOM   3023  N  N     . ALA   A 1  387 ? 20.850  68.854  68.913  1.00 25.96  ? 387 ALA   A N     1 
ATOM   3024  C  CA    . ALA   A 1  387 ? 21.005  69.040  67.482  1.00 29.03  ? 387 ALA   A CA    1 
ATOM   3025  C  C     . ALA   A 1  387 ? 22.144  68.195  66.947  1.00 37.92  ? 387 ALA   A C     1 
ATOM   3026  O  O     . ALA   A 1  387 ? 22.102  67.778  65.783  1.00 38.03  ? 387 ALA   A O     1 
ATOM   3027  C  CB    . ALA   A 1  387 ? 21.238  70.518  67.158  1.00 21.25  ? 387 ALA   A CB    1 
ATOM   3028  N  N     . TRP   A 1  388 ? 23.166  67.939  67.778  1.00 36.78  ? 388 TRP   A N     1 
ATOM   3029  C  CA    . TRP   A 1  388 ? 24.260  67.053  67.382  1.00 32.77  ? 388 TRP   A CA    1 
ATOM   3030  C  C     . TRP   A 1  388 ? 23.803  65.600  67.349  1.00 36.84  ? 388 TRP   A C     1 
ATOM   3031  O  O     . TRP   A 1  388 ? 24.194  64.834  66.456  1.00 34.54  ? 388 TRP   A O     1 
ATOM   3032  C  CB    . TRP   A 1  388 ? 25.439  67.204  68.344  1.00 33.56  ? 388 TRP   A CB    1 
ATOM   3033  C  CG    . TRP   A 1  388 ? 26.188  68.498  68.243  1.00 36.54  ? 388 TRP   A CG    1 
ATOM   3034  C  CD1   . TRP   A 1  388 ? 26.639  69.279  69.281  1.00 35.14  ? 388 TRP   A CD1   1 
ATOM   3035  C  CD2   . TRP   A 1  388 ? 26.571  69.172  67.038  1.00 30.92  ? 388 TRP   A CD2   1 
ATOM   3036  N  NE1   . TRP   A 1  388 ? 27.295  70.392  68.784  1.00 31.75  ? 388 TRP   A NE1   1 
ATOM   3037  C  CE2   . TRP   A 1  388 ? 27.254  70.354  67.414  1.00 27.16  ? 388 TRP   A CE2   1 
ATOM   3038  C  CE3   . TRP   A 1  388 ? 26.415  68.886  65.682  1.00 29.73  ? 388 TRP   A CE3   1 
ATOM   3039  C  CZ2   . TRP   A 1  388 ? 27.767  71.242  66.483  1.00 33.64  ? 388 TRP   A CZ2   1 
ATOM   3040  C  CZ3   . TRP   A 1  388 ? 26.933  69.766  64.758  1.00 34.64  ? 388 TRP   A CZ3   1 
ATOM   3041  C  CH2   . TRP   A 1  388 ? 27.602  70.933  65.160  1.00 38.05  ? 388 TRP   A CH2   1 
ATOM   3042  N  N     . ALA   A 1  389 ? 22.985  65.201  68.323  1.00 30.71  ? 389 ALA   A N     1 
ATOM   3043  C  CA    . ALA   A 1  389 ? 22.533  63.821  68.386  1.00 27.80  ? 389 ALA   A CA    1 
ATOM   3044  C  C     . ALA   A 1  389 ? 21.722  63.450  67.152  1.00 29.54  ? 389 ALA   A C     1 
ATOM   3045  O  O     . ALA   A 1  389 ? 21.918  62.387  66.566  1.00 34.64  ? 389 ALA   A O     1 
ATOM   3046  C  CB    . ALA   A 1  389 ? 21.719  63.599  69.657  1.00 26.85  ? 389 ALA   A CB    1 
ATOM   3047  N  N     . ARG   A 1  390 ? 20.795  64.304  66.735  1.00 29.84  ? 390 ARG   A N     1 
ATOM   3048  C  CA    . ARG   A 1  390 ? 19.951  63.873  65.626  1.00 33.30  ? 390 ARG   A CA    1 
ATOM   3049  C  C     . ARG   A 1  390 ? 20.712  63.876  64.303  1.00 31.46  ? 390 ARG   A C     1 
ATOM   3050  O  O     . ARG   A 1  390 ? 20.475  63.011  63.456  1.00 31.58  ? 390 ARG   A O     1 
ATOM   3051  C  CB    . ARG   A 1  390 ? 18.677  64.718  65.544  1.00 31.25  ? 390 ARG   A CB    1 
ATOM   3052  C  CG    . ARG   A 1  390 ? 18.798  66.147  66.005  1.00 38.24  ? 390 ARG   A CG    1 
ATOM   3053  C  CD    . ARG   A 1  390 ? 17.414  66.748  66.191  1.00 33.83  ? 390 ARG   A CD    1 
ATOM   3054  N  NE    . ARG   A 1  390 ? 17.070  67.601  65.068  1.00 31.35  ? 390 ARG   A NE    1 
ATOM   3055  C  CZ    . ARG   A 1  390 ? 17.288  68.904  65.060  1.00 38.43  ? 390 ARG   A CZ    1 
ATOM   3056  N  NH1   . ARG   A 1  390 ? 17.769  69.532  66.130  1.00 47.04  ? 390 ARG   A NH1   1 
ATOM   3057  N  NH2   . ARG   A 1  390 ? 17.021  69.593  63.963  1.00 30.44  ? 390 ARG   A NH2   1 
ATOM   3058  N  N     . LEU   A 1  391 ? 21.632  64.819  64.113  1.00 32.38  ? 391 LEU   A N     1 
ATOM   3059  C  CA    . LEU   A 1  391 ? 22.467  64.827  62.918  1.00 21.60  ? 391 LEU   A CA    1 
ATOM   3060  C  C     . LEU   A 1  391 ? 23.413  63.634  62.902  1.00 31.01  ? 391 LEU   A C     1 
ATOM   3061  O  O     . LEU   A 1  391 ? 23.637  63.035  61.848  1.00 36.29  ? 391 LEU   A O     1 
ATOM   3062  C  CB    . LEU   A 1  391 ? 23.237  66.137  62.865  1.00 27.24  ? 391 LEU   A CB    1 
ATOM   3063  C  CG    . LEU   A 1  391 ? 24.015  66.578  61.647  1.00 36.85  ? 391 LEU   A CG    1 
ATOM   3064  C  CD1   . LEU   A 1  391 ? 23.033  67.094  60.581  1.00 31.01  ? 391 LEU   A CD1   1 
ATOM   3065  C  CD2   . LEU   A 1  391 ? 25.026  67.654  62.079  1.00 29.57  ? 391 LEU   A CD2   1 
ATOM   3066  N  N     . ASP   A 1  392 ? 23.947  63.246  64.068  1.00 31.92  ? 392 ASP   A N     1 
ATOM   3067  C  CA    . ASP   A 1  392 ? 24.791  62.050  64.152  1.00 36.82  ? 392 ASP   A CA    1 
ATOM   3068  C  C     . ASP   A 1  392 ? 23.996  60.771  63.886  1.00 35.60  ? 392 ASP   A C     1 
ATOM   3069  O  O     . ASP   A 1  392 ? 24.526  59.808  63.321  1.00 35.45  ? 392 ASP   A O     1 
ATOM   3070  C  CB    . ASP   A 1  392 ? 25.468  61.969  65.532  1.00 35.16  ? 392 ASP   A CB    1 
ATOM   3071  C  CG    . ASP   A 1  392 ? 26.599  62.964  65.691  1.00 36.66  ? 392 ASP   A CG    1 
ATOM   3072  O  OD1   . ASP   A 1  392 ? 26.989  63.590  64.685  1.00 46.18  ? 392 ASP   A OD1   1 
ATOM   3073  O  OD2   . ASP   A 1  392 ? 27.097  63.135  66.818  1.00 39.95  ? 392 ASP   A OD2   1 
ATOM   3074  N  N     . HIS   A 1  393 ? 22.740  60.721  64.328  1.00 30.28  ? 393 HIS   A N     1 
ATOM   3075  C  CA    . HIS   A 1  393 ? 21.917  59.552  64.056  1.00 29.92  ? 393 HIS   A CA    1 
ATOM   3076  C  C     . HIS   A 1  393 ? 21.655  59.400  62.560  1.00 35.25  ? 393 HIS   A C     1 
ATOM   3077  O  O     . HIS   A 1  393 ? 21.661  58.278  62.044  1.00 34.50  ? 393 HIS   A O     1 
ATOM   3078  C  CB    . HIS   A 1  393 ? 20.613  59.650  64.846  1.00 23.65  ? 393 HIS   A CB    1 
ATOM   3079  C  CG    . HIS   A 1  393 ? 19.602  58.597  64.505  1.00 36.60  ? 393 HIS   A CG    1 
ATOM   3080  N  ND1   . HIS   A 1  393 ? 19.613  57.339  65.070  1.00 36.49  ? 393 HIS   A ND1   1 
ATOM   3081  C  CD2   . HIS   A 1  393 ? 18.524  58.629  63.679  1.00 38.90  ? 393 HIS   A CD2   1 
ATOM   3082  C  CE1   . HIS   A 1  393 ? 18.590  56.640  64.605  1.00 34.20  ? 393 HIS   A CE1   1 
ATOM   3083  N  NE2   . HIS   A 1  393 ? 17.916  57.399  63.755  1.00 38.22  ? 393 HIS   A NE2   1 
ATOM   3084  N  N     . LYS   A 1  394 ? 21.433  60.511  61.841  1.00 25.94  ? 394 LYS   A N     1 
ATOM   3085  C  CA    . LYS   A 1  394 ? 21.210  60.414  60.404  1.00 23.58  ? 394 LYS   A CA    1 
ATOM   3086  C  C     . LYS   A 1  394 ? 22.458  59.919  59.709  1.00 30.22  ? 394 LYS   A C     1 
ATOM   3087  O  O     . LYS   A 1  394 ? 22.389  59.166  58.730  1.00 31.26  ? 394 LYS   A O     1 
ATOM   3088  C  CB    . LYS   A 1  394 ? 20.794  61.763  59.825  1.00 21.98  ? 394 LYS   A CB    1 
ATOM   3089  C  CG    . LYS   A 1  394 ? 19.359  62.165  60.153  1.00 20.69  ? 394 LYS   A CG    1 
ATOM   3090  C  CD    . LYS   A 1  394 ? 19.024  63.515  59.558  1.00 16.85  ? 394 LYS   A CD    1 
ATOM   3091  C  CE    . LYS   A 1  394 ? 17.592  63.885  59.853  1.00 21.57  ? 394 LYS   A CE    1 
ATOM   3092  N  NZ    . LYS   A 1  394 ? 16.798  62.637  60.052  1.00 36.76  ? 394 LYS   A NZ    1 
ATOM   3093  N  N     . PHE   A 1  395 ? 23.611  60.352  60.199  1.00 30.38  ? 395 PHE   A N     1 
ATOM   3094  C  CA    . PHE   A 1  395 ? 24.874  59.910  59.632  1.00 29.21  ? 395 PHE   A CA    1 
ATOM   3095  C  C     . PHE   A 1  395 ? 25.022  58.397  59.788  1.00 34.27  ? 395 PHE   A C     1 
ATOM   3096  O  O     . PHE   A 1  395 ? 25.317  57.682  58.820  1.00 30.56  ? 395 PHE   A O     1 
ATOM   3097  C  CB    . PHE   A 1  395 ? 25.997  60.697  60.321  1.00 25.67  ? 395 PHE   A CB    1 
ATOM   3098  C  CG    . PHE   A 1  395 ? 27.387  60.383  59.852  1.00 26.44  ? 395 PHE   A CG    1 
ATOM   3099  C  CD1   . PHE   A 1  395 ? 28.056  59.262  60.317  1.00 23.66  ? 395 PHE   A CD1   1 
ATOM   3100  C  CD2   . PHE   A 1  395 ? 28.063  61.269  59.019  1.00 24.85  ? 395 PHE   A CD2   1 
ATOM   3101  C  CE1   . PHE   A 1  395 ? 29.354  59.014  59.922  1.00 27.60  ? 395 PHE   A CE1   1 
ATOM   3102  C  CE2   . PHE   A 1  395 ? 29.358  61.018  58.616  1.00 20.02  ? 395 PHE   A CE2   1 
ATOM   3103  C  CZ    . PHE   A 1  395 ? 30.004  59.900  59.066  1.00 23.56  ? 395 PHE   A CZ    1 
ATOM   3104  N  N     . ASP   A 1  396 ? 24.763  57.890  60.998  1.00 28.32  ? 396 ASP   A N     1 
ATOM   3105  C  CA    . ASP   A 1  396 ? 24.927  56.468  61.272  1.00 25.13  ? 396 ASP   A CA    1 
ATOM   3106  C  C     . ASP   A 1  396 ? 24.055  55.617  60.353  1.00 33.91  ? 396 ASP   A C     1 
ATOM   3107  O  O     . ASP   A 1  396 ? 24.530  54.627  59.784  1.00 42.28  ? 396 ASP   A O     1 
ATOM   3108  C  CB    . ASP   A 1  396 ? 24.619  56.179  62.746  1.00 31.22  ? 396 ASP   A CB    1 
ATOM   3109  C  CG    . ASP   A 1  396 ? 25.595  56.869  63.698  1.00 37.11  ? 396 ASP   A CG    1 
ATOM   3110  O  OD1   . ASP   A 1  396 ? 26.679  57.296  63.237  1.00 34.34  ? 396 ASP   A OD1   1 
ATOM   3111  O  OD2   . ASP   A 1  396 ? 25.275  56.982  64.902  1.00 37.02  ? 396 ASP   A OD2   1 
ATOM   3112  N  N     . LEU   A 1  397 ? 22.773  55.986  60.194  1.00 35.58  ? 397 LEU   A N     1 
ATOM   3113  C  CA    . LEU   A 1  397 ? 21.856  55.210  59.354  1.00 32.63  ? 397 LEU   A CA    1 
ATOM   3114  C  C     . LEU   A 1  397 ? 22.418  55.035  57.956  1.00 34.26  ? 397 LEU   A C     1 
ATOM   3115  O  O     . LEU   A 1  397 ? 22.472  53.916  57.431  1.00 37.65  ? 397 LEU   A O     1 
ATOM   3116  C  CB    . LEU   A 1  397 ? 20.478  55.879  59.286  1.00 29.35  ? 397 LEU   A CB    1 
ATOM   3117  C  CG    . LEU   A 1  397 ? 19.674  55.839  60.597  1.00 35.82  ? 397 LEU   A CG    1 
ATOM   3118  C  CD1   . LEU   A 1  397 ? 18.539  56.903  60.666  1.00 21.09  ? 397 LEU   A CD1   1 
ATOM   3119  C  CD2   . LEU   A 1  397 ? 19.145  54.459  60.776  1.00 19.24  ? 397 LEU   A CD2   1 
ATOM   3120  N  N     . MET   A 1  398 ? 22.852  56.141  57.344  1.00 29.73  ? 398 MET   A N     1 
ATOM   3121  C  CA    . MET   A 1  398 ? 23.412  56.079  56.002  1.00 28.71  ? 398 MET   A CA    1 
ATOM   3122  C  C     . MET   A 1  398 ? 24.778  55.416  56.004  1.00 30.01  ? 398 MET   A C     1 
ATOM   3123  O  O     . MET   A 1  398 ? 25.085  54.641  55.099  1.00 35.57  ? 398 MET   A O     1 
ATOM   3124  C  CB    . MET   A 1  398 ? 23.510  57.476  55.389  1.00 26.96  ? 398 MET   A CB    1 
ATOM   3125  C  CG    . MET   A 1  398 ? 22.183  58.116  55.039  1.00 31.26  ? 398 MET   A CG    1 
ATOM   3126  S  SD    . MET   A 1  398 ? 22.437  59.520  53.938  1.00 36.13  ? 398 MET   A SD    1 
ATOM   3127  C  CE    . MET   A 1  398 ? 23.149  60.733  55.049  1.00 38.47  ? 398 MET   A CE    1 
ATOM   3128  N  N     . TYR   A 1  399 ? 25.619  55.708  57.006  1.00 38.48  ? 399 TYR   A N     1 
ATOM   3129  C  CA    . TYR   A 1  399 ? 27.008  55.260  56.931  1.00 33.17  ? 399 TYR   A CA    1 
ATOM   3130  C  C     . TYR   A 1  399 ? 27.150  53.776  57.189  1.00 23.57  ? 399 TYR   A C     1 
ATOM   3131  O  O     . TYR   A 1  399 ? 28.128  53.174  56.750  1.00 25.53  ? 399 TYR   A O     1 
ATOM   3132  C  CB    . TYR   A 1  399 ? 27.903  56.021  57.910  1.00 32.18  ? 399 TYR   A CB    1 
ATOM   3133  C  CG    . TYR   A 1  399 ? 29.383  55.743  57.678  1.00 36.59  ? 399 TYR   A CG    1 
ATOM   3134  C  CD1   . TYR   A 1  399 ? 30.057  56.321  56.601  1.00 30.71  ? 399 TYR   A CD1   1 
ATOM   3135  C  CD2   . TYR   A 1  399 ? 30.099  54.874  58.517  1.00 31.82  ? 399 TYR   A CD2   1 
ATOM   3136  C  CE1   . TYR   A 1  399 ? 31.405  56.056  56.380  1.00 40.02  ? 399 TYR   A CE1   1 
ATOM   3137  C  CE2   . TYR   A 1  399 ? 31.432  54.597  58.292  1.00 28.61  ? 399 TYR   A CE2   1 
ATOM   3138  C  CZ    . TYR   A 1  399 ? 32.081  55.190  57.223  1.00 37.07  ? 399 TYR   A CZ    1 
ATOM   3139  O  OH    . TYR   A 1  399 ? 33.408  54.927  56.992  1.00 43.41  ? 399 TYR   A OH    1 
ATOM   3140  N  N     . ALA   A 1  400 ? 26.202  53.169  57.880  1.00 26.40  ? 400 ALA   A N     1 
ATOM   3141  C  CA    . ALA   A 1  400 ? 26.316  51.742  58.113  1.00 26.28  ? 400 ALA   A CA    1 
ATOM   3142  C  C     . ALA   A 1  400 ? 26.112  50.941  56.834  1.00 24.82  ? 400 ALA   A C     1 
ATOM   3143  O  O     . ALA   A 1  400 ? 26.458  49.758  56.797  1.00 36.44  ? 400 ALA   A O     1 
ATOM   3144  C  CB    . ALA   A 1  400 ? 25.333  51.324  59.207  1.00 19.13  ? 400 ALA   A CB    1 
ATOM   3145  N  N     . LYS   A 1  401 ? 25.566  51.560  55.799  1.00 22.67  ? 401 LYS   A N     1 
ATOM   3146  C  CA    . LYS   A 1  401 ? 25.455  50.977  54.472  1.00 30.24  ? 401 LYS   A CA    1 
ATOM   3147  C  C     . LYS   A 1  401 ? 26.399  51.612  53.458  1.00 28.79  ? 401 LYS   A C     1 
ATOM   3148  O  O     . LYS   A 1  401 ? 26.363  51.247  52.281  1.00 33.75  ? 401 LYS   A O     1 
ATOM   3149  C  CB    . LYS   A 1  401 ? 24.010  51.110  53.962  1.00 35.42  ? 401 LYS   A CB    1 
ATOM   3150  C  CG    . LYS   A 1  401 ? 22.970  50.818  55.018  1.00 35.62  ? 401 LYS   A CG    1 
ATOM   3151  C  CD    . LYS   A 1  401 ? 22.346  49.469  54.828  1.00 30.28  ? 401 LYS   A CD    1 
ATOM   3152  C  CE    . LYS   A 1  401 ? 21.312  49.212  55.889  1.00 30.51  ? 401 LYS   A CE    1 
ATOM   3153  N  NZ    . LYS   A 1  401 ? 21.932  49.279  57.246  1.00 44.18  ? 401 LYS   A NZ    1 
ATOM   3154  N  N     . ARG   A 1  402 ? 27.211  52.576  53.865  1.00 29.23  ? 402 ARG   A N     1 
ATOM   3155  C  CA    . ARG   A 1  402 ? 28.169  53.210  52.974  1.00 30.87  ? 402 ARG   A CA    1 
ATOM   3156  C  C     . ARG   A 1  402 ? 27.479  53.968  51.846  1.00 33.84  ? 402 ARG   A C     1 
ATOM   3157  O  O     . ARG   A 1  402 ? 28.113  54.351  50.856  1.00 33.87  ? 402 ARG   A O     1 
ATOM   3158  C  CB    . ARG   A 1  402 ? 29.152  52.173  52.424  1.00 32.88  ? 402 ARG   A CB    1 
ATOM   3159  C  CG    . ARG   A 1  402 ? 30.072  51.586  53.493  1.00 30.98  ? 402 ARG   A CG    1 
ATOM   3160  C  CD    . ARG   A 1  402 ? 30.826  52.713  54.183  1.00 46.78  ? 402 ARG   A CD    1 
ATOM   3161  N  NE    . ARG   A 1  402 ? 31.812  52.227  55.136  1.00 39.29  ? 402 ARG   A NE    1 
ATOM   3162  C  CZ    . ARG   A 1  402 ? 31.517  51.776  56.343  1.00 37.30  ? 402 ARG   A CZ    1 
ATOM   3163  N  NH1   . ARG   A 1  402 ? 30.271  51.729  56.776  1.00 33.48  ? 402 ARG   A NH1   1 
ATOM   3164  N  NH2   . ARG   A 1  402 ? 32.496  51.357  57.134  1.00 41.23  ? 402 ARG   A NH2   1 
ATOM   3165  N  N     . ALA   A 1  403 ? 26.188  54.215  52.009  1.00 27.80  ? 403 ALA   A N     1 
ATOM   3166  C  CA    . ALA   A 1  403 ? 25.397  54.900  51.007  1.00 27.15  ? 403 ALA   A CA    1 
ATOM   3167  C  C     . ALA   A 1  403 ? 26.032  56.233  50.650  1.00 29.75  ? 403 ALA   A C     1 
ATOM   3168  O  O     . ALA   A 1  403 ? 26.242  57.077  51.523  1.00 28.26  ? 403 ALA   A O     1 
ATOM   3169  C  CB    . ALA   A 1  403 ? 23.973  55.094  51.550  1.00 29.10  ? 403 ALA   A CB    1 
ATOM   3170  N  N     . PHE   A 1  404 ? 26.331  56.434  49.363  1.00 26.83  ? 404 PHE   A N     1 
ATOM   3171  C  CA    . PHE   A 1  404 ? 26.866  57.674  48.803  1.00 25.47  ? 404 PHE   A CA    1 
ATOM   3172  C  C     . PHE   A 1  404 ? 28.347  57.881  49.112  1.00 28.81  ? 404 PHE   A C     1 
ATOM   3173  O  O     . PHE   A 1  404 ? 28.958  58.784  48.530  1.00 28.76  ? 404 PHE   A O     1 
ATOM   3174  C  CB    . PHE   A 1  404 ? 26.125  58.928  49.291  1.00 27.59  ? 404 PHE   A CB    1 
ATOM   3175  C  CG    . PHE   A 1  404 ? 24.675  58.938  48.974  1.00 34.73  ? 404 PHE   A CG    1 
ATOM   3176  C  CD1   . PHE   A 1  404 ? 24.234  59.329  47.714  1.00 22.79  ? 404 PHE   A CD1   1 
ATOM   3177  C  CD2   . PHE   A 1  404 ? 23.734  58.600  49.960  1.00 27.47  ? 404 PHE   A CD2   1 
ATOM   3178  C  CE1   . PHE   A 1  404 ? 22.866  59.367  47.433  1.00 30.16  ? 404 PHE   A CE1   1 
ATOM   3179  C  CE2   . PHE   A 1  404 ? 22.371  58.635  49.685  1.00 21.72  ? 404 PHE   A CE2   1 
ATOM   3180  C  CZ    . PHE   A 1  404 ? 21.932  59.023  48.424  1.00 19.73  ? 404 PHE   A CZ    1 
ATOM   3181  N  N     . VAL   A 1  405 ? 28.938  57.090  50.016  1.00 25.91  ? 405 VAL   A N     1 
ATOM   3182  C  CA    . VAL   A 1  405 ? 30.337  57.222  50.408  1.00 26.45  ? 405 VAL   A CA    1 
ATOM   3183  C  C     . VAL   A 1  405 ? 31.238  57.256  49.191  1.00 36.15  ? 405 VAL   A C     1 
ATOM   3184  O  O     . VAL   A 1  405 ? 32.272  57.947  49.186  1.00 34.07  ? 405 VAL   A O     1 
ATOM   3185  C  CB    . VAL   A 1  405 ? 30.715  56.065  51.360  1.00 37.75  ? 405 VAL   A CB    1 
ATOM   3186  C  CG1   . VAL   A 1  405 ? 32.188  56.094  51.675  1.00 35.02  ? 405 VAL   A CG1   1 
ATOM   3187  C  CG2   . VAL   A 1  405 ? 29.874  56.114  52.643  1.00 25.33  ? 405 VAL   A CG2   1 
ATOM   3188  N  N     . HIS   A 1  406 ? 30.850  56.531  48.127  1.00 29.37  ? 406 HIS   A N     1 
ATOM   3189  C  CA    . HIS   A 1  406 ? 31.692  56.404  46.946  1.00 19.55  ? 406 HIS   A CA    1 
ATOM   3190  C  C     . HIS   A 1  406 ? 31.871  57.735  46.246  1.00 31.58  ? 406 HIS   A C     1 
ATOM   3191  O  O     . HIS   A 1  406 ? 32.838  57.887  45.489  1.00 29.70  ? 406 HIS   A O     1 
ATOM   3192  C  CB    . HIS   A 1  406 ? 31.120  55.342  45.983  1.00 24.28  ? 406 HIS   A CB    1 
ATOM   3193  C  CG    . HIS   A 1  406 ? 29.796  55.706  45.380  1.00 33.05  ? 406 HIS   A CG    1 
ATOM   3194  N  ND1   . HIS   A 1  406 ? 29.668  56.144  44.078  1.00 27.30  ? 406 HIS   A ND1   1 
ATOM   3195  C  CD2   . HIS   A 1  406 ? 28.545  55.715  45.905  1.00 29.43  ? 406 HIS   A CD2   1 
ATOM   3196  C  CE1   . HIS   A 1  406 ? 28.394  56.396  43.824  1.00 30.22  ? 406 HIS   A CE1   1 
ATOM   3197  N  NE2   . HIS   A 1  406 ? 27.692  56.147  44.917  1.00 24.99  ? 406 HIS   A NE2   1 
ATOM   3198  N  N     . TRP   A 1  407 ? 30.974  58.705  46.493  1.00 24.93  ? 407 TRP   A N     1 
ATOM   3199  C  CA    . TRP   A 1  407 ? 31.142  60.028  45.895  1.00 33.36  ? 407 TRP   A CA    1 
ATOM   3200  C  C     . TRP   A 1  407 ? 32.300  60.780  46.538  1.00 35.41  ? 407 TRP   A C     1 
ATOM   3201  O  O     . TRP   A 1  407 ? 32.985  61.560  45.871  1.00 37.47  ? 407 TRP   A O     1 
ATOM   3202  C  CB    . TRP   A 1  407 ? 29.859  60.868  46.018  1.00 30.52  ? 407 TRP   A CB    1 
ATOM   3203  C  CG    . TRP   A 1  407 ? 28.722  60.429  45.187  1.00 27.04  ? 407 TRP   A CG    1 
ATOM   3204  C  CD1   . TRP   A 1  407 ? 27.563  59.849  45.618  1.00 23.60  ? 407 TRP   A CD1   1 
ATOM   3205  C  CD2   . TRP   A 1  407 ? 28.619  60.525  43.760  1.00 32.85  ? 407 TRP   A CD2   1 
ATOM   3206  N  NE1   . TRP   A 1  407 ? 26.739  59.579  44.545  1.00 23.45  ? 407 TRP   A NE1   1 
ATOM   3207  C  CE2   . TRP   A 1  407 ? 27.366  59.978  43.392  1.00 29.11  ? 407 TRP   A CE2   1 
ATOM   3208  C  CE3   . TRP   A 1  407 ? 29.465  61.011  42.753  1.00 30.19  ? 407 TRP   A CE3   1 
ATOM   3209  C  CZ2   . TRP   A 1  407 ? 26.934  59.920  42.057  1.00 31.09  ? 407 TRP   A CZ2   1 
ATOM   3210  C  CZ3   . TRP   A 1  407 ? 29.027  60.945  41.408  1.00 35.30  ? 407 TRP   A CZ3   1 
ATOM   3211  C  CH2   . TRP   A 1  407 ? 27.776  60.410  41.083  1.00 28.67  ? 407 TRP   A CH2   1 
ATOM   3212  N  N     . TYR   A 1  408 ? 32.502  60.605  47.843  1.00 34.08  ? 408 TYR   A N     1 
ATOM   3213  C  CA    . TYR   A 1  408 ? 33.569  61.353  48.498  1.00 37.81  ? 408 TYR   A CA    1 
ATOM   3214  C  C     . TYR   A 1  408 ? 34.911  60.684  48.238  1.00 39.94  ? 408 TYR   A C     1 
ATOM   3215  O  O     . TYR   A 1  408 ? 35.889  61.347  47.869  1.00 36.00  ? 408 TYR   A O     1 
ATOM   3216  C  CB    . TYR   A 1  408 ? 33.295  61.460  50.000  1.00 38.90  ? 408 TYR   A CB    1 
ATOM   3217  C  CG    . TYR   A 1  408 ? 31.971  62.118  50.369  1.00 45.17  ? 408 TYR   A CG    1 
ATOM   3218  C  CD1   . TYR   A 1  408 ? 30.776  61.401  50.331  1.00 41.66  ? 408 TYR   A CD1   1 
ATOM   3219  C  CD2   . TYR   A 1  408 ? 31.925  63.446  50.779  1.00 35.36  ? 408 TYR   A CD2   1 
ATOM   3220  C  CE1   . TYR   A 1  408 ? 29.580  61.993  50.669  1.00 36.69  ? 408 TYR   A CE1   1 
ATOM   3221  C  CE2   . TYR   A 1  408 ? 30.749  64.045  51.112  1.00 34.89  ? 408 TYR   A CE2   1 
ATOM   3222  C  CZ    . TYR   A 1  408 ? 29.573  63.320  51.061  1.00 41.20  ? 408 TYR   A CZ    1 
ATOM   3223  O  OH    . TYR   A 1  408 ? 28.395  63.930  51.409  1.00 35.22  ? 408 TYR   A OH    1 
ATOM   3224  N  N     . VAL   A 1  409 ? 34.947  59.356  48.399  1.00 34.80  ? 409 VAL   A N     1 
ATOM   3225  C  CA    . VAL   A 1  409 ? 36.125  58.568  48.058  1.00 37.57  ? 409 VAL   A CA    1 
ATOM   3226  C  C     . VAL   A 1  409 ? 36.565  58.826  46.624  1.00 37.07  ? 409 VAL   A C     1 
ATOM   3227  O  O     . VAL   A 1  409 ? 37.765  58.966  46.342  1.00 42.33  ? 409 VAL   A O     1 
ATOM   3228  C  CB    . VAL   A 1  409 ? 35.850  57.077  48.293  1.00 39.48  ? 409 VAL   A CB    1 
ATOM   3229  C  CG1   . VAL   A 1  409 ? 36.996  56.277  47.724  1.00 23.26  ? 409 VAL   A CG1   1 
ATOM   3230  C  CG2   . VAL   A 1  409 ? 35.647  56.813  49.798  1.00 31.15  ? 409 VAL   A CG2   1 
ATOM   3231  N  N     . GLY   A 1  410 ? 35.607  58.900  45.697  1.00 26.30  ? 410 GLY   A N     1 
ATOM   3232  C  CA    . GLY   A 1  410 ? 35.924  59.206  44.311  1.00 18.79  ? 410 GLY   A CA    1 
ATOM   3233  C  C     . GLY   A 1  410 ? 36.660  60.515  44.116  1.00 34.41  ? 410 GLY   A C     1 
ATOM   3234  O  O     . GLY   A 1  410 ? 37.261  60.736  43.057  1.00 43.38  ? 410 GLY   A O     1 
ATOM   3235  N  N     . GLU   A 1  411 ? 36.625  61.397  45.108  1.00 40.27  ? 411 GLU   A N     1 
ATOM   3236  C  CA    . GLU   A 1  411 ? 37.343  62.657  45.040  1.00 47.47  ? 411 GLU   A CA    1 
ATOM   3237  C  C     . GLU   A 1  411 ? 38.695  62.600  45.757  1.00 44.47  ? 411 GLU   A C     1 
ATOM   3238  O  O     . GLU   A 1  411 ? 39.417  63.603  45.791  1.00 37.43  ? 411 GLU   A O     1 
ATOM   3239  C  CB    . GLU   A 1  411 ? 36.458  63.776  45.601  1.00 45.08  ? 411 GLU   A CB    1 
ATOM   3240  C  CG    . GLU   A 1  411 ? 35.160  63.963  44.830  1.00 27.83  ? 411 GLU   A CG    1 
ATOM   3241  C  CD    . GLU   A 1  411 ? 35.361  64.719  43.537  1.00 39.68  ? 411 GLU   A CD    1 
ATOM   3242  O  OE1   . GLU   A 1  411 ? 36.532  64.918  43.156  1.00 41.81  ? 411 GLU   A OE1   1 
ATOM   3243  O  OE2   . GLU   A 1  411 ? 34.358  65.131  42.905  1.00 40.37  ? 411 GLU   A OE2   1 
ATOM   3244  N  N     . GLY   A 1  412 ? 39.073  61.442  46.295  1.00 38.76  ? 412 GLY   A N     1 
ATOM   3245  C  CA    . GLY   A 1  412 ? 40.371  61.284  46.911  1.00 40.97  ? 412 GLY   A CA    1 
ATOM   3246  C  C     . GLY   A 1  412 ? 40.338  61.236  48.411  1.00 38.60  ? 412 GLY   A C     1 
ATOM   3247  O  O     . GLY   A 1  412 ? 41.389  61.050  49.029  1.00 57.58  ? 412 GLY   A O     1 
ATOM   3248  N  N     . MET   A 1  413 ? 39.170  61.404  49.012  1.00 31.28  ? 413 MET   A N     1 
ATOM   3249  C  CA    . MET   A 1  413 ? 38.988  61.245  50.441  1.00 29.72  ? 413 MET   A CA    1 
ATOM   3250  C  C     . MET   A 1  413 ? 38.896  59.771  50.816  1.00 35.00  ? 413 MET   A C     1 
ATOM   3251  O  O     . MET   A 1  413 ? 38.247  58.973  50.139  1.00 35.32  ? 413 MET   A O     1 
ATOM   3252  C  CB    . MET   A 1  413 ? 37.719  61.980  50.858  1.00 33.72  ? 413 MET   A CB    1 
ATOM   3253  C  CG    . MET   A 1  413 ? 37.590  62.337  52.320  1.00 37.70  ? 413 MET   A CG    1 
ATOM   3254  S  SD    . MET   A 1  413 ? 36.044  63.224  52.646  1.00 42.02  ? 413 MET   A SD    1 
ATOM   3255  C  CE    . MET   A 1  413 ? 35.159  61.931  53.490  1.00 20.37  ? 413 MET   A CE    1 
ATOM   3256  N  N     . GLU   A 1  414 ? 39.529  59.406  51.915  1.00 42.38  ? 414 GLU   A N     1 
ATOM   3257  C  CA    . GLU   A 1  414 ? 39.503  58.022  52.359  1.00 43.31  ? 414 GLU   A CA    1 
ATOM   3258  C  C     . GLU   A 1  414 ? 38.285  57.736  53.217  1.00 36.41  ? 414 GLU   A C     1 
ATOM   3259  O  O     . GLU   A 1  414 ? 37.936  58.516  54.100  1.00 33.75  ? 414 GLU   A O     1 
ATOM   3260  C  CB    . GLU   A 1  414 ? 40.763  57.699  53.150  1.00 41.95  ? 414 GLU   A CB    1 
ATOM   3261  C  CG    . GLU   A 1  414 ? 41.982  58.354  52.569  1.00 53.29  ? 414 GLU   A CG    1 
ATOM   3262  C  CD    . GLU   A 1  414 ? 43.219  57.895  53.263  1.00 57.59  ? 414 GLU   A CD    1 
ATOM   3263  O  OE1   . GLU   A 1  414 ? 43.483  56.671  53.232  1.00 65.30  ? 414 GLU   A OE1   1 
ATOM   3264  O  OE2   . GLU   A 1  414 ? 43.898  58.750  53.863  1.00 51.56  ? 414 GLU   A OE2   1 
ATOM   3265  N  N     . GLU   A 1  415 ? 37.665  56.588  52.975  1.00 40.63  ? 415 GLU   A N     1 
ATOM   3266  C  CA    . GLU   A 1  415 ? 36.572  56.129  53.820  1.00 42.89  ? 415 GLU   A CA    1 
ATOM   3267  C  C     . GLU   A 1  415 ? 36.823  56.459  55.286  1.00 52.70  ? 415 GLU   A C     1 
ATOM   3268  O  O     . GLU   A 1  415 ? 35.888  56.817  56.012  1.00 58.71  ? 415 GLU   A O     1 
ATOM   3269  C  CB    . GLU   A 1  415 ? 36.376  54.625  53.649  1.00 46.96  ? 415 GLU   A CB    1 
ATOM   3270  C  CG    . GLU   A 1  415 ? 35.292  53.994  54.513  1.00 43.15  ? 415 GLU   A CG    1 
ATOM   3271  C  CD    . GLU   A 1  415 ? 34.611  52.828  53.794  1.00 54.27  ? 415 GLU   A CD    1 
ATOM   3272  O  OE1   . GLU   A 1  415 ? 34.338  52.959  52.574  1.00 49.75  ? 415 GLU   A OE1   1 
ATOM   3273  O  OE2   . GLU   A 1  415 ? 34.366  51.777  54.435  1.00 59.10  ? 415 GLU   A OE2   1 
ATOM   3274  N  N     . GLY   A 1  416 ? 38.080  56.372  55.729  1.00 41.04  ? 416 GLY   A N     1 
ATOM   3275  C  CA    . GLY   A 1  416 ? 38.354  56.429  57.154  1.00 31.45  ? 416 GLY   A CA    1 
ATOM   3276  C  C     . GLY   A 1  416 ? 38.082  57.781  57.766  1.00 35.99  ? 416 GLY   A C     1 
ATOM   3277  O  O     . GLY   A 1  416 ? 37.679  57.869  58.926  1.00 39.70  ? 416 GLY   A O     1 
ATOM   3278  N  N     . GLU   A 1  417 ? 38.313  58.848  57.006  1.00 34.07  ? 417 GLU   A N     1 
ATOM   3279  C  CA    . GLU   A 1  417 ? 37.973  60.188  57.463  1.00 33.34  ? 417 GLU   A CA    1 
ATOM   3280  C  C     . GLU   A 1  417 ? 36.507  60.308  57.880  1.00 47.52  ? 417 GLU   A C     1 
ATOM   3281  O  O     . GLU   A 1  417 ? 36.158  61.186  58.680  1.00 50.54  ? 417 GLU   A O     1 
ATOM   3282  C  CB    . GLU   A 1  417 ? 38.290  61.198  56.359  1.00 34.26  ? 417 GLU   A CB    1 
ATOM   3283  C  CG    . GLU   A 1  417 ? 37.674  62.568  56.584  1.00 31.42  ? 417 GLU   A CG    1 
ATOM   3284  C  CD    . GLU   A 1  417 ? 38.313  63.629  55.714  1.00 42.08  ? 417 GLU   A CD    1 
ATOM   3285  O  OE1   . GLU   A 1  417 ? 39.097  63.255  54.793  1.00 37.60  ? 417 GLU   A OE1   1 
ATOM   3286  O  OE2   . GLU   A 1  417 ? 38.029  64.829  55.959  1.00 40.04  ? 417 GLU   A OE2   1 
ATOM   3287  N  N     . PHE   A 1  418 ? 35.626  59.463  57.337  1.00 49.03  ? 418 PHE   A N     1 
ATOM   3288  C  CA    . PHE   A 1  418 ? 34.247  59.453  57.817  1.00 39.63  ? 418 PHE   A CA    1 
ATOM   3289  C  C     . PHE   A 1  418 ? 34.196  59.034  59.283  1.00 38.20  ? 418 PHE   A C     1 
ATOM   3290  O  O     . PHE   A 1  418 ? 33.632  59.738  60.125  1.00 47.59  ? 418 PHE   A O     1 
ATOM   3291  C  CB    . PHE   A 1  418 ? 33.377  58.523  56.952  1.00 37.81  ? 418 PHE   A CB    1 
ATOM   3292  C  CG    . PHE   A 1  418 ? 32.759  59.187  55.729  1.00 36.76  ? 418 PHE   A CG    1 
ATOM   3293  C  CD1   . PHE   A 1  418 ? 33.436  59.229  54.518  1.00 44.74  ? 418 PHE   A CD1   1 
ATOM   3294  C  CD2   . PHE   A 1  418 ? 31.481  59.724  55.781  1.00 36.95  ? 418 PHE   A CD2   1 
ATOM   3295  C  CE1   . PHE   A 1  418 ? 32.860  59.819  53.391  1.00 41.53  ? 418 PHE   A CE1   1 
ATOM   3296  C  CE2   . PHE   A 1  418 ? 30.900  60.317  54.663  1.00 31.18  ? 418 PHE   A CE2   1 
ATOM   3297  C  CZ    . PHE   A 1  418 ? 31.590  60.365  53.466  1.00 37.44  ? 418 PHE   A CZ    1 
ATOM   3298  N  N     . SER   A 1  419 ? 34.787  57.891  59.618  1.00 36.40  ? 419 SER   A N     1 
ATOM   3299  C  CA    . SER   A 1  419 ? 34.708  57.439  61.003  1.00 39.58  ? 419 SER   A CA    1 
ATOM   3300  C  C     . SER   A 1  419 ? 35.503  58.354  61.938  1.00 42.74  ? 419 SER   A C     1 
ATOM   3301  O  O     . SER   A 1  419 ? 35.153  58.501  63.114  1.00 43.42  ? 419 SER   A O     1 
ATOM   3302  C  CB    . SER   A 1  419 ? 35.179  55.985  61.102  1.00 37.94  ? 419 SER   A CB    1 
ATOM   3303  O  OG    . SER   A 1  419 ? 36.362  55.788  60.344  1.00 37.45  ? 419 SER   A OG    1 
ATOM   3304  N  N     . GLU   A 1  420 ? 36.565  58.984  61.440  1.00 36.99  ? 420 GLU   A N     1 
ATOM   3305  C  CA    A GLU   A 1  420 ? 37.288  59.957  62.251  0.51 41.12  ? 420 GLU   A CA    1 
ATOM   3306  C  CA    B GLU   A 1  420 ? 37.287  59.958  62.250  0.49 41.12  ? 420 GLU   A CA    1 
ATOM   3307  C  C     . GLU   A 1  420 ? 36.375  61.115  62.647  1.00 46.42  ? 420 GLU   A C     1 
ATOM   3308  O  O     . GLU   A 1  420 ? 36.245  61.444  63.832  1.00 48.54  ? 420 GLU   A O     1 
ATOM   3309  C  CB    A GLU   A 1  420 ? 38.526  60.440  61.484  0.51 39.25  ? 420 GLU   A CB    1 
ATOM   3310  C  CB    B GLU   A 1  420 ? 38.514  60.464  61.488  0.49 39.26  ? 420 GLU   A CB    1 
ATOM   3311  C  CG    A GLU   A 1  420 ? 39.211  61.700  62.010  0.51 43.11  ? 420 GLU   A CG    1 
ATOM   3312  C  CG    B GLU   A 1  420 ? 39.833  60.173  62.168  0.49 37.28  ? 420 GLU   A CG    1 
ATOM   3313  C  CD    A GLU   A 1  420 ? 40.519  61.979  61.277  0.51 38.99  ? 420 GLU   A CD    1 
ATOM   3314  C  CD    B GLU   A 1  420 ? 40.750  59.322  61.323  0.49 38.96  ? 420 GLU   A CD    1 
ATOM   3315  O  OE1   A GLU   A 1  420 ? 41.255  61.002  61.039  0.51 39.67  ? 420 GLU   A OE1   1 
ATOM   3316  O  OE1   B GLU   A 1  420 ? 40.962  59.672  60.137  0.49 35.27  ? 420 GLU   A OE1   1 
ATOM   3317  O  OE2   A GLU   A 1  420 ? 40.799  63.151  60.926  0.51 25.04  ? 420 GLU   A OE2   1 
ATOM   3318  O  OE2   B GLU   A 1  420 ? 41.251  58.299  61.846  0.49 40.55  ? 420 GLU   A OE2   1 
ATOM   3319  N  N     . ALA   A 1  421 ? 35.715  61.733  61.664  1.00 39.54  ? 421 ALA   A N     1 
ATOM   3320  C  CA    . ALA   A 1  421 ? 34.780  62.814  61.948  1.00 41.73  ? 421 ALA   A CA    1 
ATOM   3321  C  C     . ALA   A 1  421 ? 33.676  62.363  62.905  1.00 41.79  ? 421 ALA   A C     1 
ATOM   3322  O  O     . ALA   A 1  421 ? 33.346  63.068  63.867  1.00 28.16  ? 421 ALA   A O     1 
ATOM   3323  C  CB    . ALA   A 1  421 ? 34.187  63.334  60.637  1.00 42.96  ? 421 ALA   A CB    1 
ATOM   3324  N  N     . ARG   A 1  422 ? 33.073  61.196  62.648  1.00 35.57  ? 422 ARG   A N     1 
ATOM   3325  C  CA    . ARG   A 1  422 ? 31.989  60.744  63.519  1.00 39.02  ? 422 ARG   A CA    1 
ATOM   3326  C  C     . ARG   A 1  422 ? 32.503  60.430  64.924  1.00 46.78  ? 422 ARG   A C     1 
ATOM   3327  O  O     . ARG   A 1  422 ? 31.788  60.649  65.915  1.00 39.85  ? 422 ARG   A O     1 
ATOM   3328  C  CB    . ARG   A 1  422 ? 31.283  59.526  62.900  1.00 33.36  ? 422 ARG   A CB    1 
ATOM   3329  C  CG    . ARG   A 1  422 ? 30.152  58.922  63.731  1.00 18.56  ? 422 ARG   A CG    1 
ATOM   3330  C  CD    . ARG   A 1  422 ? 28.960  59.885  63.917  1.00 27.82  ? 422 ARG   A CD    1 
ATOM   3331  N  NE    . ARG   A 1  422 ? 27.893  59.255  64.695  1.00 35.42  ? 422 ARG   A NE    1 
ATOM   3332  C  CZ    . ARG   A 1  422 ? 27.818  59.263  66.024  1.00 39.14  ? 422 ARG   A CZ    1 
ATOM   3333  N  NH1   . ARG   A 1  422 ? 28.667  59.959  66.765  1.00 35.13  ? 422 ARG   A NH1   1 
ATOM   3334  N  NH2   . ARG   A 1  422 ? 26.872  58.550  66.628  1.00 28.18  ? 422 ARG   A NH2   1 
ATOM   3335  N  N     . GLU   A 1  423 ? 33.748  59.950  65.027  1.00 46.97  ? 423 GLU   A N     1 
ATOM   3336  C  CA    . GLU   A 1  423 ? 34.336  59.658  66.330  1.00 43.67  ? 423 GLU   A CA    1 
ATOM   3337  C  C     . GLU   A 1  423 ? 34.505  60.929  67.157  1.00 41.99  ? 423 GLU   A C     1 
ATOM   3338  O  O     . GLU   A 1  423 ? 34.232  60.940  68.364  1.00 42.92  ? 423 GLU   A O     1 
ATOM   3339  C  CB    . GLU   A 1  423 ? 35.671  58.940  66.141  1.00 42.92  ? 423 GLU   A CB    1 
ATOM   3340  C  CG    . GLU   A 1  423 ? 36.081  58.119  67.349  1.00 67.31  ? 423 GLU   A CG    1 
ATOM   3341  C  CD    . GLU   A 1  423 ? 34.889  57.463  68.030  1.00 77.72  ? 423 GLU   A CD    1 
ATOM   3342  O  OE1   . GLU   A 1  423 ? 34.373  56.467  67.469  1.00 82.79  ? 423 GLU   A OE1   1 
ATOM   3343  O  OE2   . GLU   A 1  423 ? 34.461  57.957  69.110  1.00 65.83  ? 423 GLU   A OE2   1 
ATOM   3344  N  N     . ASP   A 1  424 ? 34.963  62.003  66.519  1.00 34.79  ? 424 ASP   A N     1 
ATOM   3345  C  CA    . ASP   A 1  424 ? 34.978  63.327  67.133  1.00 34.48  ? 424 ASP   A CA    1 
ATOM   3346  C  C     . ASP   A 1  424 ? 33.599  63.712  67.681  1.00 44.88  ? 424 ASP   A C     1 
ATOM   3347  O  O     . ASP   A 1  424 ? 33.459  64.085  68.855  1.00 36.72  ? 424 ASP   A O     1 
ATOM   3348  C  CB    . ASP   A 1  424 ? 35.446  64.335  66.084  1.00 33.70  ? 424 ASP   A CB    1 
ATOM   3349  C  CG    . ASP   A 1  424 ? 36.039  65.560  66.681  1.00 41.30  ? 424 ASP   A CG    1 
ATOM   3350  O  OD1   . ASP   A 1  424 ? 36.032  65.645  67.925  1.00 40.99  ? 424 ASP   A OD1   1 
ATOM   3351  O  OD2   . ASP   A 1  424 ? 36.529  66.427  65.906  1.00 45.68  ? 424 ASP   A OD2   1 
ATOM   3352  N  N     . MET   A 1  425 ? 32.567  63.634  66.828  1.00 40.43  ? 425 MET   A N     1 
ATOM   3353  C  CA    . MET   A 1  425 ? 31.216  63.982  67.245  1.00 30.43  ? 425 MET   A CA    1 
ATOM   3354  C  C     . MET   A 1  425 ? 30.753  63.113  68.393  1.00 34.11  ? 425 MET   A C     1 
ATOM   3355  O  O     . MET   A 1  425 ? 29.937  63.547  69.212  1.00 39.49  ? 425 MET   A O     1 
ATOM   3356  C  CB    . MET   A 1  425 ? 30.239  63.840  66.077  1.00 33.60  ? 425 MET   A CB    1 
ATOM   3357  C  CG    . MET   A 1  425 ? 30.557  64.683  64.883  1.00 29.81  ? 425 MET   A CG    1 
ATOM   3358  S  SD    . MET   A 1  425 ? 30.484  66.423  65.280  1.00 39.07  ? 425 MET   A SD    1 
ATOM   3359  C  CE    . MET   A 1  425 ? 28.856  66.466  66.032  1.00 36.42  ? 425 MET   A CE    1 
ATOM   3360  N  N     . ALA   A 1  426 ? 31.219  61.872  68.458  1.00 40.52  ? 426 ALA   A N     1 
ATOM   3361  C  CA    . ALA   A 1  426 ? 30.844  61.050  69.601  1.00 40.32  ? 426 ALA   A CA    1 
ATOM   3362  C  C     . ALA   A 1  426 ? 31.501  61.576  70.868  1.00 45.57  ? 426 ALA   A C     1 
ATOM   3363  O  O     . ALA   A 1  426 ? 30.853  61.661  71.917  1.00 52.22  ? 426 ALA   A O     1 
ATOM   3364  C  CB    . ALA   A 1  426 ? 31.210  59.592  69.352  1.00 28.55  ? 426 ALA   A CB    1 
ATOM   3365  N  N     . ALA   A 1  427 ? 32.783  61.949  70.786  1.00 41.48  ? 427 ALA   A N     1 
ATOM   3366  C  CA    . ALA   A 1  427 ? 33.434  62.637  71.897  1.00 46.50  ? 427 ALA   A CA    1 
ATOM   3367  C  C     . ALA   A 1  427 ? 32.681  63.916  72.265  1.00 45.58  ? 427 ALA   A C     1 
ATOM   3368  O  O     . ALA   A 1  427 ? 32.307  64.119  73.426  1.00 40.96  ? 427 ALA   A O     1 
ATOM   3369  C  CB    . ALA   A 1  427 ? 34.893  62.941  71.544  1.00 26.08  ? 427 ALA   A CB    1 
ATOM   3370  N  N     . LEU   A 1  428 ? 32.437  64.779  71.278  1.00 36.17  ? 428 LEU   A N     1 
ATOM   3371  C  CA    . LEU   A 1  428 ? 31.697  66.017  71.500  1.00 33.08  ? 428 LEU   A CA    1 
ATOM   3372  C  C     . LEU   A 1  428 ? 30.370  65.787  72.211  1.00 37.26  ? 428 LEU   A C     1 
ATOM   3373  O  O     . LEU   A 1  428 ? 29.939  66.622  73.009  1.00 42.16  ? 428 LEU   A O     1 
ATOM   3374  C  CB    . LEU   A 1  428 ? 31.442  66.720  70.161  1.00 29.91  ? 428 LEU   A CB    1 
ATOM   3375  C  CG    . LEU   A 1  428 ? 30.863  68.108  70.377  1.00 33.59  ? 428 LEU   A CG    1 
ATOM   3376  C  CD1   . LEU   A 1  428 ? 31.971  69.138  70.510  1.00 31.69  ? 428 LEU   A CD1   1 
ATOM   3377  C  CD2   . LEU   A 1  428 ? 29.877  68.471  69.287  1.00 37.72  ? 428 LEU   A CD2   1 
ATOM   3378  N  N     . GLU   A 1  429 ? 29.666  64.702  71.886  1.00 40.23  ? 429 GLU   A N     1 
ATOM   3379  C  CA    . GLU   A 1  429 ? 28.392  64.461  72.558  1.00 39.00  ? 429 GLU   A CA    1 
ATOM   3380  C  C     . GLU   A 1  429 ? 28.610  64.014  73.992  1.00 40.97  ? 429 GLU   A C     1 
ATOM   3381  O  O     . GLU   A 1  429 ? 27.746  64.237  74.848  1.00 45.77  ? 429 GLU   A O     1 
ATOM   3382  C  CB    . GLU   A 1  429 ? 27.553  63.430  71.797  1.00 28.68  ? 429 GLU   A CB    1 
ATOM   3383  C  CG    . GLU   A 1  429 ? 26.785  64.018  70.608  1.00 36.12  ? 429 GLU   A CG    1 
ATOM   3384  C  CD    . GLU   A 1  429 ? 25.789  63.035  69.986  1.00 44.17  ? 429 GLU   A CD    1 
ATOM   3385  O  OE1   . GLU   A 1  429 ? 24.745  62.748  70.620  1.00 41.06  ? 429 GLU   A OE1   1 
ATOM   3386  O  OE2   . GLU   A 1  429 ? 26.043  62.544  68.862  1.00 38.79  ? 429 GLU   A OE2   1 
ATOM   3387  N  N     . LYS   A 1  430 ? 29.752  63.387  74.272  1.00 39.46  ? 430 LYS   A N     1 
ATOM   3388  C  CA    . LYS   A 1  430 ? 30.062  62.963  75.632  1.00 51.76  ? 430 LYS   A CA    1 
ATOM   3389  C  C     . LYS   A 1  430 ? 30.472  64.160  76.483  1.00 50.46  ? 430 LYS   A C     1 
ATOM   3390  O  O     . LYS   A 1  430 ? 29.929  64.369  77.573  1.00 50.90  ? 430 LYS   A O     1 
ATOM   3391  C  CB    . LYS   A 1  430 ? 31.163  61.888  75.618  1.00 56.52  ? 430 LYS   A CB    1 
ATOM   3392  C  CG    . LYS   A 1  430 ? 30.913  60.738  74.625  1.00 66.51  ? 430 LYS   A CG    1 
ATOM   3393  C  CD    . LYS   A 1  430 ? 32.126  59.789  74.502  1.00 77.05  ? 430 LYS   A CD    1 
ATOM   3394  C  CE    . LYS   A 1  430 ? 32.166  59.024  73.152  1.00 57.84  ? 430 LYS   A CE    1 
ATOM   3395  N  NZ    . LYS   A 1  430 ? 33.473  59.226  72.419  1.00 35.88  ? 430 LYS   A NZ    1 
ATOM   3396  N  N     . ASP   A 1  431 ? 31.435  64.950  75.999  1.00 44.54  ? 431 ASP   A N     1 
ATOM   3397  C  CA    . ASP   A 1  431 ? 31.707  66.261  76.571  1.00 46.83  ? 431 ASP   A CA    1 
ATOM   3398  C  C     . ASP   A 1  431 ? 30.408  66.932  77.015  1.00 52.06  ? 431 ASP   A C     1 
ATOM   3399  O  O     . ASP   A 1  431 ? 30.229  67.271  78.195  1.00 49.08  ? 431 ASP   A O     1 
ATOM   3400  C  CB    . ASP   A 1  431 ? 32.433  67.147  75.547  1.00 35.22  ? 431 ASP   A CB    1 
ATOM   3401  C  CG    . ASP   A 1  431 ? 33.815  66.638  75.184  1.00 45.54  ? 431 ASP   A CG    1 
ATOM   3402  O  OD1   . ASP   A 1  431 ? 34.267  65.627  75.769  1.00 58.72  ? 431 ASP   A OD1   1 
ATOM   3403  O  OD2   . ASP   A 1  431 ? 34.451  67.258  74.295  1.00 54.55  ? 431 ASP   A OD2   1 
ATOM   3404  N  N     . TYR   A 1  432 ? 29.476  67.108  76.073  1.00 41.42  ? 432 TYR   A N     1 
ATOM   3405  C  CA    . TYR   A 1  432 ? 28.238  67.795  76.410  1.00 44.79  ? 432 TYR   A CA    1 
ATOM   3406  C  C     . TYR   A 1  432 ? 27.520  67.097  77.557  1.00 44.10  ? 432 TYR   A C     1 
ATOM   3407  O  O     . TYR   A 1  432 ? 27.033  67.762  78.478  1.00 49.16  ? 432 TYR   A O     1 
ATOM   3408  C  CB    . TYR   A 1  432 ? 27.330  67.920  75.186  1.00 43.97  ? 432 TYR   A CB    1 
ATOM   3409  C  CG    . TYR   A 1  432 ? 27.520  69.213  74.422  1.00 40.56  ? 432 TYR   A CG    1 
ATOM   3410  C  CD1   . TYR   A 1  432 ? 26.851  70.368  74.794  1.00 38.42  ? 432 TYR   A CD1   1 
ATOM   3411  C  CD2   . TYR   A 1  432 ? 28.362  69.277  73.320  1.00 41.69  ? 432 TYR   A CD2   1 
ATOM   3412  C  CE1   . TYR   A 1  432 ? 27.016  71.555  74.087  1.00 30.23  ? 432 TYR   A CE1   1 
ATOM   3413  C  CE2   . TYR   A 1  432 ? 28.535  70.463  72.614  1.00 39.96  ? 432 TYR   A CE2   1 
ATOM   3414  C  CZ    . TYR   A 1  432 ? 27.863  71.598  73.006  1.00 32.40  ? 432 TYR   A CZ    1 
ATOM   3415  O  OH    . TYR   A 1  432 ? 28.045  72.777  72.312  1.00 37.63  ? 432 TYR   A OH    1 
ATOM   3416  N  N     . GLU   A 1  433 ? 27.472  65.760  77.549  1.00 43.92  ? 433 GLU   A N     1 
ATOM   3417  C  CA    . GLU   A 1  433 ? 26.700  65.073  78.585  1.00 45.46  ? 433 GLU   A CA    1 
ATOM   3418  C  C     . GLU   A 1  433 ? 27.378  65.167  79.951  1.00 49.41  ? 433 GLU   A C     1 
ATOM   3419  O  O     . GLU   A 1  433 ? 26.707  65.398  80.964  1.00 43.83  ? 433 GLU   A O     1 
ATOM   3420  C  CB    . GLU   A 1  433 ? 26.449  63.622  78.203  1.00 42.73  ? 433 GLU   A CB    1 
ATOM   3421  C  CG    . GLU   A 1  433 ? 25.365  62.972  79.049  1.00 40.76  ? 433 GLU   A CG    1 
ATOM   3422  C  CD    . GLU   A 1  433 ? 24.709  61.799  78.351  1.00 66.53  ? 433 GLU   A CD    1 
ATOM   3423  O  OE1   . GLU   A 1  433 ? 25.444  60.881  77.921  1.00 71.42  ? 433 GLU   A OE1   1 
ATOM   3424  O  OE2   . GLU   A 1  433 ? 23.461  61.802  78.219  1.00 73.22  ? 433 GLU   A OE2   1 
ATOM   3425  N  N     . GLU   A 1  434 ? 28.703  65.007  80.002  1.00 47.30  ? 434 GLU   A N     1 
ATOM   3426  C  CA    . GLU   A 1  434 ? 29.426  65.224  81.250  1.00 54.81  ? 434 GLU   A CA    1 
ATOM   3427  C  C     . GLU   A 1  434 ? 29.030  66.551  81.896  1.00 57.16  ? 434 GLU   A C     1 
ATOM   3428  O  O     . GLU   A 1  434 ? 28.645  66.592  83.073  1.00 58.89  ? 434 GLU   A O     1 
ATOM   3429  C  CB    . GLU   A 1  434 ? 30.936  65.188  81.000  1.00 56.55  ? 434 GLU   A CB    1 
ATOM   3430  C  CG    . GLU   A 1  434 ? 31.540  63.799  80.827  1.00 67.21  ? 434 GLU   A CG    1 
ATOM   3431  C  CD    . GLU   A 1  434 ? 33.055  63.852  80.639  1.00 94.87  ? 434 GLU   A CD    1 
ATOM   3432  O  OE1   . GLU   A 1  434 ? 33.761  64.231  81.606  1.00 97.19  ? 434 GLU   A OE1   1 
ATOM   3433  O  OE2   . GLU   A 1  434 ? 33.535  63.538  79.520  1.00 88.72  ? 434 GLU   A OE2   1 
ATOM   3434  N  N     . VAL   A 1  435 ? 29.115  67.650  81.137  1.00 47.56  ? 435 VAL   A N     1 
ATOM   3435  C  CA    . VAL   A 1  435 ? 28.885  68.967  81.725  1.00 48.53  ? 435 VAL   A CA    1 
ATOM   3436  C  C     . VAL   A 1  435 ? 27.487  69.082  82.341  1.00 53.00  ? 435 VAL   A C     1 
ATOM   3437  O  O     . VAL   A 1  435 ? 27.326  69.729  83.385  1.00 59.93  ? 435 VAL   A O     1 
ATOM   3438  C  CB    . VAL   A 1  435 ? 29.161  70.073  80.679  1.00 48.07  ? 435 VAL   A CB    1 
ATOM   3439  C  CG1   . VAL   A 1  435 ? 28.770  71.418  81.219  1.00 42.38  ? 435 VAL   A CG1   1 
ATOM   3440  C  CG2   . VAL   A 1  435 ? 30.646  70.104  80.299  1.00 33.18  ? 435 VAL   A CG2   1 
ATOM   3441  N  N     . GLY   A 1  436 ? 26.471  68.437  81.752  1.00 49.39  ? 436 GLY   A N     1 
ATOM   3442  C  CA    . GLY   A 1  436 ? 25.099  68.540  82.246  1.00 48.53  ? 436 GLY   A CA    1 
ATOM   3443  C  C     . GLY   A 1  436 ? 24.492  67.307  82.906  1.00 62.93  ? 436 GLY   A C     1 
ATOM   3444  O  O     . GLY   A 1  436 ? 23.310  67.020  82.709  1.00 62.42  ? 436 GLY   A O     1 
ATOM   3445  N  N     . VAL   A 1  437 ? 25.269  66.613  83.747  1.00 83.63  ? 437 VAL   A N     1 
ATOM   3446  C  CA    . VAL   A 1  437 ? 24.932  65.258  84.201  1.00 88.61  ? 437 VAL   A CA    1 
ATOM   3447  C  C     . VAL   A 1  437 ? 23.941  65.234  85.368  1.00 104.01 ? 437 VAL   A C     1 
ATOM   3448  O  O     . VAL   A 1  437 ? 23.164  64.279  85.494  1.00 102.22 ? 437 VAL   A O     1 
ATOM   3449  C  CB    . VAL   A 1  437 ? 26.216  64.493  84.586  1.00 79.84  ? 437 VAL   A CB    1 
ATOM   3450  C  CG1   . VAL   A 1  437 ? 27.237  65.426  85.233  1.00 66.43  ? 437 VAL   A CG1   1 
ATOM   3451  C  CG2   . VAL   A 1  437 ? 25.879  63.343  85.539  1.00 84.95  ? 437 VAL   A CG2   1 
ATOM   3452  N  N     . ASP   A 1  438 ? 23.971  66.246  86.243  1.00 111.69 ? 438 ASP   A N     1 
ATOM   3453  C  CA    . ASP   A 1  438 ? 23.249  66.284  87.519  1.00 110.97 ? 438 ASP   A CA    1 
ATOM   3454  C  C     . ASP   A 1  438 ? 21.923  65.523  87.520  1.00 116.51 ? 438 ASP   A C     1 
ATOM   3455  O  O     . ASP   A 1  438 ? 21.918  64.287  87.515  1.00 119.19 ? 438 ASP   A O     1 
ATOM   3456  C  CB    . ASP   A 1  438 ? 23.009  67.742  87.931  1.00 115.56 ? 438 ASP   A CB    1 
ATOM   3457  C  CG    . ASP   A 1  438 ? 24.299  68.551  87.997  1.00 125.11 ? 438 ASP   A CG    1 
ATOM   3458  O  OD1   . ASP   A 1  438 ? 25.290  68.036  88.566  1.00 116.17 ? 438 ASP   A OD1   1 
ATOM   3459  O  OD2   . ASP   A 1  438 ? 24.322  69.691  87.467  1.00 114.70 ? 438 ASP   A OD2   1 
ATOM   3460  N  N     . SER   A 1  439 ? 20.797  66.241  87.564  1.00 115.27 ? 439 SER   A N     1 
ATOM   3461  C  CA    . SER   A 1  439 ? 19.476  65.597  87.572  1.00 118.58 ? 439 SER   A CA    1 
ATOM   3462  C  C     . SER   A 1  439 ? 19.247  64.754  86.316  1.00 116.41 ? 439 SER   A C     1 
ATOM   3463  O  O     . SER   A 1  439 ? 19.491  63.546  86.307  1.00 111.77 ? 439 SER   A O     1 
ATOM   3464  C  CB    . SER   A 1  439 ? 18.357  66.637  87.700  1.00 99.14  ? 439 SER   A CB    1 
ATOM   3465  O  OG    . SER   A 1  439 ? 17.119  66.110  87.240  1.00 71.33  ? 439 SER   A OG    1 
ATOM   3466  N  N     . MET   B 1  1   ? 20.549  50.992  -1.499  1.00 66.46  ? 1   MET   C N     1 
ATOM   3467  C  CA    . MET   B 1  1   ? 21.025  49.925  -2.372  1.00 55.58  ? 1   MET   C CA    1 
ATOM   3468  C  C     . MET   B 1  1   ? 20.209  48.650  -2.184  1.00 60.10  ? 1   MET   C C     1 
ATOM   3469  O  O     . MET   B 1  1   ? 19.085  48.541  -2.674  1.00 66.76  ? 1   MET   C O     1 
ATOM   3470  C  CB    . MET   B 1  1   ? 22.503  49.654  -2.109  1.00 53.74  ? 1   MET   C CB    1 
ATOM   3471  C  CG    . MET   B 1  1   ? 22.938  49.887  -0.663  1.00 59.30  ? 1   MET   C CG    1 
ATOM   3472  S  SD    . MET   B 1  1   ? 24.023  51.326  -0.481  1.00 70.89  ? 1   MET   C SD    1 
ATOM   3473  C  CE    . MET   B 1  1   ? 22.991  52.611  -1.196  1.00 68.69  ? 1   MET   C CE    1 
ATOM   3474  N  N     . ARG   B 1  2   ? 20.788  47.671  -1.489  1.00 66.62  ? 2   ARG   C N     1 
ATOM   3475  C  CA    . ARG   B 1  2   ? 20.089  46.444  -1.134  1.00 55.99  ? 2   ARG   C CA    1 
ATOM   3476  C  C     . ARG   B 1  2   ? 19.756  45.584  -2.348  1.00 43.45  ? 2   ARG   C C     1 
ATOM   3477  O  O     . ARG   B 1  2   ? 18.792  44.829  -2.318  1.00 53.18  ? 2   ARG   C O     1 
ATOM   3478  C  CB    . ARG   B 1  2   ? 18.803  46.748  -0.368  1.00 56.23  ? 2   ARG   C CB    1 
ATOM   3479  C  CG    . ARG   B 1  2   ? 18.874  47.929  0.562   1.00 71.12  ? 2   ARG   C CG    1 
ATOM   3480  C  CD    . ARG   B 1  2   ? 17.558  48.708  0.487   1.00 82.39  ? 2   ARG   C CD    1 
ATOM   3481  N  NE    . ARG   B 1  2   ? 17.243  49.093  -0.887  1.00 86.86  ? 2   ARG   C NE    1 
ATOM   3482  C  CZ    . ARG   B 1  2   ? 17.501  50.283  -1.417  1.00 78.66  ? 2   ARG   C CZ    1 
ATOM   3483  N  NH1   . ARG   B 1  2   ? 18.031  51.259  -0.693  1.00 60.53  ? 2   ARG   C NH1   1 
ATOM   3484  N  NH2   . ARG   B 1  2   ? 17.238  50.490  -2.710  1.00 65.28  ? 2   ARG   C NH2   1 
ATOM   3485  N  N     . GLU   B 1  3   ? 20.532  45.670  -3.421  1.00 37.39  ? 3   GLU   C N     1 
ATOM   3486  C  CA    . GLU   B 1  3   ? 20.252  44.862  -4.604  1.00 38.20  ? 3   GLU   C CA    1 
ATOM   3487  C  C     . GLU   B 1  3   ? 20.369  43.364  -4.311  1.00 38.69  ? 3   GLU   C C     1 
ATOM   3488  O  O     . GLU   B 1  3   ? 21.326  42.916  -3.675  1.00 43.51  ? 3   GLU   C O     1 
ATOM   3489  C  CB    . GLU   B 1  3   ? 21.218  45.222  -5.745  1.00 40.92  ? 3   GLU   C CB    1 
ATOM   3490  C  CG    . GLU   B 1  3   ? 21.123  46.654  -6.294  1.00 33.91  ? 3   GLU   C CG    1 
ATOM   3491  C  CD    . GLU   B 1  3   ? 22.141  47.595  -5.671  1.00 37.42  ? 3   GLU   C CD    1 
ATOM   3492  O  OE1   . GLU   B 1  3   ? 22.711  47.271  -4.600  1.00 35.50  ? 3   GLU   C OE1   1 
ATOM   3493  O  OE2   . GLU   B 1  3   ? 22.380  48.663  -6.265  1.00 45.08  ? 3   GLU   C OE2   1 
ATOM   3494  N  N     . CYS   B 1  4   ? 19.395  42.590  -4.807  1.00 31.34  ? 4   CYS   C N     1 
ATOM   3495  C  CA    A CYS   B 1  4   ? 19.456  41.134  -4.824  0.38 31.60  ? 4   CYS   C CA    1 
ATOM   3496  C  CA    B CYS   B 1  4   ? 19.436  41.134  -4.827  0.62 31.66  ? 4   CYS   C CA    1 
ATOM   3497  C  C     . CYS   B 1  4   ? 19.636  40.651  -6.258  1.00 29.02  ? 4   CYS   C C     1 
ATOM   3498  O  O     . CYS   B 1  4   ? 19.011  41.173  -7.178  1.00 38.06  ? 4   CYS   C O     1 
ATOM   3499  C  CB    A CYS   B 1  4   ? 18.186  40.518  -4.219  0.38 36.56  ? 4   CYS   C CB    1 
ATOM   3500  C  CB    B CYS   B 1  4   ? 18.133  40.544  -4.276  0.62 36.61  ? 4   CYS   C CB    1 
ATOM   3501  S  SG    A CYS   B 1  4   ? 18.092  38.684  -4.251  0.38 34.21  ? 4   CYS   C SG    1 
ATOM   3502  S  SG    B CYS   B 1  4   ? 17.831  40.759  -2.506  0.62 34.45  ? 4   CYS   C SG    1 
ATOM   3503  N  N     . ILE   B 1  5   ? 20.494  39.647  -6.451  1.00 27.14  ? 5   ILE   C N     1 
ATOM   3504  C  CA    . ILE   B 1  5   ? 20.731  39.049  -7.767  1.00 29.12  ? 5   ILE   C CA    1 
ATOM   3505  C  C     . ILE   B 1  5   ? 20.190  37.623  -7.766  1.00 34.19  ? 5   ILE   C C     1 
ATOM   3506  O  O     . ILE   B 1  5   ? 20.553  36.810  -6.903  1.00 29.90  ? 5   ILE   C O     1 
ATOM   3507  C  CB    . ILE   B 1  5   ? 22.223  39.035  -8.160  1.00 25.95  ? 5   ILE   C CB    1 
ATOM   3508  C  CG1   . ILE   B 1  5   ? 22.765  40.436  -8.375  1.00 28.49  ? 5   ILE   C CG1   1 
ATOM   3509  C  CG2   . ILE   B 1  5   ? 22.422  38.235  -9.443  1.00 20.87  ? 5   ILE   C CG2   1 
ATOM   3510  C  CD1   . ILE   B 1  5   ? 24.294  40.474  -8.518  1.00 29.55  ? 5   ILE   C CD1   1 
ATOM   3511  N  N     . SER   B 1  6   ? 19.356  37.308  -8.753  1.00 27.75  ? 6   SER   C N     1 
ATOM   3512  C  CA    . SER   B 1  6   ? 18.782  35.977  -8.884  1.00 29.54  ? 6   SER   C CA    1 
ATOM   3513  C  C     . SER   B 1  6   ? 19.531  35.185  -9.944  1.00 34.81  ? 6   SER   C C     1 
ATOM   3514  O  O     . SER   B 1  6   ? 19.839  35.700  -11.024 1.00 36.40  ? 6   SER   C O     1 
ATOM   3515  C  CB    . SER   B 1  6   ? 17.299  36.036  -9.241  1.00 28.58  ? 6   SER   C CB    1 
ATOM   3516  O  OG    . SER   B 1  6   ? 16.572  36.661  -8.209  1.00 26.70  ? 6   SER   C OG    1 
ATOM   3517  N  N     . ILE   B 1  7   ? 19.832  33.932  -9.614  1.00 27.46  ? 7   ILE   C N     1 
ATOM   3518  C  CA    . ILE   B 1  7   ? 20.514  33.012  -10.506 1.00 24.05  ? 7   ILE   C CA    1 
ATOM   3519  C  C     . ILE   B 1  7   ? 19.592  31.826  -10.699 1.00 28.70  ? 7   ILE   C C     1 
ATOM   3520  O  O     . ILE   B 1  7   ? 19.142  31.227  -9.716  1.00 34.77  ? 7   ILE   C O     1 
ATOM   3521  C  CB    . ILE   B 1  7   ? 21.864  32.572  -9.942  1.00 25.78  ? 7   ILE   C CB    1 
ATOM   3522  C  CG1   . ILE   B 1  7   ? 22.581  33.777  -9.299  1.00 21.30  ? 7   ILE   C CG1   1 
ATOM   3523  C  CG2   . ILE   B 1  7   ? 22.659  31.903  -11.032 1.00 22.97  ? 7   ILE   C CG2   1 
ATOM   3524  C  CD1   . ILE   B 1  7   ? 24.082  33.580  -9.112  1.00 25.19  ? 7   ILE   C CD1   1 
ATOM   3525  N  N     . HIS   B 1  8   ? 19.280  31.518  -11.957 1.00 22.95  ? 8   HIS   C N     1 
ATOM   3526  C  CA    . HIS   B 1  8   ? 18.351  30.458  -12.335 1.00 28.90  ? 8   HIS   C CA    1 
ATOM   3527  C  C     . HIS   B 1  8   ? 19.126  29.372  -13.086 1.00 29.86  ? 8   HIS   C C     1 
ATOM   3528  O  O     . HIS   B 1  8   ? 19.691  29.627  -14.156 1.00 29.08  ? 8   HIS   C O     1 
ATOM   3529  C  CB    . HIS   B 1  8   ? 17.206  31.024  -13.187 1.00 29.61  ? 8   HIS   C CB    1 
ATOM   3530  C  CG    . HIS   B 1  8   ? 16.400  32.090  -12.499 1.00 34.64  ? 8   HIS   C CG    1 
ATOM   3531  N  ND1   . HIS   B 1  8   ? 15.345  31.806  -11.655 1.00 29.00  ? 8   HIS   C ND1   1 
ATOM   3532  C  CD2   . HIS   B 1  8   ? 16.491  33.442  -12.540 1.00 35.54  ? 8   HIS   C CD2   1 
ATOM   3533  C  CE1   . HIS   B 1  8   ? 14.826  32.934  -11.203 1.00 30.55  ? 8   HIS   C CE1   1 
ATOM   3534  N  NE2   . HIS   B 1  8   ? 15.502  33.942  -11.728 1.00 38.19  ? 8   HIS   C NE2   1 
ATOM   3535  N  N     . VAL   B 1  9   ? 19.137  28.162  -12.534 1.00 24.44  ? 9   VAL   C N     1 
ATOM   3536  C  CA    . VAL   B 1  9   ? 20.041  27.095  -12.952 1.00 30.45  ? 9   VAL   C CA    1 
ATOM   3537  C  C     . VAL   B 1  9   ? 19.226  25.887  -13.409 1.00 31.54  ? 9   VAL   C C     1 
ATOM   3538  O  O     . VAL   B 1  9   ? 18.337  25.426  -12.685 1.00 34.88  ? 9   VAL   C O     1 
ATOM   3539  C  CB    . VAL   B 1  9   ? 20.992  26.712  -11.808 1.00 28.10  ? 9   VAL   C CB    1 
ATOM   3540  C  CG1   . VAL   B 1  9   ? 21.796  25.470  -12.164 1.00 26.42  ? 9   VAL   C CG1   1 
ATOM   3541  C  CG2   . VAL   B 1  9   ? 21.888  27.891  -11.476 1.00 25.97  ? 9   VAL   C CG2   1 
ATOM   3542  N  N     . GLY   B 1  10  ? 19.542  25.368  -14.603 1.00 29.75  ? 10  GLY   C N     1 
ATOM   3543  C  CA    . GLY   B 1  10  ? 18.796  24.283  -15.218 1.00 24.18  ? 10  GLY   C CA    1 
ATOM   3544  C  C     . GLY   B 1  10  ? 17.329  24.548  -15.543 1.00 29.29  ? 10  GLY   C C     1 
ATOM   3545  O  O     . GLY   B 1  10  ? 16.791  25.625  -15.263 1.00 33.75  ? 10  GLY   C O     1 
ATOM   3546  N  N     . GLN   B 1  11  ? 16.652  23.536  -16.093 1.00 21.93  ? 11  GLN   C N     1 
ATOM   3547  C  CA    . GLN   B 1  11  ? 15.282  23.704  -16.560 1.00 23.72  ? 11  GLN   C CA    1 
ATOM   3548  C  C     . GLN   B 1  11  ? 14.374  24.267  -15.462 1.00 29.65  ? 11  GLN   C C     1 
ATOM   3549  O  O     . GLN   B 1  11  ? 13.727  25.305  -15.647 1.00 27.48  ? 11  GLN   C O     1 
ATOM   3550  C  CB    . GLN   B 1  11  ? 14.754  22.370  -17.091 1.00 17.21  ? 11  GLN   C CB    1 
ATOM   3551  C  CG    . GLN   B 1  11  ? 13.301  22.424  -17.594 1.00 26.02  ? 11  GLN   C CG    1 
ATOM   3552  C  CD    . GLN   B 1  11  ? 12.820  21.096  -18.211 1.00 29.17  ? 11  GLN   C CD    1 
ATOM   3553  O  OE1   . GLN   B 1  11  ? 13.388  20.630  -19.190 1.00 28.20  ? 11  GLN   C OE1   1 
ATOM   3554  N  NE2   . GLN   B 1  11  ? 11.759  20.497  -17.643 1.00 21.81  ? 11  GLN   C NE2   1 
ATOM   3555  N  N     . ALA   B 1  12  ? 14.310  23.590  -14.309 1.00 24.88  ? 12  ALA   C N     1 
ATOM   3556  C  CA    . ALA   B 1  12  ? 13.392  24.012  -13.255 1.00 17.84  ? 12  ALA   C CA    1 
ATOM   3557  C  C     . ALA   B 1  12  ? 13.701  25.425  -12.792 1.00 25.91  ? 12  ALA   C C     1 
ATOM   3558  O  O     . ALA   B 1  12  ? 12.796  26.264  -12.676 1.00 29.63  ? 12  ALA   C O     1 
ATOM   3559  C  CB    . ALA   B 1  12  ? 13.439  23.045  -12.075 1.00 18.37  ? 12  ALA   C CB    1 
ATOM   3560  N  N     . GLY   B 1  13  ? 14.977  25.707  -12.507 1.00 18.60  ? 13  GLY   C N     1 
ATOM   3561  C  CA    . GLY   B 1  13  ? 15.348  27.067  -12.160 1.00 27.48  ? 13  GLY   C CA    1 
ATOM   3562  C  C     . GLY   B 1  13  ? 14.966  28.071  -13.233 1.00 26.04  ? 13  GLY   C C     1 
ATOM   3563  O  O     . GLY   B 1  13  ? 14.415  29.128  -12.934 1.00 32.42  ? 13  GLY   C O     1 
ATOM   3564  N  N     . VAL   B 1  14  ? 15.221  27.742  -14.495 1.00 23.87  ? 14  VAL   C N     1 
ATOM   3565  C  CA    . VAL   B 1  14  ? 14.897  28.665  -15.576 1.00 28.44  ? 14  VAL   C CA    1 
ATOM   3566  C  C     . VAL   B 1  14  ? 13.389  28.862  -15.692 1.00 27.13  ? 14  VAL   C C     1 
ATOM   3567  O  O     . VAL   B 1  14  ? 12.909  29.991  -15.813 1.00 28.86  ? 14  VAL   C O     1 
ATOM   3568  C  CB    . VAL   B 1  14  ? 15.499  28.184  -16.910 1.00 22.76  ? 14  VAL   C CB    1 
ATOM   3569  C  CG1   . VAL   B 1  14  ? 15.071  29.098  -17.983 1.00 23.38  ? 14  VAL   C CG1   1 
ATOM   3570  C  CG2   . VAL   B 1  14  ? 17.011  28.173  -16.844 1.00 25.73  ? 14  VAL   C CG2   1 
ATOM   3571  N  N     . GLN   B 1  15  ? 12.616  27.774  -15.691 1.00 27.14  ? 15  GLN   C N     1 
ATOM   3572  C  CA    . GLN   B 1  15  ? 11.182  27.917  -15.932 1.00 31.45  ? 15  GLN   C CA    1 
ATOM   3573  C  C     . GLN   B 1  15  ? 10.492  28.608  -14.758 1.00 36.15  ? 15  GLN   C C     1 
ATOM   3574  O  O     . GLN   B 1  15  ? 9.758   29.589  -14.947 1.00 36.88  ? 15  GLN   C O     1 
ATOM   3575  C  CB    . GLN   B 1  15  ? 10.551  26.562  -16.234 1.00 28.76  ? 15  GLN   C CB    1 
ATOM   3576  C  CG    . GLN   B 1  15  ? 11.325  25.806  -17.281 1.00 26.63  ? 15  GLN   C CG    1 
ATOM   3577  C  CD    . GLN   B 1  15  ? 10.477  24.872  -18.132 1.00 34.69  ? 15  GLN   C CD    1 
ATOM   3578  O  OE1   . GLN   B 1  15  ? 10.317  25.106  -19.335 1.00 36.00  ? 15  GLN   C OE1   1 
ATOM   3579  N  NE2   . GLN   B 1  15  ? 9.970   23.784  -17.529 1.00 22.48  ? 15  GLN   C NE2   1 
ATOM   3580  N  N     . ILE   B 1  16  ? 10.745  28.150  -13.532 1.00 30.73  ? 16  ILE   C N     1 
ATOM   3581  C  CA    . ILE   B 1  16  ? 10.308  28.936  -12.378 1.00 34.19  ? 16  ILE   C CA    1 
ATOM   3582  C  C     . ILE   B 1  16  ? 10.765  30.391  -12.523 1.00 36.53  ? 16  ILE   C C     1 
ATOM   3583  O  O     . ILE   B 1  16  ? 9.992   31.332  -12.305 1.00 30.01  ? 16  ILE   C O     1 
ATOM   3584  C  CB    . ILE   B 1  16  ? 10.811  28.285  -11.077 1.00 32.58  ? 16  ILE   C CB    1 
ATOM   3585  C  CG1   . ILE   B 1  16  ? 10.120  26.930  -10.890 1.00 28.16  ? 16  ILE   C CG1   1 
ATOM   3586  C  CG2   . ILE   B 1  16  ? 10.469  29.133  -9.916  1.00 31.25  ? 16  ILE   C CG2   1 
ATOM   3587  C  CD1   . ILE   B 1  16  ? 10.751  26.065  -9.865  1.00 21.44  ? 16  ILE   C CD1   1 
ATOM   3588  N  N     . GLY   B 1  17  ? 12.015  30.592  -12.937 1.00 39.58  ? 17  GLY   C N     1 
ATOM   3589  C  CA    . GLY   B 1  17  ? 12.522  31.889  -13.359 1.00 27.42  ? 17  GLY   C CA    1 
ATOM   3590  C  C     . GLY   B 1  17  ? 11.593  32.754  -14.191 1.00 35.95  ? 17  GLY   C C     1 
ATOM   3591  O  O     . GLY   B 1  17  ? 11.352  33.904  -13.812 1.00 36.33  ? 17  GLY   C O     1 
ATOM   3592  N  N     . ASN   B 1  18  ? 11.084  32.246  -15.330 1.00 36.38  ? 18  ASN   C N     1 
ATOM   3593  C  CA    . ASN   B 1  18  ? 10.202  33.061  -16.173 1.00 37.26  ? 18  ASN   C CA    1 
ATOM   3594  C  C     . ASN   B 1  18  ? 8.907   33.400  -15.448 1.00 35.85  ? 18  ASN   C C     1 
ATOM   3595  O  O     . ASN   B 1  18  ? 8.392   34.514  -15.572 1.00 34.68  ? 18  ASN   C O     1 
ATOM   3596  C  CB    . ASN   B 1  18  ? 9.831   32.353  -17.487 1.00 40.77  ? 18  ASN   C CB    1 
ATOM   3597  C  CG    . ASN   B 1  18  ? 10.990  31.644  -18.155 1.00 39.43  ? 18  ASN   C CG    1 
ATOM   3598  O  OD1   . ASN   B 1  18  ? 12.104  32.151  -18.217 1.00 44.90  ? 18  ASN   C OD1   1 
ATOM   3599  N  ND2   . ASN   B 1  18  ? 10.712  30.456  -18.687 1.00 35.47  ? 18  ASN   C ND2   1 
ATOM   3600  N  N     . ALA   B 1  19  ? 8.331   32.417  -14.748 1.00 32.93  ? 19  ALA   C N     1 
ATOM   3601  C  CA    . ALA   B 1  19  ? 7.107   32.637  -13.995 1.00 28.13  ? 19  ALA   C CA    1 
ATOM   3602  C  C     . ALA   B 1  19  ? 7.303   33.703  -12.925 1.00 38.12  ? 19  ALA   C C     1 
ATOM   3603  O  O     . ALA   B 1  19  ? 6.435   34.564  -12.732 1.00 39.70  ? 19  ALA   C O     1 
ATOM   3604  C  CB    . ALA   B 1  19  ? 6.641   31.326  -13.370 1.00 23.81  ? 19  ALA   C CB    1 
ATOM   3605  N  N     . CYS   B 1  20  ? 8.442   33.673  -12.225 1.00 31.24  ? 20  CYS   C N     1 
ATOM   3606  C  CA    . CYS   B 1  20  ? 8.696   34.684  -11.204 1.00 35.82  ? 20  CYS   C CA    1 
ATOM   3607  C  C     . CYS   B 1  20  ? 8.853   36.073  -11.809 1.00 35.46  ? 20  CYS   C C     1 
ATOM   3608  O  O     . CYS   B 1  20  ? 8.405   37.063  -11.217 1.00 38.09  ? 20  CYS   C O     1 
ATOM   3609  C  CB    . CYS   B 1  20  ? 9.928   34.319  -10.383 1.00 31.92  ? 20  CYS   C CB    1 
ATOM   3610  S  SG    . CYS   B 1  20  ? 9.583   33.078  -9.173  1.00 41.04  ? 20  CYS   C SG    1 
ATOM   3611  N  N     . TRP   B 1  21  ? 9.477   36.174  -12.985 1.00 31.09  ? 21  TRP   C N     1 
ATOM   3612  C  CA    . TRP   B 1  21  ? 9.796   37.499  -13.503 1.00 29.87  ? 21  TRP   C CA    1 
ATOM   3613  C  C     . TRP   B 1  21  ? 8.607   38.115  -14.220 1.00 36.50  ? 21  TRP   C C     1 
ATOM   3614  O  O     . TRP   B 1  21  ? 8.362   39.323  -14.103 1.00 43.16  ? 21  TRP   C O     1 
ATOM   3615  C  CB    . TRP   B 1  21  ? 11.038  37.437  -14.398 1.00 32.66  ? 21  TRP   C CB    1 
ATOM   3616  C  CG    . TRP   B 1  21  ? 12.307  37.342  -13.580 1.00 31.39  ? 21  TRP   C CG    1 
ATOM   3617  C  CD1   . TRP   B 1  21  ? 13.065  36.232  -13.370 1.00 32.26  ? 21  TRP   C CD1   1 
ATOM   3618  C  CD2   . TRP   B 1  21  ? 12.907  38.389  -12.807 1.00 31.73  ? 21  TRP   C CD2   1 
ATOM   3619  N  NE1   . TRP   B 1  21  ? 14.121  36.524  -12.537 1.00 33.17  ? 21  TRP   C NE1   1 
ATOM   3620  C  CE2   . TRP   B 1  21  ? 14.045  37.844  -12.176 1.00 34.16  ? 21  TRP   C CE2   1 
ATOM   3621  C  CE3   . TRP   B 1  21  ? 12.606  39.740  -12.604 1.00 28.97  ? 21  TRP   C CE3   1 
ATOM   3622  C  CZ2   . TRP   B 1  21  ? 14.886  38.607  -11.357 1.00 33.88  ? 21  TRP   C CZ2   1 
ATOM   3623  C  CZ3   . TRP   B 1  21  ? 13.437  40.492  -11.780 1.00 30.99  ? 21  TRP   C CZ3   1 
ATOM   3624  C  CH2   . TRP   B 1  21  ? 14.559  39.922  -11.164 1.00 24.45  ? 21  TRP   C CH2   1 
ATOM   3625  N  N     . GLU   B 1  22  ? 7.829   37.304  -14.930 1.00 34.15  ? 22  GLU   C N     1 
ATOM   3626  C  CA    . GLU   B 1  22  ? 6.588   37.815  -15.488 1.00 32.48  ? 22  GLU   C CA    1 
ATOM   3627  C  C     . GLU   B 1  22  ? 5.648   38.281  -14.386 1.00 35.24  ? 22  GLU   C C     1 
ATOM   3628  O  O     . GLU   B 1  22  ? 4.904   39.253  -14.573 1.00 38.12  ? 22  GLU   C O     1 
ATOM   3629  C  CB    . GLU   B 1  22  ? 5.918   36.747  -16.346 1.00 36.20  ? 22  GLU   C CB    1 
ATOM   3630  C  CG    . GLU   B 1  22  ? 4.413   36.895  -16.389 1.00 44.14  ? 22  GLU   C CG    1 
ATOM   3631  C  CD    . GLU   B 1  22  ? 3.793   36.197  -17.575 1.00 58.32  ? 22  GLU   C CD    1 
ATOM   3632  O  OE1   . GLU   B 1  22  ? 4.206   35.047  -17.853 1.00 55.23  ? 22  GLU   C OE1   1 
ATOM   3633  O  OE2   . GLU   B 1  22  ? 2.902   36.810  -18.225 1.00 53.67  ? 22  GLU   C OE2   1 
ATOM   3634  N  N     . LEU   B 1  23  ? 5.663   37.598  -13.235 1.00 30.75  ? 23  LEU   C N     1 
ATOM   3635  C  CA    . LEU   B 1  23  ? 4.836   38.026  -12.111 1.00 33.96  ? 23  LEU   C CA    1 
ATOM   3636  C  C     . LEU   B 1  23  ? 5.387   39.306  -11.480 1.00 46.38  ? 23  LEU   C C     1 
ATOM   3637  O  O     . LEU   B 1  23  ? 4.619   40.239  -11.199 1.00 35.88  ? 23  LEU   C O     1 
ATOM   3638  C  CB    . LEU   B 1  23  ? 4.726   36.912  -11.071 1.00 31.96  ? 23  LEU   C CB    1 
ATOM   3639  C  CG    . LEU   B 1  23  ? 3.798   37.242  -9.896  1.00 36.62  ? 23  LEU   C CG    1 
ATOM   3640  C  CD1   . LEU   B 1  23  ? 2.344   37.319  -10.359 1.00 36.87  ? 23  LEU   C CD1   1 
ATOM   3641  C  CD2   . LEU   B 1  23  ? 3.953   36.262  -8.742  1.00 30.98  ? 23  LEU   C CD2   1 
ATOM   3642  N  N     . TYR   B 1  24  ? 6.715   39.387  -11.268 1.00 40.27  ? 24  TYR   C N     1 
ATOM   3643  C  CA    . TYR   B 1  24  ? 7.304   40.654  -10.825 1.00 35.35  ? 24  TYR   C CA    1 
ATOM   3644  C  C     . TYR   B 1  24  ? 6.909   41.793  -11.758 1.00 31.23  ? 24  TYR   C C     1 
ATOM   3645  O  O     . TYR   B 1  24  ? 6.530   42.875  -11.305 1.00 34.49  ? 24  TYR   C O     1 
ATOM   3646  C  CB    . TYR   B 1  24  ? 8.830   40.571  -10.735 1.00 34.80  ? 24  TYR   C CB    1 
ATOM   3647  C  CG    . TYR   B 1  24  ? 9.376   39.604  -9.717  1.00 34.63  ? 24  TYR   C CG    1 
ATOM   3648  C  CD1   . TYR   B 1  24  ? 8.591   39.138  -8.684  1.00 30.56  ? 24  TYR   C CD1   1 
ATOM   3649  C  CD2   . TYR   B 1  24  ? 10.686  39.142  -9.808  1.00 38.21  ? 24  TYR   C CD2   1 
ATOM   3650  C  CE1   . TYR   B 1  24  ? 9.093   38.249  -7.765  1.00 34.73  ? 24  TYR   C CE1   1 
ATOM   3651  C  CE2   . TYR   B 1  24  ? 11.201  38.249  -8.894  1.00 32.93  ? 24  TYR   C CE2   1 
ATOM   3652  C  CZ    . TYR   B 1  24  ? 10.397  37.806  -7.875  1.00 35.39  ? 24  TYR   C CZ    1 
ATOM   3653  O  OH    . TYR   B 1  24  ? 10.884  36.926  -6.948  1.00 31.26  ? 24  TYR   C OH    1 
ATOM   3654  N  N     . CYS   B 1  25  ? 7.002   41.578  -13.071 1.00 35.07  ? 25  CYS   C N     1 
ATOM   3655  C  CA    . CYS   B 1  25  ? 6.687   42.668  -13.994 1.00 33.46  ? 25  CYS   C CA    1 
ATOM   3656  C  C     . CYS   B 1  25  ? 5.253   43.139  -13.798 1.00 36.36  ? 25  CYS   C C     1 
ATOM   3657  O  O     . CYS   B 1  25  ? 4.997   44.343  -13.660 1.00 32.09  ? 25  CYS   C O     1 
ATOM   3658  C  CB    . CYS   B 1  25  ? 6.937   42.245  -15.438 1.00 27.87  ? 25  CYS   C CB    1 
ATOM   3659  S  SG    . CYS   B 1  25  ? 8.682   42.143  -15.933 1.00 40.39  ? 25  CYS   C SG    1 
ATOM   3660  N  N     . LEU   B 1  26  ? 4.308   42.195  -13.730 1.00 35.00  ? 26  LEU   C N     1 
ATOM   3661  C  CA    . LEU   B 1  26  ? 2.911   42.555  -13.504 1.00 32.99  ? 26  LEU   C CA    1 
ATOM   3662  C  C     . LEU   B 1  26  ? 2.699   43.212  -12.138 1.00 34.55  ? 26  LEU   C C     1 
ATOM   3663  O  O     . LEU   B 1  26  ? 1.913   44.152  -12.009 1.00 41.18  ? 26  LEU   C O     1 
ATOM   3664  C  CB    . LEU   B 1  26  ? 2.032   41.318  -13.652 1.00 45.50  ? 26  LEU   C CB    1 
ATOM   3665  C  CG    . LEU   B 1  26  ? 1.902   40.843  -15.101 1.00 51.76  ? 26  LEU   C CG    1 
ATOM   3666  C  CD1   . LEU   B 1  26  ? 1.274   39.456  -15.181 1.00 47.36  ? 26  LEU   C CD1   1 
ATOM   3667  C  CD2   . LEU   B 1  26  ? 1.097   41.866  -15.907 1.00 44.85  ? 26  LEU   C CD2   1 
ATOM   3668  N  N     . GLU   B 1  27  ? 3.370   42.729  -11.096 1.00 40.50  ? 27  GLU   C N     1 
ATOM   3669  C  CA    . GLU   B 1  27  ? 3.187   43.368  -9.796  1.00 38.39  ? 27  GLU   C CA    1 
ATOM   3670  C  C     . GLU   B 1  27  ? 3.704   44.797  -9.800  1.00 40.19  ? 27  GLU   C C     1 
ATOM   3671  O  O     . GLU   B 1  27  ? 3.244   45.625  -9.006  1.00 41.96  ? 27  GLU   C O     1 
ATOM   3672  C  CB    . GLU   B 1  27  ? 3.900   42.592  -8.697  1.00 37.71  ? 27  GLU   C CB    1 
ATOM   3673  C  CG    . GLU   B 1  27  ? 3.258   41.304  -8.247  1.00 40.08  ? 27  GLU   C CG    1 
ATOM   3674  C  CD    . GLU   B 1  27  ? 4.086   40.672  -7.167  1.00 37.03  ? 27  GLU   C CD    1 
ATOM   3675  O  OE1   . GLU   B 1  27  ? 5.069   41.317  -6.758  1.00 35.73  ? 27  GLU   C OE1   1 
ATOM   3676  O  OE2   . GLU   B 1  27  ? 3.782   39.548  -6.743  1.00 40.98  ? 27  GLU   C OE2   1 
ATOM   3677  N  N     . HIS   B 1  28  ? 4.659   45.102  -10.676 1.00 38.98  ? 28  HIS   C N     1 
ATOM   3678  C  CA    . HIS   B 1  28  ? 5.350   46.383  -10.651 1.00 37.46  ? 28  HIS   C CA    1 
ATOM   3679  C  C     . HIS   B 1  28  ? 4.917   47.357  -11.749 1.00 39.46  ? 28  HIS   C C     1 
ATOM   3680  O  O     . HIS   B 1  28  ? 5.243   48.541  -11.650 1.00 46.87  ? 28  HIS   C O     1 
ATOM   3681  C  CB    . HIS   B 1  28  ? 6.864   46.159  -10.739 1.00 31.31  ? 28  HIS   C CB    1 
ATOM   3682  C  CG    . HIS   B 1  28  ? 7.488   45.705  -9.452  1.00 30.79  ? 28  HIS   C CG    1 
ATOM   3683  N  ND1   . HIS   B 1  28  ? 7.230   46.312  -8.239  1.00 30.28  ? 28  HIS   C ND1   1 
ATOM   3684  C  CD2   . HIS   B 1  28  ? 8.369   44.713  -9.192  1.00 26.20  ? 28  HIS   C CD2   1 
ATOM   3685  C  CE1   . HIS   B 1  28  ? 7.917   45.710  -7.289  1.00 30.36  ? 28  HIS   C CE1   1 
ATOM   3686  N  NE2   . HIS   B 1  28  ? 8.609   44.729  -7.839  1.00 40.20  ? 28  HIS   C NE2   1 
ATOM   3687  N  N     . GLY   B 1  29  ? 4.205   46.910  -12.783 1.00 31.84  ? 29  GLY   C N     1 
ATOM   3688  C  CA    . GLY   B 1  29  ? 3.893   47.786  -13.892 1.00 21.35  ? 29  GLY   C CA    1 
ATOM   3689  C  C     . GLY   B 1  29  ? 4.947   47.870  -14.977 1.00 37.25  ? 29  GLY   C C     1 
ATOM   3690  O  O     . GLY   B 1  29  ? 5.047   48.898  -15.657 1.00 37.44  ? 29  GLY   C O     1 
ATOM   3691  N  N     . ILE   B 1  30  ? 5.727   46.813  -15.172 1.00 37.34  ? 30  ILE   C N     1 
ATOM   3692  C  CA    . ILE   B 1  30  ? 6.793   46.774  -16.162 1.00 36.76  ? 30  ILE   C CA    1 
ATOM   3693  C  C     . ILE   B 1  30  ? 6.292   46.000  -17.378 1.00 42.82  ? 30  ILE   C C     1 
ATOM   3694  O  O     . ILE   B 1  30  ? 5.894   44.835  -17.261 1.00 37.39  ? 30  ILE   C O     1 
ATOM   3695  C  CB    . ILE   B 1  30  ? 8.052   46.127  -15.573 1.00 34.86  ? 30  ILE   C CB    1 
ATOM   3696  C  CG1   . ILE   B 1  30  ? 8.394   46.808  -14.247 1.00 31.45  ? 30  ILE   C CG1   1 
ATOM   3697  C  CG2   . ILE   B 1  30  ? 9.196   46.158  -16.583 1.00 31.24  ? 30  ILE   C CG2   1 
ATOM   3698  C  CD1   . ILE   B 1  30  ? 9.694   46.345  -13.644 1.00 22.65  ? 30  ILE   C CD1   1 
ATOM   3699  N  N     . GLN   B 1  31  ? 6.307   46.638  -18.545 1.00 44.80  ? 31  GLN   C N     1 
ATOM   3700  C  CA    . GLN   B 1  31  ? 5.843   45.973  -19.749 1.00 41.18  ? 31  GLN   C CA    1 
ATOM   3701  C  C     . GLN   B 1  31  ? 6.928   45.055  -20.288 1.00 39.09  ? 31  GLN   C C     1 
ATOM   3702  O  O     . GLN   B 1  31  ? 8.100   45.197  -19.942 1.00 49.88  ? 31  GLN   C O     1 
ATOM   3703  C  CB    . GLN   B 1  31  ? 5.430   46.996  -20.801 1.00 48.81  ? 31  GLN   C CB    1 
ATOM   3704  C  CG    . GLN   B 1  31  ? 4.116   47.733  -20.474 1.00 52.10  ? 31  GLN   C CG    1 
ATOM   3705  C  CD    . GLN   B 1  31  ? 4.324   49.203  -20.094 1.00 69.90  ? 31  GLN   C CD    1 
ATOM   3706  O  OE1   . GLN   B 1  31  ? 5.425   49.751  -20.247 1.00 65.30  ? 31  GLN   C OE1   1 
ATOM   3707  N  NE2   . GLN   B 1  31  ? 3.262   49.847  -19.594 1.00 66.39  ? 31  GLN   C NE2   1 
ATOM   3708  N  N     . PRO   B 1  32  ? 6.557   44.087  -21.128 1.00 41.13  ? 32  PRO   C N     1 
ATOM   3709  C  CA    . PRO   B 1  32  ? 7.549   43.113  -21.628 1.00 37.32  ? 32  PRO   C CA    1 
ATOM   3710  C  C     . PRO   B 1  32  ? 8.694   43.720  -22.436 1.00 43.26  ? 32  PRO   C C     1 
ATOM   3711  O  O     . PRO   B 1  32  ? 9.630   42.985  -22.787 1.00 45.70  ? 32  PRO   C O     1 
ATOM   3712  C  CB    . PRO   B 1  32  ? 6.705   42.167  -22.488 1.00 32.57  ? 32  PRO   C CB    1 
ATOM   3713  C  CG    . PRO   B 1  32  ? 5.308   42.307  -21.939 1.00 37.28  ? 32  PRO   C CG    1 
ATOM   3714  C  CD    . PRO   B 1  32  ? 5.177   43.724  -21.489 1.00 35.76  ? 32  PRO   C CD    1 
ATOM   3715  N  N     . ASP   B 1  33  ? 8.654   45.012  -22.765 1.00 44.83  ? 33  ASP   C N     1 
ATOM   3716  C  CA    . ASP   B 1  33  ? 9.828   45.696  -23.297 1.00 43.81  ? 33  ASP   C CA    1 
ATOM   3717  C  C     . ASP   B 1  33  ? 10.661  46.337  -22.199 1.00 43.72  ? 33  ASP   C C     1 
ATOM   3718  O  O     . ASP   B 1  33  ? 11.644  47.022  -22.497 1.00 52.53  ? 33  ASP   C O     1 
ATOM   3719  C  CB    . ASP   B 1  33  ? 9.425   46.750  -24.331 1.00 43.61  ? 33  ASP   C CB    1 
ATOM   3720  C  CG    . ASP   B 1  33  ? 8.744   47.956  -23.707 1.00 54.71  ? 33  ASP   C CG    1 
ATOM   3721  O  OD1   . ASP   B 1  33  ? 8.127   47.822  -22.623 1.00 57.02  ? 33  ASP   C OD1   1 
ATOM   3722  O  OD2   . ASP   B 1  33  ? 8.818   49.044  -24.314 1.00 58.89  ? 33  ASP   C OD2   1 
ATOM   3723  N  N     . GLY   B 1  34  ? 10.295  46.122  -20.938 1.00 47.59  ? 34  GLY   C N     1 
ATOM   3724  C  CA    . GLY   B 1  34  ? 11.022  46.672  -19.820 1.00 46.77  ? 34  GLY   C CA    1 
ATOM   3725  C  C     . GLY   B 1  34  ? 10.685  48.103  -19.483 1.00 48.73  ? 34  GLY   C C     1 
ATOM   3726  O  O     . GLY   B 1  34  ? 11.235  48.632  -18.507 1.00 48.88  ? 34  GLY   C O     1 
ATOM   3727  N  N     . GLN   B 1  35  ? 9.804   48.748  -20.247 1.00 45.43  ? 35  GLN   C N     1 
ATOM   3728  C  CA    . GLN   B 1  35  ? 9.430   50.123  -19.951 1.00 45.85  ? 35  GLN   C CA    1 
ATOM   3729  C  C     . GLN   B 1  35  ? 8.418   50.157  -18.811 1.00 42.28  ? 35  GLN   C C     1 
ATOM   3730  O  O     . GLN   B 1  35  ? 7.531   49.303  -18.722 1.00 41.58  ? 35  GLN   C O     1 
ATOM   3731  C  CB    . GLN   B 1  35  ? 8.867   50.817  -21.196 1.00 39.02  ? 35  GLN   C CB    1 
ATOM   3732  C  CG    . GLN   B 1  35  ? 9.886   51.084  -22.303 1.00 43.43  ? 35  GLN   C CG    1 
ATOM   3733  C  CD    . GLN   B 1  35  ? 10.984  52.089  -21.919 1.00 54.49  ? 35  GLN   C CD    1 
ATOM   3734  O  OE1   . GLN   B 1  35  ? 10.705  53.195  -21.437 1.00 49.61  ? 35  GLN   C OE1   1 
ATOM   3735  N  NE2   . GLN   B 1  35  ? 12.242  51.704  -22.150 1.00 46.30  ? 35  GLN   C NE2   1 
ATOM   3736  N  N     . MET   B 1  36  ? 8.551   51.161  -17.942 1.00 44.87  ? 36  MET   C N     1 
ATOM   3737  C  CA    . MET   B 1  36  ? 7.753   51.279  -16.721 1.00 41.80  ? 36  MET   C CA    1 
ATOM   3738  C  C     . MET   B 1  36  ? 7.189   52.689  -16.585 1.00 45.56  ? 36  MET   C C     1 
ATOM   3739  O  O     . MET   B 1  36  ? 7.742   53.520  -15.853 1.00 42.60  ? 36  MET   C O     1 
ATOM   3740  C  CB    . MET   B 1  36  ? 8.598   50.912  -15.504 1.00 39.28  ? 36  MET   C CB    1 
ATOM   3741  C  CG    . MET   B 1  36  ? 7.845   50.901  -14.191 1.00 42.73  ? 36  MET   C CG    1 
ATOM   3742  S  SD    . MET   B 1  36  ? 8.973   50.417  -12.888 1.00 53.96  ? 36  MET   C SD    1 
ATOM   3743  C  CE    . MET   B 1  36  ? 7.952   50.704  -11.451 1.00 40.14  ? 36  MET   C CE    1 
ATOM   3744  N  N     . PRO   B 1  37  ? 6.062   52.991  -17.273 1.00 54.80  ? 37  PRO   C N     1 
ATOM   3745  C  CA    . PRO   B 1  37  ? 5.511   54.358  -17.284 1.00 52.84  ? 37  PRO   C CA    1 
ATOM   3746  C  C     . PRO   B 1  37  ? 5.691   55.158  -16.003 1.00 54.44  ? 37  PRO   C C     1 
ATOM   3747  O  O     . PRO   B 1  37  ? 6.158   56.303  -16.037 1.00 50.77  ? 37  PRO   C O     1 
ATOM   3748  C  CB    . PRO   B 1  37  ? 4.026   54.114  -17.564 1.00 58.46  ? 37  PRO   C CB    1 
ATOM   3749  C  CG    . PRO   B 1  37  ? 3.997   52.802  -18.362 1.00 60.64  ? 37  PRO   C CG    1 
ATOM   3750  C  CD    . PRO   B 1  37  ? 5.348   52.124  -18.225 1.00 54.55  ? 37  PRO   C CD    1 
ATOM   3751  N  N     . SER   B 1  38  ? 5.344   54.550  -14.868 1.00 55.34  ? 38  SER   C N     1 
ATOM   3752  C  CA    . SER   B 1  38  ? 5.329   55.248  -13.588 1.00 51.49  ? 38  SER   C CA    1 
ATOM   3753  C  C     . SER   B 1  38  ? 6.710   55.494  -12.980 1.00 55.39  ? 38  SER   C C     1 
ATOM   3754  O  O     . SER   B 1  38  ? 6.797   56.246  -12.000 1.00 57.88  ? 38  SER   C O     1 
ATOM   3755  C  CB    . SER   B 1  38  ? 4.493   54.475  -12.577 1.00 47.46  ? 38  SER   C CB    1 
ATOM   3756  O  OG    . SER   B 1  38  ? 5.336   53.697  -11.746 1.00 62.47  ? 38  SER   C OG    1 
ATOM   3757  N  N     . ASP   B 1  39  ? 7.788   54.894  -13.488 1.00 46.08  ? 39  ASP   C N     1 
ATOM   3758  C  CA    . ASP   B 1  39  ? 9.098   55.295  -12.992 1.00 47.76  ? 39  ASP   C CA    1 
ATOM   3759  C  C     . ASP   B 1  39  ? 9.505   56.607  -13.654 1.00 50.13  ? 39  ASP   C C     1 
ATOM   3760  O  O     . ASP   B 1  39  ? 9.690   56.663  -14.874 1.00 55.61  ? 39  ASP   C O     1 
ATOM   3761  C  CB    . ASP   B 1  39  ? 10.180  54.241  -13.214 1.00 33.88  ? 39  ASP   C CB    1 
ATOM   3762  C  CG    . ASP   B 1  39  ? 11.496  54.650  -12.560 1.00 44.07  ? 39  ASP   C CG    1 
ATOM   3763  O  OD1   . ASP   B 1  39  ? 11.480  55.647  -11.820 1.00 46.22  ? 39  ASP   C OD1   1 
ATOM   3764  O  OD2   . ASP   B 1  39  ? 12.548  54.025  -12.765 1.00 47.05  ? 39  ASP   C OD2   1 
ATOM   3765  N  N     . LYS   B 1  40  ? 9.643   57.656  -12.837 1.00 52.89  ? 40  LYS   C N     1 
ATOM   3766  C  CA    . LYS   B 1  40  ? 10.206  58.936  -13.253 1.00 49.06  ? 40  LYS   C CA    1 
ATOM   3767  C  C     . LYS   B 1  40  ? 11.728  58.989  -13.131 1.00 46.34  ? 40  LYS   C C     1 
ATOM   3768  O  O     . LYS   B 1  40  ? 12.363  59.737  -13.877 1.00 49.19  ? 40  LYS   C O     1 
ATOM   3769  C  CB    . LYS   B 1  40  ? 9.583   60.063  -12.429 1.00 41.13  ? 40  LYS   C CB    1 
ATOM   3770  C  CG    . LYS   B 1  40  ? 8.081   59.950  -12.327 1.00 40.79  ? 40  LYS   C CG    1 
ATOM   3771  C  CD    . LYS   B 1  40  ? 7.489   59.699  -13.692 1.00 45.13  ? 40  LYS   C CD    1 
ATOM   3772  C  CE    . LYS   B 1  40  ? 5.987   59.597  -13.618 1.00 47.57  ? 40  LYS   C CE    1 
ATOM   3773  N  NZ    . LYS   B 1  40  ? 5.423   59.249  -14.962 1.00 62.80  ? 40  LYS   C NZ    1 
ATOM   3774  N  N     . THR   B 1  41  ? 12.318  58.240  -12.185 1.00 50.58  ? 41  THR   C N     1 
ATOM   3775  C  CA    . THR   B 1  41  ? 13.756  57.955  -12.124 1.00 51.99  ? 41  THR   C CA    1 
ATOM   3776  C  C     . THR   B 1  41  ? 14.235  57.254  -13.390 1.00 58.12  ? 41  THR   C C     1 
ATOM   3777  O  O     . THR   B 1  41  ? 14.176  56.016  -13.455 1.00 48.82  ? 41  THR   C O     1 
ATOM   3778  C  CB    . THR   B 1  41  ? 14.098  57.037  -10.938 1.00 54.30  ? 41  THR   C CB    1 
ATOM   3779  O  OG1   . THR   B 1  41  ? 13.938  55.638  -11.319 1.00 39.09  ? 41  THR   C OG1   1 
ATOM   3780  C  CG2   . THR   B 1  41  ? 13.215  57.372  -9.733  1.00 53.22  ? 41  THR   C CG2   1 
ATOM   3781  N  N     . ILE   B 1  42  ? 14.734  58.013  -14.373 1.00 51.77  ? 42  ILE   C N     1 
ATOM   3782  C  CA    . ILE   B 1  42  ? 15.122  57.477  -15.678 1.00 48.66  ? 42  ILE   C CA    1 
ATOM   3783  C  C     . ILE   B 1  42  ? 16.625  57.220  -15.704 1.00 52.59  ? 42  ILE   C C     1 
ATOM   3784  O  O     . ILE   B 1  42  ? 17.429  58.130  -15.461 1.00 55.14  ? 42  ILE   C O     1 
ATOM   3785  C  CB    . ILE   B 1  42  ? 14.723  58.424  -16.812 1.00 47.73  ? 42  ILE   C CB    1 
ATOM   3786  C  CG1   . ILE   B 1  42  ? 13.231  58.746  -16.731 1.00 43.72  ? 42  ILE   C CG1   1 
ATOM   3787  C  CG2   . ILE   B 1  42  ? 15.111  57.809  -18.142 1.00 43.87  ? 42  ILE   C CG2   1 
ATOM   3788  C  CD1   . ILE   B 1  42  ? 12.735  59.492  -17.931 1.00 48.61  ? 42  ILE   C CD1   1 
ATOM   3789  N  N     . GLY   B 1  43  ? 17.005  55.984  -16.018 1.00 45.32  ? 43  GLY   C N     1 
ATOM   3790  C  CA    . GLY   B 1  43  ? 18.386  55.564  -15.949 1.00 55.00  ? 43  GLY   C CA    1 
ATOM   3791  C  C     . GLY   B 1  43  ? 18.850  55.072  -14.590 1.00 52.80  ? 43  GLY   C C     1 
ATOM   3792  O  O     . GLY   B 1  43  ? 19.965  54.532  -14.489 1.00 57.34  ? 43  GLY   C O     1 
ATOM   3793  N  N     . GLY   B 1  44  ? 18.045  55.238  -13.549 1.00 38.20  ? 44  GLY   C N     1 
ATOM   3794  C  CA    . GLY   B 1  44  ? 18.465  54.823  -12.228 1.00 47.29  ? 44  GLY   C CA    1 
ATOM   3795  C  C     . GLY   B 1  44  ? 17.394  55.113  -11.199 1.00 50.22  ? 44  GLY   C C     1 
ATOM   3796  O  O     . GLY   B 1  44  ? 16.263  55.481  -11.532 1.00 51.92  ? 44  GLY   C O     1 
ATOM   3797  N  N     . GLY   B 1  45  ? 17.771  54.931  -9.942  1.00 47.85  ? 45  GLY   C N     1 
ATOM   3798  C  CA    . GLY   B 1  45  ? 16.905  55.218  -8.818  1.00 49.79  ? 45  GLY   C CA    1 
ATOM   3799  C  C     . GLY   B 1  45  ? 17.300  54.412  -7.602  1.00 53.73  ? 45  GLY   C C     1 
ATOM   3800  O  O     . GLY   B 1  45  ? 18.044  53.432  -7.673  1.00 48.14  ? 45  GLY   C O     1 
ATOM   3801  N  N     . ASP   B 1  46  ? 16.798  54.844  -6.450  1.00 57.60  ? 46  ASP   C N     1 
ATOM   3802  C  CA    . ASP   B 1  46  ? 16.837  54.026  -5.246  1.00 55.33  ? 46  ASP   C CA    1 
ATOM   3803  C  C     . ASP   B 1  46  ? 15.424  53.648  -4.797  1.00 54.65  ? 46  ASP   C C     1 
ATOM   3804  O  O     . ASP   B 1  46  ? 15.135  53.573  -3.602  1.00 49.70  ? 46  ASP   C O     1 
ATOM   3805  C  CB    . ASP   B 1  46  ? 17.611  54.722  -4.129  1.00 64.89  ? 46  ASP   C CB    1 
ATOM   3806  C  CG    . ASP   B 1  46  ? 18.695  53.818  -3.521  1.00 82.68  ? 46  ASP   C CG    1 
ATOM   3807  O  OD1   . ASP   B 1  46  ? 19.017  52.789  -4.164  1.00 74.14  ? 46  ASP   C OD1   1 
ATOM   3808  O  OD2   . ASP   B 1  46  ? 19.216  54.122  -2.413  1.00 76.00  ? 46  ASP   C OD2   1 
ATOM   3809  N  N     . ASP   B 1  47  ? 14.527  53.400  -5.757  1.00 43.92  ? 47  ASP   C N     1 
ATOM   3810  C  CA    . ASP   B 1  47  ? 13.211  52.867  -5.437  1.00 40.21  ? 47  ASP   C CA    1 
ATOM   3811  C  C     . ASP   B 1  47  ? 13.331  51.410  -4.985  1.00 44.54  ? 47  ASP   C C     1 
ATOM   3812  O  O     . ASP   B 1  47  ? 14.375  50.759  -5.125  1.00 35.57  ? 47  ASP   C O     1 
ATOM   3813  C  CB    . ASP   B 1  47  ? 12.265  52.964  -6.635  1.00 43.14  ? 47  ASP   C CB    1 
ATOM   3814  C  CG    . ASP   B 1  47  ? 11.689  54.360  -6.827  1.00 55.98  ? 47  ASP   C CG    1 
ATOM   3815  O  OD1   . ASP   B 1  47  ? 11.275  54.991  -5.829  1.00 53.67  ? 47  ASP   C OD1   1 
ATOM   3816  O  OD2   . ASP   B 1  47  ? 11.640  54.826  -7.991  1.00 59.22  ? 47  ASP   C OD2   1 
ATOM   3817  N  N     . SER   B 1  48  ? 12.232  50.898  -4.433  1.00 38.81  ? 48  SER   C N     1 
ATOM   3818  C  CA    . SER   B 1  48  ? 12.269  49.572  -3.838  1.00 35.12  ? 48  SER   C CA    1 
ATOM   3819  C  C     . SER   B 1  48  ? 12.334  48.477  -4.895  1.00 44.38  ? 48  SER   C C     1 
ATOM   3820  O  O     . SER   B 1  48  ? 12.943  47.425  -4.650  1.00 32.25  ? 48  SER   C O     1 
ATOM   3821  C  CB    . SER   B 1  48  ? 11.061  49.380  -2.932  1.00 32.86  ? 48  SER   C CB    1 
ATOM   3822  O  OG    . SER   B 1  48  ? 11.290  50.014  -1.681  1.00 55.86  ? 48  SER   C OG    1 
ATOM   3823  N  N     . PHE   B 1  49  ? 11.720  48.696  -6.068  1.00 35.54  ? 49  PHE   C N     1 
ATOM   3824  C  CA    . PHE   B 1  49  ? 11.820  47.704  -7.136  1.00 35.99  ? 49  PHE   C CA    1 
ATOM   3825  C  C     . PHE   B 1  49  ? 13.240  47.626  -7.706  1.00 33.12  ? 49  PHE   C C     1 
ATOM   3826  O  O     . PHE   B 1  49  ? 13.640  46.575  -8.215  1.00 29.78  ? 49  PHE   C O     1 
ATOM   3827  C  CB    . PHE   B 1  49  ? 10.794  47.998  -8.237  1.00 40.88  ? 49  PHE   C CB    1 
ATOM   3828  C  CG    . PHE   B 1  49  ? 10.934  49.372  -8.871  1.00 46.60  ? 49  PHE   C CG    1 
ATOM   3829  C  CD1   . PHE   B 1  49  ? 11.975  49.652  -9.747  1.00 39.33  ? 49  PHE   C CD1   1 
ATOM   3830  C  CD2   . PHE   B 1  49  ? 10.018  50.374  -8.595  1.00 41.25  ? 49  PHE   C CD2   1 
ATOM   3831  C  CE1   . PHE   B 1  49  ? 12.092  50.900  -10.308 1.00 45.21  ? 49  PHE   C CE1   1 
ATOM   3832  C  CE2   . PHE   B 1  49  ? 10.142  51.626  -9.165  1.00 40.00  ? 49  PHE   C CE2   1 
ATOM   3833  C  CZ    . PHE   B 1  49  ? 11.171  51.888  -10.019 1.00 37.35  ? 49  PHE   C CZ    1 
ATOM   3834  N  N     . ASN   B 1  50  ? 14.018  48.708  -7.612  1.00 36.48  ? 50  ASN   C N     1 
ATOM   3835  C  CA    . ASN   B 1  50  ? 15.424  48.687  -8.012  1.00 35.32  ? 50  ASN   C CA    1 
ATOM   3836  C  C     . ASN   B 1  50  ? 16.234  47.653  -7.251  1.00 26.08  ? 50  ASN   C C     1 
ATOM   3837  O  O     . ASN   B 1  50  ? 17.396  47.428  -7.594  1.00 30.48  ? 50  ASN   C O     1 
ATOM   3838  C  CB    . ASN   B 1  50  ? 16.098  50.060  -7.808  1.00 39.41  ? 50  ASN   C CB    1 
ATOM   3839  C  CG    . ASN   B 1  50  ? 15.563  51.143  -8.745  1.00 40.62  ? 50  ASN   C CG    1 
ATOM   3840  O  OD1   . ASN   B 1  50  ? 14.976  52.134  -8.299  1.00 46.40  ? 50  ASN   C OD1   1 
ATOM   3841  N  ND2   . ASN   B 1  50  ? 15.782  50.971  -10.035 1.00 34.87  ? 50  ASN   C ND2   1 
ATOM   3842  N  N     . THR   B 1  51  ? 15.683  47.031  -6.220  1.00 23.30  ? 51  THR   C N     1 
ATOM   3843  C  CA    . THR   B 1  51  ? 16.420  45.918  -5.637  1.00 34.42  ? 51  THR   C CA    1 
ATOM   3844  C  C     . THR   B 1  51  ? 16.468  44.718  -6.574  1.00 37.68  ? 51  THR   C C     1 
ATOM   3845  O  O     . THR   B 1  51  ? 17.363  43.876  -6.434  1.00 40.32  ? 51  THR   C O     1 
ATOM   3846  C  CB    . THR   B 1  51  ? 15.823  45.506  -4.291  1.00 32.51  ? 51  THR   C CB    1 
ATOM   3847  O  OG1   . THR   B 1  51  ? 14.626  44.735  -4.496  1.00 31.61  ? 51  THR   C OG1   1 
ATOM   3848  C  CG2   . THR   B 1  51  ? 15.526  46.750  -3.447  1.00 32.98  ? 51  THR   C CG2   1 
ATOM   3849  N  N     . PHE   B 1  52  ? 15.539  44.633  -7.537  1.00 31.76  ? 52  PHE   C N     1 
ATOM   3850  C  CA    . PHE   B 1  52  ? 15.472  43.516  -8.471  1.00 34.24  ? 52  PHE   C CA    1 
ATOM   3851  C  C     . PHE   B 1  52  ? 15.600  43.919  -9.935  1.00 35.26  ? 52  PHE   C C     1 
ATOM   3852  O  O     . PHE   B 1  52  ? 15.834  43.044  -10.776 1.00 33.97  ? 52  PHE   C O     1 
ATOM   3853  C  CB    . PHE   B 1  52  ? 14.152  42.746  -8.285  1.00 31.28  ? 52  PHE   C CB    1 
ATOM   3854  C  CG    . PHE   B 1  52  ? 14.209  41.703  -7.211  1.00 33.53  ? 52  PHE   C CG    1 
ATOM   3855  C  CD1   . PHE   B 1  52  ? 14.358  42.063  -5.884  1.00 27.75  ? 52  PHE   C CD1   1 
ATOM   3856  C  CD2   . PHE   B 1  52  ? 14.115  40.353  -7.530  1.00 36.28  ? 52  PHE   C CD2   1 
ATOM   3857  C  CE1   . PHE   B 1  52  ? 14.414  41.101  -4.896  1.00 30.64  ? 52  PHE   C CE1   1 
ATOM   3858  C  CE2   . PHE   B 1  52  ? 14.164  39.381  -6.531  1.00 43.78  ? 52  PHE   C CE2   1 
ATOM   3859  C  CZ    . PHE   B 1  52  ? 14.317  39.755  -5.217  1.00 32.75  ? 52  PHE   C CZ    1 
ATOM   3860  N  N     . PHE   B 1  53  ? 15.451  45.203  -10.262 1.00 32.61  ? 53  PHE   C N     1 
ATOM   3861  C  CA    . PHE   B 1  53  ? 15.530  45.716  -11.626 1.00 31.43  ? 53  PHE   C CA    1 
ATOM   3862  C  C     . PHE   B 1  53  ? 16.560  46.833  -11.683 1.00 38.62  ? 53  PHE   C C     1 
ATOM   3863  O  O     . PHE   B 1  53  ? 16.394  47.863  -11.012 1.00 30.21  ? 53  PHE   C O     1 
ATOM   3864  C  CB    . PHE   B 1  53  ? 14.178  46.269  -12.092 1.00 29.91  ? 53  PHE   C CB    1 
ATOM   3865  C  CG    . PHE   B 1  53  ? 13.123  45.249  -12.208 1.00 30.08  ? 53  PHE   C CG    1 
ATOM   3866  C  CD1   . PHE   B 1  53  ? 13.009  44.493  -13.349 1.00 26.13  ? 53  PHE   C CD1   1 
ATOM   3867  C  CD2   . PHE   B 1  53  ? 12.229  45.052  -11.184 1.00 25.78  ? 53  PHE   C CD2   1 
ATOM   3868  C  CE1   . PHE   B 1  53  ? 12.027  43.540  -13.455 1.00 33.81  ? 53  PHE   C CE1   1 
ATOM   3869  C  CE2   . PHE   B 1  53  ? 11.255  44.109  -11.280 1.00 24.14  ? 53  PHE   C CE2   1 
ATOM   3870  C  CZ    . PHE   B 1  53  ? 11.149  43.339  -12.420 1.00 28.10  ? 53  PHE   C CZ    1 
ATOM   3871  N  N     . SER   B 1  54  ? 17.606  46.648  -12.491 1.00 33.64  ? 54  SER   C N     1 
ATOM   3872  C  CA    . SER   B 1  54  ? 18.380  47.805  -12.909 1.00 35.02  ? 54  SER   C CA    1 
ATOM   3873  C  C     . SER   B 1  54  ? 17.579  48.571  -13.962 1.00 47.98  ? 54  SER   C C     1 
ATOM   3874  O  O     . SER   B 1  54  ? 16.583  48.070  -14.497 1.00 38.06  ? 54  SER   C O     1 
ATOM   3875  C  CB    . SER   B 1  54  ? 19.742  47.388  -13.451 1.00 31.22  ? 54  SER   C CB    1 
ATOM   3876  O  OG    . SER   B 1  54  ? 19.609  46.744  -14.706 1.00 49.02  ? 54  SER   C OG    1 
ATOM   3877  N  N     . GLU   B 1  55  ? 18.003  49.812  -14.229 1.00 52.52  ? 55  GLU   C N     1 
ATOM   3878  C  CA    . GLU   B 1  55  ? 17.399  50.670  -15.244 1.00 44.73  ? 55  GLU   C CA    1 
ATOM   3879  C  C     . GLU   B 1  55  ? 18.453  51.066  -16.278 1.00 50.95  ? 55  GLU   C C     1 
ATOM   3880  O  O     . GLU   B 1  55  ? 19.635  51.218  -15.947 1.00 53.20  ? 55  GLU   C O     1 
ATOM   3881  C  CB    . GLU   B 1  55  ? 16.800  51.951  -14.632 1.00 41.86  ? 55  GLU   C CB    1 
ATOM   3882  C  CG    . GLU   B 1  55  ? 15.894  51.822  -13.397 1.00 35.63  ? 55  GLU   C CG    1 
ATOM   3883  C  CD    . GLU   B 1  55  ? 15.120  53.127  -13.134 1.00 47.68  ? 55  GLU   C CD    1 
ATOM   3884  O  OE1   . GLU   B 1  55  ? 14.887  53.870  -14.102 1.00 58.98  ? 55  GLU   C OE1   1 
ATOM   3885  O  OE2   . GLU   B 1  55  ? 14.738  53.440  -11.987 1.00 50.12  ? 55  GLU   C OE2   1 
ATOM   3886  N  N     . THR   B 1  56  ? 18.026  51.228  -17.537 1.00 52.90  ? 56  THR   C N     1 
ATOM   3887  C  CA    . THR   B 1  56  ? 18.876  51.777  -18.594 1.00 48.34  ? 56  THR   C CA    1 
ATOM   3888  C  C     . THR   B 1  56  ? 18.514  53.230  -18.865 1.00 51.99  ? 56  THR   C C     1 
ATOM   3889  O  O     . THR   B 1  56  ? 17.362  53.646  -18.697 1.00 46.31  ? 56  THR   C O     1 
ATOM   3890  C  CB    . THR   B 1  56  ? 18.762  51.019  -19.927 1.00 44.90  ? 56  THR   C CB    1 
ATOM   3891  O  OG1   . THR   B 1  56  ? 17.453  51.208  -20.500 1.00 36.26  ? 56  THR   C OG1   1 
ATOM   3892  C  CG2   . THR   B 1  56  ? 19.084  49.539  -19.763 1.00 36.92  ? 56  THR   C CG2   1 
ATOM   3893  N  N     . GLY   B 1  57  ? 19.518  53.989  -19.311 1.00 54.90  ? 57  GLY   C N     1 
ATOM   3894  C  CA    . GLY   B 1  57  ? 19.321  55.352  -19.761 1.00 48.13  ? 57  GLY   C CA    1 
ATOM   3895  C  C     . GLY   B 1  57  ? 18.100  55.466  -20.645 1.00 49.80  ? 57  GLY   C C     1 
ATOM   3896  O  O     . GLY   B 1  57  ? 17.298  56.393  -20.481 1.00 58.03  ? 57  GLY   C O     1 
ATOM   3897  N  N     . ALA   B 1  58  ? 17.935  54.511  -21.577 1.00 40.68  ? 58  ALA   C N     1 
ATOM   3898  C  CA    . ALA   B 1  58  ? 16.747  54.424  -22.441 1.00 45.31  ? 58  ALA   C CA    1 
ATOM   3899  C  C     . ALA   B 1  58  ? 15.460  54.007  -21.693 1.00 52.92  ? 58  ALA   C C     1 
ATOM   3900  O  O     . ALA   B 1  58  ? 14.459  53.761  -22.400 1.00 50.28  ? 58  ALA   C O     1 
ATOM   3901  C  CB    . ALA   B 1  58  ? 16.991  53.447  -23.594 1.00 48.66  ? 58  ALA   C CB    1 
ATOM   3902  N  N     . GLY   B 1  59  ? 15.456  53.889  -20.362 1.00 50.00  ? 59  GLY   C N     1 
ATOM   3903  C  CA    . GLY   B 1  59  ? 14.245  53.619  -19.610 1.00 49.15  ? 59  GLY   C CA    1 
ATOM   3904  C  C     . GLY   B 1  59  ? 13.820  52.169  -19.522 1.00 51.55  ? 59  GLY   C C     1 
ATOM   3905  O  O     . GLY   B 1  59  ? 12.677  51.900  -19.124 1.00 45.81  ? 59  GLY   C O     1 
ATOM   3906  N  N     . LYS   B 1  60  ? 14.692  51.228  -19.883 1.00 43.70  ? 60  LYS   C N     1 
ATOM   3907  C  CA    . LYS   B 1  60  ? 14.380  49.815  -19.729 1.00 45.07  ? 60  LYS   C CA    1 
ATOM   3908  C  C     . LYS   B 1  60  ? 14.693  49.348  -18.309 1.00 49.25  ? 60  LYS   C C     1 
ATOM   3909  O  O     . LYS   B 1  60  ? 15.734  49.689  -17.737 1.00 44.64  ? 60  LYS   C O     1 
ATOM   3910  C  CB    . LYS   B 1  60  ? 15.163  48.974  -20.737 1.00 44.66  ? 60  LYS   C CB    1 
ATOM   3911  C  CG    . LYS   B 1  60  ? 14.819  47.500  -20.690 1.00 47.94  ? 60  LYS   C CG    1 
ATOM   3912  C  CD    . LYS   B 1  60  ? 15.880  46.662  -21.374 1.00 50.02  ? 60  LYS   C CD    1 
ATOM   3913  C  CE    . LYS   B 1  60  ? 15.528  46.366  -22.824 1.00 43.84  ? 60  LYS   C CE    1 
ATOM   3914  N  NZ    . LYS   B 1  60  ? 16.589  45.549  -23.494 1.00 38.91  ? 60  LYS   C NZ    1 
ATOM   3915  N  N     . HIS   B 1  61  ? 13.776  48.574  -17.738 1.00 49.35  ? 61  HIS   C N     1 
ATOM   3916  C  CA    . HIS   B 1  61  ? 13.985  47.949  -16.441 1.00 36.64  ? 61  HIS   C CA    1 
ATOM   3917  C  C     . HIS   B 1  61  ? 14.367  46.497  -16.683 1.00 38.70  ? 61  HIS   C C     1 
ATOM   3918  O  O     . HIS   B 1  61  ? 13.621  45.746  -17.330 1.00 46.48  ? 61  HIS   C O     1 
ATOM   3919  C  CB    . HIS   B 1  61  ? 12.746  48.081  -15.557 1.00 28.87  ? 61  HIS   C CB    1 
ATOM   3920  C  CG    . HIS   B 1  61  ? 12.393  49.502  -15.246 1.00 43.08  ? 61  HIS   C CG    1 
ATOM   3921  N  ND1   . HIS   B 1  61  ? 12.165  50.443  -16.230 1.00 43.38  ? 61  HIS   C ND1   1 
ATOM   3922  C  CD2   . HIS   B 1  61  ? 12.239  50.149  -14.066 1.00 43.38  ? 61  HIS   C CD2   1 
ATOM   3923  C  CE1   . HIS   B 1  61  ? 11.878  51.604  -15.670 1.00 36.35  ? 61  HIS   C CE1   1 
ATOM   3924  N  NE2   . HIS   B 1  61  ? 11.920  51.455  -14.359 1.00 41.57  ? 61  HIS   C NE2   1 
ATOM   3925  N  N     . VAL   B 1  62  ? 15.532  46.117  -16.176 1.00 29.85  ? 62  VAL   C N     1 
ATOM   3926  C  CA    . VAL   B 1  62  ? 16.216  44.888  -16.554 1.00 38.55  ? 62  VAL   C CA    1 
ATOM   3927  C  C     . VAL   B 1  62  ? 16.394  44.026  -15.306 1.00 33.66  ? 62  VAL   C C     1 
ATOM   3928  O  O     . VAL   B 1  62  ? 17.041  44.453  -14.347 1.00 33.19  ? 62  VAL   C O     1 
ATOM   3929  C  CB    . VAL   B 1  62  ? 17.573  45.196  -17.213 1.00 38.23  ? 62  VAL   C CB    1 
ATOM   3930  C  CG1   . VAL   B 1  62  ? 18.231  43.937  -17.740 1.00 27.99  ? 62  VAL   C CG1   1 
ATOM   3931  C  CG2   . VAL   B 1  62  ? 17.381  46.239  -18.323 1.00 43.71  ? 62  VAL   C CG2   1 
ATOM   3932  N  N     . PRO   B 1  63  ? 15.817  42.830  -15.252 1.00 30.94  ? 63  PRO   C N     1 
ATOM   3933  C  CA    . PRO   B 1  63  ? 16.004  41.974  -14.078 1.00 33.76  ? 63  PRO   C CA    1 
ATOM   3934  C  C     . PRO   B 1  63  ? 17.480  41.768  -13.751 1.00 30.69  ? 63  PRO   C C     1 
ATOM   3935  O  O     . PRO   B 1  63  ? 18.311  41.560  -14.640 1.00 25.57  ? 63  PRO   C O     1 
ATOM   3936  C  CB    . PRO   B 1  63  ? 15.329  40.660  -14.494 1.00 39.19  ? 63  PRO   C CB    1 
ATOM   3937  C  CG    . PRO   B 1  63  ? 14.297  41.066  -15.494 1.00 35.39  ? 63  PRO   C CG    1 
ATOM   3938  C  CD    . PRO   B 1  63  ? 14.877  42.241  -16.225 1.00 39.05  ? 63  PRO   C CD    1 
ATOM   3939  N  N     . ARG   B 1  64  ? 17.800  41.819  -12.451 1.00 27.22  ? 64  ARG   C N     1 
ATOM   3940  C  CA    . ARG   B 1  64  ? 19.154  41.539  -11.974 1.00 25.21  ? 64  ARG   C CA    1 
ATOM   3941  C  C     . ARG   B 1  64  ? 19.320  40.026  -11.840 1.00 22.91  ? 64  ARG   C C     1 
ATOM   3942  O  O     . ARG   B 1  64  ? 19.469  39.470  -10.755 1.00 35.97  ? 64  ARG   C O     1 
ATOM   3943  C  CB    . ARG   B 1  64  ? 19.429  42.248  -10.659 1.00 22.61  ? 64  ARG   C CB    1 
ATOM   3944  C  CG    . ARG   B 1  64  ? 19.138  43.730  -10.619 1.00 23.50  ? 64  ARG   C CG    1 
ATOM   3945  C  CD    . ARG   B 1  64  ? 19.693  44.294  -9.344  1.00 27.13  ? 64  ARG   C CD    1 
ATOM   3946  N  NE    . ARG   B 1  64  ? 19.341  45.689  -9.126  1.00 28.92  ? 64  ARG   C NE    1 
ATOM   3947  C  CZ    . ARG   B 1  64  ? 20.109  46.716  -9.465  1.00 30.06  ? 64  ARG   C CZ    1 
ATOM   3948  N  NH1   . ARG   B 1  64  ? 21.260  46.541  -10.096 1.00 30.64  ? 64  ARG   C NH1   1 
ATOM   3949  N  NH2   . ARG   B 1  64  ? 19.713  47.948  -9.162  1.00 23.79  ? 64  ARG   C NH2   1 
ATOM   3950  N  N     . ALA   B 1  65  ? 19.279  39.354  -12.985 1.00 29.35  ? 65  ALA   C N     1 
ATOM   3951  C  CA    . ALA   B 1  65  ? 19.145  37.906  -13.022 1.00 25.36  ? 65  ALA   C CA    1 
ATOM   3952  C  C     . ALA   B 1  65  ? 20.086  37.309  -14.055 1.00 27.32  ? 65  ALA   C C     1 
ATOM   3953  O  O     . ALA   B 1  65  ? 20.397  37.923  -15.073 1.00 29.27  ? 65  ALA   C O     1 
ATOM   3954  C  CB    . ALA   B 1  65  ? 17.704  37.497  -13.331 1.00 28.29  ? 65  ALA   C CB    1 
ATOM   3955  N  N     . VAL   B 1  66  ? 20.540  36.099  -13.772 1.00 34.74  ? 66  VAL   C N     1 
ATOM   3956  C  CA    . VAL   B 1  66  ? 21.284  35.287  -14.722 1.00 39.07  ? 66  VAL   C CA    1 
ATOM   3957  C  C     . VAL   B 1  66  ? 20.565  33.952  -14.855 1.00 34.41  ? 66  VAL   C C     1 
ATOM   3958  O  O     . VAL   B 1  66  ? 20.239  33.312  -13.851 1.00 33.04  ? 66  VAL   C O     1 
ATOM   3959  C  CB    . VAL   B 1  66  ? 22.746  35.087  -14.280 1.00 25.40  ? 66  VAL   C CB    1 
ATOM   3960  C  CG1   . VAL   B 1  66  ? 23.364  34.011  -15.098 1.00 31.50  ? 66  VAL   C CG1   1 
ATOM   3961  C  CG2   . VAL   B 1  66  ? 23.511  36.354  -14.498 1.00 26.75  ? 66  VAL   C CG2   1 
ATOM   3962  N  N     . PHE   B 1  67  ? 20.285  33.551  -16.082 1.00 32.53  ? 67  PHE   C N     1 
ATOM   3963  C  CA    . PHE   B 1  67  ? 19.787  32.211  -16.351 1.00 35.41  ? 67  PHE   C CA    1 
ATOM   3964  C  C     . PHE   B 1  67  ? 20.937  31.389  -16.903 1.00 32.88  ? 67  PHE   C C     1 
ATOM   3965  O  O     . PHE   B 1  67  ? 21.660  31.853  -17.782 1.00 39.71  ? 67  PHE   C O     1 
ATOM   3966  C  CB    . PHE   B 1  67  ? 18.628  32.234  -17.344 1.00 34.01  ? 67  PHE   C CB    1 
ATOM   3967  C  CG    . PHE   B 1  67  ? 17.401  32.934  -16.838 1.00 29.46  ? 67  PHE   C CG    1 
ATOM   3968  C  CD1   . PHE   B 1  67  ? 17.477  34.188  -16.289 1.00 31.78  ? 67  PHE   C CD1   1 
ATOM   3969  C  CD2   . PHE   B 1  67  ? 16.162  32.349  -16.965 1.00 32.42  ? 67  PHE   C CD2   1 
ATOM   3970  C  CE1   . PHE   B 1  67  ? 16.337  34.841  -15.852 1.00 42.49  ? 67  PHE   C CE1   1 
ATOM   3971  C  CE2   . PHE   B 1  67  ? 15.019  32.997  -16.537 1.00 35.71  ? 67  PHE   C CE2   1 
ATOM   3972  C  CZ    . PHE   B 1  67  ? 15.103  34.241  -15.972 1.00 36.96  ? 67  PHE   C CZ    1 
ATOM   3973  N  N     . VAL   B 1  68  ? 21.122  30.186  -16.379 1.00 28.88  ? 68  VAL   C N     1 
ATOM   3974  C  CA    A VAL   B 1  68  ? 22.207  29.308  -16.804 0.31 29.65  ? 68  VAL   C CA    1 
ATOM   3975  C  CA    B VAL   B 1  68  ? 22.195  29.314  -16.835 0.69 30.02  ? 68  VAL   C CA    1 
ATOM   3976  C  C     . VAL   B 1  68  ? 21.662  27.895  -16.940 1.00 29.95  ? 68  VAL   C C     1 
ATOM   3977  O  O     . VAL   B 1  68  ? 21.005  27.389  -16.025 1.00 33.67  ? 68  VAL   C O     1 
ATOM   3978  C  CB    A VAL   B 1  68  ? 23.385  29.330  -15.812 0.31 31.43  ? 68  VAL   C CB    1 
ATOM   3979  C  CB    B VAL   B 1  68  ? 23.424  29.371  -15.909 0.69 31.46  ? 68  VAL   C CB    1 
ATOM   3980  C  CG1   A VAL   B 1  68  ? 24.526  28.467  -16.328 0.31 28.81  ? 68  VAL   C CG1   1 
ATOM   3981  C  CG1   B VAL   B 1  68  ? 22.992  29.332  -14.460 0.69 29.88  ? 68  VAL   C CG1   1 
ATOM   3982  C  CG2   A VAL   B 1  68  ? 23.838  30.757  -15.561 0.31 30.39  ? 68  VAL   C CG2   1 
ATOM   3983  C  CG2   B VAL   B 1  68  ? 24.362  28.220  -16.219 0.69 28.34  ? 68  VAL   C CG2   1 
ATOM   3984  N  N     . ASP   B 1  69  ? 21.932  27.265  -18.065 1.00 34.97  ? 69  ASP   C N     1 
ATOM   3985  C  CA    . ASP   B 1  69  ? 21.566  25.885  -18.330 1.00 31.82  ? 69  ASP   C CA    1 
ATOM   3986  C  C     . ASP   B 1  69  ? 22.694  25.281  -19.148 1.00 31.82  ? 69  ASP   C C     1 
ATOM   3987  O  O     . ASP   B 1  69  ? 23.407  25.987  -19.870 1.00 29.47  ? 69  ASP   C O     1 
ATOM   3988  C  CB    . ASP   B 1  69  ? 20.233  25.783  -19.074 1.00 26.99  ? 69  ASP   C CB    1 
ATOM   3989  C  CG    . ASP   B 1  69  ? 19.557  24.449  -18.871 1.00 33.63  ? 69  ASP   C CG    1 
ATOM   3990  O  OD1   . ASP   B 1  69  ? 20.048  23.687  -18.016 1.00 31.23  ? 69  ASP   C OD1   1 
ATOM   3991  O  OD2   . ASP   B 1  69  ? 18.551  24.156  -19.576 1.00 38.24  ? 69  ASP   C OD2   1 
ATOM   3992  N  N     . LEU   B 1  70  ? 22.884  23.987  -18.998 1.00 25.65  ? 70  LEU   C N     1 
ATOM   3993  C  CA    . LEU   B 1  70  ? 23.941  23.314  -19.728 1.00 29.82  ? 70  LEU   C CA    1 
ATOM   3994  C  C     . LEU   B 1  70  ? 23.491  22.822  -21.106 1.00 31.60  ? 70  LEU   C C     1 
ATOM   3995  O  O     . LEU   B 1  70  ? 24.282  22.196  -21.818 1.00 34.90  ? 70  LEU   C O     1 
ATOM   3996  C  CB    . LEU   B 1  70  ? 24.487  22.165  -18.879 1.00 26.35  ? 70  LEU   C CB    1 
ATOM   3997  C  CG    . LEU   B 1  70  ? 25.267  22.660  -17.676 1.00 31.58  ? 70  LEU   C CG    1 
ATOM   3998  C  CD1   . LEU   B 1  70  ? 26.384  21.705  -17.292 1.00 31.48  ? 70  LEU   C CD1   1 
ATOM   3999  C  CD2   . LEU   B 1  70  ? 25.833  24.020  -18.036 1.00 33.99  ? 70  LEU   C CD2   1 
ATOM   4000  N  N     . GLU   B 1  71  ? 22.249  23.081  -21.489 1.00 34.56  ? 71  GLU   C N     1 
ATOM   4001  C  CA    . GLU   B 1  71  ? 21.744  22.848  -22.832 1.00 36.98  ? 71  GLU   C CA    1 
ATOM   4002  C  C     . GLU   B 1  71  ? 20.886  24.043  -23.213 1.00 37.74  ? 71  GLU   C C     1 
ATOM   4003  O  O     . GLU   B 1  71  ? 20.429  24.785  -22.338 1.00 40.62  ? 71  GLU   C O     1 
ATOM   4004  C  CB    . GLU   B 1  71  ? 20.943  21.543  -22.933 1.00 41.10  ? 71  GLU   C CB    1 
ATOM   4005  C  CG    . GLU   B 1  71  ? 19.764  21.434  -21.997 1.00 32.23  ? 71  GLU   C CG    1 
ATOM   4006  C  CD    . GLU   B 1  71  ? 18.419  21.498  -22.722 1.00 41.89  ? 71  GLU   C CD    1 
ATOM   4007  O  OE1   . GLU   B 1  71  ? 18.398  21.898  -23.916 1.00 38.23  ? 71  GLU   C OE1   1 
ATOM   4008  O  OE2   . GLU   B 1  71  ? 17.381  21.147  -22.095 1.00 47.50  ? 71  GLU   C OE2   1 
ATOM   4009  N  N     . PRO   B 1  72  ? 20.679  24.279  -24.508 1.00 45.15  ? 72  PRO   C N     1 
ATOM   4010  C  CA    . PRO   B 1  72  ? 20.094  25.564  -24.920 1.00 39.45  ? 72  PRO   C CA    1 
ATOM   4011  C  C     . PRO   B 1  72  ? 18.580  25.605  -24.980 1.00 37.30  ? 72  PRO   C C     1 
ATOM   4012  O  O     . PRO   B 1  72  ? 18.000  26.686  -24.864 1.00 40.70  ? 72  PRO   C O     1 
ATOM   4013  C  CB    . PRO   B 1  72  ? 20.691  25.782  -26.317 1.00 34.56  ? 72  PRO   C CB    1 
ATOM   4014  C  CG    . PRO   B 1  72  ? 20.875  24.426  -26.838 1.00 28.81  ? 72  PRO   C CG    1 
ATOM   4015  C  CD    . PRO   B 1  72  ? 21.301  23.578  -25.647 1.00 43.40  ? 72  PRO   C CD    1 
ATOM   4016  N  N     . THR   B 1  73  ? 17.910  24.471  -25.160 1.00 35.11  ? 73  THR   C N     1 
ATOM   4017  C  CA    . THR   B 1  73  ? 16.535  24.560  -25.639 1.00 37.48  ? 73  THR   C CA    1 
ATOM   4018  C  C     . THR   B 1  73  ? 15.598  25.249  -24.654 1.00 35.88  ? 73  THR   C C     1 
ATOM   4019  O  O     . THR   B 1  73  ? 14.627  25.881  -25.092 1.00 42.07  ? 73  THR   C O     1 
ATOM   4020  C  CB    . THR   B 1  73  ? 16.005  23.181  -25.994 1.00 41.90  ? 73  THR   C CB    1 
ATOM   4021  O  OG1   . THR   B 1  73  ? 15.900  22.396  -24.809 1.00 34.89  ? 73  THR   C OG1   1 
ATOM   4022  C  CG2   . THR   B 1  73  ? 16.944  22.510  -26.989 1.00 42.77  ? 73  THR   C CG2   1 
ATOM   4023  N  N     . VAL   B 1  74  ? 15.845  25.147  -23.337 1.00 41.39  ? 74  VAL   C N     1 
ATOM   4024  C  CA    . VAL   B 1  74  ? 14.936  25.785  -22.373 1.00 35.01  ? 74  VAL   C CA    1 
ATOM   4025  C  C     . VAL   B 1  74  ? 15.184  27.284  -22.301 1.00 36.43  ? 74  VAL   C C     1 
ATOM   4026  O  O     . VAL   B 1  74  ? 14.239  28.079  -22.236 1.00 36.90  ? 74  VAL   C O     1 
ATOM   4027  C  CB    . VAL   B 1  74  ? 15.044  25.156  -20.972 1.00 34.33  ? 74  VAL   C CB    1 
ATOM   4028  C  CG1   . VAL   B 1  74  ? 14.107  25.860  -20.034 1.00 26.50  ? 74  VAL   C CG1   1 
ATOM   4029  C  CG2   . VAL   B 1  74  ? 14.724  23.688  -21.005 1.00 39.76  ? 74  VAL   C CG2   1 
ATOM   4030  N  N     . ILE   B 1  75  ? 16.450  27.707  -22.307 1.00 35.18  ? 75  ILE   C N     1 
ATOM   4031  C  CA    . ILE   B 1  75  ? 16.716  29.141  -22.290 1.00 31.53  ? 75  ILE   C CA    1 
ATOM   4032  C  C     . ILE   B 1  75  ? 16.370  29.778  -23.642 1.00 35.87  ? 75  ILE   C C     1 
ATOM   4033  O  O     . ILE   B 1  75  ? 15.836  30.890  -23.681 1.00 42.63  ? 75  ILE   C O     1 
ATOM   4034  C  CB    . ILE   B 1  75  ? 18.166  29.403  -21.830 1.00 32.71  ? 75  ILE   C CB    1 
ATOM   4035  C  CG1   . ILE   B 1  75  ? 18.179  29.512  -20.293 1.00 29.37  ? 75  ILE   C CG1   1 
ATOM   4036  C  CG2   . ILE   B 1  75  ? 18.768  30.666  -22.472 1.00 28.76  ? 75  ILE   C CG2   1 
ATOM   4037  C  CD1   . ILE   B 1  75  ? 19.548  29.357  -19.647 1.00 35.26  ? 75  ILE   C CD1   1 
ATOM   4038  N  N     . ASP   B 1  76  ? 16.615  29.073  -24.763 1.00 35.53  ? 76  ASP   C N     1 
ATOM   4039  C  CA    . ASP   B 1  76  ? 16.179  29.559  -26.080 1.00 35.12  ? 76  ASP   C CA    1 
ATOM   4040  C  C     . ASP   B 1  76  ? 14.718  29.974  -26.057 1.00 35.22  ? 76  ASP   C C     1 
ATOM   4041  O  O     . ASP   B 1  76  ? 14.316  30.937  -26.719 1.00 43.27  ? 76  ASP   C O     1 
ATOM   4042  C  CB    . ASP   B 1  76  ? 16.365  28.488  -27.169 1.00 29.77  ? 76  ASP   C CB    1 
ATOM   4043  C  CG    . ASP   B 1  76  ? 17.818  28.317  -27.615 1.00 40.56  ? 76  ASP   C CG    1 
ATOM   4044  O  OD1   . ASP   B 1  76  ? 18.615  29.267  -27.473 1.00 43.87  ? 76  ASP   C OD1   1 
ATOM   4045  O  OD2   . ASP   B 1  76  ? 18.168  27.224  -28.122 1.00 40.18  ? 76  ASP   C OD2   1 
ATOM   4046  N  N     . GLU   B 1  77  ? 13.900  29.229  -25.335 1.00 31.24  ? 77  GLU   C N     1 
ATOM   4047  C  CA    . GLU   B 1  77  ? 12.490  29.554  -25.264 1.00 43.41  ? 77  GLU   C CA    1 
ATOM   4048  C  C     . GLU   B 1  77  ? 12.256  30.871  -24.541 1.00 47.63  ? 77  GLU   C C     1 
ATOM   4049  O  O     . GLU   B 1  77  ? 11.184  31.468  -24.696 1.00 49.78  ? 77  GLU   C O     1 
ATOM   4050  C  CB    . GLU   B 1  77  ? 11.734  28.408  -24.591 1.00 27.56  ? 77  GLU   C CB    1 
ATOM   4051  C  CG    . GLU   B 1  77  ? 10.737  27.751  -25.501 1.00 39.60  ? 77  GLU   C CG    1 
ATOM   4052  C  CD    . GLU   B 1  77  ? 10.402  26.363  -25.034 1.00 61.05  ? 77  GLU   C CD    1 
ATOM   4053  O  OE1   . GLU   B 1  77  ? 11.285  25.483  -25.126 1.00 58.01  ? 77  GLU   C OE1   1 
ATOM   4054  O  OE2   . GLU   B 1  77  ? 9.269   26.158  -24.547 1.00 64.98  ? 77  GLU   C OE2   1 
ATOM   4055  N  N     . VAL   B 1  78  ? 13.229  31.325  -23.751 1.00 35.51  ? 78  VAL   C N     1 
ATOM   4056  C  CA    . VAL   B 1  78  ? 13.185  32.680  -23.215 1.00 39.00  ? 78  VAL   C CA    1 
ATOM   4057  C  C     . VAL   B 1  78  ? 13.571  33.682  -24.290 1.00 44.64  ? 78  VAL   C C     1 
ATOM   4058  O  O     . VAL   B 1  78  ? 12.815  34.610  -24.599 1.00 51.56  ? 78  VAL   C O     1 
ATOM   4059  C  CB    . VAL   B 1  78  ? 14.109  32.813  -21.992 1.00 39.19  ? 78  VAL   C CB    1 
ATOM   4060  C  CG1   . VAL   B 1  78  ? 14.172  34.258  -21.560 1.00 26.70  ? 78  VAL   C CG1   1 
ATOM   4061  C  CG2   . VAL   B 1  78  ? 13.656  31.892  -20.852 1.00 34.94  ? 78  VAL   C CG2   1 
ATOM   4062  N  N     . ARG   B 1  79  ? 14.750  33.483  -24.885 1.00 41.08  ? 79  ARG   C N     1 
ATOM   4063  C  CA    . ARG   B 1  79  ? 15.338  34.347  -25.903 1.00 34.90  ? 79  ARG   C CA    1 
ATOM   4064  C  C     . ARG   B 1  79  ? 14.321  34.788  -26.945 1.00 43.14  ? 79  ARG   C C     1 
ATOM   4065  O  O     . ARG   B 1  79  ? 14.385  35.922  -27.428 1.00 44.58  ? 79  ARG   C O     1 
ATOM   4066  C  CB    . ARG   B 1  79  ? 16.512  33.631  -26.577 1.00 36.88  ? 79  ARG   C CB    1 
ATOM   4067  C  CG    . ARG   B 1  79  ? 17.694  33.314  -25.634 1.00 35.82  ? 79  ARG   C CG    1 
ATOM   4068  C  CD    . ARG   B 1  79  ? 18.784  32.488  -26.324 1.00 29.85  ? 79  ARG   C CD    1 
ATOM   4069  N  NE    . ARG   B 1  79  ? 20.066  32.537  -25.623 1.00 38.11  ? 79  ARG   C NE    1 
ATOM   4070  C  CZ    . ARG   B 1  79  ? 20.773  31.470  -25.266 1.00 40.07  ? 79  ARG   C CZ    1 
ATOM   4071  N  NH1   . ARG   B 1  79  ? 20.361  30.243  -25.545 1.00 35.54  ? 79  ARG   C NH1   1 
ATOM   4072  N  NH2   . ARG   B 1  79  ? 21.932  31.640  -24.625 1.00 31.97  ? 79  ARG   C NH2   1 
ATOM   4073  N  N     . THR   B 1  80  ? 13.361  33.918  -27.279 1.00 50.65  ? 80  THR   C N     1 
ATOM   4074  C  CA    . THR   B 1  80  ? 12.432  34.171  -28.375 1.00 45.79  ? 80  THR   C CA    1 
ATOM   4075  C  C     . THR   B 1  80  ? 10.995  34.438  -27.938 1.00 50.98  ? 80  THR   C C     1 
ATOM   4076  O  O     . THR   B 1  80  ? 10.171  34.798  -28.794 1.00 54.53  ? 80  THR   C O     1 
ATOM   4077  C  CB    . THR   B 1  80  ? 12.443  32.988  -29.365 1.00 45.59  ? 80  THR   C CB    1 
ATOM   4078  O  OG1   . THR   B 1  80  ? 11.996  31.793  -28.709 1.00 45.77  ? 80  THR   C OG1   1 
ATOM   4079  C  CG2   . THR   B 1  80  ? 13.847  32.761  -29.905 1.00 41.55  ? 80  THR   C CG2   1 
ATOM   4080  N  N     . GLY   B 1  81  ? 10.666  34.269  -26.651 1.00 48.83  ? 81  GLY   C N     1 
ATOM   4081  C  CA    . GLY   B 1  81  ? 9.304   34.406  -26.165 1.00 31.71  ? 81  GLY   C CA    1 
ATOM   4082  C  C     . GLY   B 1  81  ? 8.980   35.819  -25.735 1.00 52.82  ? 81  GLY   C C     1 
ATOM   4083  O  O     . GLY   B 1  81  ? 9.655   36.783  -26.105 1.00 54.39  ? 81  GLY   C O     1 
ATOM   4084  N  N     . THR   B 1  82  ? 7.947   35.932  -24.894 1.00 53.08  ? 82  THR   C N     1 
ATOM   4085  C  CA    . THR   B 1  82  ? 7.326   37.225  -24.606 1.00 44.87  ? 82  THR   C CA    1 
ATOM   4086  C  C     . THR   B 1  82  ? 8.244   38.217  -23.885 1.00 59.23  ? 82  THR   C C     1 
ATOM   4087  O  O     . THR   B 1  82  ? 7.999   39.431  -23.945 1.00 50.12  ? 82  THR   C O     1 
ATOM   4088  C  CB    . THR   B 1  82  ? 6.060   37.004  -23.781 1.00 51.51  ? 82  THR   C CB    1 
ATOM   4089  O  OG1   . THR   B 1  82  ? 5.124   36.249  -24.559 1.00 64.95  ? 82  THR   C OG1   1 
ATOM   4090  C  CG2   . THR   B 1  82  ? 5.430   38.337  -23.384 1.00 46.39  ? 82  THR   C CG2   1 
ATOM   4091  N  N     . TYR   B 1  83  ? 9.286   37.754  -23.197 1.00 52.82  ? 83  TYR   C N     1 
ATOM   4092  C  CA    . TYR   B 1  83  ? 10.142  38.680  -22.471 1.00 43.62  ? 83  TYR   C CA    1 
ATOM   4093  C  C     . TYR   B 1  83  ? 11.566  38.697  -23.002 1.00 51.85  ? 83  TYR   C C     1 
ATOM   4094  O  O     . TYR   B 1  83  ? 12.484  39.061  -22.266 1.00 55.64  ? 83  TYR   C O     1 
ATOM   4095  C  CB    . TYR   B 1  83  ? 10.131  38.352  -20.984 1.00 43.64  ? 83  TYR   C CB    1 
ATOM   4096  C  CG    . TYR   B 1  83  ? 8.778   38.581  -20.370 1.00 43.32  ? 83  TYR   C CG    1 
ATOM   4097  C  CD1   . TYR   B 1  83  ? 7.777   37.626  -20.493 1.00 43.07  ? 83  TYR   C CD1   1 
ATOM   4098  C  CD2   . TYR   B 1  83  ? 8.487   39.766  -19.695 1.00 35.33  ? 83  TYR   C CD2   1 
ATOM   4099  C  CE1   . TYR   B 1  83  ? 6.507   37.826  -19.936 1.00 43.39  ? 83  TYR   C CE1   1 
ATOM   4100  C  CE2   . TYR   B 1  83  ? 7.226   39.982  -19.138 1.00 39.23  ? 83  TYR   C CE2   1 
ATOM   4101  C  CZ    . TYR   B 1  83  ? 6.237   38.999  -19.261 1.00 46.02  ? 83  TYR   C CZ    1 
ATOM   4102  O  OH    . TYR   B 1  83  ? 4.974   39.182  -18.719 1.00 55.00  ? 83  TYR   C OH    1 
ATOM   4103  N  N     . ARG   B 1  84  ? 11.773  38.323  -24.267 1.00 50.20  ? 84  ARG   C N     1 
ATOM   4104  C  CA    . ARG   B 1  84  ? 13.116  38.371  -24.834 1.00 50.40  ? 84  ARG   C CA    1 
ATOM   4105  C  C     . ARG   B 1  84  ? 13.765  39.733  -24.621 1.00 52.31  ? 84  ARG   C C     1 
ATOM   4106  O  O     . ARG   B 1  84  ? 14.955  39.818  -24.293 1.00 51.46  ? 84  ARG   C O     1 
ATOM   4107  C  CB    . ARG   B 1  84  ? 13.080  38.022  -26.324 1.00 51.30  ? 84  ARG   C CB    1 
ATOM   4108  C  CG    . ARG   B 1  84  ? 12.184  38.896  -27.157 1.00 51.70  ? 84  ARG   C CG    1 
ATOM   4109  C  CD    . ARG   B 1  84  ? 11.855  38.261  -28.506 1.00 54.39  ? 84  ARG   C CD    1 
ATOM   4110  N  NE    . ARG   B 1  84  ? 10.438  38.436  -28.791 1.00 63.53  ? 84  ARG   C NE    1 
ATOM   4111  C  CZ    . ARG   B 1  84  ? 9.898   39.549  -29.270 1.00 73.42  ? 84  ARG   C CZ    1 
ATOM   4112  N  NH1   . ARG   B 1  84  ? 10.648  40.573  -29.649 1.00 71.57  ? 84  ARG   C NH1   1 
ATOM   4113  N  NH2   . ARG   B 1  84  ? 8.572   39.642  -29.358 1.00 72.12  ? 84  ARG   C NH2   1 
ATOM   4114  N  N     . GLN   B 1  85  ? 12.997  40.813  -24.797 1.00 49.09  ? 85  GLN   C N     1 
ATOM   4115  C  CA    . GLN   B 1  85  ? 13.553  42.154  -24.647 1.00 47.94  ? 85  GLN   C CA    1 
ATOM   4116  C  C     . GLN   B 1  85  ? 13.907  42.473  -23.202 1.00 48.40  ? 85  GLN   C C     1 
ATOM   4117  O  O     . GLN   B 1  85  ? 14.642  43.439  -22.946 1.00 44.74  ? 85  GLN   C O     1 
ATOM   4118  C  CB    . GLN   B 1  85  ? 12.570  43.205  -25.172 1.00 52.02  ? 85  GLN   C CB    1 
ATOM   4119  C  CG    . GLN   B 1  85  ? 12.472  43.318  -26.697 1.00 58.39  ? 85  GLN   C CG    1 
ATOM   4120  C  CD    . GLN   B 1  85  ? 11.241  44.106  -27.133 1.00 66.94  ? 85  GLN   C CD    1 
ATOM   4121  O  OE1   . GLN   B 1  85  ? 11.316  45.314  -27.412 1.00 51.71  ? 85  GLN   C OE1   1 
ATOM   4122  N  NE2   . GLN   B 1  85  ? 10.091  43.424  -27.182 1.00 63.11  ? 85  GLN   C NE2   1 
ATOM   4123  N  N     . LEU   B 1  86  ? 13.403  41.688  -22.252 1.00 40.50  ? 86  LEU   C N     1 
ATOM   4124  C  CA    . LEU   B 1  86  ? 13.618  42.022  -20.848 1.00 43.84  ? 86  LEU   C CA    1 
ATOM   4125  C  C     . LEU   B 1  86  ? 15.060  41.787  -20.426 1.00 45.63  ? 86  LEU   C C     1 
ATOM   4126  O  O     . LEU   B 1  86  ? 15.547  42.462  -19.512 1.00 38.30  ? 86  LEU   C O     1 
ATOM   4127  C  CB    . LEU   B 1  86  ? 12.670  41.209  -19.969 1.00 49.12  ? 86  LEU   C CB    1 
ATOM   4128  C  CG    . LEU   B 1  86  ? 12.418  41.751  -18.574 1.00 45.37  ? 86  LEU   C CG    1 
ATOM   4129  C  CD1   . LEU   B 1  86  ? 12.366  43.276  -18.663 1.00 46.77  ? 86  LEU   C CD1   1 
ATOM   4130  C  CD2   . LEU   B 1  86  ? 11.121  41.150  -18.005 1.00 30.58  ? 86  LEU   C CD2   1 
ATOM   4131  N  N     . PHE   B 1  87  ? 15.759  40.860  -21.088 1.00 43.39  ? 87  PHE   C N     1 
ATOM   4132  C  CA    . PHE   B 1  87  ? 17.076  40.409  -20.664 1.00 41.68  ? 87  PHE   C CA    1 
ATOM   4133  C  C     . PHE   B 1  87  ? 18.114  40.769  -21.708 1.00 51.45  ? 87  PHE   C C     1 
ATOM   4134  O  O     . PHE   B 1  87  ? 17.917  40.503  -22.900 1.00 51.90  ? 87  PHE   C O     1 
ATOM   4135  C  CB    . PHE   B 1  87  ? 17.104  38.893  -20.452 1.00 45.23  ? 87  PHE   C CB    1 
ATOM   4136  C  CG    . PHE   B 1  87  ? 15.918  38.364  -19.720 1.00 39.98  ? 87  PHE   C CG    1 
ATOM   4137  C  CD1   . PHE   B 1  87  ? 14.759  38.063  -20.396 1.00 39.85  ? 87  PHE   C CD1   1 
ATOM   4138  C  CD2   . PHE   B 1  87  ? 15.958  38.187  -18.354 1.00 34.37  ? 87  PHE   C CD2   1 
ATOM   4139  C  CE1   . PHE   B 1  87  ? 13.662  37.588  -19.716 1.00 44.14  ? 87  PHE   C CE1   1 
ATOM   4140  C  CE2   . PHE   B 1  87  ? 14.870  37.709  -17.674 1.00 42.91  ? 87  PHE   C CE2   1 
ATOM   4141  C  CZ    . PHE   B 1  87  ? 13.722  37.405  -18.353 1.00 42.22  ? 87  PHE   C CZ    1 
ATOM   4142  N  N     . HIS   B 1  88  ? 19.227  41.342  -21.253 1.00 58.71  ? 88  HIS   C N     1 
ATOM   4143  C  CA    . HIS   B 1  88  ? 20.397  41.457  -22.108 1.00 51.32  ? 88  HIS   C CA    1 
ATOM   4144  C  C     . HIS   B 1  88  ? 20.853  40.056  -22.505 1.00 50.20  ? 88  HIS   C C     1 
ATOM   4145  O  O     . HIS   B 1  88  ? 20.844  39.140  -21.675 1.00 44.85  ? 88  HIS   C O     1 
ATOM   4146  C  CB    . HIS   B 1  88  ? 21.535  42.200  -21.397 1.00 46.22  ? 88  HIS   C CB    1 
ATOM   4147  C  CG    . HIS   B 1  88  ? 22.724  42.469  -22.273 1.00 55.04  ? 88  HIS   C CG    1 
ATOM   4148  N  ND1   . HIS   B 1  88  ? 23.529  41.465  -22.771 1.00 54.55  ? 88  HIS   C ND1   1 
ATOM   4149  C  CD2   . HIS   B 1  88  ? 23.238  43.630  -22.749 1.00 59.41  ? 88  HIS   C CD2   1 
ATOM   4150  C  CE1   . HIS   B 1  88  ? 24.489  41.994  -23.510 1.00 56.76  ? 88  HIS   C CE1   1 
ATOM   4151  N  NE2   . HIS   B 1  88  ? 24.333  43.306  -23.516 1.00 61.44  ? 88  HIS   C NE2   1 
ATOM   4152  N  N     . PRO   B 1  89  ? 21.234  39.847  -23.756 1.00 51.84  ? 89  PRO   C N     1 
ATOM   4153  C  CA    . PRO   B 1  89  ? 21.693  38.513  -24.163 1.00 47.24  ? 89  PRO   C CA    1 
ATOM   4154  C  C     . PRO   B 1  89  ? 22.684  37.874  -23.209 1.00 43.18  ? 89  PRO   C C     1 
ATOM   4155  O  O     . PRO   B 1  89  ? 22.659  36.651  -23.037 1.00 49.11  ? 89  PRO   C O     1 
ATOM   4156  C  CB    . PRO   B 1  89  ? 22.311  38.791  -25.539 1.00 42.75  ? 89  PRO   C CB    1 
ATOM   4157  C  CG    . PRO   B 1  89  ? 21.417  39.831  -26.081 1.00 40.28  ? 89  PRO   C CG    1 
ATOM   4158  C  CD    . PRO   B 1  89  ? 21.094  40.748  -24.908 1.00 43.25  ? 89  PRO   C CD    1 
ATOM   4159  N  N     . GLU   B 1  90  ? 23.553  38.654  -22.573 1.00 45.54  ? 90  GLU   C N     1 
ATOM   4160  C  CA    . GLU   B 1  90  ? 24.608  38.065  -21.758 1.00 45.05  ? 90  GLU   C CA    1 
ATOM   4161  C  C     . GLU   B 1  90  ? 24.108  37.488  -20.443 1.00 47.92  ? 90  GLU   C C     1 
ATOM   4162  O  O     . GLU   B 1  90  ? 24.865  36.752  -19.797 1.00 42.48  ? 90  GLU   C O     1 
ATOM   4163  C  CB    . GLU   B 1  90  ? 25.700  39.100  -21.485 1.00 50.90  ? 90  GLU   C CB    1 
ATOM   4164  C  CG    . GLU   B 1  90  ? 26.598  39.362  -22.686 1.00 64.63  ? 90  GLU   C CG    1 
ATOM   4165  C  CD    . GLU   B 1  90  ? 27.566  40.509  -22.461 1.00 71.59  ? 90  GLU   C CD    1 
ATOM   4166  O  OE1   . GLU   B 1  90  ? 27.999  40.713  -21.304 1.00 72.89  ? 90  GLU   C OE1   1 
ATOM   4167  O  OE2   . GLU   B 1  90  ? 27.889  41.210  -23.445 1.00 76.30  ? 90  GLU   C OE2   1 
ATOM   4168  N  N     . GLN   B 1  91  ? 22.875  37.812  -20.019 1.00 47.43  ? 91  GLN   C N     1 
ATOM   4169  C  CA    . GLN   B 1  91  ? 22.271  37.186  -18.841 1.00 44.74  ? 91  GLN   C CA    1 
ATOM   4170  C  C     . GLN   B 1  91  ? 21.622  35.842  -19.146 1.00 48.63  ? 91  GLN   C C     1 
ATOM   4171  O  O     . GLN   B 1  91  ? 20.997  35.265  -18.246 1.00 48.13  ? 91  GLN   C O     1 
ATOM   4172  C  CB    . GLN   B 1  91  ? 21.196  38.074  -18.220 1.00 34.51  ? 91  GLN   C CB    1 
ATOM   4173  C  CG    . GLN   B 1  91  ? 21.556  39.495  -18.025 1.00 37.27  ? 91  GLN   C CG    1 
ATOM   4174  C  CD    . GLN   B 1  91  ? 20.333  40.323  -17.726 1.00 40.87  ? 91  GLN   C CD    1 
ATOM   4175  O  OE1   . GLN   B 1  91  ? 19.979  41.223  -18.484 1.00 32.86  ? 91  GLN   C OE1   1 
ATOM   4176  N  NE2   . GLN   B 1  91  ? 19.665  40.009  -16.622 1.00 33.57  ? 91  GLN   C NE2   1 
ATOM   4177  N  N     . LEU   B 1  92  ? 21.718  35.360  -20.388 1.00 39.25  ? 92  LEU   C N     1 
ATOM   4178  C  CA    . LEU   B 1  92  ? 21.083  34.125  -20.833 1.00 34.63  ? 92  LEU   C CA    1 
ATOM   4179  C  C     . LEU   B 1  92  ? 22.177  33.215  -21.407 1.00 43.48  ? 92  LEU   C C     1 
ATOM   4180  O  O     . LEU   B 1  92  ? 22.532  33.322  -22.587 1.00 46.57  ? 92  LEU   C O     1 
ATOM   4181  C  CB    . LEU   B 1  92  ? 19.981  34.428  -21.851 1.00 37.24  ? 92  LEU   C CB    1 
ATOM   4182  C  CG    . LEU   B 1  92  ? 18.813  35.375  -21.523 1.00 38.82  ? 92  LEU   C CG    1 
ATOM   4183  C  CD1   . LEU   B 1  92  ? 17.827  35.269  -22.642 1.00 34.92  ? 92  LEU   C CD1   1 
ATOM   4184  C  CD2   . LEU   B 1  92  ? 18.098  35.091  -20.180 1.00 36.56  ? 92  LEU   C CD2   1 
ATOM   4185  N  N     . ILE   B 1  93  ? 22.670  32.296  -20.575 1.00 39.77  ? 93  ILE   C N     1 
ATOM   4186  C  CA    . ILE   B 1  93  ? 23.898  31.538  -20.793 1.00 27.68  ? 93  ILE   C CA    1 
ATOM   4187  C  C     . ILE   B 1  93  ? 23.543  30.073  -20.946 1.00 35.00  ? 93  ILE   C C     1 
ATOM   4188  O  O     . ILE   B 1  93  ? 22.983  29.478  -20.024 1.00 39.62  ? 93  ILE   C O     1 
ATOM   4189  C  CB    . ILE   B 1  93  ? 24.863  31.695  -19.613 1.00 30.08  ? 93  ILE   C CB    1 
ATOM   4190  C  CG1   . ILE   B 1  93  ? 24.977  33.164  -19.211 1.00 34.57  ? 93  ILE   C CG1   1 
ATOM   4191  C  CG2   . ILE   B 1  93  ? 26.212  30.998  -19.883 1.00 21.48  ? 93  ILE   C CG2   1 
ATOM   4192  C  CD1   . ILE   B 1  93  ? 26.061  33.426  -18.206 1.00 34.54  ? 93  ILE   C CD1   1 
ATOM   4193  N  N     . THR   B 1  94  ? 23.936  29.469  -22.064 1.00 42.52  ? 94  THR   C N     1 
ATOM   4194  C  CA    . THR   B 1  94  ? 23.673  28.057  -22.301 1.00 36.62  ? 94  THR   C CA    1 
ATOM   4195  C  C     . THR   B 1  94  ? 24.917  27.350  -22.818 1.00 26.32  ? 94  THR   C C     1 
ATOM   4196  O  O     . THR   B 1  94  ? 25.770  27.959  -23.455 1.00 42.44  ? 94  THR   C O     1 
ATOM   4197  C  CB    . THR   B 1  94  ? 22.529  27.859  -23.312 1.00 46.99  ? 94  THR   C CB    1 
ATOM   4198  O  OG1   . THR   B 1  94  ? 22.915  28.388  -24.590 1.00 41.40  ? 94  THR   C OG1   1 
ATOM   4199  C  CG2   . THR   B 1  94  ? 21.229  28.527  -22.817 1.00 32.27  ? 94  THR   C CG2   1 
ATOM   4200  N  N     . GLY   B 1  95  ? 25.010  26.053  -22.525 1.00 34.48  ? 95  GLY   C N     1 
ATOM   4201  C  CA    . GLY   B 1  95  ? 25.950  25.169  -23.178 1.00 35.26  ? 95  GLY   C CA    1 
ATOM   4202  C  C     . GLY   B 1  95  ? 25.302  24.381  -24.314 1.00 43.49  ? 95  GLY   C C     1 
ATOM   4203  O  O     . GLY   B 1  95  ? 24.192  24.668  -24.770 1.00 43.12  ? 95  GLY   C O     1 
ATOM   4204  N  N     . LYS   B 1  96  ? 26.007  23.341  -24.761 1.00 40.45  ? 96  LYS   C N     1 
ATOM   4205  C  CA    . LYS   B 1  96  ? 25.527  22.530  -25.873 1.00 50.25  ? 96  LYS   C CA    1 
ATOM   4206  C  C     . LYS   B 1  96  ? 25.099  21.119  -25.485 1.00 46.81  ? 96  LYS   C C     1 
ATOM   4207  O  O     . LYS   B 1  96  ? 24.418  20.464  -26.281 1.00 57.15  ? 96  LYS   C O     1 
ATOM   4208  C  CB    . LYS   B 1  96  ? 26.602  22.449  -26.974 1.00 49.38  ? 96  LYS   C CB    1 
ATOM   4209  C  CG    . LYS   B 1  96  ? 26.505  23.570  -28.007 1.00 38.90  ? 96  LYS   C CG    1 
ATOM   4210  C  CD    . LYS   B 1  96  ? 27.741  23.658  -28.919 1.00 40.90  ? 96  LYS   C CD    1 
ATOM   4211  C  CE    . LYS   B 1  96  ? 27.690  24.937  -29.773 1.00 51.62  ? 96  LYS   C CE    1 
ATOM   4212  N  NZ    . LYS   B 1  96  ? 26.380  25.120  -30.495 1.00 51.25  ? 96  LYS   C NZ    1 
ATOM   4213  N  N     . GLU   B 1  97  ? 25.448  20.648  -24.292 1.00 37.45  ? 97  GLU   C N     1 
ATOM   4214  C  CA    . GLU   B 1  97  ? 25.271  19.254  -23.905 1.00 40.91  ? 97  GLU   C CA    1 
ATOM   4215  C  C     . GLU   B 1  97  ? 24.981  19.242  -22.415 1.00 37.60  ? 97  GLU   C C     1 
ATOM   4216  O  O     . GLU   B 1  97  ? 25.726  19.846  -21.642 1.00 44.91  ? 97  GLU   C O     1 
ATOM   4217  C  CB    . GLU   B 1  97  ? 26.532  18.435  -24.232 1.00 35.49  ? 97  GLU   C CB    1 
ATOM   4218  C  CG    . GLU   B 1  97  ? 26.548  17.013  -23.699 1.00 45.19  ? 97  GLU   C CG    1 
ATOM   4219  C  CD    . GLU   B 1  97  ? 27.810  16.241  -24.083 1.00 51.90  ? 97  GLU   C CD    1 
ATOM   4220  O  OE1   . GLU   B 1  97  ? 28.912  16.831  -24.094 1.00 61.21  ? 97  GLU   C OE1   1 
ATOM   4221  O  OE2   . GLU   B 1  97  ? 27.700  15.037  -24.381 1.00 55.98  ? 97  GLU   C OE2   1 
ATOM   4222  N  N     . ASP   B 1  98  ? 23.910  18.577  -22.002 1.00 35.55  ? 98  ASP   C N     1 
ATOM   4223  C  CA    . ASP   B 1  98  ? 23.454  18.822  -20.647 1.00 28.29  ? 98  ASP   C CA    1 
ATOM   4224  C  C     . ASP   B 1  98  ? 24.078  17.809  -19.686 1.00 30.31  ? 98  ASP   C C     1 
ATOM   4225  O  O     . ASP   B 1  98  ? 24.965  17.029  -20.050 1.00 34.09  ? 98  ASP   C O     1 
ATOM   4226  C  CB    . ASP   B 1  98  ? 21.917  18.879  -20.616 1.00 24.26  ? 98  ASP   C CB    1 
ATOM   4227  C  CG    . ASP   B 1  98  ? 21.245  17.520  -20.728 1.00 26.98  ? 98  ASP   C CG    1 
ATOM   4228  O  OD1   . ASP   B 1  98  ? 21.830  16.479  -20.348 1.00 28.92  ? 98  ASP   C OD1   1 
ATOM   4229  O  OD2   . ASP   B 1  98  ? 20.081  17.505  -21.165 1.00 25.98  ? 98  ASP   C OD2   1 
ATOM   4230  N  N     . ALA   B 1  99  ? 23.655  17.866  -18.422 1.00 25.49  ? 99  ALA   C N     1 
ATOM   4231  C  CA    . ALA   B 1  99  ? 24.304  17.074  -17.380 1.00 28.44  ? 99  ALA   C CA    1 
ATOM   4232  C  C     . ALA   B 1  99  ? 23.807  15.641  -17.342 1.00 23.50  ? 99  ALA   C C     1 
ATOM   4233  O  O     . ALA   B 1  99  ? 24.334  14.835  -16.559 1.00 29.17  ? 99  ALA   C O     1 
ATOM   4234  C  CB    . ALA   B 1  99  ? 24.112  17.737  -16.007 1.00 19.55  ? 99  ALA   C CB    1 
ATOM   4235  N  N     . ALA   B 1  100 ? 22.811  15.316  -18.165 1.00 15.87  ? 100 ALA   C N     1 
ATOM   4236  C  CA    . ALA   B 1  100 ? 22.235  13.963  -18.242 1.00 31.91  ? 100 ALA   C CA    1 
ATOM   4237  C  C     . ALA   B 1  100 ? 21.869  13.414  -16.856 1.00 31.99  ? 100 ALA   C C     1 
ATOM   4238  O  O     . ALA   B 1  100 ? 22.205  12.277  -16.498 1.00 30.10  ? 100 ALA   C O     1 
ATOM   4239  C  CB    . ALA   B 1  100 ? 23.181  13.003  -18.985 1.00 19.84  ? 100 ALA   C CB    1 
ATOM   4240  N  N     . ASN   B 1  101 ? 21.170  14.241  -16.069 1.00 27.21  ? 101 ASN   C N     1 
ATOM   4241  C  CA    . ASN   B 1  101 ? 20.649  13.831  -14.752 1.00 24.46  ? 101 ASN   C CA    1 
ATOM   4242  C  C     . ASN   B 1  101 ? 21.720  13.198  -13.882 1.00 28.08  ? 101 ASN   C C     1 
ATOM   4243  O  O     . ASN   B 1  101 ? 21.433  12.287  -13.103 1.00 35.99  ? 101 ASN   C O     1 
ATOM   4244  C  CB    . ASN   B 1  101 ? 19.473  12.868  -14.881 1.00 21.75  ? 101 ASN   C CB    1 
ATOM   4245  C  CG    . ASN   B 1  101 ? 18.295  13.490  -15.584 1.00 26.19  ? 101 ASN   C CG    1 
ATOM   4246  O  OD1   . ASN   B 1  101 ? 17.863  13.004  -16.622 1.00 28.91  ? 101 ASN   C OD1   1 
ATOM   4247  N  ND2   . ASN   B 1  101 ? 17.769  14.573  -15.023 1.00 31.88  ? 101 ASN   C ND2   1 
ATOM   4248  N  N     . ASN   B 1  102 ? 22.954  13.681  -14.006 1.00 26.05  ? 102 ASN   C N     1 
ATOM   4249  C  CA    . ASN   B 1  102 ? 24.107  13.142  -13.292 1.00 26.94  ? 102 ASN   C CA    1 
ATOM   4250  C  C     . ASN   B 1  102 ? 24.774  14.303  -12.563 1.00 31.43  ? 102 ASN   C C     1 
ATOM   4251  O  O     . ASN   B 1  102 ? 25.385  15.170  -13.200 1.00 34.51  ? 102 ASN   C O     1 
ATOM   4252  C  CB    . ASN   B 1  102 ? 25.072  12.456  -14.273 1.00 30.52  ? 102 ASN   C CB    1 
ATOM   4253  C  CG    . ASN   B 1  102 ? 26.246  11.755  -13.581 1.00 32.82  ? 102 ASN   C CG    1 
ATOM   4254  O  OD1   . ASN   B 1  102 ? 26.486  11.949  -12.393 1.00 32.01  ? 102 ASN   C OD1   1 
ATOM   4255  N  ND2   . ASN   B 1  102 ? 26.991  10.945  -14.339 1.00 32.73  ? 102 ASN   C ND2   1 
ATOM   4256  N  N     . TYR   B 1  103 ? 24.660  14.330  -11.231 1.00 32.95  ? 103 TYR   C N     1 
ATOM   4257  C  CA    . TYR   B 1  103 ? 25.299  15.395  -10.458 1.00 30.87  ? 103 TYR   C CA    1 
ATOM   4258  C  C     . TYR   B 1  103 ? 26.740  15.599  -10.893 1.00 31.75  ? 103 TYR   C C     1 
ATOM   4259  O  O     . TYR   B 1  103 ? 27.224  16.732  -10.951 1.00 32.56  ? 103 TYR   C O     1 
ATOM   4260  C  CB    . TYR   B 1  103 ? 25.226  15.077  -8.968  1.00 28.24  ? 103 TYR   C CB    1 
ATOM   4261  C  CG    . TYR   B 1  103 ? 26.048  15.957  -8.051  1.00 33.69  ? 103 TYR   C CG    1 
ATOM   4262  C  CD1   . TYR   B 1  103 ? 27.421  15.738  -7.890  1.00 41.12  ? 103 TYR   C CD1   1 
ATOM   4263  C  CD2   . TYR   B 1  103 ? 25.460  16.963  -7.295  1.00 32.67  ? 103 TYR   C CD2   1 
ATOM   4264  C  CE1   . TYR   B 1  103 ? 28.193  16.514  -7.033  1.00 24.84  ? 103 TYR   C CE1   1 
ATOM   4265  C  CE2   . TYR   B 1  103 ? 26.241  17.757  -6.424  1.00 36.41  ? 103 TYR   C CE2   1 
ATOM   4266  C  CZ    . TYR   B 1  103 ? 27.606  17.515  -6.305  1.00 27.28  ? 103 TYR   C CZ    1 
ATOM   4267  O  OH    . TYR   B 1  103 ? 28.396  18.269  -5.472  1.00 25.69  ? 103 TYR   C OH    1 
ATOM   4268  N  N     . ALA   B 1  104 ? 27.431  14.505  -11.238 1.00 40.30  ? 104 ALA   C N     1 
ATOM   4269  C  CA    . ALA   B 1  104 ? 28.844  14.583  -11.588 1.00 34.13  ? 104 ALA   C CA    1 
ATOM   4270  C  C     . ALA   B 1  104 ? 29.062  15.411  -12.845 1.00 35.37  ? 104 ALA   C C     1 
ATOM   4271  O  O     . ALA   B 1  104 ? 29.967  16.248  -12.900 1.00 31.30  ? 104 ALA   C O     1 
ATOM   4272  C  CB    . ALA   B 1  104 ? 29.403  13.180  -11.764 1.00 39.80  ? 104 ALA   C CB    1 
ATOM   4273  N  N     . ARG   B 1  105 ? 28.239  15.210  -13.865 1.00 38.69  ? 105 ARG   C N     1 
ATOM   4274  C  CA    . ARG   B 1  105 ? 28.424  16.017  -15.063 1.00 33.82  ? 105 ARG   C CA    1 
ATOM   4275  C  C     . ARG   B 1  105 ? 28.140  17.489  -14.783 1.00 35.10  ? 105 ARG   C C     1 
ATOM   4276  O  O     . ARG   B 1  105 ? 28.834  18.370  -15.309 1.00 38.28  ? 105 ARG   C O     1 
ATOM   4277  C  CB    . ARG   B 1  105 ? 27.552  15.473  -16.194 1.00 37.96  ? 105 ARG   C CB    1 
ATOM   4278  C  CG    . ARG   B 1  105 ? 28.037  14.125  -16.708 1.00 35.56  ? 105 ARG   C CG    1 
ATOM   4279  C  CD    . ARG   B 1  105 ? 27.068  13.512  -17.728 1.00 35.39  ? 105 ARG   C CD    1 
ATOM   4280  N  NE    . ARG   B 1  105 ? 27.080  14.235  -18.989 1.00 33.58  ? 105 ARG   C NE    1 
ATOM   4281  C  CZ    . ARG   B 1  105 ? 27.957  14.023  -19.962 1.00 40.03  ? 105 ARG   C CZ    1 
ATOM   4282  N  NH1   . ARG   B 1  105 ? 28.878  13.069  -19.874 1.00 23.57  ? 105 ARG   C NH1   1 
ATOM   4283  N  NH2   . ARG   B 1  105 ? 27.919  14.798  -21.044 1.00 42.96  ? 105 ARG   C NH2   1 
ATOM   4284  N  N     . GLY   B 1  106 ? 27.133  17.775  -13.945 1.00 39.33  ? 106 GLY   C N     1 
ATOM   4285  C  CA    . GLY   B 1  106 ? 26.854  19.154  -13.574 1.00 22.87  ? 106 GLY   C CA    1 
ATOM   4286  C  C     . GLY   B 1  106 ? 27.989  19.791  -12.790 1.00 33.01  ? 106 GLY   C C     1 
ATOM   4287  O  O     . GLY   B 1  106 ? 28.361  20.941  -13.050 1.00 31.92  ? 106 GLY   C O     1 
ATOM   4288  N  N     . HIS   B 1  107 ? 28.565  19.052  -11.827 1.00 26.21  ? 107 HIS   C N     1 
ATOM   4289  C  CA    . HIS   B 1  107 ? 29.580  19.635  -10.955 1.00 32.47  ? 107 HIS   C CA    1 
ATOM   4290  C  C     . HIS   B 1  107 ? 30.968  19.650  -11.588 1.00 41.45  ? 107 HIS   C C     1 
ATOM   4291  O  O     . HIS   B 1  107 ? 31.736  20.594  -11.362 1.00 37.30  ? 107 HIS   C O     1 
ATOM   4292  C  CB    . HIS   B 1  107 ? 29.648  18.897  -9.615  1.00 37.57  ? 107 HIS   C CB    1 
ATOM   4293  C  CG    . HIS   B 1  107 ? 30.539  19.571  -8.609  1.00 38.10  ? 107 HIS   C CG    1 
ATOM   4294  N  ND1   . HIS   B 1  107 ? 31.832  19.161  -8.357  1.00 38.54  ? 107 HIS   C ND1   1 
ATOM   4295  C  CD2   . HIS   B 1  107 ? 30.327  20.641  -7.808  1.00 38.89  ? 107 HIS   C CD2   1 
ATOM   4296  C  CE1   . HIS   B 1  107 ? 32.375  19.941  -7.441  1.00 45.39  ? 107 HIS   C CE1   1 
ATOM   4297  N  NE2   . HIS   B 1  107 ? 31.483  20.850  -7.091  1.00 52.66  ? 107 HIS   C NE2   1 
ATOM   4298  N  N     . TYR   B 1  108 ? 31.324  18.603  -12.347 1.00 39.02  ? 108 TYR   C N     1 
ATOM   4299  C  CA    . TYR   B 1  108 ? 32.666  18.480  -12.917 1.00 41.09  ? 108 TYR   C CA    1 
ATOM   4300  C  C     . TYR   B 1  108 ? 32.666  18.506  -14.452 1.00 48.39  ? 108 TYR   C C     1 
ATOM   4301  O  O     . TYR   B 1  108 ? 33.003  19.530  -15.059 1.00 42.20  ? 108 TYR   C O     1 
ATOM   4302  C  CB    . TYR   B 1  108 ? 33.355  17.192  -12.424 1.00 37.56  ? 108 TYR   C CB    1 
ATOM   4303  C  CG    . TYR   B 1  108 ? 33.390  16.978  -10.899 1.00 52.65  ? 108 TYR   C CG    1 
ATOM   4304  C  CD1   . TYR   B 1  108 ? 34.454  17.452  -10.124 1.00 52.71  ? 108 TYR   C CD1   1 
ATOM   4305  C  CD2   . TYR   B 1  108 ? 32.377  16.270  -10.242 1.00 45.49  ? 108 TYR   C CD2   1 
ATOM   4306  C  CE1   . TYR   B 1  108 ? 34.502  17.243  -8.744  1.00 52.04  ? 108 TYR   C CE1   1 
ATOM   4307  C  CE2   . TYR   B 1  108 ? 32.413  16.059  -8.857  1.00 37.20  ? 108 TYR   C CE2   1 
ATOM   4308  C  CZ    . TYR   B 1  108 ? 33.475  16.550  -8.109  1.00 52.83  ? 108 TYR   C CZ    1 
ATOM   4309  O  OH    . TYR   B 1  108 ? 33.514  16.350  -6.732  1.00 40.00  ? 108 TYR   C OH    1 
ATOM   4310  N  N     . THR   B 1  109 ? 32.260  17.393  -15.080 1.00 40.32  ? 109 THR   C N     1 
ATOM   4311  C  CA    . THR   B 1  109 ? 32.636  17.115  -16.466 1.00 34.18  ? 109 THR   C CA    1 
ATOM   4312  C  C     . THR   B 1  109 ? 32.204  18.221  -17.416 1.00 36.21  ? 109 THR   C C     1 
ATOM   4313  O  O     . THR   B 1  109 ? 32.995  18.687  -18.241 1.00 43.97  ? 109 THR   C O     1 
ATOM   4314  C  CB    . THR   B 1  109 ? 32.044  15.784  -16.909 1.00 39.02  ? 109 THR   C CB    1 
ATOM   4315  O  OG1   . THR   B 1  109 ? 32.466  14.756  -16.008 1.00 34.60  ? 109 THR   C OG1   1 
ATOM   4316  C  CG2   . THR   B 1  109 ? 32.531  15.448  -18.305 1.00 41.97  ? 109 THR   C CG2   1 
ATOM   4317  N  N     . ILE   B 1  110 ? 30.945  18.630  -17.349 1.00 34.32  ? 110 ILE   C N     1 
ATOM   4318  C  CA    . ILE   B 1  110 ? 30.423  19.662  -18.234 1.00 34.79  ? 110 ILE   C CA    1 
ATOM   4319  C  C     . ILE   B 1  110 ? 30.431  21.025  -17.558 1.00 49.59  ? 110 ILE   C C     1 
ATOM   4320  O  O     . ILE   B 1  110 ? 30.725  22.039  -18.196 1.00 45.99  ? 110 ILE   C O     1 
ATOM   4321  C  CB    . ILE   B 1  110 ? 28.998  19.288  -18.696 1.00 35.03  ? 110 ILE   C CB    1 
ATOM   4322  C  CG1   . ILE   B 1  110 ? 28.989  17.889  -19.297 1.00 40.64  ? 110 ILE   C CG1   1 
ATOM   4323  C  CG2   . ILE   B 1  110 ? 28.455  20.295  -19.677 1.00 25.81  ? 110 ILE   C CG2   1 
ATOM   4324  C  CD1   . ILE   B 1  110 ? 29.636  17.820  -20.637 1.00 44.34  ? 110 ILE   C CD1   1 
ATOM   4325  N  N     . GLY   B 1  111 ? 30.102  21.058  -16.262 1.00 42.82  ? 111 GLY   C N     1 
ATOM   4326  C  CA    . GLY   B 1  111 ? 29.966  22.333  -15.581 1.00 37.25  ? 111 GLY   C CA    1 
ATOM   4327  C  C     . GLY   B 1  111 ? 31.271  23.096  -15.499 1.00 37.11  ? 111 GLY   C C     1 
ATOM   4328  O  O     . GLY   B 1  111 ? 31.291  24.320  -15.644 1.00 42.78  ? 111 GLY   C O     1 
ATOM   4329  N  N     . LYS   B 1  112 ? 32.380  22.384  -15.261 1.00 41.69  ? 112 LYS   C N     1 
ATOM   4330  C  CA    . LYS   B 1  112 ? 33.683  23.039  -15.221 1.00 39.11  ? 112 LYS   C CA    1 
ATOM   4331  C  C     . LYS   B 1  112 ? 33.947  23.817  -16.502 1.00 41.69  ? 112 LYS   C C     1 
ATOM   4332  O  O     . LYS   B 1  112 ? 34.619  24.854  -16.470 1.00 43.75  ? 112 LYS   C O     1 
ATOM   4333  C  CB    . LYS   B 1  112 ? 34.798  22.011  -14.973 1.00 38.24  ? 112 LYS   C CB    1 
ATOM   4334  C  CG    . LYS   B 1  112 ? 35.219  21.203  -16.211 1.00 48.01  ? 112 LYS   C CG    1 
ATOM   4335  C  CD    . LYS   B 1  112 ? 36.337  20.192  -15.903 1.00 50.26  ? 112 LYS   C CD    1 
ATOM   4336  C  CE    . LYS   B 1  112 ? 35.964  19.248  -14.731 1.00 65.83  ? 112 LYS   C CE    1 
ATOM   4337  N  NZ    . LYS   B 1  112 ? 36.999  18.203  -14.370 1.00 61.88  ? 112 LYS   C NZ    1 
ATOM   4338  N  N     . GLU   B 1  113 ? 33.415  23.364  -17.635 1.00 36.44  ? 113 GLU   C N     1 
ATOM   4339  C  CA    . GLU   B 1  113 ? 33.750  24.072  -18.862 1.00 41.44  ? 113 GLU   C CA    1 
ATOM   4340  C  C     . GLU   B 1  113 ? 33.064  25.423  -18.962 1.00 38.16  ? 113 GLU   C C     1 
ATOM   4341  O  O     . GLU   B 1  113 ? 33.535  26.276  -19.721 1.00 56.27  ? 113 GLU   C O     1 
ATOM   4342  C  CB    . GLU   B 1  113 ? 33.426  23.228  -20.101 1.00 43.54  ? 113 GLU   C CB    1 
ATOM   4343  C  CG    . GLU   B 1  113 ? 34.262  21.928  -20.240 1.00 53.03  ? 113 GLU   C CG    1 
ATOM   4344  C  CD    . GLU   B 1  113 ? 35.773  22.160  -20.432 1.00 70.06  ? 113 GLU   C CD    1 
ATOM   4345  O  OE1   . GLU   B 1  113 ? 36.156  23.176  -21.060 1.00 72.92  ? 113 GLU   C OE1   1 
ATOM   4346  O  OE2   . GLU   B 1  113 ? 36.577  21.316  -19.957 1.00 76.70  ? 113 GLU   C OE2   1 
ATOM   4347  N  N     . ILE   B 1  114 ? 32.004  25.676  -18.193 1.00 35.49  ? 114 ILE   C N     1 
ATOM   4348  C  CA    . ILE   B 1  114 ? 31.243  26.912  -18.350 1.00 29.35  ? 114 ILE   C CA    1 
ATOM   4349  C  C     . ILE   B 1  114 ? 31.155  27.744  -17.075 1.00 31.12  ? 114 ILE   C C     1 
ATOM   4350  O  O     . ILE   B 1  114 ? 30.520  28.801  -17.093 1.00 32.80  ? 114 ILE   C O     1 
ATOM   4351  C  CB    . ILE   B 1  114 ? 29.832  26.629  -18.899 1.00 31.65  ? 114 ILE   C CB    1 
ATOM   4352  C  CG1   . ILE   B 1  114 ? 29.243  27.883  -19.537 1.00 30.09  ? 114 ILE   C CG1   1 
ATOM   4353  C  CG2   . ILE   B 1  114 ? 28.936  26.070  -17.807 1.00 30.89  ? 114 ILE   C CG2   1 
ATOM   4354  C  CD1   . ILE   B 1  114 ? 27.833  27.685  -20.051 1.00 33.02  ? 114 ILE   C CD1   1 
ATOM   4355  N  N     . ILE   B 1  115 ? 31.799  27.331  -15.977 1.00 37.73  ? 115 ILE   C N     1 
ATOM   4356  C  CA    . ILE   B 1  115 ? 31.616  28.034  -14.701 1.00 31.19  ? 115 ILE   C CA    1 
ATOM   4357  C  C     . ILE   B 1  115 ? 32.224  29.438  -14.750 1.00 36.42  ? 115 ILE   C C     1 
ATOM   4358  O  O     . ILE   B 1  115 ? 31.545  30.423  -14.435 1.00 38.53  ? 115 ILE   C O     1 
ATOM   4359  C  CB    . ILE   B 1  115 ? 32.174  27.201  -13.532 1.00 30.96  ? 115 ILE   C CB    1 
ATOM   4360  C  CG1   . ILE   B 1  115 ? 32.237  28.029  -12.245 1.00 35.43  ? 115 ILE   C CG1   1 
ATOM   4361  C  CG2   . ILE   B 1  115 ? 33.525  26.618  -13.861 1.00 34.04  ? 115 ILE   C CG2   1 
ATOM   4362  C  CD1   . ILE   B 1  115 ? 30.909  28.268  -11.608 1.00 28.27  ? 115 ILE   C CD1   1 
ATOM   4363  N  N     . ASP   B 1  116 ? 33.504  29.557  -15.147 1.00 35.41  ? 116 ASP   C N     1 
ATOM   4364  C  CA    . ASP   B 1  116 ? 34.136  30.875  -15.292 1.00 28.72  ? 116 ASP   C CA    1 
ATOM   4365  C  C     . ASP   B 1  116 ? 33.254  31.850  -16.066 1.00 27.93  ? 116 ASP   C C     1 
ATOM   4366  O  O     . ASP   B 1  116 ? 33.032  32.987  -15.632 1.00 32.27  ? 116 ASP   C O     1 
ATOM   4367  C  CB    . ASP   B 1  116 ? 35.495  30.764  -15.987 1.00 22.37  ? 116 ASP   C CB    1 
ATOM   4368  C  CG    . ASP   B 1  116 ? 36.509  30.029  -15.168 1.00 23.56  ? 116 ASP   C CG    1 
ATOM   4369  O  OD1   . ASP   B 1  116 ? 36.310  29.878  -13.949 1.00 30.98  ? 116 ASP   C OD1   1 
ATOM   4370  O  OD2   . ASP   B 1  116 ? 37.522  29.591  -15.751 1.00 46.59  ? 116 ASP   C OD2   1 
ATOM   4371  N  N     . LEU   B 1  117 ? 32.756  31.438  -17.226 1.00 27.21  ? 117 LEU   C N     1 
ATOM   4372  C  CA    . LEU   B 1  117 ? 31.872  32.328  -17.971 1.00 33.55  ? 117 LEU   C CA    1 
ATOM   4373  C  C     . LEU   B 1  117 ? 30.699  32.774  -17.106 1.00 35.99  ? 117 LEU   C C     1 
ATOM   4374  O  O     . LEU   B 1  117 ? 30.396  33.968  -17.003 1.00 39.52  ? 117 LEU   C O     1 
ATOM   4375  C  CB    . LEU   B 1  117 ? 31.379  31.624  -19.231 1.00 37.68  ? 117 LEU   C CB    1 
ATOM   4376  C  CG    . LEU   B 1  117 ? 30.430  32.362  -20.152 1.00 30.34  ? 117 LEU   C CG    1 
ATOM   4377  C  CD1   . LEU   B 1  117 ? 30.847  33.797  -20.285 1.00 36.37  ? 117 LEU   C CD1   1 
ATOM   4378  C  CD2   . LEU   B 1  117 ? 30.520  31.674  -21.476 1.00 40.54  ? 117 LEU   C CD2   1 
ATOM   4379  N  N     . VAL   B 1  118 ? 30.035  31.821  -16.460 1.00 35.40  ? 118 VAL   C N     1 
ATOM   4380  C  CA    . VAL   B 1  118 ? 28.877  32.142  -15.633 1.00 37.75  ? 118 VAL   C CA    1 
ATOM   4381  C  C     . VAL   B 1  118 ? 29.248  33.173  -14.566 1.00 34.65  ? 118 VAL   C C     1 
ATOM   4382  O  O     . VAL   B 1  118 ? 28.619  34.231  -14.462 1.00 29.19  ? 118 VAL   C O     1 
ATOM   4383  C  CB    . VAL   B 1  118 ? 28.304  30.846  -15.028 1.00 37.71  ? 118 VAL   C CB    1 
ATOM   4384  C  CG1   . VAL   B 1  118 ? 27.451  31.135  -13.782 1.00 31.95  ? 118 VAL   C CG1   1 
ATOM   4385  C  CG2   . VAL   B 1  118 ? 27.536  30.074  -16.109 1.00 30.98  ? 118 VAL   C CG2   1 
ATOM   4386  N  N     . LEU   B 1  119 ? 30.296  32.886  -13.779 1.00 29.45  ? 119 LEU   C N     1 
ATOM   4387  C  CA    . LEU   B 1  119 ? 30.749  33.809  -12.740 1.00 29.83  ? 119 LEU   C CA    1 
ATOM   4388  C  C     . LEU   B 1  119 ? 31.114  35.176  -13.313 1.00 39.00  ? 119 LEU   C C     1 
ATOM   4389  O  O     . LEU   B 1  119 ? 30.876  36.205  -12.666 1.00 39.91  ? 119 LEU   C O     1 
ATOM   4390  C  CB    . LEU   B 1  119 ? 31.952  33.222  -12.000 1.00 34.21  ? 119 LEU   C CB    1 
ATOM   4391  C  CG    . LEU   B 1  119 ? 31.788  32.115  -10.962 1.00 33.84  ? 119 LEU   C CG    1 
ATOM   4392  C  CD1   . LEU   B 1  119 ? 33.182  31.632  -10.610 1.00 38.28  ? 119 LEU   C CD1   1 
ATOM   4393  C  CD2   . LEU   B 1  119 ? 31.092  32.612  -9.724  1.00 18.50  ? 119 LEU   C CD2   1 
ATOM   4394  N  N     . ASP   B 1  120 ? 31.709  35.215  -14.518 1.00 37.91  ? 120 ASP   C N     1 
ATOM   4395  C  CA    A ASP   B 1  120 ? 32.027  36.498  -15.142 0.47 34.39  ? 120 ASP   C CA    1 
ATOM   4396  C  CA    B ASP   B 1  120 ? 32.032  36.505  -15.117 0.53 34.32  ? 120 ASP   C CA    1 
ATOM   4397  C  C     . ASP   B 1  120 ? 30.775  37.333  -15.356 1.00 36.53  ? 120 ASP   C C     1 
ATOM   4398  O  O     . ASP   B 1  120 ? 30.787  38.554  -15.144 1.00 36.69  ? 120 ASP   C O     1 
ATOM   4399  C  CB    A ASP   B 1  120 ? 32.752  36.284  -16.469 0.47 31.63  ? 120 ASP   C CB    1 
ATOM   4400  C  CB    B ASP   B 1  120 ? 32.811  36.321  -16.418 0.53 31.55  ? 120 ASP   C CB    1 
ATOM   4401  C  CG    A ASP   B 1  120 ? 32.827  37.553  -17.303 0.47 33.14  ? 120 ASP   C CG    1 
ATOM   4402  C  CG    B ASP   B 1  120 ? 34.265  35.905  -16.194 0.53 31.39  ? 120 ASP   C CG    1 
ATOM   4403  O  OD1   A ASP   B 1  120 ? 33.448  38.523  -16.830 0.47 35.31  ? 120 ASP   C OD1   1 
ATOM   4404  O  OD1   B ASP   B 1  120 ? 34.679  35.603  -15.046 0.53 29.04  ? 120 ASP   C OD1   1 
ATOM   4405  O  OD2   A ASP   B 1  120 ? 32.267  37.584  -18.426 0.47 32.33  ? 120 ASP   C OD2   1 
ATOM   4406  O  OD2   B ASP   B 1  120 ? 34.997  35.866  -17.202 0.53 34.44  ? 120 ASP   C OD2   1 
ATOM   4407  N  N     . ARG   B 1  121 ? 29.676  36.694  -15.787 1.00 37.10  ? 121 ARG   C N     1 
ATOM   4408  C  CA    . ARG   B 1  121 ? 28.425  37.441  -15.950 1.00 42.88  ? 121 ARG   C CA    1 
ATOM   4409  C  C     . ARG   B 1  121 ? 27.847  37.852  -14.598 1.00 44.59  ? 121 ARG   C C     1 
ATOM   4410  O  O     . ARG   B 1  121 ? 27.400  38.995  -14.435 1.00 43.40  ? 121 ARG   C O     1 
ATOM   4411  C  CB    . ARG   B 1  121 ? 27.384  36.638  -16.729 1.00 36.59  ? 121 ARG   C CB    1 
ATOM   4412  C  CG    . ARG   B 1  121 ? 27.853  36.147  -18.075 1.00 49.26  ? 121 ARG   C CG    1 
ATOM   4413  C  CD    . ARG   B 1  121 ? 28.053  37.272  -19.074 1.00 45.73  ? 121 ARG   C CD    1 
ATOM   4414  N  NE    . ARG   B 1  121 ? 28.947  36.807  -20.124 1.00 51.00  ? 121 ARG   C NE    1 
ATOM   4415  C  CZ    . ARG   B 1  121 ? 28.575  36.061  -21.156 1.00 59.05  ? 121 ARG   C CZ    1 
ATOM   4416  N  NH1   . ARG   B 1  121 ? 27.306  35.727  -21.350 1.00 50.16  ? 121 ARG   C NH1   1 
ATOM   4417  N  NH2   . ARG   B 1  121 ? 29.499  35.645  -22.021 1.00 58.53  ? 121 ARG   C NH2   1 
ATOM   4418  N  N     . ILE   B 1  122 ? 27.824  36.938  -13.620 1.00 31.46  ? 122 ILE   C N     1 
ATOM   4419  C  CA    . ILE   B 1  122 ? 27.390  37.339  -12.289 1.00 31.70  ? 122 ILE   C CA    1 
ATOM   4420  C  C     . ILE   B 1  122 ? 28.184  38.561  -11.852 1.00 39.20  ? 122 ILE   C C     1 
ATOM   4421  O  O     . ILE   B 1  122 ? 27.632  39.537  -11.321 1.00 35.89  ? 122 ILE   C O     1 
ATOM   4422  C  CB    . ILE   B 1  122 ? 27.550  36.176  -11.297 1.00 29.88  ? 122 ILE   C CB    1 
ATOM   4423  C  CG1   . ILE   B 1  122 ? 26.652  35.017  -11.674 1.00 25.13  ? 122 ILE   C CG1   1 
ATOM   4424  C  CG2   . ILE   B 1  122 ? 27.266  36.638  -9.853  1.00 27.05  ? 122 ILE   C CG2   1 
ATOM   4425  C  CD1   . ILE   B 1  122 ? 27.078  33.758  -10.989 1.00 25.29  ? 122 ILE   C CD1   1 
ATOM   4426  N  N     . ARG   B 1  123 ? 29.491  38.539  -12.117 1.00 37.84  ? 123 ARG   C N     1 
ATOM   4427  C  CA    . ARG   B 1  123 ? 30.361  39.644  -11.736 1.00 39.61  ? 123 ARG   C CA    1 
ATOM   4428  C  C     . ARG   B 1  123 ? 29.954  40.949  -12.417 1.00 34.27  ? 123 ARG   C C     1 
ATOM   4429  O  O     . ARG   B 1  123 ? 29.912  42.000  -11.772 1.00 37.58  ? 123 ARG   C O     1 
ATOM   4430  C  CB    . ARG   B 1  123 ? 31.807  39.267  -12.052 1.00 37.14  ? 123 ARG   C CB    1 
ATOM   4431  C  CG    . ARG   B 1  123 ? 32.821  40.330  -11.711 1.00 36.99  ? 123 ARG   C CG    1 
ATOM   4432  C  CD    . ARG   B 1  123 ? 32.476  41.020  -10.433 1.00 43.22  ? 123 ARG   C CD    1 
ATOM   4433  N  NE    . ARG   B 1  123 ? 33.081  40.386  -9.268  1.00 50.48  ? 123 ARG   C NE    1 
ATOM   4434  C  CZ    . ARG   B 1  123 ? 33.073  40.930  -8.057  1.00 56.97  ? 123 ARG   C CZ    1 
ATOM   4435  N  NH1   . ARG   B 1  123 ? 32.490  42.106  -7.832  1.00 50.96  ? 123 ARG   C NH1   1 
ATOM   4436  N  NH2   . ARG   B 1  123 ? 33.672  40.290  -7.054  1.00 41.68  ? 123 ARG   C NH2   1 
ATOM   4437  N  N     . LYS   B 1  124 ? 29.620  40.905  -13.710 1.00 38.51  ? 124 LYS   C N     1 
ATOM   4438  C  CA    . LYS   B 1  124 ? 29.139  42.115  -14.385 1.00 36.22  ? 124 LYS   C CA    1 
ATOM   4439  C  C     . LYS   B 1  124 ? 27.884  42.677  -13.716 1.00 36.80  ? 124 LYS   C C     1 
ATOM   4440  O  O     . LYS   B 1  124 ? 27.712  43.895  -13.635 1.00 42.31  ? 124 LYS   C O     1 
ATOM   4441  C  CB    . LYS   B 1  124 ? 28.875  41.827  -15.867 1.00 38.65  ? 124 LYS   C CB    1 
ATOM   4442  C  CG    . LYS   B 1  124 ? 27.608  42.511  -16.416 1.00 62.36  ? 124 LYS   C CG    1 
ATOM   4443  C  CD    . LYS   B 1  124 ? 27.190  42.004  -17.817 1.00 62.59  ? 124 LYS   C CD    1 
ATOM   4444  C  CE    . LYS   B 1  124 ? 25.730  42.358  -18.134 1.00 55.60  ? 124 LYS   C CE    1 
ATOM   4445  N  NZ    . LYS   B 1  124 ? 25.369  42.066  -19.542 1.00 52.92  ? 124 LYS   C NZ    1 
ATOM   4446  N  N     . LEU   B 1  125 ? 26.986  41.803  -13.244 1.00 47.45  ? 125 LEU   C N     1 
ATOM   4447  C  CA    . LEU   B 1  125 ? 25.798  42.261  -12.524 1.00 35.86  ? 125 LEU   C CA    1 
ATOM   4448  C  C     . LEU   B 1  125 ? 26.165  42.856  -11.171 1.00 38.54  ? 125 LEU   C C     1 
ATOM   4449  O  O     . LEU   B 1  125 ? 25.576  43.858  -10.748 1.00 38.44  ? 125 LEU   C O     1 
ATOM   4450  C  CB    . LEU   B 1  125 ? 24.802  41.110  -12.346 1.00 33.21  ? 125 LEU   C CB    1 
ATOM   4451  C  CG    . LEU   B 1  125 ? 24.086  40.591  -13.602 1.00 39.64  ? 125 LEU   C CG    1 
ATOM   4452  C  CD1   . LEU   B 1  125 ? 23.310  39.302  -13.356 1.00 26.58  ? 125 LEU   C CD1   1 
ATOM   4453  C  CD2   . LEU   B 1  125 ? 23.157  41.638  -14.139 1.00 37.80  ? 125 LEU   C CD2   1 
ATOM   4454  N  N     . ALA   B 1  126 ? 27.130  42.249  -10.472 1.00 35.88  ? 126 ALA   C N     1 
ATOM   4455  C  CA    . ALA   B 1  126 ? 27.479  42.729  -9.138  1.00 37.86  ? 126 ALA   C CA    1 
ATOM   4456  C  C     . ALA   B 1  126 ? 28.072  44.130  -9.179  1.00 36.28  ? 126 ALA   C C     1 
ATOM   4457  O  O     . ALA   B 1  126 ? 27.845  44.926  -8.259  1.00 35.63  ? 126 ALA   C O     1 
ATOM   4458  C  CB    . ALA   B 1  126 ? 28.446  41.759  -8.460  1.00 33.18  ? 126 ALA   C CB    1 
ATOM   4459  N  N     . ASP   B 1  127 ? 28.799  44.463  -10.249 1.00 42.96  ? 127 ASP   C N     1 
ATOM   4460  C  CA    . ASP   B 1  127 ? 29.447  45.770  -10.340 1.00 41.98  ? 127 ASP   C CA    1 
ATOM   4461  C  C     . ASP   B 1  127 ? 28.464  46.895  -10.636 1.00 38.70  ? 127 ASP   C C     1 
ATOM   4462  O  O     . ASP   B 1  127 ? 28.770  48.045  -10.319 1.00 49.60  ? 127 ASP   C O     1 
ATOM   4463  C  CB    . ASP   B 1  127 ? 30.566  45.739  -11.386 1.00 40.28  ? 127 ASP   C CB    1 
ATOM   4464  C  CG    . ASP   B 1  127 ? 31.790  44.913  -10.933 1.00 47.07  ? 127 ASP   C CG    1 
ATOM   4465  O  OD1   . ASP   B 1  127 ? 31.978  44.682  -9.710  1.00 44.18  ? 127 ASP   C OD1   1 
ATOM   4466  O  OD2   . ASP   B 1  127 ? 32.569  44.489  -11.814 1.00 43.32  ? 127 ASP   C OD2   1 
ATOM   4467  N  N     . GLN   B 1  128 ? 27.298  46.596  -11.223 1.00 43.51  ? 128 GLN   C N     1 
ATOM   4468  C  CA    . GLN   B 1  128 ? 26.186  47.549  -11.297 1.00 48.22  ? 128 GLN   C CA    1 
ATOM   4469  C  C     . GLN   B 1  128 ? 25.568  47.890  -9.943  1.00 47.76  ? 128 GLN   C C     1 
ATOM   4470  O  O     . GLN   B 1  128 ? 24.654  48.720  -9.897  1.00 48.01  ? 128 GLN   C O     1 
ATOM   4471  C  CB    . GLN   B 1  128 ? 25.042  47.002  -12.148 1.00 40.85  ? 128 GLN   C CB    1 
ATOM   4472  C  CG    . GLN   B 1  128 ? 25.265  46.904  -13.625 1.00 56.04  ? 128 GLN   C CG    1 
ATOM   4473  C  CD    . GLN   B 1  128 ? 23.939  46.681  -14.342 1.00 70.94  ? 128 GLN   C CD    1 
ATOM   4474  O  OE1   . GLN   B 1  128 ? 23.423  47.584  -15.006 1.00 75.64  ? 128 GLN   C OE1   1 
ATOM   4475  N  NE2   . GLN   B 1  128 ? 23.360  45.482  -14.179 1.00 53.88  ? 128 GLN   C NE2   1 
ATOM   4476  N  N     . CYS   B 1  129 ? 25.987  47.246  -8.856  1.00 45.66  ? 129 CYS   C N     1 
ATOM   4477  C  CA    . CYS   B 1  129 ? 25.290  47.358  -7.579  1.00 46.18  ? 129 CYS   C CA    1 
ATOM   4478  C  C     . CYS   B 1  129 ? 26.027  48.330  -6.676  1.00 41.69  ? 129 CYS   C C     1 
ATOM   4479  O  O     . CYS   B 1  129 ? 27.259  48.317  -6.608  1.00 47.85  ? 129 CYS   C O     1 
ATOM   4480  C  CB    . CYS   B 1  129 ? 25.173  45.995  -6.868  1.00 55.75  ? 129 CYS   C CB    1 
ATOM   4481  S  SG    . CYS   B 1  129 ? 24.123  44.702  -7.652  1.00 42.14  ? 129 CYS   C SG    1 
ATOM   4482  N  N     . THR   B 1  130 ? 25.273  49.167  -5.981  1.00 39.55  ? 130 THR   C N     1 
ATOM   4483  C  CA    . THR   B 1  130 ? 25.882  50.065  -5.010  1.00 42.67  ? 130 THR   C CA    1 
ATOM   4484  C  C     . THR   B 1  130 ? 25.941  49.479  -3.607  1.00 37.56  ? 130 THR   C C     1 
ATOM   4485  O  O     . THR   B 1  130 ? 26.788  49.904  -2.820  1.00 49.07  ? 130 THR   C O     1 
ATOM   4486  C  CB    . THR   B 1  130 ? 25.134  51.396  -4.986  1.00 41.96  ? 130 THR   C CB    1 
ATOM   4487  O  OG1   . THR   B 1  130 ? 23.764  51.150  -5.280  1.00 45.40  ? 130 THR   C OG1   1 
ATOM   4488  C  CG2   . THR   B 1  130 ? 25.699  52.347  -6.039  1.00 49.46  ? 130 THR   C CG2   1 
ATOM   4489  N  N     . GLY   B 1  131 ? 25.090  48.503  -3.288  1.00 37.19  ? 131 GLY   C N     1 
ATOM   4490  C  CA    . GLY   B 1  131 ? 25.087  47.857  -1.988  1.00 37.59  ? 131 GLY   C CA    1 
ATOM   4491  C  C     . GLY   B 1  131 ? 24.496  46.459  -2.018  1.00 45.02  ? 131 GLY   C C     1 
ATOM   4492  O  O     . GLY   B 1  131 ? 23.520  46.156  -1.317  1.00 41.98  ? 131 GLY   C O     1 
ATOM   4493  N  N     . LEU   B 1  132 ? 25.096  45.601  -2.842  1.00 45.36  ? 132 LEU   C N     1 
ATOM   4494  C  CA    . LEU   B 1  132 ? 24.616  44.242  -3.045  1.00 31.69  ? 132 LEU   C CA    1 
ATOM   4495  C  C     . LEU   B 1  132 ? 24.439  43.500  -1.731  1.00 35.00  ? 132 LEU   C C     1 
ATOM   4496  O  O     . LEU   B 1  132 ? 25.324  43.494  -0.874  1.00 35.54  ? 132 LEU   C O     1 
ATOM   4497  C  CB    . LEU   B 1  132 ? 25.594  43.493  -3.931  1.00 27.40  ? 132 LEU   C CB    1 
ATOM   4498  C  CG    . LEU   B 1  132 ? 25.279  42.042  -4.218  1.00 29.35  ? 132 LEU   C CG    1 
ATOM   4499  C  CD1   . LEU   B 1  132 ? 24.006  41.949  -5.038  1.00 21.28  ? 132 LEU   C CD1   1 
ATOM   4500  C  CD2   . LEU   B 1  132 ? 26.490  41.406  -4.911  1.00 22.55  ? 132 LEU   C CD2   1 
ATOM   4501  N  N     . GLN   B 1  133 ? 23.293  42.841  -1.596  1.00 39.81  ? 133 GLN   C N     1 
ATOM   4502  C  CA    . GLN   B 1  133 ? 22.945  42.109  -0.394  1.00 28.04  ? 133 GLN   C CA    1 
ATOM   4503  C  C     . GLN   B 1  133 ? 23.155  40.607  -0.510  1.00 35.99  ? 133 GLN   C C     1 
ATOM   4504  O  O     . GLN   B 1  133 ? 23.501  39.972  0.483   1.00 37.71  ? 133 GLN   C O     1 
ATOM   4505  C  CB    . GLN   B 1  133 ? 21.486  42.387  -0.039  1.00 42.70  ? 133 GLN   C CB    1 
ATOM   4506  C  CG    . GLN   B 1  133 ? 21.106  41.979  1.376   1.00 58.47  ? 133 GLN   C CG    1 
ATOM   4507  C  CD    . GLN   B 1  133 ? 20.045  42.891  1.939   1.00 63.78  ? 133 GLN   C CD    1 
ATOM   4508  O  OE1   . GLN   B 1  133 ? 20.014  44.082  1.621   1.00 81.64  ? 133 GLN   C OE1   1 
ATOM   4509  N  NE2   . GLN   B 1  133 ? 19.157  42.345  2.759   1.00 52.65  ? 133 GLN   C NE2   1 
ATOM   4510  N  N     . GLY   B 1  134 ? 22.947  40.019  -1.679  1.00 42.91  ? 134 GLY   C N     1 
ATOM   4511  C  CA    . GLY   B 1  134 ? 23.110  38.587  -1.833  1.00 40.48  ? 134 GLY   C CA    1 
ATOM   4512  C  C     . GLY   B 1  134 ? 22.374  38.074  -3.054  1.00 33.82  ? 134 GLY   C C     1 
ATOM   4513  O  O     . GLY   B 1  134 ? 21.765  38.833  -3.807  1.00 32.90  ? 134 GLY   C O     1 
ATOM   4514  N  N     . PHE   B 1  135 ? 22.410  36.746  -3.198  1.00 27.87  ? 135 PHE   C N     1 
ATOM   4515  C  CA    . PHE   B 1  135 ? 21.866  36.021  -4.342  1.00 33.83  ? 135 PHE   C CA    1 
ATOM   4516  C  C     . PHE   B 1  135 ? 20.654  35.171  -3.967  1.00 30.59  ? 135 PHE   C C     1 
ATOM   4517  O  O     . PHE   B 1  135 ? 20.559  34.665  -2.844  1.00 31.46  ? 135 PHE   C O     1 
ATOM   4518  C  CB    . PHE   B 1  135 ? 22.933  35.097  -4.929  1.00 30.75  ? 135 PHE   C CB    1 
ATOM   4519  C  CG    . PHE   B 1  135 ? 24.226  35.757  -5.127  1.00 30.75  ? 135 PHE   C CG    1 
ATOM   4520  C  CD1   . PHE   B 1  135 ? 25.167  35.776  -4.110  1.00 41.28  ? 135 PHE   C CD1   1 
ATOM   4521  C  CD2   . PHE   B 1  135 ? 24.501  36.401  -6.310  1.00 26.49  ? 135 PHE   C CD2   1 
ATOM   4522  C  CE1   . PHE   B 1  135 ? 26.377  36.416  -4.288  1.00 32.17  ? 135 PHE   C CE1   1 
ATOM   4523  C  CE2   . PHE   B 1  135 ? 25.706  37.025  -6.493  1.00 29.41  ? 135 PHE   C CE2   1 
ATOM   4524  C  CZ    . PHE   B 1  135 ? 26.641  37.039  -5.482  1.00 27.40  ? 135 PHE   C CZ    1 
ATOM   4525  N  N     . LEU   B 1  136 ? 19.750  34.975  -4.934  1.00 24.86  ? 136 LEU   C N     1 
ATOM   4526  C  CA    . LEU   B 1  136 ? 18.698  33.962  -4.837  1.00 24.18  ? 136 LEU   C CA    1 
ATOM   4527  C  C     . LEU   B 1  136 ? 18.925  32.943  -5.939  1.00 30.06  ? 136 LEU   C C     1 
ATOM   4528  O  O     . LEU   B 1  136 ? 18.908  33.296  -7.122  1.00 34.53  ? 136 LEU   C O     1 
ATOM   4529  C  CB    . LEU   B 1  136 ? 17.297  34.557  -4.961  1.00 24.12  ? 136 LEU   C CB    1 
ATOM   4530  C  CG    . LEU   B 1  136 ? 16.894  35.755  -4.108  1.00 22.21  ? 136 LEU   C CG    1 
ATOM   4531  C  CD1   . LEU   B 1  136 ? 15.449  36.120  -4.436  1.00 23.15  ? 136 LEU   C CD1   1 
ATOM   4532  C  CD2   . LEU   B 1  136 ? 17.063  35.443  -2.653  1.00 26.79  ? 136 LEU   C CD2   1 
ATOM   4533  N  N     . VAL   B 1  137 ? 19.135  31.688  -5.560  1.00 22.96  ? 137 VAL   C N     1 
ATOM   4534  C  CA    . VAL   B 1  137 ? 19.564  30.656  -6.491  1.00 18.42  ? 137 VAL   C CA    1 
ATOM   4535  C  C     . VAL   B 1  137 ? 18.415  29.670  -6.616  1.00 26.51  ? 137 VAL   C C     1 
ATOM   4536  O  O     . VAL   B 1  137 ? 18.064  29.002  -5.640  1.00 28.75  ? 137 VAL   C O     1 
ATOM   4537  C  CB    . VAL   B 1  137 ? 20.851  29.974  -6.016  1.00 21.65  ? 137 VAL   C CB    1 
ATOM   4538  C  CG1   . VAL   B 1  137 ? 21.294  28.881  -6.988  1.00 28.74  ? 137 VAL   C CG1   1 
ATOM   4539  C  CG2   . VAL   B 1  137 ? 21.971  31.015  -5.801  1.00 21.95  ? 137 VAL   C CG2   1 
ATOM   4540  N  N     . PHE   B 1  138 ? 17.801  29.611  -7.802  1.00 28.38  ? 138 PHE   C N     1 
ATOM   4541  C  CA    . PHE   B 1  138 ? 16.653  28.748  -8.088  1.00 25.17  ? 138 PHE   C CA    1 
ATOM   4542  C  C     . PHE   B 1  138 ? 17.133  27.561  -8.916  1.00 29.14  ? 138 PHE   C C     1 
ATOM   4543  O  O     . PHE   B 1  138 ? 17.644  27.744  -10.026 1.00 28.94  ? 138 PHE   C O     1 
ATOM   4544  C  CB    . PHE   B 1  138 ? 15.558  29.480  -8.871  1.00 21.32  ? 138 PHE   C CB    1 
ATOM   4545  C  CG    . PHE   B 1  138 ? 15.056  30.721  -8.229  1.00 23.69  ? 138 PHE   C CG    1 
ATOM   4546  C  CD1   . PHE   B 1  138 ? 15.899  31.818  -8.044  1.00 26.56  ? 138 PHE   C CD1   1 
ATOM   4547  C  CD2   . PHE   B 1  138 ? 13.714  30.825  -7.860  1.00 22.75  ? 138 PHE   C CD2   1 
ATOM   4548  C  CE1   . PHE   B 1  138 ? 15.431  32.982  -7.453  1.00 21.45  ? 138 PHE   C CE1   1 
ATOM   4549  C  CE2   . PHE   B 1  138 ? 13.242  31.975  -7.268  1.00 21.88  ? 138 PHE   C CE2   1 
ATOM   4550  C  CZ    . PHE   B 1  138 ? 14.109  33.060  -7.066  1.00 24.26  ? 138 PHE   C CZ    1 
ATOM   4551  N  N     . HIS   B 1  139 ? 16.920  26.355  -8.405  1.00 22.69  ? 139 HIS   C N     1 
ATOM   4552  C  CA    . HIS   B 1  139 ? 17.463  25.155  -9.016  1.00 21.30  ? 139 HIS   C CA    1 
ATOM   4553  C  C     . HIS   B 1  139 ? 16.620  23.982  -8.538  1.00 30.10  ? 139 HIS   C C     1 
ATOM   4554  O  O     . HIS   B 1  139 ? 15.923  24.076  -7.522  1.00 29.15  ? 139 HIS   C O     1 
ATOM   4555  C  CB    . HIS   B 1  139 ? 18.938  24.952  -8.641  1.00 23.06  ? 139 HIS   C CB    1 
ATOM   4556  C  CG    . HIS   B 1  139 ? 19.157  24.718  -7.175  1.00 18.17  ? 139 HIS   C CG    1 
ATOM   4557  N  ND1   . HIS   B 1  139 ? 19.361  23.469  -6.640  1.00 17.19  ? 139 HIS   C ND1   1 
ATOM   4558  C  CD2   . HIS   B 1  139 ? 19.170  25.577  -6.127  1.00 29.03  ? 139 HIS   C CD2   1 
ATOM   4559  C  CE1   . HIS   B 1  139 ? 19.498  23.564  -5.331  1.00 25.18  ? 139 HIS   C CE1   1 
ATOM   4560  N  NE2   . HIS   B 1  139 ? 19.382  24.834  -4.990  1.00 24.08  ? 139 HIS   C NE2   1 
ATOM   4561  N  N     . SER   B 1  140 ? 16.681  22.887  -9.296  1.00 19.44  ? 140 SER   C N     1 
ATOM   4562  C  CA    . SER   B 1  140 ? 16.111  21.608  -8.904  1.00 22.82  ? 140 SER   C CA    1 
ATOM   4563  C  C     . SER   B 1  140 ? 17.122  20.783  -8.094  1.00 28.47  ? 140 SER   C C     1 
ATOM   4564  O  O     . SER   B 1  140 ? 18.338  20.923  -8.251  1.00 22.46  ? 140 SER   C O     1 
ATOM   4565  C  CB    . SER   B 1  140 ? 15.684  20.810  -10.148 1.00 29.46  ? 140 SER   C CB    1 
ATOM   4566  O  OG    . SER   B 1  140 ? 16.803  20.132  -10.736 1.00 21.53  ? 140 SER   C OG    1 
ATOM   4567  N  N     . PHE   B 1  141 ? 16.600  19.912  -7.227  1.00 22.89  ? 141 PHE   C N     1 
ATOM   4568  C  CA    . PHE   B 1  141 ? 17.448  18.918  -6.581  1.00 21.52  ? 141 PHE   C CA    1 
ATOM   4569  C  C     . PHE   B 1  141 ? 17.837  17.827  -7.555  1.00 29.24  ? 141 PHE   C C     1 
ATOM   4570  O  O     . PHE   B 1  141 ? 18.967  17.322  -7.501  1.00 32.83  ? 141 PHE   C O     1 
ATOM   4571  C  CB    . PHE   B 1  141 ? 16.736  18.251  -5.402  1.00 21.29  ? 141 PHE   C CB    1 
ATOM   4572  C  CG    . PHE   B 1  141 ? 16.890  18.957  -4.103  1.00 27.57  ? 141 PHE   C CG    1 
ATOM   4573  C  CD1   . PHE   B 1  141 ? 17.836  19.943  -3.931  1.00 24.70  ? 141 PHE   C CD1   1 
ATOM   4574  C  CD2   . PHE   B 1  141 ? 16.095  18.599  -3.020  1.00 31.24  ? 141 PHE   C CD2   1 
ATOM   4575  C  CE1   . PHE   B 1  141 ? 17.959  20.581  -2.715  1.00 22.80  ? 141 PHE   C CE1   1 
ATOM   4576  C  CE2   . PHE   B 1  141 ? 16.219  19.238  -1.797  1.00 31.84  ? 141 PHE   C CE2   1 
ATOM   4577  C  CZ    . PHE   B 1  141 ? 17.151  20.234  -1.646  1.00 25.00  ? 141 PHE   C CZ    1 
ATOM   4578  N  N     . GLY   B 1  142 ? 16.899  17.431  -8.434  1.00 29.44  ? 142 GLY   C N     1 
ATOM   4579  C  CA    . GLY   B 1  142 ? 16.930  16.136  -9.115  1.00 24.31  ? 142 GLY   C CA    1 
ATOM   4580  C  C     . GLY   B 1  142 ? 17.730  16.079  -10.404 1.00 31.94  ? 142 GLY   C C     1 
ATOM   4581  O  O     . GLY   B 1  142 ? 18.306  15.037  -10.746 1.00 33.64  ? 142 GLY   C O     1 
ATOM   4582  N  N     . GLY   B 1  143 ? 17.756  17.199  -11.132 1.00 32.09  ? 143 GLY   C N     1 
ATOM   4583  C  CA    . GLY   B 1  143 ? 18.494  17.297  -12.370 1.00 21.21  ? 143 GLY   C CA    1 
ATOM   4584  C  C     . GLY   B 1  143 ? 19.983  17.283  -12.120 1.00 29.58  ? 143 GLY   C C     1 
ATOM   4585  O  O     . GLY   B 1  143 ? 20.450  17.351  -10.982 1.00 33.14  ? 143 GLY   C O     1 
ATOM   4586  N  N     . GLY   B 1  144 ? 20.739  17.158  -13.216 1.00 25.84  ? 144 GLY   C N     1 
ATOM   4587  C  CA    . GLY   B 1  144 ? 22.181  17.073  -13.155 1.00 23.65  ? 144 GLY   C CA    1 
ATOM   4588  C  C     . GLY   B 1  144 ? 22.811  18.440  -13.032 1.00 29.88  ? 144 GLY   C C     1 
ATOM   4589  O  O     . GLY   B 1  144 ? 23.798  18.613  -12.311 1.00 33.73  ? 144 GLY   C O     1 
ATOM   4590  N  N     . THR   B 1  145 ? 22.241  19.414  -13.750 1.00 23.26  ? 145 THR   C N     1 
ATOM   4591  C  CA    . THR   B 1  145 ? 22.654  20.804  -13.647 1.00 19.25  ? 145 THR   C CA    1 
ATOM   4592  C  C     . THR   B 1  145 ? 22.133  21.419  -12.355 1.00 29.07  ? 145 THR   C C     1 
ATOM   4593  O  O     . THR   B 1  145 ? 22.910  21.954  -11.552 1.00 33.90  ? 145 THR   C O     1 
ATOM   4594  C  CB    . THR   B 1  145 ? 22.148  21.568  -14.869 1.00 22.98  ? 145 THR   C CB    1 
ATOM   4595  O  OG1   . THR   B 1  145 ? 22.683  20.970  -16.052 1.00 29.37  ? 145 THR   C OG1   1 
ATOM   4596  C  CG2   . THR   B 1  145 ? 22.529  23.044  -14.816 1.00 28.86  ? 145 THR   C CG2   1 
ATOM   4597  N  N     . GLY   B 1  146 ? 20.822  21.296  -12.122 1.00 26.50  ? 146 GLY   C N     1 
ATOM   4598  C  CA    . GLY   B 1  146 ? 20.218  21.821  -10.913 1.00 25.87  ? 146 GLY   C CA    1 
ATOM   4599  C  C     . GLY   B 1  146 ? 20.877  21.323  -9.645  1.00 26.62  ? 146 GLY   C C     1 
ATOM   4600  O  O     . GLY   B 1  146 ? 20.861  22.009  -8.627  1.00 24.82  ? 146 GLY   C O     1 
ATOM   4601  N  N     . SER   B 1  147 ? 21.487  20.142  -9.685  1.00 24.42  ? 147 SER   C N     1 
ATOM   4602  C  CA    . SER   B 1  147 ? 22.150  19.621  -8.497  1.00 26.48  ? 147 SER   C CA    1 
ATOM   4603  C  C     . SER   B 1  147 ? 23.649  19.934  -8.483  1.00 29.71  ? 147 SER   C C     1 
ATOM   4604  O  O     . SER   B 1  147 ? 24.135  20.630  -7.582  1.00 26.79  ? 147 SER   C O     1 
ATOM   4605  C  CB    . SER   B 1  147 ? 21.876  18.110  -8.373  1.00 27.19  ? 147 SER   C CB    1 
ATOM   4606  O  OG    . SER   B 1  147 ? 22.404  17.360  -9.451  1.00 29.64  ? 147 SER   C OG    1 
ATOM   4607  N  N     . GLY   B 1  148 ? 24.393  19.446  -9.483  1.00 30.23  ? 148 GLY   C N     1 
ATOM   4608  C  CA    . GLY   B 1  148 ? 25.847  19.536  -9.444  1.00 28.20  ? 148 GLY   C CA    1 
ATOM   4609  C  C     . GLY   B 1  148 ? 26.417  20.851  -9.935  1.00 27.88  ? 148 GLY   C C     1 
ATOM   4610  O  O     . GLY   B 1  148 ? 27.453  21.297  -9.441  1.00 27.13  ? 148 GLY   C O     1 
ATOM   4611  N  N     . PHE   B 1  149 ? 25.762  21.500  -10.897 1.00 25.31  ? 149 PHE   C N     1 
ATOM   4612  C  CA    . PHE   B 1  149 ? 26.261  22.811  -11.296 1.00 24.51  ? 149 PHE   C CA    1 
ATOM   4613  C  C     . PHE   B 1  149 ? 25.888  23.880  -10.274 1.00 24.88  ? 149 PHE   C C     1 
ATOM   4614  O  O     . PHE   B 1  149 ? 26.659  24.818  -10.054 1.00 24.18  ? 149 PHE   C O     1 
ATOM   4615  C  CB    . PHE   B 1  149 ? 25.755  23.198  -12.698 1.00 29.06  ? 149 PHE   C CB    1 
ATOM   4616  C  CG    . PHE   B 1  149 ? 26.250  24.540  -13.154 1.00 30.47  ? 149 PHE   C CG    1 
ATOM   4617  C  CD1   . PHE   B 1  149 ? 27.528  24.683  -13.666 1.00 30.21  ? 149 PHE   C CD1   1 
ATOM   4618  C  CD2   . PHE   B 1  149 ? 25.462  25.671  -13.020 1.00 26.76  ? 149 PHE   C CD2   1 
ATOM   4619  C  CE1   . PHE   B 1  149 ? 28.001  25.933  -14.061 1.00 24.16  ? 149 PHE   C CE1   1 
ATOM   4620  C  CE2   . PHE   B 1  149 ? 25.936  26.913  -13.409 1.00 29.82  ? 149 PHE   C CE2   1 
ATOM   4621  C  CZ    . PHE   B 1  149 ? 27.206  27.039  -13.923 1.00 28.81  ? 149 PHE   C CZ    1 
ATOM   4622  N  N     . THR   B 1  150 ? 24.720  23.746  -9.638  1.00 31.42  ? 150 THR   C N     1 
ATOM   4623  C  CA    . THR   B 1  150 ? 24.355  24.636  -8.542  1.00 22.64  ? 150 THR   C CA    1 
ATOM   4624  C  C     . THR   B 1  150 ? 25.371  24.567  -7.403  1.00 26.63  ? 150 THR   C C     1 
ATOM   4625  O  O     . THR   B 1  150 ? 25.818  25.598  -6.901  1.00 23.09  ? 150 THR   C O     1 
ATOM   4626  C  CB    . THR   B 1  150 ? 22.955  24.287  -8.046  1.00 25.10  ? 150 THR   C CB    1 
ATOM   4627  O  OG1   . THR   B 1  150 ? 22.032  24.392  -9.131  1.00 25.21  ? 150 THR   C OG1   1 
ATOM   4628  C  CG2   . THR   B 1  150 ? 22.528  25.227  -6.947  1.00 29.30  ? 150 THR   C CG2   1 
ATOM   4629  N  N     . SER   B 1  151 ? 25.750  23.355  -6.975  1.00 30.84  ? 151 SER   C N     1 
ATOM   4630  C  CA    A SER   B 1  151 ? 26.689  23.239  -5.863  0.29 27.37  ? 151 SER   C CA    1 
ATOM   4631  C  CA    B SER   B 1  151 ? 26.700  23.219  -5.872  0.71 28.87  ? 151 SER   C CA    1 
ATOM   4632  C  C     . SER   B 1  151 ? 28.033  23.868  -6.213  1.00 30.37  ? 151 SER   C C     1 
ATOM   4633  O  O     . SER   B 1  151 ? 28.604  24.623  -5.411  1.00 28.59  ? 151 SER   C O     1 
ATOM   4634  C  CB    A SER   B 1  151 ? 26.859  21.772  -5.469  0.29 29.62  ? 151 SER   C CB    1 
ATOM   4635  C  CB    B SER   B 1  151 ? 26.913  21.745  -5.540  0.71 31.26  ? 151 SER   C CB    1 
ATOM   4636  O  OG    A SER   B 1  151 ? 27.555  21.053  -6.469  0.29 32.01  ? 151 SER   C OG    1 
ATOM   4637  O  OG    B SER   B 1  151 ? 25.859  21.223  -4.768  0.71 34.18  ? 151 SER   C OG    1 
ATOM   4638  N  N     . LEU   B 1  152 ? 28.556  23.564  -7.408  1.00 28.77  ? 152 LEU   C N     1 
ATOM   4639  C  CA    . LEU   B 1  152 ? 29.819  24.144  -7.849  1.00 26.90  ? 152 LEU   C CA    1 
ATOM   4640  C  C     . LEU   B 1  152 ? 29.750  25.665  -7.869  1.00 27.59  ? 152 LEU   C C     1 
ATOM   4641  O  O     . LEU   B 1  152 ? 30.720  26.337  -7.502  1.00 31.04  ? 152 LEU   C O     1 
ATOM   4642  C  CB    . LEU   B 1  152 ? 30.193  23.607  -9.234  1.00 31.30  ? 152 LEU   C CB    1 
ATOM   4643  C  CG    . LEU   B 1  152 ? 31.377  24.330  -9.909  1.00 43.55  ? 152 LEU   C CG    1 
ATOM   4644  C  CD1   . LEU   B 1  152 ? 32.702  23.821  -9.347  1.00 22.93  ? 152 LEU   C CD1   1 
ATOM   4645  C  CD2   . LEU   B 1  152 ? 31.337  24.314  -11.458 1.00 21.32  ? 152 LEU   C CD2   1 
ATOM   4646  N  N     . LEU   B 1  153 ? 28.608  26.220  -8.294  1.00 22.29  ? 153 LEU   C N     1 
ATOM   4647  C  CA    . LEU   B 1  153 ? 28.416  27.666  -8.340  1.00 24.39  ? 153 LEU   C CA    1 
ATOM   4648  C  C     . LEU   B 1  153 ? 28.348  28.273  -6.946  1.00 27.64  ? 153 LEU   C C     1 
ATOM   4649  O  O     . LEU   B 1  153 ? 28.889  29.358  -6.700  1.00 30.49  ? 153 LEU   C O     1 
ATOM   4650  C  CB    . LEU   B 1  153 ? 27.131  27.992  -9.096  1.00 26.51  ? 153 LEU   C CB    1 
ATOM   4651  C  CG    . LEU   B 1  153 ? 26.728  29.462  -9.019  1.00 28.84  ? 153 LEU   C CG    1 
ATOM   4652  C  CD1   . LEU   B 1  153 ? 27.528  30.281  -10.027 1.00 24.94  ? 153 LEU   C CD1   1 
ATOM   4653  C  CD2   . LEU   B 1  153 ? 25.239  29.628  -9.204  1.00 25.35  ? 153 LEU   C CD2   1 
ATOM   4654  N  N     . MET   B 1  154 ? 27.645  27.610  -6.040  1.00 25.58  ? 154 MET   C N     1 
ATOM   4655  C  CA    . MET   B 1  154 ? 27.594  28.064  -4.662  1.00 30.28  ? 154 MET   C CA    1 
ATOM   4656  C  C     . MET   B 1  154 ? 28.976  28.048  -4.032  1.00 36.45  ? 154 MET   C C     1 
ATOM   4657  O  O     . MET   B 1  154 ? 29.356  29.004  -3.346  1.00 34.32  ? 154 MET   C O     1 
ATOM   4658  C  CB    . MET   B 1  154 ? 26.618  27.201  -3.867  1.00 24.25  ? 154 MET   C CB    1 
ATOM   4659  C  CG    . MET   B 1  154 ? 25.205  27.325  -4.391  1.00 20.53  ? 154 MET   C CG    1 
ATOM   4660  S  SD    . MET   B 1  154 ? 24.466  28.861  -3.839  1.00 32.75  ? 154 MET   C SD    1 
ATOM   4661  C  CE    . MET   B 1  154 ? 23.841  28.327  -2.259  1.00 23.05  ? 154 MET   C CE    1 
ATOM   4662  N  N     . GLU   B 1  155 ? 29.751  26.981  -4.251  1.00 31.67  ? 155 GLU   C N     1 
ATOM   4663  C  CA    . GLU   B 1  155 ? 31.127  27.000  -3.764  1.00 32.57  ? 155 GLU   C CA    1 
ATOM   4664  C  C     . GLU   B 1  155 ? 31.877  28.193  -4.338  1.00 38.41  ? 155 GLU   C C     1 
ATOM   4665  O  O     . GLU   B 1  155 ? 32.543  28.941  -3.608  1.00 44.40  ? 155 GLU   C O     1 
ATOM   4666  C  CB    . GLU   B 1  155 ? 31.844  25.705  -4.118  1.00 38.69  ? 155 GLU   C CB    1 
ATOM   4667  C  CG    . GLU   B 1  155 ? 31.417  24.512  -3.288  1.00 35.51  ? 155 GLU   C CG    1 
ATOM   4668  C  CD    . GLU   B 1  155 ? 31.711  23.210  -3.991  1.00 39.53  ? 155 GLU   C CD    1 
ATOM   4669  O  OE1   . GLU   B 1  155 ? 32.433  23.225  -5.003  1.00 46.61  ? 155 GLU   C OE1   1 
ATOM   4670  O  OE2   . GLU   B 1  155 ? 31.213  22.166  -3.548  1.00 41.73  ? 155 GLU   C OE2   1 
ATOM   4671  N  N     . ARG   B 1  156 ? 31.745  28.413  -5.643  1.00 29.30  ? 156 ARG   C N     1 
ATOM   4672  C  CA    . ARG   B 1  156 ? 32.483  29.502  -6.268  1.00 27.24  ? 156 ARG   C CA    1 
ATOM   4673  C  C     . ARG   B 1  156 ? 32.030  30.860  -5.753  1.00 32.50  ? 156 ARG   C C     1 
ATOM   4674  O  O     . ARG   B 1  156 ? 32.847  31.780  -5.662  1.00 36.16  ? 156 ARG   C O     1 
ATOM   4675  C  CB    . ARG   B 1  156 ? 32.352  29.417  -7.789  1.00 28.02  ? 156 ARG   C CB    1 
ATOM   4676  C  CG    . ARG   B 1  156 ? 32.957  28.131  -8.362  1.00 33.95  ? 156 ARG   C CG    1 
ATOM   4677  C  CD    . ARG   B 1  156 ? 34.460  28.083  -8.146  1.00 25.60  ? 156 ARG   C CD    1 
ATOM   4678  N  NE    . ARG   B 1  156 ? 35.082  29.155  -8.910  1.00 39.73  ? 156 ARG   C NE    1 
ATOM   4679  C  CZ    . ARG   B 1  156 ? 35.497  29.039  -10.165 1.00 38.90  ? 156 ARG   C CZ    1 
ATOM   4680  N  NH1   . ARG   B 1  156 ? 35.497  27.864  -10.792 1.00 32.57  ? 156 ARG   C NH1   1 
ATOM   4681  N  NH2   . ARG   B 1  156 ? 35.907  30.130  -10.814 1.00 18.93  ? 156 ARG   C NH2   1 
ATOM   4682  N  N     . LEU   B 1  157 ? 30.745  31.010  -5.413  1.00 34.76  ? 157 LEU   C N     1 
ATOM   4683  C  CA    . LEU   B 1  157 ? 30.255  32.297  -4.922  1.00 26.12  ? 157 LEU   C CA    1 
ATOM   4684  C  C     . LEU   B 1  157 ? 30.781  32.593  -3.522  1.00 27.41  ? 157 LEU   C C     1 
ATOM   4685  O  O     . LEU   B 1  157 ? 31.115  33.738  -3.212  1.00 29.93  ? 157 LEU   C O     1 
ATOM   4686  C  CB    . LEU   B 1  157 ? 28.729  32.326  -4.952  1.00 24.94  ? 157 LEU   C CB    1 
ATOM   4687  C  CG    . LEU   B 1  157 ? 28.098  32.362  -6.352  1.00 30.42  ? 157 LEU   C CG    1 
ATOM   4688  C  CD1   . LEU   B 1  157 ? 26.566  32.565  -6.293  1.00 23.33  ? 157 LEU   C CD1   1 
ATOM   4689  C  CD2   . LEU   B 1  157 ? 28.747  33.448  -7.214  1.00 26.98  ? 157 LEU   C CD2   1 
ATOM   4690  N  N     . SER   B 1  158 ? 30.877  31.572  -2.670  1.00 32.02  ? 158 SER   C N     1 
ATOM   4691  C  CA    . SER   B 1  158 ? 31.507  31.748  -1.367  1.00 28.24  ? 158 SER   C CA    1 
ATOM   4692  C  C     . SER   B 1  158 ? 32.922  32.290  -1.513  1.00 38.80  ? 158 SER   C C     1 
ATOM   4693  O  O     . SER   B 1  158 ? 33.368  33.112  -0.704  1.00 32.27  ? 158 SER   C O     1 
ATOM   4694  C  CB    . SER   B 1  158 ? 31.530  30.420  -0.607  1.00 34.34  ? 158 SER   C CB    1 
ATOM   4695  O  OG    . SER   B 1  158 ? 30.233  29.994  -0.219  1.00 39.14  ? 158 SER   C OG    1 
ATOM   4696  N  N     . VAL   B 1  159 ? 33.653  31.835  -2.537  1.00 44.22  ? 159 VAL   C N     1 
ATOM   4697  C  CA    . VAL   B 1  159 ? 35.017  32.314  -2.729  1.00 36.50  ? 159 VAL   C CA    1 
ATOM   4698  C  C     . VAL   B 1  159 ? 35.014  33.766  -3.199  1.00 36.72  ? 159 VAL   C C     1 
ATOM   4699  O  O     . VAL   B 1  159 ? 35.701  34.618  -2.624  1.00 45.34  ? 159 VAL   C O     1 
ATOM   4700  C  CB    . VAL   B 1  159 ? 35.781  31.397  -3.696  1.00 34.86  ? 159 VAL   C CB    1 
ATOM   4701  C  CG1   . VAL   B 1  159 ? 37.054  32.067  -4.157  1.00 35.14  ? 159 VAL   C CG1   1 
ATOM   4702  C  CG2   . VAL   B 1  159 ? 36.109  30.090  -3.009  1.00 38.47  ? 159 VAL   C CG2   1 
ATOM   4703  N  N     . ASP   B 1  160 ? 34.220  34.080  -4.220  1.00 27.79  ? 160 ASP   C N     1 
ATOM   4704  C  CA    . ASP   B 1  160 ? 34.223  35.419  -4.803  1.00 32.86  ? 160 ASP   C CA    1 
ATOM   4705  C  C     . ASP   B 1  160 ? 33.454  36.457  -3.993  1.00 32.14  ? 160 ASP   C C     1 
ATOM   4706  O  O     . ASP   B 1  160 ? 33.545  37.649  -4.308  1.00 34.91  ? 160 ASP   C O     1 
ATOM   4707  C  CB    . ASP   B 1  160 ? 33.633  35.388  -6.225  1.00 34.89  ? 160 ASP   C CB    1 
ATOM   4708  C  CG    . ASP   B 1  160 ? 34.478  34.566  -7.204  1.00 44.24  ? 160 ASP   C CG    1 
ATOM   4709  O  OD1   . ASP   B 1  160 ? 35.268  33.686  -6.746  1.00 35.49  ? 160 ASP   C OD1   1 
ATOM   4710  O  OD2   . ASP   B 1  160 ? 34.340  34.817  -8.433  1.00 34.34  ? 160 ASP   C OD2   1 
ATOM   4711  N  N     . TYR   B 1  161 ? 32.664  36.050  -3.005  1.00 30.99  ? 161 TYR   C N     1 
ATOM   4712  C  CA    . TYR   B 1  161 ? 31.777  36.991  -2.335  1.00 24.67  ? 161 TYR   C CA    1 
ATOM   4713  C  C     . TYR   B 1  161 ? 31.765  36.807  -0.826  1.00 35.44  ? 161 TYR   C C     1 
ATOM   4714  O  O     . TYR   B 1  161 ? 30.965  37.460  -0.148  1.00 43.45  ? 161 TYR   C O     1 
ATOM   4715  C  CB    . TYR   B 1  161 ? 30.355  36.880  -2.883  1.00 23.11  ? 161 TYR   C CB    1 
ATOM   4716  C  CG    . TYR   B 1  161 ? 30.289  37.327  -4.302  1.00 31.55  ? 161 TYR   C CG    1 
ATOM   4717  C  CD1   . TYR   B 1  161 ? 30.251  38.674  -4.617  1.00 21.79  ? 161 TYR   C CD1   1 
ATOM   4718  C  CD2   . TYR   B 1  161 ? 30.336  36.398  -5.352  1.00 34.50  ? 161 TYR   C CD2   1 
ATOM   4719  C  CE1   . TYR   B 1  161 ? 30.228  39.102  -5.947  1.00 31.18  ? 161 TYR   C CE1   1 
ATOM   4720  C  CE2   . TYR   B 1  161 ? 30.316  36.816  -6.684  1.00 26.83  ? 161 TYR   C CE2   1 
ATOM   4721  C  CZ    . TYR   B 1  161 ? 30.253  38.166  -6.976  1.00 29.18  ? 161 TYR   C CZ    1 
ATOM   4722  O  OH    . TYR   B 1  161 ? 30.222  38.583  -8.289  1.00 29.18  ? 161 TYR   C OH    1 
ATOM   4723  N  N     . GLY   B 1  162 ? 32.636  35.968  -0.278  1.00 38.25  ? 162 GLY   C N     1 
ATOM   4724  C  CA    . GLY   B 1  162 ? 32.655  35.804  1.151   1.00 40.58  ? 162 GLY   C CA    1 
ATOM   4725  C  C     . GLY   B 1  162 ? 31.305  35.341  1.657   1.00 46.66  ? 162 GLY   C C     1 
ATOM   4726  O  O     . GLY   B 1  162 ? 30.541  34.662  0.956   1.00 46.39  ? 162 GLY   C O     1 
ATOM   4727  N  N     . LYS   B 1  163 ? 31.005  35.728  2.900   1.00 48.69  ? 163 LYS   C N     1 
ATOM   4728  C  CA    . LYS   B 1  163 ? 29.783  35.334  3.589   1.00 47.53  ? 163 LYS   C CA    1 
ATOM   4729  C  C     . LYS   B 1  163 ? 28.541  36.047  3.057   1.00 47.61  ? 163 LYS   C C     1 
ATOM   4730  O  O     . LYS   B 1  163 ? 27.444  35.794  3.583   1.00 45.78  ? 163 LYS   C O     1 
ATOM   4731  C  CB    . LYS   B 1  163 ? 29.929  35.589  5.097   1.00 46.61  ? 163 LYS   C CB    1 
ATOM   4732  C  CG    . LYS   B 1  163 ? 30.991  34.742  5.786   1.00 47.91  ? 163 LYS   C CG    1 
ATOM   4733  C  CD    . LYS   B 1  163 ? 30.747  33.261  5.583   1.00 43.00  ? 163 LYS   C CD    1 
ATOM   4734  C  CE    . LYS   B 1  163 ? 30.866  32.501  6.899   1.00 53.24  ? 163 LYS   C CE    1 
ATOM   4735  N  NZ    . LYS   B 1  163 ? 30.673  31.019  6.748   1.00 55.49  ? 163 LYS   C NZ    1 
ATOM   4736  N  N     . LYS   B 1  164 ? 28.701  36.941  2.072   1.00 38.68  ? 164 LYS   C N     1 
ATOM   4737  C  CA    . LYS   B 1  164 ? 27.590  37.550  1.344   1.00 36.05  ? 164 LYS   C CA    1 
ATOM   4738  C  C     . LYS   B 1  164 ? 26.507  36.519  1.061   1.00 37.69  ? 164 LYS   C C     1 
ATOM   4739  O  O     . LYS   B 1  164 ? 26.788  35.425  0.560   1.00 38.49  ? 164 LYS   C O     1 
ATOM   4740  C  CB    . LYS   B 1  164 ? 28.109  38.135  0.038   1.00 34.93  ? 164 LYS   C CB    1 
ATOM   4741  C  CG    . LYS   B 1  164 ? 27.054  38.493  -0.921  1.00 32.10  ? 164 LYS   C CG    1 
ATOM   4742  C  CD    . LYS   B 1  164 ? 26.631  39.891  -0.643  1.00 44.67  ? 164 LYS   C CD    1 
ATOM   4743  C  CE    . LYS   B 1  164 ? 27.779  40.843  -0.910  1.00 49.55  ? 164 LYS   C CE    1 
ATOM   4744  N  NZ    . LYS   B 1  164 ? 27.598  42.139  -0.167  1.00 47.90  ? 164 LYS   C NZ    1 
ATOM   4745  N  N     . SER   B 1  165 ? 25.266  36.870  1.377   1.00 35.66  ? 165 SER   C N     1 
ATOM   4746  C  CA    . SER   B 1  165 ? 24.297  35.826  1.672   1.00 29.57  ? 165 SER   C CA    1 
ATOM   4747  C  C     . SER   B 1  165 ? 23.711  35.203  0.407   1.00 32.39  ? 165 SER   C C     1 
ATOM   4748  O  O     . SER   B 1  165 ? 23.667  35.810  -0.671  1.00 34.12  ? 165 SER   C O     1 
ATOM   4749  C  CB    . SER   B 1  165 ? 23.189  36.353  2.580   1.00 21.10  ? 165 SER   C CB    1 
ATOM   4750  O  OG    . SER   B 1  165 ? 22.225  37.050  1.861   1.00 26.96  ? 165 SER   C OG    1 
ATOM   4751  N  N     . LYS   B 1  166 ? 23.293  33.951  0.554   1.00 25.15  ? 166 LYS   C N     1 
ATOM   4752  C  CA    . LYS   B 1  166 ? 22.829  33.130  -0.551  1.00 22.27  ? 166 LYS   C CA    1 
ATOM   4753  C  C     . LYS   B 1  166 ? 21.597  32.380  -0.066  1.00 27.62  ? 166 LYS   C C     1 
ATOM   4754  O  O     . LYS   B 1  166 ? 21.705  31.494  0.781   1.00 30.26  ? 166 LYS   C O     1 
ATOM   4755  C  CB    . LYS   B 1  166 ? 23.930  32.178  -1.013  1.00 17.74  ? 166 LYS   C CB    1 
ATOM   4756  C  CG    . LYS   B 1  166 ? 25.255  32.914  -1.228  1.00 28.02  ? 166 LYS   C CG    1 
ATOM   4757  C  CD    . LYS   B 1  166 ? 26.167  32.268  -2.271  1.00 32.79  ? 166 LYS   C CD    1 
ATOM   4758  C  CE    . LYS   B 1  166 ? 27.048  31.172  -1.661  1.00 37.69  ? 166 LYS   C CE    1 
ATOM   4759  N  NZ    . LYS   B 1  166 ? 28.025  31.680  -0.639  1.00 41.35  ? 166 LYS   C NZ    1 
ATOM   4760  N  N     . LEU   B 1  167 ? 20.432  32.782  -0.559  1.00 27.93  ? 167 LEU   C N     1 
ATOM   4761  C  CA    . LEU   B 1  167 ? 19.174  32.084  -0.357  1.00 24.76  ? 167 LEU   C CA    1 
ATOM   4762  C  C     . LEU   B 1  167 ? 18.908  31.157  -1.536  1.00 27.24  ? 167 LEU   C C     1 
ATOM   4763  O  O     . LEU   B 1  167 ? 19.193  31.502  -2.687  1.00 31.87  ? 167 LEU   C O     1 
ATOM   4764  C  CB    . LEU   B 1  167 ? 18.010  33.070  -0.199  1.00 20.61  ? 167 LEU   C CB    1 
ATOM   4765  C  CG    . LEU   B 1  167 ? 17.982  33.727  1.182   1.00 25.40  ? 167 LEU   C CG    1 
ATOM   4766  C  CD1   . LEU   B 1  167 ? 19.009  34.839  1.303   1.00 34.44  ? 167 LEU   C CD1   1 
ATOM   4767  C  CD2   . LEU   B 1  167 ? 16.605  34.218  1.516   1.00 24.81  ? 167 LEU   C CD2   1 
ATOM   4768  N  N     . GLU   B 1  168 ? 18.350  29.992  -1.241  1.00 18.19  ? 168 GLU   C N     1 
ATOM   4769  C  CA    . GLU   B 1  168 ? 18.007  28.991  -2.231  1.00 18.93  ? 168 GLU   C CA    1 
ATOM   4770  C  C     . GLU   B 1  168 ? 16.506  28.829  -2.351  1.00 30.11  ? 168 GLU   C C     1 
ATOM   4771  O  O     . GLU   B 1  168 ? 15.782  28.877  -1.344  1.00 34.66  ? 168 GLU   C O     1 
ATOM   4772  C  CB    . GLU   B 1  168 ? 18.577  27.639  -1.856  1.00 24.68  ? 168 GLU   C CB    1 
ATOM   4773  C  CG    . GLU   B 1  168 ? 19.993  27.475  -2.177  1.00 23.31  ? 168 GLU   C CG    1 
ATOM   4774  C  CD    . GLU   B 1  168 ? 20.452  26.165  -1.731  1.00 22.19  ? 168 GLU   C CD    1 
ATOM   4775  O  OE1   . GLU   B 1  168 ? 20.721  26.061  -0.514  1.00 27.44  ? 168 GLU   C OE1   1 
ATOM   4776  O  OE2   . GLU   B 1  168 ? 20.499  25.240  -2.584  1.00 25.88  ? 168 GLU   C OE2   1 
ATOM   4777  N  N     . PHE   B 1  169 ? 16.054  28.612  -3.586  1.00 24.08  ? 169 PHE   C N     1 
ATOM   4778  C  CA    . PHE   B 1  169 ? 14.765  27.992  -3.862  1.00 20.83  ? 169 PHE   C CA    1 
ATOM   4779  C  C     . PHE   B 1  169 ? 15.072  26.678  -4.563  1.00 30.48  ? 169 PHE   C C     1 
ATOM   4780  O  O     . PHE   B 1  169 ? 15.589  26.669  -5.685  1.00 32.09  ? 169 PHE   C O     1 
ATOM   4781  C  CB    . PHE   B 1  169 ? 13.869  28.899  -4.697  1.00 17.96  ? 169 PHE   C CB    1 
ATOM   4782  C  CG    . PHE   B 1  169 ? 13.326  30.070  -3.928  1.00 30.40  ? 169 PHE   C CG    1 
ATOM   4783  C  CD1   . PHE   B 1  169 ? 14.052  31.251  -3.818  1.00 35.95  ? 169 PHE   C CD1   1 
ATOM   4784  C  CD2   . PHE   B 1  169 ? 12.107  29.991  -3.291  1.00 29.31  ? 169 PHE   C CD2   1 
ATOM   4785  C  CE1   . PHE   B 1  169 ? 13.555  32.344  -3.098  1.00 26.72  ? 169 PHE   C CE1   1 
ATOM   4786  C  CE2   . PHE   B 1  169 ? 11.610  31.078  -2.576  1.00 33.22  ? 169 PHE   C CE2   1 
ATOM   4787  C  CZ    . PHE   B 1  169 ? 12.335  32.256  -2.491  1.00 24.41  ? 169 PHE   C CZ    1 
ATOM   4788  N  N     . SER   B 1  170 ? 14.796  25.570  -3.886  1.00 27.96  ? 170 SER   C N     1 
ATOM   4789  C  CA    . SER   B 1  170 ? 15.157  24.250  -4.377  1.00 25.23  ? 170 SER   C CA    1 
ATOM   4790  C  C     . SER   B 1  170 ? 13.892  23.454  -4.622  1.00 25.92  ? 170 SER   C C     1 
ATOM   4791  O  O     . SER   B 1  170 ? 13.054  23.321  -3.725  1.00 27.12  ? 170 SER   C O     1 
ATOM   4792  C  CB    . SER   B 1  170 ? 16.041  23.501  -3.380  1.00 24.19  ? 170 SER   C CB    1 
ATOM   4793  O  OG    . SER   B 1  170 ? 17.020  24.339  -2.823  1.00 32.78  ? 170 SER   C OG    1 
ATOM   4794  N  N     . ILE   B 1  171 ? 13.771  22.905  -5.818  1.00 24.46  ? 171 ILE   C N     1 
ATOM   4795  C  CA    . ILE   B 1  171 ? 12.695  21.982  -6.135  1.00 20.09  ? 171 ILE   C CA    1 
ATOM   4796  C  C     . ILE   B 1  171 ? 13.155  20.597  -5.718  1.00 21.19  ? 171 ILE   C C     1 
ATOM   4797  O  O     . ILE   B 1  171 ? 14.205  20.124  -6.151  1.00 33.67  ? 171 ILE   C O     1 
ATOM   4798  C  CB    . ILE   B 1  171 ? 12.338  22.040  -7.625  1.00 15.85  ? 171 ILE   C CB    1 
ATOM   4799  C  CG1   . ILE   B 1  171 ? 12.287  23.489  -8.048  1.00 19.40  ? 171 ILE   C CG1   1 
ATOM   4800  C  CG2   . ILE   B 1  171 ? 11.007  21.490  -7.852  1.00 20.93  ? 171 ILE   C CG2   1 
ATOM   4801  C  CD1   . ILE   B 1  171 ? 11.384  24.275  -7.180  1.00 29.49  ? 171 ILE   C CD1   1 
ATOM   4802  N  N     . TYR   B 1  172 ? 12.412  19.980  -4.855  1.00 20.43  ? 172 TYR   C N     1 
ATOM   4803  C  CA    . TYR   B 1  172 ? 12.500  18.680  -4.222  1.00 24.92  ? 172 TYR   C CA    1 
ATOM   4804  C  C     . TYR   B 1  172 ? 11.694  17.684  -5.061  1.00 29.07  ? 172 TYR   C C     1 
ATOM   4805  O  O     . TYR   B 1  172 ? 10.651  18.045  -5.614  1.00 29.04  ? 172 TYR   C O     1 
ATOM   4806  C  CB    . TYR   B 1  172 ? 11.964  18.786  -2.780  1.00 21.05  ? 172 TYR   C CB    1 
ATOM   4807  C  CG    . TYR   B 1  172 ? 11.896  17.520  -1.945  1.00 25.91  ? 172 TYR   C CG    1 
ATOM   4808  C  CD1   . TYR   B 1  172 ? 10.823  16.634  -2.066  1.00 25.90  ? 172 TYR   C CD1   1 
ATOM   4809  C  CD2   . TYR   B 1  172 ? 12.875  17.231  -1.004  1.00 23.12  ? 172 TYR   C CD2   1 
ATOM   4810  C  CE1   . TYR   B 1  172 ? 10.743  15.499  -1.287  1.00 22.05  ? 172 TYR   C CE1   1 
ATOM   4811  C  CE2   . TYR   B 1  172 ? 12.795  16.086  -0.220  1.00 26.08  ? 172 TYR   C CE2   1 
ATOM   4812  C  CZ    . TYR   B 1  172 ? 11.724  15.231  -0.371  1.00 24.10  ? 172 TYR   C CZ    1 
ATOM   4813  O  OH    . TYR   B 1  172 ? 11.643  14.106  0.397   1.00 26.47  ? 172 TYR   C OH    1 
ATOM   4814  N  N     . PRO   B 1  173 ? 12.149  16.455  -5.279  1.00 30.67  ? 173 PRO   C N     1 
ATOM   4815  C  CA    . PRO   B 1  173 ? 11.551  15.632  -6.341  1.00 27.78  ? 173 PRO   C CA    1 
ATOM   4816  C  C     . PRO   B 1  173 ? 10.325  14.837  -5.915  1.00 28.97  ? 173 PRO   C C     1 
ATOM   4817  O  O     . PRO   B 1  173 ? 10.196  14.372  -4.785  1.00 40.74  ? 173 PRO   C O     1 
ATOM   4818  C  CB    . PRO   B 1  173 ? 12.702  14.701  -6.755  1.00 17.43  ? 173 PRO   C CB    1 
ATOM   4819  C  CG    . PRO   B 1  173 ? 13.683  14.726  -5.670  1.00 21.91  ? 173 PRO   C CG    1 
ATOM   4820  C  CD    . PRO   B 1  173 ? 13.431  15.919  -4.791  1.00 33.33  ? 173 PRO   C CD    1 
ATOM   4821  N  N     . ALA   B 1  174 ? 9.402   14.705  -6.860  1.00 38.74  ? 174 ALA   C N     1 
ATOM   4822  C  CA    . ALA   B 1  174 ? 8.172   13.938  -6.704  1.00 40.11  ? 174 ALA   C CA    1 
ATOM   4823  C  C     . ALA   B 1  174 ? 7.991   12.979  -7.875  1.00 33.83  ? 174 ALA   C C     1 
ATOM   4824  O  O     . ALA   B 1  174 ? 8.163   13.371  -9.036  1.00 33.26  ? 174 ALA   C O     1 
ATOM   4825  C  CB    . ALA   B 1  174 ? 6.955   14.869  -6.615  1.00 39.90  ? 174 ALA   C CB    1 
ATOM   4826  N  N     . PRO   B 1  175 ? 7.592   11.736  -7.611  1.00 35.99  ? 175 PRO   C N     1 
ATOM   4827  C  CA    . PRO   B 1  175 ? 7.453   10.760  -8.710  1.00 39.41  ? 175 PRO   C CA    1 
ATOM   4828  C  C     . PRO   B 1  175 ? 6.440   11.147  -9.777  1.00 36.76  ? 175 PRO   C C     1 
ATOM   4829  O  O     . PRO   B 1  175 ? 6.553   10.669  -10.910 1.00 31.70  ? 175 PRO   C O     1 
ATOM   4830  C  CB    . PRO   B 1  175 ? 7.008   9.483   -7.988  1.00 35.39  ? 175 PRO   C CB    1 
ATOM   4831  C  CG    . PRO   B 1  175 ? 7.073   9.795   -6.518  1.00 44.58  ? 175 PRO   C CG    1 
ATOM   4832  C  CD    . PRO   B 1  175 ? 6.943   11.263  -6.386  1.00 31.43  ? 175 PRO   C CD    1 
ATOM   4833  N  N     . GLN   B 1  176 ? 5.439   11.973  -9.451  1.00 39.55  ? 176 GLN   C N     1 
ATOM   4834  C  CA    . GLN   B 1  176 ? 4.450   12.352  -10.451 1.00 30.44  ? 176 GLN   C CA    1 
ATOM   4835  C  C     . GLN   B 1  176 ? 5.090   13.048  -11.640 1.00 37.99  ? 176 GLN   C C     1 
ATOM   4836  O  O     . GLN   B 1  176 ? 4.564   12.947  -12.754 1.00 43.79  ? 176 GLN   C O     1 
ATOM   4837  C  CB    . GLN   B 1  176 ? 3.374   13.266  -9.863  1.00 36.45  ? 176 GLN   C CB    1 
ATOM   4838  C  CG    . GLN   B 1  176 ? 2.480   12.658  -8.834  1.00 35.52  ? 176 GLN   C CG    1 
ATOM   4839  C  CD    . GLN   B 1  176 ? 3.149   12.553  -7.488  1.00 42.84  ? 176 GLN   C CD    1 
ATOM   4840  O  OE1   . GLN   B 1  176 ? 4.357   12.774  -7.364  1.00 40.76  ? 176 GLN   C OE1   1 
ATOM   4841  N  NE2   . GLN   B 1  176 ? 2.372   12.216  -6.461  1.00 40.54  ? 176 GLN   C NE2   1 
ATOM   4842  N  N     . VAL   B 1  177 ? 6.195   13.776  -11.430 1.00 41.43  ? 177 VAL   C N     1 
ATOM   4843  C  CA    . VAL   B 1  177 ? 6.827   14.557  -12.493 1.00 39.00  ? 177 VAL   C CA    1 
ATOM   4844  C  C     . VAL   B 1  177 ? 8.312   14.262  -12.669 1.00 29.54  ? 177 VAL   C C     1 
ATOM   4845  O  O     . VAL   B 1  177 ? 8.934   14.843  -13.551 1.00 42.46  ? 177 VAL   C O     1 
ATOM   4846  C  CB    . VAL   B 1  177 ? 6.621   16.085  -12.312 1.00 33.55  ? 177 VAL   C CB    1 
ATOM   4847  C  CG1   . VAL   B 1  177 ? 5.191   16.506  -12.600 1.00 38.67  ? 177 VAL   C CG1   1 
ATOM   4848  C  CG2   . VAL   B 1  177 ? 7.035   16.539  -10.930 1.00 35.65  ? 177 VAL   C CG2   1 
ATOM   4849  N  N     . SER   B 1  178 ? 8.908   13.371  -11.888 1.00 31.90  ? 178 SER   C N     1 
ATOM   4850  C  CA    . SER   B 1  178 ? 10.356  13.183  -11.956 1.00 38.87  ? 178 SER   C CA    1 
ATOM   4851  C  C     . SER   B 1  178 ? 10.778  12.412  -13.209 1.00 49.38  ? 178 SER   C C     1 
ATOM   4852  O  O     . SER   B 1  178 ? 10.058  11.530  -13.696 1.00 49.93  ? 178 SER   C O     1 
ATOM   4853  C  CB    . SER   B 1  178 ? 10.855  12.423  -10.735 1.00 41.44  ? 178 SER   C CB    1 
ATOM   4854  O  OG    . SER   B 1  178 ? 10.822  11.037  -11.039 1.00 47.82  ? 178 SER   C OG    1 
ATOM   4855  N  N     . THR   B 1  179 ? 11.993  12.713  -13.704 1.00 39.61  ? 179 THR   C N     1 
ATOM   4856  C  CA    . THR   B 1  179 ? 12.443  12.125  -14.965 1.00 46.26  ? 179 THR   C CA    1 
ATOM   4857  C  C     . THR   B 1  179 ? 13.786  11.409  -14.846 1.00 44.91  ? 179 THR   C C     1 
ATOM   4858  O  O     . THR   B 1  179 ? 14.433  11.149  -15.874 1.00 45.31  ? 179 THR   C O     1 
ATOM   4859  C  CB    . THR   B 1  179 ? 12.506  13.174  -16.095 1.00 53.64  ? 179 THR   C CB    1 
ATOM   4860  O  OG1   . THR   B 1  179 ? 13.343  14.285  -15.729 1.00 37.90  ? 179 THR   C OG1   1 
ATOM   4861  C  CG2   . THR   B 1  179 ? 11.092  13.675  -16.450 1.00 45.05  ? 179 THR   C CG2   1 
ATOM   4862  N  N     . ALA   B 1  180 ? 14.213  11.063  -13.630 1.00 43.22  ? 180 ALA   C N     1 
ATOM   4863  C  CA    . ALA   B 1  180 ? 15.430  10.278  -13.443 1.00 34.82  ? 180 ALA   C CA    1 
ATOM   4864  C  C     . ALA   B 1  180 ? 15.339  9.495   -12.142 1.00 38.85  ? 180 ALA   C C     1 
ATOM   4865  O  O     . ALA   B 1  180 ? 14.947  10.031  -11.097 1.00 33.12  ? 180 ALA   C O     1 
ATOM   4866  C  CB    . ALA   B 1  180 ? 16.691  11.156  -13.449 1.00 16.44  ? 180 ALA   C CB    1 
ATOM   4867  N  N     . VAL   B 1  181 ? 15.705  8.216   -12.222 1.00 36.01  ? 181 VAL   C N     1 
ATOM   4868  C  CA    . VAL   B 1  181 ? 15.727  7.343   -11.067 1.00 25.42  ? 181 VAL   C CA    1 
ATOM   4869  C  C     . VAL   B 1  181 ? 16.760  7.777   -10.032 1.00 30.51  ? 181 VAL   C C     1 
ATOM   4870  O  O     . VAL   B 1  181 ? 16.604  7.469   -8.846  1.00 40.67  ? 181 VAL   C O     1 
ATOM   4871  C  CB    . VAL   B 1  181 ? 15.965  5.902   -11.577 1.00 34.91  ? 181 VAL   C CB    1 
ATOM   4872  C  CG1   . VAL   B 1  181 ? 15.994  4.895   -10.454 1.00 20.86  ? 181 VAL   C CG1   1 
ATOM   4873  C  CG2   . VAL   B 1  181 ? 14.891  5.548   -12.603 1.00 35.64  ? 181 VAL   C CG2   1 
ATOM   4874  N  N     . VAL   B 1  182 ? 17.814  8.495   -10.443 1.00 28.07  ? 182 VAL   C N     1 
ATOM   4875  C  CA    . VAL   B 1  182 ? 18.915  8.817   -9.534  1.00 26.60  ? 182 VAL   C CA    1 
ATOM   4876  C  C     . VAL   B 1  182 ? 18.680  10.106  -8.750  1.00 34.77  ? 182 VAL   C C     1 
ATOM   4877  O  O     . VAL   B 1  182 ? 19.546  10.515  -7.957  1.00 34.69  ? 182 VAL   C O     1 
ATOM   4878  C  CB    . VAL   B 1  182 ? 20.270  8.913   -10.281 1.00 30.51  ? 182 VAL   C CB    1 
ATOM   4879  C  CG1   . VAL   B 1  182 ? 20.811  7.551   -10.588 1.00 28.29  ? 182 VAL   C CG1   1 
ATOM   4880  C  CG2   . VAL   B 1  182 ? 20.131  9.690   -11.565 1.00 27.61  ? 182 VAL   C CG2   1 
ATOM   4881  N  N     . GLU   B 1  183 ? 17.532  10.753  -8.925  1.00 33.23  ? 183 GLU   C N     1 
ATOM   4882  C  CA    . GLU   B 1  183 ? 17.274  11.994  -8.202  1.00 32.17  ? 183 GLU   C CA    1 
ATOM   4883  C  C     . GLU   B 1  183 ? 17.588  11.902  -6.706  1.00 31.46  ? 183 GLU   C C     1 
ATOM   4884  O  O     . GLU   B 1  183 ? 18.156  12.867  -6.158  1.00 34.06  ? 183 GLU   C O     1 
ATOM   4885  C  CB    . GLU   B 1  183 ? 15.829  12.443  -8.474  1.00 30.84  ? 183 GLU   C CB    1 
ATOM   4886  C  CG    . GLU   B 1  183 ? 15.565  12.699  -9.962  1.00 32.46  ? 183 GLU   C CG    1 
ATOM   4887  C  CD    . GLU   B 1  183 ? 14.413  13.668  -10.221 1.00 39.59  ? 183 GLU   C CD    1 
ATOM   4888  O  OE1   . GLU   B 1  183 ? 14.327  14.664  -9.489  1.00 46.11  ? 183 GLU   C OE1   1 
ATOM   4889  O  OE2   . GLU   B 1  183 ? 13.609  13.461  -11.163 1.00 37.48  ? 183 GLU   C OE2   1 
ATOM   4890  N  N     . PRO   B 1  184 ? 17.305  10.811  -6.003  1.00 26.00  ? 184 PRO   C N     1 
ATOM   4891  C  CA    . PRO   B 1  184 ? 17.810  10.709  -4.620  1.00 24.12  ? 184 PRO   C CA    1 
ATOM   4892  C  C     . PRO   B 1  184 ? 19.322  10.864  -4.504  1.00 27.98  ? 184 PRO   C C     1 
ATOM   4893  O  O     . PRO   B 1  184 ? 19.785  11.365  -3.481  1.00 29.10  ? 184 PRO   C O     1 
ATOM   4894  C  CB    . PRO   B 1  184 ? 17.356  9.319   -4.182  1.00 16.80  ? 184 PRO   C CB    1 
ATOM   4895  C  CG    . PRO   B 1  184 ? 16.248  9.008   -5.069  1.00 19.80  ? 184 PRO   C CG    1 
ATOM   4896  C  CD    . PRO   B 1  184 ? 16.513  9.646   -6.385  1.00 15.43  ? 184 PRO   C CD    1 
ATOM   4897  N  N     . TYR   B 1  185 ? 20.112  10.454  -5.509  1.00 29.17  ? 185 TYR   C N     1 
ATOM   4898  C  CA    . TYR   B 1  185 ? 21.563  10.656  -5.434  1.00 34.93  ? 185 TYR   C CA    1 
ATOM   4899  C  C     . TYR   B 1  185 ? 21.916  12.129  -5.612  1.00 30.18  ? 185 TYR   C C     1 
ATOM   4900  O  O     . TYR   B 1  185 ? 22.639  12.724  -4.800  1.00 26.74  ? 185 TYR   C O     1 
ATOM   4901  C  CB    . TYR   B 1  185 ? 22.299  9.813   -6.487  1.00 33.34  ? 185 TYR   C CB    1 
ATOM   4902  C  CG    . TYR   B 1  185 ? 22.391  8.325   -6.198  1.00 33.40  ? 185 TYR   C CG    1 
ATOM   4903  C  CD1   . TYR   B 1  185 ? 22.096  7.818   -4.941  1.00 32.48  ? 185 TYR   C CD1   1 
ATOM   4904  C  CD2   . TYR   B 1  185 ? 22.771  7.427   -7.195  1.00 33.81  ? 185 TYR   C CD2   1 
ATOM   4905  C  CE1   . TYR   B 1  185 ? 22.176  6.453   -4.682  1.00 35.60  ? 185 TYR   C CE1   1 
ATOM   4906  C  CE2   . TYR   B 1  185 ? 22.849  6.071   -6.952  1.00 30.23  ? 185 TYR   C CE2   1 
ATOM   4907  C  CZ    . TYR   B 1  185 ? 22.554  5.586   -5.693  1.00 39.55  ? 185 TYR   C CZ    1 
ATOM   4908  O  OH    . TYR   B 1  185 ? 22.633  4.236   -5.435  1.00 35.84  ? 185 TYR   C OH    1 
ATOM   4909  N  N     . ASN   B 1  186 ? 21.417  12.735  -6.675  1.00 29.31  ? 186 ASN   C N     1 
ATOM   4910  C  CA    . ASN   B 1  186 ? 21.691  14.147  -6.874  1.00 30.12  ? 186 ASN   C CA    1 
ATOM   4911  C  C     . ASN   B 1  186 ? 21.223  14.954  -5.665  1.00 33.97  ? 186 ASN   C C     1 
ATOM   4912  O  O     . ASN   B 1  186 ? 21.983  15.752  -5.104  1.00 33.14  ? 186 ASN   C O     1 
ATOM   4913  C  CB    . ASN   B 1  186 ? 21.034  14.614  -8.175  1.00 29.42  ? 186 ASN   C CB    1 
ATOM   4914  C  CG    . ASN   B 1  186 ? 21.473  13.776  -9.383  1.00 34.79  ? 186 ASN   C CG    1 
ATOM   4915  O  OD1   . ASN   B 1  186 ? 22.520  13.104  -9.354  1.00 25.69  ? 186 ASN   C OD1   1 
ATOM   4916  N  ND2   . ASN   B 1  186 ? 20.668  13.809  -10.450 1.00 32.90  ? 186 ASN   C ND2   1 
ATOM   4917  N  N     . SER   B 1  187 ? 19.983  14.725  -5.220  1.00 34.85  ? 187 SER   C N     1 
ATOM   4918  C  CA    . SER   B 1  187 ? 19.439  15.501  -4.108  1.00 26.88  ? 187 SER   C CA    1 
ATOM   4919  C  C     . SER   B 1  187 ? 20.392  15.499  -2.921  1.00 27.34  ? 187 SER   C C     1 
ATOM   4920  O  O     . SER   B 1  187 ? 20.692  16.552  -2.361  1.00 25.22  ? 187 SER   C O     1 
ATOM   4921  C  CB    . SER   B 1  187 ? 18.072  14.946  -3.689  1.00 31.67  ? 187 SER   C CB    1 
ATOM   4922  O  OG    . SER   B 1  187 ? 17.117  15.058  -4.728  1.00 36.77  ? 187 SER   C OG    1 
ATOM   4923  N  N     . ILE   B 1  188 ? 20.874  14.315  -2.522  1.00 30.67  ? 188 ILE   C N     1 
ATOM   4924  C  CA    . ILE   B 1  188 ? 21.692  14.201  -1.320  1.00 22.75  ? 188 ILE   C CA    1 
ATOM   4925  C  C     . ILE   B 1  188 ? 23.084  14.759  -1.553  1.00 26.88  ? 188 ILE   C C     1 
ATOM   4926  O  O     . ILE   B 1  188 ? 23.692  15.320  -0.635  1.00 27.65  ? 188 ILE   C O     1 
ATOM   4927  C  CB    . ILE   B 1  188 ? 21.761  12.742  -0.833  1.00 28.21  ? 188 ILE   C CB    1 
ATOM   4928  C  CG1   . ILE   B 1  188 ? 20.648  12.439  0.183   1.00 30.11  ? 188 ILE   C CG1   1 
ATOM   4929  C  CG2   . ILE   B 1  188 ? 23.109  12.482  -0.193  1.00 27.07  ? 188 ILE   C CG2   1 
ATOM   4930  C  CD1   . ILE   B 1  188 ? 19.284  12.233  -0.429  1.00 27.14  ? 188 ILE   C CD1   1 
ATOM   4931  N  N     . LEU   B 1  189 ? 23.627  14.609  -2.765  1.00 30.21  ? 189 LEU   C N     1 
ATOM   4932  C  CA    . LEU   B 1  189 ? 24.947  15.168  -3.043  1.00 23.22  ? 189 LEU   C CA    1 
ATOM   4933  C  C     . LEU   B 1  189 ? 24.915  16.697  -3.042  1.00 24.44  ? 189 LEU   C C     1 
ATOM   4934  O  O     . LEU   B 1  189 ? 25.714  17.337  -2.355  1.00 37.18  ? 189 LEU   C O     1 
ATOM   4935  C  CB    . LEU   B 1  189 ? 25.491  14.619  -4.366  1.00 26.36  ? 189 LEU   C CB    1 
ATOM   4936  C  CG    . LEU   B 1  189 ? 25.915  13.144  -4.399  1.00 24.63  ? 189 LEU   C CG    1 
ATOM   4937  C  CD1   . LEU   B 1  189 ? 26.085  12.721  -5.828  1.00 27.94  ? 189 LEU   C CD1   1 
ATOM   4938  C  CD2   . LEU   B 1  189 ? 27.214  12.903  -3.639  1.00 21.84  ? 189 LEU   C CD2   1 
ATOM   4939  N  N     . THR   B 1  190 ? 23.993  17.310  -3.787  1.00 29.49  ? 190 THR   C N     1 
ATOM   4940  C  CA    . THR   B 1  190 ? 23.938  18.774  -3.822  1.00 26.19  ? 190 THR   C CA    1 
ATOM   4941  C  C     . THR   B 1  190 ? 23.621  19.377  -2.456  1.00 24.35  ? 190 THR   C C     1 
ATOM   4942  O  O     . THR   B 1  190 ? 24.119  20.455  -2.119  1.00 30.34  ? 190 THR   C O     1 
ATOM   4943  C  CB    . THR   B 1  190 ? 22.907  19.247  -4.838  1.00 28.94  ? 190 THR   C CB    1 
ATOM   4944  O  OG1   . THR   B 1  190 ? 22.972  20.673  -4.919  1.00 36.52  ? 190 THR   C OG1   1 
ATOM   4945  C  CG2   . THR   B 1  190 ? 21.493  18.836  -4.422  1.00 23.19  ? 190 THR   C CG2   1 
ATOM   4946  N  N     . THR   B 1  191 ? 22.815  18.693  -1.657  1.00 23.25  ? 191 THR   C N     1 
ATOM   4947  C  CA    . THR   B 1  191 ? 22.474  19.182  -0.332  1.00 26.58  ? 191 THR   C CA    1 
ATOM   4948  C  C     . THR   B 1  191 ? 23.670  19.104  0.604   1.00 27.74  ? 191 THR   C C     1 
ATOM   4949  O  O     . THR   B 1  191 ? 23.937  20.051  1.354   1.00 34.93  ? 191 THR   C O     1 
ATOM   4950  C  CB    . THR   B 1  191 ? 21.274  18.396  0.222   1.00 27.14  ? 191 THR   C CB    1 
ATOM   4951  O  OG1   . THR   B 1  191 ? 20.091  18.774  -0.499  1.00 26.30  ? 191 THR   C OG1   1 
ATOM   4952  C  CG2   . THR   B 1  191 ? 21.072  18.651  1.736   1.00 16.26  ? 191 THR   C CG2   1 
ATOM   4953  N  N     . HIS   B 1  192 ? 24.397  17.985  0.586   1.00 27.87  ? 192 HIS   C N     1 
ATOM   4954  C  CA    . HIS   B 1  192 ? 25.604  17.892  1.398   1.00 30.77  ? 192 HIS   C CA    1 
ATOM   4955  C  C     . HIS   B 1  192 ? 26.637  18.924  0.968   1.00 31.87  ? 192 HIS   C C     1 
ATOM   4956  O  O     . HIS   B 1  192 ? 27.304  19.535  1.802   1.00 33.66  ? 192 HIS   C O     1 
ATOM   4957  C  CB    . HIS   B 1  192 ? 26.218  16.505  1.296   1.00 29.47  ? 192 HIS   C CB    1 
ATOM   4958  C  CG    . HIS   B 1  192 ? 27.655  16.469  1.723   1.00 38.92  ? 192 HIS   C CG    1 
ATOM   4959  N  ND1   . HIS   B 1  192 ? 28.095  17.062  2.892   1.00 35.09  ? 192 HIS   C ND1   1 
ATOM   4960  C  CD2   . HIS   B 1  192 ? 28.753  15.926  1.139   1.00 30.37  ? 192 HIS   C CD2   1 
ATOM   4961  C  CE1   . HIS   B 1  192 ? 29.401  16.873  3.010   1.00 39.44  ? 192 HIS   C CE1   1 
ATOM   4962  N  NE2   . HIS   B 1  192 ? 29.823  16.178  1.965   1.00 27.58  ? 192 HIS   C NE2   1 
ATOM   4963  N  N     . THR   B 1  193 ? 26.800  19.108  -0.332  1.00 29.65  ? 193 THR   C N     1 
ATOM   4964  C  CA    . THR   B 1  193 ? 27.860  19.964  -0.828  1.00 29.86  ? 193 THR   C CA    1 
ATOM   4965  C  C     . THR   B 1  193 ? 27.515  21.432  -0.730  1.00 26.57  ? 193 THR   C C     1 
ATOM   4966  O  O     . THR   B 1  193 ? 28.419  22.268  -0.693  1.00 32.52  ? 193 THR   C O     1 
ATOM   4967  C  CB    . THR   B 1  193 ? 28.186  19.594  -2.280  1.00 30.50  ? 193 THR   C CB    1 
ATOM   4968  O  OG1   . THR   B 1  193 ? 29.135  18.515  -2.297  1.00 28.47  ? 193 THR   C OG1   1 
ATOM   4969  C  CG2   . THR   B 1  193 ? 28.757  20.780  -3.006  1.00 28.49  ? 193 THR   C CG2   1 
ATOM   4970  N  N     . THR   B 1  194 ? 26.240  21.761  -0.668  1.00 27.11  ? 194 THR   C N     1 
ATOM   4971  C  CA    A THR   B 1  194 ? 25.799  23.139  -0.597  1.00 26.15  ? 194 THR   C CA    1 
ATOM   4972  C  CA    B THR   B 1  194 ? 25.818  23.151  -0.592  0.00 27.71  ? 194 THR   C CA    1 
ATOM   4973  C  C     . THR   B 1  194 ? 25.508  23.613  0.825   1.00 23.62  ? 194 THR   C C     1 
ATOM   4974  O  O     . THR   B 1  194 ? 25.405  24.825  1.048   1.00 22.36  ? 194 THR   C O     1 
ATOM   4975  C  CB    A THR   B 1  194 ? 24.569  23.290  -1.495  1.00 24.13  ? 194 THR   C CB    1 
ATOM   4976  C  CB    B THR   B 1  194 ? 24.584  23.385  -1.475  0.00 25.26  ? 194 THR   C CB    1 
ATOM   4977  O  OG1   A THR   B 1  194 ? 25.014  23.400  -2.849  1.00 29.23  ? 194 THR   C OG1   1 
ATOM   4978  O  OG1   B THR   B 1  194 ? 23.558  22.448  -1.127  0.00 27.76  ? 194 THR   C OG1   1 
ATOM   4979  C  CG2   A THR   B 1  194 ? 23.750  24.493  -1.149  1.00 18.67  ? 194 THR   C CG2   1 
ATOM   4980  C  CG2   B THR   B 1  194 ? 24.940  23.226  -2.943  0.00 28.85  ? 194 THR   C CG2   1 
ATOM   4981  N  N     . LEU   B 1  195 ? 25.393  22.687  1.788   1.00 27.38  ? 195 LEU   C N     1 
ATOM   4982  C  CA    . LEU   B 1  195 ? 24.869  23.009  3.123   1.00 26.61  ? 195 LEU   C CA    1 
ATOM   4983  C  C     . LEU   B 1  195 ? 25.579  24.202  3.757   1.00 29.98  ? 195 LEU   C C     1 
ATOM   4984  O  O     . LEU   B 1  195 ? 24.930  25.116  4.269   1.00 33.06  ? 195 LEU   C O     1 
ATOM   4985  C  CB    . LEU   B 1  195 ? 24.967  21.783  4.033   1.00 23.40  ? 195 LEU   C CB    1 
ATOM   4986  C  CG    . LEU   B 1  195 ? 24.099  21.635  5.273   1.00 22.71  ? 195 LEU   C CG    1 
ATOM   4987  C  CD1   . LEU   B 1  195 ? 22.655  21.985  5.002   1.00 25.29  ? 195 LEU   C CD1   1 
ATOM   4988  C  CD2   . LEU   B 1  195 ? 24.180  20.197  5.732   1.00 25.58  ? 195 LEU   C CD2   1 
ATOM   4989  N  N     . GLU   B 1  196 ? 26.911  24.231  3.715   1.00 31.18  ? 196 GLU   C N     1 
ATOM   4990  C  CA    . GLU   B 1  196 ? 27.635  25.293  4.397   1.00 24.43  ? 196 GLU   C CA    1 
ATOM   4991  C  C     . GLU   B 1  196 ? 27.848  26.530  3.541   1.00 24.34  ? 196 GLU   C C     1 
ATOM   4992  O  O     . GLU   B 1  196 ? 28.481  27.479  4.012   1.00 26.34  ? 196 GLU   C O     1 
ATOM   4993  C  CB    . GLU   B 1  196 ? 28.982  24.785  4.912   1.00 24.77  ? 196 GLU   C CB    1 
ATOM   4994  C  CG    . GLU   B 1  196 ? 30.015  24.635  3.839   1.00 42.42  ? 196 GLU   C CG    1 
ATOM   4995  C  CD    . GLU   B 1  196 ? 31.240  23.928  4.352   1.00 51.75  ? 196 GLU   C CD    1 
ATOM   4996  O  OE1   . GLU   B 1  196 ? 31.313  23.703  5.582   1.00 43.91  ? 196 GLU   C OE1   1 
ATOM   4997  O  OE2   . GLU   B 1  196 ? 32.117  23.599  3.527   1.00 59.29  ? 196 GLU   C OE2   1 
ATOM   4998  N  N     . HIS   B 1  197 ? 27.295  26.566  2.333   1.00 21.82  ? 197 HIS   C N     1 
ATOM   4999  C  CA    . HIS   B 1  197 ? 27.374  27.729  1.467   1.00 16.89  ? 197 HIS   C CA    1 
ATOM   5000  C  C     . HIS   B 1  197 ? 26.039  28.432  1.277   1.00 30.63  ? 197 HIS   C C     1 
ATOM   5001  O  O     . HIS   B 1  197 ? 25.934  29.312  0.416   1.00 35.14  ? 197 HIS   C O     1 
ATOM   5002  C  CB    . HIS   B 1  197 ? 27.945  27.339  0.110   1.00 22.94  ? 197 HIS   C CB    1 
ATOM   5003  C  CG    . HIS   B 1  197 ? 29.349  26.841  0.179   1.00 30.33  ? 197 HIS   C CG    1 
ATOM   5004  N  ND1   . HIS   B 1  197 ? 30.423  27.677  0.396   1.00 32.19  ? 197 HIS   C ND1   1 
ATOM   5005  C  CD2   . HIS   B 1  197 ? 29.857  25.591  0.083   1.00 32.18  ? 197 HIS   C CD2   1 
ATOM   5006  C  CE1   . HIS   B 1  197 ? 31.533  26.965  0.425   1.00 31.76  ? 197 HIS   C CE1   1 
ATOM   5007  N  NE2   . HIS   B 1  197 ? 31.219  25.696  0.238   1.00 37.59  ? 197 HIS   C NE2   1 
ATOM   5008  N  N     . SER   B 1  198 ? 25.023  28.091  2.058   1.00 27.95  ? 198 SER   C N     1 
ATOM   5009  C  CA    . SER   B 1  198 ? 23.720  28.710  1.905   1.00 22.96  ? 198 SER   C CA    1 
ATOM   5010  C  C     . SER   B 1  198 ? 23.227  29.169  3.262   1.00 21.70  ? 198 SER   C C     1 
ATOM   5011  O  O     . SER   B 1  198 ? 23.345  28.436  4.239   1.00 25.96  ? 198 SER   C O     1 
ATOM   5012  C  CB    . SER   B 1  198 ? 22.708  27.746  1.283   1.00 28.17  ? 198 SER   C CB    1 
ATOM   5013  O  OG    . SER   B 1  198 ? 21.380  28.266  1.383   1.00 29.80  ? 198 SER   C OG    1 
ATOM   5014  N  N     . ASP   B 1  199 ? 22.637  30.364  3.315   1.00 20.87  ? 199 ASP   C N     1 
ATOM   5015  C  CA    . ASP   B 1  199 ? 22.195  30.912  4.589   1.00 21.35  ? 199 ASP   C CA    1 
ATOM   5016  C  C     . ASP   B 1  199 ? 20.749  30.574  4.925   1.00 20.13  ? 199 ASP   C C     1 
ATOM   5017  O  O     . ASP   B 1  199 ? 20.350  30.664  6.090   1.00 32.01  ? 199 ASP   C O     1 
ATOM   5018  C  CB    . ASP   B 1  199 ? 22.397  32.427  4.586   1.00 27.53  ? 199 ASP   C CB    1 
ATOM   5019  C  CG    . ASP   B 1  199 ? 23.754  32.815  4.057   1.00 27.47  ? 199 ASP   C CG    1 
ATOM   5020  O  OD1   . ASP   B 1  199 ? 24.773  32.449  4.685   1.00 24.37  ? 199 ASP   C OD1   1 
ATOM   5021  O  OD2   . ASP   B 1  199 ? 23.809  33.430  2.969   1.00 35.92  ? 199 ASP   C OD2   1 
ATOM   5022  N  N     . CYS   B 1  200 ? 19.966  30.188  3.939   1.00 23.12  ? 200 CYS   C N     1 
ATOM   5023  C  CA    . CYS   B 1  200 ? 18.546  29.952  4.096   1.00 21.94  ? 200 CYS   C CA    1 
ATOM   5024  C  C     . CYS   B 1  200 ? 18.071  29.318  2.805   1.00 29.01  ? 200 CYS   C C     1 
ATOM   5025  O  O     . CYS   B 1  200 ? 18.430  29.806  1.728   1.00 26.43  ? 200 CYS   C O     1 
ATOM   5026  C  CB    . CYS   B 1  200 ? 17.790  31.250  4.365   1.00 23.86  ? 200 CYS   C CB    1 
ATOM   5027  S  SG    . CYS   B 1  200 ? 16.033  30.944  4.578   1.00 32.53  ? 200 CYS   C SG    1 
ATOM   5028  N  N     . ALA   B 1  201 ? 17.291  28.237  2.888   1.00 19.33  ? 201 ALA   C N     1 
ATOM   5029  C  CA    . ALA   B 1  201 ? 16.835  27.531  1.695   1.00 20.13  ? 201 ALA   C CA    1 
ATOM   5030  C  C     . ALA   B 1  201 ? 15.370  27.162  1.851   1.00 27.53  ? 201 ALA   C C     1 
ATOM   5031  O  O     . ALA   B 1  201 ? 15.001  26.490  2.815   1.00 31.45  ? 201 ALA   C O     1 
ATOM   5032  C  CB    . ALA   B 1  201 ? 17.674  26.279  1.447   1.00 22.23  ? 201 ALA   C CB    1 
ATOM   5033  N  N     . PHE   B 1  202 ? 14.536  27.594  0.912   1.00 22.88  ? 202 PHE   C N     1 
ATOM   5034  C  CA    . PHE   B 1  202 ? 13.130  27.216  0.891   1.00 24.57  ? 202 PHE   C CA    1 
ATOM   5035  C  C     . PHE   B 1  202 ? 12.946  26.050  -0.077  1.00 29.95  ? 202 PHE   C C     1 
ATOM   5036  O  O     . PHE   B 1  202 ? 12.987  26.246  -1.298  1.00 27.20  ? 202 PHE   C O     1 
ATOM   5037  C  CB    . PHE   B 1  202 ? 12.262  28.393  0.474   1.00 19.24  ? 202 PHE   C CB    1 
ATOM   5038  C  CG    . PHE   B 1  202 ? 12.521  29.611  1.251   1.00 28.66  ? 202 PHE   C CG    1 
ATOM   5039  C  CD1   . PHE   B 1  202 ? 13.482  30.507  0.845   1.00 26.86  ? 202 PHE   C CD1   1 
ATOM   5040  C  CD2   . PHE   B 1  202 ? 11.820  29.862  2.412   1.00 35.31  ? 202 PHE   C CD2   1 
ATOM   5041  C  CE1   . PHE   B 1  202 ? 13.723  31.608  1.568   1.00 23.54  ? 202 PHE   C CE1   1 
ATOM   5042  C  CE2   . PHE   B 1  202 ? 12.068  30.980  3.141   1.00 26.31  ? 202 PHE   C CE2   1 
ATOM   5043  C  CZ    . PHE   B 1  202 ? 13.018  31.849  2.719   1.00 26.78  ? 202 PHE   C CZ    1 
ATOM   5044  N  N     . MET   B 1  203 ? 12.720  24.847  0.464   1.00 21.76  ? 203 MET   C N     1 
ATOM   5045  C  CA    . MET   B 1  203 ? 12.408  23.688  -0.364  1.00 22.79  ? 203 MET   C CA    1 
ATOM   5046  C  C     . MET   B 1  203 ? 10.949  23.707  -0.803  1.00 29.18  ? 203 MET   C C     1 
ATOM   5047  O  O     . MET   B 1  203 ? 10.047  23.982  -0.003  1.00 34.77  ? 203 MET   C O     1 
ATOM   5048  C  CB    . MET   B 1  203 ? 12.678  22.388  0.392   1.00 24.13  ? 203 MET   C CB    1 
ATOM   5049  C  CG    . MET   B 1  203 ? 14.149  22.085  0.652   1.00 21.14  ? 203 MET   C CG    1 
ATOM   5050  S  SD    . MET   B 1  203 ? 14.307  20.423  1.261   1.00 33.42  ? 203 MET   C SD    1 
ATOM   5051  C  CE    . MET   B 1  203 ? 13.670  20.592  2.926   1.00 23.14  ? 203 MET   C CE    1 
ATOM   5052  N  N     . VAL   B 1  204 ? 10.720  23.373  -2.072  1.00 28.56  ? 204 VAL   C N     1 
ATOM   5053  C  CA    . VAL   B 1  204 ? 9.380   23.207  -2.642  1.00 29.98  ? 204 VAL   C CA    1 
ATOM   5054  C  C     . VAL   B 1  204 ? 9.227   21.747  -3.047  1.00 23.15  ? 204 VAL   C C     1 
ATOM   5055  O  O     . VAL   B 1  204 ? 9.795   21.323  -4.057  1.00 27.98  ? 204 VAL   C O     1 
ATOM   5056  C  CB    . VAL   B 1  204 ? 9.145   24.132  -3.838  1.00 27.80  ? 204 VAL   C CB    1 
ATOM   5057  C  CG1   . VAL   B 1  204 ? 7.697   24.135  -4.203  1.00 21.43  ? 204 VAL   C CG1   1 
ATOM   5058  C  CG2   . VAL   B 1  204 ? 9.640   25.527  -3.527  1.00 21.87  ? 204 VAL   C CG2   1 
ATOM   5059  N  N     . ASP   B 1  205 ? 8.476   20.972  -2.260  1.00 28.28  ? 205 ASP   C N     1 
ATOM   5060  C  CA    . ASP   B 1  205 ? 8.163   19.583  -2.606  1.00 25.73  ? 205 ASP   C CA    1 
ATOM   5061  C  C     . ASP   B 1  205 ? 7.271   19.552  -3.855  1.00 32.22  ? 205 ASP   C C     1 
ATOM   5062  O  O     . ASP   B 1  205 ? 6.142   20.057  -3.838  1.00 30.50  ? 205 ASP   C O     1 
ATOM   5063  C  CB    . ASP   B 1  205 ? 7.474   18.896  -1.412  1.00 27.96  ? 205 ASP   C CB    1 
ATOM   5064  C  CG    . ASP   B 1  205 ? 7.204   17.386  -1.628  1.00 34.39  ? 205 ASP   C CG    1 
ATOM   5065  O  OD1   . ASP   B 1  205 ? 7.292   16.898  -2.777  1.00 35.23  ? 205 ASP   C OD1   1 
ATOM   5066  O  OD2   . ASP   B 1  205 ? 6.892   16.685  -0.634  1.00 30.43  ? 205 ASP   C OD2   1 
ATOM   5067  N  N     . ASN   B 1  206 ? 7.779   18.998  -4.956  1.00 30.91  ? 206 ASN   C N     1 
ATOM   5068  C  CA    . ASN   B 1  206 ? 6.958   19.003  -6.164  1.00 42.51  ? 206 ASN   C CA    1 
ATOM   5069  C  C     . ASN   B 1  206 ? 5.650   18.269  -5.935  1.00 44.03  ? 206 ASN   C C     1 
ATOM   5070  O  O     . ASN   B 1  206 ? 4.639   18.584  -6.574  1.00 36.99  ? 206 ASN   C O     1 
ATOM   5071  C  CB    . ASN   B 1  206 ? 7.699   18.395  -7.355  1.00 28.45  ? 206 ASN   C CB    1 
ATOM   5072  C  CG    . ASN   B 1  206 ? 8.092   19.448  -8.370  1.00 22.62  ? 206 ASN   C CG    1 
ATOM   5073  O  OD1   . ASN   B 1  206 ? 7.645   20.585  -8.289  1.00 26.27  ? 206 ASN   C OD1   1 
ATOM   5074  N  ND2   . ASN   B 1  206 ? 8.936   19.082  -9.320  1.00 26.24  ? 206 ASN   C ND2   1 
ATOM   5075  N  N     . GLU   B 1  207 ? 5.640   17.310  -5.012  1.00 32.71  ? 207 GLU   C N     1 
ATOM   5076  C  CA    . GLU   B 1  207 ? 4.411   16.588  -4.799  1.00 27.25  ? 207 GLU   C CA    1 
ATOM   5077  C  C     . GLU   B 1  207 ? 3.441   17.400  -3.960  1.00 29.99  ? 207 GLU   C C     1 
ATOM   5078  O  O     . GLU   B 1  207 ? 2.233   17.214  -4.086  1.00 33.74  ? 207 GLU   C O     1 
ATOM   5079  C  CB    . GLU   B 1  207 ? 4.705   15.234  -4.170  1.00 29.78  ? 207 GLU   C CB    1 
ATOM   5080  C  CG    . GLU   B 1  207 ? 3.472   14.368  -3.996  1.00 34.88  ? 207 GLU   C CG    1 
ATOM   5081  C  CD    . GLU   B 1  207 ? 3.818   13.004  -3.498  1.00 33.87  ? 207 GLU   C CD    1 
ATOM   5082  O  OE1   . GLU   B 1  207 ? 5.018   12.701  -3.420  1.00 38.07  ? 207 GLU   C OE1   1 
ATOM   5083  O  OE2   . GLU   B 1  207 ? 2.905   12.229  -3.186  1.00 46.23  ? 207 GLU   C OE2   1 
ATOM   5084  N  N     . ALA   B 1  208 ? 3.942   18.299  -3.111  1.00 30.03  ? 208 ALA   C N     1 
ATOM   5085  C  CA    . ALA   B 1  208 ? 3.056   19.199  -2.375  1.00 30.11  ? 208 ALA   C CA    1 
ATOM   5086  C  C     . ALA   B 1  208 ? 2.332   20.136  -3.330  1.00 37.02  ? 208 ALA   C C     1 
ATOM   5087  O  O     . ALA   B 1  208 ? 1.112   20.314  -3.246  1.00 32.75  ? 208 ALA   C O     1 
ATOM   5088  C  CB    . ALA   B 1  208 ? 3.851   20.007  -1.343  1.00 27.11  ? 208 ALA   C CB    1 
ATOM   5089  N  N     . ILE   B 1  209 ? 3.087   20.756  -4.243  1.00 39.69  ? 209 ILE   C N     1 
ATOM   5090  C  CA    . ILE   B 1  209 ? 2.511   21.682  -5.206  1.00 36.59  ? 209 ILE   C CA    1 
ATOM   5091  C  C     . ILE   B 1  209 ? 1.550   20.936  -6.114  1.00 38.82  ? 209 ILE   C C     1 
ATOM   5092  O  O     . ILE   B 1  209 ? 0.467   21.432  -6.456  1.00 40.53  ? 209 ILE   C O     1 
ATOM   5093  C  CB    . ILE   B 1  209 ? 3.636   22.377  -6.002  1.00 31.44  ? 209 ILE   C CB    1 
ATOM   5094  C  CG1   . ILE   B 1  209 ? 4.554   23.096  -5.050  1.00 24.78  ? 209 ILE   C CG1   1 
ATOM   5095  C  CG2   . ILE   B 1  209 ? 3.087   23.419  -6.950  1.00 32.35  ? 209 ILE   C CG2   1 
ATOM   5096  C  CD1   . ILE   B 1  209 ? 3.854   24.100  -4.267  1.00 25.59  ? 209 ILE   C CD1   1 
ATOM   5097  N  N     . TYR   B 1  210 ? 1.930   19.725  -6.506  1.00 31.80  ? 210 TYR   C N     1 
ATOM   5098  C  CA    . TYR   B 1  210 ? 1.074   18.932  -7.371  1.00 33.68  ? 210 TYR   C CA    1 
ATOM   5099  C  C     . TYR   B 1  210 ? -0.301  18.739  -6.741  1.00 36.05  ? 210 TYR   C C     1 
ATOM   5100  O  O     . TYR   B 1  210 ? -1.329  18.976  -7.377  1.00 37.90  ? 210 TYR   C O     1 
ATOM   5101  C  CB    . TYR   B 1  210 ? 1.745   17.593  -7.647  1.00 24.14  ? 210 TYR   C CB    1 
ATOM   5102  C  CG    . TYR   B 1  210 ? 1.231   16.894  -8.861  1.00 40.79  ? 210 TYR   C CG    1 
ATOM   5103  C  CD1   . TYR   B 1  210 ? 1.579   17.330  -10.143 1.00 35.41  ? 210 TYR   C CD1   1 
ATOM   5104  C  CD2   . TYR   B 1  210 ? 0.415   15.773  -8.738  1.00 46.02  ? 210 TYR   C CD2   1 
ATOM   5105  C  CE1   . TYR   B 1  210 ? 1.115   16.670  -11.265 1.00 48.69  ? 210 TYR   C CE1   1 
ATOM   5106  C  CE2   . TYR   B 1  210 ? -0.052  15.100  -9.851  1.00 38.71  ? 210 TYR   C CE2   1 
ATOM   5107  C  CZ    . TYR   B 1  210 ? 0.294   15.547  -11.110 1.00 50.68  ? 210 TYR   C CZ    1 
ATOM   5108  O  OH    . TYR   B 1  210 ? -0.184  14.869  -12.207 1.00 41.48  ? 210 TYR   C OH    1 
ATOM   5109  N  N     . ASP   B 1  211 ? -0.338  18.330  -5.479  1.00 33.59  ? 211 ASP   C N     1 
ATOM   5110  C  CA    . ASP   B 1  211 ? -1.617  18.009  -4.865  1.00 38.31  ? 211 ASP   C CA    1 
ATOM   5111  C  C     . ASP   B 1  211 ? -2.481  19.251  -4.715  1.00 44.35  ? 211 ASP   C C     1 
ATOM   5112  O  O     . ASP   B 1  211 ? -3.678  19.218  -5.016  1.00 40.79  ? 211 ASP   C O     1 
ATOM   5113  C  CB    . ASP   B 1  211 ? -1.388  17.333  -3.519  1.00 32.26  ? 211 ASP   C CB    1 
ATOM   5114  C  CG    . ASP   B 1  211 ? -0.933  15.911  -3.666  1.00 38.36  ? 211 ASP   C CG    1 
ATOM   5115  O  OD1   . ASP   B 1  211 ? -1.412  15.241  -4.613  1.00 48.38  ? 211 ASP   C OD1   1 
ATOM   5116  O  OD2   . ASP   B 1  211 ? -0.090  15.466  -2.855  1.00 38.62  ? 211 ASP   C OD2   1 
ATOM   5117  N  N     . ILE   B 1  212 ? -1.883  20.353  -4.257  1.00 41.85  ? 212 ILE   C N     1 
ATOM   5118  C  CA    . ILE   B 1  212 ? -2.599  21.616  -4.117  1.00 34.37  ? 212 ILE   C CA    1 
ATOM   5119  C  C     . ILE   B 1  212 ? -3.302  21.987  -5.423  1.00 40.88  ? 212 ILE   C C     1 
ATOM   5120  O  O     . ILE   B 1  212 ? -4.490  22.348  -5.435  1.00 36.59  ? 212 ILE   C O     1 
ATOM   5121  C  CB    . ILE   B 1  212 ? -1.626  22.711  -3.651  1.00 33.71  ? 212 ILE   C CB    1 
ATOM   5122  C  CG1   . ILE   B 1  212 ? -1.235  22.452  -2.187  1.00 40.08  ? 212 ILE   C CG1   1 
ATOM   5123  C  CG2   . ILE   B 1  212 ? -2.229  24.090  -3.875  1.00 31.69  ? 212 ILE   C CG2   1 
ATOM   5124  C  CD1   . ILE   B 1  212 ? -0.017  23.217  -1.687  1.00 38.48  ? 212 ILE   C CD1   1 
ATOM   5125  N  N     . CYS   B 1  213 ? -2.587  21.883  -6.546  1.00 31.96  ? 213 CYS   C N     1 
ATOM   5126  C  CA    . CYS   B 1  213 ? -3.206  22.180  -7.835  1.00 35.03  ? 213 CYS   C CA    1 
ATOM   5127  C  C     . CYS   B 1  213 ? -4.368  21.235  -8.133  1.00 42.73  ? 213 CYS   C C     1 
ATOM   5128  O  O     . CYS   B 1  213 ? -5.388  21.650  -8.697  1.00 45.35  ? 213 CYS   C O     1 
ATOM   5129  C  CB    . CYS   B 1  213 ? -2.169  22.104  -8.948  1.00 39.49  ? 213 CYS   C CB    1 
ATOM   5130  S  SG    . CYS   B 1  213 ? -0.998  23.448  -8.938  1.00 39.95  ? 213 CYS   C SG    1 
ATOM   5131  N  N     . ARG   B 1  214 ? -4.228  19.959  -7.779  1.00 39.75  ? 214 ARG   C N     1 
ATOM   5132  C  CA    . ARG   B 1  214 ? -5.334  19.022  -7.942  1.00 42.58  ? 214 ARG   C CA    1 
ATOM   5133  C  C     . ARG   B 1  214 ? -6.504  19.366  -7.024  1.00 44.94  ? 214 ARG   C C     1 
ATOM   5134  O  O     . ARG   B 1  214 ? -7.640  19.506  -7.490  1.00 52.52  ? 214 ARG   C O     1 
ATOM   5135  C  CB    . ARG   B 1  214 ? -4.853  17.599  -7.694  1.00 29.46  ? 214 ARG   C CB    1 
ATOM   5136  C  CG    . ARG   B 1  214 ? -3.990  17.093  -8.800  1.00 34.08  ? 214 ARG   C CG    1 
ATOM   5137  C  CD    . ARG   B 1  214 ? -4.030  15.585  -8.909  1.00 42.36  ? 214 ARG   C CD    1 
ATOM   5138  N  NE    . ARG   B 1  214 ? -3.041  14.946  -8.050  1.00 54.86  ? 214 ARG   C NE    1 
ATOM   5139  C  CZ    . ARG   B 1  214 ? -2.777  13.647  -8.057  1.00 55.31  ? 214 ARG   C CZ    1 
ATOM   5140  N  NH1   . ARG   B 1  214 ? -3.448  12.815  -8.838  1.00 50.36  ? 214 ARG   C NH1   1 
ATOM   5141  N  NH2   . ARG   B 1  214 ? -1.815  13.175  -7.263  1.00 45.32  ? 214 ARG   C NH2   1 
ATOM   5142  N  N     . ARG   B 1  215 ? -6.241  19.541  -5.718  1.00 37.59  ? 215 ARG   C N     1 
ATOM   5143  C  CA    . ARG   B 1  215 ? -7.302  19.645  -4.714  1.00 36.75  ? 215 ARG   C CA    1 
ATOM   5144  C  C     . ARG   B 1  215 ? -7.884  21.039  -4.550  1.00 41.06  ? 215 ARG   C C     1 
ATOM   5145  O  O     . ARG   B 1  215 ? -8.964  21.158  -3.967  1.00 58.46  ? 215 ARG   C O     1 
ATOM   5146  C  CB    . ARG   B 1  215 ? -6.814  19.225  -3.324  1.00 46.79  ? 215 ARG   C CB    1 
ATOM   5147  C  CG    . ARG   B 1  215 ? -6.467  17.763  -3.122  1.00 54.30  ? 215 ARG   C CG    1 
ATOM   5148  C  CD    . ARG   B 1  215 ? -5.767  17.567  -1.755  1.00 74.11  ? 215 ARG   C CD    1 
ATOM   5149  N  NE    . ARG   B 1  215 ? -5.410  16.170  -1.522  1.00 90.99  ? 215 ARG   C NE    1 
ATOM   5150  C  CZ    . ARG   B 1  215 ? -4.556  15.477  -2.268  1.00 77.95  ? 215 ARG   C CZ    1 
ATOM   5151  N  NH1   . ARG   B 1  215 ? -3.946  16.023  -3.313  1.00 50.47  ? 215 ARG   C NH1   1 
ATOM   5152  N  NH2   . ARG   B 1  215 ? -4.321  14.200  -1.967  1.00 69.21  ? 215 ARG   C NH2   1 
ATOM   5153  N  N     . ASN   B 1  216 ? -7.178  22.099  -4.957  1.00 45.67  ? 216 ASN   C N     1 
ATOM   5154  C  CA    . ASN   B 1  216 ? -7.659  23.463  -4.762  1.00 29.80  ? 216 ASN   C CA    1 
ATOM   5155  C  C     . ASN   B 1  216 ? -7.952  24.188  -6.056  1.00 43.60  ? 216 ASN   C C     1 
ATOM   5156  O  O     . ASN   B 1  216 ? -8.667  25.200  -6.026  1.00 48.92  ? 216 ASN   C O     1 
ATOM   5157  C  CB    . ASN   B 1  216 ? -6.639  24.323  -3.990  1.00 40.19  ? 216 ASN   C CB    1 
ATOM   5158  C  CG    . ASN   B 1  216 ? -6.221  23.735  -2.653  1.00 36.13  ? 216 ASN   C CG    1 
ATOM   5159  O  OD1   . ASN   B 1  216 ? -6.100  22.527  -2.487  1.00 39.49  ? 216 ASN   C OD1   1 
ATOM   5160  N  ND2   . ASN   B 1  216 ? -5.956  24.610  -1.702  1.00 35.61  ? 216 ASN   C ND2   1 
ATOM   5161  N  N     . LEU   B 1  217 ? -7.391  23.734  -7.177  1.00 42.60  ? 217 LEU   C N     1 
ATOM   5162  C  CA    . LEU   B 1  217 ? -7.612  24.324  -8.483  1.00 32.31  ? 217 LEU   C CA    1 
ATOM   5163  C  C     . LEU   B 1  217 ? -8.318  23.381  -9.446  1.00 46.37  ? 217 LEU   C C     1 
ATOM   5164  O  O     . LEU   B 1  217 ? -8.569  23.765  -10.598 1.00 38.26  ? 217 LEU   C O     1 
ATOM   5165  C  CB    . LEU   B 1  217 ? -6.273  24.763  -9.077  1.00 34.71  ? 217 LEU   C CB    1 
ATOM   5166  C  CG    . LEU   B 1  217 ? -5.559  25.677  -8.099  1.00 39.11  ? 217 LEU   C CG    1 
ATOM   5167  C  CD1   . LEU   B 1  217 ? -4.293  26.206  -8.720  1.00 40.20  ? 217 LEU   C CD1   1 
ATOM   5168  C  CD2   . LEU   B 1  217 ? -6.488  26.816  -7.684  1.00 38.20  ? 217 LEU   C CD2   1 
ATOM   5169  N  N     . ASP   B 1  218 ? -8.614  22.150  -9.021  1.00 48.43  ? 218 ASP   C N     1 
ATOM   5170  C  CA    . ASP   B 1  218 ? -9.344  21.170  -9.827  1.00 54.40  ? 218 ASP   C CA    1 
ATOM   5171  C  C     . ASP   B 1  218 ? -8.632  20.834  -11.142 1.00 50.08  ? 218 ASP   C C     1 
ATOM   5172  O  O     . ASP   B 1  218 ? -9.262  20.337  -12.084 1.00 51.58  ? 218 ASP   C O     1 
ATOM   5173  C  CB    . ASP   B 1  218 ? -10.779 21.649  -10.084 1.00 53.37  ? 218 ASP   C CB    1 
ATOM   5174  C  CG    . ASP   B 1  218 ? -11.567 21.874  -8.778  1.00 73.50  ? 218 ASP   C CG    1 
ATOM   5175  O  OD1   . ASP   B 1  218 ? -11.975 20.857  -8.174  1.00 76.93  ? 218 ASP   C OD1   1 
ATOM   5176  O  OD2   . ASP   B 1  218 ? -11.764 23.051  -8.346  1.00 64.39  ? 218 ASP   C OD2   1 
ATOM   5177  N  N     . ILE   B 1  219 ? -7.320  21.063  -11.211 1.00 50.10  ? 219 ILE   C N     1 
ATOM   5178  C  CA    . ILE   B 1  219 ? -6.519  20.700  -12.380 1.00 47.80  ? 219 ILE   C CA    1 
ATOM   5179  C  C     . ILE   B 1  219 ? -6.291  19.194  -12.348 1.00 43.93  ? 219 ILE   C C     1 
ATOM   5180  O  O     . ILE   B 1  219 ? -5.681  18.671  -11.410 1.00 47.39  ? 219 ILE   C O     1 
ATOM   5181  C  CB    . ILE   B 1  219 ? -5.187  21.471  -12.407 1.00 47.32  ? 219 ILE   C CB    1 
ATOM   5182  C  CG1   . ILE   B 1  219 ? -5.444  22.983  -12.405 1.00 46.29  ? 219 ILE   C CG1   1 
ATOM   5183  C  CG2   . ILE   B 1  219 ? -4.325  21.080  -13.623 1.00 32.56  ? 219 ILE   C CG2   1 
ATOM   5184  C  CD1   . ILE   B 1  219 ? -4.379  23.795  -11.689 1.00 40.01  ? 219 ILE   C CD1   1 
ATOM   5185  N  N     . GLU   B 1  220 ? -6.795  18.492  -13.368 1.00 51.76  ? 220 GLU   C N     1 
ATOM   5186  C  CA    . GLU   B 1  220 ? -6.745  17.030  -13.375 1.00 51.73  ? 220 GLU   C CA    1 
ATOM   5187  C  C     . GLU   B 1  220 ? -5.312  16.526  -13.289 1.00 51.30  ? 220 GLU   C C     1 
ATOM   5188  O  O     . GLU   B 1  220 ? -4.971  15.706  -12.427 1.00 46.87  ? 220 GLU   C O     1 
ATOM   5189  C  CB    . GLU   B 1  220 ? -7.403  16.476  -14.641 1.00 49.73  ? 220 GLU   C CB    1 
ATOM   5190  C  CG    . GLU   B 1  220 ? -8.709  17.103  -15.038 1.00 75.06  ? 220 GLU   C CG    1 
ATOM   5191  C  CD    . GLU   B 1  220 ? -9.308  16.378  -16.219 1.00 90.09  ? 220 GLU   C CD    1 
ATOM   5192  O  OE1   . GLU   B 1  220 ? -8.735  15.319  -16.574 1.00 64.32  ? 220 GLU   C OE1   1 
ATOM   5193  O  OE2   . GLU   B 1  220 ? -10.326 16.860  -16.780 1.00 90.29  ? 220 GLU   C OE2   1 
ATOM   5194  N  N     . ARG   B 1  221 ? -4.469  16.981  -14.212 1.00 43.34  ? 221 ARG   C N     1 
ATOM   5195  C  CA    . ARG   B 1  221 ? -3.082  16.538  -14.321 1.00 56.51  ? 221 ARG   C CA    1 
ATOM   5196  C  C     . ARG   B 1  221 ? -2.254  17.807  -14.484 1.00 56.41  ? 221 ARG   C C     1 
ATOM   5197  O  O     . ARG   B 1  221 ? -2.044  18.295  -15.608 1.00 58.36  ? 221 ARG   C O     1 
ATOM   5198  C  CB    . ARG   B 1  221 ? -2.912  15.547  -15.474 1.00 47.82  ? 221 ARG   C CB    1 
ATOM   5199  C  CG    . ARG   B 1  221 ? -1.491  15.208  -15.826 1.00 49.49  ? 221 ARG   C CG    1 
ATOM   5200  C  CD    . ARG   B 1  221 ? -0.889  14.283  -14.806 1.00 54.60  ? 221 ARG   C CD    1 
ATOM   5201  N  NE    . ARG   B 1  221 ? 0.425   13.776  -15.196 1.00 55.73  ? 221 ARG   C NE    1 
ATOM   5202  C  CZ    . ARG   B 1  221 ? 1.543   14.493  -15.225 1.00 52.69  ? 221 ARG   C CZ    1 
ATOM   5203  N  NH1   . ARG   B 1  221 ? 1.540   15.798  -14.991 1.00 52.65  ? 221 ARG   C NH1   1 
ATOM   5204  N  NH2   . ARG   B 1  221 ? 2.695   13.887  -15.499 1.00 50.91  ? 221 ARG   C NH2   1 
ATOM   5205  N  N     . PRO   B 1  222 ? -1.799  18.394  -13.375 1.00 51.98  ? 222 PRO   C N     1 
ATOM   5206  C  CA    . PRO   B 1  222 ? -1.122  19.693  -13.450 1.00 45.49  ? 222 PRO   C CA    1 
ATOM   5207  C  C     . PRO   B 1  222 ? 0.182   19.608  -14.222 1.00 38.45  ? 222 PRO   C C     1 
ATOM   5208  O  O     . PRO   B 1  222 ? 0.912   18.619  -14.153 1.00 40.40  ? 222 PRO   C O     1 
ATOM   5209  C  CB    . PRO   B 1  222 ? -0.878  20.051  -11.981 1.00 42.78  ? 222 PRO   C CB    1 
ATOM   5210  C  CG    . PRO   B 1  222 ? -1.844  19.247  -11.218 1.00 43.23  ? 222 PRO   C CG    1 
ATOM   5211  C  CD    . PRO   B 1  222 ? -2.041  17.979  -11.985 1.00 43.97  ? 222 PRO   C CD    1 
ATOM   5212  N  N     . THR   B 1  223 ? 0.456   20.662  -14.974 1.00 42.90  ? 223 THR   C N     1 
ATOM   5213  C  CA    . THR   B 1  223 ? 1.671   20.807  -15.760 1.00 34.16  ? 223 THR   C CA    1 
ATOM   5214  C  C     . THR   B 1  223 ? 2.672   21.671  -14.997 1.00 41.20  ? 223 THR   C C     1 
ATOM   5215  O  O     . THR   B 1  223 ? 2.361   22.251  -13.951 1.00 41.04  ? 223 THR   C O     1 
ATOM   5216  C  CB    . THR   B 1  223 ? 1.351   21.438  -17.118 1.00 31.72  ? 223 THR   C CB    1 
ATOM   5217  O  OG1   . THR   B 1  223 ? 0.921   22.788  -16.921 1.00 36.61  ? 223 THR   C OG1   1 
ATOM   5218  C  CG2   . THR   B 1  223 ? 0.245   20.670  -17.839 1.00 29.23  ? 223 THR   C CG2   1 
ATOM   5219  N  N     . TYR   B 1  224 ? 3.894   21.761  -15.525 1.00 31.48  ? 224 TYR   C N     1 
ATOM   5220  C  CA    . TYR   B 1  224 ? 4.849   22.649  -14.876 1.00 28.50  ? 224 TYR   C CA    1 
ATOM   5221  C  C     . TYR   B 1  224 ? 4.336   24.085  -14.855 1.00 34.88  ? 224 TYR   C C     1 
ATOM   5222  O  O     . TYR   B 1  224 ? 4.688   24.857  -13.957 1.00 34.48  ? 224 TYR   C O     1 
ATOM   5223  C  CB    . TYR   B 1  224 ? 6.202   22.579  -15.568 1.00 22.36  ? 224 TYR   C CB    1 
ATOM   5224  C  CG    . TYR   B 1  224 ? 6.994   21.307  -15.357 1.00 21.20  ? 224 TYR   C CG    1 
ATOM   5225  C  CD1   . TYR   B 1  224 ? 7.046   20.687  -14.121 1.00 18.64  ? 224 TYR   C CD1   1 
ATOM   5226  C  CD2   . TYR   B 1  224 ? 7.696   20.723  -16.423 1.00 20.09  ? 224 TYR   C CD2   1 
ATOM   5227  C  CE1   . TYR   B 1  224 ? 7.792   19.526  -13.943 1.00 19.84  ? 224 TYR   C CE1   1 
ATOM   5228  C  CE2   . TYR   B 1  224 ? 8.432   19.577  -16.271 1.00 13.18  ? 224 TYR   C CE2   1 
ATOM   5229  C  CZ    . TYR   B 1  224 ? 8.490   18.979  -15.024 1.00 26.82  ? 224 TYR   C CZ    1 
ATOM   5230  O  OH    . TYR   B 1  224 ? 9.250   17.837  -14.858 1.00 28.19  ? 224 TYR   C OH    1 
ATOM   5231  N  N     . THR   B 1  225 ? 3.502   24.466  -15.826 1.00 35.47  ? 225 THR   C N     1 
ATOM   5232  C  CA    . THR   B 1  225 ? 2.958   25.818  -15.829 1.00 33.39  ? 225 THR   C CA    1 
ATOM   5233  C  C     . THR   B 1  225 ? 2.028   26.024  -14.637 1.00 40.44  ? 225 THR   C C     1 
ATOM   5234  O  O     . THR   B 1  225 ? 2.129   27.026  -13.920 1.00 40.88  ? 225 THR   C O     1 
ATOM   5235  C  CB    . THR   B 1  225 ? 2.230   26.100  -17.149 1.00 40.31  ? 225 THR   C CB    1 
ATOM   5236  O  OG1   . THR   B 1  225 ? 3.051   25.709  -18.263 1.00 43.15  ? 225 THR   C OG1   1 
ATOM   5237  C  CG2   . THR   B 1  225 ? 1.890   27.591  -17.274 1.00 31.19  ? 225 THR   C CG2   1 
ATOM   5238  N  N     . ASN   B 1  226 ? 1.120   25.083  -14.393 1.00 35.19  ? 226 ASN   C N     1 
ATOM   5239  C  CA    . ASN   B 1  226 ? 0.353   25.152  -13.154 1.00 35.10  ? 226 ASN   C CA    1 
ATOM   5240  C  C     . ASN   B 1  226 ? 1.287   25.251  -11.945 1.00 39.11  ? 226 ASN   C C     1 
ATOM   5241  O  O     . ASN   B 1  226 ? 1.173   26.166  -11.117 1.00 40.33  ? 226 ASN   C O     1 
ATOM   5242  C  CB    . ASN   B 1  226 ? -0.556  23.932  -13.028 1.00 38.42  ? 226 ASN   C CB    1 
ATOM   5243  C  CG    . ASN   B 1  226 ? -1.438  23.724  -14.248 1.00 42.16  ? 226 ASN   C CG    1 
ATOM   5244  O  OD1   . ASN   B 1  226 ? -1.553  22.613  -14.769 1.00 36.64  ? 226 ASN   C OD1   1 
ATOM   5245  N  ND2   . ASN   B 1  226 ? -2.070  24.792  -14.702 1.00 53.55  ? 226 ASN   C ND2   1 
ATOM   5246  N  N     . LEU   B 1  227 ? 2.233   24.316  -11.839 1.00 32.34  ? 227 LEU   C N     1 
ATOM   5247  C  CA    . LEU   B 1  227 ? 3.148   24.308  -10.703 1.00 24.94  ? 227 LEU   C CA    1 
ATOM   5248  C  C     . LEU   B 1  227 ? 3.892   25.625  -10.584 1.00 34.52  ? 227 LEU   C C     1 
ATOM   5249  O  O     . LEU   B 1  227 ? 3.893   26.258  -9.524  1.00 37.85  ? 227 LEU   C O     1 
ATOM   5250  C  CB    . LEU   B 1  227 ? 4.134   23.156  -10.837 1.00 23.62  ? 227 LEU   C CB    1 
ATOM   5251  C  CG    . LEU   B 1  227 ? 3.677   21.816  -10.259 1.00 34.69  ? 227 LEU   C CG    1 
ATOM   5252  C  CD1   . LEU   B 1  227 ? 2.234   21.533  -10.625 1.00 30.56  ? 227 LEU   C CD1   1 
ATOM   5253  C  CD2   . LEU   B 1  227 ? 4.591   20.704  -10.740 1.00 27.59  ? 227 LEU   C CD2   1 
ATOM   5254  N  N     . ASN   B 1  228 ? 4.538   26.057  -11.667 1.00 34.48  ? 228 ASN   C N     1 
ATOM   5255  C  CA    . ASN   B 1  228 ? 5.411   27.212  -11.571 1.00 20.73  ? 228 ASN   C CA    1 
ATOM   5256  C  C     . ASN   B 1  228 ? 4.636   28.423  -11.134 1.00 32.18  ? 228 ASN   C C     1 
ATOM   5257  O  O     . ASN   B 1  228 ? 5.101   29.192  -10.288 1.00 38.90  ? 228 ASN   C O     1 
ATOM   5258  C  CB    . ASN   B 1  228 ? 6.100   27.470  -12.900 1.00 33.61  ? 228 ASN   C CB    1 
ATOM   5259  C  CG    . ASN   B 1  228 ? 7.165   26.445  -13.200 1.00 31.53  ? 228 ASN   C CG    1 
ATOM   5260  O  OD1   . ASN   B 1  228 ? 7.525   25.645  -12.333 1.00 28.02  ? 228 ASN   C OD1   1 
ATOM   5261  N  ND2   . ASN   B 1  228 ? 7.688   26.465  -14.429 1.00 33.95  ? 228 ASN   C ND2   1 
ATOM   5262  N  N     . ARG   B 1  229 ? 3.431   28.591  -11.673 1.00 37.06  ? 229 ARG   C N     1 
ATOM   5263  C  CA    . ARG   B 1  229 ? 2.626   29.748  -11.314 1.00 33.96  ? 229 ARG   C CA    1 
ATOM   5264  C  C     . ARG   B 1  229 ? 2.354   29.787  -9.818  1.00 39.37  ? 229 ARG   C C     1 
ATOM   5265  O  O     . ARG   B 1  229 ? 2.491   30.843  -9.185  1.00 40.94  ? 229 ARG   C O     1 
ATOM   5266  C  CB    . ARG   B 1  229 ? 1.339   29.748  -12.129 1.00 31.74  ? 229 ARG   C CB    1 
ATOM   5267  C  CG    . ARG   B 1  229 ? 1.568   30.441  -13.472 1.00 37.08  ? 229 ARG   C CG    1 
ATOM   5268  C  CD    . ARG   B 1  229 ? 0.584   30.011  -14.522 1.00 54.52  ? 229 ARG   C CD    1 
ATOM   5269  N  NE    . ARG   B 1  229 ? 0.623   30.931  -15.650 1.00 61.29  ? 229 ARG   C NE    1 
ATOM   5270  C  CZ    . ARG   B 1  229 ? -0.115  30.814  -16.744 1.00 61.10  ? 229 ARG   C CZ    1 
ATOM   5271  N  NH1   . ARG   B 1  229 ? -0.970  29.809  -16.897 1.00 53.80  ? 229 ARG   C NH1   1 
ATOM   5272  N  NH2   . ARG   B 1  229 ? 0.018   31.720  -17.711 1.00 58.87  ? 229 ARG   C NH2   1 
ATOM   5273  N  N     . LEU   B 1  230 ? 2.009   28.643  -9.222  1.00 31.72  ? 230 LEU   C N     1 
ATOM   5274  C  CA    . LEU   B 1  230 ? 1.817   28.618  -7.778  1.00 30.21  ? 230 LEU   C CA    1 
ATOM   5275  C  C     . LEU   B 1  230 ? 3.120   28.927  -7.048  1.00 36.90  ? 230 LEU   C C     1 
ATOM   5276  O  O     . LEU   B 1  230 ? 3.139   29.731  -6.105  1.00 39.05  ? 230 LEU   C O     1 
ATOM   5277  C  CB    . LEU   B 1  230 ? 1.251   27.264  -7.356  1.00 41.53  ? 230 LEU   C CB    1 
ATOM   5278  C  CG    . LEU   B 1  230 ? 0.809   27.004  -5.920  1.00 31.57  ? 230 LEU   C CG    1 
ATOM   5279  C  CD1   . LEU   B 1  230 ? 0.079   28.190  -5.332  1.00 29.14  ? 230 LEU   C CD1   1 
ATOM   5280  C  CD2   . LEU   B 1  230 ? -0.109  25.831  -6.009  1.00 36.59  ? 230 LEU   C CD2   1 
ATOM   5281  N  N     . ILE   B 1  231 ? 4.228   28.318  -7.486  1.00 33.35  ? 231 ILE   C N     1 
ATOM   5282  C  CA    . ILE   B 1  231 ? 5.526   28.641  -6.903  1.00 30.06  ? 231 ILE   C CA    1 
ATOM   5283  C  C     . ILE   B 1  231 ? 5.854   30.123  -7.064  1.00 36.67  ? 231 ILE   C C     1 
ATOM   5284  O  O     . ILE   B 1  231 ? 6.478   30.730  -6.182  1.00 32.60  ? 231 ILE   C O     1 
ATOM   5285  C  CB    . ILE   B 1  231 ? 6.601   27.746  -7.528  1.00 26.72  ? 231 ILE   C CB    1 
ATOM   5286  C  CG1   . ILE   B 1  231 ? 6.101   26.296  -7.518  1.00 29.81  ? 231 ILE   C CG1   1 
ATOM   5287  C  CG2   . ILE   B 1  231 ? 7.930   27.904  -6.780  1.00 20.33  ? 231 ILE   C CG2   1 
ATOM   5288  C  CD1   . ILE   B 1  231 ? 7.184   25.291  -7.739  1.00 27.18  ? 231 ILE   C CD1   1 
ATOM   5289  N  N     . SER   B 1  232 ? 5.425   30.739  -8.173  1.00 36.36  ? 232 SER   C N     1 
ATOM   5290  C  CA    . SER   B 1  232 ? 5.709   32.156  -8.390  1.00 31.10  ? 232 SER   C CA    1 
ATOM   5291  C  C     . SER   B 1  232 ? 4.990   33.026  -7.369  1.00 40.06  ? 232 SER   C C     1 
ATOM   5292  O  O     . SER   B 1  232 ? 5.535   34.039  -6.906  1.00 35.81  ? 232 SER   C O     1 
ATOM   5293  C  CB    . SER   B 1  232 ? 5.306   32.555  -9.799  1.00 39.68  ? 232 SER   C CB    1 
ATOM   5294  O  OG    . SER   B 1  232 ? 5.545   31.499  -10.722 1.00 51.81  ? 232 SER   C OG    1 
ATOM   5295  N  N     . GLN   B 1  233 ? 3.757   32.649  -7.021  1.00 40.45  ? 233 GLN   C N     1 
ATOM   5296  C  CA    . GLN   B 1  233 ? 3.057   33.287  -5.914  1.00 32.42  ? 233 GLN   C CA    1 
ATOM   5297  C  C     . GLN   B 1  233 ? 3.867   33.198  -4.630  1.00 32.51  ? 233 GLN   C C     1 
ATOM   5298  O  O     . GLN   B 1  233 ? 4.102   34.205  -3.957  1.00 35.32  ? 233 GLN   C O     1 
ATOM   5299  C  CB    . GLN   B 1  233 ? 1.677   32.648  -5.742  1.00 36.06  ? 233 GLN   C CB    1 
ATOM   5300  C  CG    . GLN   B 1  233 ? 0.765   32.915  -6.931  1.00 32.01  ? 233 GLN   C CG    1 
ATOM   5301  C  CD    . GLN   B 1  233 ? 0.679   34.399  -7.228  1.00 28.63  ? 233 GLN   C CD    1 
ATOM   5302  O  OE1   . GLN   B 1  233 ? 1.144   35.223  -6.448  1.00 33.94  ? 233 GLN   C OE1   1 
ATOM   5303  N  NE2   . GLN   B 1  233 ? 0.081   34.744  -8.344  1.00 26.50  ? 233 GLN   C NE2   1 
ATOM   5304  N  N     . ILE   B 1  234 ? 4.328   32.003  -4.278  1.00 35.26  ? 234 ILE   C N     1 
ATOM   5305  C  CA    . ILE   B 1  234 ? 5.031   31.867  -3.006  1.00 32.64  ? 234 ILE   C CA    1 
ATOM   5306  C  C     . ILE   B 1  234 ? 6.359   32.620  -3.036  1.00 33.52  ? 234 ILE   C C     1 
ATOM   5307  O  O     . ILE   B 1  234 ? 6.709   33.323  -2.078  1.00 36.06  ? 234 ILE   C O     1 
ATOM   5308  C  CB    . ILE   B 1  234 ? 5.201   30.379  -2.667  1.00 33.02  ? 234 ILE   C CB    1 
ATOM   5309  C  CG1   . ILE   B 1  234 ? 3.813   29.750  -2.476  1.00 36.86  ? 234 ILE   C CG1   1 
ATOM   5310  C  CG2   . ILE   B 1  234 ? 6.088   30.214  -1.459  1.00 25.43  ? 234 ILE   C CG2   1 
ATOM   5311  C  CD1   . ILE   B 1  234 ? 3.537   28.483  -3.301  1.00 33.23  ? 234 ILE   C CD1   1 
ATOM   5312  N  N     . VAL   B 1  235 ? 7.109   32.516  -4.138  1.00 32.56  ? 235 VAL   C N     1 
ATOM   5313  C  CA    . VAL   B 1  235 ? 8.394   33.215  -4.226  1.00 31.87  ? 235 VAL   C CA    1 
ATOM   5314  C  C     . VAL   B 1  235 ? 8.199   34.730  -4.082  1.00 34.75  ? 235 VAL   C C     1 
ATOM   5315  O  O     . VAL   B 1  235 ? 8.918   35.395  -3.331  1.00 33.21  ? 235 VAL   C O     1 
ATOM   5316  C  CB    . VAL   B 1  235 ? 9.117   32.846  -5.538  1.00 29.59  ? 235 VAL   C CB    1 
ATOM   5317  C  CG1   . VAL   B 1  235 ? 10.287  33.778  -5.775  1.00 26.98  ? 235 VAL   C CG1   1 
ATOM   5318  C  CG2   . VAL   B 1  235 ? 9.590   31.384  -5.519  1.00 19.52  ? 235 VAL   C CG2   1 
ATOM   5319  N  N     . SER   B 1  236 ? 7.207   35.295  -4.783  1.00 34.06  ? 236 SER   C N     1 
ATOM   5320  C  CA    . SER   B 1  236 ? 6.942   36.732  -4.708  1.00 31.24  ? 236 SER   C CA    1 
ATOM   5321  C  C     . SER   B 1  236 ? 6.527   37.191  -3.309  1.00 36.59  ? 236 SER   C C     1 
ATOM   5322  O  O     . SER   B 1  236 ? 6.816   38.332  -2.919  1.00 40.31  ? 236 SER   C O     1 
ATOM   5323  C  CB    . SER   B 1  236 ? 5.854   37.120  -5.715  1.00 41.96  ? 236 SER   C CB    1 
ATOM   5324  O  OG    . SER   B 1  236 ? 5.134   38.272  -5.277  1.00 39.64  ? 236 SER   C OG    1 
ATOM   5325  N  N     . SER   B 1  237 ? 5.817   36.355  -2.550  1.00 36.09  ? 237 SER   C N     1 
ATOM   5326  C  CA    . SER   B 1  237 ? 5.499   36.734  -1.177  1.00 31.50  ? 237 SER   C CA    1 
ATOM   5327  C  C     . SER   B 1  237 ? 6.765   36.851  -0.344  1.00 35.49  ? 237 SER   C C     1 
ATOM   5328  O  O     . SER   B 1  237 ? 6.921   37.807  0.425   1.00 36.37  ? 237 SER   C O     1 
ATOM   5329  C  CB    . SER   B 1  237 ? 4.540   35.729  -0.544  1.00 30.46  ? 237 SER   C CB    1 
ATOM   5330  O  OG    . SER   B 1  237 ? 3.800   35.057  -1.531  1.00 29.75  ? 237 SER   C OG    1 
ATOM   5331  N  N     . ILE   B 1  238 ? 7.682   35.884  -0.479  1.00 35.15  ? 238 ILE   C N     1 
ATOM   5332  C  CA    . ILE   B 1  238 ? 8.940   35.962  0.261   1.00 34.84  ? 238 ILE   C CA    1 
ATOM   5333  C  C     . ILE   B 1  238 ? 9.722   37.201  -0.149  1.00 38.51  ? 238 ILE   C C     1 
ATOM   5334  O  O     . ILE   B 1  238 ? 10.271  37.915  0.705   1.00 45.79  ? 238 ILE   C O     1 
ATOM   5335  C  CB    . ILE   B 1  238 ? 9.787   34.689  0.066   1.00 37.57  ? 238 ILE   C CB    1 
ATOM   5336  C  CG1   . ILE   B 1  238 ? 9.337   33.561  0.998   1.00 33.65  ? 238 ILE   C CG1   1 
ATOM   5337  C  CG2   . ILE   B 1  238 ? 11.264  35.014  0.255   1.00 31.93  ? 238 ILE   C CG2   1 
ATOM   5338  C  CD1   . ILE   B 1  238 ? 8.508   32.510  0.312   1.00 31.30  ? 238 ILE   C CD1   1 
ATOM   5339  N  N     . THR   B 1  239 ? 9.800   37.475  -1.455  1.00 28.63  ? 239 THR   C N     1 
ATOM   5340  C  CA    . THR   B 1  239 ? 10.587  38.610  -1.933  1.00 43.63  ? 239 THR   C CA    1 
ATOM   5341  C  C     . THR   B 1  239 ? 9.831   39.929  -1.956  1.00 39.93  ? 239 THR   C C     1 
ATOM   5342  O  O     . THR   B 1  239 ? 10.452  40.966  -2.208  1.00 37.50  ? 239 THR   C O     1 
ATOM   5343  C  CB    . THR   B 1  239 ? 11.093  38.369  -3.345  1.00 38.90  ? 239 THR   C CB    1 
ATOM   5344  O  OG1   . THR   B 1  239 ? 9.978   38.436  -4.241  1.00 35.72  ? 239 THR   C OG1   1 
ATOM   5345  C  CG2   . THR   B 1  239 ? 11.804  37.013  -3.448  1.00 39.99  ? 239 THR   C CG2   1 
ATOM   5346  N  N     . ALA   B 1  240 ? 8.513   39.908  -1.738  1.00 38.66  ? 240 ALA   C N     1 
ATOM   5347  C  CA    . ALA   B 1  240 ? 7.720   41.125  -1.862  1.00 42.09  ? 240 ALA   C CA    1 
ATOM   5348  C  C     . ALA   B 1  240 ? 8.202   42.205  -0.911  1.00 41.77  ? 240 ALA   C C     1 
ATOM   5349  O  O     . ALA   B 1  240 ? 8.024   43.400  -1.189  1.00 42.13  ? 240 ALA   C O     1 
ATOM   5350  C  CB    . ALA   B 1  240 ? 6.242   40.820  -1.616  1.00 33.90  ? 240 ALA   C CB    1 
ATOM   5351  N  N     . SER   B 1  241 ? 8.826   41.803  0.204   1.00 44.59  ? 241 SER   C N     1 
ATOM   5352  C  CA    . SER   B 1  241 ? 9.298   42.759  1.204   1.00 44.83  ? 241 SER   C CA    1 
ATOM   5353  C  C     . SER   B 1  241 ? 10.493  43.557  0.697   1.00 48.25  ? 241 SER   C C     1 
ATOM   5354  O  O     . SER   B 1  241 ? 10.636  44.738  1.043   1.00 46.19  ? 241 SER   C O     1 
ATOM   5355  C  CB    . SER   B 1  241 ? 9.657   42.022  2.491   1.00 47.20  ? 241 SER   C CB    1 
ATOM   5356  O  OG    . SER   B 1  241 ? 8.928   40.802  2.576   1.00 49.54  ? 241 SER   C OG    1 
ATOM   5357  N  N     . LEU   B 1  242 ? 11.357  42.936  -0.123  1.00 39.13  ? 242 LEU   C N     1 
ATOM   5358  C  CA    . LEU   B 1  242 ? 12.482  43.665  -0.701  1.00 38.69  ? 242 LEU   C CA    1 
ATOM   5359  C  C     . LEU   B 1  242 ? 12.058  44.555  -1.854  1.00 42.22  ? 242 LEU   C C     1 
ATOM   5360  O  O     . LEU   B 1  242 ? 12.701  45.584  -2.097  1.00 41.76  ? 242 LEU   C O     1 
ATOM   5361  C  CB    . LEU   B 1  242 ? 13.564  42.710  -1.197  1.00 36.69  ? 242 LEU   C CB    1 
ATOM   5362  C  CG    . LEU   B 1  242 ? 13.862  41.508  -0.311  1.00 35.66  ? 242 LEU   C CG    1 
ATOM   5363  C  CD1   . LEU   B 1  242 ? 15.182  40.918  -0.687  1.00 30.80  ? 242 LEU   C CD1   1 
ATOM   5364  C  CD2   . LEU   B 1  242 ? 13.853  41.899  1.143   1.00 47.04  ? 242 LEU   C CD2   1 
ATOM   5365  N  N     . ARG   B 1  243 ? 10.994  44.175  -2.572  1.00 39.74  ? 243 ARG   C N     1 
ATOM   5366  C  CA    . ARG   B 1  243 ? 10.582  44.888  -3.772  1.00 37.15  ? 243 ARG   C CA    1 
ATOM   5367  C  C     . ARG   B 1  243 ? 9.567   45.982  -3.491  1.00 44.57  ? 243 ARG   C C     1 
ATOM   5368  O  O     . ARG   B 1  243 ? 9.394   46.870  -4.337  1.00 45.07  ? 243 ARG   C O     1 
ATOM   5369  C  CB    . ARG   B 1  243 ? 9.998   43.919  -4.807  1.00 40.56  ? 243 ARG   C CB    1 
ATOM   5370  C  CG    . ARG   B 1  243 ? 10.985  42.890  -5.323  1.00 34.75  ? 243 ARG   C CG    1 
ATOM   5371  C  CD    . ARG   B 1  243 ? 10.313  41.904  -6.243  1.00 30.14  ? 243 ARG   C CD    1 
ATOM   5372  N  NE    . ARG   B 1  243 ? 9.400   41.008  -5.546  1.00 33.11  ? 243 ARG   C NE    1 
ATOM   5373  C  CZ    . ARG   B 1  243 ? 8.089   40.967  -5.733  1.00 31.56  ? 243 ARG   C CZ    1 
ATOM   5374  N  NH1   . ARG   B 1  243 ? 7.482   41.797  -6.567  1.00 32.47  ? 243 ARG   C NH1   1 
ATOM   5375  N  NH2   . ARG   B 1  243 ? 7.369   40.066  -5.072  1.00 29.03  ? 243 ARG   C NH2   1 
ATOM   5376  N  N     . PHE   B 1  244 ? 8.896   45.941  -2.336  1.00 42.17  ? 244 PHE   C N     1 
ATOM   5377  C  CA    . PHE   B 1  244 ? 7.979   46.997  -1.930  1.00 48.12  ? 244 PHE   C CA    1 
ATOM   5378  C  C     . PHE   B 1  244 ? 8.356   47.515  -0.552  1.00 51.20  ? 244 PHE   C C     1 
ATOM   5379  O  O     . PHE   B 1  244 ? 8.960   46.805  0.257   1.00 64.98  ? 244 PHE   C O     1 
ATOM   5380  C  CB    . PHE   B 1  244 ? 6.534   46.513  -1.906  1.00 46.28  ? 244 PHE   C CB    1 
ATOM   5381  C  CG    . PHE   B 1  244 ? 6.006   46.145  -3.244  1.00 40.35  ? 244 PHE   C CG    1 
ATOM   5382  C  CD1   . PHE   B 1  244 ? 5.521   47.119  -4.097  1.00 41.48  ? 244 PHE   C CD1   1 
ATOM   5383  C  CD2   . PHE   B 1  244 ? 5.984   44.825  -3.651  1.00 39.19  ? 244 PHE   C CD2   1 
ATOM   5384  C  CE1   . PHE   B 1  244 ? 5.021   46.788  -5.336  1.00 38.67  ? 244 PHE   C CE1   1 
ATOM   5385  C  CE2   . PHE   B 1  244 ? 5.489   44.483  -4.883  1.00 40.27  ? 244 PHE   C CE2   1 
ATOM   5386  C  CZ    . PHE   B 1  244 ? 5.007   45.473  -5.736  1.00 42.52  ? 244 PHE   C CZ    1 
ATOM   5387  N  N     . ASP   B 1  245 ? 7.994   48.755  -0.277  1.00 47.00  ? 245 ASP   C N     1 
ATOM   5388  C  CA    . ASP   B 1  245 ? 8.213   49.288  1.054   1.00 61.09  ? 245 ASP   C CA    1 
ATOM   5389  C  C     . ASP   B 1  245 ? 6.898   49.809  1.616   1.00 55.44  ? 245 ASP   C C     1 
ATOM   5390  O  O     . ASP   B 1  245 ? 5.979   50.165  0.878   1.00 47.58  ? 245 ASP   C O     1 
ATOM   5391  C  CB    . ASP   B 1  245 ? 9.294   50.382  1.055   1.00 62.10  ? 245 ASP   C CB    1 
ATOM   5392  C  CG    . ASP   B 1  245 ? 10.326  50.183  2.169   1.00 69.72  ? 245 ASP   C CG    1 
ATOM   5393  O  OD1   . ASP   B 1  245 ? 9.924   49.832  3.299   1.00 67.84  ? 245 ASP   C OD1   1 
ATOM   5394  O  OD2   . ASP   B 1  245 ? 11.540  50.370  1.916   1.00 75.10  ? 245 ASP   C OD2   1 
ATOM   5395  N  N     . GLY   B 1  246 ? 6.814   49.816  2.936   1.00 60.07  ? 246 GLY   C N     1 
ATOM   5396  C  CA    . GLY   B 1  246 ? 5.618   50.209  3.643   1.00 45.36  ? 246 GLY   C CA    1 
ATOM   5397  C  C     . GLY   B 1  246 ? 5.901   50.143  5.123   1.00 53.88  ? 246 GLY   C C     1 
ATOM   5398  O  O     . GLY   B 1  246 ? 6.720   49.323  5.556   1.00 51.43  ? 246 GLY   C O     1 
ATOM   5399  N  N     . ALA   B 1  247 ? 5.249   51.005  5.908   1.00 58.12  ? 247 ALA   C N     1 
ATOM   5400  C  CA    . ALA   B 1  247 ? 5.540   51.065  7.338   1.00 58.23  ? 247 ALA   C CA    1 
ATOM   5401  C  C     . ALA   B 1  247 ? 5.433   49.688  7.996   1.00 61.81  ? 247 ALA   C C     1 
ATOM   5402  O  O     . ALA   B 1  247 ? 6.277   49.325  8.831   1.00 54.16  ? 247 ALA   C O     1 
ATOM   5403  C  CB    . ALA   B 1  247 ? 4.604   52.068  8.018   1.00 61.06  ? 247 ALA   C CB    1 
ATOM   5404  N  N     . LEU   B 1  248 ? 4.407   48.898  7.621   1.00 43.91  ? 248 LEU   C N     1 
ATOM   5405  C  CA    . LEU   B 1  248 ? 4.181   47.590  8.225   1.00 40.26  ? 248 LEU   C CA    1 
ATOM   5406  C  C     . LEU   B 1  248 ? 4.922   46.463  7.525   1.00 42.65  ? 248 LEU   C C     1 
ATOM   5407  O  O     . LEU   B 1  248 ? 4.890   45.326  8.017   1.00 43.16  ? 248 LEU   C O     1 
ATOM   5408  C  CB    . LEU   B 1  248 ? 2.687   47.274  8.264   1.00 42.46  ? 248 LEU   C CB    1 
ATOM   5409  C  CG    . LEU   B 1  248 ? 1.938   48.159  9.260   1.00 49.90  ? 248 LEU   C CG    1 
ATOM   5410  C  CD1   . LEU   B 1  248 ? 0.513   47.685  9.444   1.00 45.29  ? 248 LEU   C CD1   1 
ATOM   5411  C  CD2   . LEU   B 1  248 ? 2.688   48.232  10.612  1.00 43.27  ? 248 LEU   C CD2   1 
ATOM   5412  N  N     . ASN   B 1  249 ? 5.591   46.750  6.408   1.00 49.09  ? 249 ASN   C N     1 
ATOM   5413  C  CA    . ASN   B 1  249 ? 6.475   45.780  5.771   1.00 52.43  ? 249 ASN   C CA    1 
ATOM   5414  C  C     . ASN   B 1  249 ? 7.656   45.447  6.687   1.00 51.86  ? 249 ASN   C C     1 
ATOM   5415  O  O     . ASN   B 1  249 ? 8.159   46.291  7.439   1.00 54.19  ? 249 ASN   C O     1 
ATOM   5416  C  CB    . ASN   B 1  249 ? 6.972   46.325  4.425   1.00 49.51  ? 249 ASN   C CB    1 
ATOM   5417  C  CG    . ASN   B 1  249 ? 7.380   45.224  3.460   1.00 65.44  ? 249 ASN   C CG    1 
ATOM   5418  O  OD1   . ASN   B 1  249 ? 6.557   44.371  3.076   1.00 57.99  ? 249 ASN   C OD1   1 
ATOM   5419  N  ND2   . ASN   B 1  249 ? 8.652   45.238  3.051   1.00 58.17  ? 249 ASN   C ND2   1 
ATOM   5420  N  N     . VAL   B 1  250 ? 8.095   44.197  6.628   1.00 42.99  ? 250 VAL   C N     1 
ATOM   5421  C  CA    . VAL   B 1  250 ? 9.213   43.725  7.429   1.00 46.54  ? 250 VAL   C CA    1 
ATOM   5422  C  C     . VAL   B 1  250 ? 10.178  43.005  6.504   1.00 54.80  ? 250 VAL   C C     1 
ATOM   5423  O  O     . VAL   B 1  250 ? 9.772   42.095  5.772   1.00 60.80  ? 250 VAL   C O     1 
ATOM   5424  C  CB    . VAL   B 1  250 ? 8.745   42.799  8.565   1.00 46.07  ? 250 VAL   C CB    1 
ATOM   5425  C  CG1   . VAL   B 1  250 ? 9.914   42.434  9.453   1.00 52.34  ? 250 VAL   C CG1   1 
ATOM   5426  C  CG2   . VAL   B 1  250 ? 7.652   43.476  9.362   1.00 44.78  ? 250 VAL   C CG2   1 
ATOM   5427  N  N     . ASP   B 1  251 ? 11.449  43.411  6.534   1.00 65.74  ? 251 ASP   C N     1 
ATOM   5428  C  CA    . ASP   B 1  251 ? 12.416  42.918  5.554   1.00 71.01  ? 251 ASP   C CA    1 
ATOM   5429  C  C     . ASP   B 1  251 ? 12.575  41.407  5.671   1.00 56.51  ? 251 ASP   C C     1 
ATOM   5430  O  O     . ASP   B 1  251 ? 12.467  40.835  6.760   1.00 53.15  ? 251 ASP   C O     1 
ATOM   5431  C  CB    . ASP   B 1  251 ? 13.784  43.602  5.735   1.00 64.91  ? 251 ASP   C CB    1 
ATOM   5432  C  CG    . ASP   B 1  251 ? 14.401  44.051  4.403   1.00 69.17  ? 251 ASP   C CG    1 
ATOM   5433  O  OD1   . ASP   B 1  251 ? 13.672  44.672  3.592   1.00 59.69  ? 251 ASP   C OD1   1 
ATOM   5434  O  OD2   . ASP   B 1  251 ? 15.610  43.799  4.168   1.00 68.56  ? 251 ASP   C OD2   1 
ATOM   5435  N  N     . LEU   B 1  252 ? 12.834  40.765  4.523   1.00 54.54  ? 252 LEU   C N     1 
ATOM   5436  C  CA    . LEU   B 1  252 ? 13.115  39.332  4.514   1.00 43.67  ? 252 LEU   C CA    1 
ATOM   5437  C  C     . LEU   B 1  252 ? 14.320  38.989  5.385   1.00 47.52  ? 252 LEU   C C     1 
ATOM   5438  O  O     . LEU   B 1  252 ? 14.326  37.951  6.055   1.00 45.31  ? 252 LEU   C O     1 
ATOM   5439  C  CB    . LEU   B 1  252 ? 13.341  38.838  3.091   1.00 39.92  ? 252 LEU   C CB    1 
ATOM   5440  C  CG    . LEU   B 1  252 ? 13.682  37.340  3.018   1.00 49.04  ? 252 LEU   C CG    1 
ATOM   5441  C  CD1   . LEU   B 1  252 ? 12.812  36.467  3.968   1.00 33.35  ? 252 LEU   C CD1   1 
ATOM   5442  C  CD2   . LEU   B 1  252 ? 13.581  36.846  1.581   1.00 35.90  ? 252 LEU   C CD2   1 
ATOM   5443  N  N     . THR   B 1  253 ? 15.354  39.839  5.397   1.00 48.46  ? 253 THR   C N     1 
ATOM   5444  C  CA    . THR   B 1  253 ? 16.478  39.569  6.292   1.00 48.92  ? 253 THR   C CA    1 
ATOM   5445  C  C     . THR   B 1  253 ? 15.992  39.458  7.726   1.00 40.21  ? 253 THR   C C     1 
ATOM   5446  O  O     . THR   B 1  253 ? 16.340  38.518  8.447   1.00 37.69  ? 253 THR   C O     1 
ATOM   5447  C  CB    . THR   B 1  253 ? 17.557  40.652  6.194   1.00 44.50  ? 253 THR   C CB    1 
ATOM   5448  O  OG1   . THR   B 1  253 ? 17.714  41.076  4.839   1.00 37.00  ? 253 THR   C OG1   1 
ATOM   5449  C  CG2   . THR   B 1  253 ? 18.909  40.103  6.705   1.00 52.59  ? 253 THR   C CG2   1 
ATOM   5450  N  N     . GLU   B 1  254 ? 15.158  40.407  8.144   1.00 44.50  ? 254 GLU   C N     1 
ATOM   5451  C  CA    . GLU   B 1  254 ? 14.692  40.441  9.523   1.00 48.40  ? 254 GLU   C CA    1 
ATOM   5452  C  C     . GLU   B 1  254 ? 13.869  39.201  9.872   1.00 51.26  ? 254 GLU   C C     1 
ATOM   5453  O  O     . GLU   B 1  254 ? 13.939  38.700  11.008  1.00 45.54  ? 254 GLU   C O     1 
ATOM   5454  C  CB    . GLU   B 1  254 ? 13.891  41.720  9.757   1.00 57.58  ? 254 GLU   C CB    1 
ATOM   5455  C  CG    . GLU   B 1  254 ? 13.742  42.104  11.222  1.00 63.88  ? 254 GLU   C CG    1 
ATOM   5456  C  CD    . GLU   B 1  254 ? 13.214  43.510  11.362  1.00 69.16  ? 254 GLU   C CD    1 
ATOM   5457  O  OE1   . GLU   B 1  254 ? 13.702  44.372  10.592  1.00 70.38  ? 254 GLU   C OE1   1 
ATOM   5458  O  OE2   . GLU   B 1  254 ? 12.302  43.737  12.201  1.00 57.19  ? 254 GLU   C OE2   1 
ATOM   5459  N  N     . PHE   B 1  255 ? 13.074  38.689  8.919   1.00 41.18  ? 255 PHE   C N     1 
ATOM   5460  C  CA    . PHE   B 1  255 ? 12.477  37.380  9.150   1.00 32.23  ? 255 PHE   C CA    1 
ATOM   5461  C  C     . PHE   B 1  255 ? 13.555  36.323  9.249   1.00 32.20  ? 255 PHE   C C     1 
ATOM   5462  O  O     . PHE   B 1  255 ? 13.423  35.384  10.035  1.00 41.63  ? 255 PHE   C O     1 
ATOM   5463  C  CB    . PHE   B 1  255 ? 11.497  37.004  8.044   1.00 40.81  ? 255 PHE   C CB    1 
ATOM   5464  C  CG    . PHE   B 1  255 ? 10.176  37.715  8.114   1.00 35.92  ? 255 PHE   C CG    1 
ATOM   5465  C  CD1   . PHE   B 1  255 ? 9.329   37.536  9.192   1.00 40.98  ? 255 PHE   C CD1   1 
ATOM   5466  C  CD2   . PHE   B 1  255 ? 9.754   38.512  7.064   1.00 41.91  ? 255 PHE   C CD2   1 
ATOM   5467  C  CE1   . PHE   B 1  255 ? 8.096   38.172  9.250   1.00 31.17  ? 255 PHE   C CE1   1 
ATOM   5468  C  CE2   . PHE   B 1  255 ? 8.527   39.156  7.107   1.00 51.53  ? 255 PHE   C CE2   1 
ATOM   5469  C  CZ    . PHE   B 1  255 ? 7.698   38.990  8.205   1.00 41.23  ? 255 PHE   C CZ    1 
ATOM   5470  N  N     . GLN   B 1  256 ? 14.643  36.481  8.490   1.00 27.86  ? 256 GLN   C N     1 
ATOM   5471  C  CA    . GLN   B 1  256 ? 15.710  35.487  8.484   1.00 30.57  ? 256 GLN   C CA    1 
ATOM   5472  C  C     . GLN   B 1  256 ? 16.364  35.344  9.862   1.00 34.65  ? 256 GLN   C C     1 
ATOM   5473  O  O     . GLN   B 1  256 ? 16.746  34.235  10.267  1.00 31.95  ? 256 GLN   C O     1 
ATOM   5474  C  CB    . GLN   B 1  256 ? 16.734  35.857  7.412   1.00 34.78  ? 256 GLN   C CB    1 
ATOM   5475  C  CG    . GLN   B 1  256 ? 17.772  34.797  7.066   1.00 39.58  ? 256 GLN   C CG    1 
ATOM   5476  C  CD    . GLN   B 1  256 ? 18.539  35.134  5.769   1.00 52.83  ? 256 GLN   C CD    1 
ATOM   5477  O  OE1   . GLN   B 1  256 ? 17.944  35.663  4.822   1.00 47.53  ? 256 GLN   C OE1   1 
ATOM   5478  N  NE2   . GLN   B 1  256 ? 19.856  34.825  5.725   1.00 28.15  ? 256 GLN   C NE2   1 
ATOM   5479  N  N     . THR   B 1  257 ? 16.496  36.447  10.604  1.00 27.15  ? 257 THR   C N     1 
ATOM   5480  C  CA    . THR   B 1  257 ? 17.059  36.359  11.945  1.00 23.95  ? 257 THR   C CA    1 
ATOM   5481  C  C     . THR   B 1  257 ? 16.284  35.373  12.796  1.00 25.07  ? 257 THR   C C     1 
ATOM   5482  O  O     . THR   B 1  257 ? 16.875  34.585  13.542  1.00 27.74  ? 257 THR   C O     1 
ATOM   5483  C  CB    . THR   B 1  257 ? 17.069  37.725  12.629  1.00 36.62  ? 257 THR   C CB    1 
ATOM   5484  O  OG1   . THR   B 1  257 ? 17.648  38.713  11.756  1.00 39.17  ? 257 THR   C OG1   1 
ATOM   5485  C  CG2   . THR   B 1  257 ? 17.869  37.643  13.936  1.00 19.32  ? 257 THR   C CG2   1 
ATOM   5486  N  N     . ASN   B 1  258 ? 14.960  35.402  12.697  1.00 30.92  ? 258 ASN   C N     1 
ATOM   5487  C  CA    . ASN   B 1  258 ? 14.105  34.499  13.462  1.00 28.37  ? 258 ASN   C CA    1 
ATOM   5488  C  C     . ASN   B 1  258 ? 14.038  33.090  12.882  1.00 31.43  ? 258 ASN   C C     1 
ATOM   5489  O  O     . ASN   B 1  258 ? 13.746  32.146  13.625  1.00 31.65  ? 258 ASN   C O     1 
ATOM   5490  C  CB    . ASN   B 1  258 ? 12.688  35.074  13.558  1.00 28.10  ? 258 ASN   C CB    1 
ATOM   5491  C  CG    . ASN   B 1  258 ? 12.576  36.183  14.585  1.00 23.94  ? 258 ASN   C CG    1 
ATOM   5492  O  OD1   . ASN   B 1  258 ? 13.569  36.772  14.985  1.00 33.82  ? 258 ASN   C OD1   1 
ATOM   5493  N  ND2   . ASN   B 1  258 ? 11.373  36.451  15.027  1.00 23.51  ? 258 ASN   C ND2   1 
ATOM   5494  N  N     . LEU   B 1  259 ? 14.325  32.920  11.588  1.00 30.70  ? 259 LEU   C N     1 
ATOM   5495  C  CA    . LEU   B 1  259 ? 14.115  31.634  10.929  1.00 26.32  ? 259 LEU   C CA    1 
ATOM   5496  C  C     . LEU   B 1  259 ? 15.280  30.661  11.101  1.00 25.39  ? 259 LEU   C C     1 
ATOM   5497  O  O     . LEU   B 1  259 ? 15.066  29.448  11.010  1.00 36.25  ? 259 LEU   C O     1 
ATOM   5498  C  CB    . LEU   B 1  259 ? 13.813  31.885  9.446   1.00 30.99  ? 259 LEU   C CB    1 
ATOM   5499  C  CG    . LEU   B 1  259 ? 12.364  32.385  9.334   1.00 28.10  ? 259 LEU   C CG    1 
ATOM   5500  C  CD1   . LEU   B 1  259 ? 11.954  33.040  8.002   1.00 17.29  ? 259 LEU   C CD1   1 
ATOM   5501  C  CD2   . LEU   B 1  259 ? 11.424  31.236  9.726   1.00 24.25  ? 259 LEU   C CD2   1 
ATOM   5502  N  N     . VAL   B 1  260 ? 16.482  31.143  11.387  1.00 27.24  ? 260 VAL   C N     1 
ATOM   5503  C  CA    . VAL   B 1  260 ? 17.687  30.322  11.415  1.00 24.23  ? 260 VAL   C CA    1 
ATOM   5504  C  C     . VAL   B 1  260 ? 18.324  30.394  12.805  1.00 23.14  ? 260 VAL   C C     1 
ATOM   5505  O  O     . VAL   B 1  260 ? 19.122  31.287  13.091  1.00 21.47  ? 260 VAL   C O     1 
ATOM   5506  C  CB    . VAL   B 1  260 ? 18.677  30.769  10.329  1.00 22.32  ? 260 VAL   C CB    1 
ATOM   5507  C  CG1   . VAL   B 1  260 ? 19.905  29.913  10.384  1.00 15.23  ? 260 VAL   C CG1   1 
ATOM   5508  C  CG2   . VAL   B 1  260 ? 17.989  30.729  8.980   1.00 17.69  ? 260 VAL   C CG2   1 
ATOM   5509  N  N     . PRO   B 1  261 ? 18.044  29.419  13.679  1.00 19.83  ? 261 PRO   C N     1 
ATOM   5510  C  CA    . PRO   B 1  261 ? 18.613  29.437  15.036  1.00 22.60  ? 261 PRO   C CA    1 
ATOM   5511  C  C     . PRO   B 1  261 ? 20.011  28.829  15.123  1.00 26.46  ? 261 PRO   C C     1 
ATOM   5512  O  O     . PRO   B 1  261 ? 20.680  28.978  16.152  1.00 25.98  ? 261 PRO   C O     1 
ATOM   5513  C  CB    . PRO   B 1  261 ? 17.612  28.603  15.828  1.00 19.69  ? 261 PRO   C CB    1 
ATOM   5514  C  CG    . PRO   B 1  261 ? 17.206  27.558  14.822  1.00 19.43  ? 261 PRO   C CG    1 
ATOM   5515  C  CD    . PRO   B 1  261 ? 17.242  28.210  13.457  1.00 22.15  ? 261 PRO   C CD    1 
ATOM   5516  N  N     . TYR   B 1  262 ? 20.450  28.114  14.098  1.00 25.13  ? 262 TYR   C N     1 
ATOM   5517  C  CA    . TYR   B 1  262 ? 21.796  27.582  13.987  1.00 22.96  ? 262 TYR   C CA    1 
ATOM   5518  C  C     . TYR   B 1  262 ? 22.109  27.534  12.503  1.00 24.92  ? 262 TYR   C C     1 
ATOM   5519  O  O     . TYR   B 1  262 ? 21.186  27.417  11.687  1.00 23.92  ? 262 TYR   C O     1 
ATOM   5520  C  CB    . TYR   B 1  262 ? 21.913  26.189  14.601  1.00 18.02  ? 262 TYR   C CB    1 
ATOM   5521  C  CG    . TYR   B 1  262 ? 21.408  26.088  16.011  1.00 29.96  ? 262 TYR   C CG    1 
ATOM   5522  C  CD1   . TYR   B 1  262 ? 20.065  25.763  16.280  1.00 23.44  ? 262 TYR   C CD1   1 
ATOM   5523  C  CD2   . TYR   B 1  262 ? 22.270  26.311  17.089  1.00 24.51  ? 262 TYR   C CD2   1 
ATOM   5524  C  CE1   . TYR   B 1  262 ? 19.605  25.668  17.581  1.00 23.22  ? 262 TYR   C CE1   1 
ATOM   5525  C  CE2   . TYR   B 1  262 ? 21.822  26.221  18.385  1.00 23.51  ? 262 TYR   C CE2   1 
ATOM   5526  C  CZ    . TYR   B 1  262 ? 20.500  25.891  18.630  1.00 26.67  ? 262 TYR   C CZ    1 
ATOM   5527  O  OH    . TYR   B 1  262 ? 20.090  25.815  19.933  1.00 25.50  ? 262 TYR   C OH    1 
ATOM   5528  N  N     . PRO   B 1  263 ? 23.378  27.627  12.116  1.00 24.37  ? 263 PRO   C N     1 
ATOM   5529  C  CA    . PRO   B 1  263 ? 23.673  27.695  10.673  1.00 25.92  ? 263 PRO   C CA    1 
ATOM   5530  C  C     . PRO   B 1  263 ? 23.019  26.571  9.878   1.00 23.37  ? 263 PRO   C C     1 
ATOM   5531  O  O     . PRO   B 1  263 ? 22.454  26.832  8.813   1.00 21.82  ? 263 PRO   C O     1 
ATOM   5532  C  CB    . PRO   B 1  263 ? 25.208  27.638  10.630  1.00 14.53  ? 263 PRO   C CB    1 
ATOM   5533  C  CG    . PRO   B 1  263 ? 25.633  28.169  11.949  1.00 15.69  ? 263 PRO   C CG    1 
ATOM   5534  C  CD    . PRO   B 1  263 ? 24.597  27.694  12.933  1.00 21.18  ? 263 PRO   C CD    1 
ATOM   5535  N  N     . ARG   B 1  264 ? 23.047  25.331  10.385  1.00 27.84  ? 264 ARG   C N     1 
ATOM   5536  C  CA    . ARG   B 1  264 ? 22.541  24.200  9.609   1.00 27.35  ? 264 ARG   C CA    1 
ATOM   5537  C  C     . ARG   B 1  264 ? 21.008  24.133  9.584   1.00 27.68  ? 264 ARG   C C     1 
ATOM   5538  O  O     . ARG   B 1  264 ? 20.436  23.620  8.616   1.00 27.45  ? 264 ARG   C O     1 
ATOM   5539  C  CB    . ARG   B 1  264 ? 23.145  22.892  10.146  1.00 20.03  ? 264 ARG   C CB    1 
ATOM   5540  C  CG    . ARG   B 1  264 ? 24.621  22.709  9.811   1.00 11.92  ? 264 ARG   C CG    1 
ATOM   5541  C  CD    . ARG   B 1  264 ? 25.296  21.598  10.649  1.00 10.94  ? 264 ARG   C CD    1 
ATOM   5542  N  NE    . ARG   B 1  264 ? 24.801  20.257  10.350  1.00 17.05  ? 264 ARG   C NE    1 
ATOM   5543  C  CZ    . ARG   B 1  264 ? 25.186  19.524  9.303   1.00 25.67  ? 264 ARG   C CZ    1 
ATOM   5544  N  NH1   . ARG   B 1  264 ? 26.101  19.958  8.453   1.00 21.84  ? 264 ARG   C NH1   1 
ATOM   5545  N  NH2   . ARG   B 1  264 ? 24.636  18.325  9.103   1.00 22.55  ? 264 ARG   C NH2   1 
ATOM   5546  N  N     . ILE   B 1  265 ? 20.330  24.627  10.625  1.00 26.53  ? 265 ILE   C N     1 
ATOM   5547  C  CA    . ILE   B 1  265 ? 18.868  24.635  10.689  1.00 24.90  ? 265 ILE   C CA    1 
ATOM   5548  C  C     . ILE   B 1  265 ? 18.353  25.851  9.917   1.00 21.71  ? 265 ILE   C C     1 
ATOM   5549  O  O     . ILE   B 1  265 ? 17.856  26.820  10.503  1.00 21.21  ? 265 ILE   C O     1 
ATOM   5550  C  CB    . ILE   B 1  265 ? 18.373  24.632  12.157  1.00 28.62  ? 265 ILE   C CB    1 
ATOM   5551  C  CG1   . ILE   B 1  265 ? 19.108  23.560  12.978  1.00 25.60  ? 265 ILE   C CG1   1 
ATOM   5552  C  CG2   . ILE   B 1  265 ? 16.859  24.402  12.252  1.00 21.19  ? 265 ILE   C CG2   1 
ATOM   5553  C  CD1   . ILE   B 1  265 ? 19.112  22.190  12.322  1.00 21.59  ? 265 ILE   C CD1   1 
ATOM   5554  N  N     . HIS   B 1  266 ? 18.455  25.809  8.595   1.00 18.43  ? 266 HIS   C N     1 
ATOM   5555  C  CA    . HIS   B 1  266 ? 18.188  26.977  7.774   1.00 15.73  ? 266 HIS   C CA    1 
ATOM   5556  C  C     . HIS   B 1  266 ? 17.248  26.631  6.624   1.00 19.79  ? 266 HIS   C C     1 
ATOM   5557  O  O     . HIS   B 1  266 ? 17.368  27.170  5.522   1.00 25.86  ? 266 HIS   C O     1 
ATOM   5558  C  CB    . HIS   B 1  266 ? 19.495  27.595  7.267   1.00 19.85  ? 266 HIS   C CB    1 
ATOM   5559  C  CG    . HIS   B 1  266 ? 20.235  26.762  6.254   1.00 20.63  ? 266 HIS   C CG    1 
ATOM   5560  N  ND1   . HIS   B 1  266 ? 21.533  26.336  6.445   1.00 31.95  ? 266 HIS   C ND1   1 
ATOM   5561  C  CD2   . HIS   B 1  266 ? 19.877  26.309  5.030   1.00 21.41  ? 266 HIS   C CD2   1 
ATOM   5562  C  CE1   . HIS   B 1  266 ? 21.935  25.646  5.393   1.00 21.53  ? 266 HIS   C CE1   1 
ATOM   5563  N  NE2   . HIS   B 1  266 ? 20.951  25.621  4.517   1.00 27.10  ? 266 HIS   C NE2   1 
ATOM   5564  N  N     . PHE   B 1  267 ? 16.279  25.744  6.876   1.00 21.80  ? 267 PHE   C N     1 
ATOM   5565  C  CA    . PHE   B 1  267 ? 15.302  25.269  5.891   1.00 19.43  ? 267 PHE   C CA    1 
ATOM   5566  C  C     . PHE   B 1  267 ? 13.871  25.560  6.342   1.00 24.47  ? 267 PHE   C C     1 
ATOM   5567  O  O     . PHE   B 1  267 ? 13.221  24.681  6.940   1.00 25.78  ? 267 PHE   C O     1 
ATOM   5568  C  CB    . PHE   B 1  267 ? 15.458  23.760  5.678   1.00 14.40  ? 267 PHE   C CB    1 
ATOM   5569  C  CG    . PHE   B 1  267 ? 16.770  23.359  5.123   1.00 21.01  ? 267 PHE   C CG    1 
ATOM   5570  C  CD1   . PHE   B 1  267 ? 17.002  23.420  3.737   1.00 17.64  ? 267 PHE   C CD1   1 
ATOM   5571  C  CD2   . PHE   B 1  267 ? 17.789  22.901  5.968   1.00 16.24  ? 267 PHE   C CD2   1 
ATOM   5572  C  CE1   . PHE   B 1  267 ? 18.215  23.041  3.206   1.00 13.33  ? 267 PHE   C CE1   1 
ATOM   5573  C  CE2   . PHE   B 1  267 ? 18.998  22.523  5.444   1.00 23.48  ? 267 PHE   C CE2   1 
ATOM   5574  C  CZ    . PHE   B 1  267 ? 19.221  22.595  4.038   1.00 16.35  ? 267 PHE   C CZ    1 
ATOM   5575  N  N     . PRO   B 1  268 ? 13.323  26.746  6.068   1.00 17.07  ? 268 PRO   C N     1 
ATOM   5576  C  CA    . PRO   B 1  268 ? 11.974  27.058  6.554   1.00 21.48  ? 268 PRO   C CA    1 
ATOM   5577  C  C     . PRO   B 1  268 ? 10.896  26.403  5.704   1.00 26.05  ? 268 PRO   C C     1 
ATOM   5578  O  O     . PRO   B 1  268 ? 11.069  26.165  4.511   1.00 31.57  ? 268 PRO   C O     1 
ATOM   5579  C  CB    . PRO   B 1  268 ? 11.892  28.594  6.452   1.00 26.42  ? 268 PRO   C CB    1 
ATOM   5580  C  CG    . PRO   B 1  268 ? 13.284  29.074  6.129   1.00 22.92  ? 268 PRO   C CG    1 
ATOM   5581  C  CD    . PRO   B 1  268 ? 13.929  27.911  5.408   1.00 27.16  ? 268 PRO   C CD    1 
ATOM   5582  N  N     . LEU   B 1  269 ? 9.774   26.099  6.348   1.00 20.86  ? 269 LEU   C N     1 
ATOM   5583  C  CA    . LEU   B 1  269 ? 8.622   25.516  5.686   1.00 21.00  ? 269 LEU   C CA    1 
ATOM   5584  C  C     . LEU   B 1  269 ? 7.679   26.642  5.271   1.00 27.01  ? 269 LEU   C C     1 
ATOM   5585  O  O     . LEU   B 1  269 ? 7.221   27.410  6.119   1.00 39.60  ? 269 LEU   C O     1 
ATOM   5586  C  CB    . LEU   B 1  269 ? 7.922   24.543  6.626   1.00 20.35  ? 269 LEU   C CB    1 
ATOM   5587  C  CG    . LEU   B 1  269 ? 6.702   23.809  6.075   1.00 31.99  ? 269 LEU   C CG    1 
ATOM   5588  C  CD1   . LEU   B 1  269 ? 7.132   22.829  4.985   1.00 35.43  ? 269 LEU   C CD1   1 
ATOM   5589  C  CD2   . LEU   B 1  269 ? 5.929   23.078  7.187   1.00 24.81  ? 269 LEU   C CD2   1 
ATOM   5590  N  N     . ALA   B 1  270 ? 7.411   26.762  3.980   1.00 20.15  ? 270 ALA   C N     1 
ATOM   5591  C  CA    . ALA   B 1  270 ? 6.536   27.803  3.464   1.00 23.87  ? 270 ALA   C CA    1 
ATOM   5592  C  C     . ALA   B 1  270 ? 5.136   27.238  3.311   1.00 27.24  ? 270 ALA   C C     1 
ATOM   5593  O  O     . ALA   B 1  270 ? 4.966   26.081  2.918   1.00 26.85  ? 270 ALA   C O     1 
ATOM   5594  C  CB    . ALA   B 1  270 ? 7.028   28.344  2.111   1.00 19.03  ? 270 ALA   C CB    1 
ATOM   5595  N  N     . THR   B 1  271 ? 4.132   28.053  3.645   1.00 27.19  ? 271 THR   C N     1 
ATOM   5596  C  CA    . THR   B 1  271 ? 2.731   27.690  3.438   1.00 32.72  ? 271 THR   C CA    1 
ATOM   5597  C  C     . THR   B 1  271 ? 2.001   28.910  2.907   1.00 34.25  ? 271 THR   C C     1 
ATOM   5598  O  O     . THR   B 1  271 ? 2.183   30.017  3.421   1.00 38.12  ? 271 THR   C O     1 
ATOM   5599  C  CB    . THR   B 1  271 ? 2.024   27.215  4.717   1.00 36.75  ? 271 THR   C CB    1 
ATOM   5600  O  OG1   . THR   B 1  271 ? 2.776   26.169  5.363   1.00 44.35  ? 271 THR   C OG1   1 
ATOM   5601  C  CG2   . THR   B 1  271 ? 0.665   26.687  4.355   1.00 38.26  ? 271 THR   C CG2   1 
ATOM   5602  N  N     . TYR   B 1  272 ? 1.166   28.707  1.893   1.00 26.74  ? 272 TYR   C N     1 
ATOM   5603  C  CA    . TYR   B 1  272 ? 0.539   29.825  1.204   1.00 35.86  ? 272 TYR   C CA    1 
ATOM   5604  C  C     . TYR   B 1  272 ? -0.973  29.624  1.123   1.00 38.28  ? 272 TYR   C C     1 
ATOM   5605  O  O     . TYR   B 1  272 ? -1.446  28.506  0.907   1.00 45.25  ? 272 TYR   C O     1 
ATOM   5606  C  CB    . TYR   B 1  272 ? 1.147   29.995  -0.202  1.00 27.98  ? 272 TYR   C CB    1 
ATOM   5607  C  CG    . TYR   B 1  272 ? 0.539   31.117  -0.986  1.00 29.88  ? 272 TYR   C CG    1 
ATOM   5608  C  CD1   . TYR   B 1  272 ? 1.058   32.389  -0.914  1.00 27.19  ? 272 TYR   C CD1   1 
ATOM   5609  C  CD2   . TYR   B 1  272 ? -0.565  30.902  -1.807  1.00 33.62  ? 272 TYR   C CD2   1 
ATOM   5610  C  CE1   . TYR   B 1  272 ? 0.504   33.423  -1.632  1.00 22.97  ? 272 TYR   C CE1   1 
ATOM   5611  C  CE2   . TYR   B 1  272 ? -1.132  31.940  -2.534  1.00 30.12  ? 272 TYR   C CE2   1 
ATOM   5612  C  CZ    . TYR   B 1  272 ? -0.593  33.201  -2.436  1.00 23.14  ? 272 TYR   C CZ    1 
ATOM   5613  O  OH    . TYR   B 1  272 ? -1.148  34.252  -3.136  1.00 27.83  ? 272 TYR   C OH    1 
ATOM   5614  N  N     . ALA   B 1  273 ? -1.725  30.707  1.293   1.00 26.03  ? 273 ALA   C N     1 
ATOM   5615  C  CA    . ALA   B 1  273 ? -3.167  30.690  1.105   1.00 26.21  ? 273 ALA   C CA    1 
ATOM   5616  C  C     . ALA   B 1  273 ? -3.603  32.094  0.726   1.00 26.95  ? 273 ALA   C C     1 
ATOM   5617  O  O     . ALA   B 1  273 ? -2.903  33.060  1.028   1.00 34.19  ? 273 ALA   C O     1 
ATOM   5618  C  CB    . ALA   B 1  273 ? -3.893  30.219  2.370   1.00 20.77  ? 273 ALA   C CB    1 
ATOM   5619  N  N     . PRO   B 1  274 ? -4.736  32.246  0.054   1.00 22.52  ? 274 PRO   C N     1 
ATOM   5620  C  CA    . PRO   B 1  274 ? -5.641  31.222  -0.479  1.00 29.42  ? 274 PRO   C CA    1 
ATOM   5621  C  C     . PRO   B 1  274 ? -5.177  30.748  -1.844  1.00 24.71  ? 274 PRO   C C     1 
ATOM   5622  O  O     . PRO   B 1  274 ? -4.744  31.563  -2.646  1.00 28.29  ? 274 PRO   C O     1 
ATOM   5623  C  CB    . PRO   B 1  274 ? -6.983  31.970  -0.573  1.00 28.82  ? 274 PRO   C CB    1 
ATOM   5624  C  CG    . PRO   B 1  274 ? -6.570  33.366  -0.950  1.00 31.41  ? 274 PRO   C CG    1 
ATOM   5625  C  CD    . PRO   B 1  274 ? -5.242  33.606  -0.211  1.00 26.75  ? 274 PRO   C CD    1 
ATOM   5626  N  N     . VAL   B 1  275 ? -5.236  29.449  -2.118  1.00 27.14  ? 275 VAL   C N     1 
ATOM   5627  C  CA    . VAL   B 1  275 ? -5.067  28.897  -3.461  1.00 32.56  ? 275 VAL   C CA    1 
ATOM   5628  C  C     . VAL   B 1  275 ? -6.443  28.414  -3.887  1.00 32.75  ? 275 VAL   C C     1 
ATOM   5629  O  O     . VAL   B 1  275 ? -6.948  27.408  -3.371  1.00 28.33  ? 275 VAL   C O     1 
ATOM   5630  C  CB    . VAL   B 1  275 ? -4.030  27.763  -3.508  1.00 30.19  ? 275 VAL   C CB    1 
ATOM   5631  C  CG1   . VAL   B 1  275 ? -3.812  27.292  -4.959  1.00 26.41  ? 275 VAL   C CG1   1 
ATOM   5632  C  CG2   . VAL   B 1  275 ? -2.728  28.234  -2.916  1.00 28.57  ? 275 VAL   C CG2   1 
ATOM   5633  N  N     . ILE   B 1  276 ? -7.064  29.146  -4.806  1.00 32.81  ? 276 ILE   C N     1 
ATOM   5634  C  CA    . ILE   B 1  276 ? -8.472  28.962  -5.111  1.00 26.13  ? 276 ILE   C CA    1 
ATOM   5635  C  C     . ILE   B 1  276 ? -8.716  29.348  -6.559  1.00 38.09  ? 276 ILE   C C     1 
ATOM   5636  O  O     . ILE   B 1  276 ? -8.065  30.245  -7.101  1.00 34.40  ? 276 ILE   C O     1 
ATOM   5637  C  CB    . ILE   B 1  276 ? -9.330  29.815  -4.163  1.00 38.72  ? 276 ILE   C CB    1 
ATOM   5638  C  CG1   . ILE   B 1  276 ? -10.607 29.074  -3.761  1.00 46.74  ? 276 ILE   C CG1   1 
ATOM   5639  C  CG2   . ILE   B 1  276 ? -9.649  31.139  -4.826  1.00 37.46  ? 276 ILE   C CG2   1 
ATOM   5640  C  CD1   . ILE   B 1  276 ? -11.639 29.996  -3.114  1.00 43.51  ? 276 ILE   C CD1   1 
ATOM   5641  N  N     . SER   B 1  277 ? -9.676  28.672  -7.187  1.00 48.47  ? 277 SER   C N     1 
ATOM   5642  C  CA    . SER   B 1  277 ? -10.058 28.989  -8.559  1.00 36.15  ? 277 SER   C CA    1 
ATOM   5643  C  C     . SER   B 1  277 ? -10.942 30.239  -8.614  1.00 35.53  ? 277 SER   C C     1 
ATOM   5644  O  O     . SER   B 1  277 ? -11.571 30.633  -7.630  1.00 36.74  ? 277 SER   C O     1 
ATOM   5645  C  CB    . SER   B 1  277 ? -10.799 27.814  -9.174  1.00 45.91  ? 277 SER   C CB    1 
ATOM   5646  O  OG    . SER   B 1  277 ? -11.915 27.480  -8.357  1.00 53.14  ? 277 SER   C OG    1 
ATOM   5647  N  N     . ALA   B 1  278 ? -10.975 30.871  -9.787  1.00 35.66  ? 278 ALA   C N     1 
ATOM   5648  C  CA    . ALA   B 1  278 ? -11.939 31.942  -10.026 1.00 35.79  ? 278 ALA   C CA    1 
ATOM   5649  C  C     . ALA   B 1  278 ? -13.359 31.493  -9.684  1.00 38.49  ? 278 ALA   C C     1 
ATOM   5650  O  O     . ALA   B 1  278 ? -14.083 32.173  -8.945  1.00 36.42  ? 278 ALA   C O     1 
ATOM   5651  C  CB    . ALA   B 1  278 ? -11.866 32.407  -11.486 1.00 25.18  ? 278 ALA   C CB    1 
ATOM   5652  N  N     . GLU   B 1  279 ? -13.770 30.343  -10.215 1.00 31.03  ? 279 GLU   C N     1 
ATOM   5653  C  CA    . GLU   B 1  279 ? -15.156 29.909  -10.078 1.00 34.05  ? 279 GLU   C CA    1 
ATOM   5654  C  C     . GLU   B 1  279 ? -15.574 29.781  -8.619  1.00 45.84  ? 279 GLU   C C     1 
ATOM   5655  O  O     . GLU   B 1  279 ? -16.754 29.975  -8.296  1.00 46.66  ? 279 GLU   C O     1 
ATOM   5656  C  CB    . GLU   B 1  279 ? -15.370 28.569  -10.805 1.00 37.65  ? 279 GLU   C CB    1 
ATOM   5657  C  CG    . GLU   B 1  279 ? -15.009 28.546  -12.301 1.00 36.29  ? 279 GLU   C CG    1 
ATOM   5658  C  CD    . GLU   B 1  279 ? -13.589 28.084  -12.585 1.00 54.85  ? 279 GLU   C CD    1 
ATOM   5659  O  OE1   . GLU   B 1  279 ? -12.705 28.223  -11.711 1.00 54.26  ? 279 GLU   C OE1   1 
ATOM   5660  O  OE2   . GLU   B 1  279 ? -13.346 27.582  -13.701 1.00 68.68  ? 279 GLU   C OE2   1 
ATOM   5661  N  N     . LYS   B 1  280 ? -14.629 29.453  -7.724  1.00 49.15  ? 280 LYS   C N     1 
ATOM   5662  C  CA    . LYS   B 1  280 ? -14.928 29.257  -6.305  1.00 47.47  ? 280 LYS   C CA    1 
ATOM   5663  C  C     . LYS   B 1  280 ? -14.604 30.466  -5.425  1.00 40.98  ? 280 LYS   C C     1 
ATOM   5664  O  O     . LYS   B 1  280 ? -15.082 30.530  -4.288  1.00 42.17  ? 280 LYS   C O     1 
ATOM   5665  C  CB    . LYS   B 1  280 ? -14.185 28.026  -5.776  1.00 43.86  ? 280 LYS   C CB    1 
ATOM   5666  C  CG    . LYS   B 1  280 ? -15.045 27.172  -4.874  1.00 61.14  ? 280 LYS   C CG    1 
ATOM   5667  C  CD    . LYS   B 1  280 ? -14.562 25.722  -4.807  1.00 77.08  ? 280 LYS   C CD    1 
ATOM   5668  C  CE    . LYS   B 1  280 ? -15.094 25.011  -3.549  1.00 77.19  ? 280 LYS   C CE    1 
ATOM   5669  N  NZ    . LYS   B 1  280 ? -14.546 25.593  -2.268  1.00 52.16  ? 280 LYS   C NZ    1 
ATOM   5670  N  N     . ALA   B 1  281 ? -13.824 31.429  -5.914  1.00 44.69  ? 281 ALA   C N     1 
ATOM   5671  C  CA    . ALA   B 1  281 ? -13.635 32.687  -5.199  1.00 44.64  ? 281 ALA   C CA    1 
ATOM   5672  C  C     . ALA   B 1  281 ? -14.730 33.687  -5.498  1.00 42.67  ? 281 ALA   C C     1 
ATOM   5673  O  O     . ALA   B 1  281 ? -14.738 34.763  -4.895  1.00 45.31  ? 281 ALA   C O     1 
ATOM   5674  C  CB    . ALA   B 1  281 ? -12.292 33.329  -5.555  1.00 36.94  ? 281 ALA   C CB    1 
ATOM   5675  N  N     . TYR   B 1  282 ? -15.615 33.371  -6.437  1.00 42.06  ? 282 TYR   C N     1 
ATOM   5676  C  CA    . TYR   B 1  282 ? -16.691 34.275  -6.812  1.00 37.96  ? 282 TYR   C CA    1 
ATOM   5677  C  C     . TYR   B 1  282 ? -17.702 34.414  -5.675  1.00 34.78  ? 282 TYR   C C     1 
ATOM   5678  O  O     . TYR   B 1  282 ? -18.110 33.419  -5.069  1.00 37.99  ? 282 TYR   C O     1 
ATOM   5679  C  CB    . TYR   B 1  282 ? -17.367 33.760  -8.079  1.00 38.84  ? 282 TYR   C CB    1 
ATOM   5680  C  CG    . TYR   B 1  282 ? -18.412 34.694  -8.607  1.00 38.44  ? 282 TYR   C CG    1 
ATOM   5681  C  CD1   . TYR   B 1  282 ? -18.065 35.962  -9.041  1.00 41.44  ? 282 TYR   C CD1   1 
ATOM   5682  C  CD2   . TYR   B 1  282 ? -19.749 34.323  -8.642  1.00 39.61  ? 282 TYR   C CD2   1 
ATOM   5683  C  CE1   . TYR   B 1  282 ? -19.013 36.838  -9.496  1.00 40.41  ? 282 TYR   C CE1   1 
ATOM   5684  C  CE2   . TYR   B 1  282 ? -20.706 35.188  -9.104  1.00 42.40  ? 282 TYR   C CE2   1 
ATOM   5685  C  CZ    . TYR   B 1  282 ? -20.330 36.446  -9.528  1.00 41.45  ? 282 TYR   C CZ    1 
ATOM   5686  O  OH    . TYR   B 1  282 ? -21.279 37.323  -9.991  1.00 60.49  ? 282 TYR   C OH    1 
ATOM   5687  N  N     . HIS   B 1  283 ? -18.085 35.660  -5.372  1.00 47.01  ? 283 HIS   C N     1 
ATOM   5688  C  CA    . HIS   B 1  283 ? -19.027 35.999  -4.298  1.00 63.09  ? 283 HIS   C CA    1 
ATOM   5689  C  C     . HIS   B 1  283 ? -18.600 35.439  -2.939  1.00 55.64  ? 283 HIS   C C     1 
ATOM   5690  O  O     . HIS   B 1  283 ? -19.406 35.364  -2.004  1.00 55.84  ? 283 HIS   C O     1 
ATOM   5691  C  CB    . HIS   B 1  283 ? -20.459 35.522  -4.621  1.00 63.68  ? 283 HIS   C CB    1 
ATOM   5692  C  CG    . HIS   B 1  283 ? -21.177 36.357  -5.638  1.00 56.25  ? 283 HIS   C CG    1 
ATOM   5693  N  ND1   . HIS   B 1  283 ? -22.406 36.000  -6.155  1.00 47.74  ? 283 HIS   C ND1   1 
ATOM   5694  C  CD2   . HIS   B 1  283 ? -20.844 37.533  -6.228  1.00 48.64  ? 283 HIS   C CD2   1 
ATOM   5695  C  CE1   . HIS   B 1  283 ? -22.795 36.916  -7.026  1.00 51.81  ? 283 HIS   C CE1   1 
ATOM   5696  N  NE2   . HIS   B 1  283 ? -21.868 37.857  -7.089  1.00 50.25  ? 283 HIS   C NE2   1 
ATOM   5697  N  N     . GLU   B 1  284 ? -17.348 35.030  -2.796  1.00 53.74  ? 284 GLU   C N     1 
ATOM   5698  C  CA    . GLU   B 1  284 ? -16.883 34.369  -1.582  1.00 52.13  ? 284 GLU   C CA    1 
ATOM   5699  C  C     . GLU   B 1  284 ? -15.589 35.060  -1.163  1.00 59.01  ? 284 GLU   C C     1 
ATOM   5700  O  O     . GLU   B 1  284 ? -14.517 34.720  -1.668  1.00 73.10  ? 284 GLU   C O     1 
ATOM   5701  C  CB    . GLU   B 1  284 ? -16.694 32.879  -1.830  1.00 53.99  ? 284 GLU   C CB    1 
ATOM   5702  C  CG    . GLU   B 1  284 ? -17.385 32.011  -0.813  1.00 54.24  ? 284 GLU   C CG    1 
ATOM   5703  C  CD    . GLU   B 1  284 ? -16.743 32.113  0.554   1.00 67.14  ? 284 GLU   C CD    1 
ATOM   5704  O  OE1   . GLU   B 1  284 ? -15.667 31.502  0.749   1.00 65.44  ? 284 GLU   C OE1   1 
ATOM   5705  O  OE2   . GLU   B 1  284 ? -17.306 32.815  1.430   1.00 73.63  ? 284 GLU   C OE2   1 
ATOM   5706  N  N     . GLN   B 1  285 ? -15.692 36.040  -0.267  1.00 47.97  ? 285 GLN   C N     1 
ATOM   5707  C  CA    . GLN   B 1  285 ? -14.509 36.722  0.236   1.00 52.43  ? 285 GLN   C CA    1 
ATOM   5708  C  C     . GLN   B 1  285 ? -13.763 35.821  1.221   1.00 44.42  ? 285 GLN   C C     1 
ATOM   5709  O  O     . GLN   B 1  285 ? -14.352 34.976  1.895   1.00 48.38  ? 285 GLN   C O     1 
ATOM   5710  C  CB    . GLN   B 1  285 ? -14.901 38.047  0.903   1.00 51.72  ? 285 GLN   C CB    1 
ATOM   5711  C  CG    . GLN   B 1  285 ? -13.751 39.069  1.058   1.00 65.89  ? 285 GLN   C CG    1 
ATOM   5712  C  CD    . GLN   B 1  285 ? -13.402 39.817  -0.250  1.00 75.46  ? 285 GLN   C CD    1 
ATOM   5713  O  OE1   . GLN   B 1  285 ? -13.725 39.359  -1.359  1.00 71.91  ? 285 GLN   C OE1   1 
ATOM   5714  N  NE2   . GLN   B 1  285 ? -12.746 40.975  -0.115  1.00 45.21  ? 285 GLN   C NE2   1 
ATOM   5715  N  N     . LEU   B 1  286 ? -12.450 35.999  1.295   1.00 46.50  ? 286 LEU   C N     1 
ATOM   5716  C  CA    . LEU   B 1  286 ? -11.591 35.145  2.114   1.00 42.27  ? 286 LEU   C CA    1 
ATOM   5717  C  C     . LEU   B 1  286 ? -10.930 36.020  3.175   1.00 37.26  ? 286 LEU   C C     1 
ATOM   5718  O  O     . LEU   B 1  286 ? -10.145 36.918  2.854   1.00 37.51  ? 286 LEU   C O     1 
ATOM   5719  C  CB    . LEU   B 1  286 ? -10.568 34.423  1.235   1.00 56.24  ? 286 LEU   C CB    1 
ATOM   5720  C  CG    . LEU   B 1  286 ? -11.102 33.984  -0.153  1.00 56.22  ? 286 LEU   C CG    1 
ATOM   5721  C  CD1   . LEU   B 1  286 ? -11.013 35.109  -1.230  1.00 31.63  ? 286 LEU   C CD1   1 
ATOM   5722  C  CD2   . LEU   B 1  286 ? -10.493 32.644  -0.649  1.00 35.18  ? 286 LEU   C CD2   1 
ATOM   5723  N  N     . SER   B 1  287 ? -11.263 35.779  4.433   1.00 41.70  ? 287 SER   C N     1 
ATOM   5724  C  CA    . SER   B 1  287 ? -10.907 36.704  5.494   1.00 35.90  ? 287 SER   C CA    1 
ATOM   5725  C  C     . SER   B 1  287 ? -9.495  36.439  5.990   1.00 41.91  ? 287 SER   C C     1 
ATOM   5726  O  O     . SER   B 1  287 ? -8.969  35.325  5.873   1.00 41.90  ? 287 SER   C O     1 
ATOM   5727  C  CB    . SER   B 1  287 ? -11.858 36.565  6.673   1.00 33.16  ? 287 SER   C CB    1 
ATOM   5728  O  OG    . SER   B 1  287 ? -11.438 35.495  7.507   1.00 34.46  ? 287 SER   C OG    1 
ATOM   5729  N  N     . VAL   B 1  288 ? -8.896  37.470  6.586   1.00 33.20  ? 288 VAL   C N     1 
ATOM   5730  C  CA    . VAL   B 1  288 ? -7.635  37.343  7.307   1.00 32.77  ? 288 VAL   C CA    1 
ATOM   5731  C  C     . VAL   B 1  288 ? -7.671  36.090  8.192   1.00 36.40  ? 288 VAL   C C     1 
ATOM   5732  O  O     . VAL   B 1  288 ? -6.694  35.329  8.253   1.00 32.97  ? 288 VAL   C O     1 
ATOM   5733  C  CB    . VAL   B 1  288 ? -7.343  38.616  8.129   1.00 23.32  ? 288 VAL   C CB    1 
ATOM   5734  C  CG1   . VAL   B 1  288 ? -6.157  38.404  9.047   1.00 26.58  ? 288 VAL   C CG1   1 
ATOM   5735  C  CG2   . VAL   B 1  288 ? -7.059  39.761  7.203   1.00 25.59  ? 288 VAL   C CG2   1 
ATOM   5736  N  N     . ALA   B 1  289 ? -8.811  35.838  8.850   1.00 35.03  ? 289 ALA   C N     1 
ATOM   5737  C  CA    . ALA   B 1  289 ? -8.892  34.701  9.769   1.00 36.65  ? 289 ALA   C CA    1 
ATOM   5738  C  C     . ALA   B 1  289 ? -8.816  33.373  9.024   1.00 36.85  ? 289 ALA   C C     1 
ATOM   5739  O  O     . ALA   B 1  289 ? -8.186  32.421  9.499   1.00 39.63  ? 289 ALA   C O     1 
ATOM   5740  C  CB    . ALA   B 1  289 ? -10.175 34.783  10.603  1.00 27.12  ? 289 ALA   C CB    1 
ATOM   5741  N  N     . GLU   B 1  290 ? -9.434  33.293  7.848   1.00 44.89  ? 290 GLU   C N     1 
ATOM   5742  C  CA    . GLU   B 1  290 ? -9.448  32.033  7.116   1.00 42.61  ? 290 GLU   C CA    1 
ATOM   5743  C  C     . GLU   B 1  290 ? -8.109  31.733  6.438   1.00 36.91  ? 290 GLU   C C     1 
ATOM   5744  O  O     . GLU   B 1  290 ? -7.670  30.578  6.452   1.00 39.92  ? 290 GLU   C O     1 
ATOM   5745  C  CB    . GLU   B 1  290 ? -10.605 32.043  6.115   1.00 44.93  ? 290 GLU   C CB    1 
ATOM   5746  C  CG    . GLU   B 1  290 ? -11.958 31.906  6.821   1.00 52.05  ? 290 GLU   C CG    1 
ATOM   5747  C  CD    . GLU   B 1  290 ? -13.124 32.436  6.000   1.00 52.39  ? 290 GLU   C CD    1 
ATOM   5748  O  OE1   . GLU   B 1  290 ? -12.967 33.486  5.344   1.00 35.15  ? 290 GLU   C OE1   1 
ATOM   5749  O  OE2   . GLU   B 1  290 ? -14.198 31.797  6.011   1.00 50.12  ? 290 GLU   C OE2   1 
ATOM   5750  N  N     . ILE   B 1  291 ? -7.436  32.748  5.862   1.00 34.59  ? 291 ILE   C N     1 
ATOM   5751  C  CA    . ILE   B 1  291 ? -6.123  32.532  5.231   1.00 29.09  ? 291 ILE   C CA    1 
ATOM   5752  C  C     . ILE   B 1  291 ? -5.052  32.232  6.276   1.00 33.90  ? 291 ILE   C C     1 
ATOM   5753  O  O     . ILE   B 1  291 ? -4.160  31.409  6.044   1.00 32.16  ? 291 ILE   C O     1 
ATOM   5754  C  CB    . ILE   B 1  291 ? -5.716  33.729  4.352   1.00 31.95  ? 291 ILE   C CB    1 
ATOM   5755  C  CG1   . ILE   B 1  291 ? -5.477  34.990  5.188   1.00 26.03  ? 291 ILE   C CG1   1 
ATOM   5756  C  CG2   . ILE   B 1  291 ? -6.761  33.978  3.247   1.00 32.88  ? 291 ILE   C CG2   1 
ATOM   5757  C  CD1   . ILE   B 1  291 ? -5.009  36.144  4.345   1.00 24.61  ? 291 ILE   C CD1   1 
ATOM   5758  N  N     . THR   B 1  292 ? -5.107  32.893  7.435   1.00 36.65  ? 292 THR   C N     1 
ATOM   5759  C  CA    . THR   B 1  292 ? -4.230  32.505  8.536   1.00 34.64  ? 292 THR   C CA    1 
ATOM   5760  C  C     . THR   B 1  292 ? -4.488  31.059  8.931   1.00 32.06  ? 292 THR   C C     1 
ATOM   5761  O  O     . THR   B 1  292 ? -3.591  30.210  8.892   1.00 28.62  ? 292 THR   C O     1 
ATOM   5762  C  CB    . THR   B 1  292 ? -4.443  33.437  9.735   1.00 30.18  ? 292 THR   C CB    1 
ATOM   5763  O  OG1   . THR   B 1  292 ? -4.149  34.777  9.350   1.00 35.95  ? 292 THR   C OG1   1 
ATOM   5764  C  CG2   . THR   B 1  292 ? -3.531  33.069  10.889  1.00 20.11  ? 292 THR   C CG2   1 
ATOM   5765  N  N     . ASN   B 1  293 ? -5.727  30.770  9.322   1.00 35.44  ? 293 ASN   C N     1 
ATOM   5766  C  CA    . ASN   B 1  293 ? -6.146  29.407  9.635   1.00 39.76  ? 293 ASN   C CA    1 
ATOM   5767  C  C     . ASN   B 1  293 ? -5.694  28.410  8.559   1.00 36.62  ? 293 ASN   C C     1 
ATOM   5768  O  O     . ASN   B 1  293 ? -5.119  27.358  8.862   1.00 35.41  ? 293 ASN   C O     1 
ATOM   5769  C  CB    . ASN   B 1  293 ? -7.664  29.416  9.796   1.00 42.17  ? 293 ASN   C CB    1 
ATOM   5770  C  CG    . ASN   B 1  293 ? -8.164  28.332  10.700  1.00 61.35  ? 293 ASN   C CG    1 
ATOM   5771  O  OD1   . ASN   B 1  293 ? -7.389  27.532  11.232  1.00 71.60  ? 293 ASN   C OD1   1 
ATOM   5772  N  ND2   . ASN   B 1  293 ? -9.478  28.293  10.886  1.00 74.96  ? 293 ASN   C ND2   1 
ATOM   5773  N  N     . ALA   B 1  294 ? -5.950  28.736  7.289   1.00 37.71  ? 294 ALA   C N     1 
ATOM   5774  C  CA    . ALA   B 1  294 ? -5.453  27.942  6.168   1.00 36.00  ? 294 ALA   C CA    1 
ATOM   5775  C  C     . ALA   B 1  294 ? -3.963  27.616  6.270   1.00 43.01  ? 294 ALA   C C     1 
ATOM   5776  O  O     . ALA   B 1  294 ? -3.531  26.569  5.776   1.00 42.74  ? 294 ALA   C O     1 
ATOM   5777  C  CB    . ALA   B 1  294 ? -5.716  28.680  4.859   1.00 25.50  ? 294 ALA   C CB    1 
ATOM   5778  N  N     . CYS   B 1  295 ? -3.159  28.496  6.891   1.00 45.39  ? 295 CYS   C N     1 
ATOM   5779  C  CA    . CYS   B 1  295 ? -1.703  28.317  6.920   1.00 37.17  ? 295 CYS   C CA    1 
ATOM   5780  C  C     . CYS   B 1  295 ? -1.251  27.172  7.804   1.00 37.11  ? 295 CYS   C C     1 
ATOM   5781  O  O     . CYS   B 1  295 ? -0.089  26.764  7.695   1.00 39.85  ? 295 CYS   C O     1 
ATOM   5782  C  CB    . CYS   B 1  295 ? -0.990  29.563  7.427   1.00 33.65  ? 295 CYS   C CB    1 
ATOM   5783  S  SG    . CYS   B 1  295 ? -0.980  30.942  6.347   1.00 38.18  ? 295 CYS   C SG    1 
ATOM   5784  N  N     . PHE   B 1  296 ? -2.119  26.677  8.690   1.00 33.70  ? 296 PHE   C N     1 
ATOM   5785  C  CA    . PHE   B 1  296 ? -1.771  25.624  9.633   1.00 31.98  ? 296 PHE   C CA    1 
ATOM   5786  C  C     . PHE   B 1  296 ? -2.434  24.299  9.312   1.00 39.31  ? 296 PHE   C C     1 
ATOM   5787  O  O     . PHE   B 1  296 ? -2.369  23.380  10.134  1.00 47.98  ? 296 PHE   C O     1 
ATOM   5788  C  CB    . PHE   B 1  296 ? -2.120  26.043  11.054  1.00 42.70  ? 296 PHE   C CB    1 
ATOM   5789  C  CG    . PHE   B 1  296 ? -1.216  27.095  11.606  1.00 41.70  ? 296 PHE   C CG    1 
ATOM   5790  C  CD1   . PHE   B 1  296 ? -0.043  26.741  12.273  1.00 34.74  ? 296 PHE   C CD1   1 
ATOM   5791  C  CD2   . PHE   B 1  296 ? -1.526  28.436  11.456  1.00 29.20  ? 296 PHE   C CD2   1 
ATOM   5792  C  CE1   . PHE   B 1  296 ? 0.791   27.704  12.787  1.00 34.65  ? 296 PHE   C CE1   1 
ATOM   5793  C  CE2   . PHE   B 1  296 ? -0.696  29.401  11.958  1.00 29.02  ? 296 PHE   C CE2   1 
ATOM   5794  C  CZ    . PHE   B 1  296 ? 0.471   29.038  12.637  1.00 32.54  ? 296 PHE   C CZ    1 
ATOM   5795  N  N     . GLU   B 1  297 ? -3.070  24.181  8.148   1.00 44.17  ? 297 GLU   C N     1 
ATOM   5796  C  CA    . GLU   B 1  297 ? -3.478  22.876  7.611   1.00 46.18  ? 297 GLU   C CA    1 
ATOM   5797  C  C     . GLU   B 1  297 ? -2.282  22.209  6.940   1.00 42.37  ? 297 GLU   C C     1 
ATOM   5798  O  O     . GLU   B 1  297 ? -1.705  22.796  6.018   1.00 50.00  ? 297 GLU   C O     1 
ATOM   5799  C  CB    . GLU   B 1  297 ? -4.592  23.047  6.583   1.00 46.18  ? 297 GLU   C CB    1 
ATOM   5800  C  CG    . GLU   B 1  297 ? -5.650  24.046  6.973   1.00 51.07  ? 297 GLU   C CG    1 
ATOM   5801  C  CD    . GLU   B 1  297 ? -6.660  23.448  7.933   1.00 70.68  ? 297 GLU   C CD    1 
ATOM   5802  O  OE1   . GLU   B 1  297 ? -6.707  22.197  8.030   1.00 65.18  ? 297 GLU   C OE1   1 
ATOM   5803  O  OE2   . GLU   B 1  297 ? -7.394  24.226  8.587   1.00 72.11  ? 297 GLU   C OE2   1 
ATOM   5804  N  N     . PRO   B 1  298 ? -1.882  20.997  7.338   1.00 44.26  ? 298 PRO   C N     1 
ATOM   5805  C  CA    . PRO   B 1  298 ? -0.658  20.426  6.755   1.00 45.15  ? 298 PRO   C CA    1 
ATOM   5806  C  C     . PRO   B 1  298 ? -0.718  20.284  5.251   1.00 40.79  ? 298 PRO   C C     1 
ATOM   5807  O  O     . PRO   B 1  298 ? 0.306   19.974  4.637   1.00 52.93  ? 298 PRO   C O     1 
ATOM   5808  C  CB    . PRO   B 1  298 ? -0.528  19.063  7.458   1.00 37.47  ? 298 PRO   C CB    1 
ATOM   5809  C  CG    . PRO   B 1  298 ? -1.204  19.259  8.760   1.00 28.52  ? 298 PRO   C CG    1 
ATOM   5810  C  CD    . PRO   B 1  298 ? -2.409  20.130  8.407   1.00 39.36  ? 298 PRO   C CD    1 
ATOM   5811  N  N     . ALA   B 1  299 ? -1.856  20.544  4.626   1.00 48.33  ? 299 ALA   C N     1 
ATOM   5812  C  CA    . ALA   B 1  299 ? -2.012  20.310  3.200   1.00 41.96  ? 299 ALA   C CA    1 
ATOM   5813  C  C     . ALA   B 1  299 ? -1.899  21.569  2.356   1.00 43.55  ? 299 ALA   C C     1 
ATOM   5814  O  O     . ALA   B 1  299 ? -2.029  21.483  1.130   1.00 53.43  ? 299 ALA   C O     1 
ATOM   5815  C  CB    . ALA   B 1  299 ? -3.356  19.631  2.930   1.00 46.04  ? 299 ALA   C CB    1 
ATOM   5816  N  N     . ASN   B 1  300 ? -1.678  22.734  2.958   1.00 35.83  ? 300 ASN   C N     1 
ATOM   5817  C  CA    . ASN   B 1  300 ? -1.310  23.903  2.172   1.00 40.77  ? 300 ASN   C CA    1 
ATOM   5818  C  C     . ASN   B 1  300 ? 0.193   24.153  2.163   1.00 43.45  ? 300 ASN   C C     1 
ATOM   5819  O  O     . ASN   B 1  300 ? 0.630   25.225  1.731   1.00 45.90  ? 300 ASN   C O     1 
ATOM   5820  C  CB    . ASN   B 1  300 ? -2.046  25.139  2.672   1.00 39.97  ? 300 ASN   C CB    1 
ATOM   5821  C  CG    . ASN   B 1  300 ? -3.513  25.019  2.500   1.00 36.57  ? 300 ASN   C CG    1 
ATOM   5822  O  OD1   . ASN   B 1  300 ? -3.973  24.374  1.575   1.00 43.77  ? 300 ASN   C OD1   1 
ATOM   5823  N  ND2   . ASN   B 1  300 ? -4.268  25.624  3.394   1.00 43.59  ? 300 ASN   C ND2   1 
ATOM   5824  N  N     . GLN   B 1  301 ? 0.990   23.176  2.594   1.00 41.11  ? 301 GLN   C N     1 
ATOM   5825  C  CA    . GLN   B 1  301 ? 2.427   23.328  2.748   1.00 39.25  ? 301 GLN   C CA    1 
ATOM   5826  C  C     . GLN   B 1  301 ? 3.183   23.075  1.453   1.00 32.26  ? 301 GLN   C C     1 
ATOM   5827  O  O     . GLN   B 1  301 ? 2.728   22.336  0.583   1.00 49.74  ? 301 GLN   C O     1 
ATOM   5828  C  CB    . GLN   B 1  301 ? 2.907   22.382  3.833   1.00 32.47  ? 301 GLN   C CB    1 
ATOM   5829  C  CG    . GLN   B 1  301 ? 1.981   22.471  4.996   1.00 37.44  ? 301 GLN   C CG    1 
ATOM   5830  C  CD    . GLN   B 1  301 ? 2.624   22.024  6.272   1.00 48.24  ? 301 GLN   C CD    1 
ATOM   5831  O  OE1   . GLN   B 1  301 ? 2.881   22.841  7.161   1.00 55.67  ? 301 GLN   C OE1   1 
ATOM   5832  N  NE2   . GLN   B 1  301 ? 2.891   20.722  6.382   1.00 35.85  ? 301 GLN   C NE2   1 
ATOM   5833  N  N     . MET   B 1  302 ? 4.348   23.714  1.328   1.00 37.14  ? 302 MET   C N     1 
ATOM   5834  C  CA    . MET   B 1  302 ? 5.211   23.519  0.164   1.00 28.13  ? 302 MET   C CA    1 
ATOM   5835  C  C     . MET   B 1  302 ? 5.990   22.226  0.236   1.00 24.89  ? 302 MET   C C     1 
ATOM   5836  O  O     . MET   B 1  302 ? 6.460   21.751  -0.796  1.00 34.27  ? 302 MET   C O     1 
ATOM   5837  C  CB    . MET   B 1  302 ? 6.217   24.666  0.008   1.00 25.56  ? 302 MET   C CB    1 
ATOM   5838  C  CG    . MET   B 1  302 ? 5.620   25.974  -0.442  1.00 40.94  ? 302 MET   C CG    1 
ATOM   5839  S  SD    . MET   B 1  302 ? 4.178   25.753  -1.513  1.00 65.12  ? 302 MET   C SD    1 
ATOM   5840  C  CE    . MET   B 1  302 ? 2.867   25.562  -0.309  1.00 47.56  ? 302 MET   C CE    1 
ATOM   5841  N  N     . VAL   B 1  303 ? 6.159   21.665  1.424   1.00 23.34  ? 303 VAL   C N     1 
ATOM   5842  C  CA    . VAL   B 1  303 ? 6.833   20.387  1.605   1.00 31.65  ? 303 VAL   C CA    1 
ATOM   5843  C  C     . VAL   B 1  303 ? 5.896   19.482  2.380   1.00 32.14  ? 303 VAL   C C     1 
ATOM   5844  O  O     . VAL   B 1  303 ? 5.375   19.882  3.428   1.00 34.12  ? 303 VAL   C O     1 
ATOM   5845  C  CB    . VAL   B 1  303 ? 8.171   20.525  2.360   1.00 24.62  ? 303 VAL   C CB    1 
ATOM   5846  C  CG1   . VAL   B 1  303 ? 8.789   19.130  2.644   1.00 16.30  ? 303 VAL   C CG1   1 
ATOM   5847  C  CG2   . VAL   B 1  303 ? 9.116   21.421  1.600   1.00 30.80  ? 303 VAL   C CG2   1 
ATOM   5848  N  N     . LYS   B 1  304 ? 5.700   18.267  1.886   1.00 29.37  ? 304 LYS   C N     1 
ATOM   5849  C  CA    . LYS   B 1  304 ? 4.877   17.301  2.601   1.00 27.17  ? 304 LYS   C CA    1 
ATOM   5850  C  C     . LYS   B 1  304 ? 5.587   16.796  3.854   1.00 25.86  ? 304 LYS   C C     1 
ATOM   5851  O  O     . LYS   B 1  304 ? 6.653   16.183  3.762   1.00 30.20  ? 304 LYS   C O     1 
ATOM   5852  C  CB    . LYS   B 1  304 ? 4.530   16.142  1.678   1.00 30.51  ? 304 LYS   C CB    1 
ATOM   5853  C  CG    . LYS   B 1  304 ? 3.404   16.441  0.715   1.00 20.66  ? 304 LYS   C CG    1 
ATOM   5854  C  CD    . LYS   B 1  304 ? 2.765   15.132  0.330   1.00 31.53  ? 304 LYS   C CD    1 
ATOM   5855  C  CE    . LYS   B 1  304 ? 1.383   15.283  -0.256  1.00 40.82  ? 304 LYS   C CE    1 
ATOM   5856  N  NZ    . LYS   B 1  304 ? 0.817   13.925  -0.320  1.00 39.95  ? 304 LYS   C NZ    1 
ATOM   5857  N  N     . CYS   B 1  305 ? 4.966   17.011  5.015   1.00 26.21  ? 305 CYS   C N     1 
ATOM   5858  C  CA    . CYS   B 1  305 ? 5.466   16.685  6.352   1.00 28.69  ? 305 CYS   C CA    1 
ATOM   5859  C  C     . CYS   B 1  305 ? 4.371   17.088  7.336   1.00 26.02  ? 305 CYS   C C     1 
ATOM   5860  O  O     . CYS   B 1  305 ? 3.426   17.784  6.962   1.00 30.84  ? 305 CYS   C O     1 
ATOM   5861  C  CB    . CYS   B 1  305 ? 6.776   17.424  6.663   1.00 38.31  ? 305 CYS   C CB    1 
ATOM   5862  S  SG    . CYS   B 1  305 ? 6.576   19.242  6.733   1.00 29.81  ? 305 CYS   C SG    1 
ATOM   5863  N  N     . ASP   B 1  306 ? 4.500   16.675  8.596   1.00 28.26  ? 306 ASP   C N     1 
ATOM   5864  C  CA    . ASP   B 1  306 ? 3.457   16.973  9.587   1.00 36.24  ? 306 ASP   C CA    1 
ATOM   5865  C  C     . ASP   B 1  306 ? 3.950   17.841  10.731  1.00 31.75  ? 306 ASP   C C     1 
ATOM   5866  O  O     . ASP   B 1  306 ? 4.526   17.327  11.712  1.00 30.61  ? 306 ASP   C O     1 
ATOM   5867  C  CB    . ASP   B 1  306 ? 2.828   15.701  10.160  1.00 43.10  ? 306 ASP   C CB    1 
ATOM   5868  C  CG    . ASP   B 1  306 ? 1.409   15.953  10.701  1.00 43.97  ? 306 ASP   C CG    1 
ATOM   5869  O  OD1   . ASP   B 1  306 ? 1.098   17.102  11.081  1.00 41.17  ? 306 ASP   C OD1   1 
ATOM   5870  O  OD2   . ASP   B 1  306 ? 0.588   15.015  10.717  1.00 65.41  ? 306 ASP   C OD2   1 
ATOM   5871  N  N     . PRO   B 1  307 ? 3.668   19.137  10.698  1.00 29.31  ? 307 PRO   C N     1 
ATOM   5872  C  CA    . PRO   B 1  307 ? 4.164   20.019  11.767  1.00 41.86  ? 307 PRO   C CA    1 
ATOM   5873  C  C     . PRO   B 1  307 ? 3.440   19.841  13.100  1.00 38.50  ? 307 PRO   C C     1 
ATOM   5874  O  O     . PRO   B 1  307 ? 4.046   20.099  14.150  1.00 36.95  ? 307 PRO   C O     1 
ATOM   5875  C  CB    . PRO   B 1  307 ? 3.954   21.424  11.185  1.00 29.25  ? 307 PRO   C CB    1 
ATOM   5876  C  CG    . PRO   B 1  307 ? 3.605   21.198  9.718   1.00 28.07  ? 307 PRO   C CG    1 
ATOM   5877  C  CD    . PRO   B 1  307 ? 2.942   19.877  9.662   1.00 32.64  ? 307 PRO   C CD    1 
ATOM   5878  N  N     . ARG   B 1  308 ? 2.169   19.415  13.095  1.00 35.78  ? 308 ARG   C N     1 
ATOM   5879  C  CA    . ARG   B 1  308 ? 1.464   19.172  14.356  1.00 38.34  ? 308 ARG   C CA    1 
ATOM   5880  C  C     . ARG   B 1  308 ? 2.197   18.142  15.200  1.00 42.55  ? 308 ARG   C C     1 
ATOM   5881  O  O     . ARG   B 1  308 ? 2.077   18.152  16.431  1.00 49.09  ? 308 ARG   C O     1 
ATOM   5882  C  CB    . ARG   B 1  308 ? 0.018   18.711  14.114  1.00 38.69  ? 308 ARG   C CB    1 
ATOM   5883  C  CG    . ARG   B 1  308 ? -0.760  19.546  13.091  1.00 50.90  ? 308 ARG   C CG    1 
ATOM   5884  C  CD    . ARG   B 1  308 ? -2.114  18.950  12.735  1.00 54.22  ? 308 ARG   C CD    1 
ATOM   5885  N  NE    . ARG   B 1  308 ? -2.002  17.563  12.296  1.00 71.82  ? 308 ARG   C NE    1 
ATOM   5886  C  CZ    . ARG   B 1  308 ? -2.017  16.510  13.111  1.00 71.84  ? 308 ARG   C CZ    1 
ATOM   5887  N  NH1   . ARG   B 1  308 ? -2.183  16.647  14.423  1.00 54.72  ? 308 ARG   C NH1   1 
ATOM   5888  N  NH2   . ARG   B 1  308 ? -1.851  15.289  12.597  1.00 53.01  ? 308 ARG   C NH2   1 
ATOM   5889  N  N     . HIS   B 1  309 ? 2.968   17.255  14.562  1.00 35.25  ? 309 HIS   C N     1 
ATOM   5890  C  CA    . HIS   B 1  309 ? 3.786   16.270  15.259  1.00 35.75  ? 309 HIS   C CA    1 
ATOM   5891  C  C     . HIS   B 1  309 ? 5.253   16.689  15.325  1.00 41.64  ? 309 HIS   C C     1 
ATOM   5892  O  O     . HIS   B 1  309 ? 6.146   15.833  15.414  1.00 41.05  ? 309 HIS   C O     1 
ATOM   5893  C  CB    . HIS   B 1  309 ? 3.647   14.891  14.606  1.00 42.45  ? 309 HIS   C CB    1 
ATOM   5894  C  CG    . HIS   B 1  309 ? 2.262   14.318  14.684  1.00 47.83  ? 309 HIS   C CG    1 
ATOM   5895  N  ND1   . HIS   B 1  309 ? 1.636   13.730  13.603  1.00 52.86  ? 309 HIS   C ND1   1 
ATOM   5896  C  CD2   . HIS   B 1  309 ? 1.383   14.242  15.713  1.00 48.30  ? 309 HIS   C CD2   1 
ATOM   5897  C  CE1   . HIS   B 1  309 ? 0.428   13.330  13.958  1.00 53.26  ? 309 HIS   C CE1   1 
ATOM   5898  N  NE2   . HIS   B 1  309 ? 0.249   13.627  15.234  1.00 62.58  ? 309 HIS   C NE2   1 
ATOM   5899  N  N     . GLY   B 1  310 ? 5.517   17.995  15.269  1.00 37.10  ? 310 GLY   C N     1 
ATOM   5900  C  CA    . GLY   B 1  310 ? 6.863   18.514  15.408  1.00 38.10  ? 310 GLY   C CA    1 
ATOM   5901  C  C     . GLY   B 1  310 ? 6.909   19.687  16.368  1.00 40.54  ? 310 GLY   C C     1 
ATOM   5902  O  O     . GLY   B 1  310 ? 5.911   19.982  17.039  1.00 39.46  ? 310 GLY   C O     1 
ATOM   5903  N  N     . LYS   B 1  311 ? 8.046   20.363  16.464  1.00 26.29  ? 311 LYS   C N     1 
ATOM   5904  C  CA    . LYS   B 1  311 ? 8.122   21.557  17.287  1.00 33.57  ? 311 LYS   C CA    1 
ATOM   5905  C  C     . LYS   B 1  311 ? 8.542   22.727  16.423  1.00 33.62  ? 311 LYS   C C     1 
ATOM   5906  O  O     . LYS   B 1  311 ? 9.435   22.597  15.583  1.00 38.53  ? 311 LYS   C O     1 
ATOM   5907  C  CB    . LYS   B 1  311 ? 9.078   21.386  18.491  1.00 27.73  ? 311 LYS   C CB    1 
ATOM   5908  C  CG    . LYS   B 1  311 ? 8.398   20.686  19.687  1.00 25.49  ? 311 LYS   C CG    1 
ATOM   5909  C  CD    . LYS   B 1  311 ? 9.378   20.308  20.758  1.00 34.52  ? 311 LYS   C CD    1 
ATOM   5910  C  CE    . LYS   B 1  311 ? 8.815   19.247  21.650  1.00 38.25  ? 311 LYS   C CE    1 
ATOM   5911  N  NZ    . LYS   B 1  311 ? 9.616   19.100  22.899  1.00 48.48  ? 311 LYS   C NZ    1 
ATOM   5912  N  N     . TYR   B 1  312 ? 7.866   23.857  16.630  1.00 32.19  ? 312 TYR   C N     1 
ATOM   5913  C  CA    . TYR   B 1  312 ? 8.218   25.111  15.988  1.00 28.17  ? 312 TYR   C CA    1 
ATOM   5914  C  C     . TYR   B 1  312 ? 9.394   25.764  16.697  1.00 34.22  ? 312 TYR   C C     1 
ATOM   5915  O  O     . TYR   B 1  312 ? 9.400   25.908  17.924  1.00 27.27  ? 312 TYR   C O     1 
ATOM   5916  C  CB    . TYR   B 1  312 ? 7.033   26.068  16.004  1.00 27.75  ? 312 TYR   C CB    1 
ATOM   5917  C  CG    . TYR   B 1  312 ? 5.927   25.645  15.112  1.00 27.44  ? 312 TYR   C CG    1 
ATOM   5918  C  CD1   . TYR   B 1  312 ? 5.880   26.067  13.776  1.00 28.93  ? 312 TYR   C CD1   1 
ATOM   5919  C  CD2   . TYR   B 1  312 ? 4.915   24.814  15.590  1.00 31.04  ? 312 TYR   C CD2   1 
ATOM   5920  C  CE1   . TYR   B 1  312 ? 4.832   25.672  12.944  1.00 31.40  ? 312 TYR   C CE1   1 
ATOM   5921  C  CE2   . TYR   B 1  312 ? 3.875   24.410  14.771  1.00 35.07  ? 312 TYR   C CE2   1 
ATOM   5922  C  CZ    . TYR   B 1  312 ? 3.833   24.839  13.455  1.00 34.66  ? 312 TYR   C CZ    1 
ATOM   5923  O  OH    . TYR   B 1  312 ? 2.796   24.424  12.665  1.00 34.74  ? 312 TYR   C OH    1 
ATOM   5924  N  N     . MET   B 1  313 ? 10.384  26.168  15.918  1.00 29.26  ? 313 MET   C N     1 
ATOM   5925  C  CA    . MET   B 1  313 ? 11.376  27.094  16.407  1.00 26.78  ? 313 MET   C CA    1 
ATOM   5926  C  C     . MET   B 1  313 ? 11.067  28.512  15.985  1.00 28.63  ? 313 MET   C C     1 
ATOM   5927  O  O     . MET   B 1  313 ? 11.794  29.431  16.365  1.00 28.39  ? 313 MET   C O     1 
ATOM   5928  C  CB    . MET   B 1  313 ? 12.760  26.691  15.920  1.00 25.28  ? 313 MET   C CB    1 
ATOM   5929  C  CG    . MET   B 1  313 ? 13.260  25.447  16.540  1.00 21.54  ? 313 MET   C CG    1 
ATOM   5930  S  SD    . MET   B 1  313 ? 13.885  24.397  15.256  1.00 40.36  ? 313 MET   C SD    1 
ATOM   5931  C  CE    . MET   B 1  313 ? 15.546  24.265  15.841  1.00 30.32  ? 313 MET   C CE    1 
ATOM   5932  N  N     . ALA   B 1  314 ? 10.006  28.711  15.209  1.00 27.94  ? 314 ALA   C N     1 
ATOM   5933  C  CA    . ALA   B 1  314 ? 9.714   30.032  14.663  1.00 26.42  ? 314 ALA   C CA    1 
ATOM   5934  C  C     . ALA   B 1  314 ? 8.541   29.957  13.702  1.00 26.24  ? 314 ALA   C C     1 
ATOM   5935  O  O     . ALA   B 1  314 ? 8.260   28.913  13.109  1.00 25.30  ? 314 ALA   C O     1 
ATOM   5936  C  CB    . ALA   B 1  314 ? 10.934  30.628  13.958  1.00 21.57  ? 314 ALA   C CB    1 
ATOM   5937  N  N     . CYS   B 1  315 ? 7.851   31.079  13.548  1.00 34.09  ? 315 CYS   C N     1 
ATOM   5938  C  CA    . CYS   B 1  315 ? 6.602   31.106  12.804  1.00 23.28  ? 315 CYS   C CA    1 
ATOM   5939  C  C     . CYS   B 1  315 ? 6.405   32.532  12.320  1.00 20.93  ? 315 CYS   C C     1 
ATOM   5940  O  O     . CYS   B 1  315 ? 6.122   33.420  13.126  1.00 22.94  ? 315 CYS   C O     1 
ATOM   5941  C  CB    . CYS   B 1  315 ? 5.467   30.652  13.693  1.00 26.56  ? 315 CYS   C CB    1 
ATOM   5942  S  SG    . CYS   B 1  315 ? 4.170   29.936  12.811  1.00 45.54  ? 315 CYS   C SG    1 
ATOM   5943  N  N     . CYS   B 1  316 ? 6.587   32.747  11.021  1.00 17.91  ? 316 CYS   C N     1 
ATOM   5944  C  CA    . CYS   B 1  316 ? 6.544   34.074  10.421  1.00 27.10  ? 316 CYS   C CA    1 
ATOM   5945  C  C     . CYS   B 1  316 ? 5.410   34.145  9.419   1.00 26.20  ? 316 CYS   C C     1 
ATOM   5946  O  O     . CYS   B 1  316 ? 5.275   33.276  8.558   1.00 31.89  ? 316 CYS   C O     1 
ATOM   5947  C  CB    . CYS   B 1  316 ? 7.877   34.433  9.739   1.00 23.22  ? 316 CYS   C CB    1 
ATOM   5948  S  SG    . CYS   B 1  316 ? 9.274   34.195  10.848  1.00 30.48  ? 316 CYS   C SG    1 
ATOM   5949  N  N     . LEU   B 1  317 ? 4.613   35.187  9.522   1.00 27.54  ? 317 LEU   C N     1 
ATOM   5950  C  CA    . LEU   B 1  317 ? 3.477   35.391  8.648   1.00 25.66  ? 317 LEU   C CA    1 
ATOM   5951  C  C     . LEU   B 1  317 ? 3.739   36.651  7.847   1.00 27.92  ? 317 LEU   C C     1 
ATOM   5952  O  O     . LEU   B 1  317 ? 4.058   37.697  8.415   1.00 32.37  ? 317 LEU   C O     1 
ATOM   5953  C  CB    . LEU   B 1  317 ? 2.172   35.489  9.456   1.00 25.10  ? 317 LEU   C CB    1 
ATOM   5954  C  CG    . LEU   B 1  317 ? 1.779   34.212  10.205  1.00 24.01  ? 317 LEU   C CG    1 
ATOM   5955  C  CD1   . LEU   B 1  317 ? 1.036   34.514  11.488  1.00 31.29  ? 317 LEU   C CD1   1 
ATOM   5956  C  CD2   . LEU   B 1  317 ? 0.910   33.363  9.324   1.00 35.68  ? 317 LEU   C CD2   1 
ATOM   5957  N  N     . LEU   B 1  318 ? 3.636   36.539  6.530   1.00 33.54  ? 318 LEU   C N     1 
ATOM   5958  C  CA    . LEU   B 1  318 ? 3.853   37.650  5.615   1.00 28.23  ? 318 LEU   C CA    1 
ATOM   5959  C  C     . LEU   B 1  318 ? 2.523   37.893  4.903   1.00 37.07  ? 318 LEU   C C     1 
ATOM   5960  O  O     . LEU   B 1  318 ? 2.224   37.258  3.885   1.00 33.66  ? 318 LEU   C O     1 
ATOM   5961  C  CB    . LEU   B 1  318 ? 4.982   37.343  4.643   1.00 20.52  ? 318 LEU   C CB    1 
ATOM   5962  C  CG    . LEU   B 1  318 ? 6.398   37.211  5.189   1.00 24.72  ? 318 LEU   C CG    1 
ATOM   5963  C  CD1   . LEU   B 1  318 ? 6.469   36.201  6.333   1.00 33.67  ? 318 LEU   C CD1   1 
ATOM   5964  C  CD2   . LEU   B 1  318 ? 7.269   36.741  4.070   1.00 29.72  ? 318 LEU   C CD2   1 
ATOM   5965  N  N     . TYR   B 1  319 ? 1.720   38.805  5.456   1.00 25.44  ? 319 TYR   C N     1 
ATOM   5966  C  CA    . TYR   B 1  319 ? 0.426   39.118  4.874   1.00 25.04  ? 319 TYR   C CA    1 
ATOM   5967  C  C     . TYR   B 1  319 ? 0.588   40.043  3.689   1.00 32.14  ? 319 TYR   C C     1 
ATOM   5968  O  O     . TYR   B 1  319 ? 1.519   40.855  3.631   1.00 28.81  ? 319 TYR   C O     1 
ATOM   5969  C  CB    . TYR   B 1  319 ? -0.504  39.765  5.898   1.00 25.64  ? 319 TYR   C CB    1 
ATOM   5970  C  CG    . TYR   B 1  319 ? -0.944  38.815  6.991   1.00 27.89  ? 319 TYR   C CG    1 
ATOM   5971  C  CD1   . TYR   B 1  319 ? -2.021  37.961  6.805   1.00 24.60  ? 319 TYR   C CD1   1 
ATOM   5972  C  CD2   . TYR   B 1  319 ? -0.263  38.758  8.202   1.00 25.18  ? 319 TYR   C CD2   1 
ATOM   5973  C  CE1   . TYR   B 1  319 ? -2.419  37.092  7.805   1.00 25.53  ? 319 TYR   C CE1   1 
ATOM   5974  C  CE2   . TYR   B 1  319 ? -0.657  37.901  9.206   1.00 27.65  ? 319 TYR   C CE2   1 
ATOM   5975  C  CZ    . TYR   B 1  319 ? -1.728  37.065  9.000   1.00 25.19  ? 319 TYR   C CZ    1 
ATOM   5976  O  OH    . TYR   B 1  319 ? -2.107  36.208  9.993   1.00 24.96  ? 319 TYR   C OH    1 
ATOM   5977  N  N     . ARG   B 1  320 ? -0.356  39.930  2.747   1.00 37.61  ? 320 ARG   C N     1 
ATOM   5978  C  CA    . ARG   B 1  320 ? -0.315  40.717  1.520   1.00 36.22  ? 320 ARG   C CA    1 
ATOM   5979  C  C     . ARG   B 1  320 ? -1.699  41.227  1.141   1.00 34.64  ? 320 ARG   C C     1 
ATOM   5980  O  O     . ARG   B 1  320 ? -2.648  40.442  1.047   1.00 39.14  ? 320 ARG   C O     1 
ATOM   5981  C  CB    . ARG   B 1  320 ? 0.256   39.889  0.372   1.00 29.04  ? 320 ARG   C CB    1 
ATOM   5982  C  CG    . ARG   B 1  320 ? 0.604   40.730  -0.811  1.00 38.25  ? 320 ARG   C CG    1 
ATOM   5983  C  CD    . ARG   B 1  320 ? 1.769   40.143  -1.505  1.00 37.52  ? 320 ARG   C CD    1 
ATOM   5984  N  NE    . ARG   B 1  320 ? 2.271   41.049  -2.516  1.00 33.47  ? 320 ARG   C NE    1 
ATOM   5985  C  CZ    . ARG   B 1  320 ? 3.055   40.659  -3.506  1.00 50.85  ? 320 ARG   C CZ    1 
ATOM   5986  N  NH1   . ARG   B 1  320 ? 3.412   39.389  -3.643  1.00 40.66  ? 320 ARG   C NH1   1 
ATOM   5987  N  NH2   . ARG   B 1  320 ? 3.484   41.561  -4.386  1.00 55.16  ? 320 ARG   C NH2   1 
ATOM   5988  N  N     . GLY   B 1  321 ? -1.799  42.531  0.886   1.00 33.54  ? 321 GLY   C N     1 
ATOM   5989  C  CA    . GLY   B 1  321 ? -3.046  43.159  0.492   1.00 34.46  ? 321 GLY   C CA    1 
ATOM   5990  C  C     . GLY   B 1  321 ? -3.859  43.777  1.620   1.00 41.81  ? 321 GLY   C C     1 
ATOM   5991  O  O     . GLY   B 1  321 ? -3.294  44.373  2.542   1.00 41.03  ? 321 GLY   C O     1 
ATOM   5992  N  N     . ASP   B 1  322 ? -5.188  43.623  1.554   1.00 34.75  ? 322 ASP   C N     1 
ATOM   5993  C  CA    . ASP   B 1  322 ? -6.157  44.288  2.429   1.00 40.70  ? 322 ASP   C CA    1 
ATOM   5994  C  C     . ASP   B 1  322 ? -6.136  43.611  3.793   1.00 29.82  ? 322 ASP   C C     1 
ATOM   5995  O  O     . ASP   B 1  322 ? -6.932  42.727  4.082   1.00 30.32  ? 322 ASP   C O     1 
ATOM   5996  C  CB    . ASP   B 1  322 ? -7.553  44.246  1.802   1.00 45.36  ? 322 ASP   C CB    1 
ATOM   5997  C  CG    . ASP   B 1  322 ? -8.663  44.719  2.753   1.00 44.25  ? 322 ASP   C CG    1 
ATOM   5998  O  OD1   . ASP   B 1  322 ? -8.378  45.304  3.811   1.00 43.53  ? 322 ASP   C OD1   1 
ATOM   5999  O  OD2   . ASP   B 1  322 ? -9.848  44.494  2.438   1.00 61.96  ? 322 ASP   C OD2   1 
ATOM   6000  N  N     . VAL   B 1  323 ? -5.224  44.059  4.648   1.00 31.04  ? 323 VAL   C N     1 
ATOM   6001  C  CA    . VAL   B 1  323 ? -4.950  43.432  5.934   1.00 31.04  ? 323 VAL   C CA    1 
ATOM   6002  C  C     . VAL   B 1  323 ? -4.524  44.518  6.913   1.00 37.43  ? 323 VAL   C C     1 
ATOM   6003  O  O     . VAL   B 1  323 ? -3.582  45.270  6.643   1.00 43.66  ? 323 VAL   C O     1 
ATOM   6004  C  CB    . VAL   B 1  323 ? -3.851  42.357  5.819   1.00 31.38  ? 323 VAL   C CB    1 
ATOM   6005  C  CG1   . VAL   B 1  323 ? -3.567  41.747  7.191   1.00 40.25  ? 323 VAL   C CG1   1 
ATOM   6006  C  CG2   . VAL   B 1  323 ? -4.258  41.280  4.849   1.00 32.71  ? 323 VAL   C CG2   1 
ATOM   6007  N  N     . VAL   B 1  324 ? -5.207  44.600  8.049   1.00 31.03  ? 324 VAL   C N     1 
ATOM   6008  C  CA    . VAL   B 1  324 ? -4.854  45.584  9.068   1.00 27.39  ? 324 VAL   C CA    1 
ATOM   6009  C  C     . VAL   B 1  324 ? -4.531  44.901  10.392  1.00 27.82  ? 324 VAL   C C     1 
ATOM   6010  O  O     . VAL   B 1  324 ? -5.130  43.867  10.739  1.00 26.63  ? 324 VAL   C O     1 
ATOM   6011  C  CB    . VAL   B 1  324 ? -5.976  46.614  9.272   1.00 29.83  ? 324 VAL   C CB    1 
ATOM   6012  C  CG1   . VAL   B 1  324 ? -6.028  47.554  8.147   1.00 16.14  ? 324 VAL   C CG1   1 
ATOM   6013  C  CG2   . VAL   B 1  324 ? -7.296  45.910  9.444   1.00 26.34  ? 324 VAL   C CG2   1 
ATOM   6014  N  N     . PRO   B 1  325 ? -3.633  45.474  11.167  1.00 23.82  ? 325 PRO   C N     1 
ATOM   6015  C  CA    . PRO   B 1  325 ? -3.205  44.853  12.428  1.00 25.99  ? 325 PRO   C CA    1 
ATOM   6016  C  C     . PRO   B 1  325 ? -4.306  44.180  13.240  1.00 29.14  ? 325 PRO   C C     1 
ATOM   6017  O  O     . PRO   B 1  325 ? -4.134  43.025  13.640  1.00 32.42  ? 325 PRO   C O     1 
ATOM   6018  C  CB    . PRO   B 1  325 ? -2.584  46.035  13.176  1.00 27.57  ? 325 PRO   C CB    1 
ATOM   6019  C  CG    . PRO   B 1  325 ? -1.908  46.826  12.048  1.00 31.24  ? 325 PRO   C CG    1 
ATOM   6020  C  CD    . PRO   B 1  325 ? -2.811  46.645  10.813  1.00 29.38  ? 325 PRO   C CD    1 
ATOM   6021  N  N     . LYS   B 1  326 ? -5.437  44.851  13.478  1.00 33.16  ? 326 LYS   C N     1 
ATOM   6022  C  CA    . LYS   B 1  326 ? -6.474  44.262  14.328  1.00 31.71  ? 326 LYS   C CA    1 
ATOM   6023  C  C     . LYS   B 1  326 ? -6.874  42.865  13.856  1.00 34.35  ? 326 LYS   C C     1 
ATOM   6024  O  O     . LYS   B 1  326 ? -6.901  41.919  14.652  1.00 42.50  ? 326 LYS   C O     1 
ATOM   6025  C  CB    . LYS   B 1  326 ? -7.695  45.174  14.384  1.00 38.15  ? 326 LYS   C CB    1 
ATOM   6026  C  CG    . LYS   B 1  326 ? -7.847  45.929  15.685  1.00 39.41  ? 326 LYS   C CG    1 
ATOM   6027  C  CD    . LYS   B 1  326 ? -9.270  46.455  15.821  1.00 60.23  ? 326 LYS   C CD    1 
ATOM   6028  C  CE    . LYS   B 1  326 ? -10.280 45.379  15.403  1.00 56.23  ? 326 LYS   C CE    1 
ATOM   6029  N  NZ    . LYS   B 1  326 ? -11.675 45.680  15.827  1.00 49.60  ? 326 LYS   C NZ    1 
ATOM   6030  N  N     . ASP   B 1  327 ? -7.185  42.708  12.563  1.00 35.69  ? 327 ASP   C N     1 
ATOM   6031  C  CA    . ASP   B 1  327 ? -7.488  41.381  12.022  1.00 30.97  ? 327 ASP   C CA    1 
ATOM   6032  C  C     . ASP   B 1  327 ? -6.420  40.355  12.408  1.00 38.88  ? 327 ASP   C C     1 
ATOM   6033  O  O     . ASP   B 1  327 ? -6.715  39.344  13.058  1.00 33.20  ? 327 ASP   C O     1 
ATOM   6034  C  CB    . ASP   B 1  327 ? -7.611  41.439  10.501  1.00 44.30  ? 327 ASP   C CB    1 
ATOM   6035  C  CG    . ASP   B 1  327 ? -8.507  42.577  10.015  1.00 51.37  ? 327 ASP   C CG    1 
ATOM   6036  O  OD1   . ASP   B 1  327 ? -9.498  42.896  10.716  1.00 39.38  ? 327 ASP   C OD1   1 
ATOM   6037  O  OD2   . ASP   B 1  327 ? -8.206  43.129  8.916   1.00 45.01  ? 327 ASP   C OD2   1 
ATOM   6038  N  N     . VAL   B 1  328 ? -5.166  40.604  11.998  1.00 34.28  ? 328 VAL   C N     1 
ATOM   6039  C  CA    . VAL   B 1  328 ? -4.069  39.670  12.258  1.00 21.97  ? 328 VAL   C CA    1 
ATOM   6040  C  C     . VAL   B 1  328 ? -4.061  39.247  13.722  1.00 30.29  ? 328 VAL   C C     1 
ATOM   6041  O  O     . VAL   B 1  328 ? -4.045  38.049  14.050  1.00 23.83  ? 328 VAL   C O     1 
ATOM   6042  C  CB    . VAL   B 1  328 ? -2.724  40.300  11.844  1.00 28.65  ? 328 VAL   C CB    1 
ATOM   6043  C  CG1   . VAL   B 1  328 ? -1.582  39.352  12.101  1.00 25.67  ? 328 VAL   C CG1   1 
ATOM   6044  C  CG2   . VAL   B 1  328 ? -2.732  40.709  10.371  1.00 30.44  ? 328 VAL   C CG2   1 
ATOM   6045  N  N     . ASN   B 1  329 ? -4.069  40.226  14.630  1.00 26.62  ? 329 ASN   C N     1 
ATOM   6046  C  CA    . ASN   B 1  329 ? -4.073  39.896  16.052  1.00 26.51  ? 329 ASN   C CA    1 
ATOM   6047  C  C     . ASN   B 1  329 ? -5.181  38.902  16.378  1.00 28.14  ? 329 ASN   C C     1 
ATOM   6048  O  O     . ASN   B 1  329 ? -4.924  37.834  16.948  1.00 29.81  ? 329 ASN   C O     1 
ATOM   6049  C  CB    . ASN   B 1  329 ? -4.214  41.159  16.904  1.00 24.29  ? 329 ASN   C CB    1 
ATOM   6050  C  CG    . ASN   B 1  329 ? -3.001  42.073  16.811  1.00 23.14  ? 329 ASN   C CG    1 
ATOM   6051  O  OD1   . ASN   B 1  329 ? -2.408  42.213  15.762  1.00 34.24  ? 329 ASN   C OD1   1 
ATOM   6052  N  ND2   . ASN   B 1  329 ? -2.631  42.686  17.911  1.00 29.74  ? 329 ASN   C ND2   1 
ATOM   6053  N  N     . ALA   B 1  330 ? -6.426  39.233  16.017  1.00 25.62  ? 330 ALA   C N     1 
ATOM   6054  C  CA    . ALA   B 1  330 ? -7.545  38.313  16.257  1.00 27.69  ? 330 ALA   C CA    1 
ATOM   6055  C  C     . ALA   B 1  330 ? -7.274  36.913  15.712  1.00 24.86  ? 330 ALA   C C     1 
ATOM   6056  O  O     . ALA   B 1  330 ? -7.518  35.918  16.402  1.00 36.24  ? 330 ALA   C O     1 
ATOM   6057  C  CB    . ALA   B 1  330 ? -8.821  38.880  15.644  1.00 23.55  ? 330 ALA   C CB    1 
ATOM   6058  N  N     . ALA   B 1  331 ? -6.728  36.821  14.492  1.00 25.05  ? 331 ALA   C N     1 
ATOM   6059  C  CA    . ALA   B 1  331 ? -6.517  35.533  13.829  1.00 25.68  ? 331 ALA   C CA    1 
ATOM   6060  C  C     . ALA   B 1  331 ? -5.445  34.691  14.524  1.00 30.93  ? 331 ALA   C C     1 
ATOM   6061  O  O     . ALA   B 1  331 ? -5.593  33.467  14.633  1.00 29.91  ? 331 ALA   C O     1 
ATOM   6062  C  CB    . ALA   B 1  331 ? -6.162  35.760  12.355  1.00 19.52  ? 331 ALA   C CB    1 
ATOM   6063  N  N     . ILE   B 1  332 ? -4.349  35.317  14.978  1.00 31.17  ? 332 ILE   C N     1 
ATOM   6064  C  CA    . ILE   B 1  332 ? -3.332  34.570  15.718  1.00 28.36  ? 332 ILE   C CA    1 
ATOM   6065  C  C     . ILE   B 1  332 ? -3.873  34.134  17.077  1.00 34.94  ? 332 ILE   C C     1 
ATOM   6066  O  O     . ILE   B 1  332 ? -3.563  33.034  17.563  1.00 35.66  ? 332 ILE   C O     1 
ATOM   6067  C  CB    . ILE   B 1  332 ? -2.042  35.395  15.858  1.00 26.47  ? 332 ILE   C CB    1 
ATOM   6068  C  CG1   . ILE   B 1  332 ? -1.464  35.717  14.476  1.00 33.59  ? 332 ILE   C CG1   1 
ATOM   6069  C  CG2   . ILE   B 1  332 ? -1.023  34.641  16.700  1.00 26.49  ? 332 ILE   C CG2   1 
ATOM   6070  C  CD1   . ILE   B 1  332 ? -0.306  36.688  14.517  1.00 16.98  ? 332 ILE   C CD1   1 
ATOM   6071  N  N     . ALA   B 1  333 ? -4.693  34.981  17.707  1.00 28.52  ? 333 ALA   C N     1 
ATOM   6072  C  CA    . ALA   B 1  333 ? -5.329  34.628  18.977  1.00 38.99  ? 333 ALA   C CA    1 
ATOM   6073  C  C     . ALA   B 1  333 ? -6.074  33.301  18.884  1.00 41.88  ? 333 ALA   C C     1 
ATOM   6074  O  O     . ALA   B 1  333 ? -5.952  32.443  19.767  1.00 38.79  ? 333 ALA   C O     1 
ATOM   6075  C  CB    . ALA   B 1  333 ? -6.285  35.746  19.407  1.00 37.12  ? 333 ALA   C CB    1 
ATOM   6076  N  N     . THR   B 1  334 ? -6.867  33.122  17.821  1.00 41.85  ? 334 THR   C N     1 
ATOM   6077  C  CA    . THR   B 1  334 ? -7.554  31.851  17.607  1.00 43.30  ? 334 THR   C CA    1 
ATOM   6078  C  C     . THR   B 1  334 ? -6.561  30.708  17.502  1.00 45.69  ? 334 THR   C C     1 
ATOM   6079  O  O     . THR   B 1  334 ? -6.657  29.715  18.234  1.00 56.97  ? 334 THR   C O     1 
ATOM   6080  C  CB    . THR   B 1  334 ? -8.403  31.891  16.338  1.00 49.60  ? 334 THR   C CB    1 
ATOM   6081  O  OG1   . THR   B 1  334 ? -9.294  33.016  16.370  1.00 39.93  ? 334 THR   C OG1   1 
ATOM   6082  C  CG2   . THR   B 1  334 ? -9.201  30.607  16.240  1.00 40.88  ? 334 THR   C CG2   1 
ATOM   6083  N  N     . ILE   B 1  335 ? -5.609  30.824  16.569  1.00 41.31  ? 335 ILE   C N     1 
ATOM   6084  C  CA    . ILE   B 1  335 ? -4.643  29.750  16.353  1.00 41.43  ? 335 ILE   C CA    1 
ATOM   6085  C  C     . ILE   B 1  335 ? -4.048  29.317  17.679  1.00 41.39  ? 335 ILE   C C     1 
ATOM   6086  O  O     . ILE   B 1  335 ? -3.956  28.122  17.976  1.00 49.84  ? 335 ILE   C O     1 
ATOM   6087  C  CB    . ILE   B 1  335 ? -3.546  30.188  15.360  1.00 46.40  ? 335 ILE   C CB    1 
ATOM   6088  C  CG1   . ILE   B 1  335 ? -4.147  30.780  14.084  1.00 41.32  ? 335 ILE   C CG1   1 
ATOM   6089  C  CG2   . ILE   B 1  335 ? -2.712  28.999  14.939  1.00 48.36  ? 335 ILE   C CG2   1 
ATOM   6090  C  CD1   . ILE   B 1  335 ? -4.762  29.730  13.160  1.00 37.24  ? 335 ILE   C CD1   1 
ATOM   6091  N  N     . LYS   B 1  336 ? -3.672  30.285  18.514  1.00 48.03  ? 336 LYS   C N     1 
ATOM   6092  C  CA    . LYS   B 1  336 ? -2.931  29.959  19.730  1.00 56.42  ? 336 LYS   C CA    1 
ATOM   6093  C  C     . LYS   B 1  336 ? -3.774  29.139  20.697  1.00 57.87  ? 336 LYS   C C     1 
ATOM   6094  O  O     . LYS   B 1  336 ? -3.279  28.170  21.284  1.00 54.45  ? 336 LYS   C O     1 
ATOM   6095  C  CB    . LYS   B 1  336 ? -2.402  31.239  20.388  1.00 44.50  ? 336 LYS   C CB    1 
ATOM   6096  C  CG    . LYS   B 1  336 ? -1.095  31.744  19.743  1.00 39.20  ? 336 LYS   C CG    1 
ATOM   6097  C  CD    . LYS   B 1  336 ? -0.666  33.110  20.224  1.00 43.03  ? 336 LYS   C CD    1 
ATOM   6098  C  CE    . LYS   B 1  336 ? 0.065   33.072  21.562  1.00 41.84  ? 336 LYS   C CE    1 
ATOM   6099  N  NZ    . LYS   B 1  336 ? 0.724   34.409  21.871  1.00 43.41  ? 336 LYS   C NZ    1 
ATOM   6100  N  N     . THR   B 1  337 ? -5.054  29.483  20.852  1.00 53.56  ? 337 THR   C N     1 
ATOM   6101  C  CA    . THR   B 1  337 ? -5.913  28.709  21.743  1.00 59.59  ? 337 THR   C CA    1 
ATOM   6102  C  C     . THR   B 1  337 ? -6.318  27.370  21.123  1.00 62.42  ? 337 THR   C C     1 
ATOM   6103  O  O     . THR   B 1  337 ? -6.035  26.302  21.675  1.00 67.71  ? 337 THR   C O     1 
ATOM   6104  C  CB    . THR   B 1  337 ? -7.159  29.517  22.106  1.00 57.79  ? 337 THR   C CB    1 
ATOM   6105  O  OG1   . THR   B 1  337 ? -8.155  29.329  21.095  1.00 53.46  ? 337 THR   C OG1   1 
ATOM   6106  C  CG2   . THR   B 1  337 ? -6.819  30.993  22.201  1.00 55.25  ? 337 THR   C CG2   1 
ATOM   6107  N  N     . LYS   B 1  338 ? -6.977  27.403  19.971  1.00 53.22  ? 338 LYS   C N     1 
ATOM   6108  C  CA    . LYS   B 1  338 ? -7.631  26.215  19.428  1.00 57.46  ? 338 LYS   C CA    1 
ATOM   6109  C  C     . LYS   B 1  338 ? -6.800  25.516  18.357  1.00 67.63  ? 338 LYS   C C     1 
ATOM   6110  O  O     . LYS   B 1  338 ? -7.346  25.009  17.369  1.00 73.33  ? 338 LYS   C O     1 
ATOM   6111  C  CB    . LYS   B 1  338 ? -9.002  26.594  18.882  1.00 62.52  ? 338 LYS   C CB    1 
ATOM   6112  C  CG    . LYS   B 1  338 ? -9.884  27.275  19.921  1.00 69.31  ? 338 LYS   C CG    1 
ATOM   6113  C  CD    . LYS   B 1  338 ? -11.174 27.764  19.304  1.00 61.41  ? 338 LYS   C CD    1 
ATOM   6114  C  CE    . LYS   B 1  338 ? -10.936 28.192  17.867  1.00 59.44  ? 338 LYS   C CE    1 
ATOM   6115  N  NZ    . LYS   B 1  338 ? -12.096 28.967  17.332  1.00 56.66  ? 338 LYS   C NZ    1 
ATOM   6116  N  N     . ARG   B 1  339 ? -5.481  25.453  18.515  1.00 64.70  ? 339 ARG   C N     1 
ATOM   6117  C  CA    . ARG   B 1  339 ? -4.659  24.749  17.544  1.00 65.35  ? 339 ARG   C CA    1 
ATOM   6118  C  C     . ARG   B 1  339 ? -3.391  24.261  18.224  1.00 71.57  ? 339 ARG   C C     1 
ATOM   6119  O  O     . ARG   B 1  339 ? -2.915  24.864  19.195  1.00 66.83  ? 339 ARG   C O     1 
ATOM   6120  C  CB    . ARG   B 1  339 ? -4.316  25.625  16.334  1.00 68.29  ? 339 ARG   C CB    1 
ATOM   6121  C  CG    . ARG   B 1  339 ? -3.661  24.855  15.197  1.00 70.85  ? 339 ARG   C CG    1 
ATOM   6122  C  CD    . ARG   B 1  339 ? -3.709  25.622  13.874  1.00 71.16  ? 339 ARG   C CD    1 
ATOM   6123  N  NE    . ARG   B 1  339 ? -5.015  25.618  13.210  1.00 74.29  ? 339 ARG   C NE    1 
ATOM   6124  C  CZ    . ARG   B 1  339 ? -5.396  24.734  12.293  1.00 73.25  ? 339 ARG   C CZ    1 
ATOM   6125  N  NH1   . ARG   B 1  339 ? -4.642  23.691  11.980  1.00 62.83  ? 339 ARG   C NH1   1 
ATOM   6126  N  NH2   . ARG   B 1  339 ? -6.560  24.906  11.667  1.00 70.58  ? 339 ARG   C NH2   1 
ATOM   6127  N  N     . SER   B 1  340 ? -2.858  23.149  17.707  1.00 73.69  ? 340 SER   C N     1 
ATOM   6128  C  CA    . SER   B 1  340 ? -1.707  22.473  18.309  1.00 84.62  ? 340 SER   C CA    1 
ATOM   6129  C  C     . SER   B 1  340 ? -0.439  23.107  17.756  1.00 68.88  ? 340 SER   C C     1 
ATOM   6130  O  O     . SER   B 1  340 ? 0.028   22.764  16.667  1.00 67.94  ? 340 SER   C O     1 
ATOM   6131  C  CB    . SER   B 1  340 ? -1.751  20.963  18.063  1.00 81.42  ? 340 SER   C CB    1 
ATOM   6132  O  OG    . SER   B 1  340 ? -1.905  20.621  16.694  1.00 57.82  ? 340 SER   C OG    1 
ATOM   6133  N  N     . ILE   B 1  341 ? 0.117   24.046  18.513  1.00 63.31  ? 341 ILE   C N     1 
ATOM   6134  C  CA    . ILE   B 1  341 ? 1.341   24.750  18.136  1.00 56.59  ? 341 ILE   C CA    1 
ATOM   6135  C  C     . ILE   B 1  341 ? 2.218   24.716  19.384  1.00 53.27  ? 341 ILE   C C     1 
ATOM   6136  O  O     . ILE   B 1  341 ? 2.074   25.547  20.285  1.00 62.96  ? 341 ILE   C O     1 
ATOM   6137  C  CB    . ILE   B 1  341 ? 1.078   26.185  17.672  1.00 53.67  ? 341 ILE   C CB    1 
ATOM   6138  C  CG1   . ILE   B 1  341 ? -0.068  26.216  16.677  1.00 53.46  ? 341 ILE   C CG1   1 
ATOM   6139  C  CG2   . ILE   B 1  341 ? 2.305   26.821  17.018  1.00 44.68  ? 341 ILE   C CG2   1 
ATOM   6140  C  CD1   . ILE   B 1  341 ? -0.251  27.576  16.079  1.00 52.46  ? 341 ILE   C CD1   1 
ATOM   6141  N  N     . GLN   B 1  342 ? 3.104   23.724  19.471  1.00 49.05  ? 342 GLN   C N     1 
ATOM   6142  C  CA    . GLN   B 1  342 ? 4.104   23.650  20.530  1.00 47.70  ? 342 GLN   C CA    1 
ATOM   6143  C  C     . GLN   B 1  342 ? 5.408   24.255  20.018  1.00 45.55  ? 342 GLN   C C     1 
ATOM   6144  O  O     . GLN   B 1  342 ? 5.959   23.788  19.014  1.00 40.43  ? 342 GLN   C O     1 
ATOM   6145  C  CB    . GLN   B 1  342 ? 4.323   22.202  20.981  1.00 59.82  ? 342 GLN   C CB    1 
ATOM   6146  C  CG    . GLN   B 1  342 ? 5.148   22.056  22.285  1.00 68.28  ? 342 GLN   C CG    1 
ATOM   6147  C  CD    . GLN   B 1  342 ? 5.621   20.612  22.571  1.00 75.15  ? 342 GLN   C CD    1 
ATOM   6148  O  OE1   . GLN   B 1  342 ? 5.488   19.714  21.729  1.00 59.37  ? 342 GLN   C OE1   1 
ATOM   6149  N  NE2   . GLN   B 1  342 ? 6.178   20.397  23.767  1.00 76.98  ? 342 GLN   C NE2   1 
ATOM   6150  N  N     . PHE   B 1  343 ? 5.892   25.299  20.694  1.00 45.40  ? 343 PHE   C N     1 
ATOM   6151  C  CA    . PHE   B 1  343 ? 7.203   25.871  20.401  1.00 30.44  ? 343 PHE   C CA    1 
ATOM   6152  C  C     . PHE   B 1  343 ? 8.272   25.189  21.249  1.00 32.05  ? 343 PHE   C C     1 
ATOM   6153  O  O     . PHE   B 1  343 ? 8.008   24.728  22.367  1.00 35.18  ? 343 PHE   C O     1 
ATOM   6154  C  CB    . PHE   B 1  343 ? 7.217   27.382  20.662  1.00 31.20  ? 343 PHE   C CB    1 
ATOM   6155  C  CG    . PHE   B 1  343 ? 6.612   28.221  19.549  1.00 34.62  ? 343 PHE   C CG    1 
ATOM   6156  C  CD1   . PHE   B 1  343 ? 5.251   28.460  19.500  1.00 31.00  ? 343 PHE   C CD1   1 
ATOM   6157  C  CD2   . PHE   B 1  343 ? 7.420   28.781  18.560  1.00 36.33  ? 343 PHE   C CD2   1 
ATOM   6158  C  CE1   . PHE   B 1  343 ? 4.701   29.225  18.495  1.00 34.15  ? 343 PHE   C CE1   1 
ATOM   6159  C  CE2   . PHE   B 1  343 ? 6.882   29.556  17.557  1.00 29.28  ? 343 PHE   C CE2   1 
ATOM   6160  C  CZ    . PHE   B 1  343 ? 5.520   29.778  17.520  1.00 38.34  ? 343 PHE   C CZ    1 
ATOM   6161  N  N     . VAL   B 1  344 ? 9.484   25.092  20.697  1.00 27.78  ? 344 VAL   C N     1 
ATOM   6162  C  CA    . VAL   B 1  344 ? 10.567  24.547  21.503  1.00 24.86  ? 344 VAL   C CA    1 
ATOM   6163  C  C     . VAL   B 1  344 ? 10.743  25.432  22.733  1.00 28.53  ? 344 VAL   C C     1 
ATOM   6164  O  O     . VAL   B 1  344 ? 10.373  26.612  22.741  1.00 33.14  ? 344 VAL   C O     1 
ATOM   6165  C  CB    . VAL   B 1  344 ? 11.882  24.412  20.717  1.00 27.11  ? 344 VAL   C CB    1 
ATOM   6166  C  CG1   . VAL   B 1  344 ? 11.729  23.419  19.589  1.00 30.31  ? 344 VAL   C CG1   1 
ATOM   6167  C  CG2   . VAL   B 1  344 ? 12.378  25.752  20.200  1.00 30.60  ? 344 VAL   C CG2   1 
ATOM   6168  N  N     . ASP   B 1  345 ? 11.296  24.847  23.799  1.00 31.98  ? 345 ASP   C N     1 
ATOM   6169  C  CA    . ASP   B 1  345 ? 11.333  25.588  25.062  1.00 32.50  ? 345 ASP   C CA    1 
ATOM   6170  C  C     . ASP   B 1  345 ? 12.375  26.691  25.059  1.00 35.25  ? 345 ASP   C C     1 
ATOM   6171  O  O     . ASP   B 1  345 ? 12.396  27.499  25.994  1.00 51.01  ? 345 ASP   C O     1 
ATOM   6172  C  CB    . ASP   B 1  345 ? 11.576  24.654  26.263  1.00 27.52  ? 345 ASP   C CB    1 
ATOM   6173  C  CG    . ASP   B 1  345 ? 12.984  24.050  26.280  1.00 43.95  ? 345 ASP   C CG    1 
ATOM   6174  O  OD1   . ASP   B 1  345 ? 13.850  24.527  25.514  1.00 44.54  ? 345 ASP   C OD1   1 
ATOM   6175  O  OD2   . ASP   B 1  345 ? 13.228  23.089  27.055  1.00 38.69  ? 345 ASP   C OD2   1 
ATOM   6176  N  N     . TRP   B 1  346 ? 13.237  26.742  24.050  1.00 31.81  ? 346 TRP   C N     1 
ATOM   6177  C  CA    . TRP   B 1  346 ? 14.254  27.774  23.952  1.00 32.35  ? 346 TRP   C CA    1 
ATOM   6178  C  C     . TRP   B 1  346 ? 13.881  28.869  22.957  1.00 30.15  ? 346 TRP   C C     1 
ATOM   6179  O  O     . TRP   B 1  346 ? 14.718  29.706  22.615  1.00 29.57  ? 346 TRP   C O     1 
ATOM   6180  C  CB    . TRP   B 1  346 ? 15.608  27.143  23.592  1.00 33.70  ? 346 TRP   C CB    1 
ATOM   6181  C  CG    . TRP   B 1  346 ? 15.611  26.231  22.369  1.00 37.99  ? 346 TRP   C CG    1 
ATOM   6182  C  CD1   . TRP   B 1  346 ? 15.573  24.855  22.363  1.00 32.00  ? 346 TRP   C CD1   1 
ATOM   6183  C  CD2   . TRP   B 1  346 ? 15.694  26.636  20.983  1.00 31.16  ? 346 TRP   C CD2   1 
ATOM   6184  N  NE1   . TRP   B 1  346 ? 15.618  24.390  21.063  1.00 32.36  ? 346 TRP   C NE1   1 
ATOM   6185  C  CE2   . TRP   B 1  346 ? 15.686  25.461  20.202  1.00 32.02  ? 346 TRP   C CE2   1 
ATOM   6186  C  CE3   . TRP   B 1  346 ? 15.775  27.875  20.336  1.00 28.84  ? 346 TRP   C CE3   1 
ATOM   6187  C  CZ2   . TRP   B 1  346 ? 15.755  25.492  18.807  1.00 29.85  ? 346 TRP   C CZ2   1 
ATOM   6188  C  CZ3   . TRP   B 1  346 ? 15.834  27.906  18.941  1.00 30.54  ? 346 TRP   C CZ3   1 
ATOM   6189  C  CH2   . TRP   B 1  346 ? 15.831  26.719  18.197  1.00 33.82  ? 346 TRP   C CH2   1 
ATOM   6190  N  N     . CYS   B 1  347 ? 12.649  28.896  22.479  1.00 24.91  ? 347 CYS   C N     1 
ATOM   6191  C  CA    . CYS   B 1  347 ? 12.219  29.981  21.609  1.00 41.09  ? 347 CYS   C CA    1 
ATOM   6192  C  C     . CYS   B 1  347 ? 10.917  30.562  22.136  1.00 39.81  ? 347 CYS   C C     1 
ATOM   6193  O  O     . CYS   B 1  347 ? 9.832   30.036  21.869  1.00 46.30  ? 347 CYS   C O     1 
ATOM   6194  C  CB    . CYS   B 1  347 ? 12.078  29.520  20.161  1.00 41.08  ? 347 CYS   C CB    1 
ATOM   6195  S  SG    . CYS   B 1  347 ? 11.425  30.824  19.135  1.00 50.92  ? 347 CYS   C SG    1 
ATOM   6196  N  N     . PRO   B 1  348 ? 10.990  31.602  22.923  1.00 54.23  ? 348 PRO   C N     1 
ATOM   6197  C  CA    . PRO   B 1  348 ? 9.816   32.467  23.092  1.00 72.28  ? 348 PRO   C CA    1 
ATOM   6198  C  C     . PRO   B 1  348 ? 9.897   33.672  22.154  1.00 66.96  ? 348 PRO   C C     1 
ATOM   6199  O  O     . PRO   B 1  348 ? 10.988  34.042  21.694  1.00 55.99  ? 348 PRO   C O     1 
ATOM   6200  C  CB    . PRO   B 1  348 ? 9.873   32.853  24.578  1.00 82.79  ? 348 PRO   C CB    1 
ATOM   6201  C  CG    . PRO   B 1  348 ? 11.352  32.781  24.939  1.00 71.09  ? 348 PRO   C CG    1 
ATOM   6202  C  CD    . PRO   B 1  348 ? 12.022  31.837  23.953  1.00 60.25  ? 348 PRO   C CD    1 
ATOM   6203  N  N     . THR   B 1  349 ? 8.743   34.303  21.910  1.00 66.67  ? 349 THR   C N     1 
ATOM   6204  C  CA    . THR   B 1  349 ? 8.425   35.139  20.746  1.00 64.61  ? 349 THR   C CA    1 
ATOM   6205  C  C     . THR   B 1  349 ? 7.738   34.252  19.720  1.00 64.12  ? 349 THR   C C     1 
ATOM   6206  O  O     . THR   B 1  349 ? 6.517   34.341  19.537  1.00 73.32  ? 349 THR   C O     1 
ATOM   6207  C  CB    . THR   B 1  349 ? 9.635   35.844  20.097  1.00 60.73  ? 349 THR   C CB    1 
ATOM   6208  O  OG1   . THR   B 1  349 ? 10.628  34.889  19.690  1.00 60.69  ? 349 THR   C OG1   1 
ATOM   6209  C  CG2   . THR   B 1  349 ? 10.228  36.913  21.019  1.00 45.45  ? 349 THR   C CG2   1 
ATOM   6210  N  N     . GLY   B 1  350 ? 8.498   33.382  19.059  1.00 44.99  ? 350 GLY   C N     1 
ATOM   6211  C  CA    . GLY   B 1  350 ? 7.877   32.480  18.111  1.00 53.25  ? 350 GLY   C CA    1 
ATOM   6212  C  C     . GLY   B 1  350 ? 7.217   33.164  16.929  1.00 41.53  ? 350 GLY   C C     1 
ATOM   6213  O  O     . GLY   B 1  350 ? 7.726   33.053  15.807  1.00 43.51  ? 350 GLY   C O     1 
ATOM   6214  N  N     . PHE   B 1  351 ? 6.103   33.873  17.156  1.00 35.12  ? 351 PHE   C N     1 
ATOM   6215  C  CA    . PHE   B 1  351 ? 5.353   34.510  16.073  1.00 36.41  ? 351 PHE   C CA    1 
ATOM   6216  C  C     . PHE   B 1  351 ? 5.951   35.857  15.677  1.00 34.80  ? 351 PHE   C C     1 
ATOM   6217  O  O     . PHE   B 1  351 ? 6.168   36.720  16.526  1.00 42.16  ? 351 PHE   C O     1 
ATOM   6218  C  CB    . PHE   B 1  351 ? 3.896   34.698  16.478  1.00 32.39  ? 351 PHE   C CB    1 
ATOM   6219  C  CG    . PHE   B 1  351 ? 3.082   33.451  16.375  1.00 47.06  ? 351 PHE   C CG    1 
ATOM   6220  C  CD1   . PHE   B 1  351 ? 2.522   33.069  15.164  1.00 53.53  ? 351 PHE   C CD1   1 
ATOM   6221  C  CD2   . PHE   B 1  351 ? 2.880   32.648  17.483  1.00 44.12  ? 351 PHE   C CD2   1 
ATOM   6222  C  CE1   . PHE   B 1  351 ? 1.765   31.906  15.066  1.00 41.49  ? 351 PHE   C CE1   1 
ATOM   6223  C  CE2   . PHE   B 1  351 ? 2.134   31.505  17.390  1.00 37.86  ? 351 PHE   C CE2   1 
ATOM   6224  C  CZ    . PHE   B 1  351 ? 1.581   31.130  16.174  1.00 39.17  ? 351 PHE   C CZ    1 
ATOM   6225  N  N     . LYS   B 1  352 ? 6.204   36.037  14.384  1.00 29.38  ? 352 LYS   C N     1 
ATOM   6226  C  CA    . LYS   B 1  352 ? 6.667   37.296  13.826  1.00 25.96  ? 352 LYS   C CA    1 
ATOM   6227  C  C     . LYS   B 1  352 ? 5.809   37.625  12.622  1.00 29.01  ? 352 LYS   C C     1 
ATOM   6228  O  O     . LYS   B 1  352 ? 5.438   36.734  11.860  1.00 33.65  ? 352 LYS   C O     1 
ATOM   6229  C  CB    . LYS   B 1  352 ? 8.132   37.235  13.408  1.00 31.39  ? 352 LYS   C CB    1 
ATOM   6230  C  CG    . LYS   B 1  352 ? 8.633   38.540  12.774  1.00 25.60  ? 352 LYS   C CG    1 
ATOM   6231  C  CD    . LYS   B 1  352 ? 10.122  38.485  12.430  1.00 31.85  ? 352 LYS   C CD    1 
ATOM   6232  C  CE    . LYS   B 1  352 ? 10.720  39.893  12.310  1.00 40.54  ? 352 LYS   C CE    1 
ATOM   6233  N  NZ    . LYS   B 1  352 ? 10.996  40.575  13.620  1.00 28.76  ? 352 LYS   C NZ    1 
ATOM   6234  N  N     . VAL   B 1  353 ? 5.542   38.909  12.417  1.00 31.80  ? 353 VAL   C N     1 
ATOM   6235  C  CA    . VAL   B 1  353 ? 4.377   39.324  11.636  1.00 33.70  ? 353 VAL   C CA    1 
ATOM   6236  C  C     . VAL   B 1  353 ? 4.693   40.596  10.841  1.00 28.61  ? 353 VAL   C C     1 
ATOM   6237  O  O     . VAL   B 1  353 ? 5.216   41.576  11.372  1.00 37.96  ? 353 VAL   C O     1 
ATOM   6238  C  CB    . VAL   B 1  353 ? 3.175   39.501  12.594  1.00 31.07  ? 353 VAL   C CB    1 
ATOM   6239  C  CG1   . VAL   B 1  353 ? 2.182   40.412  12.047  1.00 30.99  ? 353 VAL   C CG1   1 
ATOM   6240  C  CG2   . VAL   B 1  353 ? 2.524   38.162  12.854  1.00 28.08  ? 353 VAL   C CG2   1 
ATOM   6241  N  N     . GLY   B 1  354 ? 4.376   40.581  9.560   1.00 27.93  ? 354 GLY   C N     1 
ATOM   6242  C  CA    . GLY   B 1  354 ? 4.474   41.775  8.755   1.00 29.54  ? 354 GLY   C CA    1 
ATOM   6243  C  C     . GLY   B 1  354 ? 3.353   41.770  7.739   1.00 30.44  ? 354 GLY   C C     1 
ATOM   6244  O  O     . GLY   B 1  354 ? 2.730   40.744  7.486   1.00 33.03  ? 354 GLY   C O     1 
ATOM   6245  N  N     . ILE   B 1  355 ? 3.114   42.938  7.158   1.00 31.86  ? 355 ILE   C N     1 
ATOM   6246  C  CA    . ILE   B 1  355 ? 2.032   43.176  6.213   1.00 24.74  ? 355 ILE   C CA    1 
ATOM   6247  C  C     . ILE   B 1  355 ? 2.607   43.991  5.079   1.00 29.65  ? 355 ILE   C C     1 
ATOM   6248  O  O     . ILE   B 1  355 ? 3.267   45.007  5.317   1.00 33.91  ? 355 ILE   C O     1 
ATOM   6249  C  CB    . ILE   B 1  355 ? 0.862   43.954  6.849   1.00 27.94  ? 355 ILE   C CB    1 
ATOM   6250  C  CG1   . ILE   B 1  355 ? 0.140   43.136  7.893   1.00 18.55  ? 355 ILE   C CG1   1 
ATOM   6251  C  CG2   . ILE   B 1  355 ? -0.115  44.414  5.809   1.00 25.46  ? 355 ILE   C CG2   1 
ATOM   6252  C  CD1   . ILE   B 1  355 ? -1.074  43.835  8.345   1.00 28.62  ? 355 ILE   C CD1   1 
ATOM   6253  N  N     . ASN   B 1  356 ? 2.350   43.576  3.849   1.00 37.78  ? 356 ASN   C N     1 
ATOM   6254  C  CA    . ASN   B 1  356 ? 2.758   44.349  2.683   1.00 34.78  ? 356 ASN   C CA    1 
ATOM   6255  C  C     . ASN   B 1  356 ? 1.496   44.776  1.951   1.00 40.31  ? 356 ASN   C C     1 
ATOM   6256  O  O     . ASN   B 1  356 ? 0.736   43.929  1.478   1.00 43.46  ? 356 ASN   C O     1 
ATOM   6257  C  CB    . ASN   B 1  356 ? 3.687   43.544  1.778   1.00 34.45  ? 356 ASN   C CB    1 
ATOM   6258  C  CG    . ASN   B 1  356 ? 4.265   44.380  0.674   1.00 61.54  ? 356 ASN   C CG    1 
ATOM   6259  O  OD1   . ASN   B 1  356 ? 3.638   44.569  -0.377  1.00 60.57  ? 356 ASN   C OD1   1 
ATOM   6260  N  ND2   . ASN   B 1  356 ? 5.462   44.922  0.910   1.00 67.39  ? 356 ASN   C ND2   1 
ATOM   6261  N  N     . TYR   B 1  357 ? 1.259   46.083  1.876   1.00 41.69  ? 357 TYR   C N     1 
ATOM   6262  C  CA    . TYR   B 1  357 ? -0.059  46.541  1.466   1.00 46.38  ? 357 TYR   C CA    1 
ATOM   6263  C  C     . TYR   B 1  357 ? -0.355  46.242  0.005   1.00 46.94  ? 357 TYR   C C     1 
ATOM   6264  O  O     . TYR   B 1  357 ? -1.534  46.160  -0.361  1.00 48.91  ? 357 TYR   C O     1 
ATOM   6265  C  CB    . TYR   B 1  357 ? -0.213  48.034  1.782   1.00 36.64  ? 357 TYR   C CB    1 
ATOM   6266  C  CG    . TYR   B 1  357 ? -0.415  48.227  3.270   1.00 54.80  ? 357 TYR   C CG    1 
ATOM   6267  C  CD1   . TYR   B 1  357 ? -1.319  47.426  3.957   1.00 49.53  ? 357 TYR   C CD1   1 
ATOM   6268  C  CD2   . TYR   B 1  357 ? 0.333   49.152  4.007   1.00 64.69  ? 357 TYR   C CD2   1 
ATOM   6269  C  CE1   . TYR   B 1  357 ? -1.505  47.547  5.314   1.00 46.34  ? 357 TYR   C CE1   1 
ATOM   6270  C  CE2   . TYR   B 1  357 ? 0.146   49.283  5.385   1.00 50.95  ? 357 TYR   C CE2   1 
ATOM   6271  C  CZ    . TYR   B 1  357 ? -0.776  48.466  6.025   1.00 47.34  ? 357 TYR   C CZ    1 
ATOM   6272  O  OH    . TYR   B 1  357 ? -1.004  48.545  7.381   1.00 57.08  ? 357 TYR   C OH    1 
ATOM   6273  N  N     . GLN   B 1  358 ? 0.671   46.027  -0.817  1.00 33.26  ? 358 GLN   C N     1 
ATOM   6274  C  CA    . GLN   B 1  358 ? 0.439   45.879  -2.246  1.00 46.15  ? 358 GLN   C CA    1 
ATOM   6275  C  C     . GLN   B 1  358 ? -0.290  44.560  -2.532  1.00 46.19  ? 358 GLN   C C     1 
ATOM   6276  O  O     . GLN   B 1  358 ? 0.061   43.510  -1.974  1.00 44.01  ? 358 GLN   C O     1 
ATOM   6277  C  CB    . GLN   B 1  358 ? 1.769   45.966  -3.011  1.00 50.59  ? 358 GLN   C CB    1 
ATOM   6278  C  CG    . GLN   B 1  358 ? 1.756   45.286  -4.393  1.00 58.05  ? 358 GLN   C CG    1 
ATOM   6279  C  CD    . GLN   B 1  358 ? 1.272   46.190  -5.536  1.00 69.15  ? 358 GLN   C CD    1 
ATOM   6280  O  OE1   . GLN   B 1  358 ? 0.992   47.376  -5.331  1.00 73.73  ? 358 GLN   C OE1   1 
ATOM   6281  N  NE2   . GLN   B 1  358 ? 1.183   45.625  -6.750  1.00 54.71  ? 358 GLN   C NE2   1 
ATOM   6282  N  N     . PRO   B 1  359 ? -1.302  44.575  -3.397  1.00 51.95  ? 359 PRO   C N     1 
ATOM   6283  C  CA    . PRO   B 1  359 ? -2.246  43.446  -3.461  1.00 45.83  ? 359 PRO   C CA    1 
ATOM   6284  C  C     . PRO   B 1  359 ? -1.683  42.280  -4.252  1.00 39.68  ? 359 PRO   C C     1 
ATOM   6285  O  O     . PRO   B 1  359 ? -0.801  42.452  -5.107  1.00 45.83  ? 359 PRO   C O     1 
ATOM   6286  C  CB    . PRO   B 1  359 ? -3.472  44.049  -4.164  1.00 39.65  ? 359 PRO   C CB    1 
ATOM   6287  C  CG    . PRO   B 1  359 ? -3.017  45.388  -4.727  1.00 45.20  ? 359 PRO   C CG    1 
ATOM   6288  C  CD    . PRO   B 1  359 ? -1.552  45.548  -4.471  1.00 51.53  ? 359 PRO   C CD    1 
ATOM   6289  N  N     . PRO   B 1  360 ? -2.182  41.075  -4.003  1.00 37.29  ? 360 PRO   C N     1 
ATOM   6290  C  CA    . PRO   B 1  360 ? -1.748  39.924  -4.804  1.00 35.82  ? 360 PRO   C CA    1 
ATOM   6291  C  C     . PRO   B 1  360 ? -2.061  40.127  -6.284  1.00 37.03  ? 360 PRO   C C     1 
ATOM   6292  O  O     . PRO   B 1  360 ? -3.021  40.794  -6.658  1.00 41.49  ? 360 PRO   C O     1 
ATOM   6293  C  CB    . PRO   B 1  360 ? -2.543  38.747  -4.216  1.00 34.27  ? 360 PRO   C CB    1 
ATOM   6294  C  CG    . PRO   B 1  360 ? -3.090  39.228  -2.893  1.00 32.06  ? 360 PRO   C CG    1 
ATOM   6295  C  CD    . PRO   B 1  360 ? -3.190  40.725  -2.985  1.00 33.24  ? 360 PRO   C CD    1 
ATOM   6296  N  N     . THR   B 1  361 ? -1.229  39.536  -7.125  1.00 43.39  ? 361 THR   C N     1 
ATOM   6297  C  CA    . THR   B 1  361 ? -1.317  39.648  -8.570  1.00 41.83  ? 361 THR   C CA    1 
ATOM   6298  C  C     . THR   B 1  361 ? -1.462  38.251  -9.154  1.00 35.36  ? 361 THR   C C     1 
ATOM   6299  O  O     . THR   B 1  361 ? -0.992  37.271  -8.573  1.00 32.74  ? 361 THR   C O     1 
ATOM   6300  C  CB    . THR   B 1  361 ? -0.043  40.336  -9.131  1.00 45.58  ? 361 THR   C CB    1 
ATOM   6301  O  OG1   . THR   B 1  361 ? -0.062  41.727  -8.818  1.00 41.44  ? 361 THR   C OG1   1 
ATOM   6302  C  CG2   . THR   B 1  361 ? 0.113   40.154  -10.636 1.00 37.42  ? 361 THR   C CG2   1 
ATOM   6303  N  N     . VAL   B 1  362 ? -2.096  38.152  -10.310 1.00 33.81  ? 362 VAL   C N     1 
ATOM   6304  C  CA    . VAL   B 1  362 ? -2.214  36.859  -10.963 1.00 33.60  ? 362 VAL   C CA    1 
ATOM   6305  C  C     . VAL   B 1  362 ? -1.895  37.030  -12.434 1.00 40.40  ? 362 VAL   C C     1 
ATOM   6306  O  O     . VAL   B 1  362 ? -2.308  38.004  -13.066 1.00 44.60  ? 362 VAL   C O     1 
ATOM   6307  C  CB    . VAL   B 1  362 ? -3.603  36.227  -10.765 1.00 35.92  ? 362 VAL   C CB    1 
ATOM   6308  C  CG1   . VAL   B 1  362 ? -3.679  35.517  -9.396  1.00 30.28  ? 362 VAL   C CG1   1 
ATOM   6309  C  CG2   . VAL   B 1  362 ? -4.700  37.285  -10.927 1.00 38.35  ? 362 VAL   C CG2   1 
ATOM   6310  N  N     . VAL   B 1  363 ? -1.151  36.070  -12.967 1.00 43.99  ? 363 VAL   C N     1 
ATOM   6311  C  CA    A VAL   B 1  363 ? -0.773  36.100  -14.378 1.00 45.29  ? 363 VAL   C CA    1 
ATOM   6312  C  CA    B VAL   B 1  363 ? -0.772  36.109  -14.381 0.00 45.43  ? 363 VAL   C CA    1 
ATOM   6313  C  C     . VAL   B 1  363 ? -2.026  36.036  -15.237 1.00 41.11  ? 363 VAL   C C     1 
ATOM   6314  O  O     . VAL   B 1  363 ? -2.990  35.344  -14.864 1.00 33.96  ? 363 VAL   C O     1 
ATOM   6315  C  CB    A VAL   B 1  363 ? 0.177   34.933  -14.690 1.00 46.89  ? 363 VAL   C CB    1 
ATOM   6316  C  CB    B VAL   B 1  363 ? 0.191   34.958  -14.717 0.00 46.97  ? 363 VAL   C CB    1 
ATOM   6317  C  CG1   A VAL   B 1  363 ? 0.077   34.530  -16.161 1.00 56.77  ? 363 VAL   C CG1   1 
ATOM   6318  C  CG1   B VAL   B 1  363 ? 0.540   34.971  -16.197 0.00 52.45  ? 363 VAL   C CG1   1 
ATOM   6319  C  CG2   A VAL   B 1  363 ? 1.584   35.317  -14.340 1.00 38.93  ? 363 VAL   C CG2   1 
ATOM   6320  C  CG2   B VAL   B 1  363 ? 1.448   35.052  -13.865 0.00 43.71  ? 363 VAL   C CG2   1 
ATOM   6321  N  N     . PRO   B 1  364 ? -2.075  36.725  -16.378 1.00 63.20  ? 364 PRO   C N     1 
ATOM   6322  C  CA    . PRO   B 1  364 ? -3.236  36.625  -17.276 1.00 60.25  ? 364 PRO   C CA    1 
ATOM   6323  C  C     . PRO   B 1  364 ? -3.603  35.182  -17.589 1.00 57.25  ? 364 PRO   C C     1 
ATOM   6324  O  O     . PRO   B 1  364 ? -2.745  34.353  -17.904 1.00 58.25  ? 364 PRO   C O     1 
ATOM   6325  C  CB    . PRO   B 1  364 ? -2.760  37.361  -18.534 1.00 57.83  ? 364 PRO   C CB    1 
ATOM   6326  C  CG    . PRO   B 1  364 ? -1.804  38.381  -18.015 1.00 62.50  ? 364 PRO   C CG    1 
ATOM   6327  C  CD    . PRO   B 1  364 ? -1.082  37.696  -16.876 1.00 67.24  ? 364 PRO   C CD    1 
ATOM   6328  N  N     . GLY   B 1  365 ? -4.897  34.884  -17.510 1.00 54.34  ? 365 GLY   C N     1 
ATOM   6329  C  CA    . GLY   B 1  365 ? -5.380  33.564  -17.861 1.00 60.29  ? 365 GLY   C CA    1 
ATOM   6330  C  C     . GLY   B 1  365 ? -4.698  32.438  -17.110 1.00 57.56  ? 365 GLY   C C     1 
ATOM   6331  O  O     . GLY   B 1  365 ? -4.300  31.429  -17.703 1.00 55.89  ? 365 GLY   C O     1 
ATOM   6332  N  N     . GLY   B 1  366 ? -4.543  32.607  -15.799 1.00 59.12  ? 366 GLY   C N     1 
ATOM   6333  C  CA    . GLY   B 1  366 ? -4.048  31.557  -14.940 1.00 50.07  ? 366 GLY   C CA    1 
ATOM   6334  C  C     . GLY   B 1  366 ? -5.181  30.784  -14.296 1.00 47.18  ? 366 GLY   C C     1 
ATOM   6335  O  O     . GLY   B 1  366 ? -6.361  30.964  -14.606 1.00 48.64  ? 366 GLY   C O     1 
ATOM   6336  N  N     . ASP   B 1  367 ? -4.799  29.898  -13.378 1.00 49.24  ? 367 ASP   C N     1 
ATOM   6337  C  CA    . ASP   B 1  367 ? -5.755  29.126  -12.599 1.00 45.15  ? 367 ASP   C CA    1 
ATOM   6338  C  C     . ASP   B 1  367 ? -6.056  29.745  -11.251 1.00 43.43  ? 367 ASP   C C     1 
ATOM   6339  O  O     . ASP   B 1  367 ? -7.095  29.433  -10.664 1.00 49.37  ? 367 ASP   C O     1 
ATOM   6340  C  CB    . ASP   B 1  367 ? -5.223  27.717  -12.374 1.00 52.61  ? 367 ASP   C CB    1 
ATOM   6341  C  CG    . ASP   B 1  367 ? -4.446  27.210  -13.555 1.00 62.25  ? 367 ASP   C CG    1 
ATOM   6342  O  OD1   . ASP   B 1  367 ? -5.104  26.884  -14.575 1.00 61.55  ? 367 ASP   C OD1   1 
ATOM   6343  O  OD2   . ASP   B 1  367 ? -3.189  27.174  -13.468 1.00 55.08  ? 367 ASP   C OD2   1 
ATOM   6344  N  N     . LEU   B 1  368 ? -5.174  30.608  -10.764 1.00 40.95  ? 368 LEU   C N     1 
ATOM   6345  C  CA    . LEU   B 1  368 ? -5.267  31.165  -9.426  1.00 34.75  ? 368 LEU   C CA    1 
ATOM   6346  C  C     . LEU   B 1  368 ? -6.210  32.359  -9.421  1.00 32.41  ? 368 LEU   C C     1 
ATOM   6347  O  O     . LEU   B 1  368 ? -5.952  33.359  -10.092 1.00 46.40  ? 368 LEU   C O     1 
ATOM   6348  C  CB    . LEU   B 1  368 ? -3.876  31.576  -8.962  1.00 34.02  ? 368 LEU   C CB    1 
ATOM   6349  C  CG    . LEU   B 1  368 ? -3.538  31.273  -7.514  1.00 52.32  ? 368 LEU   C CG    1 
ATOM   6350  C  CD1   . LEU   B 1  368 ? -4.105  29.901  -7.114  1.00 42.23  ? 368 LEU   C CD1   1 
ATOM   6351  C  CD2   . LEU   B 1  368 ? -2.026  31.313  -7.360  1.00 44.80  ? 368 LEU   C CD2   1 
ATOM   6352  N  N     . ALA   B 1  369 ? -7.300  32.266  -8.670  1.00 39.03  ? 369 ALA   C N     1 
ATOM   6353  C  CA    . ALA   B 1  369 ? -8.174  33.426  -8.487  1.00 34.32  ? 369 ALA   C CA    1 
ATOM   6354  C  C     . ALA   B 1  369 ? -7.371  34.630  -8.018  1.00 27.06  ? 369 ALA   C C     1 
ATOM   6355  O  O     . ALA   B 1  369 ? -6.433  34.498  -7.230  1.00 37.46  ? 369 ALA   C O     1 
ATOM   6356  C  CB    . ALA   B 1  369 ? -9.271  33.114  -7.465  1.00 28.90  ? 369 ALA   C CB    1 
ATOM   6357  N  N     . LYS   B 1  370 ? -7.747  35.810  -8.489  1.00 29.61  ? 370 LYS   C N     1 
ATOM   6358  C  CA    . LYS   B 1  370 ? -7.171  37.033  -7.937  1.00 36.84  ? 370 LYS   C CA    1 
ATOM   6359  C  C     . LYS   B 1  370 ? -7.894  37.398  -6.636  1.00 35.97  ? 370 LYS   C C     1 
ATOM   6360  O  O     . LYS   B 1  370 ? -9.092  37.695  -6.641  1.00 30.69  ? 370 LYS   C O     1 
ATOM   6361  C  CB    . LYS   B 1  370 ? -7.243  38.179  -8.940  1.00 27.48  ? 370 LYS   C CB    1 
ATOM   6362  C  CG    . LYS   B 1  370 ? -6.641  39.472  -8.416  1.00 35.42  ? 370 LYS   C CG    1 
ATOM   6363  C  CD    . LYS   B 1  370 ? -6.289  40.427  -9.556  1.00 38.01  ? 370 LYS   C CD    1 
ATOM   6364  C  CE    . LYS   B 1  370 ? -5.715  41.741  -9.049  1.00 48.22  ? 370 LYS   C CE    1 
ATOM   6365  N  NZ    . LYS   B 1  370 ? -6.745  42.676  -8.483  1.00 62.88  ? 370 LYS   C NZ    1 
ATOM   6366  N  N     . VAL   B 1  371 ? -7.172  37.368  -5.520  1.00 33.00  ? 371 VAL   C N     1 
ATOM   6367  C  CA    . VAL   B 1  371 ? -7.774  37.607  -4.221  1.00 32.51  ? 371 VAL   C CA    1 
ATOM   6368  C  C     . VAL   B 1  371 ? -7.322  38.962  -3.694  1.00 34.58  ? 371 VAL   C C     1 
ATOM   6369  O  O     . VAL   B 1  371 ? -6.382  39.589  -4.194  1.00 32.98  ? 371 VAL   C O     1 
ATOM   6370  C  CB    . VAL   B 1  371 ? -7.458  36.478  -3.219  1.00 32.44  ? 371 VAL   C CB    1 
ATOM   6371  C  CG1   . VAL   B 1  371 ? -8.178  35.190  -3.636  1.00 25.44  ? 371 VAL   C CG1   1 
ATOM   6372  C  CG2   . VAL   B 1  371 ? -5.947  36.251  -3.143  1.00 41.66  ? 371 VAL   C CG2   1 
ATOM   6373  N  N     . GLN   B 1  372 ? -8.037  39.432  -2.684  1.00 40.79  ? 372 GLN   C N     1 
ATOM   6374  C  CA    . GLN   B 1  372 ? -7.752  40.745  -2.142  1.00 37.41  ? 372 GLN   C CA    1 
ATOM   6375  C  C     . GLN   B 1  372 ? -6.659  40.724  -1.086  1.00 39.43  ? 372 GLN   C C     1 
ATOM   6376  O  O     . GLN   B 1  372 ? -6.053  41.772  -0.815  1.00 41.33  ? 372 GLN   C O     1 
ATOM   6377  C  CB    . GLN   B 1  372 ? -9.032  41.351  -1.560  1.00 40.83  ? 372 GLN   C CB    1 
ATOM   6378  C  CG    . GLN   B 1  372 ? -9.711  42.329  -2.499  1.00 41.73  ? 372 GLN   C CG    1 
ATOM   6379  C  CD    . GLN   B 1  372 ? -10.849 43.072  -1.818  1.00 66.32  ? 372 GLN   C CD    1 
ATOM   6380  O  OE1   . GLN   B 1  372 ? -11.615 42.482  -1.038  1.00 62.83  ? 372 GLN   C OE1   1 
ATOM   6381  N  NE2   . GLN   B 1  372 ? -10.958 44.381  -2.093  1.00 58.70  ? 372 GLN   C NE2   1 
ATOM   6382  N  N     . ARG   B 1  373 ? -6.383  39.562  -0.503  1.00 29.60  ? 373 ARG   C N     1 
ATOM   6383  C  CA    . ARG   B 1  373 ? -5.473  39.474  0.625   1.00 30.55  ? 373 ARG   C CA    1 
ATOM   6384  C  C     . ARG   B 1  373 ? -4.937  38.056  0.677   1.00 34.38  ? 373 ARG   C C     1 
ATOM   6385  O  O     . ARG   B 1  373 ? -5.717  37.104  0.683   1.00 38.10  ? 373 ARG   C O     1 
ATOM   6386  C  CB    . ARG   B 1  373 ? -6.197  39.843  1.927   1.00 37.55  ? 373 ARG   C CB    1 
ATOM   6387  C  CG    . ARG   B 1  373 ? -7.245  38.833  2.360   1.00 31.79  ? 373 ARG   C CG    1 
ATOM   6388  C  CD    . ARG   B 1  373 ? -8.142  39.392  3.466   1.00 40.64  ? 373 ARG   C CD    1 
ATOM   6389  N  NE    . ARG   B 1  373 ? -8.875  40.585  3.041   1.00 53.37  ? 373 ARG   C NE    1 
ATOM   6390  C  CZ    . ARG   B 1  373 ? -10.036 40.592  2.386   1.00 51.73  ? 373 ARG   C CZ    1 
ATOM   6391  N  NH1   . ARG   B 1  373 ? -10.656 39.469  2.045   1.00 36.84  ? 373 ARG   C NH1   1 
ATOM   6392  N  NH2   . ARG   B 1  373 ? -10.583 41.759  2.054   1.00 42.93  ? 373 ARG   C NH2   1 
ATOM   6393  N  N     . ALA   B 1  374 ? -3.619  37.913  0.677   1.00 32.55  ? 374 ALA   C N     1 
ATOM   6394  C  CA    . ALA   B 1  374 ? -2.990  36.605  0.770   1.00 26.47  ? 374 ALA   C CA    1 
ATOM   6395  C  C     . ALA   B 1  374 ? -2.023  36.591  1.947   1.00 31.31  ? 374 ALA   C C     1 
ATOM   6396  O  O     . ALA   B 1  374 ? -1.715  37.634  2.545   1.00 35.33  ? 374 ALA   C O     1 
ATOM   6397  C  CB    . ALA   B 1  374 ? -2.274  36.240  -0.537  1.00 22.38  ? 374 ALA   C CB    1 
ATOM   6398  N  N     . VAL   B 1  375 ? -1.548  35.393  2.280   1.00 22.13  ? 375 VAL   C N     1 
ATOM   6399  C  CA    . VAL   B 1  375 ? -0.574  35.219  3.353   1.00 28.02  ? 375 VAL   C CA    1 
ATOM   6400  C  C     . VAL   B 1  375 ? 0.364   34.086  2.976   1.00 28.10  ? 375 VAL   C C     1 
ATOM   6401  O  O     . VAL   B 1  375 ? -0.063  33.060  2.448   1.00 37.18  ? 375 VAL   C O     1 
ATOM   6402  C  CB    . VAL   B 1  375 ? -1.251  34.929  4.709   1.00 33.06  ? 375 VAL   C CB    1 
ATOM   6403  C  CG1   . VAL   B 1  375 ? -1.999  33.604  4.651   1.00 27.79  ? 375 VAL   C CG1   1 
ATOM   6404  C  CG2   . VAL   B 1  375 ? -0.204  34.910  5.820   1.00 31.83  ? 375 VAL   C CG2   1 
ATOM   6405  N  N     . CYS   B 1  376 ? 1.646   34.275  3.250   1.00 29.35  ? 376 CYS   C N     1 
ATOM   6406  C  CA    . CYS   B 1  376 ? 2.631   33.209  3.179   1.00 25.11  ? 376 CYS   C CA    1 
ATOM   6407  C  C     . CYS   B 1  376 ? 3.219   33.049  4.571   1.00 35.92  ? 376 CYS   C C     1 
ATOM   6408  O  O     . CYS   B 1  376 ? 3.631   34.040  5.186   1.00 41.72  ? 376 CYS   C O     1 
ATOM   6409  C  CB    . CYS   B 1  376 ? 3.731   33.518  2.159   1.00 18.64  ? 376 CYS   C CB    1 
ATOM   6410  S  SG    . CYS   B 1  376 ? 5.033   32.235  2.117   1.00 31.21  ? 376 CYS   C SG    1 
ATOM   6411  N  N     . MET   B 1  377 ? 3.226   31.825  5.089   1.00 30.61  ? 377 MET   C N     1 
ATOM   6412  C  CA    . MET   B 1  377 ? 3.820   31.565  6.392   1.00 26.91  ? 377 MET   C CA    1 
ATOM   6413  C  C     . MET   B 1  377 ? 5.184   30.909  6.220   1.00 29.71  ? 377 MET   C C     1 
ATOM   6414  O  O     . MET   B 1  377 ? 5.342   29.993  5.406   1.00 29.90  ? 377 MET   C O     1 
ATOM   6415  C  CB    . MET   B 1  377 ? 2.921   30.694  7.265   1.00 25.51  ? 377 MET   C CB    1 
ATOM   6416  C  CG    . MET   B 1  377 ? 3.533   30.418  8.628   1.00 27.75  ? 377 MET   C CG    1 
ATOM   6417  S  SD    . MET   B 1  377 ? 2.390   29.917  9.921   1.00 42.95  ? 377 MET   C SD    1 
ATOM   6418  C  CE    . MET   B 1  377 ? 2.263   28.168  9.642   1.00 23.06  ? 377 MET   C CE    1 
ATOM   6419  N  N     . LEU   B 1  378 ? 6.169   31.400  6.981   1.00 28.83  ? 378 LEU   C N     1 
ATOM   6420  C  CA    . LEU   B 1  378 ? 7.519   30.842  7.032   1.00 25.91  ? 378 LEU   C CA    1 
ATOM   6421  C  C     . LEU   B 1  378 ? 7.687   30.245  8.417   1.00 27.80  ? 378 LEU   C C     1 
ATOM   6422  O  O     . LEU   B 1  378 ? 7.948   30.962  9.386   1.00 34.73  ? 378 LEU   C O     1 
ATOM   6423  C  CB    . LEU   B 1  378 ? 8.585   31.896  6.741   1.00 20.90  ? 378 LEU   C CB    1 
ATOM   6424  C  CG    . LEU   B 1  378 ? 8.463   32.500  5.329   1.00 31.85  ? 378 LEU   C CG    1 
ATOM   6425  C  CD1   . LEU   B 1  378 ? 9.411   33.670  5.095   1.00 28.62  ? 378 LEU   C CD1   1 
ATOM   6426  C  CD2   . LEU   B 1  378 ? 8.651   31.436  4.261   1.00 30.14  ? 378 LEU   C CD2   1 
ATOM   6427  N  N     . SER   B 1  379 ? 7.516   28.939  8.516   1.00 24.75  ? 379 SER   C N     1 
ATOM   6428  C  CA    . SER   B 1  379 ? 7.727   28.263  9.781   1.00 29.18  ? 379 SER   C CA    1 
ATOM   6429  C  C     . SER   B 1  379 ? 9.047   27.515  9.708   1.00 29.82  ? 379 SER   C C     1 
ATOM   6430  O  O     . SER   B 1  379 ? 9.476   27.094  8.632   1.00 34.64  ? 379 SER   C O     1 
ATOM   6431  C  CB    . SER   B 1  379 ? 6.566   27.313  10.130  1.00 31.37  ? 379 SER   C CB    1 
ATOM   6432  O  OG    . SER   B 1  379 ? 5.848   26.828  8.997   1.00 36.03  ? 379 SER   C OG    1 
ATOM   6433  N  N     . ASN   B 1  380 ? 9.729   27.431  10.851  1.00 25.56  ? 380 ASN   C N     1 
ATOM   6434  C  CA    . ASN   B 1  380 ? 10.887  26.566  11.023  1.00 24.28  ? 380 ASN   C CA    1 
ATOM   6435  C  C     . ASN   B 1  380 ? 10.477  25.472  11.998  1.00 27.08  ? 380 ASN   C C     1 
ATOM   6436  O  O     . ASN   B 1  380 ? 10.342  25.711  13.202  1.00 29.82  ? 380 ASN   C O     1 
ATOM   6437  C  CB    . ASN   B 1  380 ? 12.110  27.322  11.530  1.00 23.33  ? 380 ASN   C CB    1 
ATOM   6438  C  CG    . ASN   B 1  380 ? 13.261  26.375  11.915  1.00 31.57  ? 380 ASN   C CG    1 
ATOM   6439  O  OD1   . ASN   B 1  380 ? 13.942  26.585  12.910  1.00 27.18  ? 380 ASN   C OD1   1 
ATOM   6440  N  ND2   . ASN   B 1  380 ? 13.466  25.328  11.118  1.00 32.71  ? 380 ASN   C ND2   1 
ATOM   6441  N  N     . THR   B 1  381 ? 10.281  24.285  11.486  1.00 21.67  ? 381 THR   C N     1 
ATOM   6442  C  CA    . THR   B 1  381 ? 9.686   23.230  12.274  1.00 22.44  ? 381 THR   C CA    1 
ATOM   6443  C  C     . THR   B 1  381 ? 10.517  21.981  12.088  1.00 26.84  ? 381 THR   C C     1 
ATOM   6444  O  O     . THR   B 1  381 ? 11.059  21.748  11.005  1.00 25.15  ? 381 THR   C O     1 
ATOM   6445  C  CB    . THR   B 1  381 ? 8.211   22.991  11.874  1.00 26.06  ? 381 THR   C CB    1 
ATOM   6446  O  OG1   . THR   B 1  381 ? 7.773   21.732  12.399  1.00 43.27  ? 381 THR   C OG1   1 
ATOM   6447  C  CG2   . THR   B 1  381 ? 8.018   23.012  10.362  1.00 17.06  ? 381 THR   C CG2   1 
ATOM   6448  N  N     . THR   B 1  382 ? 10.655  21.203  13.162  1.00 26.56  ? 382 THR   C N     1 
ATOM   6449  C  CA    . THR   B 1  382 ? 11.422  19.972  13.067  1.00 27.54  ? 382 THR   C CA    1 
ATOM   6450  C  C     . THR   B 1  382 ? 10.824  19.007  12.056  1.00 28.81  ? 382 THR   C C     1 
ATOM   6451  O  O     . THR   B 1  382 ? 11.503  18.069  11.626  1.00 31.85  ? 382 THR   C O     1 
ATOM   6452  C  CB    . THR   B 1  382 ? 11.492  19.306  14.429  1.00 30.76  ? 382 THR   C CB    1 
ATOM   6453  O  OG1   . THR   B 1  382 ? 10.161  19.098  14.906  1.00 27.01  ? 382 THR   C OG1   1 
ATOM   6454  C  CG2   . THR   B 1  382 ? 12.264  20.191  15.385  1.00 27.66  ? 382 THR   C CG2   1 
ATOM   6455  N  N     . ALA   B 1  383 ? 9.568   19.222  11.666  1.00 28.39  ? 383 ALA   C N     1 
ATOM   6456  C  CA    . ALA   B 1  383 ? 8.907   18.299  10.756  1.00 31.59  ? 383 ALA   C CA    1 
ATOM   6457  C  C     . ALA   B 1  383 ? 9.613   18.251  9.404   1.00 34.89  ? 383 ALA   C C     1 
ATOM   6458  O  O     . ALA   B 1  383 ? 9.712   17.182  8.788   1.00 35.08  ? 383 ALA   C O     1 
ATOM   6459  C  CB    . ALA   B 1  383 ? 7.436   18.690  10.592  1.00 27.38  ? 383 ALA   C CB    1 
ATOM   6460  N  N     . ILE   B 1  384 ? 10.108  19.393  8.921   1.00 25.87  ? 384 ILE   C N     1 
ATOM   6461  C  CA    . ILE   B 1  384 ? 10.669  19.458  7.580   1.00 21.27  ? 384 ILE   C CA    1 
ATOM   6462  C  C     . ILE   B 1  384 ? 11.674  18.324  7.427   1.00 27.27  ? 384 ILE   C C     1 
ATOM   6463  O  O     . ILE   B 1  384 ? 11.971  17.883  6.314   1.00 31.46  ? 384 ILE   C O     1 
ATOM   6464  C  CB    . ILE   B 1  384 ? 11.319  20.827  7.310   1.00 24.51  ? 384 ILE   C CB    1 
ATOM   6465  C  CG1   . ILE   B 1  384 ? 11.426  21.062  5.802   1.00 19.17  ? 384 ILE   C CG1   1 
ATOM   6466  C  CG2   . ILE   B 1  384 ? 12.700  20.929  8.010   1.00 19.55  ? 384 ILE   C CG2   1 
ATOM   6467  C  CD1   . ILE   B 1  384 ? 10.694  22.256  5.299   1.00 17.88  ? 384 ILE   C CD1   1 
ATOM   6468  N  N     . ALA   B 1  385 ? 12.187  17.828  8.553   1.00 26.38  ? 385 ALA   C N     1 
ATOM   6469  C  CA    . ALA   B 1  385 ? 13.171  16.759  8.523   1.00 21.43  ? 385 ALA   C CA    1 
ATOM   6470  C  C     . ALA   B 1  385 ? 12.624  15.509  7.850   1.00 28.38  ? 385 ALA   C C     1 
ATOM   6471  O  O     . ALA   B 1  385 ? 13.379  14.791  7.190   1.00 34.68  ? 385 ALA   C O     1 
ATOM   6472  C  CB    . ALA   B 1  385 ? 13.639  16.454  9.943   1.00 15.68  ? 385 ALA   C CB    1 
ATOM   6473  N  N     . GLU   B 1  386 ? 11.326  15.225  8.002   1.00 28.66  ? 386 GLU   C N     1 
ATOM   6474  C  CA    . GLU   B 1  386 ? 10.699  14.110  7.289   1.00 26.91  ? 386 GLU   C CA    1 
ATOM   6475  C  C     . GLU   B 1  386 ? 11.128  14.068  5.824   1.00 31.90  ? 386 GLU   C C     1 
ATOM   6476  O  O     . GLU   B 1  386 ? 11.595  13.037  5.329   1.00 30.96  ? 386 GLU   C O     1 
ATOM   6477  C  CB    . GLU   B 1  386 ? 9.173   14.211  7.369   1.00 26.47  ? 386 GLU   C CB    1 
ATOM   6478  C  CG    . GLU   B 1  386 ? 8.560   14.204  8.759   1.00 22.47  ? 386 GLU   C CG    1 
ATOM   6479  C  CD    . GLU   B 1  386 ? 7.058   14.391  8.697   1.00 34.57  ? 386 GLU   C CD    1 
ATOM   6480  O  OE1   . GLU   B 1  386 ? 6.412   13.831  7.789   1.00 43.29  ? 386 GLU   C OE1   1 
ATOM   6481  O  OE2   . GLU   B 1  386 ? 6.511   15.115  9.537   1.00 45.56  ? 386 GLU   C OE2   1 
ATOM   6482  N  N     . ALA   B 1  387 ? 10.952  15.189  5.116   1.00 24.02  ? 387 ALA   C N     1 
ATOM   6483  C  CA    . ALA   B 1  387 ? 11.490  15.358  3.774   1.00 24.05  ? 387 ALA   C CA    1 
ATOM   6484  C  C     . ALA   B 1  387 ? 12.891  14.771  3.608   1.00 29.73  ? 387 ALA   C C     1 
ATOM   6485  O  O     . ALA   B 1  387 ? 13.142  14.009  2.667   1.00 37.86  ? 387 ALA   C O     1 
ATOM   6486  C  CB    . ALA   B 1  387 ? 11.498  16.842  3.409   1.00 27.77  ? 387 ALA   C CB    1 
ATOM   6487  N  N     . TRP   B 1  388 ? 13.832  15.131  4.482   1.00 19.06  ? 388 TRP   C N     1 
ATOM   6488  C  CA    . TRP   B 1  388 ? 15.159  14.520  4.402   1.00 26.52  ? 388 TRP   C CA    1 
ATOM   6489  C  C     . TRP   B 1  388 ? 15.074  13.004  4.608   1.00 29.01  ? 388 TRP   C C     1 
ATOM   6490  O  O     . TRP   B 1  388 ? 15.687  12.221  3.874   1.00 28.58  ? 388 TRP   C O     1 
ATOM   6491  C  CB    . TRP   B 1  388 ? 16.121  15.129  5.440   1.00 26.11  ? 388 TRP   C CB    1 
ATOM   6492  C  CG    . TRP   B 1  388 ? 16.308  16.617  5.408   1.00 25.63  ? 388 TRP   C CG    1 
ATOM   6493  C  CD1   . TRP   B 1  388 ? 16.192  17.494  6.471   1.00 24.27  ? 388 TRP   C CD1   1 
ATOM   6494  C  CD2   . TRP   B 1  388 ? 16.639  17.412  4.272   1.00 25.36  ? 388 TRP   C CD2   1 
ATOM   6495  N  NE1   . TRP   B 1  388 ? 16.447  18.780  6.053   1.00 23.49  ? 388 TRP   C NE1   1 
ATOM   6496  C  CE2   . TRP   B 1  388 ? 16.715  18.757  4.706   1.00 21.82  ? 388 TRP   C CE2   1 
ATOM   6497  C  CE3   . TRP   B 1  388 ? 16.886  17.121  2.931   1.00 29.59  ? 388 TRP   C CE3   1 
ATOM   6498  C  CZ2   . TRP   B 1  388 ? 17.028  19.797  3.841   1.00 21.53  ? 388 TRP   C CZ2   1 
ATOM   6499  C  CZ3   . TRP   B 1  388 ? 17.205  18.171  2.064   1.00 29.20  ? 388 TRP   C CZ3   1 
ATOM   6500  C  CH2   . TRP   B 1  388 ? 17.269  19.482  2.522   1.00 27.59  ? 388 TRP   C CH2   1 
ATOM   6501  N  N     . ALA   B 1  389 ? 14.324  12.570  5.620   1.00 29.57  ? 389 ALA   C N     1 
ATOM   6502  C  CA    . ALA   B 1  389 ? 14.185  11.142  5.880   1.00 31.83  ? 389 ALA   C CA    1 
ATOM   6503  C  C     . ALA   B 1  389 ? 13.763  10.371  4.618   1.00 33.89  ? 389 ALA   C C     1 
ATOM   6504  O  O     . ALA   B 1  389 ? 14.404  9.390   4.219   1.00 31.71  ? 389 ALA   C O     1 
ATOM   6505  C  CB    . ALA   B 1  389 ? 13.185  10.941  7.007   1.00 22.22  ? 389 ALA   C CB    1 
ATOM   6506  N  N     . ARG   B 1  390 ? 12.696  10.811  3.963   1.00 21.84  ? 390 ARG   C N     1 
ATOM   6507  C  CA    . ARG   B 1  390 ? 12.237  10.085  2.796   1.00 22.42  ? 390 ARG   C CA    1 
ATOM   6508  C  C     . ARG   B 1  390 ? 13.327  10.009  1.732   1.00 34.34  ? 390 ARG   C C     1 
ATOM   6509  O  O     . ARG   B 1  390 ? 13.596  8.934   1.184   1.00 39.89  ? 390 ARG   C O     1 
ATOM   6510  C  CB    . ARG   B 1  390 ? 10.958  10.725  2.263   1.00 25.28  ? 390 ARG   C CB    1 
ATOM   6511  C  CG    . ARG   B 1  390 ? 9.759   10.531  3.186   1.00 19.16  ? 390 ARG   C CG    1 
ATOM   6512  C  CD    . ARG   B 1  390 ? 8.487   11.050  2.558   1.00 22.66  ? 390 ARG   C CD    1 
ATOM   6513  N  NE    . ARG   B 1  390 ? 8.608   12.381  1.976   1.00 20.85  ? 390 ARG   C NE    1 
ATOM   6514  C  CZ    . ARG   B 1  390 ? 8.338   13.503  2.632   1.00 30.07  ? 390 ARG   C CZ    1 
ATOM   6515  N  NH1   . ARG   B 1  390 ? 8.042   13.492  3.926   1.00 27.09  ? 390 ARG   C NH1   1 
ATOM   6516  N  NH2   . ARG   B 1  390 ? 8.349   14.663  1.974   1.00 24.95  ? 390 ARG   C NH2   1 
ATOM   6517  N  N     . LEU   B 1  391 ? 13.978  11.134  1.426   1.00 35.16  ? 391 LEU   C N     1 
ATOM   6518  C  CA    . LEU   B 1  391 ? 15.055  11.094  0.439   1.00 35.66  ? 391 LEU   C CA    1 
ATOM   6519  C  C     . LEU   B 1  391 ? 16.191  10.202  0.919   1.00 40.74  ? 391 LEU   C C     1 
ATOM   6520  O  O     . LEU   B 1  391 ? 16.655  9.318   0.189   1.00 35.54  ? 391 LEU   C O     1 
ATOM   6521  C  CB    . LEU   B 1  391 ? 15.572  12.503  0.146   1.00 36.65  ? 391 LEU   C CB    1 
ATOM   6522  C  CG    . LEU   B 1  391 ? 15.006  13.157  -1.115  1.00 38.44  ? 391 LEU   C CG    1 
ATOM   6523  C  CD1   . LEU   B 1  391 ? 15.569  14.555  -1.312  1.00 38.74  ? 391 LEU   C CD1   1 
ATOM   6524  C  CD2   . LEU   B 1  391 ? 15.284  12.286  -2.334  1.00 33.97  ? 391 LEU   C CD2   1 
ATOM   6525  N  N     . ASP   B 1  392 ? 16.656  10.427  2.153   1.00 37.47  ? 392 ASP   C N     1 
ATOM   6526  C  CA    . ASP   B 1  392 ? 17.742  9.617   2.689   1.00 34.42  ? 392 ASP   C CA    1 
ATOM   6527  C  C     . ASP   B 1  392 ? 17.402  8.131   2.644   1.00 40.58  ? 392 ASP   C C     1 
ATOM   6528  O  O     . ASP   B 1  392 ? 18.303  7.283   2.587   1.00 37.54  ? 392 ASP   C O     1 
ATOM   6529  C  CB    . ASP   B 1  392 ? 18.069  10.064  4.115   1.00 31.05  ? 392 ASP   C CB    1 
ATOM   6530  C  CG    . ASP   B 1  392 ? 18.909  11.329  4.150   1.00 35.00  ? 392 ASP   C CG    1 
ATOM   6531  O  OD1   . ASP   B 1  392 ? 19.528  11.649  3.111   1.00 38.28  ? 392 ASP   C OD1   1 
ATOM   6532  O  OD2   . ASP   B 1  392 ? 18.958  12.004  5.207   1.00 34.85  ? 392 ASP   C OD2   1 
ATOM   6533  N  N     . HIS   B 1  393 ? 16.113  7.791   2.656   1.00 38.37  ? 393 HIS   C N     1 
ATOM   6534  C  CA    . HIS   B 1  393 ? 15.759  6.380   2.587   1.00 37.21  ? 393 HIS   C CA    1 
ATOM   6535  C  C     . HIS   B 1  393 ? 15.851  5.853   1.153   1.00 40.99  ? 393 HIS   C C     1 
ATOM   6536  O  O     . HIS   B 1  393 ? 16.396  4.763   0.922   1.00 39.27  ? 393 HIS   C O     1 
ATOM   6537  C  CB    . HIS   B 1  393 ? 14.359  6.140   3.162   1.00 32.87  ? 393 HIS   C CB    1 
ATOM   6538  C  CG    . HIS   B 1  393 ? 13.997  4.692   3.205   1.00 43.67  ? 393 HIS   C CG    1 
ATOM   6539  N  ND1   . HIS   B 1  393 ? 14.705  3.776   3.959   1.00 47.63  ? 393 HIS   C ND1   1 
ATOM   6540  C  CD2   . HIS   B 1  393 ? 13.053  3.986   2.538   1.00 28.38  ? 393 HIS   C CD2   1 
ATOM   6541  C  CE1   . HIS   B 1  393 ? 14.184  2.575   3.782   1.00 45.17  ? 393 HIS   C CE1   1 
ATOM   6542  N  NE2   . HIS   B 1  393 ? 13.191  2.673   2.914   1.00 36.97  ? 393 HIS   C NE2   1 
ATOM   6543  N  N     . LYS   B 1  394 ? 15.309  6.598   0.177   1.00 28.75  ? 394 LYS   C N     1 
ATOM   6544  C  CA    . LYS   B 1  394 ? 15.465  6.187   -1.216  1.00 30.46  ? 394 LYS   C CA    1 
ATOM   6545  C  C     . LYS   B 1  394 ? 16.936  6.053   -1.572  1.00 31.93  ? 394 LYS   C C     1 
ATOM   6546  O  O     . LYS   B 1  394 ? 17.335  5.117   -2.273  1.00 36.34  ? 394 LYS   C O     1 
ATOM   6547  C  CB    . LYS   B 1  394 ? 14.758  7.167   -2.149  1.00 23.44  ? 394 LYS   C CB    1 
ATOM   6548  C  CG    . LYS   B 1  394 ? 13.246  6.963   -2.172  1.00 28.69  ? 394 LYS   C CG    1 
ATOM   6549  C  CD    . LYS   B 1  394 ? 12.538  8.122   -2.844  1.00 25.34  ? 394 LYS   C CD    1 
ATOM   6550  C  CE    . LYS   B 1  394 ? 11.066  8.228   -2.458  1.00 24.19  ? 394 LYS   C CE    1 
ATOM   6551  N  NZ    . LYS   B 1  394 ? 10.272  6.986   -2.753  1.00 36.12  ? 394 LYS   C NZ    1 
ATOM   6552  N  N     . PHE   B 1  395 ? 17.761  6.964   -1.064  1.00 34.96  ? 395 PHE   C N     1 
ATOM   6553  C  CA    . PHE   B 1  395 ? 19.198  6.874   -1.275  1.00 33.09  ? 395 PHE   C CA    1 
ATOM   6554  C  C     . PHE   B 1  395 ? 19.749  5.555   -0.734  1.00 34.12  ? 395 PHE   C C     1 
ATOM   6555  O  O     . PHE   B 1  395 ? 20.515  4.857   -1.414  1.00 29.39  ? 395 PHE   C O     1 
ATOM   6556  C  CB    . PHE   B 1  395 ? 19.858  8.085   -0.617  1.00 31.88  ? 395 PHE   C CB    1 
ATOM   6557  C  CG    . PHE   B 1  395 ? 21.348  8.136   -0.748  1.00 27.54  ? 395 PHE   C CG    1 
ATOM   6558  C  CD1   . PHE   B 1  395 ? 22.163  7.338   0.054   1.00 26.92  ? 395 PHE   C CD1   1 
ATOM   6559  C  CD2   . PHE   B 1  395 ? 21.943  9.026   -1.638  1.00 28.35  ? 395 PHE   C CD2   1 
ATOM   6560  C  CE1   . PHE   B 1  395 ? 23.548  7.403   -0.041  1.00 27.64  ? 395 PHE   C CE1   1 
ATOM   6561  C  CE2   . PHE   B 1  395 ? 23.332  9.101   -1.741  1.00 28.95  ? 395 PHE   C CE2   1 
ATOM   6562  C  CZ    . PHE   B 1  395 ? 24.140  8.294   -0.934  1.00 28.09  ? 395 PHE   C CZ    1 
ATOM   6563  N  N     . ASP   B 1  396 ? 19.347  5.181   0.481   1.00 31.62  ? 396 ASP   C N     1 
ATOM   6564  C  CA    . ASP   B 1  396 ? 19.934  3.992   1.104   1.00 31.11  ? 396 ASP   C CA    1 
ATOM   6565  C  C     . ASP   B 1  396 ? 19.582  2.718   0.347   1.00 31.89  ? 396 ASP   C C     1 
ATOM   6566  O  O     . ASP   B 1  396 ? 20.414  1.814   0.228   1.00 32.55  ? 396 ASP   C O     1 
ATOM   6567  C  CB    . ASP   B 1  396 ? 19.495  3.893   2.555   1.00 18.83  ? 396 ASP   C CB    1 
ATOM   6568  C  CG    . ASP   B 1  396 ? 20.097  4.988   3.406   1.00 34.57  ? 396 ASP   C CG    1 
ATOM   6569  O  OD1   . ASP   B 1  396 ? 21.093  5.600   2.958   1.00 32.43  ? 396 ASP   C OD1   1 
ATOM   6570  O  OD2   . ASP   B 1  396 ? 19.576  5.249   4.510   1.00 37.00  ? 396 ASP   C OD2   1 
ATOM   6571  N  N     . LEU   B 1  397 ? 18.354  2.622   -0.165  1.00 37.67  ? 397 LEU   C N     1 
ATOM   6572  C  CA    . LEU   B 1  397 ? 17.969  1.463   -0.955  1.00 32.20  ? 397 LEU   C CA    1 
ATOM   6573  C  C     . LEU   B 1  397 ? 18.938  1.242   -2.104  1.00 42.01  ? 397 LEU   C C     1 
ATOM   6574  O  O     . LEU   B 1  397 ? 19.509  0.155   -2.254  1.00 39.62  ? 397 LEU   C O     1 
ATOM   6575  C  CB    . LEU   B 1  397 ? 16.552  1.645   -1.481  1.00 33.95  ? 397 LEU   C CB    1 
ATOM   6576  C  CG    . LEU   B 1  397 ? 15.516  1.692   -0.365  1.00 41.74  ? 397 LEU   C CG    1 
ATOM   6577  C  CD1   . LEU   B 1  397 ? 14.129  2.150   -0.876  1.00 24.92  ? 397 LEU   C CD1   1 
ATOM   6578  C  CD2   . LEU   B 1  397 ? 15.477  0.332   0.283   1.00 24.71  ? 397 LEU   C CD2   1 
ATOM   6579  N  N     . MET   B 1  398 ? 19.148  2.277   -2.923  1.00 43.70  ? 398 MET   C N     1 
ATOM   6580  C  CA    . MET   B 1  398 ? 19.995  2.125   -4.099  1.00 33.43  ? 398 MET   C CA    1 
ATOM   6581  C  C     . MET   B 1  398 ? 21.454  1.945   -3.720  1.00 27.08  ? 398 MET   C C     1 
ATOM   6582  O  O     . MET   B 1  398 ? 22.129  1.043   -4.225  1.00 33.17  ? 398 MET   C O     1 
ATOM   6583  C  CB    . MET   B 1  398 ? 19.830  3.326   -5.010  1.00 33.53  ? 398 MET   C CB    1 
ATOM   6584  C  CG    . MET   B 1  398 ? 18.491  3.387   -5.691  1.00 34.27  ? 398 MET   C CG    1 
ATOM   6585  S  SD    . MET   B 1  398 ? 18.386  4.956   -6.543  1.00 35.75  ? 398 MET   C SD    1 
ATOM   6586  C  CE    . MET   B 1  398 ? 17.207  4.496   -7.786  1.00 44.55  ? 398 MET   C CE    1 
ATOM   6587  N  N     . TYR   B 1  399 ? 21.966  2.795   -2.832  1.00 33.31  ? 399 TYR   C N     1 
ATOM   6588  C  CA    . TYR   B 1  399 ? 23.402  2.772   -2.574  1.00 34.72  ? 399 TYR   C CA    1 
ATOM   6589  C  C     . TYR   B 1  399 ? 23.848  1.485   -1.879  1.00 33.56  ? 399 TYR   C C     1 
ATOM   6590  O  O     . TYR   B 1  399 ? 24.993  1.056   -2.057  1.00 33.28  ? 399 TYR   C O     1 
ATOM   6591  C  CB    . TYR   B 1  399 ? 23.818  3.992   -1.770  1.00 27.61  ? 399 TYR   C CB    1 
ATOM   6592  C  CG    . TYR   B 1  399 ? 25.302  4.184   -1.773  1.00 27.17  ? 399 TYR   C CG    1 
ATOM   6593  C  CD1   . TYR   B 1  399 ? 25.949  4.740   -2.864  1.00 30.63  ? 399 TYR   C CD1   1 
ATOM   6594  C  CD2   . TYR   B 1  399 ? 26.065  3.777   -0.697  1.00 26.47  ? 399 TYR   C CD2   1 
ATOM   6595  C  CE1   . TYR   B 1  399 ? 27.321  4.894   -2.864  1.00 37.57  ? 399 TYR   C CE1   1 
ATOM   6596  C  CE2   . TYR   B 1  399 ? 27.418  3.936   -0.677  1.00 22.56  ? 399 TYR   C CE2   1 
ATOM   6597  C  CZ    . TYR   B 1  399 ? 28.050  4.492   -1.751  1.00 37.59  ? 399 TYR   C CZ    1 
ATOM   6598  O  OH    . TYR   B 1  399 ? 29.419  4.632   -1.698  1.00 47.69  ? 399 TYR   C OH    1 
ATOM   6599  N  N     . ALA   B 1  400 ? 22.971  0.849   -1.100  1.00 30.73  ? 400 ALA   C N     1 
ATOM   6600  C  CA    . ALA   B 1  400 ? 23.314  -0.447  -0.527  1.00 36.82  ? 400 ALA   C CA    1 
ATOM   6601  C  C     . ALA   B 1  400 ? 23.674  -1.471  -1.607  1.00 38.30  ? 400 ALA   C C     1 
ATOM   6602  O  O     . ALA   B 1  400 ? 24.420  -2.424  -1.341  1.00 34.18  ? 400 ALA   C O     1 
ATOM   6603  C  CB    . ALA   B 1  400 ? 22.159  -0.952  0.337   1.00 39.18  ? 400 ALA   C CB    1 
ATOM   6604  N  N     . LYS   B 1  401 ? 23.153  -1.307  -2.820  1.00 32.76  ? 401 LYS   C N     1 
ATOM   6605  C  CA    . LYS   B 1  401 ? 23.496  -2.192  -3.919  1.00 31.02  ? 401 LYS   C CA    1 
ATOM   6606  C  C     . LYS   B 1  401 ? 24.357  -1.498  -4.955  1.00 36.22  ? 401 LYS   C C     1 
ATOM   6607  O  O     . LYS   B 1  401 ? 24.563  -2.048  -6.035  1.00 50.62  ? 401 LYS   C O     1 
ATOM   6608  C  CB    . LYS   B 1  401 ? 22.234  -2.768  -4.565  1.00 34.58  ? 401 LYS   C CB    1 
ATOM   6609  C  CG    . LYS   B 1  401 ? 21.571  -3.914  -3.769  1.00 37.02  ? 401 LYS   C CG    1 
ATOM   6610  C  CD    . LYS   B 1  401 ? 21.304  -3.483  -2.316  1.00 48.10  ? 401 LYS   C CD    1 
ATOM   6611  C  CE    . LYS   B 1  401 ? 20.712  -4.578  -1.442  1.00 36.88  ? 401 LYS   C CE    1 
ATOM   6612  N  NZ    . LYS   B 1  401 ? 19.361  -4.919  -1.922  1.00 47.09  ? 401 LYS   C NZ    1 
ATOM   6613  N  N     . ARG   B 1  402 ? 24.881  -0.313  -4.642  1.00 32.08  ? 402 ARG   C N     1 
ATOM   6614  C  CA    . ARG   B 1  402 ? 25.673  0.501   -5.570  1.00 34.60  ? 402 ARG   C CA    1 
ATOM   6615  C  C     . ARG   B 1  402 ? 24.977  0.730   -6.909  1.00 38.38  ? 402 ARG   C C     1 
ATOM   6616  O  O     . ARG   B 1  402 ? 25.648  1.003   -7.913  1.00 34.20  ? 402 ARG   C O     1 
ATOM   6617  C  CB    . ARG   B 1  402 ? 27.050  -0.099  -5.832  1.00 24.91  ? 402 ARG   C CB    1 
ATOM   6618  C  CG    . ARG   B 1  402 ? 27.991  -0.035  -4.675  1.00 24.89  ? 402 ARG   C CG    1 
ATOM   6619  C  CD    . ARG   B 1  402 ? 27.775  1.171   -3.815  1.00 33.26  ? 402 ARG   C CD    1 
ATOM   6620  N  NE    . ARG   B 1  402 ? 28.726  1.139   -2.711  1.00 41.86  ? 402 ARG   C NE    1 
ATOM   6621  C  CZ    . ARG   B 1  402 ? 28.434  0.800   -1.462  1.00 34.87  ? 402 ARG   C CZ    1 
ATOM   6622  N  NH1   . ARG   B 1  402 ? 27.187  0.597   -1.070  1.00 26.83  ? 402 ARG   C NH1   1 
ATOM   6623  N  NH2   . ARG   B 1  402 ? 29.421  0.666   -0.584  1.00 33.92  ? 402 ARG   C NH2   1 
ATOM   6624  N  N     . ALA   B 1  403 ? 23.651  0.643   -6.945  1.00 28.02  ? 403 ALA   C N     1 
ATOM   6625  C  CA    . ALA   B 1  403 ? 22.935  0.849   -8.189  1.00 28.18  ? 403 ALA   C CA    1 
ATOM   6626  C  C     . ALA   B 1  403 ? 23.251  2.226   -8.758  1.00 32.11  ? 403 ALA   C C     1 
ATOM   6627  O  O     . ALA   B 1  403 ? 23.212  3.224   -8.040  1.00 34.86  ? 403 ALA   C O     1 
ATOM   6628  C  CB    . ALA   B 1  403 ? 21.431  0.696   -7.955  1.00 27.09  ? 403 ALA   C CB    1 
ATOM   6629  N  N     . PHE   B 1  404 ? 23.576  2.272   -10.053 1.00 27.79  ? 404 PHE   C N     1 
ATOM   6630  C  CA    . PHE   B 1  404 ? 23.828  3.497   -10.813 1.00 23.11  ? 404 PHE   C CA    1 
ATOM   6631  C  C     . PHE   B 1  404 ? 25.120  4.221   -10.427 1.00 26.42  ? 404 PHE   C C     1 
ATOM   6632  O  O     . PHE   B 1  404 ? 25.563  5.131   -11.136 1.00 30.26  ? 404 PHE   C O     1 
ATOM   6633  C  CB    . PHE   B 1  404 ? 22.664  4.465   -10.679 1.00 22.24  ? 404 PHE   C CB    1 
ATOM   6634  C  CG    . PHE   B 1  404 ? 21.343  3.884   -11.067 1.00 32.34  ? 404 PHE   C CG    1 
ATOM   6635  C  CD1   . PHE   B 1  404 ? 20.918  3.916   -12.389 1.00 31.83  ? 404 PHE   C CD1   1 
ATOM   6636  C  CD2   . PHE   B 1  404 ? 20.508  3.329   -10.106 1.00 28.21  ? 404 PHE   C CD2   1 
ATOM   6637  C  CE1   . PHE   B 1  404 ? 19.695  3.385   -12.758 1.00 31.85  ? 404 PHE   C CE1   1 
ATOM   6638  C  CE2   . PHE   B 1  404 ? 19.287  2.798   -10.466 1.00 36.70  ? 404 PHE   C CE2   1 
ATOM   6639  C  CZ    . PHE   B 1  404 ? 18.876  2.824   -11.801 1.00 34.36  ? 404 PHE   C CZ    1 
ATOM   6640  N  N     . VAL   B 1  405 ? 25.744  3.832   -9.313  1.00 24.94  ? 405 VAL   C N     1 
ATOM   6641  C  CA    . VAL   B 1  405 ? 26.966  4.507   -8.897  1.00 32.54  ? 405 VAL   C CA    1 
ATOM   6642  C  C     . VAL   B 1  405 ? 28.037  4.503   -9.993  1.00 38.92  ? 405 VAL   C C     1 
ATOM   6643  O  O     . VAL   B 1  405 ? 28.929  5.373   -9.998  1.00 31.69  ? 405 VAL   C O     1 
ATOM   6644  C  CB    . VAL   B 1  405 ? 27.496  3.857   -7.600  1.00 26.40  ? 405 VAL   C CB    1 
ATOM   6645  C  CG1   . VAL   B 1  405 ? 28.809  4.509   -7.197  1.00 26.01  ? 405 VAL   C CG1   1 
ATOM   6646  C  CG2   . VAL   B 1  405 ? 26.469  3.963   -6.493  1.00 24.22  ? 405 VAL   C CG2   1 
ATOM   6647  N  N     . HIS   B 1  406 ? 27.987  3.545   -10.927 1.00 25.96  ? 406 HIS   C N     1 
ATOM   6648  C  CA    . HIS   B 1  406 ? 29.019  3.526   -11.955 1.00 24.10  ? 406 HIS   C CA    1 
ATOM   6649  C  C     . HIS   B 1  406 ? 28.913  4.749   -12.850 1.00 28.59  ? 406 HIS   C C     1 
ATOM   6650  O  O     . HIS   B 1  406 ? 29.927  5.203   -13.384 1.00 31.57  ? 406 HIS   C O     1 
ATOM   6651  C  CB    . HIS   B 1  406 ? 28.969  2.224   -12.781 1.00 25.80  ? 406 HIS   C CB    1 
ATOM   6652  C  CG    . HIS   B 1  406 ? 27.775  2.101   -13.674 1.00 26.47  ? 406 HIS   C CG    1 
ATOM   6653  N  ND1   . HIS   B 1  406 ? 26.530  1.733   -13.207 1.00 37.50  ? 406 HIS   C ND1   1 
ATOM   6654  C  CD2   . HIS   B 1  406 ? 27.631  2.304   -15.003 1.00 31.65  ? 406 HIS   C CD2   1 
ATOM   6655  C  CE1   . HIS   B 1  406 ? 25.668  1.723   -14.210 1.00 35.40  ? 406 HIS   C CE1   1 
ATOM   6656  N  NE2   . HIS   B 1  406 ? 26.312  2.060   -15.313 1.00 35.55  ? 406 HIS   C NE2   1 
ATOM   6657  N  N     . TRP   B 1  407 ? 27.711  5.311   -13.003 1.00 26.66  ? 407 TRP   C N     1 
ATOM   6658  C  CA    . TRP   B 1  407 ? 27.571  6.532   -13.787 1.00 27.38  ? 407 TRP   C CA    1 
ATOM   6659  C  C     . TRP   B 1  407 ? 28.294  7.703   -13.146 1.00 31.15  ? 407 TRP   C C     1 
ATOM   6660  O  O     . TRP   B 1  407 ? 28.743  8.615   -13.855 1.00 34.91  ? 407 TRP   C O     1 
ATOM   6661  C  CB    . TRP   B 1  407 ? 26.101  6.894   -13.980 1.00 23.81  ? 407 TRP   C CB    1 
ATOM   6662  C  CG    . TRP   B 1  407 ? 25.353  5.947   -14.854 1.00 31.71  ? 407 TRP   C CG    1 
ATOM   6663  C  CD1   . TRP   B 1  407 ? 24.400  5.068   -14.465 1.00 29.50  ? 407 TRP   C CD1   1 
ATOM   6664  C  CD2   . TRP   B 1  407 ? 25.506  5.776   -16.267 1.00 32.74  ? 407 TRP   C CD2   1 
ATOM   6665  N  NE1   . TRP   B 1  407 ? 23.943  4.358   -15.542 1.00 36.32  ? 407 TRP   C NE1   1 
ATOM   6666  C  CE2   . TRP   B 1  407 ? 24.612  4.770   -16.662 1.00 39.19  ? 407 TRP   C CE2   1 
ATOM   6667  C  CE3   . TRP   B 1  407 ? 26.327  6.366   -17.234 1.00 32.51  ? 407 TRP   C CE3   1 
ATOM   6668  C  CZ2   . TRP   B 1  407 ? 24.503  4.346   -17.981 1.00 41.27  ? 407 TRP   C CZ2   1 
ATOM   6669  C  CZ3   . TRP   B 1  407 ? 26.208  5.963   -18.532 1.00 29.80  ? 407 TRP   C CZ3   1 
ATOM   6670  C  CH2   . TRP   B 1  407 ? 25.305  4.958   -18.900 1.00 41.44  ? 407 TRP   C CH2   1 
ATOM   6671  N  N     . TYR   B 1  408 ? 28.384  7.722   -11.818 1.00 28.00  ? 408 TYR   C N     1 
ATOM   6672  C  CA    . TYR   B 1  408 ? 29.051  8.842   -11.167 1.00 35.74  ? 408 TYR   C CA    1 
ATOM   6673  C  C     . TYR   B 1  408 ? 30.551  8.619   -11.148 1.00 27.12  ? 408 TYR   C C     1 
ATOM   6674  O  O     . TYR   B 1  408 ? 31.320  9.513   -11.503 1.00 29.89  ? 408 TYR   C O     1 
ATOM   6675  C  CB    . TYR   B 1  408 ? 28.506  9.053   -9.742  1.00 28.57  ? 408 TYR   C CB    1 
ATOM   6676  C  CG    . TYR   B 1  408 ? 27.044  9.389   -9.720  1.00 27.68  ? 408 TYR   C CG    1 
ATOM   6677  C  CD1   . TYR   B 1  408 ? 26.099  8.439   -10.073 1.00 35.17  ? 408 TYR   C CD1   1 
ATOM   6678  C  CD2   . TYR   B 1  408 ? 26.600  10.657  -9.375  1.00 30.84  ? 408 TYR   C CD2   1 
ATOM   6679  C  CE1   . TYR   B 1  408 ? 24.749  8.737   -10.085 1.00 34.16  ? 408 TYR   C CE1   1 
ATOM   6680  C  CE2   . TYR   B 1  408 ? 25.239  10.965  -9.365  1.00 32.18  ? 408 TYR   C CE2   1 
ATOM   6681  C  CZ    . TYR   B 1  408 ? 24.321  9.996   -9.727  1.00 33.91  ? 408 TYR   C CZ    1 
ATOM   6682  O  OH    . TYR   B 1  408 ? 22.968  10.261  -9.735  1.00 38.10  ? 408 TYR   C OH    1 
ATOM   6683  N  N     . VAL   B 1  409 ? 30.965  7.417   -10.746 1.00 24.80  ? 409 VAL   C N     1 
ATOM   6684  C  CA    . VAL   B 1  409 ? 32.375  7.043   -10.739 1.00 29.07  ? 409 VAL   C CA    1 
ATOM   6685  C  C     . VAL   B 1  409 ? 33.006  7.290   -12.106 1.00 39.02  ? 409 VAL   C C     1 
ATOM   6686  O  O     . VAL   B 1  409 ? 34.013  8.000   -12.229 1.00 35.93  ? 409 VAL   C O     1 
ATOM   6687  C  CB    . VAL   B 1  409 ? 32.519  5.574   -10.320 1.00 31.77  ? 409 VAL   C CB    1 
ATOM   6688  C  CG1   . VAL   B 1  409 ? 33.968  5.138   -10.474 1.00 31.03  ? 409 VAL   C CG1   1 
ATOM   6689  C  CG2   . VAL   B 1  409 ? 31.981  5.378   -8.904  1.00 22.81  ? 409 VAL   C CG2   1 
ATOM   6690  N  N     . GLY   B 1  410 ? 32.409  6.714   -13.156 1.00 34.15  ? 410 GLY   C N     1 
ATOM   6691  C  CA    . GLY   B 1  410 ? 32.838  6.916   -14.524 1.00 28.74  ? 410 GLY   C CA    1 
ATOM   6692  C  C     . GLY   B 1  410 ? 33.110  8.350   -14.922 1.00 38.21  ? 410 GLY   C C     1 
ATOM   6693  O  O     . GLY   B 1  410 ? 33.845  8.607   -15.877 1.00 50.15  ? 410 GLY   C O     1 
ATOM   6694  N  N     . GLU   B 1  411 ? 32.530  9.304   -14.207 1.00 38.30  ? 411 GLU   C N     1 
ATOM   6695  C  CA    . GLU   B 1  411 ? 32.762  10.711  -14.487 1.00 34.57  ? 411 GLU   C CA    1 
ATOM   6696  C  C     . GLU   B 1  411 ? 33.724  11.348  -13.496 1.00 34.38  ? 411 GLU   C C     1 
ATOM   6697  O  O     . GLU   B 1  411 ? 33.843  12.572  -13.476 1.00 31.97  ? 411 GLU   C O     1 
ATOM   6698  C  CB    . GLU   B 1  411 ? 31.435  11.480  -14.500 1.00 33.31  ? 411 GLU   C CB    1 
ATOM   6699  C  CG    . GLU   B 1  411 ? 30.466  11.068  -15.610 1.00 35.16  ? 411 GLU   C CG    1 
ATOM   6700  C  CD    . GLU   B 1  411 ? 30.866  11.588  -16.972 1.00 35.74  ? 411 GLU   C CD    1 
ATOM   6701  O  OE1   . GLU   B 1  411 ? 32.015  12.028  -17.121 1.00 51.85  ? 411 GLU   C OE1   1 
ATOM   6702  O  OE2   . GLU   B 1  411 ? 30.034  11.573  -17.898 1.00 33.85  ? 411 GLU   C OE2   1 
ATOM   6703  N  N     . GLY   B 1  412 ? 34.419  10.558  -12.680 1.00 25.87  ? 412 GLY   C N     1 
ATOM   6704  C  CA    . GLY   B 1  412 ? 35.438  11.081  -11.798 1.00 32.54  ? 412 GLY   C CA    1 
ATOM   6705  C  C     . GLY   B 1  412 ? 35.149  10.949  -10.312 1.00 38.43  ? 412 GLY   C C     1 
ATOM   6706  O  O     . GLY   B 1  412 ? 36.080  11.079  -9.511  1.00 29.98  ? 412 GLY   C O     1 
ATOM   6707  N  N     . MET   B 1  413 ? 33.900  10.690  -9.913  1.00 39.89  ? 413 MET   C N     1 
ATOM   6708  C  CA    . MET   B 1  413 ? 33.566  10.615  -8.494  1.00 40.62  ? 413 MET   C CA    1 
ATOM   6709  C  C     . MET   B 1  413 ? 34.040  9.294   -7.892  1.00 35.13  ? 413 MET   C C     1 
ATOM   6710  O  O     . MET   B 1  413 ? 34.163  8.285   -8.587  1.00 44.68  ? 413 MET   C O     1 
ATOM   6711  C  CB    . MET   B 1  413 ? 32.056  10.792  -8.277  1.00 34.62  ? 413 MET   C CB    1 
ATOM   6712  C  CG    . MET   B 1  413 ? 31.552  12.178  -8.712  1.00 42.66  ? 413 MET   C CG    1 
ATOM   6713  S  SD    . MET   B 1  413 ? 29.941  12.754  -8.086  1.00 36.51  ? 413 MET   C SD    1 
ATOM   6714  C  CE    . MET   B 1  413 ? 30.060  12.406  -6.343  1.00 27.62  ? 413 MET   C CE    1 
ATOM   6715  N  N     . GLU   B 1  414 ? 34.329  9.320   -6.594  1.00 29.04  ? 414 GLU   C N     1 
ATOM   6716  C  CA    . GLU   B 1  414 ? 34.644  8.132   -5.817  1.00 29.66  ? 414 GLU   C CA    1 
ATOM   6717  C  C     . GLU   B 1  414 ? 33.466  7.774   -4.917  1.00 40.73  ? 414 GLU   C C     1 
ATOM   6718  O  O     . GLU   B 1  414 ? 32.548  8.573   -4.693  1.00 33.52  ? 414 GLU   C O     1 
ATOM   6719  C  CB    . GLU   B 1  414 ? 35.892  8.335   -4.958  1.00 29.31  ? 414 GLU   C CB    1 
ATOM   6720  C  CG    . GLU   B 1  414 ? 37.105  8.893   -5.702  1.00 43.63  ? 414 GLU   C CG    1 
ATOM   6721  C  CD    . GLU   B 1  414 ? 38.034  9.653   -4.764  1.00 47.73  ? 414 GLU   C CD    1 
ATOM   6722  O  OE1   . GLU   B 1  414 ? 37.541  10.084  -3.703  1.00 55.06  ? 414 GLU   C OE1   1 
ATOM   6723  O  OE2   . GLU   B 1  414 ? 39.239  9.823   -5.066  1.00 44.80  ? 414 GLU   C OE2   1 
ATOM   6724  N  N     . GLU   B 1  415 ? 33.482  6.543   -4.407  1.00 41.42  ? 415 GLU   C N     1 
ATOM   6725  C  CA    . GLU   B 1  415 ? 32.450  6.166   -3.454  1.00 42.32  ? 415 GLU   C CA    1 
ATOM   6726  C  C     . GLU   B 1  415 ? 32.456  7.083   -2.231  1.00 41.18  ? 415 GLU   C C     1 
ATOM   6727  O  O     . GLU   B 1  415 ? 31.421  7.225   -1.567  1.00 35.26  ? 415 GLU   C O     1 
ATOM   6728  C  CB    . GLU   B 1  415 ? 32.635  4.704   -3.031  1.00 41.30  ? 415 GLU   C CB    1 
ATOM   6729  C  CG    . GLU   B 1  415 ? 32.331  3.692   -4.119  1.00 52.22  ? 415 GLU   C CG    1 
ATOM   6730  C  CD    . GLU   B 1  415 ? 31.886  2.349   -3.562  1.00 51.04  ? 415 GLU   C CD    1 
ATOM   6731  O  OE1   . GLU   B 1  415 ? 32.317  1.999   -2.442  1.00 53.74  ? 415 GLU   C OE1   1 
ATOM   6732  O  OE2   . GLU   B 1  415 ? 31.098  1.652   -4.238  1.00 46.86  ? 415 GLU   C OE2   1 
ATOM   6733  N  N     . GLY   B 1  416 ? 33.592  7.729   -1.946  1.00 40.25  ? 416 GLY   C N     1 
ATOM   6734  C  CA    . GLY   B 1  416 ? 33.743  8.478   -0.708  1.00 36.29  ? 416 GLY   C CA    1 
ATOM   6735  C  C     . GLY   B 1  416 ? 32.911  9.742   -0.637  1.00 33.11  ? 416 GLY   C C     1 
ATOM   6736  O  O     . GLY   B 1  416 ? 32.483  10.137  0.448   1.00 25.96  ? 416 GLY   C O     1 
ATOM   6737  N  N     . GLU   B 1  417 ? 32.677  10.404  -1.774  1.00 28.61  ? 417 GLU   C N     1 
ATOM   6738  C  CA    A GLU   B 1  417 ? 31.788  11.561  -1.743  0.45 33.76  ? 417 GLU   C CA    1 
ATOM   6739  C  CA    B GLU   B 1  417 ? 31.789  11.560  -1.770  0.55 34.13  ? 417 GLU   C CA    1 
ATOM   6740  C  C     . GLU   B 1  417 ? 30.336  11.147  -1.514  1.00 39.10  ? 417 GLU   C C     1 
ATOM   6741  O  O     . GLU   B 1  417 ? 29.547  11.949  -0.992  1.00 36.61  ? 417 GLU   C O     1 
ATOM   6742  C  CB    A GLU   B 1  417 ? 31.920  12.391  -3.025  0.45 27.67  ? 417 GLU   C CB    1 
ATOM   6743  C  CB    B GLU   B 1  417 ? 31.940  12.323  -3.087  0.55 26.03  ? 417 GLU   C CB    1 
ATOM   6744  C  CG    A GLU   B 1  417 ? 31.165  13.729  -2.982  0.45 28.51  ? 417 GLU   C CG    1 
ATOM   6745  C  CG    B GLU   B 1  417 ? 33.397  12.562  -3.465  0.55 23.79  ? 417 GLU   C CG    1 
ATOM   6746  C  CD    A GLU   B 1  417 ? 31.534  14.653  -4.137  0.45 29.45  ? 417 GLU   C CD    1 
ATOM   6747  C  CD    B GLU   B 1  417 ? 33.580  12.966  -4.923  0.55 28.78  ? 417 GLU   C CD    1 
ATOM   6748  O  OE1   A GLU   B 1  417 ? 32.401  14.257  -4.952  0.45 31.57  ? 417 GLU   C OE1   1 
ATOM   6749  O  OE1   B GLU   B 1  417 ? 33.183  14.090  -5.290  0.55 27.22  ? 417 GLU   C OE1   1 
ATOM   6750  O  OE2   A GLU   B 1  417 ? 30.970  15.769  -4.231  0.45 20.20  ? 417 GLU   C OE2   1 
ATOM   6751  O  OE2   B GLU   B 1  417 ? 34.123  12.155  -5.706  0.55 29.85  ? 417 GLU   C OE2   1 
ATOM   6752  N  N     . PHE   B 1  418 ? 29.975  9.904   -1.858  1.00 30.18  ? 418 PHE   C N     1 
ATOM   6753  C  CA    . PHE   B 1  418 ? 28.644  9.389   -1.549  1.00 32.38  ? 418 PHE   C CA    1 
ATOM   6754  C  C     . PHE   B 1  418 ? 28.477  9.132   -0.062  1.00 28.45  ? 418 PHE   C C     1 
ATOM   6755  O  O     . PHE   B 1  418 ? 27.503  9.571   0.547   1.00 29.32  ? 418 PHE   C O     1 
ATOM   6756  C  CB    . PHE   B 1  418 ? 28.382  8.091   -2.312  1.00 34.84  ? 418 PHE   C CB    1 
ATOM   6757  C  CG    . PHE   B 1  418 ? 27.829  8.289   -3.689  1.00 32.96  ? 418 PHE   C CG    1 
ATOM   6758  C  CD1   . PHE   B 1  418 ? 28.670  8.514   -4.765  1.00 29.83  ? 418 PHE   C CD1   1 
ATOM   6759  C  CD2   . PHE   B 1  418 ? 26.476  8.231   -3.911  1.00 29.86  ? 418 PHE   C CD2   1 
ATOM   6760  C  CE1   . PHE   B 1  418 ? 28.169  8.689   -6.031  1.00 24.08  ? 418 PHE   C CE1   1 
ATOM   6761  C  CE2   . PHE   B 1  418 ? 25.971  8.408   -5.193  1.00 32.27  ? 418 PHE   C CE2   1 
ATOM   6762  C  CZ    . PHE   B 1  418 ? 26.829  8.634   -6.245  1.00 26.34  ? 418 PHE   C CZ    1 
ATOM   6763  N  N     . SER   B 1  419 ? 29.376  8.363   0.536   1.00 30.58  ? 419 SER   C N     1 
ATOM   6764  C  CA    . SER   B 1  419 ? 29.197  8.072   1.951   1.00 30.59  ? 419 SER   C CA    1 
ATOM   6765  C  C     . SER   B 1  419 ? 29.289  9.351   2.776   1.00 35.98  ? 419 SER   C C     1 
ATOM   6766  O  O     . SER   B 1  419 ? 28.493  9.559   3.702   1.00 38.54  ? 419 SER   C O     1 
ATOM   6767  C  CB    . SER   B 1  419 ? 30.196  7.006   2.427   1.00 24.69  ? 419 SER   C CB    1 
ATOM   6768  O  OG    . SER   B 1  419 ? 31.539  7.287   2.085   1.00 40.53  ? 419 SER   C OG    1 
ATOM   6769  N  N     . GLU   B 1  420 ? 30.220  10.239  2.424   1.00 29.33  ? 420 GLU   C N     1 
ATOM   6770  C  CA    . GLU   B 1  420 ? 30.335  11.520  3.115   1.00 23.75  ? 420 GLU   C CA    1 
ATOM   6771  C  C     . GLU   B 1  420 ? 29.030  12.310  3.036   1.00 29.49  ? 420 GLU   C C     1 
ATOM   6772  O  O     . GLU   B 1  420 ? 28.514  12.792  4.053   1.00 27.07  ? 420 GLU   C O     1 
ATOM   6773  C  CB    . GLU   B 1  420 ? 31.493  12.302  2.505   1.00 24.47  ? 420 GLU   C CB    1 
ATOM   6774  C  CG    . GLU   B 1  420 ? 31.774  13.645  3.088   1.00 37.59  ? 420 GLU   C CG    1 
ATOM   6775  C  CD    . GLU   B 1  420 ? 32.989  14.277  2.442   1.00 58.32  ? 420 GLU   C CD    1 
ATOM   6776  O  OE1   . GLU   B 1  420 ? 33.876  13.505  2.008   1.00 48.63  ? 420 GLU   C OE1   1 
ATOM   6777  O  OE2   . GLU   B 1  420 ? 33.045  15.531  2.359   1.00 57.97  ? 420 GLU   C OE2   1 
ATOM   6778  N  N     . ALA   B 1  421 ? 28.489  12.468  1.826   1.00 28.04  ? 421 ALA   C N     1 
ATOM   6779  C  CA    . ALA   B 1  421 ? 27.207  13.139  1.667   1.00 23.73  ? 421 ALA   C CA    1 
ATOM   6780  C  C     . ALA   B 1  421 ? 26.163  12.539  2.591   1.00 30.44  ? 421 ALA   C C     1 
ATOM   6781  O  O     . ALA   B 1  421 ? 25.511  13.257  3.355   1.00 32.42  ? 421 ALA   C O     1 
ATOM   6782  C  CB    . ALA   B 1  421 ? 26.735  13.047  0.217   1.00 28.01  ? 421 ALA   C CB    1 
ATOM   6783  N  N     . ARG   B 1  422 ? 26.002  11.211  2.541   1.00 23.95  ? 422 ARG   C N     1 
ATOM   6784  C  CA    . ARG   B 1  422 ? 24.926  10.562  3.278   1.00 20.35  ? 422 ARG   C CA    1 
ATOM   6785  C  C     . ARG   B 1  422 ? 25.102  10.712  4.792   1.00 34.11  ? 422 ARG   C C     1 
ATOM   6786  O  O     . ARG   B 1  422 ? 24.119  10.669  5.544   1.00 28.64  ? 422 ARG   C O     1 
ATOM   6787  C  CB    . ARG   B 1  422 ? 24.859  9.089   2.890   1.00 22.18  ? 422 ARG   C CB    1 
ATOM   6788  C  CG    . ARG   B 1  422 ? 23.817  8.270   3.635   1.00 20.63  ? 422 ARG   C CG    1 
ATOM   6789  C  CD    . ARG   B 1  422 ? 22.425  8.678   3.197   1.00 26.07  ? 422 ARG   C CD    1 
ATOM   6790  N  NE    . ARG   B 1  422 ? 21.401  8.031   4.005   1.00 34.49  ? 422 ARG   C NE    1 
ATOM   6791  C  CZ    . ARG   B 1  422 ? 21.051  8.420   5.226   1.00 34.51  ? 422 ARG   C CZ    1 
ATOM   6792  N  NH1   . ARG   B 1  422 ? 21.598  9.482   5.798   1.00 26.80  ? 422 ARG   C NH1   1 
ATOM   6793  N  NH2   . ARG   B 1  422 ? 20.143  7.715   5.896   1.00 20.67  ? 422 ARG   C NH2   1 
ATOM   6794  N  N     . GLU   B 1  423 ? 26.334  10.875  5.264   1.00 25.69  ? 423 GLU   C N     1 
ATOM   6795  C  CA    . GLU   B 1  423 ? 26.526  11.036  6.694   1.00 27.76  ? 423 GLU   C CA    1 
ATOM   6796  C  C     . GLU   B 1  423 ? 26.279  12.478  7.109   1.00 31.11  ? 423 GLU   C C     1 
ATOM   6797  O  O     . GLU   B 1  423 ? 25.722  12.732  8.177   1.00 28.78  ? 423 GLU   C O     1 
ATOM   6798  C  CB    . GLU   B 1  423 ? 27.925  10.569  7.102   1.00 21.97  ? 423 GLU   C CB    1 
ATOM   6799  C  CG    . GLU   B 1  423 ? 27.875  9.306   7.961   1.00 40.27  ? 423 GLU   C CG    1 
ATOM   6800  C  CD    . GLU   B 1  423 ? 27.048  9.492   9.254   1.00 58.23  ? 423 GLU   C CD    1 
ATOM   6801  O  OE1   . GLU   B 1  423 ? 26.929  10.658  9.734   1.00 46.19  ? 423 GLU   C OE1   1 
ATOM   6802  O  OE2   . GLU   B 1  423 ? 26.523  8.472   9.789   1.00 47.85  ? 423 GLU   C OE2   1 
ATOM   6803  N  N     . ASP   B 1  424 ? 26.663  13.436  6.273   1.00 28.86  ? 424 ASP   C N     1 
ATOM   6804  C  CA    . ASP   B 1  424 ? 26.214  14.795  6.514   1.00 24.85  ? 424 ASP   C CA    1 
ATOM   6805  C  C     . ASP   B 1  424 ? 24.698  14.816  6.675   1.00 29.10  ? 424 ASP   C C     1 
ATOM   6806  O  O     . ASP   B 1  424 ? 24.182  15.453  7.602   1.00 28.34  ? 424 ASP   C O     1 
ATOM   6807  C  CB    . ASP   B 1  424 ? 26.683  15.710  5.379   1.00 25.38  ? 424 ASP   C CB    1 
ATOM   6808  C  CG    . ASP   B 1  424 ? 26.688  17.172  5.768   1.00 31.97  ? 424 ASP   C CG    1 
ATOM   6809  O  OD1   . ASP   B 1  424 ? 26.593  17.473  6.978   1.00 28.64  ? 424 ASP   C OD1   1 
ATOM   6810  O  OD2   . ASP   B 1  424 ? 26.797  18.020  4.852   1.00 35.82  ? 424 ASP   C OD2   1 
ATOM   6811  N  N     . MET   B 1  425 ? 23.970  14.072  5.819   1.00 24.02  ? 425 MET   C N     1 
ATOM   6812  C  CA    . MET   B 1  425 ? 22.512  13.987  5.943   1.00 26.04  ? 425 MET   C CA    1 
ATOM   6813  C  C     . MET   B 1  425 ? 22.095  13.293  7.234   1.00 28.28  ? 425 MET   C C     1 
ATOM   6814  O  O     . MET   B 1  425 ? 21.079  13.645  7.843   1.00 29.79  ? 425 MET   C O     1 
ATOM   6815  C  CB    . MET   B 1  425 ? 21.908  13.254  4.751   1.00 24.54  ? 425 MET   C CB    1 
ATOM   6816  C  CG    . MET   B 1  425 ? 22.108  13.933  3.411   1.00 29.53  ? 425 MET   C CG    1 
ATOM   6817  S  SD    . MET   B 1  425 ? 21.574  15.644  3.388   1.00 32.37  ? 425 MET   C SD    1 
ATOM   6818  C  CE    . MET   B 1  425 ? 19.816  15.453  3.692   1.00 26.70  ? 425 MET   C CE    1 
ATOM   6819  N  N     . ALA   B 1  426 ? 22.849  12.284  7.650   1.00 25.54  ? 426 ALA   C N     1 
ATOM   6820  C  CA    . ALA   B 1  426 ? 22.607  11.671  8.945   1.00 19.82  ? 426 ALA   C CA    1 
ATOM   6821  C  C     . ALA   B 1  426 ? 22.781  12.695  10.061  1.00 26.16  ? 426 ALA   C C     1 
ATOM   6822  O  O     . ALA   B 1  426 ? 22.028  12.705  11.042  1.00 27.13  ? 426 ALA   C O     1 
ATOM   6823  C  CB    . ALA   B 1  426 ? 23.565  10.487  9.126   1.00 15.80  ? 426 ALA   C CB    1 
ATOM   6824  N  N     . ALA   B 1  427 ? 23.798  13.549  9.933   1.00 24.20  ? 427 ALA   C N     1 
ATOM   6825  C  CA    . ALA   B 1  427 ? 24.015  14.615  10.897  1.00 27.05  ? 427 ALA   C CA    1 
ATOM   6826  C  C     . ALA   B 1  427 ? 22.825  15.565  10.928  1.00 28.75  ? 427 ALA   C C     1 
ATOM   6827  O  O     . ALA   B 1  427 ? 22.334  15.922  12.000  1.00 28.64  ? 427 ALA   C O     1 
ATOM   6828  C  CB    . ALA   B 1  427 ? 25.307  15.363  10.558  1.00 19.39  ? 427 ALA   C CB    1 
ATOM   6829  N  N     . LEU   B 1  428 ? 22.332  15.964  9.753   1.00 28.38  ? 428 LEU   C N     1 
ATOM   6830  C  CA    . LEU   B 1  428 ? 21.266  16.948  9.705   1.00 27.25  ? 428 LEU   C CA    1 
ATOM   6831  C  C     . LEU   B 1  428 ? 19.999  16.415  10.373  1.00 33.39  ? 428 LEU   C C     1 
ATOM   6832  O  O     . LEU   B 1  428 ? 19.338  17.127  11.148  1.00 33.75  ? 428 LEU   C O     1 
ATOM   6833  C  CB    . LEU   B 1  428 ? 21.014  17.352  8.256   1.00 29.23  ? 428 LEU   C CB    1 
ATOM   6834  C  CG    . LEU   B 1  428 ? 20.300  18.674  7.995   1.00 24.07  ? 428 LEU   C CG    1 
ATOM   6835  C  CD1   . LEU   B 1  428 ? 21.166  19.784  8.475   1.00 27.29  ? 428 LEU   C CD1   1 
ATOM   6836  C  CD2   . LEU   B 1  428 ? 20.016  18.847  6.514   1.00 22.54  ? 428 LEU   C CD2   1 
ATOM   6837  N  N     . GLU   B 1  429 ? 19.648  15.161  10.111  1.00 25.74  ? 429 GLU   C N     1 
ATOM   6838  C  CA    . GLU   B 1  429 ? 18.463  14.626  10.771  1.00 30.25  ? 429 GLU   C CA    1 
ATOM   6839  C  C     . GLU   B 1  429 ? 18.679  14.553  12.276  1.00 30.44  ? 429 GLU   C C     1 
ATOM   6840  O  O     . GLU   B 1  429 ? 17.770  14.836  13.064  1.00 34.71  ? 429 GLU   C O     1 
ATOM   6841  C  CB    . GLU   B 1  429 ? 18.099  13.257  10.197  1.00 27.50  ? 429 GLU   C CB    1 
ATOM   6842  C  CG    . GLU   B 1  429 ? 17.618  13.323  8.754   1.00 28.12  ? 429 GLU   C CG    1 
ATOM   6843  C  CD    . GLU   B 1  429 ? 17.124  11.984  8.248   1.00 35.80  ? 429 GLU   C CD    1 
ATOM   6844  O  OE1   . GLU   B 1  429 ? 16.454  11.270  9.025   1.00 30.80  ? 429 GLU   C OE1   1 
ATOM   6845  O  OE2   . GLU   B 1  429 ? 17.416  11.637  7.078   1.00 42.85  ? 429 GLU   C OE2   1 
ATOM   6846  N  N     . LYS   B 1  430 ? 19.893  14.215  12.697  1.00 30.22  ? 430 LYS   C N     1 
ATOM   6847  C  CA    . LYS   B 1  430 ? 20.177  14.204  14.123  1.00 35.94  ? 430 LYS   C CA    1 
ATOM   6848  C  C     . LYS   B 1  430 ? 20.085  15.612  14.716  1.00 35.78  ? 430 LYS   C C     1 
ATOM   6849  O  O     . LYS   B 1  430 ? 19.553  15.789  15.817  1.00 36.99  ? 430 LYS   C O     1 
ATOM   6850  C  CB    . LYS   B 1  430 ? 21.544  13.574  14.369  1.00 27.59  ? 430 LYS   C CB    1 
ATOM   6851  C  CG    . LYS   B 1  430 ? 21.653  12.912  15.703  1.00 38.29  ? 430 LYS   C CG    1 
ATOM   6852  C  CD    . LYS   B 1  430 ? 22.942  12.136  15.830  1.00 48.29  ? 430 LYS   C CD    1 
ATOM   6853  C  CE    . LYS   B 1  430 ? 23.496  12.249  17.246  1.00 65.34  ? 430 LYS   C CE    1 
ATOM   6854  N  NZ    . LYS   B 1  430 ? 23.923  13.654  17.568  1.00 67.42  ? 430 LYS   C NZ    1 
ATOM   6855  N  N     . ASP   B 1  431 ? 20.571  16.627  13.987  1.00 22.80  ? 431 ASP   C N     1 
ATOM   6856  C  CA    . ASP   B 1  431 ? 20.437  18.007  14.439  1.00 23.95  ? 431 ASP   C CA    1 
ATOM   6857  C  C     . ASP   B 1  431 ? 18.970  18.403  14.614  1.00 26.98  ? 431 ASP   C C     1 
ATOM   6858  O  O     . ASP   B 1  431 ? 18.605  19.063  15.590  1.00 23.66  ? 431 ASP   C O     1 
ATOM   6859  C  CB    . ASP   B 1  431 ? 21.110  18.957  13.446  1.00 19.31  ? 431 ASP   C CB    1 
ATOM   6860  C  CG    . ASP   B 1  431 ? 22.564  18.667  13.247  1.00 25.49  ? 431 ASP   C CG    1 
ATOM   6861  O  OD1   . ASP   B 1  431 ? 23.243  18.225  14.202  1.00 32.00  ? 431 ASP   C OD1   1 
ATOM   6862  O  OD2   . ASP   B 1  431 ? 23.036  18.905  12.115  1.00 33.36  ? 431 ASP   C OD2   1 
ATOM   6863  N  N     . TYR   B 1  432 ? 18.115  18.063  13.650  1.00 26.60  ? 432 TYR   C N     1 
ATOM   6864  C  CA    . TYR   B 1  432 ? 16.717  18.434  13.815  1.00 23.84  ? 432 TYR   C CA    1 
ATOM   6865  C  C     . TYR   B 1  432 ? 16.099  17.721  15.017  1.00 26.50  ? 432 TYR   C C     1 
ATOM   6866  O  O     . TYR   B 1  432 ? 15.297  18.316  15.742  1.00 30.36  ? 432 TYR   C O     1 
ATOM   6867  C  CB    . TYR   B 1  432 ? 15.953  18.178  12.515  1.00 29.33  ? 432 TYR   C CB    1 
ATOM   6868  C  CG    . TYR   B 1  432 ? 16.042  19.358  11.556  1.00 28.05  ? 432 TYR   C CG    1 
ATOM   6869  C  CD1   . TYR   B 1  432 ? 15.158  20.412  11.660  1.00 25.89  ? 432 TYR   C CD1   1 
ATOM   6870  C  CD2   . TYR   B 1  432 ? 17.019  19.433  10.578  1.00 29.89  ? 432 TYR   C CD2   1 
ATOM   6871  C  CE1   . TYR   B 1  432 ? 15.231  21.482  10.836  1.00 25.86  ? 432 TYR   C CE1   1 
ATOM   6872  C  CE2   . TYR   B 1  432 ? 17.102  20.538  9.731   1.00 27.19  ? 432 TYR   C CE2   1 
ATOM   6873  C  CZ    . TYR   B 1  432 ? 16.202  21.559  9.870   1.00 25.85  ? 432 TYR   C CZ    1 
ATOM   6874  O  OH    . TYR   B 1  432 ? 16.226  22.678  9.063   1.00 32.88  ? 432 TYR   C OH    1 
ATOM   6875  N  N     . GLU   B 1  433 ? 16.508  16.476  15.283  1.00 28.61  ? 433 GLU   C N     1 
ATOM   6876  C  CA    . GLU   B 1  433 ? 16.111  15.789  16.517  1.00 37.91  ? 433 GLU   C CA    1 
ATOM   6877  C  C     . GLU   B 1  433 ? 16.549  16.561  17.760  1.00 32.66  ? 433 GLU   C C     1 
ATOM   6878  O  O     . GLU   B 1  433 ? 15.745  16.821  18.664  1.00 27.34  ? 433 GLU   C O     1 
ATOM   6879  C  CB    . GLU   B 1  433 ? 16.731  14.394  16.565  1.00 40.25  ? 433 GLU   C CB    1 
ATOM   6880  C  CG    . GLU   B 1  433 ? 15.872  13.213  16.163  1.00 38.75  ? 433 GLU   C CG    1 
ATOM   6881  C  CD    . GLU   B 1  433 ? 16.720  11.939  16.089  1.00 61.43  ? 433 GLU   C CD    1 
ATOM   6882  O  OE1   . GLU   B 1  433 ? 17.330  11.570  17.128  1.00 52.21  ? 433 GLU   C OE1   1 
ATOM   6883  O  OE2   . GLU   B 1  433 ? 16.814  11.341  14.986  1.00 62.00  ? 433 GLU   C OE2   1 
ATOM   6884  N  N     . GLU   B 1  434 ? 17.846  16.873  17.839  1.00 27.32  ? 434 GLU   C N     1 
ATOM   6885  C  CA    . GLU   B 1  434 ? 18.415  17.573  18.983  1.00 32.83  ? 434 GLU   C CA    1 
ATOM   6886  C  C     . GLU   B 1  434 ? 17.697  18.890  19.269  1.00 32.26  ? 434 GLU   C C     1 
ATOM   6887  O  O     . GLU   B 1  434 ? 17.353  19.180  20.425  1.00 32.49  ? 434 GLU   C O     1 
ATOM   6888  C  CB    . GLU   B 1  434 ? 19.914  17.804  18.753  1.00 27.13  ? 434 GLU   C CB    1 
ATOM   6889  C  CG    . GLU   B 1  434 ? 20.696  16.497  18.801  1.00 32.58  ? 434 GLU   C CG    1 
ATOM   6890  C  CD    . GLU   B 1  434 ? 22.213  16.634  18.637  1.00 46.91  ? 434 GLU   C CD    1 
ATOM   6891  O  OE1   . GLU   B 1  434 ? 22.734  17.752  18.380  1.00 44.16  ? 434 GLU   C OE1   1 
ATOM   6892  O  OE2   . GLU   B 1  434 ? 22.886  15.586  18.765  1.00 47.27  ? 434 GLU   C OE2   1 
ATOM   6893  N  N     . VAL   B 1  435 ? 17.458  19.706  18.238  1.00 24.99  ? 435 VAL   C N     1 
ATOM   6894  C  CA    . VAL   B 1  435 ? 16.922  21.035  18.522  1.00 29.33  ? 435 VAL   C CA    1 
ATOM   6895  C  C     . VAL   B 1  435 ? 15.550  20.941  19.167  1.00 25.46  ? 435 VAL   C C     1 
ATOM   6896  O  O     . VAL   B 1  435 ? 15.138  21.852  19.898  1.00 35.81  ? 435 VAL   C O     1 
ATOM   6897  C  CB    . VAL   B 1  435 ? 16.889  21.919  17.253  1.00 25.33  ? 435 VAL   C CB    1 
ATOM   6898  C  CG1   . VAL   B 1  435 ? 18.306  22.204  16.767  1.00 18.55  ? 435 VAL   C CG1   1 
ATOM   6899  C  CG2   . VAL   B 1  435 ? 16.063  21.260  16.149  1.00 29.16  ? 435 VAL   C CG2   1 
ATOM   6900  N  N     . GLY   B 1  436 ? 14.846  19.841  18.952  1.00 23.02  ? 436 GLY   C N     1 
ATOM   6901  C  CA    . GLY   B 1  436 ? 13.477  19.726  19.409  1.00 27.15  ? 436 GLY   C CA    1 
ATOM   6902  C  C     . GLY   B 1  436 ? 13.327  19.147  20.772  1.00 33.69  ? 436 GLY   C C     1 
ATOM   6903  O  O     . GLY   B 1  436 ? 12.242  19.245  21.354  1.00 37.46  ? 436 GLY   C O     1 
ATOM   6904  N  N     . VAL   B 1  437 ? 14.400  18.533  21.280  1.00 27.78  ? 437 VAL   C N     1 
ATOM   6905  C  CA    . VAL   B 1  437 ? 14.425  17.983  22.627  1.00 28.73  ? 437 VAL   C CA    1 
ATOM   6906  C  C     . VAL   B 1  437 ? 14.366  19.105  23.658  1.00 32.73  ? 437 VAL   C C     1 
ATOM   6907  O  O     . VAL   B 1  437 ? 14.994  20.162  23.491  1.00 30.65  ? 437 VAL   C O     1 
ATOM   6908  C  CB    . VAL   B 1  437 ? 15.698  17.140  22.809  1.00 35.83  ? 437 VAL   C CB    1 
ATOM   6909  C  CG1   . VAL   B 1  437 ? 16.037  17.019  24.275  1.00 36.25  ? 437 VAL   C CG1   1 
ATOM   6910  C  CG2   . VAL   B 1  437 ? 15.548  15.763  22.166  1.00 27.86  ? 437 VAL   C CG2   1 
ATOM   6911  N  N     . ASP   B 1  438 ? 13.621  18.873  24.738  1.00 33.87  ? 438 ASP   C N     1 
ATOM   6912  C  CA    . ASP   B 1  438 ? 13.509  19.857  25.808  1.00 39.29  ? 438 ASP   C CA    1 
ATOM   6913  C  C     . ASP   B 1  438 ? 14.830  20.029  26.542  1.00 46.30  ? 438 ASP   C C     1 
ATOM   6914  O  O     . ASP   B 1  438 ? 15.634  19.101  26.645  1.00 39.38  ? 438 ASP   C O     1 
ATOM   6915  C  CB    . ASP   B 1  438 ? 12.431  19.447  26.799  1.00 41.64  ? 438 ASP   C CB    1 
ATOM   6916  C  CG    . ASP   B 1  438 ? 11.043  19.671  26.257  1.00 64.17  ? 438 ASP   C CG    1 
ATOM   6917  O  OD1   . ASP   B 1  438 ? 10.800  20.756  25.675  1.00 61.56  ? 438 ASP   C OD1   1 
ATOM   6918  O  OD2   . ASP   B 1  438 ? 10.198  18.761  26.404  1.00 77.59  ? 438 ASP   C OD2   1 
ATOM   6919  N  N     . SER   B 1  439 ? 15.046  21.234  27.069  1.00 49.98  ? 439 SER   C N     1 
ATOM   6920  C  CA    . SER   B 1  439 ? 16.290  21.547  27.760  1.00 42.52  ? 439 SER   C CA    1 
ATOM   6921  C  C     . SER   B 1  439 ? 16.286  20.978  29.170  1.00 49.37  ? 439 SER   C C     1 
ATOM   6922  O  O     . SER   B 1  439 ? 15.248  20.573  29.706  1.00 51.56  ? 439 SER   C O     1 
ATOM   6923  C  CB    . SER   B 1  439 ? 16.513  23.050  27.823  1.00 39.13  ? 439 SER   C CB    1 
ATOM   6924  O  OG    . SER   B 1  439 ? 16.595  23.588  26.521  1.00 37.53  ? 439 SER   C OG    1 
ATOM   6925  N  N     . VAL   B 1  440 ? 17.468  20.971  29.780  1.00 59.05  ? 440 VAL   C N     1 
ATOM   6926  C  CA    . VAL   B 1  440 ? 17.639  20.403  31.119  1.00 70.02  ? 440 VAL   C CA    1 
ATOM   6927  C  C     . VAL   B 1  440 ? 17.722  21.493  32.189  1.00 59.53  ? 440 VAL   C C     1 
ATOM   6928  O  O     . VAL   B 1  440 ? 18.265  21.272  33.274  1.00 70.69  ? 440 VAL   C O     1 
ATOM   6929  C  CB    . VAL   B 1  440 ? 18.887  19.503  31.178  1.00 71.47  ? 440 VAL   C CB    1 
ATOM   6930  C  CG1   . VAL   B 1  440 ? 18.814  18.392  30.117  1.00 46.76  ? 440 VAL   C CG1   1 
ATOM   6931  C  CG2   . VAL   B 1  440 ? 20.154  20.347  31.028  1.00 72.51  ? 440 VAL   C CG2   1 
ATOM   6932  N  N     . MET   C 2  1   ? 21.546  20.195  -31.130 1.00 87.74  ? 1   MET   D N     1 
ATOM   6933  C  CA    . MET   C 2  1   ? 20.667  19.337  -31.918 1.00 82.56  ? 1   MET   D CA    1 
ATOM   6934  C  C     . MET   C 2  1   ? 21.218  17.902  -31.950 1.00 79.90  ? 1   MET   D C     1 
ATOM   6935  O  O     . MET   C 2  1   ? 21.277  17.274  -33.012 1.00 77.88  ? 1   MET   D O     1 
ATOM   6936  C  CB    . MET   C 2  1   ? 20.512  19.911  -33.326 1.00 75.58  ? 1   MET   D CB    1 
ATOM   6937  C  CG    . MET   C 2  1   ? 20.671  21.427  -33.337 1.00 88.57  ? 1   MET   D CG    1 
ATOM   6938  S  SD    . MET   C 2  1   ? 20.800  22.171  -34.972 1.00 147.44 ? 1   MET   D SD    1 
ATOM   6939  C  CE    . MET   C 2  1   ? 21.407  23.813  -34.570 1.00 110.00 ? 1   MET   D CE    1 
ATOM   6940  N  N     . ARG   C 2  2   ? 21.620  17.414  -30.765 1.00 66.51  ? 2   ARG   D N     1 
ATOM   6941  C  CA    . ARG   C 2  2   ? 22.152  16.073  -30.527 1.00 46.01  ? 2   ARG   D CA    1 
ATOM   6942  C  C     . ARG   C 2  2   ? 21.847  15.093  -31.660 1.00 52.39  ? 2   ARG   D C     1 
ATOM   6943  O  O     . ARG   C 2  2   ? 20.693  14.718  -31.890 1.00 46.28  ? 2   ARG   D O     1 
ATOM   6944  C  CB    . ARG   C 2  2   ? 21.602  15.537  -29.200 1.00 42.93  ? 2   ARG   D CB    1 
ATOM   6945  C  CG    . ARG   C 2  2   ? 21.423  16.581  -28.099 1.00 44.34  ? 2   ARG   D CG    1 
ATOM   6946  C  CD    . ARG   C 2  2   ? 22.740  16.915  -27.388 1.00 48.46  ? 2   ARG   D CD    1 
ATOM   6947  N  NE    . ARG   C 2  2   ? 23.501  15.703  -27.102 1.00 55.29  ? 2   ARG   D NE    1 
ATOM   6948  C  CZ    . ARG   C 2  2   ? 23.421  14.996  -25.979 1.00 53.09  ? 2   ARG   D CZ    1 
ATOM   6949  N  NH1   . ARG   C 2  2   ? 22.707  15.419  -24.943 1.00 47.19  ? 2   ARG   D NH1   1 
ATOM   6950  N  NH2   . ARG   C 2  2   ? 24.067  13.831  -25.897 1.00 43.97  ? 2   ARG   D NH2   1 
ATOM   6951  N  N     . GLU   C 2  3   ? 22.881  14.668  -32.375 1.00 63.16  ? 3   GLU   D N     1 
ATOM   6952  C  CA    . GLU   C 2  3   ? 22.733  13.809  -33.540 1.00 52.43  ? 3   GLU   D CA    1 
ATOM   6953  C  C     . GLU   C 2  3   ? 23.051  12.365  -33.180 1.00 54.17  ? 3   GLU   D C     1 
ATOM   6954  O  O     . GLU   C 2  3   ? 23.983  12.093  -32.414 1.00 52.04  ? 3   GLU   D O     1 
ATOM   6955  C  CB    . GLU   C 2  3   ? 23.659  14.256  -34.672 1.00 48.49  ? 3   GLU   D CB    1 
ATOM   6956  C  CG    . GLU   C 2  3   ? 23.411  15.657  -35.195 1.00 55.03  ? 3   GLU   D CG    1 
ATOM   6957  C  CD    . GLU   C 2  3   ? 24.095  16.740  -34.374 1.00 62.13  ? 3   GLU   D CD    1 
ATOM   6958  O  OE1   . GLU   C 2  3   ? 24.764  16.411  -33.366 1.00 61.29  ? 3   GLU   D OE1   1 
ATOM   6959  O  OE2   . GLU   C 2  3   ? 23.964  17.929  -34.740 1.00 60.56  ? 3   GLU   D OE2   1 
ATOM   6960  N  N     . ILE   C 2  4   ? 22.280  11.441  -33.741 1.00 54.31  ? 4   ILE   D N     1 
ATOM   6961  C  CA    . ILE   C 2  4   ? 22.596  10.022  -33.658 1.00 50.85  ? 4   ILE   D CA    1 
ATOM   6962  C  C     . ILE   C 2  4   ? 23.103  9.577   -35.025 1.00 45.42  ? 4   ILE   D C     1 
ATOM   6963  O  O     . ILE   C 2  4   ? 22.728  10.134  -36.062 1.00 43.08  ? 4   ILE   D O     1 
ATOM   6964  C  CB    . ILE   C 2  4   ? 21.393  9.169   -33.190 1.00 35.01  ? 4   ILE   D CB    1 
ATOM   6965  C  CG1   . ILE   C 2  4   ? 20.884  9.663   -31.831 1.00 38.16  ? 4   ILE   D CG1   1 
ATOM   6966  C  CG2   . ILE   C 2  4   ? 21.800  7.720   -33.086 1.00 38.74  ? 4   ILE   D CG2   1 
ATOM   6967  C  CD1   . ILE   C 2  4   ? 19.653  8.932   -31.279 1.00 32.18  ? 4   ILE   D CD1   1 
ATOM   6968  N  N     . VAL   C 2  5   ? 23.991  8.590   -35.018 1.00 39.90  ? 5   VAL   D N     1 
ATOM   6969  C  CA    . VAL   C 2  5   ? 24.590  8.053   -36.229 1.00 40.89  ? 5   VAL   D CA    1 
ATOM   6970  C  C     . VAL   C 2  5   ? 24.214  6.577   -36.312 1.00 44.64  ? 5   VAL   D C     1 
ATOM   6971  O  O     . VAL   C 2  5   ? 24.585  5.784   -35.434 1.00 43.04  ? 5   VAL   D O     1 
ATOM   6972  C  CB    . VAL   C 2  5   ? 26.116  8.269   -36.250 1.00 43.07  ? 5   VAL   D CB    1 
ATOM   6973  C  CG1   . VAL   C 2  5   ? 26.788  7.453   -37.345 1.00 34.06  ? 5   VAL   D CG1   1 
ATOM   6974  C  CG2   . VAL   C 2  5   ? 26.427  9.739   -36.450 1.00 41.06  ? 5   VAL   D CG2   1 
ATOM   6975  N  N     . HIS   C 2  6   ? 23.456  6.222   -37.357 1.00 52.01  ? 6   HIS   D N     1 
ATOM   6976  C  CA    . HIS   C 2  6   ? 22.962  4.863   -37.568 1.00 44.31  ? 6   HIS   D CA    1 
ATOM   6977  C  C     . HIS   C 2  6   ? 23.922  4.069   -38.440 1.00 45.94  ? 6   HIS   D C     1 
ATOM   6978  O  O     . HIS   C 2  6   ? 24.263  4.490   -39.551 1.00 49.06  ? 6   HIS   D O     1 
ATOM   6979  C  CB    . HIS   C 2  6   ? 21.578  4.875   -38.219 1.00 47.40  ? 6   HIS   D CB    1 
ATOM   6980  C  CG    . HIS   C 2  6   ? 21.078  3.514   -38.596 1.00 51.44  ? 6   HIS   D CG    1 
ATOM   6981  N  ND1   . HIS   C 2  6   ? 20.099  2.856   -37.882 1.00 53.31  ? 6   HIS   D ND1   1 
ATOM   6982  C  CD2   . HIS   C 2  6   ? 21.425  2.684   -39.610 1.00 56.55  ? 6   HIS   D CD2   1 
ATOM   6983  C  CE1   . HIS   C 2  6   ? 19.869  1.678   -38.436 1.00 59.76  ? 6   HIS   D CE1   1 
ATOM   6984  N  NE2   . HIS   C 2  6   ? 20.657  1.550   -39.489 1.00 54.38  ? 6   HIS   D NE2   1 
ATOM   6985  N  N     . ILE   C 2  7   ? 24.333  2.914   -37.931 1.00 48.80  ? 7   ILE   D N     1 
ATOM   6986  C  CA    . ILE   C 2  7   ? 25.187  1.960   -38.622 1.00 48.26  ? 7   ILE   D CA    1 
ATOM   6987  C  C     . ILE   C 2  7   ? 24.406  0.657   -38.650 1.00 51.79  ? 7   ILE   D C     1 
ATOM   6988  O  O     . ILE   C 2  7   ? 24.223  0.023   -37.607 1.00 49.46  ? 7   ILE   D O     1 
ATOM   6989  C  CB    . ILE   C 2  7   ? 26.540  1.768   -37.918 1.00 43.62  ? 7   ILE   D CB    1 
ATOM   6990  C  CG1   . ILE   C 2  7   ? 27.354  3.053   -37.920 1.00 44.27  ? 7   ILE   D CG1   1 
ATOM   6991  C  CG2   . ILE   C 2  7   ? 27.348  0.652   -38.554 1.00 44.29  ? 7   ILE   D CG2   1 
ATOM   6992  C  CD1   . ILE   C 2  7   ? 28.764  2.835   -37.396 1.00 44.76  ? 7   ILE   D CD1   1 
ATOM   6993  N  N     . GLN   C 2  8   ? 23.921  0.270   -39.828 1.00 59.90  ? 8   GLN   D N     1 
ATOM   6994  C  CA    . GLN   C 2  8   ? 23.299  -1.030  -40.049 1.00 50.10  ? 8   GLN   D CA    1 
ATOM   6995  C  C     . GLN   C 2  8   ? 24.255  -1.895  -40.858 1.00 54.53  ? 8   GLN   D C     1 
ATOM   6996  O  O     . GLN   C 2  8   ? 24.825  -1.431  -41.853 1.00 53.88  ? 8   GLN   D O     1 
ATOM   6997  C  CB    . GLN   C 2  8   ? 21.970  -0.880  -40.784 1.00 55.06  ? 8   GLN   D CB    1 
ATOM   6998  C  CG    . GLN   C 2  8   ? 22.107  -0.332  -42.176 1.00 57.00  ? 8   GLN   D CG    1 
ATOM   6999  C  CD    . GLN   C 2  8   ? 20.805  0.223   -42.679 1.00 58.09  ? 8   GLN   D CD    1 
ATOM   7000  O  OE1   . GLN   C 2  8   ? 20.168  1.035   -41.995 1.00 50.25  ? 8   GLN   D OE1   1 
ATOM   7001  N  NE2   . GLN   C 2  8   ? 20.385  -0.215  -43.875 1.00 47.47  ? 8   GLN   D NE2   1 
ATOM   7002  N  N     . ALA   C 2  9   ? 24.430  -3.144  -40.437 1.00 47.60  ? 9   ALA   D N     1 
ATOM   7003  C  CA    . ALA   C 2  9   ? 25.518  -3.957  -40.951 1.00 40.25  ? 9   ALA   D CA    1 
ATOM   7004  C  C     . ALA   C 2  9   ? 25.038  -5.378  -41.136 1.00 48.31  ? 9   ALA   D C     1 
ATOM   7005  O  O     . ALA   C 2  9   ? 24.401  -5.935  -40.242 1.00 53.46  ? 9   ALA   D O     1 
ATOM   7006  C  CB    . ALA   C 2  9   ? 26.725  -3.939  -40.017 1.00 32.98  ? 9   ALA   D CB    1 
ATOM   7007  N  N     . GLY   C 2  10  ? 25.372  -5.963  -42.286 1.00 58.62  ? 10  GLY   D N     1 
ATOM   7008  C  CA    . GLY   C 2  10  ? 24.972  -7.316  -42.600 1.00 55.38  ? 10  GLY   D CA    1 
ATOM   7009  C  C     . GLY   C 2  10  ? 23.609  -7.374  -43.256 1.00 61.75  ? 10  GLY   D C     1 
ATOM   7010  O  O     . GLY   C 2  10  ? 22.938  -6.364  -43.525 1.00 46.10  ? 10  GLY   D O     1 
ATOM   7011  N  N     . GLN   C 2  11  ? 23.198  -8.612  -43.525 1.00 59.38  ? 11  GLN   D N     1 
ATOM   7012  C  CA    . GLN   C 2  11  ? 21.915  -8.829  -44.178 1.00 63.65  ? 11  GLN   D CA    1 
ATOM   7013  C  C     . GLN   C 2  11  ? 20.771  -8.487  -43.234 1.00 65.31  ? 11  GLN   D C     1 
ATOM   7014  O  O     . GLN   C 2  11  ? 19.988  -7.561  -43.487 1.00 57.05  ? 11  GLN   D O     1 
ATOM   7015  C  CB    . GLN   C 2  11  ? 21.828  -10.277 -44.655 1.00 78.37  ? 11  GLN   D CB    1 
ATOM   7016  C  CG    . GLN   C 2  11  ? 21.092  -10.447 -45.969 1.00 89.25  ? 11  GLN   D CG    1 
ATOM   7017  C  CD    . GLN   C 2  11  ? 19.732  -11.071 -45.780 1.00 80.48  ? 11  GLN   D CD    1 
ATOM   7018  O  OE1   . GLN   C 2  11  ? 18.704  -10.420 -46.000 1.00 74.80  ? 11  GLN   D OE1   1 
ATOM   7019  N  NE2   . GLN   C 2  11  ? 19.714  -12.344 -45.368 1.00 62.74  ? 11  GLN   D NE2   1 
ATOM   7020  N  N     . CYS   C 2  12  ? 20.677  -9.216  -42.117 1.00 64.28  ? 12  CYS   D N     1 
ATOM   7021  C  CA    . CYS   C 2  12  ? 19.651  -8.920  -41.125 1.00 60.06  ? 12  CYS   D CA    1 
ATOM   7022  C  C     . CYS   C 2  12  ? 19.666  -7.453  -40.739 1.00 59.91  ? 12  CYS   D C     1 
ATOM   7023  O  O     . CYS   C 2  12  ? 18.632  -6.776  -40.793 1.00 51.26  ? 12  CYS   D O     1 
ATOM   7024  C  CB    . CYS   C 2  12  ? 19.845  -9.775  -39.877 1.00 67.53  ? 12  CYS   D CB    1 
ATOM   7025  S  SG    . CYS   C 2  12  ? 18.770  -9.234  -38.529 1.00 60.52  ? 12  CYS   D SG    1 
ATOM   7026  N  N     . GLY   C 2  13  ? 20.837  -6.955  -40.321 1.00 60.47  ? 13  GLY   D N     1 
ATOM   7027  C  CA    . GLY   C 2  13  ? 20.952  -5.555  -39.946 1.00 49.41  ? 13  GLY   D CA    1 
ATOM   7028  C  C     . GLY   C 2  13  ? 20.398  -4.611  -40.994 1.00 54.34  ? 13  GLY   D C     1 
ATOM   7029  O  O     . GLY   C 2  13  ? 19.638  -3.688  -40.679 1.00 53.15  ? 13  GLY   D O     1 
ATOM   7030  N  N     . ASN   C 2  14  ? 20.764  -4.829  -42.265 1.00 53.44  ? 14  ASN   D N     1 
ATOM   7031  C  CA    . ASN   C 2  14  ? 20.340  -3.905  -43.312 1.00 49.16  ? 14  ASN   D CA    1 
ATOM   7032  C  C     . ASN   C 2  14  ? 18.849  -4.002  -43.591 1.00 56.78  ? 14  ASN   D C     1 
ATOM   7033  O  O     . ASN   C 2  14  ? 18.221  -3.014  -44.004 1.00 45.12  ? 14  ASN   D O     1 
ATOM   7034  C  CB    . ASN   C 2  14  ? 21.129  -4.164  -44.580 1.00 53.74  ? 14  ASN   D CB    1 
ATOM   7035  C  CG    . ASN   C 2  14  ? 22.390  -3.371  -44.633 1.00 51.29  ? 14  ASN   D CG    1 
ATOM   7036  O  OD1   . ASN   C 2  14  ? 22.348  -2.153  -44.800 1.00 53.68  ? 14  ASN   D OD1   1 
ATOM   7037  N  ND2   . ASN   C 2  14  ? 23.528  -4.046  -44.492 1.00 48.22  ? 14  ASN   D ND2   1 
ATOM   7038  N  N     . GLN   C 2  15  ? 18.269  -5.181  -43.373 1.00 61.29  ? 15  GLN   D N     1 
ATOM   7039  C  CA    . GLN   C 2  15  ? 16.836  -5.353  -43.572 1.00 62.02  ? 15  GLN   D CA    1 
ATOM   7040  C  C     . GLN   C 2  15  ? 16.035  -4.549  -42.550 1.00 58.35  ? 15  GLN   D C     1 
ATOM   7041  O  O     . GLN   C 2  15  ? 15.198  -3.707  -42.912 1.00 53.25  ? 15  GLN   D O     1 
ATOM   7042  C  CB    . GLN   C 2  15  ? 16.498  -6.839  -43.505 1.00 67.10  ? 15  GLN   D CB    1 
ATOM   7043  C  CG    . GLN   C 2  15  ? 17.091  -7.625  -44.653 1.00 61.36  ? 15  GLN   D CG    1 
ATOM   7044  C  CD    . GLN   C 2  15  ? 16.313  -7.415  -45.927 1.00 70.67  ? 15  GLN   D CD    1 
ATOM   7045  O  OE1   . GLN   C 2  15  ? 15.323  -6.672  -45.951 1.00 65.41  ? 15  GLN   D OE1   1 
ATOM   7046  N  NE2   . GLN   C 2  15  ? 16.748  -8.073  -46.998 1.00 80.21  ? 15  GLN   D NE2   1 
ATOM   7047  N  N     . ILE   C 2  16  ? 16.285  -4.778  -41.259 1.00 57.44  ? 16  ILE   D N     1 
ATOM   7048  C  CA    . ILE   C 2  16  ? 15.543  -4.023  -40.257 1.00 51.62  ? 16  ILE   D CA    1 
ATOM   7049  C  C     . ILE   C 2  16  ? 15.918  -2.552  -40.325 1.00 48.48  ? 16  ILE   D C     1 
ATOM   7050  O  O     . ILE   C 2  16  ? 15.054  -1.672  -40.226 1.00 49.72  ? 16  ILE   D O     1 
ATOM   7051  C  CB    . ILE   C 2  16  ? 15.746  -4.624  -38.854 1.00 47.46  ? 16  ILE   D CB    1 
ATOM   7052  C  CG1   . ILE   C 2  16  ? 17.169  -4.448  -38.353 1.00 44.81  ? 16  ILE   D CG1   1 
ATOM   7053  C  CG2   . ILE   C 2  16  ? 15.409  -6.118  -38.857 1.00 52.38  ? 16  ILE   D CG2   1 
ATOM   7054  C  CD1   . ILE   C 2  16  ? 17.460  -5.370  -37.168 1.00 44.54  ? 16  ILE   D CD1   1 
ATOM   7055  N  N     . GLY   C 2  17  ? 17.197  -2.256  -40.549 1.00 51.82  ? 17  GLY   D N     1 
ATOM   7056  C  CA    . GLY   C 2  17  ? 17.588  -0.874  -40.767 1.00 53.97  ? 17  GLY   D CA    1 
ATOM   7057  C  C     . GLY   C 2  17  ? 16.772  -0.184  -41.844 1.00 48.62  ? 17  GLY   D C     1 
ATOM   7058  O  O     . GLY   C 2  17  ? 16.503  1.016   -41.755 1.00 52.57  ? 17  GLY   D O     1 
ATOM   7059  N  N     . ALA   C 2  18  ? 16.356  -0.929  -42.867 1.00 57.14  ? 18  ALA   D N     1 
ATOM   7060  C  CA    . ALA   C 2  18  ? 15.609  -0.326  -43.969 1.00 66.69  ? 18  ALA   D CA    1 
ATOM   7061  C  C     . ALA   C 2  18  ? 14.172  -0.014  -43.560 1.00 58.59  ? 18  ALA   D C     1 
ATOM   7062  O  O     . ALA   C 2  18  ? 13.674  1.098   -43.783 1.00 44.20  ? 18  ALA   D O     1 
ATOM   7063  C  CB    . ALA   C 2  18  ? 15.640  -1.257  -45.183 1.00 61.48  ? 18  ALA   D CB    1 
ATOM   7064  N  N     . LYS   C 2  19  ? 13.483  -0.998  -42.980 1.00 58.30  ? 19  LYS   D N     1 
ATOM   7065  C  CA    . LYS   C 2  19  ? 12.124  -0.765  -42.509 1.00 58.10  ? 19  LYS   D CA    1 
ATOM   7066  C  C     . LYS   C 2  19  ? 12.100  0.347   -41.474 1.00 64.78  ? 19  LYS   D C     1 
ATOM   7067  O  O     . LYS   C 2  19  ? 11.235  1.232   -41.517 1.00 63.32  ? 19  LYS   D O     1 
ATOM   7068  C  CB    . LYS   C 2  19  ? 11.545  -2.062  -41.942 1.00 59.20  ? 19  LYS   D CB    1 
ATOM   7069  C  CG    . LYS   C 2  19  ? 10.998  -2.992  -43.016 1.00 67.25  ? 19  LYS   D CG    1 
ATOM   7070  C  CD    . LYS   C 2  19  ? 9.948   -2.263  -43.859 1.00 75.68  ? 19  LYS   D CD    1 
ATOM   7071  C  CE    . LYS   C 2  19  ? 9.489   -3.088  -45.051 1.00 78.61  ? 19  LYS   D CE    1 
ATOM   7072  N  NZ    . LYS   C 2  19  ? 8.650   -2.271  -45.974 1.00 70.89  ? 19  LYS   D NZ    1 
ATOM   7073  N  N     . PHE   C 2  20  ? 13.059  0.326   -40.543 1.00 64.33  ? 20  PHE   D N     1 
ATOM   7074  C  CA    . PHE   C 2  20  ? 13.206  1.421   -39.596 1.00 53.42  ? 20  PHE   D CA    1 
ATOM   7075  C  C     . PHE   C 2  20  ? 13.152  2.762   -40.302 1.00 58.87  ? 20  PHE   D C     1 
ATOM   7076  O  O     . PHE   C 2  20  ? 12.295  3.599   -40.003 1.00 65.93  ? 20  PHE   D O     1 
ATOM   7077  C  CB    . PHE   C 2  20  ? 14.518  1.300   -38.838 1.00 56.43  ? 20  PHE   D CB    1 
ATOM   7078  C  CG    . PHE   C 2  20  ? 14.802  2.482   -37.968 1.00 54.52  ? 20  PHE   D CG    1 
ATOM   7079  C  CD1   . PHE   C 2  20  ? 14.023  2.732   -36.852 1.00 59.16  ? 20  PHE   D CD1   1 
ATOM   7080  C  CD2   . PHE   C 2  20  ? 15.831  3.351   -38.273 1.00 54.58  ? 20  PHE   D CD2   1 
ATOM   7081  C  CE1   . PHE   C 2  20  ? 14.266  3.822   -36.047 1.00 58.72  ? 20  PHE   D CE1   1 
ATOM   7082  C  CE2   . PHE   C 2  20  ? 16.082  4.446   -37.481 1.00 61.90  ? 20  PHE   D CE2   1 
ATOM   7083  C  CZ    . PHE   C 2  20  ? 15.295  4.685   -36.361 1.00 66.21  ? 20  PHE   D CZ    1 
ATOM   7084  N  N     . TRP   C 2  21  ? 14.074  2.985   -41.246 1.00 52.67  ? 21  TRP   D N     1 
ATOM   7085  C  CA    . TRP   C 2  21  ? 14.163  4.297   -41.879 1.00 56.51  ? 21  TRP   D CA    1 
ATOM   7086  C  C     . TRP   C 2  21  ? 12.871  4.640   -42.604 1.00 54.75  ? 21  TRP   D C     1 
ATOM   7087  O  O     . TRP   C 2  21  ? 12.428  5.797   -42.594 1.00 49.18  ? 21  TRP   D O     1 
ATOM   7088  C  CB    . TRP   C 2  21  ? 15.374  4.352   -42.813 1.00 46.84  ? 21  TRP   D CB    1 
ATOM   7089  C  CG    . TRP   C 2  21  ? 16.633  4.624   -42.042 1.00 51.13  ? 21  TRP   D CG    1 
ATOM   7090  C  CD1   . TRP   C 2  21  ? 17.628  3.739   -41.755 1.00 54.94  ? 21  TRP   D CD1   1 
ATOM   7091  C  CD2   . TRP   C 2  21  ? 16.999  5.857   -41.408 1.00 47.67  ? 21  TRP   D CD2   1 
ATOM   7092  N  NE1   . TRP   C 2  21  ? 18.598  4.345   -40.996 1.00 50.51  ? 21  TRP   D NE1   1 
ATOM   7093  C  CE2   . TRP   C 2  21  ? 18.237  5.647   -40.772 1.00 47.93  ? 21  TRP   D CE2   1 
ATOM   7094  C  CE3   . TRP   C 2  21  ? 16.402  7.121   -41.323 1.00 57.60  ? 21  TRP   D CE3   1 
ATOM   7095  C  CZ2   . TRP   C 2  21  ? 18.890  6.651   -40.056 1.00 42.83  ? 21  TRP   D CZ2   1 
ATOM   7096  C  CZ3   . TRP   C 2  21  ? 17.055  8.124   -40.612 1.00 51.44  ? 21  TRP   D CZ3   1 
ATOM   7097  C  CH2   . TRP   C 2  21  ? 18.286  7.878   -39.988 1.00 45.07  ? 21  TRP   D CH2   1 
ATOM   7098  N  N     . GLU   C 2  22  ? 12.230  3.640   -43.206 1.00 63.32  ? 22  GLU   D N     1 
ATOM   7099  C  CA    . GLU   C 2  22  ? 10.938  3.869   -43.838 1.00 66.17  ? 22  GLU   D CA    1 
ATOM   7100  C  C     . GLU   C 2  22  ? 9.958   4.482   -42.845 1.00 60.12  ? 22  GLU   D C     1 
ATOM   7101  O  O     . GLU   C 2  22  ? 9.422   5.570   -43.076 1.00 49.04  ? 22  GLU   D O     1 
ATOM   7102  C  CB    . GLU   C 2  22  ? 10.396  2.554   -44.410 1.00 70.26  ? 22  GLU   D CB    1 
ATOM   7103  C  CG    . GLU   C 2  22  ? 11.163  2.024   -45.620 1.00 82.57  ? 22  GLU   D CG    1 
ATOM   7104  C  CD    . GLU   C 2  22  ? 10.796  0.586   -45.972 1.00 87.63  ? 22  GLU   D CD    1 
ATOM   7105  O  OE1   . GLU   C 2  22  ? 9.795   0.077   -45.418 1.00 86.22  ? 22  GLU   D OE1   1 
ATOM   7106  O  OE2   . GLU   C 2  22  ? 11.515  -0.035  -46.793 1.00 80.10  ? 22  GLU   D OE2   1 
ATOM   7107  N  N     . VAL   C 2  23  ? 9.749   3.803   -41.708 1.00 65.88  ? 23  VAL   D N     1 
ATOM   7108  C  CA    . VAL   C 2  23  ? 8.721   4.208   -40.742 1.00 61.53  ? 23  VAL   D CA    1 
ATOM   7109  C  C     . VAL   C 2  23  ? 8.962   5.631   -40.245 1.00 61.76  ? 23  VAL   D C     1 
ATOM   7110  O  O     . VAL   C 2  23  ? 8.101   6.507   -40.395 1.00 64.23  ? 23  VAL   D O     1 
ATOM   7111  C  CB    . VAL   C 2  23  ? 8.659   3.218   -39.566 1.00 63.68  ? 23  VAL   D CB    1 
ATOM   7112  C  CG1   . VAL   C 2  23  ? 7.377   3.427   -38.773 1.00 60.67  ? 23  VAL   D CG1   1 
ATOM   7113  C  CG2   . VAL   C 2  23  ? 8.765   1.795   -40.070 1.00 58.45  ? 23  VAL   D CG2   1 
ATOM   7114  N  N     . ILE   C 2  24  ? 10.120  5.885   -39.619 1.00 60.48  ? 24  ILE   D N     1 
ATOM   7115  C  CA    . ILE   C 2  24  ? 10.311  7.204   -39.005 1.00 62.91  ? 24  ILE   D CA    1 
ATOM   7116  C  C     . ILE   C 2  24  ? 10.269  8.289   -40.069 1.00 54.74  ? 24  ILE   D C     1 
ATOM   7117  O  O     . ILE   C 2  24  ? 9.855   9.419   -39.793 1.00 57.10  ? 24  ILE   D O     1 
ATOM   7118  C  CB    . ILE   C 2  24  ? 11.607  7.287   -38.155 1.00 54.88  ? 24  ILE   D CB    1 
ATOM   7119  C  CG1   . ILE   C 2  24  ? 12.779  7.835   -38.962 1.00 55.52  ? 24  ILE   D CG1   1 
ATOM   7120  C  CG2   . ILE   C 2  24  ? 11.994  5.928   -37.529 1.00 46.59  ? 24  ILE   D CG2   1 
ATOM   7121  C  CD1   . ILE   C 2  24  ? 14.107  7.677   -38.238 1.00 52.08  ? 24  ILE   D CD1   1 
ATOM   7122  N  N     . SER   C 2  25  ? 10.672  7.968   -41.302 1.00 64.25  ? 25  SER   D N     1 
ATOM   7123  C  CA    . SER   C 2  25  ? 10.477  8.899   -42.415 1.00 64.48  ? 25  SER   D CA    1 
ATOM   7124  C  C     . SER   C 2  25  ? 8.999   9.225   -42.589 1.00 65.96  ? 25  SER   D C     1 
ATOM   7125  O  O     . SER   C 2  25  ? 8.607   10.397  -42.660 1.00 66.70  ? 25  SER   D O     1 
ATOM   7126  C  CB    . SER   C 2  25  ? 11.041  8.307   -43.708 1.00 58.65  ? 25  SER   D CB    1 
ATOM   7127  O  OG    . SER   C 2  25  ? 12.442  8.424   -43.765 1.00 56.22  ? 25  SER   D OG    1 
ATOM   7128  N  N     . ASP   C 2  26  ? 8.171   8.185   -42.688 1.00 62.78  ? 26  ASP   D N     1 
ATOM   7129  C  CA    . ASP   C 2  26  ? 6.723   8.288   -42.612 1.00 58.79  ? 26  ASP   D CA    1 
ATOM   7130  C  C     . ASP   C 2  26  ? 6.314   9.243   -41.493 1.00 69.72  ? 26  ASP   D C     1 
ATOM   7131  O  O     . ASP   C 2  26  ? 5.822   10.345  -41.767 1.00 70.60  ? 26  ASP   D O     1 
ATOM   7132  C  CB    . ASP   C 2  26  ? 6.135   6.889   -42.409 1.00 63.42  ? 26  ASP   D CB    1 
ATOM   7133  C  CG    . ASP   C 2  26  ? 4.719   6.911   -41.870 1.00 78.60  ? 26  ASP   D CG    1 
ATOM   7134  O  OD1   . ASP   C 2  26  ? 3.860   7.570   -42.503 1.00 77.86  ? 26  ASP   D OD1   1 
ATOM   7135  O  OD2   . ASP   C 2  26  ? 4.468   6.247   -40.830 1.00 68.59  ? 26  ASP   D OD2   1 
ATOM   7136  N  N     . GLU   C 2  27  ? 6.547   8.845   -40.235 1.00 56.68  ? 27  GLU   D N     1 
ATOM   7137  C  CA    . GLU   C 2  27  ? 6.142   9.661   -39.093 1.00 59.08  ? 27  GLU   D CA    1 
ATOM   7138  C  C     . GLU   C 2  27  ? 6.562   11.123  -39.263 1.00 65.73  ? 27  GLU   D C     1 
ATOM   7139  O  O     . GLU   C 2  27  ? 5.732   12.036  -39.176 1.00 64.87  ? 27  GLU   D O     1 
ATOM   7140  C  CB    . GLU   C 2  27  ? 6.720   9.066   -37.803 1.00 54.92  ? 27  GLU   D CB    1 
ATOM   7141  C  CG    . GLU   C 2  27  ? 6.225   7.659   -37.516 1.00 53.64  ? 27  GLU   D CG    1 
ATOM   7142  C  CD    . GLU   C 2  27  ? 6.720   7.100   -36.194 1.00 59.37  ? 27  GLU   D CD    1 
ATOM   7143  O  OE1   . GLU   C 2  27  ? 7.312   7.853   -35.376 1.00 56.00  ? 27  GLU   D OE1   1 
ATOM   7144  O  OE2   . GLU   C 2  27  ? 6.502   5.892   -35.971 1.00 52.99  ? 27  GLU   D OE2   1 
ATOM   7145  N  N     . HIS   C 2  28  ? 7.848   11.365  -39.524 1.00 60.18  ? 28  HIS   D N     1 
ATOM   7146  C  CA    . HIS   C 2  28  ? 8.334   12.733  -39.649 1.00 62.93  ? 28  HIS   D CA    1 
ATOM   7147  C  C     . HIS   C 2  28  ? 7.905   13.415  -40.936 1.00 64.59  ? 28  HIS   D C     1 
ATOM   7148  O  O     . HIS   C 2  28  ? 8.071   14.636  -41.050 1.00 54.76  ? 28  HIS   D O     1 
ATOM   7149  C  CB    . HIS   C 2  28  ? 9.850   12.750  -39.551 1.00 63.67  ? 28  HIS   D CB    1 
ATOM   7150  C  CG    . HIS   C 2  28  ? 10.349  12.375  -38.199 1.00 58.39  ? 28  HIS   D CG    1 
ATOM   7151  N  ND1   . HIS   C 2  28  ? 10.436  13.281  -37.168 1.00 50.33  ? 28  HIS   D ND1   1 
ATOM   7152  C  CD2   . HIS   C 2  28  ? 10.753  11.185  -37.695 1.00 57.03  ? 28  HIS   D CD2   1 
ATOM   7153  C  CE1   . HIS   C 2  28  ? 10.893  12.669  -36.091 1.00 62.65  ? 28  HIS   D CE1   1 
ATOM   7154  N  NE2   . HIS   C 2  28  ? 11.091  11.396  -36.384 1.00 54.69  ? 28  HIS   D NE2   1 
ATOM   7155  N  N     . GLY   C 2  29  ? 7.380   12.667  -41.902 1.00 67.14  ? 29  GLY   D N     1 
ATOM   7156  C  CA    . GLY   C 2  29  ? 6.919   13.259  -43.140 1.00 71.91  ? 29  GLY   D CA    1 
ATOM   7157  C  C     . GLY   C 2  29  ? 8.028   13.632  -44.102 1.00 75.71  ? 29  GLY   D C     1 
ATOM   7158  O  O     . GLY   C 2  29  ? 8.060   14.761  -44.601 1.00 79.54  ? 29  GLY   D O     1 
ATOM   7159  N  N     . ILE   C 2  30  ? 8.947   12.705  -44.365 1.00 66.31  ? 30  ILE   D N     1 
ATOM   7160  C  CA    . ILE   C 2  30  ? 9.947   12.864  -45.414 1.00 77.51  ? 30  ILE   D CA    1 
ATOM   7161  C  C     . ILE   C 2  30  ? 9.703   11.772  -46.448 1.00 81.02  ? 30  ILE   D C     1 
ATOM   7162  O  O     . ILE   C 2  30  ? 9.666   10.582  -46.105 1.00 70.64  ? 30  ILE   D O     1 
ATOM   7163  C  CB    . ILE   C 2  30  ? 11.381  12.801  -44.864 1.00 72.07  ? 30  ILE   D CB    1 
ATOM   7164  C  CG1   . ILE   C 2  30  ? 11.649  13.983  -43.940 1.00 68.87  ? 30  ILE   D CG1   1 
ATOM   7165  C  CG2   . ILE   C 2  30  ? 12.390  12.820  -45.988 1.00 75.60  ? 30  ILE   D CG2   1 
ATOM   7166  C  CD1   . ILE   C 2  30  ? 11.214  13.746  -42.528 1.00 63.47  ? 30  ILE   D CD1   1 
ATOM   7167  N  N     . ASP   C 2  31  ? 9.521   12.173  -47.704 1.00 80.80  ? 31  ASP   D N     1 
ATOM   7168  C  CA    . ASP   C 2  31  ? 9.309   11.212  -48.780 1.00 90.23  ? 31  ASP   D CA    1 
ATOM   7169  C  C     . ASP   C 2  31  ? 10.644  10.637  -49.247 1.00 94.93  ? 31  ASP   D C     1 
ATOM   7170  O  O     . ASP   C 2  31  ? 11.719  11.095  -48.848 1.00 92.19  ? 31  ASP   D O     1 
ATOM   7171  C  CB    . ASP   C 2  31  ? 8.550   11.871  -49.932 1.00 78.33  ? 31  ASP   D CB    1 
ATOM   7172  C  CG    . ASP   C 2  31  ? 9.354   12.959  -50.627 1.00 86.36  ? 31  ASP   D CG    1 
ATOM   7173  O  OD1   . ASP   C 2  31  ? 10.514  12.699  -51.010 1.00 85.32  ? 31  ASP   D OD1   1 
ATOM   7174  O  OD2   . ASP   C 2  31  ? 8.819   14.072  -50.815 1.00 81.42  ? 31  ASP   D OD2   1 
ATOM   7175  N  N     . PRO   C 2  32  ? 10.614  9.618   -50.111 1.00 90.54  ? 32  PRO   D N     1 
ATOM   7176  C  CA    . PRO   C 2  32  ? 11.869  8.962   -50.510 1.00 95.31  ? 32  PRO   D CA    1 
ATOM   7177  C  C     . PRO   C 2  32  ? 12.793  9.844   -51.338 1.00 92.36  ? 32  PRO   D C     1 
ATOM   7178  O  O     . PRO   C 2  32  ? 13.722  9.329   -51.967 1.00 100.52 ? 32  PRO   D O     1 
ATOM   7179  C  CB    . PRO   C 2  32  ? 11.390  7.747   -51.318 1.00 92.37  ? 32  PRO   D CB    1 
ATOM   7180  C  CG    . PRO   C 2  32  ? 9.991   7.505   -50.841 1.00 89.36  ? 32  PRO   D CG    1 
ATOM   7181  C  CD    . PRO   C 2  32  ? 9.431   8.868   -50.563 1.00 83.84  ? 32  PRO   D CD    1 
ATOM   7182  N  N     . THR   C 2  33  ? 12.564  11.162  -51.346 1.00 88.95  ? 33  THR   D N     1 
ATOM   7183  C  CA    . THR   C 2  33  ? 13.411  12.104  -52.076 1.00 91.15  ? 33  THR   D CA    1 
ATOM   7184  C  C     . THR   C 2  33  ? 13.959  13.203  -51.171 1.00 94.10  ? 33  THR   D C     1 
ATOM   7185  O  O     . THR   C 2  33  ? 14.414  14.245  -51.670 1.00 79.56  ? 33  THR   D O     1 
ATOM   7186  C  CB    . THR   C 2  33  ? 12.649  12.732  -53.247 1.00 90.49  ? 33  THR   D CB    1 
ATOM   7187  O  OG1   . THR   C 2  33  ? 12.186  14.044  -52.884 1.00 76.27  ? 33  THR   D OG1   1 
ATOM   7188  C  CG2   . THR   C 2  33  ? 11.464  11.861  -53.632 1.00 87.46  ? 33  THR   D CG2   1 
ATOM   7189  N  N     . GLY   C 2  34  ? 13.916  12.995  -49.852 1.00 92.05  ? 34  GLY   D N     1 
ATOM   7190  C  CA    . GLY   C 2  34  ? 14.358  14.003  -48.907 1.00 84.80  ? 34  GLY   D CA    1 
ATOM   7191  C  C     . GLY   C 2  34  ? 13.492  15.242  -48.835 1.00 80.29  ? 34  GLY   D C     1 
ATOM   7192  O  O     . GLY   C 2  34  ? 13.976  16.302  -48.430 1.00 76.08  ? 34  GLY   D O     1 
ATOM   7193  N  N     . SER   C 2  35  ? 12.224  15.145  -49.227 1.00 85.10  ? 35  SER   D N     1 
ATOM   7194  C  CA    . SER   C 2  35  ? 11.284  16.256  -49.147 1.00 83.50  ? 35  SER   D CA    1 
ATOM   7195  C  C     . SER   C 2  35  ? 10.360  16.054  -47.952 1.00 77.27  ? 35  SER   D C     1 
ATOM   7196  O  O     . SER   C 2  35  ? 9.972   14.924  -47.633 1.00 81.63  ? 35  SER   D O     1 
ATOM   7197  C  CB    . SER   C 2  35  ? 10.456  16.383  -50.437 1.00 82.98  ? 35  SER   D CB    1 
ATOM   7198  O  OG    . SER   C 2  35  ? 11.250  16.749  -51.561 1.00 65.18  ? 35  SER   D OG    1 
ATOM   7199  N  N     . TYR   C 2  36  ? 10.018  17.152  -47.286 1.00 73.99  ? 36  TYR   D N     1 
ATOM   7200  C  CA    . TYR   C 2  36  ? 9.104   17.098  -46.147 1.00 77.27  ? 36  TYR   D CA    1 
ATOM   7201  C  C     . TYR   C 2  36  ? 7.684   17.306  -46.663 1.00 79.39  ? 36  TYR   D C     1 
ATOM   7202  O  O     . TYR   C 2  36  ? 7.263   18.433  -46.940 1.00 75.19  ? 36  TYR   D O     1 
ATOM   7203  C  CB    . TYR   C 2  36  ? 9.491   18.124  -45.090 1.00 71.45  ? 36  TYR   D CB    1 
ATOM   7204  C  CG    . TYR   C 2  36  ? 8.449   18.323  -44.010 1.00 75.03  ? 36  TYR   D CG    1 
ATOM   7205  C  CD1   . TYR   C 2  36  ? 8.108   17.294  -43.147 1.00 71.51  ? 36  TYR   D CD1   1 
ATOM   7206  C  CD2   . TYR   C 2  36  ? 7.821   19.551  -43.844 1.00 76.58  ? 36  TYR   D CD2   1 
ATOM   7207  C  CE1   . TYR   C 2  36  ? 7.162   17.482  -42.162 1.00 77.39  ? 36  TYR   D CE1   1 
ATOM   7208  C  CE2   . TYR   C 2  36  ? 6.877   19.747  -42.863 1.00 70.98  ? 36  TYR   D CE2   1 
ATOM   7209  C  CZ    . TYR   C 2  36  ? 6.546   18.711  -42.029 1.00 72.85  ? 36  TYR   D CZ    1 
ATOM   7210  O  OH    . TYR   C 2  36  ? 5.599   18.910  -41.054 1.00 74.44  ? 36  TYR   D OH    1 
ATOM   7211  N  N     . HIS   C 2  37  ? 6.953   16.202  -46.812 1.00 81.77  ? 37  HIS   D N     1 
ATOM   7212  C  CA    . HIS   C 2  37  ? 5.545   16.228  -47.183 1.00 79.69  ? 37  HIS   D CA    1 
ATOM   7213  C  C     . HIS   C 2  37  ? 4.679   15.906  -45.974 1.00 82.83  ? 37  HIS   D C     1 
ATOM   7214  O  O     . HIS   C 2  37  ? 3.937   14.919  -45.984 1.00 84.61  ? 37  HIS   D O     1 
ATOM   7215  C  CB    . HIS   C 2  37  ? 5.266   15.238  -48.316 1.00 85.21  ? 37  HIS   D CB    1 
ATOM   7216  C  CG    . HIS   C 2  37  ? 5.707   15.727  -49.663 1.00 98.26  ? 37  HIS   D CG    1 
ATOM   7217  N  ND1   . HIS   C 2  37  ? 5.350   15.100  -50.838 1.00 106.20 ? 37  HIS   D ND1   1 
ATOM   7218  C  CD2   . HIS   C 2  37  ? 6.471   16.787  -50.021 1.00 91.28  ? 37  HIS   D CD2   1 
ATOM   7219  C  CE1   . HIS   C 2  37  ? 5.876   15.750  -51.861 1.00 99.23  ? 37  HIS   D CE1   1 
ATOM   7220  N  NE2   . HIS   C 2  37  ? 6.562   16.778  -51.392 1.00 94.48  ? 37  HIS   D NE2   1 
ATOM   7221  N  N     . GLY   C 2  38  ? 4.785   16.726  -44.926 1.00 85.45  ? 38  GLY   D N     1 
ATOM   7222  C  CA    . GLY   C 2  38  ? 4.032   16.549  -43.697 1.00 78.68  ? 38  GLY   D CA    1 
ATOM   7223  C  C     . GLY   C 2  38  ? 3.322   17.824  -43.301 1.00 72.96  ? 38  GLY   D C     1 
ATOM   7224  O  O     . GLY   C 2  38  ? 3.294   18.775  -44.088 1.00 88.16  ? 38  GLY   D O     1 
ATOM   7225  N  N     . ASP   C 2  39  ? 2.766   17.884  -42.087 1.00 76.39  ? 39  ASP   D N     1 
ATOM   7226  C  CA    . ASP   C 2  39  ? 1.883   18.992  -41.742 1.00 80.16  ? 39  ASP   D CA    1 
ATOM   7227  C  C     . ASP   C 2  39  ? 2.115   19.626  -40.372 1.00 78.62  ? 39  ASP   D C     1 
ATOM   7228  O  O     . ASP   C 2  39  ? 1.447   20.620  -40.062 1.00 75.45  ? 39  ASP   D O     1 
ATOM   7229  C  CB    . ASP   C 2  39  ? 0.418   18.529  -41.832 1.00 79.06  ? 39  ASP   D CB    1 
ATOM   7230  C  CG    . ASP   C 2  39  ? 0.057   17.502  -40.761 1.00 77.62  ? 39  ASP   D CG    1 
ATOM   7231  O  OD1   . ASP   C 2  39  ? 0.928   17.162  -39.925 1.00 70.34  ? 39  ASP   D OD1   1 
ATOM   7232  O  OD2   . ASP   C 2  39  ? -1.106  17.040  -40.754 1.00 62.00  ? 39  ASP   D OD2   1 
ATOM   7233  N  N     . SER   C 2  40  ? 3.023   19.105  -39.545 1.00 76.81  ? 40  SER   D N     1 
ATOM   7234  C  CA    . SER   C 2  40  ? 3.142   19.557  -38.162 1.00 82.93  ? 40  SER   D CA    1 
ATOM   7235  C  C     . SER   C 2  40  ? 4.592   19.853  -37.803 1.00 79.95  ? 40  SER   D C     1 
ATOM   7236  O  O     . SER   C 2  40  ? 5.469   19.006  -38.004 1.00 74.56  ? 40  SER   D O     1 
ATOM   7237  C  CB    . SER   C 2  40  ? 2.580   18.512  -37.194 1.00 69.91  ? 40  SER   D CB    1 
ATOM   7238  O  OG    . SER   C 2  40  ? 2.783   18.929  -35.856 1.00 74.38  ? 40  SER   D OG    1 
ATOM   7239  N  N     . ASP   C 2  41  ? 4.833   21.044  -37.239 1.00 71.78  ? 41  ASP   D N     1 
ATOM   7240  C  CA    . ASP   C 2  41  ? 6.172   21.401  -36.780 1.00 69.36  ? 41  ASP   D CA    1 
ATOM   7241  C  C     . ASP   C 2  41  ? 6.736   20.383  -35.795 1.00 79.02  ? 41  ASP   D C     1 
ATOM   7242  O  O     . ASP   C 2  41  ? 7.960   20.301  -35.634 1.00 76.74  ? 41  ASP   D O     1 
ATOM   7243  C  CB    . ASP   C 2  41  ? 6.159   22.788  -36.139 1.00 74.88  ? 41  ASP   D CB    1 
ATOM   7244  C  CG    . ASP   C 2  41  ? 6.341   23.911  -37.151 1.00 78.20  ? 41  ASP   D CG    1 
ATOM   7245  O  OD1   . ASP   C 2  41  ? 7.235   23.797  -38.022 1.00 69.24  ? 41  ASP   D OD1   1 
ATOM   7246  O  OD2   . ASP   C 2  41  ? 5.596   24.914  -37.062 1.00 66.64  ? 41  ASP   D OD2   1 
ATOM   7247  N  N     . LEU   C 2  42  ? 5.869   19.613  -35.132 1.00 76.14  ? 42  LEU   D N     1 
ATOM   7248  C  CA    . LEU   C 2  42  ? 6.319   18.529  -34.268 1.00 67.77  ? 42  LEU   D CA    1 
ATOM   7249  C  C     . LEU   C 2  42  ? 7.081   17.453  -35.033 1.00 72.03  ? 42  LEU   D C     1 
ATOM   7250  O  O     . LEU   C 2  42  ? 7.879   16.724  -34.432 1.00 71.99  ? 42  LEU   D O     1 
ATOM   7251  C  CB    . LEU   C 2  42  ? 5.119   17.911  -33.554 1.00 64.94  ? 42  LEU   D CB    1 
ATOM   7252  C  CG    . LEU   C 2  42  ? 5.131   18.073  -32.037 1.00 65.82  ? 42  LEU   D CG    1 
ATOM   7253  C  CD1   . LEU   C 2  42  ? 5.778   19.394  -31.640 1.00 67.77  ? 42  LEU   D CD1   1 
ATOM   7254  C  CD2   . LEU   C 2  42  ? 3.721   18.002  -31.517 1.00 68.48  ? 42  LEU   D CD2   1 
ATOM   7255  N  N     . GLN   C 2  43  ? 6.840   17.313  -36.336 1.00 70.75  ? 45  GLN   D N     1 
ATOM   7256  C  CA    . GLN   C 2  43  ? 7.635   16.377  -37.118 1.00 69.04  ? 45  GLN   D CA    1 
ATOM   7257  C  C     . GLN   C 2  43  ? 9.037   16.909  -37.375 1.00 61.13  ? 45  GLN   D C     1 
ATOM   7258  O  O     . GLN   C 2  43  ? 9.942   16.131  -37.689 1.00 55.88  ? 45  GLN   D O     1 
ATOM   7259  C  CB    . GLN   C 2  43  ? 6.944   16.077  -38.448 1.00 66.50  ? 45  GLN   D CB    1 
ATOM   7260  C  CG    . GLN   C 2  43  ? 5.584   15.408  -38.336 1.00 59.69  ? 45  GLN   D CG    1 
ATOM   7261  C  CD    . GLN   C 2  43  ? 4.763   15.555  -39.614 1.00 66.19  ? 45  GLN   D CD    1 
ATOM   7262  O  OE1   . GLN   C 2  43  ? 4.713   16.629  -40.212 1.00 73.79  ? 45  GLN   D OE1   1 
ATOM   7263  N  NE2   . GLN   C 2  43  ? 4.127   14.475  -40.038 1.00 61.31  ? 45  GLN   D NE2   1 
ATOM   7264  N  N     . LEU   C 2  44  ? 9.238   18.213  -37.240 1.00 59.69  ? 46  LEU   D N     1 
ATOM   7265  C  CA    . LEU   C 2  44  ? 10.493  18.840  -37.609 1.00 62.74  ? 46  LEU   D CA    1 
ATOM   7266  C  C     . LEU   C 2  44  ? 11.351  19.235  -36.420 1.00 68.71  ? 46  LEU   D C     1 
ATOM   7267  O  O     . LEU   C 2  44  ? 12.577  19.155  -36.514 1.00 60.40  ? 46  LEU   D O     1 
ATOM   7268  C  CB    . LEU   C 2  44  ? 10.227  20.085  -38.469 1.00 62.87  ? 46  LEU   D CB    1 
ATOM   7269  C  CG    . LEU   C 2  44  ? 10.474  20.051  -39.987 1.00 68.05  ? 46  LEU   D CG    1 
ATOM   7270  C  CD1   . LEU   C 2  44  ? 10.484  18.641  -40.595 1.00 64.51  ? 46  LEU   D CD1   1 
ATOM   7271  C  CD2   . LEU   C 2  44  ? 9.441   20.919  -40.683 1.00 73.97  ? 46  LEU   D CD2   1 
ATOM   7272  N  N     . GLU   C 2  45  ? 10.741  19.636  -35.301 1.00 68.41  ? 47  GLU   D N     1 
ATOM   7273  C  CA    . GLU   C 2  45  ? 11.480  20.262  -34.211 1.00 64.98  ? 47  GLU   D CA    1 
ATOM   7274  C  C     . GLU   C 2  45  ? 12.783  19.523  -33.920 1.00 64.18  ? 47  GLU   D C     1 
ATOM   7275  O  O     . GLU   C 2  45  ? 13.835  20.154  -33.757 1.00 59.14  ? 47  GLU   D O     1 
ATOM   7276  C  CB    . GLU   C 2  45  ? 10.613  20.349  -32.947 1.00 68.21  ? 47  GLU   D CB    1 
ATOM   7277  C  CG    . GLU   C 2  45  ? 10.749  21.685  -32.185 1.00 71.63  ? 47  GLU   D CG    1 
ATOM   7278  C  CD    . GLU   C 2  45  ? 10.021  21.696  -30.845 1.00 74.40  ? 47  GLU   D CD    1 
ATOM   7279  O  OE1   . GLU   C 2  45  ? 9.385   20.682  -30.494 1.00 75.81  ? 47  GLU   D OE1   1 
ATOM   7280  O  OE2   . GLU   C 2  45  ? 10.087  22.721  -30.136 1.00 77.65  ? 47  GLU   D OE2   1 
ATOM   7281  N  N     . ARG   C 2  46  ? 12.735  18.189  -33.877 1.00 57.66  ? 48  ARG   D N     1 
ATOM   7282  C  CA    . ARG   C 2  46  ? 13.908  17.381  -33.554 1.00 56.61  ? 48  ARG   D CA    1 
ATOM   7283  C  C     . ARG   C 2  46  ? 14.289  16.441  -34.695 1.00 64.17  ? 48  ARG   D C     1 
ATOM   7284  O  O     . ARG   C 2  46  ? 14.765  15.324  -34.463 1.00 54.09  ? 48  ARG   D O     1 
ATOM   7285  C  CB    . ARG   C 2  46  ? 13.676  16.599  -32.264 1.00 53.90  ? 48  ARG   D CB    1 
ATOM   7286  C  CG    . ARG   C 2  46  ? 13.523  17.501  -31.056 1.00 52.78  ? 48  ARG   D CG    1 
ATOM   7287  C  CD    . ARG   C 2  46  ? 14.281  16.953  -29.906 1.00 47.97  ? 48  ARG   D CD    1 
ATOM   7288  N  NE    . ARG   C 2  46  ? 13.656  15.728  -29.430 1.00 57.80  ? 48  ARG   D NE    1 
ATOM   7289  C  CZ    . ARG   C 2  46  ? 14.188  14.929  -28.515 1.00 57.93  ? 48  ARG   D CZ    1 
ATOM   7290  N  NH1   . ARG   C 2  46  ? 15.382  15.172  -28.000 1.00 49.56  ? 48  ARG   D NH1   1 
ATOM   7291  N  NH2   . ARG   C 2  46  ? 13.501  13.862  -28.105 1.00 52.99  ? 48  ARG   D NH2   1 
ATOM   7292  N  N     . ILE   C 2  47  ? 14.095  16.900  -35.938 1.00 63.03  ? 49  ILE   D N     1 
ATOM   7293  C  CA    . ILE   C 2  47  ? 14.375  16.076  -37.111 1.00 52.54  ? 49  ILE   D CA    1 
ATOM   7294  C  C     . ILE   C 2  47  ? 15.866  15.835  -37.254 1.00 59.08  ? 49  ILE   D C     1 
ATOM   7295  O  O     . ILE   C 2  47  ? 16.292  14.848  -37.868 1.00 51.68  ? 49  ILE   D O     1 
ATOM   7296  C  CB    . ILE   C 2  47  ? 13.805  16.741  -38.373 1.00 56.11  ? 49  ILE   D CB    1 
ATOM   7297  C  CG1   . ILE   C 2  47  ? 13.734  15.720  -39.504 1.00 47.23  ? 49  ILE   D CG1   1 
ATOM   7298  C  CG2   . ILE   C 2  47  ? 14.662  17.953  -38.775 1.00 53.25  ? 49  ILE   D CG2   1 
ATOM   7299  C  CD1   . ILE   C 2  47  ? 13.025  14.465  -39.099 1.00 44.54  ? 49  ILE   D CD1   1 
ATOM   7300  N  N     . ASN   C 2  48  ? 16.686  16.737  -36.724 1.00 58.03  ? 50  ASN   D N     1 
ATOM   7301  C  CA    . ASN   C 2  48  ? 18.124  16.655  -36.913 1.00 52.94  ? 50  ASN   D CA    1 
ATOM   7302  C  C     . ASN   C 2  48  ? 18.780  15.626  -36.006 1.00 58.36  ? 50  ASN   D C     1 
ATOM   7303  O  O     . ASN   C 2  48  ? 20.006  15.498  -36.043 1.00 63.25  ? 50  ASN   D O     1 
ATOM   7304  C  CB    . ASN   C 2  48  ? 18.745  18.040  -36.711 1.00 74.37  ? 50  ASN   D CB    1 
ATOM   7305  C  CG    . ASN   C 2  48  ? 18.486  18.978  -37.905 1.00 92.24  ? 50  ASN   D CG    1 
ATOM   7306  O  OD1   . ASN   C 2  48  ? 17.359  19.459  -38.121 1.00 78.72  ? 50  ASN   D OD1   1 
ATOM   7307  N  ND2   . ASN   C 2  48  ? 19.533  19.235  -38.686 1.00 94.97  ? 50  ASN   D ND2   1 
ATOM   7308  N  N     . VAL   C 2  49  ? 18.003  14.874  -35.219 1.00 55.89  ? 51  VAL   D N     1 
ATOM   7309  C  CA    . VAL   C 2  49  ? 18.577  13.797  -34.415 1.00 47.10  ? 51  VAL   D CA    1 
ATOM   7310  C  C     . VAL   C 2  49  ? 18.980  12.629  -35.300 1.00 47.00  ? 51  VAL   D C     1 
ATOM   7311  O  O     . VAL   C 2  49  ? 20.048  12.032  -35.112 1.00 50.59  ? 51  VAL   D O     1 
ATOM   7312  C  CB    . VAL   C 2  49  ? 17.598  13.341  -33.316 1.00 46.39  ? 51  VAL   D CB    1 
ATOM   7313  C  CG1   . VAL   C 2  49  ? 18.061  12.015  -32.730 1.00 34.78  ? 51  VAL   D CG1   1 
ATOM   7314  C  CG2   . VAL   C 2  49  ? 17.484  14.386  -32.224 1.00 42.47  ? 51  VAL   D CG2   1 
ATOM   7315  N  N     . TYR   C 2  50  ? 18.126  12.267  -36.261 1.00 46.74  ? 52  TYR   D N     1 
ATOM   7316  C  CA    . TYR   C 2  50  ? 18.398  11.161  -37.166 1.00 47.54  ? 52  TYR   D CA    1 
ATOM   7317  C  C     . TYR   C 2  50  ? 18.592  11.583  -38.617 1.00 54.04  ? 52  TYR   D C     1 
ATOM   7318  O  O     . TYR   C 2  50  ? 18.933  10.732  -39.443 1.00 51.92  ? 52  TYR   D O     1 
ATOM   7319  C  CB    . TYR   C 2  50  ? 17.265  10.138  -37.111 1.00 40.85  ? 52  TYR   D CB    1 
ATOM   7320  C  CG    . TYR   C 2  50  ? 17.332  9.154   -35.969 1.00 52.57  ? 52  TYR   D CG    1 
ATOM   7321  C  CD1   . TYR   C 2  50  ? 18.257  8.120   -35.968 1.00 52.64  ? 52  TYR   D CD1   1 
ATOM   7322  C  CD2   . TYR   C 2  50  ? 16.429  9.227   -34.911 1.00 52.99  ? 52  TYR   D CD2   1 
ATOM   7323  C  CE1   . TYR   C 2  50  ? 18.306  7.202   -34.926 1.00 51.75  ? 52  TYR   D CE1   1 
ATOM   7324  C  CE2   . TYR   C 2  50  ? 16.468  8.321   -33.866 1.00 42.14  ? 52  TYR   D CE2   1 
ATOM   7325  C  CZ    . TYR   C 2  50  ? 17.408  7.313   -33.875 1.00 46.80  ? 52  TYR   D CZ    1 
ATOM   7326  O  OH    . TYR   C 2  50  ? 17.443  6.407   -32.836 1.00 46.38  ? 52  TYR   D OH    1 
ATOM   7327  N  N     . TYR   C 2  51  ? 18.381  12.856  -38.953 1.00 51.87  ? 53  TYR   D N     1 
ATOM   7328  C  CA    . TYR   C 2  51  ? 18.412  13.313  -40.337 1.00 53.81  ? 53  TYR   D CA    1 
ATOM   7329  C  C     . TYR   C 2  51  ? 19.372  14.478  -40.473 1.00 58.85  ? 53  TYR   D C     1 
ATOM   7330  O  O     . TYR   C 2  51  ? 19.334  15.417  -39.673 1.00 74.65  ? 53  TYR   D O     1 
ATOM   7331  C  CB    . TYR   C 2  51  ? 17.020  13.756  -40.830 1.00 56.92  ? 53  TYR   D CB    1 
ATOM   7332  C  CG    . TYR   C 2  51  ? 16.053  12.621  -41.107 1.00 57.45  ? 53  TYR   D CG    1 
ATOM   7333  C  CD1   . TYR   C 2  51  ? 16.205  11.808  -42.224 1.00 65.19  ? 53  TYR   D CD1   1 
ATOM   7334  C  CD2   . TYR   C 2  51  ? 14.987  12.368  -40.260 1.00 50.32  ? 53  TYR   D CD2   1 
ATOM   7335  C  CE1   . TYR   C 2  51  ? 15.336  10.770  -42.484 1.00 56.44  ? 53  TYR   D CE1   1 
ATOM   7336  C  CE2   . TYR   C 2  51  ? 14.106  11.340  -40.513 1.00 56.16  ? 53  TYR   D CE2   1 
ATOM   7337  C  CZ    . TYR   C 2  51  ? 14.287  10.543  -41.628 1.00 62.84  ? 53  TYR   D CZ    1 
ATOM   7338  O  OH    . TYR   C 2  51  ? 13.416  9.516   -41.891 1.00 58.95  ? 53  TYR   D OH    1 
ATOM   7339  N  N     . ASN   C 2  52  ? 20.216  14.425  -41.493 1.00 68.73  ? 54  ASN   D N     1 
ATOM   7340  C  CA    . ASN   C 2  52  ? 20.953  15.605  -41.923 1.00 65.91  ? 54  ASN   D CA    1 
ATOM   7341  C  C     . ASN   C 2  52  ? 20.056  16.471  -42.800 1.00 70.18  ? 54  ASN   D C     1 
ATOM   7342  O  O     . ASN   C 2  52  ? 19.368  15.964  -43.692 1.00 76.16  ? 54  ASN   D O     1 
ATOM   7343  C  CB    . ASN   C 2  52  ? 22.210  15.201  -42.690 1.00 64.73  ? 54  ASN   D CB    1 
ATOM   7344  C  CG    . ASN   C 2  52  ? 23.375  14.922  -41.781 1.00 59.26  ? 54  ASN   D CG    1 
ATOM   7345  O  OD1   . ASN   C 2  52  ? 23.814  15.811  -41.055 1.00 54.61  ? 54  ASN   D OD1   1 
ATOM   7346  N  ND2   . ASN   C 2  52  ? 23.896  13.686  -41.820 1.00 48.78  ? 54  ASN   D ND2   1 
ATOM   7347  N  N     . GLU   C 2  53  ? 20.053  17.777  -42.541 1.00 76.39  ? 55  GLU   D N     1 
ATOM   7348  C  CA    . GLU   C 2  53  ? 19.306  18.721  -43.368 1.00 80.05  ? 55  GLU   D CA    1 
ATOM   7349  C  C     . GLU   C 2  53  ? 20.185  19.093  -44.561 1.00 85.61  ? 55  GLU   D C     1 
ATOM   7350  O  O     . GLU   C 2  53  ? 20.829  20.145  -44.606 1.00 75.07  ? 55  GLU   D O     1 
ATOM   7351  C  CB    . GLU   C 2  53  ? 18.890  19.941  -42.555 1.00 84.56  ? 55  GLU   D CB    1 
ATOM   7352  C  CG    . GLU   C 2  53  ? 17.965  20.892  -43.294 1.00 83.18  ? 55  GLU   D CG    1 
ATOM   7353  C  CD    . GLU   C 2  53  ? 17.434  21.985  -42.397 1.00 91.92  ? 55  GLU   D CD    1 
ATOM   7354  O  OE1   . GLU   C 2  53  ? 17.894  22.066  -41.236 1.00 98.15  ? 55  GLU   D OE1   1 
ATOM   7355  O  OE2   . GLU   C 2  53  ? 16.558  22.758  -42.850 1.00 96.64  ? 55  GLU   D OE2   1 
ATOM   7356  N  N     . ALA   C 2  54  ? 20.214  18.192  -45.544 1.00 88.22  ? 56  ALA   D N     1 
ATOM   7357  C  CA    . ALA   C 2  54  ? 21.024  18.402  -46.738 1.00 95.30  ? 56  ALA   D CA    1 
ATOM   7358  C  C     . ALA   C 2  54  ? 20.395  19.466  -47.631 1.00 92.29  ? 56  ALA   D C     1 
ATOM   7359  O  O     . ALA   C 2  54  ? 19.218  19.376  -47.997 1.00 94.19  ? 56  ALA   D O     1 
ATOM   7360  C  CB    . ALA   C 2  54  ? 21.191  17.094  -47.508 1.00 84.16  ? 56  ALA   D CB    1 
ATOM   7361  N  N     . THR   C 2  55  ? 21.198  20.464  -47.995 1.00 96.64  ? 57  THR   D N     1 
ATOM   7362  C  CA    . THR   C 2  55  ? 20.738  21.656  -48.702 1.00 108.38 ? 57  THR   D CA    1 
ATOM   7363  C  C     . THR   C 2  55  ? 19.777  21.360  -49.857 1.00 97.75  ? 57  THR   D C     1 
ATOM   7364  O  O     . THR   C 2  55  ? 19.767  20.259  -50.419 1.00 91.55  ? 57  THR   D O     1 
ATOM   7365  C  CB    . THR   C 2  55  ? 21.951  22.442  -49.198 1.00 100.46 ? 57  THR   D CB    1 
ATOM   7366  O  OG1   . THR   C 2  55  ? 22.759  21.592  -50.021 1.00 94.81  ? 57  THR   D OG1   1 
ATOM   7367  C  CG2   . THR   C 2  55  ? 22.774  22.931  -48.009 1.00 75.47  ? 57  THR   D CG2   1 
ATOM   7368  N  N     . GLY   C 2  56  ? 18.981  22.355  -50.229 1.00 89.26  ? 58  GLY   D N     1 
ATOM   7369  C  CA    . GLY   C 2  56  ? 17.802  22.116  -51.018 1.00 89.10  ? 58  GLY   D CA    1 
ATOM   7370  C  C     . GLY   C 2  56  ? 16.585  21.808  -50.183 1.00 96.52  ? 58  GLY   D C     1 
ATOM   7371  O  O     . GLY   C 2  56  ? 15.581  21.327  -50.726 1.00 97.37  ? 58  GLY   D O     1 
ATOM   7372  N  N     . ASN   C 2  57  ? 16.643  22.070  -48.877 1.00 90.63  ? 59  ASN   D N     1 
ATOM   7373  C  CA    . ASN   C 2  57  ? 15.594  21.695  -47.935 1.00 93.05  ? 59  ASN   D CA    1 
ATOM   7374  C  C     . ASN   C 2  57  ? 15.339  20.189  -47.937 1.00 92.28  ? 59  ASN   D C     1 
ATOM   7375  O  O     . ASN   C 2  57  ? 14.280  19.731  -47.479 1.00 85.09  ? 59  ASN   D O     1 
ATOM   7376  C  CB    . ASN   C 2  57  ? 14.296  22.464  -48.213 1.00 93.99  ? 59  ASN   D CB    1 
ATOM   7377  C  CG    . ASN   C 2  57  ? 14.040  23.566  -47.199 1.00 83.30  ? 59  ASN   D CG    1 
ATOM   7378  O  OD1   . ASN   C 2  57  ? 14.926  23.934  -46.428 1.00 88.77  ? 59  ASN   D OD1   1 
ATOM   7379  N  ND2   . ASN   C 2  57  ? 12.822  24.095  -47.194 1.00 77.36  ? 59  ASN   D ND2   1 
ATOM   7380  N  N     . LYS   C 2  58  ? 16.293  19.415  -48.454 1.00 87.96  ? 60  LYS   D N     1 
ATOM   7381  C  CA    . LYS   C 2  58  ? 16.222  17.963  -48.421 1.00 82.04  ? 60  LYS   D CA    1 
ATOM   7382  C  C     . LYS   C 2  58  ? 16.711  17.444  -47.073 1.00 75.07  ? 60  LYS   D C     1 
ATOM   7383  O  O     . LYS   C 2  58  ? 17.390  18.146  -46.319 1.00 75.06  ? 60  LYS   D O     1 
ATOM   7384  C  CB    . LYS   C 2  58  ? 17.046  17.353  -49.557 1.00 86.25  ? 60  LYS   D CB    1 
ATOM   7385  C  CG    . LYS   C 2  58  ? 16.302  17.223  -50.894 1.00 91.01  ? 60  LYS   D CG    1 
ATOM   7386  C  CD    . LYS   C 2  58  ? 17.209  16.617  -51.968 1.00 91.66  ? 60  LYS   D CD    1 
ATOM   7387  C  CE    . LYS   C 2  58  ? 16.460  16.321  -53.262 1.00 90.71  ? 60  LYS   D CE    1 
ATOM   7388  N  NZ    . LYS   C 2  58  ? 17.371  15.782  -54.329 1.00 75.89  ? 60  LYS   D NZ    1 
ATOM   7389  N  N     . TYR   C 2  59  ? 16.345  16.197  -46.768 1.00 74.30  ? 61  TYR   D N     1 
ATOM   7390  C  CA    . TYR   C 2  59  ? 16.684  15.564  -45.495 1.00 71.07  ? 61  TYR   D CA    1 
ATOM   7391  C  C     . TYR   C 2  59  ? 17.316  14.205  -45.762 1.00 69.24  ? 61  TYR   D C     1 
ATOM   7392  O  O     . TYR   C 2  59  ? 16.651  13.303  -46.282 1.00 64.00  ? 61  TYR   D O     1 
ATOM   7393  C  CB    . TYR   C 2  59  ? 15.446  15.424  -44.598 1.00 62.21  ? 61  TYR   D CB    1 
ATOM   7394  C  CG    . TYR   C 2  59  ? 15.031  16.723  -43.949 1.00 59.74  ? 61  TYR   D CG    1 
ATOM   7395  C  CD1   . TYR   C 2  59  ? 15.798  17.286  -42.942 1.00 67.14  ? 61  TYR   D CD1   1 
ATOM   7396  C  CD2   . TYR   C 2  59  ? 13.887  17.392  -44.347 1.00 63.13  ? 61  TYR   D CD2   1 
ATOM   7397  C  CE1   . TYR   C 2  59  ? 15.436  18.472  -42.349 1.00 65.68  ? 61  TYR   D CE1   1 
ATOM   7398  C  CE2   . TYR   C 2  59  ? 13.520  18.584  -43.762 1.00 56.54  ? 61  TYR   D CE2   1 
ATOM   7399  C  CZ    . TYR   C 2  59  ? 14.297  19.117  -42.759 1.00 66.70  ? 61  TYR   D CZ    1 
ATOM   7400  O  OH    . TYR   C 2  59  ? 13.943  20.306  -42.157 1.00 76.88  ? 61  TYR   D OH    1 
ATOM   7401  N  N     . VAL   C 2  60  ? 18.581  14.054  -45.399 1.00 65.03  ? 62  VAL   D N     1 
ATOM   7402  C  CA    . VAL   C 2  60  ? 19.351  12.849  -45.696 1.00 69.90  ? 62  VAL   D CA    1 
ATOM   7403  C  C     . VAL   C 2  60  ? 19.462  12.003  -44.432 1.00 60.21  ? 62  VAL   D C     1 
ATOM   7404  O  O     . VAL   C 2  60  ? 19.925  12.511  -43.403 1.00 58.55  ? 62  VAL   D O     1 
ATOM   7405  C  CB    . VAL   C 2  60  ? 20.745  13.190  -46.248 1.00 67.29  ? 62  VAL   D CB    1 
ATOM   7406  C  CG1   . VAL   C 2  60  ? 21.455  11.919  -46.699 1.00 69.78  ? 62  VAL   D CG1   1 
ATOM   7407  C  CG2   . VAL   C 2  60  ? 20.614  14.148  -47.396 1.00 72.15  ? 62  VAL   D CG2   1 
ATOM   7408  N  N     . PRO   C 2  61  ? 19.066  10.734  -44.465 1.00 51.09  ? 63  PRO   D N     1 
ATOM   7409  C  CA    . PRO   C 2  61  ? 19.281  9.865   -43.303 1.00 55.98  ? 63  PRO   D CA    1 
ATOM   7410  C  C     . PRO   C 2  61  ? 20.759  9.772   -42.972 1.00 61.12  ? 63  PRO   D C     1 
ATOM   7411  O  O     . PRO   C 2  61  ? 21.566  9.301   -43.780 1.00 67.48  ? 63  PRO   D O     1 
ATOM   7412  C  CB    . PRO   C 2  61  ? 18.727  8.510   -43.759 1.00 46.75  ? 63  PRO   D CB    1 
ATOM   7413  C  CG    . PRO   C 2  61  ? 17.794  8.826   -44.846 1.00 55.85  ? 63  PRO   D CG    1 
ATOM   7414  C  CD    . PRO   C 2  61  ? 18.342  10.049  -45.539 1.00 61.96  ? 63  PRO   D CD    1 
ATOM   7415  N  N     . ARG   C 2  62  ? 21.110  10.219  -41.768 1.00 54.54  ? 64  ARG   D N     1 
ATOM   7416  C  CA    . ARG   C 2  62  ? 22.461  10.028  -41.265 1.00 44.58  ? 64  ARG   D CA    1 
ATOM   7417  C  C     . ARG   C 2  62  ? 22.735  8.546   -41.050 1.00 52.73  ? 64  ARG   D C     1 
ATOM   7418  O  O     . ARG   C 2  62  ? 22.956  8.103   -39.912 1.00 43.88  ? 64  ARG   D O     1 
ATOM   7419  C  CB    . ARG   C 2  62  ? 22.673  10.803  -39.971 1.00 45.78  ? 64  ARG   D CB    1 
ATOM   7420  C  CG    . ARG   C 2  62  ? 24.121  10.863  -39.581 1.00 49.32  ? 64  ARG   D CG    1 
ATOM   7421  C  CD    . ARG   C 2  62  ? 24.324  11.696  -38.350 1.00 51.98  ? 64  ARG   D CD    1 
ATOM   7422  N  NE    . ARG   C 2  62  ? 23.689  13.003  -38.455 1.00 51.38  ? 64  ARG   D NE    1 
ATOM   7423  C  CZ    . ARG   C 2  62  ? 22.542  13.319  -37.872 1.00 51.43  ? 64  ARG   D CZ    1 
ATOM   7424  N  NH1   . ARG   C 2  62  ? 21.826  12.414  -37.227 1.00 47.25  ? 64  ARG   D NH1   1 
ATOM   7425  N  NH2   . ARG   C 2  62  ? 22.116  14.578  -37.918 1.00 45.77  ? 64  ARG   D NH2   1 
ATOM   7426  N  N     . ALA   C 2  63  ? 22.724  7.771   -42.140 1.00 49.88  ? 65  ALA   D N     1 
ATOM   7427  C  CA    . ALA   C 2  63  ? 22.867  6.326   -42.059 1.00 51.84  ? 65  ALA   D CA    1 
ATOM   7428  C  C     . ALA   C 2  63  ? 24.088  5.853   -42.833 1.00 52.91  ? 65  ALA   D C     1 
ATOM   7429  O  O     . ALA   C 2  63  ? 24.461  6.420   -43.863 1.00 60.62  ? 65  ALA   D O     1 
ATOM   7430  C  CB    . ALA   C 2  63  ? 21.624  5.613   -42.573 1.00 39.71  ? 65  ALA   D CB    1 
ATOM   7431  N  N     . ILE   C 2  64  ? 24.718  4.816   -42.299 1.00 44.80  ? 66  ILE   D N     1 
ATOM   7432  C  CA    . ILE   C 2  64  ? 25.842  4.144   -42.923 1.00 46.13  ? 66  ILE   D CA    1 
ATOM   7433  C  C     . ILE   C 2  64  ? 25.435  2.687   -43.087 1.00 56.33  ? 66  ILE   D C     1 
ATOM   7434  O  O     . ILE   C 2  64  ? 24.989  2.053   -42.121 1.00 57.95  ? 66  ILE   D O     1 
ATOM   7435  C  CB    . ILE   C 2  64  ? 27.127  4.296   -42.081 1.00 47.82  ? 66  ILE   D CB    1 
ATOM   7436  C  CG1   . ILE   C 2  64  ? 27.719  5.690   -42.261 1.00 55.30  ? 66  ILE   D CG1   1 
ATOM   7437  C  CG2   . ILE   C 2  64  ? 28.187  3.277   -42.460 1.00 44.75  ? 66  ILE   D CG2   1 
ATOM   7438  C  CD1   . ILE   C 2  64  ? 26.829  6.810   -41.810 1.00 55.97  ? 66  ILE   D CD1   1 
ATOM   7439  N  N     . LEU   C 2  65  ? 25.535  2.174   -44.315 1.00 57.00  ? 67  LEU   D N     1 
ATOM   7440  C  CA    . LEU   C 2  65  ? 25.151  0.805   -44.632 1.00 52.61  ? 67  LEU   D CA    1 
ATOM   7441  C  C     . LEU   C 2  65  ? 26.404  -0.013  -44.905 1.00 52.02  ? 67  LEU   D C     1 
ATOM   7442  O  O     . LEU   C 2  65  ? 27.347  0.486   -45.517 1.00 63.62  ? 67  LEU   D O     1 
ATOM   7443  C  CB    . LEU   C 2  65  ? 24.209  0.766   -45.832 1.00 47.51  ? 67  LEU   D CB    1 
ATOM   7444  C  CG    . LEU   C 2  65  ? 22.946  1.636   -45.736 1.00 61.10  ? 67  LEU   D CG    1 
ATOM   7445  C  CD1   . LEU   C 2  65  ? 23.198  3.122   -46.075 1.00 43.22  ? 67  LEU   D CD1   1 
ATOM   7446  C  CD2   . LEU   C 2  65  ? 21.820  1.054   -46.597 1.00 59.06  ? 67  LEU   D CD2   1 
ATOM   7447  N  N     . VAL   C 2  66  ? 26.413  -1.268  -44.451 1.00 45.45  ? 68  VAL   D N     1 
ATOM   7448  C  CA    . VAL   C 2  66  ? 27.630  -2.074  -44.444 1.00 53.16  ? 68  VAL   D CA    1 
ATOM   7449  C  C     . VAL   C 2  66  ? 27.299  -3.549  -44.634 1.00 65.01  ? 68  VAL   D C     1 
ATOM   7450  O  O     . VAL   C 2  66  ? 26.594  -4.145  -43.813 1.00 62.52  ? 68  VAL   D O     1 
ATOM   7451  C  CB    . VAL   C 2  66  ? 28.409  -1.869  -43.128 1.00 62.07  ? 68  VAL   D CB    1 
ATOM   7452  C  CG1   . VAL   C 2  66  ? 29.554  -2.896  -42.984 1.00 54.43  ? 68  VAL   D CG1   1 
ATOM   7453  C  CG2   . VAL   C 2  66  ? 28.917  -0.435  -43.018 1.00 53.21  ? 68  VAL   D CG2   1 
ATOM   7454  N  N     . ASP   C 2  67  ? 27.822  -4.164  -45.695 1.00 71.34  ? 69  ASP   D N     1 
ATOM   7455  C  CA    . ASP   C 2  67  ? 27.720  -5.614  -45.844 1.00 65.91  ? 69  ASP   D CA    1 
ATOM   7456  C  C     . ASP   C 2  67  ? 29.011  -6.152  -46.440 1.00 65.77  ? 69  ASP   D C     1 
ATOM   7457  O  O     . ASP   C 2  67  ? 29.545  -5.589  -47.402 1.00 67.85  ? 69  ASP   D O     1 
ATOM   7458  C  CB    . ASP   C 2  67  ? 26.518  -6.014  -46.712 1.00 71.18  ? 69  ASP   D CB    1 
ATOM   7459  C  CG    . ASP   C 2  67  ? 25.988  -7.418  -46.383 1.00 67.66  ? 69  ASP   D CG    1 
ATOM   7460  O  OD1   . ASP   C 2  67  ? 26.721  -8.224  -45.767 1.00 57.48  ? 69  ASP   D OD1   1 
ATOM   7461  O  OD2   . ASP   C 2  67  ? 24.830  -7.715  -46.752 1.00 66.33  ? 69  ASP   D OD2   1 
ATOM   7462  N  N     . LEU   C 2  68  ? 29.508  -7.241  -45.866 1.00 62.44  ? 70  LEU   D N     1 
ATOM   7463  C  CA    . LEU   C 2  68  ? 30.718  -7.879  -46.359 1.00 68.64  ? 70  LEU   D CA    1 
ATOM   7464  C  C     . LEU   C 2  68  ? 30.465  -8.565  -47.697 1.00 78.60  ? 70  LEU   D C     1 
ATOM   7465  O  O     . LEU   C 2  68  ? 31.184  -9.498  -48.070 1.00 80.31  ? 70  LEU   D O     1 
ATOM   7466  C  CB    . LEU   C 2  68  ? 31.217  -8.901  -45.343 1.00 59.10  ? 70  LEU   D CB    1 
ATOM   7467  C  CG    . LEU   C 2  68  ? 32.489  -8.562  -44.583 1.00 60.11  ? 70  LEU   D CG    1 
ATOM   7468  C  CD1   . LEU   C 2  68  ? 32.876  -9.753  -43.731 1.00 57.33  ? 70  LEU   D CD1   1 
ATOM   7469  C  CD2   . LEU   C 2  68  ? 33.595  -8.183  -45.552 1.00 55.44  ? 70  LEU   D CD2   1 
ATOM   7470  N  N     . GLU   C 2  69  ? 29.454  -8.118  -48.425 1.00 76.75  ? 71  GLU   D N     1 
ATOM   7471  C  CA    . GLU   C 2  69  ? 28.942  -8.933  -49.511 1.00 80.49  ? 71  GLU   D CA    1 
ATOM   7472  C  C     . GLU   C 2  69  ? 27.739  -8.238  -50.129 1.00 79.23  ? 71  GLU   D C     1 
ATOM   7473  O  O     . GLU   C 2  69  ? 26.643  -8.279  -49.556 1.00 76.80  ? 71  GLU   D O     1 
ATOM   7474  C  CB    . GLU   C 2  69  ? 28.564  -10.317 -48.981 1.00 79.75  ? 71  GLU   D CB    1 
ATOM   7475  C  CG    . GLU   C 2  69  ? 28.427  -11.393 -50.029 1.00 91.08  ? 71  GLU   D CG    1 
ATOM   7476  C  CD    . GLU   C 2  69  ? 27.143  -12.169 -49.873 1.00 80.41  ? 71  GLU   D CD    1 
ATOM   7477  O  OE1   . GLU   C 2  69  ? 26.122  -11.528 -49.524 1.00 76.15  ? 71  GLU   D OE1   1 
ATOM   7478  O  OE2   . GLU   C 2  69  ? 27.163  -13.407 -50.086 1.00 49.77  ? 71  GLU   D OE2   1 
ATOM   7479  N  N     . PRO   C 2  70  ? 27.901  -7.607  -51.299 1.00 80.75  ? 72  PRO   D N     1 
ATOM   7480  C  CA    . PRO   C 2  70  ? 26.836  -6.753  -51.848 1.00 88.74  ? 72  PRO   D CA    1 
ATOM   7481  C  C     . PRO   C 2  70  ? 25.530  -7.486  -52.082 1.00 94.51  ? 72  PRO   D C     1 
ATOM   7482  O  O     . PRO   C 2  70  ? 25.324  -8.602  -51.595 1.00 101.18 ? 72  PRO   D O     1 
ATOM   7483  C  CB    . PRO   C 2  70  ? 27.424  -6.260  -53.177 1.00 85.90  ? 72  PRO   D CB    1 
ATOM   7484  C  CG    . PRO   C 2  70  ? 28.896  -6.470  -53.057 1.00 89.20  ? 72  PRO   D CG    1 
ATOM   7485  C  CD    . PRO   C 2  70  ? 29.073  -7.671  -52.183 1.00 85.24  ? 72  PRO   D CD    1 
ATOM   7486  N  N     . GLY   C 2  71  ? 24.647  -6.864  -52.852 1.00 95.37  ? 73  GLY   D N     1 
ATOM   7487  C  CA    . GLY   C 2  71  ? 23.318  -7.402  -53.044 1.00 101.11 ? 73  GLY   D CA    1 
ATOM   7488  C  C     . GLY   C 2  71  ? 22.343  -6.796  -52.061 1.00 101.94 ? 73  GLY   D C     1 
ATOM   7489  O  O     . GLY   C 2  71  ? 21.506  -5.964  -52.438 1.00 98.36  ? 73  GLY   D O     1 
ATOM   7490  N  N     . THR   C 2  72  ? 22.451  -7.202  -50.793 1.00 99.87  ? 74  THR   D N     1 
ATOM   7491  C  CA    . THR   C 2  72  ? 21.684  -6.574  -49.723 1.00 107.31 ? 74  THR   D CA    1 
ATOM   7492  C  C     . THR   C 2  72  ? 21.694  -5.060  -49.927 1.00 107.28 ? 74  THR   D C     1 
ATOM   7493  O  O     . THR   C 2  72  ? 20.652  -4.399  -49.828 1.00 101.33 ? 74  THR   D O     1 
ATOM   7494  C  CB    . THR   C 2  72  ? 22.255  -6.949  -48.347 1.00 97.65  ? 74  THR   D CB    1 
ATOM   7495  O  OG1   . THR   C 2  72  ? 23.473  -6.226  -48.108 1.00 85.73  ? 74  THR   D OG1   1 
ATOM   7496  C  CG2   . THR   C 2  72  ? 22.530  -8.459  -48.263 1.00 83.72  ? 74  THR   D CG2   1 
ATOM   7497  N  N     . MET   C 2  73  ? 22.872  -4.515  -50.250 1.00 96.64  ? 75  MET   D N     1 
ATOM   7498  C  CA    . MET   C 2  73  ? 22.984  -3.093  -50.544 1.00 94.04  ? 75  MET   D CA    1 
ATOM   7499  C  C     . MET   C 2  73  ? 22.212  -2.717  -51.804 1.00 97.17  ? 75  MET   D C     1 
ATOM   7500  O  O     . MET   C 2  73  ? 21.753  -1.575  -51.928 1.00 95.40  ? 75  MET   D O     1 
ATOM   7501  C  CB    . MET   C 2  73  ? 24.459  -2.699  -50.690 1.00 99.67  ? 75  MET   D CB    1 
ATOM   7502  C  CG    . MET   C 2  73  ? 25.419  -3.391  -49.701 1.00 105.09 ? 75  MET   D CG    1 
ATOM   7503  S  SD    . MET   C 2  73  ? 25.684  -2.560  -48.108 1.00 84.04  ? 75  MET   D SD    1 
ATOM   7504  C  CE    . MET   C 2  73  ? 26.182  -0.926  -48.673 1.00 64.45  ? 75  MET   D CE    1 
ATOM   7505  N  N     . ASP   C 2  74  ? 22.057  -3.650  -52.747 1.00 95.37  ? 76  ASP   D N     1 
ATOM   7506  C  CA    . ASP   C 2  74  ? 21.357  -3.329  -53.989 1.00 100.40 ? 76  ASP   D CA    1 
ATOM   7507  C  C     . ASP   C 2  74  ? 19.857  -3.196  -53.753 1.00 96.59  ? 76  ASP   D C     1 
ATOM   7508  O  O     . ASP   C 2  74  ? 19.231  -2.221  -54.190 1.00 90.03  ? 76  ASP   D O     1 
ATOM   7509  C  CB    . ASP   C 2  74  ? 21.639  -4.397  -55.047 1.00 100.91 ? 76  ASP   D CB    1 
ATOM   7510  C  CG    . ASP   C 2  74  ? 23.103  -4.495  -55.405 1.00 101.11 ? 76  ASP   D CG    1 
ATOM   7511  O  OD1   . ASP   C 2  74  ? 23.949  -4.136  -54.556 1.00 98.02  ? 76  ASP   D OD1   1 
ATOM   7512  O  OD2   . ASP   C 2  74  ? 23.404  -4.926  -56.540 1.00 102.41 ? 76  ASP   D OD2   1 
ATOM   7513  N  N     . SER   C 2  75  ? 19.264  -4.184  -53.080 1.00 89.16  ? 77  SER   D N     1 
ATOM   7514  C  CA    . SER   C 2  75  ? 17.856  -4.126  -52.701 1.00 89.85  ? 77  SER   D CA    1 
ATOM   7515  C  C     . SER   C 2  75  ? 17.511  -2.804  -52.021 1.00 104.27 ? 77  SER   D C     1 
ATOM   7516  O  O     . SER   C 2  75  ? 16.621  -2.071  -52.468 1.00 103.46 ? 77  SER   D O     1 
ATOM   7517  C  CB    . SER   C 2  75  ? 17.556  -5.295  -51.775 1.00 88.04  ? 77  SER   D CB    1 
ATOM   7518  O  OG    . SER   C 2  75  ? 18.668  -5.502  -50.920 1.00 93.10  ? 77  SER   D OG    1 
ATOM   7519  N  N     . VAL   C 2  76  ? 18.206  -2.502  -50.916 1.00 106.41 ? 78  VAL   D N     1 
ATOM   7520  C  CA    . VAL   C 2  76  ? 18.009  -1.242  -50.197 1.00 94.11  ? 78  VAL   D CA    1 
ATOM   7521  C  C     . VAL   C 2  76  ? 18.049  -0.062  -51.159 1.00 98.76  ? 78  VAL   D C     1 
ATOM   7522  O  O     . VAL   C 2  76  ? 17.124  0.759   -51.209 1.00 104.10 ? 78  VAL   D O     1 
ATOM   7523  C  CB    . VAL   C 2  76  ? 19.068  -1.090  -49.089 1.00 87.68  ? 78  VAL   D CB    1 
ATOM   7524  C  CG1   . VAL   C 2  76  ? 19.328  0.384   -48.801 1.00 74.29  ? 78  VAL   D CG1   1 
ATOM   7525  C  CG2   . VAL   C 2  76  ? 18.635  -1.829  -47.829 1.00 77.30  ? 78  VAL   D CG2   1 
ATOM   7526  N  N     . ARG   C 2  77  ? 19.136  0.046   -51.929 1.00 102.42 ? 79  ARG   D N     1 
ATOM   7527  C  CA    . ARG   C 2  77  ? 19.274  1.137   -52.886 1.00 95.50  ? 79  ARG   D CA    1 
ATOM   7528  C  C     . ARG   C 2  77  ? 18.108  1.183   -53.863 1.00 98.56  ? 79  ARG   D C     1 
ATOM   7529  O  O     . ARG   C 2  77  ? 17.829  2.246   -54.428 1.00 103.30 ? 79  ARG   D O     1 
ATOM   7530  C  CB    . ARG   C 2  77  ? 20.603  0.997   -53.643 1.00 84.87  ? 79  ARG   D CB    1 
ATOM   7531  C  CG    . ARG   C 2  77  ? 21.152  2.300   -54.212 1.00 85.17  ? 79  ARG   D CG    1 
ATOM   7532  C  CD    . ARG   C 2  77  ? 22.231  2.059   -55.266 1.00 85.69  ? 79  ARG   D CD    1 
ATOM   7533  N  NE    . ARG   C 2  77  ? 23.594  2.056   -54.742 1.00 76.29  ? 79  ARG   D NE    1 
ATOM   7534  C  CZ    . ARG   C 2  77  ? 24.228  0.980   -54.295 1.00 75.61  ? 79  ARG   D CZ    1 
ATOM   7535  N  NH1   . ARG   C 2  77  ? 23.618  -0.193  -54.201 1.00 79.45  ? 79  ARG   D NH1   1 
ATOM   7536  N  NH2   . ARG   C 2  77  ? 25.508  1.082   -53.932 1.00 67.00  ? 79  ARG   D NH2   1 
ATOM   7537  N  N     . SER   C 2  78  ? 17.407  0.063   -54.053 1.00 105.78 ? 80  SER   D N     1 
ATOM   7538  C  CA    . SER   C 2  78  ? 16.343  -0.066  -55.044 1.00 110.59 ? 80  SER   D CA    1 
ATOM   7539  C  C     . SER   C 2  78  ? 14.945  0.071   -54.455 1.00 105.89 ? 80  SER   D C     1 
ATOM   7540  O  O     . SER   C 2  78  ? 14.091  0.739   -55.049 1.00 100.57 ? 80  SER   D O     1 
ATOM   7541  C  CB    . SER   C 2  78  ? 16.457  -1.415  -55.761 1.00 107.04 ? 80  SER   D CB    1 
ATOM   7542  O  OG    . SER   C 2  78  ? 15.662  -1.429  -56.933 1.00 126.02 ? 80  SER   D OG    1 
ATOM   7543  N  N     . GLY   C 2  79  ? 14.686  -0.556  -53.310 1.00 105.56 ? 81  GLY   D N     1 
ATOM   7544  C  CA    . GLY   C 2  79  ? 13.411  -0.435  -52.647 1.00 103.83 ? 81  GLY   D CA    1 
ATOM   7545  C  C     . GLY   C 2  79  ? 13.102  0.998   -52.264 1.00 103.40 ? 81  GLY   D C     1 
ATOM   7546  O  O     . GLY   C 2  79  ? 13.923  1.905   -52.440 1.00 97.10  ? 81  GLY   D O     1 
ATOM   7547  N  N     . PRO   C 2  80  ? 11.908  1.230   -51.716 1.00 106.32 ? 82  PRO   D N     1 
ATOM   7548  C  CA    . PRO   C 2  80  ? 11.513  2.603   -51.382 1.00 105.07 ? 82  PRO   D CA    1 
ATOM   7549  C  C     . PRO   C 2  80  ? 12.413  3.150   -50.288 1.00 108.31 ? 82  PRO   D C     1 
ATOM   7550  O  O     . PRO   C 2  80  ? 12.705  2.469   -49.301 1.00 97.78  ? 82  PRO   D O     1 
ATOM   7551  C  CB    . PRO   C 2  80  ? 10.067  2.452   -50.902 1.00 94.29  ? 82  PRO   D CB    1 
ATOM   7552  C  CG    . PRO   C 2  80  ? 10.051  1.091   -50.291 1.00 93.15  ? 82  PRO   D CG    1 
ATOM   7553  C  CD    . PRO   C 2  80  ? 10.971  0.243   -51.150 1.00 100.44 ? 82  PRO   D CD    1 
ATOM   7554  N  N     . PHE   C 2  81  ? 12.862  4.384   -50.482 1.00 111.73 ? 83  PHE   D N     1 
ATOM   7555  C  CA    . PHE   C 2  81  ? 13.741  5.095   -49.566 1.00 107.41 ? 83  PHE   D CA    1 
ATOM   7556  C  C     . PHE   C 2  81  ? 15.190  4.649   -49.721 1.00 97.74  ? 83  PHE   D C     1 
ATOM   7557  O  O     . PHE   C 2  81  ? 16.039  5.018   -48.887 1.00 90.71  ? 83  PHE   D O     1 
ATOM   7558  C  CB    . PHE   C 2  81  ? 13.274  4.949   -48.113 1.00 96.14  ? 83  PHE   D CB    1 
ATOM   7559  C  CG    . PHE   C 2  81  ? 11.905  5.529   -47.862 1.00 90.38  ? 83  PHE   D CG    1 
ATOM   7560  C  CD1   . PHE   C 2  81  ? 11.748  6.882   -47.603 1.00 84.55  ? 83  PHE   D CD1   1 
ATOM   7561  C  CD2   . PHE   C 2  81  ? 10.776  4.722   -47.906 1.00 90.07  ? 83  PHE   D CD2   1 
ATOM   7562  C  CE1   . PHE   C 2  81  ? 10.494  7.421   -47.382 1.00 88.28  ? 83  PHE   D CE1   1 
ATOM   7563  C  CE2   . PHE   C 2  81  ? 9.519   5.251   -47.684 1.00 85.49  ? 83  PHE   D CE2   1 
ATOM   7564  C  CZ    . PHE   C 2  81  ? 9.377   6.603   -47.422 1.00 88.92  ? 83  PHE   D CZ    1 
ATOM   7565  N  N     . GLY   C 2  82  ? 15.510  3.867   -50.757 1.00 96.48  ? 84  GLY   D N     1 
ATOM   7566  C  CA    . GLY   C 2  82  ? 16.899  3.734   -51.157 1.00 93.49  ? 84  GLY   D CA    1 
ATOM   7567  C  C     . GLY   C 2  82  ? 17.441  5.016   -51.756 1.00 89.80  ? 84  GLY   D C     1 
ATOM   7568  O  O     . GLY   C 2  82  ? 18.637  5.304   -51.647 1.00 86.79  ? 84  GLY   D O     1 
ATOM   7569  N  N     . GLN   C 2  83  ? 16.569  5.812   -52.373 1.00 91.79  ? 85  GLN   D N     1 
ATOM   7570  C  CA    . GLN   C 2  83  ? 16.952  7.069   -53.001 1.00 92.11  ? 85  GLN   D CA    1 
ATOM   7571  C  C     . GLN   C 2  83  ? 17.138  8.200   -51.997 1.00 89.79  ? 85  GLN   D C     1 
ATOM   7572  O  O     . GLN   C 2  83  ? 17.635  9.269   -52.373 1.00 87.81  ? 85  GLN   D O     1 
ATOM   7573  C  CB    . GLN   C 2  83  ? 15.899  7.472   -54.043 1.00 96.46  ? 85  GLN   D CB    1 
ATOM   7574  C  CG    . GLN   C 2  83  ? 15.781  6.524   -55.246 1.00 104.79 ? 85  GLN   D CG    1 
ATOM   7575  C  CD    . GLN   C 2  83  ? 15.101  5.195   -54.916 1.00 112.32 ? 85  GLN   D CD    1 
ATOM   7576  O  OE1   . GLN   C 2  83  ? 14.380  5.073   -53.919 1.00 109.38 ? 85  GLN   D OE1   1 
ATOM   7577  N  NE2   . GLN   C 2  83  ? 15.331  4.191   -55.760 1.00 101.95 ? 85  GLN   D NE2   1 
ATOM   7578  N  N     . ILE   C 2  84  ? 16.747  7.995   -50.741 1.00 93.48  ? 86  ILE   D N     1 
ATOM   7579  C  CA    . ILE   C 2  84  ? 16.871  9.041   -49.730 1.00 90.71  ? 86  ILE   D CA    1 
ATOM   7580  C  C     . ILE   C 2  84  ? 18.260  9.043   -49.094 1.00 73.69  ? 86  ILE   D C     1 
ATOM   7581  O  O     . ILE   C 2  84  ? 18.727  10.093  -48.632 1.00 61.53  ? 86  ILE   D O     1 
ATOM   7582  C  CB    . ILE   C 2  84  ? 15.764  8.873   -48.668 1.00 82.02  ? 86  ILE   D CB    1 
ATOM   7583  C  CG1   . ILE   C 2  84  ? 15.648  10.114  -47.789 1.00 75.87  ? 86  ILE   D CG1   1 
ATOM   7584  C  CG2   . ILE   C 2  84  ? 16.019  7.657   -47.799 1.00 69.60  ? 86  ILE   D CG2   1 
ATOM   7585  C  CD1   . ILE   C 2  84  ? 14.656  9.939   -46.670 1.00 67.96  ? 86  ILE   D CD1   1 
ATOM   7586  N  N     . PHE   C 2  85  ? 18.932  7.894   -49.094 1.00 62.02  ? 87  PHE   D N     1 
ATOM   7587  C  CA    . PHE   C 2  85  ? 20.218  7.721   -48.442 1.00 61.79  ? 87  PHE   D CA    1 
ATOM   7588  C  C     . PHE   C 2  85  ? 21.313  8.513   -49.166 1.00 72.31  ? 87  PHE   D C     1 
ATOM   7589  O  O     . PHE   C 2  85  ? 21.058  9.362   -50.024 1.00 83.33  ? 87  PHE   D O     1 
ATOM   7590  C  CB    . PHE   C 2  85  ? 20.550  6.237   -48.351 1.00 60.95  ? 87  PHE   D CB    1 
ATOM   7591  C  CG    . PHE   C 2  85  ? 19.654  5.483   -47.417 1.00 70.90  ? 87  PHE   D CG    1 
ATOM   7592  C  CD1   . PHE   C 2  85  ? 19.534  5.872   -46.093 1.00 63.32  ? 87  PHE   D CD1   1 
ATOM   7593  C  CD2   . PHE   C 2  85  ? 18.932  4.386   -47.857 1.00 81.37  ? 87  PHE   D CD2   1 
ATOM   7594  C  CE1   . PHE   C 2  85  ? 18.707  5.188   -45.227 1.00 57.25  ? 87  PHE   D CE1   1 
ATOM   7595  C  CE2   . PHE   C 2  85  ? 18.102  3.693   -46.993 1.00 77.25  ? 87  PHE   D CE2   1 
ATOM   7596  C  CZ    . PHE   C 2  85  ? 17.990  4.096   -45.676 1.00 68.85  ? 87  PHE   D CZ    1 
ATOM   7597  N  N     . ARG   C 2  86  ? 22.562  8.230   -48.805 1.00 71.03  ? 88  ARG   D N     1 
ATOM   7598  C  CA    . ARG   C 2  86  ? 23.727  8.982   -49.267 1.00 76.34  ? 88  ARG   D CA    1 
ATOM   7599  C  C     . ARG   C 2  86  ? 24.729  7.999   -49.856 1.00 68.65  ? 88  ARG   D C     1 
ATOM   7600  O  O     . ARG   C 2  86  ? 25.455  7.325   -49.105 1.00 67.61  ? 88  ARG   D O     1 
ATOM   7601  C  CB    . ARG   C 2  86  ? 24.339  9.779   -48.118 1.00 77.89  ? 88  ARG   D CB    1 
ATOM   7602  C  CG    . ARG   C 2  86  ? 25.805  10.156  -48.283 1.00 80.03  ? 88  ARG   D CG    1 
ATOM   7603  C  CD    . ARG   C 2  86  ? 26.293  11.011  -47.111 1.00 74.39  ? 88  ARG   D CD    1 
ATOM   7604  N  NE    . ARG   C 2  86  ? 26.724  12.334  -47.544 1.00 82.18  ? 88  ARG   D NE    1 
ATOM   7605  C  CZ    . ARG   C 2  86  ? 25.973  13.426  -47.485 1.00 95.69  ? 88  ARG   D CZ    1 
ATOM   7606  N  NH1   . ARG   C 2  86  ? 24.743  13.397  -46.991 1.00 82.13  ? 88  ARG   D NH1   1 
ATOM   7607  N  NH2   . ARG   C 2  86  ? 26.468  14.577  -47.934 1.00 104.62 ? 88  ARG   D NH2   1 
ATOM   7608  N  N     . PRO   C 2  87  ? 24.818  7.908   -51.185 1.00 69.21  ? 89  PRO   D N     1 
ATOM   7609  C  CA    . PRO   C 2  87  ? 25.613  6.828   -51.796 1.00 63.79  ? 89  PRO   D CA    1 
ATOM   7610  C  C     . PRO   C 2  87  ? 27.056  6.794   -51.327 1.00 66.78  ? 89  PRO   D C     1 
ATOM   7611  O  O     . PRO   C 2  87  ? 27.650  5.711   -51.249 1.00 59.34  ? 89  PRO   D O     1 
ATOM   7612  C  CB    . PRO   C 2  87  ? 25.510  7.132   -53.294 1.00 58.41  ? 89  PRO   D CB    1 
ATOM   7613  C  CG    . PRO   C 2  87  ? 25.330  8.623   -53.337 1.00 79.45  ? 89  PRO   D CG    1 
ATOM   7614  C  CD    . PRO   C 2  87  ? 24.448  8.945   -52.161 1.00 71.60  ? 89  PRO   D CD    1 
ATOM   7615  N  N     . ASP   C 2  88  ? 27.641  7.932   -50.995 1.00 65.49  ? 90  ASP   D N     1 
ATOM   7616  C  CA    . ASP   C 2  88  ? 28.951  7.735   -50.400 1.00 65.04  ? 90  ASP   D CA    1 
ATOM   7617  C  C     . ASP   C 2  88  ? 28.886  7.069   -49.014 1.00 72.60  ? 90  ASP   D C     1 
ATOM   7618  O  O     . ASP   C 2  88  ? 29.939  6.973   -48.379 1.00 70.31  ? 90  ASP   D O     1 
ATOM   7619  C  CB    . ASP   C 2  88  ? 29.697  9.067   -50.324 1.00 75.50  ? 90  ASP   D CB    1 
ATOM   7620  C  CG    . ASP   C 2  88  ? 30.415  9.401   -51.625 1.00 88.03  ? 90  ASP   D CG    1 
ATOM   7621  O  OD1   . ASP   C 2  88  ? 30.274  8.609   -52.583 1.00 86.97  ? 90  ASP   D OD1   1 
ATOM   7622  O  OD2   . ASP   C 2  88  ? 31.120  10.438  -51.694 1.00 76.60  ? 90  ASP   D OD2   1 
ATOM   7623  N  N     . ASN   C 2  89  ? 27.723  6.606   -48.534 1.00 75.43  ? 91  ASN   D N     1 
ATOM   7624  C  CA    . ASN   C 2  89  ? 27.622  5.864   -47.281 1.00 67.89  ? 91  ASN   D CA    1 
ATOM   7625  C  C     . ASN   C 2  89  ? 27.366  4.373   -47.472 1.00 63.87  ? 91  ASN   D C     1 
ATOM   7626  O  O     . ASN   C 2  89  ? 27.421  3.627   -46.489 1.00 56.06  ? 91  ASN   D O     1 
ATOM   7627  C  CB    . ASN   C 2  89  ? 26.509  6.444   -46.392 1.00 68.25  ? 91  ASN   D CB    1 
ATOM   7628  C  CG    . ASN   C 2  89  ? 26.817  7.847   -45.901 1.00 71.15  ? 91  ASN   D CG    1 
ATOM   7629  O  OD1   . ASN   C 2  89  ? 27.588  8.579   -46.523 1.00 77.25  ? 91  ASN   D OD1   1 
ATOM   7630  N  ND2   . ASN   C 2  89  ? 26.208  8.231   -44.780 1.00 61.48  ? 91  ASN   D ND2   1 
ATOM   7631  N  N     . PHE   C 2  90  ? 27.061  3.923   -48.690 1.00 70.45  ? 92  PHE   D N     1 
ATOM   7632  C  CA    . PHE   C 2  90  ? 27.037  2.493   -48.989 1.00 61.66  ? 92  PHE   D CA    1 
ATOM   7633  C  C     . PHE   C 2  90  ? 28.471  1.991   -49.045 1.00 56.95  ? 92  PHE   D C     1 
ATOM   7634  O  O     . PHE   C 2  90  ? 29.186  2.266   -50.011 1.00 60.44  ? 92  PHE   D O     1 
ATOM   7635  C  CB    . PHE   C 2  90  ? 26.336  2.214   -50.316 1.00 56.62  ? 92  PHE   D CB    1 
ATOM   7636  C  CG    . PHE   C 2  90  ? 24.867  2.540   -50.331 1.00 61.84  ? 92  PHE   D CG    1 
ATOM   7637  C  CD1   . PHE   C 2  90  ? 24.427  3.830   -50.589 1.00 58.72  ? 92  PHE   D CD1   1 
ATOM   7638  C  CD2   . PHE   C 2  90  ? 23.923  1.546   -50.143 1.00 64.65  ? 92  PHE   D CD2   1 
ATOM   7639  C  CE1   . PHE   C 2  90  ? 23.077  4.124   -50.631 1.00 54.40  ? 92  PHE   D CE1   1 
ATOM   7640  C  CE2   . PHE   C 2  90  ? 22.570  1.843   -50.183 1.00 66.04  ? 92  PHE   D CE2   1 
ATOM   7641  C  CZ    . PHE   C 2  90  ? 22.150  3.134   -50.431 1.00 57.20  ? 92  PHE   D CZ    1 
ATOM   7642  N  N     . VAL   C 2  91  ? 28.892  1.269   -48.013 1.00 45.63  ? 93  VAL   D N     1 
ATOM   7643  C  CA    . VAL   C 2  91  ? 30.211  0.658   -47.937 1.00 46.74  ? 93  VAL   D CA    1 
ATOM   7644  C  C     . VAL   C 2  91  ? 29.978  -0.842  -47.944 1.00 61.69  ? 93  VAL   D C     1 
ATOM   7645  O  O     . VAL   C 2  91  ? 29.445  -1.396  -46.974 1.00 63.54  ? 93  VAL   D O     1 
ATOM   7646  C  CB    . VAL   C 2  91  ? 30.979  1.104   -46.682 1.00 56.73  ? 93  VAL   D CB    1 
ATOM   7647  C  CG1   . VAL   C 2  91  ? 32.333  0.412   -46.579 1.00 42.23  ? 93  VAL   D CG1   1 
ATOM   7648  C  CG2   . VAL   C 2  91  ? 31.141  2.613   -46.668 1.00 54.00  ? 93  VAL   D CG2   1 
ATOM   7649  N  N     . PHE   C 2  92  ? 30.358  -1.506  -49.040 1.00 72.37  ? 94  PHE   D N     1 
ATOM   7650  C  CA    . PHE   C 2  92  ? 30.012  -2.903  -49.263 1.00 73.94  ? 94  PHE   D CA    1 
ATOM   7651  C  C     . PHE   C 2  92  ? 31.257  -3.733  -49.536 1.00 71.06  ? 94  PHE   D C     1 
ATOM   7652  O  O     . PHE   C 2  92  ? 32.173  -3.285  -50.229 1.00 75.23  ? 94  PHE   D O     1 
ATOM   7653  C  CB    . PHE   C 2  92  ? 29.015  -3.048  -50.428 1.00 78.92  ? 94  PHE   D CB    1 
ATOM   7654  C  CG    . PHE   C 2  92  ? 29.400  -2.283  -51.672 1.00 85.33  ? 94  PHE   D CG    1 
ATOM   7655  C  CD1   . PHE   C 2  92  ? 30.494  -2.671  -52.439 1.00 95.97  ? 94  PHE   D CD1   1 
ATOM   7656  C  CD2   . PHE   C 2  92  ? 28.647  -1.195  -52.093 1.00 81.16  ? 94  PHE   D CD2   1 
ATOM   7657  C  CE1   . PHE   C 2  92  ? 30.846  -1.971  -53.593 1.00 97.82  ? 94  PHE   D CE1   1 
ATOM   7658  C  CE2   . PHE   C 2  92  ? 28.988  -0.492  -53.245 1.00 86.85  ? 94  PHE   D CE2   1 
ATOM   7659  C  CZ    . PHE   C 2  92  ? 30.090  -0.881  -53.995 1.00 90.26  ? 94  PHE   D CZ    1 
ATOM   7660  N  N     . GLY   C 2  93  ? 31.278  -4.951  -48.995 1.00 72.06  ? 95  GLY   D N     1 
ATOM   7661  C  CA    . GLY   C 2  93  ? 32.351  -5.890  -49.252 1.00 81.83  ? 95  GLY   D CA    1 
ATOM   7662  C  C     . GLY   C 2  93  ? 32.174  -6.658  -50.551 1.00 82.00  ? 95  GLY   D C     1 
ATOM   7663  O  O     . GLY   C 2  93  ? 31.524  -6.207  -51.497 1.00 84.17  ? 95  GLY   D O     1 
ATOM   7664  N  N     . GLN   C 2  94  ? 32.785  -7.839  -50.594 1.00 76.35  ? 96  GLN   D N     1 
ATOM   7665  C  CA    . GLN   C 2  94  ? 32.642  -8.741  -51.729 1.00 78.74  ? 96  GLN   D CA    1 
ATOM   7666  C  C     . GLN   C 2  94  ? 32.650  -10.178 -51.235 1.00 93.39  ? 96  GLN   D C     1 
ATOM   7667  O  O     . GLN   C 2  94  ? 31.869  -11.014 -51.704 1.00 84.96  ? 96  GLN   D O     1 
ATOM   7668  C  CB    . GLN   C 2  94  ? 33.771  -8.536  -52.741 1.00 89.82  ? 96  GLN   D CB    1 
ATOM   7669  C  CG    . GLN   C 2  94  ? 33.936  -7.108  -53.238 1.00 94.28  ? 96  GLN   D CG    1 
ATOM   7670  C  CD    . GLN   C 2  94  ? 32.753  -6.632  -54.062 1.00 100.06 ? 96  GLN   D CD    1 
ATOM   7671  O  OE1   . GLN   C 2  94  ? 31.998  -7.436  -54.615 1.00 90.54  ? 96  GLN   D OE1   1 
ATOM   7672  N  NE2   . GLN   C 2  94  ? 32.582  -5.316  -54.142 1.00 102.25 ? 96  GLN   D NE2   1 
ATOM   7673  N  N     . SER   C 2  95  ? 33.524  -10.452 -50.260 1.00 102.29 ? 97  SER   D N     1 
ATOM   7674  C  CA    . SER   C 2  95  ? 33.792  -11.823 -49.834 1.00 97.55  ? 97  SER   D CA    1 
ATOM   7675  C  C     . SER   C 2  95  ? 32.533  -12.516 -49.322 1.00 100.75 ? 97  SER   D C     1 
ATOM   7676  O  O     . SER   C 2  95  ? 32.318  -13.703 -49.597 1.00 107.46 ? 97  SER   D O     1 
ATOM   7677  C  CB    . SER   C 2  95  ? 34.882  -11.829 -48.757 1.00 91.11  ? 97  SER   D CB    1 
ATOM   7678  O  OG    . SER   C 2  95  ? 35.605  -13.051 -48.755 1.00 90.94  ? 97  SER   D OG    1 
ATOM   7679  N  N     . GLY   C 2  96  ? 31.691  -11.798 -48.578 1.00 84.59  ? 98  GLY   D N     1 
ATOM   7680  C  CA    . GLY   C 2  96  ? 30.602  -12.445 -47.870 1.00 83.24  ? 98  GLY   D CA    1 
ATOM   7681  C  C     . GLY   C 2  96  ? 31.142  -13.318 -46.753 1.00 87.89  ? 98  GLY   D C     1 
ATOM   7682  O  O     . GLY   C 2  96  ? 31.893  -14.266 -47.003 1.00 101.70 ? 98  GLY   D O     1 
ATOM   7683  N  N     . ALA   C 2  97  ? 30.788  -12.999 -45.508 1.00 76.78  ? 99  ALA   D N     1 
ATOM   7684  C  CA    . ALA   C 2  97  ? 31.381  -13.697 -44.373 1.00 82.29  ? 99  ALA   D CA    1 
ATOM   7685  C  C     . ALA   C 2  97  ? 30.870  -15.124 -44.259 1.00 72.37  ? 99  ALA   D C     1 
ATOM   7686  O  O     . ALA   C 2  97  ? 31.509  -15.960 -43.606 1.00 60.65  ? 99  ALA   D O     1 
ATOM   7687  C  CB    . ALA   C 2  97  ? 31.108  -12.916 -43.081 1.00 65.20  ? 99  ALA   D CB    1 
ATOM   7688  N  N     . GLY   C 2  98  ? 29.737  -15.414 -44.884 1.00 68.28  ? 100 GLY   D N     1 
ATOM   7689  C  CA    . GLY   C 2  98  ? 29.216  -16.757 -44.898 1.00 67.93  ? 100 GLY   D CA    1 
ATOM   7690  C  C     . GLY   C 2  98  ? 28.965  -17.288 -43.510 1.00 63.89  ? 100 GLY   D C     1 
ATOM   7691  O  O     . GLY   C 2  98  ? 29.503  -18.336 -43.137 1.00 65.55  ? 100 GLY   D O     1 
ATOM   7692  N  N     . ASN   C 2  99  ? 28.155  -16.557 -42.738 1.00 62.01  ? 101 ASN   D N     1 
ATOM   7693  C  CA    . ASN   C 2  99  ? 27.660  -17.036 -41.443 1.00 53.77  ? 101 ASN   D CA    1 
ATOM   7694  C  C     . ASN   C 2  99  ? 28.812  -17.458 -40.536 1.00 55.36  ? 101 ASN   D C     1 
ATOM   7695  O  O     . ASN   C 2  99  ? 28.698  -18.412 -39.762 1.00 64.99  ? 101 ASN   D O     1 
ATOM   7696  C  CB    . ASN   C 2  99  ? 26.659  -18.190 -41.628 1.00 63.36  ? 101 ASN   D CB    1 
ATOM   7697  C  CG    . ASN   C 2  99  ? 25.346  -17.751 -42.306 1.00 66.12  ? 101 ASN   D CG    1 
ATOM   7698  O  OD1   . ASN   C 2  99  ? 24.259  -17.970 -41.770 1.00 67.00  ? 101 ASN   D OD1   1 
ATOM   7699  N  ND2   . ASN   C 2  99  ? 25.449  -17.132 -43.483 1.00 63.07  ? 101 ASN   D ND2   1 
ATOM   7700  N  N     . ASN   C 2  100 ? 29.937  -16.748 -40.635 1.00 62.80  ? 102 ASN   D N     1 
ATOM   7701  C  CA    . ASN   C 2  100 ? 31.154  -17.061 -39.888 1.00 71.91  ? 102 ASN   D CA    1 
ATOM   7702  C  C     . ASN   C 2  100 ? 31.599  -15.821 -39.113 1.00 75.14  ? 102 ASN   D C     1 
ATOM   7703  O  O     . ASN   C 2  100 ? 31.955  -14.799 -39.712 1.00 66.69  ? 102 ASN   D O     1 
ATOM   7704  C  CB    . ASN   C 2  100 ? 32.258  -17.549 -40.839 1.00 63.86  ? 102 ASN   D CB    1 
ATOM   7705  C  CG    . ASN   C 2  100 ? 33.486  -18.066 -40.109 1.00 67.15  ? 102 ASN   D CG    1 
ATOM   7706  O  OD1   . ASN   C 2  100 ? 34.015  -17.402 -39.218 1.00 65.44  ? 102 ASN   D OD1   1 
ATOM   7707  N  ND2   . ASN   C 2  100 ? 33.956  -19.255 -40.495 1.00 74.45  ? 102 ASN   D ND2   1 
ATOM   7708  N  N     . TRP   C 2  101 ? 31.571  -15.911 -37.781 1.00 75.51  ? 103 TRP   D N     1 
ATOM   7709  C  CA    . TRP   C 2  101 ? 32.018  -14.797 -36.948 1.00 75.59  ? 103 TRP   D CA    1 
ATOM   7710  C  C     . TRP   C 2  101 ? 33.467  -14.444 -37.257 1.00 62.15  ? 103 TRP   D C     1 
ATOM   7711  O  O     . TRP   C 2  101 ? 33.778  -13.304 -37.619 1.00 54.85  ? 103 TRP   D O     1 
ATOM   7712  C  CB    . TRP   C 2  101 ? 31.847  -15.148 -35.459 1.00 76.30  ? 103 TRP   D CB    1 
ATOM   7713  C  CG    . TRP   C 2  101 ? 31.918  -13.969 -34.470 1.00 70.82  ? 103 TRP   D CG    1 
ATOM   7714  C  CD1   . TRP   C 2  101 ? 30.916  -13.083 -34.178 1.00 61.53  ? 103 TRP   D CD1   1 
ATOM   7715  C  CD2   . TRP   C 2  101 ? 33.036  -13.593 -33.636 1.00 62.24  ? 103 TRP   D CD2   1 
ATOM   7716  N  NE1   . TRP   C 2  101 ? 31.344  -12.180 -33.233 1.00 63.04  ? 103 TRP   D NE1   1 
ATOM   7717  C  CE2   . TRP   C 2  101 ? 32.634  -12.474 -32.879 1.00 56.20  ? 103 TRP   D CE2   1 
ATOM   7718  C  CE3   . TRP   C 2  101 ? 34.333  -14.094 -33.462 1.00 55.33  ? 103 TRP   D CE3   1 
ATOM   7719  C  CZ2   . TRP   C 2  101 ? 33.481  -11.843 -31.969 1.00 57.13  ? 103 TRP   D CZ2   1 
ATOM   7720  C  CZ3   . TRP   C 2  101 ? 35.172  -13.465 -32.555 1.00 59.83  ? 103 TRP   D CZ3   1 
ATOM   7721  C  CH2   . TRP   C 2  101 ? 34.740  -12.354 -31.817 1.00 61.04  ? 103 TRP   D CH2   1 
ATOM   7722  N  N     . ALA   C 2  102 ? 34.367  -15.423 -37.116 1.00 64.53  ? 104 ALA   D N     1 
ATOM   7723  C  CA    . ALA   C 2  102 ? 35.783  -15.200 -37.390 1.00 61.23  ? 104 ALA   D CA    1 
ATOM   7724  C  C     . ALA   C 2  102 ? 35.968  -14.291 -38.596 1.00 59.32  ? 104 ALA   D C     1 
ATOM   7725  O  O     . ALA   C 2  102 ? 36.730  -13.322 -38.554 1.00 61.75  ? 104 ALA   D O     1 
ATOM   7726  C  CB    . ALA   C 2  102 ? 36.491  -16.540 -37.614 1.00 57.50  ? 104 ALA   D CB    1 
ATOM   7727  N  N     . LYS   C 2  103 ? 35.237  -14.561 -39.671 1.00 60.15  ? 105 LYS   D N     1 
ATOM   7728  C  CA    . LYS   C 2  103 ? 35.494  -13.830 -40.901 1.00 62.52  ? 105 LYS   D CA    1 
ATOM   7729  C  C     . LYS   C 2  103 ? 34.991  -12.393 -40.811 1.00 56.32  ? 105 LYS   D C     1 
ATOM   7730  O  O     . LYS   C 2  103 ? 35.685  -11.466 -41.240 1.00 62.49  ? 105 LYS   D O     1 
ATOM   7731  C  CB    . LYS   C 2  103 ? 34.900  -14.598 -42.090 1.00 73.66  ? 105 LYS   D CB    1 
ATOM   7732  C  CG    . LYS   C 2  103 ? 35.736  -15.861 -42.435 1.00 69.75  ? 105 LYS   D CG    1 
ATOM   7733  C  CD    . LYS   C 2  103 ? 35.073  -16.803 -43.431 1.00 71.96  ? 105 LYS   D CD    1 
ATOM   7734  C  CE    . LYS   C 2  103 ? 35.055  -16.229 -44.838 1.00 80.26  ? 105 LYS   D CE    1 
ATOM   7735  N  NZ    . LYS   C 2  103 ? 34.478  -17.197 -45.821 1.00 80.14  ? 105 LYS   D NZ    1 
ATOM   7736  N  N     . GLY   C 2  104 ? 33.809  -12.174 -40.229 1.00 63.14  ? 106 GLY   D N     1 
ATOM   7737  C  CA    . GLY   C 2  104 ? 33.319  -10.813 -40.040 1.00 55.24  ? 106 GLY   D CA    1 
ATOM   7738  C  C     . GLY   C 2  104 ? 34.088  -10.000 -39.002 1.00 56.76  ? 106 GLY   D C     1 
ATOM   7739  O  O     . GLY   C 2  104 ? 34.106  -8.765  -39.079 1.00 49.23  ? 106 GLY   D O     1 
ATOM   7740  N  N     . HIS   C 2  105 ? 34.741  -10.664 -38.051 1.00 40.38  ? 107 HIS   D N     1 
ATOM   7741  C  CA    . HIS   C 2  105 ? 35.433  -9.995  -36.966 1.00 48.03  ? 107 HIS   D CA    1 
ATOM   7742  C  C     . HIS   C 2  105 ? 36.931  -9.843  -37.210 1.00 57.29  ? 107 HIS   D C     1 
ATOM   7743  O  O     . HIS   C 2  105 ? 37.460  -8.737  -37.084 1.00 65.22  ? 107 HIS   D O     1 
ATOM   7744  C  CB    . HIS   C 2  105 ? 35.181  -10.764 -35.658 1.00 64.60  ? 107 HIS   D CB    1 
ATOM   7745  C  CG    . HIS   C 2  105 ? 35.354  -9.935  -34.421 1.00 67.03  ? 107 HIS   D CG    1 
ATOM   7746  N  ND1   . HIS   C 2  105 ? 34.551  -8.851  -34.130 1.00 58.84  ? 107 HIS   D ND1   1 
ATOM   7747  C  CD2   . HIS   C 2  105 ? 36.242  -10.030 -33.403 1.00 61.11  ? 107 HIS   D CD2   1 
ATOM   7748  C  CE1   . HIS   C 2  105 ? 34.939  -8.316  -32.986 1.00 58.25  ? 107 HIS   D CE1   1 
ATOM   7749  N  NE2   . HIS   C 2  105 ? 35.960  -9.015  -32.523 1.00 55.64  ? 107 HIS   D NE2   1 
ATOM   7750  N  N     . TYR   C 2  106 ? 37.626  -10.926 -37.578 1.00 64.48  ? 108 TYR   D N     1 
ATOM   7751  C  CA    . TYR   C 2  106 ? 39.086  -10.983 -37.554 1.00 66.09  ? 108 TYR   D CA    1 
ATOM   7752  C  C     . TYR   C 2  106 ? 39.768  -10.935 -38.915 1.00 64.57  ? 108 TYR   D C     1 
ATOM   7753  O  O     . TYR   C 2  106 ? 40.926  -10.524 -38.986 1.00 69.68  ? 108 TYR   D O     1 
ATOM   7754  C  CB    . TYR   C 2  106 ? 39.554  -12.258 -36.849 1.00 63.03  ? 108 TYR   D CB    1 
ATOM   7755  C  CG    . TYR   C 2  106 ? 39.336  -12.250 -35.364 1.00 66.95  ? 108 TYR   D CG    1 
ATOM   7756  C  CD1   . TYR   C 2  106 ? 39.679  -11.146 -34.598 1.00 69.22  ? 108 TYR   D CD1   1 
ATOM   7757  C  CD2   . TYR   C 2  106 ? 38.789  -13.351 -34.723 1.00 67.32  ? 108 TYR   D CD2   1 
ATOM   7758  C  CE1   . TYR   C 2  106 ? 39.482  -11.139 -33.228 1.00 66.76  ? 108 TYR   D CE1   1 
ATOM   7759  C  CE2   . TYR   C 2  106 ? 38.587  -13.355 -33.361 1.00 71.72  ? 108 TYR   D CE2   1 
ATOM   7760  C  CZ    . TYR   C 2  106 ? 38.930  -12.247 -32.615 1.00 65.57  ? 108 TYR   D CZ    1 
ATOM   7761  O  OH    . TYR   C 2  106 ? 38.730  -12.263 -31.254 1.00 67.50  ? 108 TYR   D OH    1 
ATOM   7762  N  N     . THR   C 2  107 ? 39.118  -11.375 -39.989 1.00 62.44  ? 109 THR   D N     1 
ATOM   7763  C  CA    . THR   C 2  107 ? 39.815  -11.485 -41.266 1.00 55.87  ? 109 THR   D CA    1 
ATOM   7764  C  C     . THR   C 2  107 ? 39.111  -10.655 -42.337 1.00 58.95  ? 109 THR   D C     1 
ATOM   7765  O  O     . THR   C 2  107 ? 39.494  -9.507  -42.589 1.00 55.85  ? 109 THR   D O     1 
ATOM   7766  C  CB    . THR   C 2  107 ? 39.924  -12.957 -41.705 1.00 61.01  ? 109 THR   D CB    1 
ATOM   7767  O  OG1   . THR   C 2  107 ? 38.635  -13.572 -41.650 1.00 64.94  ? 109 THR   D OG1   1 
ATOM   7768  C  CG2   . THR   C 2  107 ? 40.887  -13.760 -40.824 1.00 48.15  ? 109 THR   D CG2   1 
ATOM   7769  N  N     . GLU   C 2  108 ? 38.081  -11.217 -42.972 1.00 54.78  ? 110 GLU   D N     1 
ATOM   7770  C  CA    . GLU   C 2  108 ? 37.407  -10.508 -44.056 1.00 56.06  ? 110 GLU   D CA    1 
ATOM   7771  C  C     . GLU   C 2  108 ? 36.899  -9.150  -43.591 1.00 61.61  ? 110 GLU   D C     1 
ATOM   7772  O  O     . GLU   C 2  108 ? 37.229  -8.115  -44.179 1.00 64.05  ? 110 GLU   D O     1 
ATOM   7773  C  CB    . GLU   C 2  108 ? 36.256  -11.348 -44.616 1.00 70.24  ? 110 GLU   D CB    1 
ATOM   7774  C  CG    . GLU   C 2  108 ? 36.578  -12.107 -45.893 1.00 70.14  ? 110 GLU   D CG    1 
ATOM   7775  C  CD    . GLU   C 2  108 ? 36.816  -13.586 -45.654 1.00 75.01  ? 110 GLU   D CD    1 
ATOM   7776  O  OE1   . GLU   C 2  108 ? 37.449  -13.950 -44.642 1.00 64.09  ? 110 GLU   D OE1   1 
ATOM   7777  O  OE2   . GLU   C 2  108 ? 36.363  -14.391 -46.488 1.00 93.92  ? 110 GLU   D OE2   1 
ATOM   7778  N  N     . GLY   C 2  109 ? 36.091  -9.133  -42.527 1.00 64.05  ? 111 GLY   D N     1 
ATOM   7779  C  CA    . GLY   C 2  109 ? 35.547  -7.872  -42.042 1.00 56.37  ? 111 GLY   D CA    1 
ATOM   7780  C  C     . GLY   C 2  109 ? 36.618  -6.900  -41.574 1.00 64.65  ? 111 GLY   D C     1 
ATOM   7781  O  O     . GLY   C 2  109 ? 36.478  -5.682  -41.740 1.00 58.89  ? 111 GLY   D O     1 
ATOM   7782  N  N     . ALA   C 2  110 ? 37.698  -7.426  -40.973 1.00 58.03  ? 112 ALA   D N     1 
ATOM   7783  C  CA    . ALA   C 2  110 ? 38.808  -6.580  -40.528 1.00 58.01  ? 112 ALA   D CA    1 
ATOM   7784  C  C     . ALA   C 2  110 ? 39.447  -5.833  -41.694 1.00 60.66  ? 112 ALA   D C     1 
ATOM   7785  O  O     . ALA   C 2  110 ? 39.819  -4.662  -41.565 1.00 58.33  ? 112 ALA   D O     1 
ATOM   7786  C  CB    . ALA   C 2  110 ? 39.858  -7.424  -39.803 1.00 58.89  ? 112 ALA   D CB    1 
ATOM   7787  N  N     . GLU   C 2  111 ? 39.592  -6.496  -42.833 1.00 60.60  ? 113 GLU   D N     1 
ATOM   7788  C  CA    . GLU   C 2  111 ? 40.117  -5.879  -44.040 1.00 58.95  ? 113 GLU   D CA    1 
ATOM   7789  C  C     . GLU   C 2  111 ? 39.137  -4.891  -44.683 1.00 57.80  ? 113 GLU   D C     1 
ATOM   7790  O  O     . GLU   C 2  111 ? 39.308  -4.501  -45.838 1.00 62.91  ? 113 GLU   D O     1 
ATOM   7791  C  CB    . GLU   C 2  111 ? 40.499  -6.973  -45.039 1.00 61.71  ? 113 GLU   D CB    1 
ATOM   7792  C  CG    . GLU   C 2  111 ? 41.573  -7.915  -44.540 1.00 53.52  ? 113 GLU   D CG    1 
ATOM   7793  C  CD    . GLU   C 2  111 ? 41.662  -9.190  -45.365 1.00 73.09  ? 113 GLU   D CD    1 
ATOM   7794  O  OE1   . GLU   C 2  111 ? 40.924  -9.291  -46.377 1.00 66.75  ? 113 GLU   D OE1   1 
ATOM   7795  O  OE2   . GLU   C 2  111 ? 42.459  -10.091 -44.989 1.00 60.53  ? 113 GLU   D OE2   1 
ATOM   7796  N  N     . LEU   C 2  112 ? 38.089  -4.474  -43.983 1.00 56.88  ? 114 LEU   D N     1 
ATOM   7797  C  CA    . LEU   C 2  112 ? 37.140  -3.501  -44.517 1.00 57.10  ? 114 LEU   D CA    1 
ATOM   7798  C  C     . LEU   C 2  112 ? 36.681  -2.477  -43.481 1.00 65.75  ? 114 LEU   D C     1 
ATOM   7799  O  O     . LEU   C 2  112 ? 36.173  -1.412  -43.869 1.00 49.66  ? 114 LEU   D O     1 
ATOM   7800  C  CB    . LEU   C 2  112 ? 35.919  -4.228  -45.105 1.00 54.28  ? 114 LEU   D CB    1 
ATOM   7801  C  CG    . LEU   C 2  112 ? 34.669  -3.451  -45.557 1.00 70.21  ? 114 LEU   D CG    1 
ATOM   7802  C  CD1   . LEU   C 2  112 ? 34.969  -2.416  -46.643 1.00 43.38  ? 114 LEU   D CD1   1 
ATOM   7803  C  CD2   . LEU   C 2  112 ? 33.561  -4.410  -46.008 1.00 64.64  ? 114 LEU   D CD2   1 
ATOM   7804  N  N     . VAL   C 2  113 ? 36.888  -2.744  -42.185 1.00 60.67  ? 115 VAL   D N     1 
ATOM   7805  C  CA    . VAL   C 2  113 ? 36.462  -1.848  -41.111 1.00 57.67  ? 115 VAL   D CA    1 
ATOM   7806  C  C     . VAL   C 2  113 ? 36.949  -0.423  -41.345 1.00 55.68  ? 115 VAL   D C     1 
ATOM   7807  O  O     . VAL   C 2  113 ? 36.206  0.549   -41.155 1.00 49.83  ? 115 VAL   D O     1 
ATOM   7808  C  CB    . VAL   C 2  113 ? 36.962  -2.396  -39.764 1.00 58.91  ? 115 VAL   D CB    1 
ATOM   7809  C  CG1   . VAL   C 2  113 ? 38.425  -2.777  -39.883 1.00 54.72  ? 115 VAL   D CG1   1 
ATOM   7810  C  CG2   . VAL   C 2  113 ? 36.750  -1.375  -38.660 1.00 59.37  ? 115 VAL   D CG2   1 
ATOM   7811  N  N     . ASP   C 2  114 ? 38.210  -0.269  -41.737 1.00 51.91  ? 116 ASP   D N     1 
ATOM   7812  C  CA    . ASP   C 2  114 ? 38.722  1.077   -41.948 1.00 51.60  ? 116 ASP   D CA    1 
ATOM   7813  C  C     . ASP   C 2  114 ? 37.906  1.818   -43.000 1.00 52.53  ? 116 ASP   D C     1 
ATOM   7814  O  O     . ASP   C 2  114 ? 37.674  3.027   -42.888 1.00 46.63  ? 116 ASP   D O     1 
ATOM   7815  C  CB    . ASP   C 2  114 ? 40.188  1.002   -42.333 1.00 41.35  ? 116 ASP   D CB    1 
ATOM   7816  C  CG    . ASP   C 2  114 ? 40.971  0.127   -41.395 1.00 53.07  ? 116 ASP   D CG    1 
ATOM   7817  O  OD1   . ASP   C 2  114 ? 41.181  0.530   -40.229 1.00 45.40  ? 116 ASP   D OD1   1 
ATOM   7818  O  OD2   . ASP   C 2  114 ? 41.350  -0.986  -41.815 1.00 60.90  ? 116 ASP   D OD2   1 
ATOM   7819  N  N     . SER   C 2  115 ? 37.445  1.112   -44.027 1.00 61.37  ? 117 SER   D N     1 
ATOM   7820  C  CA    . SER   C 2  115 ? 36.619  1.787   -45.020 1.00 65.65  ? 117 SER   D CA    1 
ATOM   7821  C  C     . SER   C 2  115 ? 35.326  2.309   -44.400 1.00 64.75  ? 117 SER   D C     1 
ATOM   7822  O  O     . SER   C 2  115 ? 34.830  3.373   -44.803 1.00 52.40  ? 117 SER   D O     1 
ATOM   7823  C  CB    . SER   C 2  115 ? 36.337  0.842   -46.187 1.00 53.72  ? 117 SER   D CB    1 
ATOM   7824  O  OG    . SER   C 2  115 ? 37.556  0.297   -46.661 1.00 62.70  ? 117 SER   D OG    1 
ATOM   7825  N  N     . VAL   C 2  116 ? 34.775  1.581   -43.418 1.00 58.40  ? 118 VAL   D N     1 
ATOM   7826  C  CA    . VAL   C 2  116 ? 33.557  2.015   -42.738 1.00 55.83  ? 118 VAL   D CA    1 
ATOM   7827  C  C     . VAL   C 2  116 ? 33.857  3.153   -41.778 1.00 55.47  ? 118 VAL   D C     1 
ATOM   7828  O  O     . VAL   C 2  116 ? 33.185  4.192   -41.796 1.00 47.08  ? 118 VAL   D O     1 
ATOM   7829  C  CB    . VAL   C 2  116 ? 32.895  0.832   -42.003 1.00 58.18  ? 118 VAL   D CB    1 
ATOM   7830  C  CG1   . VAL   C 2  116 ? 31.659  1.309   -41.228 1.00 57.61  ? 118 VAL   D CG1   1 
ATOM   7831  C  CG2   . VAL   C 2  116 ? 32.539  -0.279  -42.964 1.00 58.91  ? 118 VAL   D CG2   1 
ATOM   7832  N  N     . LEU   C 2  117 ? 34.867  2.953   -40.926 1.00 51.10  ? 119 LEU   D N     1 
ATOM   7833  C  CA    . LEU   C 2  117 ? 35.271  3.967   -39.963 1.00 46.27  ? 119 LEU   D CA    1 
ATOM   7834  C  C     . LEU   C 2  117 ? 35.466  5.319   -40.630 1.00 52.83  ? 119 LEU   D C     1 
ATOM   7835  O  O     . LEU   C 2  117 ? 35.141  6.362   -40.046 1.00 57.52  ? 119 LEU   D O     1 
ATOM   7836  C  CB    . LEU   C 2  117 ? 36.548  3.521   -39.256 1.00 46.36  ? 119 LEU   D CB    1 
ATOM   7837  C  CG    . LEU   C 2  117 ? 36.340  2.368   -38.276 1.00 54.50  ? 119 LEU   D CG    1 
ATOM   7838  C  CD1   . LEU   C 2  117 ? 37.613  2.009   -37.544 1.00 56.12  ? 119 LEU   D CD1   1 
ATOM   7839  C  CD2   . LEU   C 2  117 ? 35.245  2.718   -37.269 1.00 58.55  ? 119 LEU   D CD2   1 
ATOM   7840  N  N     . ASP   C 2  118 ? 35.989  5.321   -41.858 1.00 48.84  ? 120 ASP   D N     1 
ATOM   7841  C  CA    . ASP   C 2  118 ? 36.137  6.566   -42.609 1.00 53.07  ? 120 ASP   D CA    1 
ATOM   7842  C  C     . ASP   C 2  118 ? 34.796  7.272   -42.786 1.00 51.88  ? 120 ASP   D C     1 
ATOM   7843  O  O     . ASP   C 2  118 ? 34.697  8.491   -42.607 1.00 52.08  ? 120 ASP   D O     1 
ATOM   7844  C  CB    . ASP   C 2  118 ? 36.775  6.289   -43.975 1.00 52.10  ? 120 ASP   D CB    1 
ATOM   7845  C  CG    . ASP   C 2  118 ? 38.275  6.133   -43.901 1.00 47.91  ? 120 ASP   D CG    1 
ATOM   7846  O  OD1   . ASP   C 2  118 ? 38.862  6.403   -42.836 1.00 50.04  ? 120 ASP   D OD1   1 
ATOM   7847  O  OD2   . ASP   C 2  118 ? 38.872  5.725   -44.914 1.00 61.63  ? 120 ASP   D OD2   1 
ATOM   7848  N  N     . VAL   C 2  119 ? 33.756  6.524   -43.167 1.00 54.31  ? 121 VAL   D N     1 
ATOM   7849  C  CA    . VAL   C 2  119 ? 32.427  7.117   -43.329 1.00 55.31  ? 121 VAL   D CA    1 
ATOM   7850  C  C     . VAL   C 2  119 ? 31.914  7.624   -41.991 1.00 53.51  ? 121 VAL   D C     1 
ATOM   7851  O  O     . VAL   C 2  119 ? 31.433  8.754   -41.874 1.00 41.96  ? 121 VAL   D O     1 
ATOM   7852  C  CB    . VAL   C 2  119 ? 31.450  6.094   -43.933 1.00 56.74  ? 121 VAL   D CB    1 
ATOM   7853  C  CG1   . VAL   C 2  119 ? 30.289  6.805   -44.611 1.00 56.31  ? 121 VAL   D CG1   1 
ATOM   7854  C  CG2   . VAL   C 2  119 ? 32.178  5.141   -44.873 1.00 66.02  ? 121 VAL   D CG2   1 
ATOM   7855  N  N     . VAL   C 2  120 ? 31.994  6.778   -40.963 1.00 53.12  ? 122 VAL   D N     1 
ATOM   7856  C  CA    . VAL   C 2  120 ? 31.541  7.176   -39.638 1.00 52.84  ? 122 VAL   D CA    1 
ATOM   7857  C  C     . VAL   C 2  120 ? 32.136  8.533   -39.275 1.00 61.08  ? 122 VAL   D C     1 
ATOM   7858  O  O     . VAL   C 2  120 ? 31.417  9.471   -38.900 1.00 61.40  ? 122 VAL   D O     1 
ATOM   7859  C  CB    . VAL   C 2  120 ? 31.900  6.088   -38.610 1.00 52.70  ? 122 VAL   D CB    1 
ATOM   7860  C  CG1   . VAL   C 2  120 ? 31.048  6.211   -37.367 1.00 51.86  ? 122 VAL   D CG1   1 
ATOM   7861  C  CG2   . VAL   C 2  120 ? 31.731  4.716   -39.229 1.00 57.44  ? 122 VAL   D CG2   1 
ATOM   7862  N  N     . ARG   C 2  121 ? 33.459  8.669   -39.435 1.00 64.34  ? 123 ARG   D N     1 
ATOM   7863  C  CA    . ARG   C 2  121 ? 34.151  9.902   -39.070 1.00 49.29  ? 123 ARG   D CA    1 
ATOM   7864  C  C     . ARG   C 2  121 ? 33.525  11.119  -39.744 1.00 56.96  ? 123 ARG   D C     1 
ATOM   7865  O  O     . ARG   C 2  121 ? 33.099  12.066  -39.071 1.00 55.60  ? 123 ARG   D O     1 
ATOM   7866  C  CB    . ARG   C 2  121 ? 35.630  9.794   -39.427 1.00 47.96  ? 123 ARG   D CB    1 
ATOM   7867  C  CG    . ARG   C 2  121 ? 36.416  8.861   -38.533 1.00 60.61  ? 123 ARG   D CG    1 
ATOM   7868  C  CD    . ARG   C 2  121 ? 37.897  8.878   -38.892 1.00 50.51  ? 123 ARG   D CD    1 
ATOM   7869  N  NE    . ARG   C 2  121 ? 38.638  7.848   -38.176 1.00 51.52  ? 123 ARG   D NE    1 
ATOM   7870  C  CZ    . ARG   C 2  121 ? 38.984  6.676   -38.690 1.00 51.82  ? 123 ARG   D CZ    1 
ATOM   7871  N  NH1   . ARG   C 2  121 ? 38.685  6.355   -39.937 1.00 60.98  ? 123 ARG   D NH1   1 
ATOM   7872  N  NH2   . ARG   C 2  121 ? 39.651  5.804   -37.936 1.00 53.05  ? 123 ARG   D NH2   1 
ATOM   7873  N  N     . LYS   C 2  122 ? 33.467  11.116  -41.082 1.00 56.87  ? 124 LYS   D N     1 
ATOM   7874  C  CA    . LYS   C 2  122 ? 32.862  12.244  -41.792 1.00 61.51  ? 124 LYS   D CA    1 
ATOM   7875  C  C     . LYS   C 2  122 ? 31.445  12.515  -41.299 1.00 57.62  ? 124 LYS   D C     1 
ATOM   7876  O  O     . LYS   C 2  122 ? 30.974  13.661  -41.334 1.00 52.13  ? 124 LYS   D O     1 
ATOM   7877  C  CB    . LYS   C 2  122 ? 32.874  11.997  -43.309 1.00 52.26  ? 124 LYS   D CB    1 
ATOM   7878  C  CG    . LYS   C 2  122 ? 34.265  12.059  -43.928 1.00 71.74  ? 124 LYS   D CG    1 
ATOM   7879  C  CD    . LYS   C 2  122 ? 34.241  12.696  -45.309 1.00 86.95  ? 124 LYS   D CD    1 
ATOM   7880  C  CE    . LYS   C 2  122 ? 33.979  14.200  -45.236 1.00 88.67  ? 124 LYS   D CE    1 
ATOM   7881  N  NZ    . LYS   C 2  122 ? 33.870  14.817  -46.593 1.00 87.08  ? 124 LYS   D NZ    1 
ATOM   7882  N  N     . GLU   C 2  123 ? 30.750  11.476  -40.835 1.00 54.65  ? 125 GLU   D N     1 
ATOM   7883  C  CA    . GLU   C 2  123 ? 29.462  11.682  -40.195 1.00 48.75  ? 125 GLU   D CA    1 
ATOM   7884  C  C     . GLU   C 2  123 ? 29.639  12.321  -38.827 1.00 51.98  ? 125 GLU   D C     1 
ATOM   7885  O  O     . GLU   C 2  123 ? 29.025  13.353  -38.524 1.00 56.60  ? 125 GLU   D O     1 
ATOM   7886  C  CB    . GLU   C 2  123 ? 28.708  10.360  -40.094 1.00 52.35  ? 125 GLU   D CB    1 
ATOM   7887  C  CG    . GLU   C 2  123 ? 28.083  9.913   -41.415 1.00 49.70  ? 125 GLU   D CG    1 
ATOM   7888  C  CD    . GLU   C 2  123 ? 27.214  10.996  -42.054 1.00 51.44  ? 125 GLU   D CD    1 
ATOM   7889  O  OE1   . GLU   C 2  123 ? 27.027  12.065  -41.435 1.00 50.80  ? 125 GLU   D OE1   1 
ATOM   7890  O  OE2   . GLU   C 2  123 ? 26.713  10.781  -43.178 1.00 49.99  ? 125 GLU   D OE2   1 
ATOM   7891  N  N     . SER   C 2  124 ? 30.501  11.750  -37.996 1.00 48.35  ? 126 SER   D N     1 
ATOM   7892  C  CA    . SER   C 2  124 ? 30.639  12.296  -36.651 1.00 59.46  ? 126 SER   D CA    1 
ATOM   7893  C  C     . SER   C 2  124 ? 31.218  13.710  -36.644 1.00 66.81  ? 126 SER   D C     1 
ATOM   7894  O  O     . SER   C 2  124 ? 30.963  14.459  -35.691 1.00 61.91  ? 126 SER   D O     1 
ATOM   7895  C  CB    . SER   C 2  124 ? 31.487  11.360  -35.798 1.00 46.96  ? 126 SER   D CB    1 
ATOM   7896  O  OG    . SER   C 2  124 ? 30.822  10.126  -35.650 1.00 43.57  ? 126 SER   D OG    1 
ATOM   7897  N  N     . GLU   C 2  125 ? 31.957  14.099  -37.696 1.00 65.14  ? 127 GLU   D N     1 
ATOM   7898  C  CA    . GLU   C 2  125 ? 32.638  15.396  -37.716 1.00 59.94  ? 127 GLU   D CA    1 
ATOM   7899  C  C     . GLU   C 2  125 ? 31.661  16.545  -37.953 1.00 54.36  ? 127 GLU   D C     1 
ATOM   7900  O  O     . GLU   C 2  125 ? 31.789  17.612  -37.344 1.00 62.77  ? 127 GLU   D O     1 
ATOM   7901  C  CB    . GLU   C 2  125 ? 33.730  15.401  -38.790 1.00 70.29  ? 127 GLU   D CB    1 
ATOM   7902  C  CG    . GLU   C 2  125 ? 33.195  15.499  -40.238 1.00 78.59  ? 127 GLU   D CG    1 
ATOM   7903  C  CD    . GLU   C 2  125 ? 34.284  15.379  -41.319 1.00 86.49  ? 127 GLU   D CD    1 
ATOM   7904  O  OE1   . GLU   C 2  125 ? 35.407  14.907  -41.009 1.00 83.64  ? 127 GLU   D OE1   1 
ATOM   7905  O  OE2   . GLU   C 2  125 ? 34.009  15.757  -42.486 1.00 78.65  ? 127 GLU   D OE2   1 
ATOM   7906  N  N     . SER   C 2  126 ? 30.691  16.361  -38.835 1.00 56.45  ? 128 SER   D N     1 
ATOM   7907  C  CA    . SER   C 2  126 ? 29.719  17.417  -39.118 1.00 59.96  ? 128 SER   D CA    1 
ATOM   7908  C  C     . SER   C 2  126 ? 28.578  17.482  -38.097 1.00 76.80  ? 128 SER   D C     1 
ATOM   7909  O  O     . SER   C 2  126 ? 27.429  17.754  -38.471 1.00 77.28  ? 128 SER   D O     1 
ATOM   7910  C  CB    . SER   C 2  126 ? 29.172  17.217  -40.529 1.00 70.53  ? 128 SER   D CB    1 
ATOM   7911  O  OG    . SER   C 2  126 ? 27.771  17.463  -40.583 1.00 78.01  ? 128 SER   D OG    1 
ATOM   7912  N  N     . CYS   C 2  127 ? 28.858  17.255  -36.809 1.00 61.52  ? 129 CYS   D N     1 
ATOM   7913  C  CA    . CYS   C 2  127 ? 27.822  17.097  -35.794 1.00 53.50  ? 129 CYS   D CA    1 
ATOM   7914  C  C     . CYS   C 2  127 ? 27.943  18.189  -34.734 1.00 63.48  ? 129 CYS   D C     1 
ATOM   7915  O  O     . CYS   C 2  127 ? 28.998  18.341  -34.113 1.00 57.22  ? 129 CYS   D O     1 
ATOM   7916  C  CB    . CYS   C 2  127 ? 27.907  15.712  -35.149 1.00 57.68  ? 129 CYS   D CB    1 
ATOM   7917  S  SG    . CYS   C 2  127 ? 26.895  14.434  -35.927 1.00 50.69  ? 129 CYS   D SG    1 
ATOM   7918  N  N     . ASP   C 2  128 ? 26.854  18.936  -34.526 1.00 68.09  ? 130 ASP   D N     1 
ATOM   7919  C  CA    . ASP   C 2  128 ? 26.778  19.923  -33.450 1.00 57.77  ? 130 ASP   D CA    1 
ATOM   7920  C  C     . ASP   C 2  128 ? 27.235  19.330  -32.130 1.00 51.23  ? 130 ASP   D C     1 
ATOM   7921  O  O     . ASP   C 2  128 ? 28.127  19.861  -31.461 1.00 60.06  ? 130 ASP   D O     1 
ATOM   7922  C  CB    . ASP   C 2  128 ? 25.335  20.431  -33.303 1.00 67.97  ? 130 ASP   D CB    1 
ATOM   7923  C  CG    . ASP   C 2  128 ? 25.089  21.742  -34.013 1.00 80.48  ? 130 ASP   D CG    1 
ATOM   7924  O  OD1   . ASP   C 2  128 ? 26.018  22.573  -34.050 1.00 103.41 ? 130 ASP   D OD1   1 
ATOM   7925  O  OD2   . ASP   C 2  128 ? 23.963  21.947  -34.523 1.00 75.34  ? 130 ASP   D OD2   1 
ATOM   7926  N  N     . CYS   C 2  129 ? 26.579  18.246  -31.719 1.00 61.07  ? 131 CYS   D N     1 
ATOM   7927  C  CA    . CYS   C 2  129 ? 26.779  17.616  -30.419 1.00 59.09  ? 131 CYS   D CA    1 
ATOM   7928  C  C     . CYS   C 2  129 ? 26.328  16.167  -30.514 1.00 60.06  ? 131 CYS   D C     1 
ATOM   7929  O  O     . CYS   C 2  129 ? 25.184  15.836  -30.177 1.00 61.67  ? 131 CYS   D O     1 
ATOM   7930  C  CB    . CYS   C 2  129 ? 26.006  18.358  -29.325 1.00 60.60  ? 131 CYS   D CB    1 
ATOM   7931  S  SG    . CYS   C 2  129 ? 25.877  17.459  -27.771 1.00 66.46  ? 131 CYS   D SG    1 
ATOM   7932  N  N     . LEU   C 2  130 ? 27.224  15.308  -30.994 1.00 52.34  ? 132 LEU   D N     1 
ATOM   7933  C  CA    . LEU   C 2  130 ? 26.886  13.924  -31.287 1.00 48.02  ? 132 LEU   D CA    1 
ATOM   7934  C  C     . LEU   C 2  130 ? 26.554  13.155  -30.009 1.00 54.10  ? 132 LEU   D C     1 
ATOM   7935  O  O     . LEU   C 2  130 ? 27.232  13.288  -28.985 1.00 52.99  ? 132 LEU   D O     1 
ATOM   7936  C  CB    . LEU   C 2  130 ? 28.047  13.273  -32.038 1.00 44.55  ? 132 LEU   D CB    1 
ATOM   7937  C  CG    . LEU   C 2  130 ? 28.283  11.764  -32.013 1.00 40.27  ? 132 LEU   D CG    1 
ATOM   7938  C  CD1   . LEU   C 2  130 ? 27.322  11.026  -32.929 1.00 43.74  ? 132 LEU   D CD1   1 
ATOM   7939  C  CD2   . LEU   C 2  130 ? 29.715  11.496  -32.412 1.00 34.78  ? 132 LEU   D CD2   1 
ATOM   7940  N  N     . GLN   C 2  131 ? 25.488  12.352  -30.067 1.00 48.03  ? 133 GLN   D N     1 
ATOM   7941  C  CA    . GLN   C 2  131 ? 25.084  11.577  -28.899 1.00 43.36  ? 133 GLN   D CA    1 
ATOM   7942  C  C     . GLN   C 2  131 ? 25.846  10.271  -28.783 1.00 39.87  ? 133 GLN   D C     1 
ATOM   7943  O  O     . GLN   C 2  131 ? 26.209  9.855   -27.682 1.00 46.68  ? 133 GLN   D O     1 
ATOM   7944  C  CB    . GLN   C 2  131 ? 23.602  11.247  -28.965 1.00 51.85  ? 133 GLN   D CB    1 
ATOM   7945  C  CG    . GLN   C 2  131 ? 22.687  12.402  -29.069 1.00 44.75  ? 133 GLN   D CG    1 
ATOM   7946  C  CD    . GLN   C 2  131 ? 21.281  11.937  -29.043 1.00 36.98  ? 133 GLN   D CD    1 
ATOM   7947  O  OE1   . GLN   C 2  131 ? 20.859  11.278  -28.095 1.00 41.49  ? 133 GLN   D OE1   1 
ATOM   7948  N  NE2   . GLN   C 2  131 ? 20.540  12.238  -30.100 1.00 45.93  ? 133 GLN   D NE2   1 
ATOM   7949  N  N     . GLY   C 2  132 ? 26.056  9.601   -29.893 1.00 49.30  ? 134 GLY   D N     1 
ATOM   7950  C  CA    . GLY   C 2  132 ? 26.509  8.230   -29.894 1.00 41.03  ? 134 GLY   D CA    1 
ATOM   7951  C  C     . GLY   C 2  132 ? 25.981  7.560   -31.141 1.00 42.87  ? 134 GLY   D C     1 
ATOM   7952  O  O     . GLY   C 2  132 ? 25.486  8.219   -32.053 1.00 40.57  ? 134 GLY   D O     1 
ATOM   7953  N  N     . PHE   C 2  133 ? 26.063  6.233   -31.150 1.00 49.20  ? 135 PHE   D N     1 
ATOM   7954  C  CA    . PHE   C 2  133 ? 25.795  5.456   -32.352 1.00 57.74  ? 135 PHE   D CA    1 
ATOM   7955  C  C     . PHE   C 2  133 ? 24.698  4.430   -32.107 1.00 45.24  ? 135 PHE   D C     1 
ATOM   7956  O  O     . PHE   C 2  133 ? 24.501  3.965   -30.982 1.00 48.14  ? 135 PHE   D O     1 
ATOM   7957  C  CB    . PHE   C 2  133 ? 27.074  4.755   -32.847 1.00 52.37  ? 135 PHE   D CB    1 
ATOM   7958  C  CG    . PHE   C 2  133 ? 28.249  5.665   -32.946 1.00 45.74  ? 135 PHE   D CG    1 
ATOM   7959  C  CD1   . PHE   C 2  133 ? 28.961  6.015   -31.816 1.00 40.03  ? 135 PHE   D CD1   1 
ATOM   7960  C  CD2   . PHE   C 2  133 ? 28.627  6.195   -34.169 1.00 43.42  ? 135 PHE   D CD2   1 
ATOM   7961  C  CE1   . PHE   C 2  133 ? 30.037  6.882   -31.906 1.00 48.27  ? 135 PHE   D CE1   1 
ATOM   7962  C  CE2   . PHE   C 2  133 ? 29.703  7.045   -34.266 1.00 45.35  ? 135 PHE   D CE2   1 
ATOM   7963  C  CZ    . PHE   C 2  133 ? 30.411  7.396   -33.132 1.00 44.62  ? 135 PHE   D CZ    1 
ATOM   7964  N  N     . GLN   C 2  134 ? 23.998  4.077   -33.186 1.00 45.47  ? 136 GLN   D N     1 
ATOM   7965  C  CA    . GLN   C 2  134 ? 22.864  3.156   -33.160 1.00 41.06  ? 136 GLN   D CA    1 
ATOM   7966  C  C     . GLN   C 2  134 ? 23.082  2.138   -34.268 1.00 39.80  ? 136 GLN   D C     1 
ATOM   7967  O  O     . GLN   C 2  134 ? 22.988  2.487   -35.444 1.00 48.71  ? 136 GLN   D O     1 
ATOM   7968  C  CB    . GLN   C 2  134 ? 21.559  3.929   -33.364 1.00 47.27  ? 136 GLN   D CB    1 
ATOM   7969  C  CG    . GLN   C 2  134 ? 20.295  3.109   -33.573 1.00 52.32  ? 136 GLN   D CG    1 
ATOM   7970  C  CD    . GLN   C 2  134 ? 19.097  3.980   -33.983 1.00 53.53  ? 136 GLN   D CD    1 
ATOM   7971  O  OE1   . GLN   C 2  134 ? 18.330  4.452   -33.136 1.00 51.00  ? 136 GLN   D OE1   1 
ATOM   7972  N  NE2   . GLN   C 2  134 ? 18.935  4.189   -35.285 1.00 48.81  ? 136 GLN   D NE2   1 
ATOM   7973  N  N     . LEU   C 2  135 ? 23.383  0.893   -33.907 1.00 38.61  ? 137 LEU   D N     1 
ATOM   7974  C  CA    . LEU   C 2  135 ? 23.682  -0.165  -34.870 1.00 40.75  ? 137 LEU   D CA    1 
ATOM   7975  C  C     . LEU   C 2  135 ? 22.583  -1.219  -34.853 1.00 43.98  ? 137 LEU   D C     1 
ATOM   7976  O  O     . LEU   C 2  135 ? 22.273  -1.768  -33.794 1.00 54.37  ? 137 LEU   D O     1 
ATOM   7977  C  CB    . LEU   C 2  135 ? 25.026  -0.824  -34.562 1.00 45.57  ? 137 LEU   D CB    1 
ATOM   7978  C  CG    . LEU   C 2  135 ? 25.248  -2.192  -35.224 1.00 44.67  ? 137 LEU   D CG    1 
ATOM   7979  C  CD1   . LEU   C 2  135 ? 25.681  -2.047  -36.682 1.00 43.31  ? 137 LEU   D CD1   1 
ATOM   7980  C  CD2   . LEU   C 2  135 ? 26.240  -3.081  -34.446 1.00 40.17  ? 137 LEU   D CD2   1 
ATOM   7981  N  N     . THR   C 2  136 ? 21.992  -1.490  -36.020 1.00 49.54  ? 138 THR   D N     1 
ATOM   7982  C  CA    . THR   C 2  136 ? 21.118  -2.644  -36.228 1.00 46.08  ? 138 THR   D CA    1 
ATOM   7983  C  C     . THR   C 2  136 ? 21.938  -3.757  -36.854 1.00 48.09  ? 138 THR   D C     1 
ATOM   7984  O  O     . THR   C 2  136 ? 22.652  -3.534  -37.838 1.00 46.55  ? 138 THR   D O     1 
ATOM   7985  C  CB    . THR   C 2  136 ? 19.937  -2.331  -37.148 1.00 47.89  ? 138 THR   D CB    1 
ATOM   7986  O  OG1   . THR   C 2  136 ? 20.432  -1.812  -38.378 1.00 53.53  ? 138 THR   D OG1   1 
ATOM   7987  C  CG2   . THR   C 2  136 ? 18.976  -1.317  -36.530 1.00 57.55  ? 138 THR   D CG2   1 
ATOM   7988  N  N     . HIS   C 2  137 ? 21.836  -4.946  -36.288 1.00 46.92  ? 139 HIS   D N     1 
ATOM   7989  C  CA    . HIS   C 2  137 ? 22.670  -6.050  -36.734 1.00 54.97  ? 139 HIS   D CA    1 
ATOM   7990  C  C     . HIS   C 2  137 ? 22.082  -7.330  -36.167 1.00 55.35  ? 139 HIS   D C     1 
ATOM   7991  O  O     . HIS   C 2  137 ? 21.357  -7.305  -35.169 1.00 56.38  ? 139 HIS   D O     1 
ATOM   7992  C  CB    . HIS   C 2  137 ? 24.122  -5.881  -36.278 1.00 47.57  ? 139 HIS   D CB    1 
ATOM   7993  C  CG    . HIS   C 2  137 ? 24.336  -6.210  -34.834 1.00 48.62  ? 139 HIS   D CG    1 
ATOM   7994  N  ND1   . HIS   C 2  137 ? 25.313  -7.083  -34.405 1.00 48.50  ? 139 HIS   D ND1   1 
ATOM   7995  C  CD2   . HIS   C 2  137 ? 23.690  -5.791  -33.719 1.00 49.42  ? 139 HIS   D CD2   1 
ATOM   7996  C  CE1   . HIS   C 2  137 ? 25.263  -7.185  -33.088 1.00 46.48  ? 139 HIS   D CE1   1 
ATOM   7997  N  NE2   . HIS   C 2  137 ? 24.287  -6.412  -32.647 1.00 50.45  ? 139 HIS   D NE2   1 
ATOM   7998  N  N     . SER   C 2  138 ? 22.396  -8.442  -36.813 1.00 42.41  ? 140 SER   D N     1 
ATOM   7999  C  CA    . SER   C 2  138 ? 21.993  -9.745  -36.316 1.00 49.64  ? 140 SER   D CA    1 
ATOM   8000  C  C     . SER   C 2  138 ? 23.162  -10.397 -35.593 1.00 47.00  ? 140 SER   D C     1 
ATOM   8001  O  O     . SER   C 2  138 ? 24.309  -9.973  -35.726 1.00 44.15  ? 140 SER   D O     1 
ATOM   8002  C  CB    . SER   C 2  138 ? 21.501  -10.634 -37.457 1.00 53.62  ? 140 SER   D CB    1 
ATOM   8003  O  OG    . SER   C 2  138 ? 21.780  -11.989 -37.181 1.00 60.71  ? 140 SER   D OG    1 
ATOM   8004  N  N     . LEU   C 2  139 ? 22.856  -11.430 -34.807 1.00 46.03  ? 141 LEU   D N     1 
ATOM   8005  C  CA    . LEU   C 2  139 ? 23.868  -12.125 -34.022 1.00 47.92  ? 141 LEU   D CA    1 
ATOM   8006  C  C     . LEU   C 2  139 ? 24.207  -13.507 -34.544 1.00 49.46  ? 141 LEU   D C     1 
ATOM   8007  O  O     . LEU   C 2  139 ? 25.280  -14.023 -34.215 1.00 48.29  ? 141 LEU   D O     1 
ATOM   8008  C  CB    . LEU   C 2  139 ? 23.427  -12.256 -32.553 1.00 51.26  ? 141 LEU   D CB    1 
ATOM   8009  C  CG    . LEU   C 2  139 ? 23.780  -11.114 -31.589 1.00 50.12  ? 141 LEU   D CG    1 
ATOM   8010  C  CD1   . LEU   C 2  139 ? 23.251  -9.790  -32.106 1.00 44.66  ? 141 LEU   D CD1   1 
ATOM   8011  C  CD2   . LEU   C 2  139 ? 23.243  -11.372 -30.182 1.00 56.56  ? 141 LEU   D CD2   1 
ATOM   8012  N  N     . GLY   C 2  140 ? 23.327  -14.115 -35.339 1.00 56.02  ? 142 GLY   D N     1 
ATOM   8013  C  CA    . GLY   C 2  140 ? 23.550  -15.453 -35.858 1.00 58.88  ? 142 GLY   D CA    1 
ATOM   8014  C  C     . GLY   C 2  140 ? 24.325  -15.492 -37.162 1.00 65.32  ? 142 GLY   D C     1 
ATOM   8015  O  O     . GLY   C 2  140 ? 25.207  -16.342 -37.334 1.00 64.62  ? 142 GLY   D O     1 
ATOM   8016  N  N     . GLY   C 2  141 ? 24.000  -14.576 -38.082 1.00 64.53  ? 143 GLY   D N     1 
ATOM   8017  C  CA    . GLY   C 2  141 ? 24.684  -14.445 -39.358 1.00 63.44  ? 143 GLY   D CA    1 
ATOM   8018  C  C     . GLY   C 2  141 ? 26.183  -14.211 -39.280 1.00 60.22  ? 143 GLY   D C     1 
ATOM   8019  O  O     . GLY   C 2  141 ? 26.839  -14.632 -38.323 1.00 52.55  ? 143 GLY   D O     1 
ATOM   8020  N  N     . GLY   C 2  142 ? 26.744  -13.542 -40.285 1.00 63.52  ? 144 GLY   D N     1 
ATOM   8021  C  CA    . GLY   C 2  142 ? 28.190  -13.452 -40.355 1.00 53.09  ? 144 GLY   D CA    1 
ATOM   8022  C  C     . GLY   C 2  142 ? 28.761  -12.057 -40.220 1.00 58.94  ? 144 GLY   D C     1 
ATOM   8023  O  O     . GLY   C 2  142 ? 29.554  -11.802 -39.308 1.00 51.80  ? 144 GLY   D O     1 
ATOM   8024  N  N     . THR   C 2  143 ? 28.376  -11.154 -41.132 1.00 65.40  ? 145 THR   D N     1 
ATOM   8025  C  CA    . THR   C 2  143 ? 28.896  -9.786  -41.112 1.00 59.85  ? 145 THR   D CA    1 
ATOM   8026  C  C     . THR   C 2  143 ? 28.374  -9.016  -39.900 1.00 60.30  ? 145 THR   D C     1 
ATOM   8027  O  O     . THR   C 2  143 ? 29.155  -8.464  -39.115 1.00 57.76  ? 145 THR   D O     1 
ATOM   8028  C  CB    . THR   C 2  143 ? 28.524  -9.051  -42.408 1.00 53.08  ? 145 THR   D CB    1 
ATOM   8029  O  OG1   . THR   C 2  143 ? 28.696  -9.918  -43.531 1.00 63.64  ? 145 THR   D OG1   1 
ATOM   8030  C  CG2   . THR   C 2  143 ? 29.401  -7.851  -42.601 1.00 45.79  ? 145 THR   D CG2   1 
ATOM   8031  N  N     . GLY   C 2  144 ? 27.049  -8.951  -39.738 1.00 57.59  ? 146 GLY   D N     1 
ATOM   8032  C  CA    . GLY   C 2  144 ? 26.491  -8.198  -38.621 1.00 58.53  ? 146 GLY   D CA    1 
ATOM   8033  C  C     . GLY   C 2  144 ? 27.015  -8.672  -37.275 1.00 58.35  ? 146 GLY   D C     1 
ATOM   8034  O  O     . GLY   C 2  144 ? 27.405  -7.871  -36.423 1.00 55.92  ? 146 GLY   D O     1 
ATOM   8035  N  N     . SER   C 2  145 ? 27.029  -9.982  -37.062 1.00 55.10  ? 147 SER   D N     1 
ATOM   8036  C  CA    . SER   C 2  145 ? 27.527  -10.497 -35.796 1.00 49.80  ? 147 SER   D CA    1 
ATOM   8037  C  C     . SER   C 2  145 ? 29.006  -10.178 -35.629 1.00 53.85  ? 147 SER   D C     1 
ATOM   8038  O  O     . SER   C 2  145 ? 29.404  -9.504  -34.674 1.00 56.94  ? 147 SER   D O     1 
ATOM   8039  C  CB    . SER   C 2  145 ? 27.271  -12.003 -35.714 1.00 54.21  ? 147 SER   D CB    1 
ATOM   8040  O  OG    . SER   C 2  145 ? 28.181  -12.625 -34.830 1.00 61.87  ? 147 SER   D OG    1 
ATOM   8041  N  N     . GLY   C 2  146 ? 29.839  -10.641 -36.567 1.00 64.27  ? 148 GLY   D N     1 
ATOM   8042  C  CA    . GLY   C 2  146 ? 31.283  -10.562 -36.394 1.00 59.06  ? 148 GLY   D CA    1 
ATOM   8043  C  C     . GLY   C 2  146 ? 31.888  -9.209  -36.703 1.00 52.12  ? 148 GLY   D C     1 
ATOM   8044  O  O     . GLY   C 2  146 ? 32.860  -8.806  -36.053 1.00 55.23  ? 148 GLY   D O     1 
ATOM   8045  N  N     . MET   C 2  147 ? 31.324  -8.481  -37.665 1.00 37.34  ? 149 MET   D N     1 
ATOM   8046  C  CA    . MET   C 2  147 ? 31.866  -7.189  -38.060 1.00 54.16  ? 149 MET   D CA    1 
ATOM   8047  C  C     . MET   C 2  147 ? 31.161  -6.017  -37.384 1.00 56.20  ? 149 MET   D C     1 
ATOM   8048  O  O     . MET   C 2  147 ? 31.755  -4.934  -37.265 1.00 46.81  ? 149 MET   D O     1 
ATOM   8049  C  CB    . MET   C 2  147 ? 31.800  -7.027  -39.591 1.00 42.57  ? 149 MET   D CB    1 
ATOM   8050  C  CG    . MET   C 2  147 ? 32.781  -5.990  -40.148 1.00 37.12  ? 149 MET   D CG    1 
ATOM   8051  S  SD    . MET   C 2  147 ? 32.206  -5.105  -41.620 1.00 51.50  ? 149 MET   D SD    1 
ATOM   8052  C  CE    . MET   C 2  147 ? 33.516  -3.888  -41.831 1.00 53.62  ? 149 MET   D CE    1 
ATOM   8053  N  N     . GLY   C 2  148 ? 29.910  -6.207  -36.956 1.00 52.99  ? 150 GLY   D N     1 
ATOM   8054  C  CA    . GLY   C 2  148 ? 29.266  -5.215  -36.114 1.00 46.71  ? 150 GLY   D CA    1 
ATOM   8055  C  C     . GLY   C 2  148 ? 29.941  -5.085  -34.760 1.00 52.15  ? 150 GLY   D C     1 
ATOM   8056  O  O     . GLY   C 2  148 ? 30.034  -3.985  -34.210 1.00 48.83  ? 150 GLY   D O     1 
ATOM   8057  N  N     . THR   C 2  149 ? 30.434  -6.201  -34.206 1.00 42.21  ? 151 THR   D N     1 
ATOM   8058  C  CA    . THR   C 2  149 ? 31.127  -6.116  -32.928 1.00 46.29  ? 151 THR   D CA    1 
ATOM   8059  C  C     . THR   C 2  149 ? 32.560  -5.634  -33.078 1.00 55.24  ? 151 THR   D C     1 
ATOM   8060  O  O     . THR   C 2  149 ? 33.127  -5.116  -32.110 1.00 63.98  ? 151 THR   D O     1 
ATOM   8061  C  CB    . THR   C 2  149 ? 31.099  -7.463  -32.179 1.00 60.63  ? 151 THR   D CB    1 
ATOM   8062  O  OG1   . THR   C 2  149 ? 31.330  -8.556  -33.079 1.00 61.82  ? 151 THR   D OG1   1 
ATOM   8063  C  CG2   . THR   C 2  149 ? 29.756  -7.664  -31.479 1.00 57.00  ? 151 THR   D CG2   1 
ATOM   8064  N  N     . LEU   C 2  150 ? 33.162  -5.779  -34.259 1.00 60.69  ? 152 LEU   D N     1 
ATOM   8065  C  CA    . LEU   C 2  150 ? 34.437  -5.113  -34.483 1.00 55.17  ? 152 LEU   D CA    1 
ATOM   8066  C  C     . LEU   C 2  150 ? 34.232  -3.630  -34.749 1.00 49.82  ? 152 LEU   D C     1 
ATOM   8067  O  O     . LEU   C 2  150 ? 35.037  -2.807  -34.310 1.00 63.05  ? 152 LEU   D O     1 
ATOM   8068  C  CB    . LEU   C 2  150 ? 35.196  -5.764  -35.641 1.00 66.05  ? 152 LEU   D CB    1 
ATOM   8069  C  CG    . LEU   C 2  150 ? 36.683  -5.392  -35.764 1.00 64.64  ? 152 LEU   D CG    1 
ATOM   8070  C  CD1   . LEU   C 2  150 ? 37.505  -5.982  -34.606 1.00 50.77  ? 152 LEU   D CD1   1 
ATOM   8071  C  CD2   . LEU   C 2  150 ? 37.243  -5.830  -37.117 1.00 62.15  ? 152 LEU   D CD2   1 
ATOM   8072  N  N     . LEU   C 2  151 ? 33.166  -3.265  -35.465 1.00 43.63  ? 153 LEU   D N     1 
ATOM   8073  C  CA    . LEU   C 2  151 ? 32.845  -1.850  -35.619 1.00 47.63  ? 153 LEU   D CA    1 
ATOM   8074  C  C     . LEU   C 2  151 ? 32.605  -1.180  -34.265 1.00 54.84  ? 153 LEU   D C     1 
ATOM   8075  O  O     . LEU   C 2  151 ? 32.965  -0.012  -34.068 1.00 53.63  ? 153 LEU   D O     1 
ATOM   8076  C  CB    . LEU   C 2  151 ? 31.623  -1.676  -36.518 1.00 40.08  ? 153 LEU   D CB    1 
ATOM   8077  C  CG    . LEU   C 2  151 ? 31.927  -1.538  -37.995 1.00 54.02  ? 153 LEU   D CG    1 
ATOM   8078  C  CD1   . LEU   C 2  151 ? 30.730  -0.985  -38.723 1.00 59.06  ? 153 LEU   D CD1   1 
ATOM   8079  C  CD2   . LEU   C 2  151 ? 33.121  -0.629  -38.172 1.00 62.49  ? 153 LEU   D CD2   1 
ATOM   8080  N  N     . ILE   C 2  152 ? 31.993  -1.896  -33.317 1.00 45.13  ? 154 ILE   D N     1 
ATOM   8081  C  CA    . ILE   C 2  152 ? 31.690  -1.284  -32.026 1.00 48.48  ? 154 ILE   D CA    1 
ATOM   8082  C  C     . ILE   C 2  152 ? 32.973  -1.004  -31.247 1.00 50.79  ? 154 ILE   D C     1 
ATOM   8083  O  O     . ILE   C 2  152 ? 33.155  0.097   -30.719 1.00 49.85  ? 154 ILE   D O     1 
ATOM   8084  C  CB    . ILE   C 2  152 ? 30.714  -2.160  -31.223 1.00 49.71  ? 154 ILE   D CB    1 
ATOM   8085  C  CG1   . ILE   C 2  152 ? 29.339  -2.184  -31.891 1.00 41.46  ? 154 ILE   D CG1   1 
ATOM   8086  C  CG2   . ILE   C 2  152 ? 30.582  -1.635  -29.820 1.00 35.44  ? 154 ILE   D CG2   1 
ATOM   8087  C  CD1   . ILE   C 2  152 ? 28.489  -3.288  -31.401 1.00 30.69  ? 154 ILE   D CD1   1 
ATOM   8088  N  N     . SER   C 2  153 ? 33.885  -1.985  -31.173 1.00 42.76  ? 155 SER   D N     1 
ATOM   8089  C  CA    A SER   C 2  153 ? 35.155  -1.757  -30.493 0.00 45.69  ? 155 SER   D CA    1 
ATOM   8090  C  CA    B SER   C 2  153 ? 35.166  -1.763  -30.504 1.00 45.20  ? 155 SER   D CA    1 
ATOM   8091  C  C     . SER   C 2  153 ? 35.935  -0.617  -31.139 1.00 52.19  ? 155 SER   D C     1 
ATOM   8092  O  O     . SER   C 2  153 ? 36.524  0.218   -30.438 1.00 49.71  ? 155 SER   D O     1 
ATOM   8093  C  CB    A SER   C 2  153 ? 35.986  -3.041  -30.490 0.00 49.01  ? 155 SER   D CB    1 
ATOM   8094  C  CB    B SER   C 2  153 ? 36.019  -3.020  -30.552 1.00 48.72  ? 155 SER   D CB    1 
ATOM   8095  O  OG    A SER   C 2  153 ? 35.305  -4.087  -29.820 0.00 60.59  ? 155 SER   D OG    1 
ATOM   8096  O  OG    B SER   C 2  153 ? 35.314  -4.114  -30.015 1.00 62.82  ? 155 SER   D OG    1 
ATOM   8097  N  N     . LYS   C 2  154 ? 35.955  -0.563  -32.469 1.00 47.10  ? 156 LYS   D N     1 
ATOM   8098  C  CA    . LYS   C 2  154 ? 36.736  0.469   -33.133 1.00 51.45  ? 156 LYS   D CA    1 
ATOM   8099  C  C     . LYS   C 2  154 ? 36.131  1.844   -32.899 1.00 49.54  ? 156 LYS   D C     1 
ATOM   8100  O  O     . LYS   C 2  154 ? 36.859  2.817   -32.678 1.00 48.69  ? 156 LYS   D O     1 
ATOM   8101  C  CB    . LYS   C 2  154 ? 36.860  0.159   -34.629 1.00 58.72  ? 156 LYS   D CB    1 
ATOM   8102  C  CG    . LYS   C 2  154 ? 37.846  -0.966  -34.944 1.00 54.77  ? 156 LYS   D CG    1 
ATOM   8103  C  CD    . LYS   C 2  154 ? 38.631  -1.374  -33.696 1.00 56.30  ? 156 LYS   D CD    1 
ATOM   8104  C  CE    . LYS   C 2  154 ? 39.846  -2.240  -34.035 1.00 61.86  ? 156 LYS   D CE    1 
ATOM   8105  N  NZ    . LYS   C 2  154 ? 40.970  -1.476  -34.646 1.00 49.57  ? 156 LYS   D NZ    1 
ATOM   8106  N  N     . ILE   C 2  155 ? 34.802  1.949   -32.934 1.00 52.18  ? 157 ILE   D N     1 
ATOM   8107  C  CA    . ILE   C 2  155 ? 34.163  3.231   -32.644 1.00 56.03  ? 157 ILE   D CA    1 
ATOM   8108  C  C     . ILE   C 2  155 ? 34.402  3.622   -31.186 1.00 49.45  ? 157 ILE   D C     1 
ATOM   8109  O  O     . ILE   C 2  155 ? 34.752  4.768   -30.875 1.00 43.74  ? 157 ILE   D O     1 
ATOM   8110  C  CB    . ILE   C 2  155 ? 32.665  3.153   -33.001 1.00 46.12  ? 157 ILE   D CB    1 
ATOM   8111  C  CG1   . ILE   C 2  155 ? 32.510  3.011   -34.523 1.00 47.37  ? 157 ILE   D CG1   1 
ATOM   8112  C  CG2   . ILE   C 2  155 ? 31.911  4.351   -32.480 1.00 39.37  ? 157 ILE   D CG2   1 
ATOM   8113  C  CD1   . ILE   C 2  155 ? 31.061  2.915   -35.025 1.00 49.91  ? 157 ILE   D CD1   1 
ATOM   8114  N  N     . ARG   C 2  156 ? 34.264  2.661   -30.279 1.00 51.98  ? 158 ARG   D N     1 
ATOM   8115  C  CA    . ARG   C 2  156 ? 34.601  2.882   -28.881 1.00 47.72  ? 158 ARG   D CA    1 
ATOM   8116  C  C     . ARG   C 2  156 ? 36.006  3.459   -28.718 1.00 47.61  ? 158 ARG   D C     1 
ATOM   8117  O  O     . ARG   C 2  156 ? 36.241  4.286   -27.833 1.00 55.46  ? 158 ARG   D O     1 
ATOM   8118  C  CB    . ARG   C 2  156 ? 34.470  1.564   -28.131 1.00 44.64  ? 158 ARG   D CB    1 
ATOM   8119  C  CG    . ARG   C 2  156 ? 34.135  1.703   -26.706 1.00 46.31  ? 158 ARG   D CG    1 
ATOM   8120  C  CD    . ARG   C 2  156 ? 32.710  2.116   -26.523 1.00 47.28  ? 158 ARG   D CD    1 
ATOM   8121  N  NE    . ARG   C 2  156 ? 32.269  1.775   -25.175 1.00 54.55  ? 158 ARG   D NE    1 
ATOM   8122  C  CZ    . ARG   C 2  156 ? 31.104  2.135   -24.655 1.00 41.59  ? 158 ARG   D CZ    1 
ATOM   8123  N  NH1   . ARG   C 2  156 ? 30.263  2.906   -25.322 1.00 30.50  ? 158 ARG   D NH1   1 
ATOM   8124  N  NH2   . ARG   C 2  156 ? 30.774  1.701   -23.441 1.00 36.51  ? 158 ARG   D NH2   1 
ATOM   8125  N  N     . GLU   C 2  157 ? 36.960  3.038   -29.552 1.00 50.34  ? 159 GLU   D N     1 
ATOM   8126  C  CA    . GLU   C 2  157 ? 38.312  3.589   -29.440 1.00 43.79  ? 159 GLU   D CA    1 
ATOM   8127  C  C     . GLU   C 2  157 ? 38.349  5.065   -29.822 1.00 45.79  ? 159 GLU   D C     1 
ATOM   8128  O  O     . GLU   C 2  157 ? 38.968  5.876   -29.126 1.00 52.97  ? 159 GLU   D O     1 
ATOM   8129  C  CB    . GLU   C 2  157 ? 39.291  2.806   -30.305 1.00 49.16  ? 159 GLU   D CB    1 
ATOM   8130  C  CG    . GLU   C 2  157 ? 39.804  1.505   -29.725 1.00 56.75  ? 159 GLU   D CG    1 
ATOM   8131  C  CD    . GLU   C 2  157 ? 40.743  0.798   -30.696 1.00 72.74  ? 159 GLU   D CD    1 
ATOM   8132  O  OE1   . GLU   C 2  157 ? 41.537  1.497   -31.374 1.00 64.54  ? 159 GLU   D OE1   1 
ATOM   8133  O  OE2   . GLU   C 2  157 ? 40.669  -0.450  -30.797 1.00 77.27  ? 159 GLU   D OE2   1 
ATOM   8134  N  N     . GLU   C 2  158 ? 37.700  5.437   -30.930 1.00 43.22  ? 160 GLU   D N     1 
ATOM   8135  C  CA    . GLU   C 2  158 ? 37.704  6.833   -31.353 1.00 43.88  ? 160 GLU   D CA    1 
ATOM   8136  C  C     . GLU   C 2  158 ? 36.681  7.690   -30.618 1.00 50.88  ? 160 GLU   D C     1 
ATOM   8137  O  O     . GLU   C 2  158 ? 36.840  8.915   -30.575 1.00 54.26  ? 160 GLU   D O     1 
ATOM   8138  C  CB    . GLU   C 2  158 ? 37.476  6.947   -32.866 1.00 33.75  ? 160 GLU   D CB    1 
ATOM   8139  C  CG    . GLU   C 2  158 ? 38.760  6.717   -33.675 1.00 57.18  ? 160 GLU   D CG    1 
ATOM   8140  C  CD    . GLU   C 2  158 ? 38.586  5.796   -34.889 1.00 68.42  ? 160 GLU   D CD    1 
ATOM   8141  O  OE1   . GLU   C 2  158 ? 38.004  6.271   -35.888 1.00 58.91  ? 160 GLU   D OE1   1 
ATOM   8142  O  OE2   . GLU   C 2  158 ? 39.043  4.614   -34.850 1.00 54.14  ? 160 GLU   D OE2   1 
ATOM   8143  N  N     . TYR   C 2  159 ? 35.641  7.098   -30.033 1.00 45.05  ? 161 TYR   D N     1 
ATOM   8144  C  CA    . TYR   C 2  159 ? 34.538  7.875   -29.464 1.00 43.54  ? 161 TYR   D CA    1 
ATOM   8145  C  C     . TYR   C 2  159 ? 34.169  7.360   -28.085 1.00 45.13  ? 161 TYR   D C     1 
ATOM   8146  O  O     . TYR   C 2  159 ? 32.996  7.155   -27.785 1.00 47.64  ? 161 TYR   D O     1 
ATOM   8147  C  CB    . TYR   C 2  159 ? 33.325  7.832   -30.383 1.00 46.27  ? 161 TYR   D CB    1 
ATOM   8148  C  CG    . TYR   C 2  159 ? 33.592  8.417   -31.740 1.00 46.95  ? 161 TYR   D CG    1 
ATOM   8149  C  CD1   . TYR   C 2  159 ? 33.475  9.775   -31.957 1.00 45.73  ? 161 TYR   D CD1   1 
ATOM   8150  C  CD2   . TYR   C 2  159 ? 33.962  7.615   -32.804 1.00 47.65  ? 161 TYR   D CD2   1 
ATOM   8151  C  CE1   . TYR   C 2  159 ? 33.720  10.322  -33.192 1.00 49.90  ? 161 TYR   D CE1   1 
ATOM   8152  C  CE2   . TYR   C 2  159 ? 34.218  8.166   -34.051 1.00 48.99  ? 161 TYR   D CE2   1 
ATOM   8153  C  CZ    . TYR   C 2  159 ? 34.089  9.520   -34.233 1.00 44.84  ? 161 TYR   D CZ    1 
ATOM   8154  O  OH    . TYR   C 2  159 ? 34.333  10.090  -35.457 1.00 57.54  ? 161 TYR   D OH    1 
ATOM   8155  N  N     . PRO   C 2  160 ? 35.154  7.179   -27.203 1.00 52.53  ? 162 PRO   D N     1 
ATOM   8156  C  CA    . PRO   C 2  160 ? 34.926  6.362   -26.002 1.00 50.36  ? 162 PRO   D CA    1 
ATOM   8157  C  C     . PRO   C 2  160 ? 33.921  6.953   -25.024 1.00 52.34  ? 162 PRO   D C     1 
ATOM   8158  O  O     . PRO   C 2  160 ? 33.421  6.220   -24.163 1.00 47.62  ? 162 PRO   D O     1 
ATOM   8159  C  CB    . PRO   C 2  160 ? 36.323  6.268   -25.384 1.00 48.80  ? 162 PRO   D CB    1 
ATOM   8160  C  CG    . PRO   C 2  160 ? 36.995  7.489   -25.834 1.00 48.89  ? 162 PRO   D CG    1 
ATOM   8161  C  CD    . PRO   C 2  160 ? 36.475  7.823   -27.187 1.00 42.23  ? 162 PRO   D CD    1 
ATOM   8162  N  N     . ASP   C 2  161 ? 33.607  8.244   -25.127 1.00 54.30  ? 163 ASP   D N     1 
ATOM   8163  C  CA    . ASP   C 2  161 ? 32.654  8.895   -24.239 1.00 53.22  ? 163 ASP   D CA    1 
ATOM   8164  C  C     . ASP   C 2  161 ? 31.361  9.247   -24.965 1.00 51.09  ? 163 ASP   D C     1 
ATOM   8165  O  O     . ASP   C 2  161 ? 30.706  10.239  -24.634 1.00 46.76  ? 163 ASP   D O     1 
ATOM   8166  C  CB    . ASP   C 2  161 ? 33.270  10.144  -23.601 1.00 38.26  ? 163 ASP   D CB    1 
ATOM   8167  C  CG    . ASP   C 2  161 ? 33.768  11.142  -24.638 1.00 62.14  ? 163 ASP   D CG    1 
ATOM   8168  O  OD1   . ASP   C 2  161 ? 33.630  10.866  -25.854 1.00 57.05  ? 163 ASP   D OD1   1 
ATOM   8169  O  OD2   . ASP   C 2  161 ? 34.303  12.204  -24.239 1.00 69.92  ? 163 ASP   D OD2   1 
ATOM   8170  N  N     . ARG   C 2  162 ? 31.001  8.459   -25.974 1.00 44.86  ? 164 ARG   D N     1 
ATOM   8171  C  CA    . ARG   C 2  162 ? 29.705  8.560   -26.628 1.00 43.25  ? 164 ARG   D CA    1 
ATOM   8172  C  C     . ARG   C 2  162 ? 28.922  7.281   -26.356 1.00 35.21  ? 164 ARG   D C     1 
ATOM   8173  O  O     . ARG   C 2  162 ? 29.485  6.258   -25.965 1.00 37.32  ? 164 ARG   D O     1 
ATOM   8174  C  CB    . ARG   C 2  162 ? 29.858  8.815   -28.130 1.00 38.86  ? 164 ARG   D CB    1 
ATOM   8175  C  CG    . ARG   C 2  162 ? 30.617  10.101  -28.471 1.00 42.80  ? 164 ARG   D CG    1 
ATOM   8176  C  CD    . ARG   C 2  162 ? 29.745  11.351  -28.431 1.00 48.13  ? 164 ARG   D CD    1 
ATOM   8177  N  NE    . ARG   C 2  162 ? 29.972  12.197  -27.256 1.00 69.99  ? 164 ARG   D NE    1 
ATOM   8178  C  CZ    . ARG   C 2  162 ? 29.081  12.438  -26.291 1.00 64.39  ? 164 ARG   D CZ    1 
ATOM   8179  N  NH1   . ARG   C 2  162 ? 27.880  11.880  -26.297 1.00 54.24  ? 164 ARG   D NH1   1 
ATOM   8180  N  NH2   . ARG   C 2  162 ? 29.398  13.277  -25.302 1.00 53.61  ? 164 ARG   D NH2   1 
ATOM   8181  N  N     . ILE   C 2  163 ? 27.612  7.352   -26.509 1.00 34.91  ? 165 ILE   D N     1 
ATOM   8182  C  CA    . ILE   C 2  163 ? 26.750  6.236   -26.145 1.00 33.15  ? 165 ILE   D CA    1 
ATOM   8183  C  C     . ILE   C 2  163 ? 26.681  5.270   -27.321 1.00 36.54  ? 165 ILE   D C     1 
ATOM   8184  O  O     . ILE   C 2  163 ? 26.487  5.696   -28.468 1.00 39.28  ? 165 ILE   D O     1 
ATOM   8185  C  CB    . ILE   C 2  163 ? 25.353  6.733   -25.728 1.00 32.42  ? 165 ILE   D CB    1 
ATOM   8186  C  CG1   . ILE   C 2  163 ? 25.441  7.546   -24.434 1.00 35.10  ? 165 ILE   D CG1   1 
ATOM   8187  C  CG2   . ILE   C 2  163 ? 24.412  5.572   -25.508 1.00 32.38  ? 165 ILE   D CG2   1 
ATOM   8188  C  CD1   . ILE   C 2  163 ? 25.721  6.722   -23.208 1.00 18.83  ? 165 ILE   D CD1   1 
ATOM   8189  N  N     . MET   C 2  164 ? 26.872  3.965   -27.038 1.00 34.25  ? 166 MET   D N     1 
ATOM   8190  C  CA    . MET   C 2  164 ? 26.780  2.892   -28.029 1.00 28.46  ? 166 MET   D CA    1 
ATOM   8191  C  C     . MET   C 2  164 ? 25.460  2.148   -27.856 1.00 41.35  ? 166 MET   D C     1 
ATOM   8192  O  O     . MET   C 2  164 ? 25.271  1.406   -26.880 1.00 37.28  ? 166 MET   D O     1 
ATOM   8193  C  CB    . MET   C 2  164 ? 27.949  1.919   -27.903 1.00 40.77  ? 166 MET   D CB    1 
ATOM   8194  C  CG    . MET   C 2  164 ? 28.008  0.822   -28.983 1.00 35.23  ? 166 MET   D CG    1 
ATOM   8195  S  SD    . MET   C 2  164 ? 28.717  1.503   -30.495 1.00 50.50  ? 166 MET   D SD    1 
ATOM   8196  C  CE    . MET   C 2  164 ? 27.413  2.618   -30.950 1.00 49.97  ? 166 MET   D CE    1 
ATOM   8197  N  N     . ASN   C 2  165 ? 24.563  2.342   -28.815 1.00 42.86  ? 167 ASN   D N     1 
ATOM   8198  C  CA    . ASN   C 2  165 ? 23.265  1.684   -28.895 1.00 49.68  ? 167 ASN   D CA    1 
ATOM   8199  C  C     . ASN   C 2  165 ? 23.368  0.516   -29.869 1.00 46.19  ? 167 ASN   D C     1 
ATOM   8200  O  O     . ASN   C 2  165 ? 24.046  0.634   -30.891 1.00 52.74  ? 167 ASN   D O     1 
ATOM   8201  C  CB    . ASN   C 2  165 ? 22.218  2.689   -29.401 1.00 47.54  ? 167 ASN   D CB    1 
ATOM   8202  C  CG    . ASN   C 2  165 ? 20.819  2.319   -29.024 1.00 46.93  ? 167 ASN   D CG    1 
ATOM   8203  O  OD1   . ASN   C 2  165 ? 20.619  1.487   -28.151 1.00 53.48  ? 167 ASN   D OD1   1 
ATOM   8204  N  ND2   . ASN   C 2  165 ? 19.832  2.957   -29.659 1.00 42.56  ? 167 ASN   D ND2   1 
ATOM   8205  N  N     . THR   C 2  166 ? 22.693  -0.602  -29.576 1.00 42.93  ? 168 THR   D N     1 
ATOM   8206  C  CA    . THR   C 2  166 ? 22.491  -1.625  -30.607 1.00 49.01  ? 168 THR   D CA    1 
ATOM   8207  C  C     . THR   C 2  166 ? 21.053  -2.144  -30.622 1.00 55.41  ? 168 THR   D C     1 
ATOM   8208  O  O     . THR   C 2  166 ? 20.349  -2.162  -29.603 1.00 50.28  ? 168 THR   D O     1 
ATOM   8209  C  CB    . THR   C 2  166 ? 23.408  -2.856  -30.471 1.00 42.16  ? 168 THR   D CB    1 
ATOM   8210  O  OG1   . THR   C 2  166 ? 23.014  -3.627  -29.328 1.00 38.99  ? 168 THR   D OG1   1 
ATOM   8211  C  CG2   . THR   C 2  166 ? 24.881  -2.465  -30.381 1.00 35.70  ? 168 THR   D CG2   1 
ATOM   8212  N  N     . PHE   C 2  167 ? 20.633  -2.577  -31.809 1.00 54.51  ? 169 PHE   D N     1 
ATOM   8213  C  CA    . PHE   C 2  167 ? 19.473  -3.438  -32.004 1.00 43.72  ? 169 PHE   D CA    1 
ATOM   8214  C  C     . PHE   C 2  167 ? 19.995  -4.783  -32.497 1.00 42.73  ? 169 PHE   D C     1 
ATOM   8215  O  O     . PHE   C 2  167 ? 20.375  -4.916  -33.660 1.00 49.14  ? 169 PHE   D O     1 
ATOM   8216  C  CB    . PHE   C 2  167 ? 18.518  -2.821  -32.998 1.00 43.44  ? 169 PHE   D CB    1 
ATOM   8217  C  CG    . PHE   C 2  167 ? 17.861  -1.587  -32.505 1.00 43.94  ? 169 PHE   D CG    1 
ATOM   8218  C  CD1   . PHE   C 2  167 ? 18.487  -0.367  -32.622 1.00 45.66  ? 169 PHE   D CD1   1 
ATOM   8219  C  CD2   . PHE   C 2  167 ? 16.598  -1.642  -31.935 1.00 46.09  ? 169 PHE   D CD2   1 
ATOM   8220  C  CE1   . PHE   C 2  167 ? 17.865  0.791   -32.177 1.00 51.41  ? 169 PHE   D CE1   1 
ATOM   8221  C  CE2   . PHE   C 2  167 ? 15.973  -0.495  -31.493 1.00 48.73  ? 169 PHE   D CE2   1 
ATOM   8222  C  CZ    . PHE   C 2  167 ? 16.606  0.729   -31.620 1.00 43.78  ? 169 PHE   D CZ    1 
ATOM   8223  N  N     . SER   C 2  168 ? 20.020  -5.771  -31.611 1.00 40.24  ? 170 SER   D N     1 
ATOM   8224  C  CA    . SER   C 2  168 ? 20.657  -7.059  -31.855 1.00 41.48  ? 170 SER   D CA    1 
ATOM   8225  C  C     . SER   C 2  168 ? 19.582  -8.138  -31.935 1.00 55.37  ? 170 SER   D C     1 
ATOM   8226  O  O     . SER   C 2  168 ? 18.997  -8.508  -30.910 1.00 52.61  ? 170 SER   D O     1 
ATOM   8227  C  CB    . SER   C 2  168 ? 21.656  -7.382  -30.747 1.00 42.50  ? 170 SER   D CB    1 
ATOM   8228  O  OG    . SER   C 2  168 ? 22.578  -6.329  -30.557 1.00 44.37  ? 170 SER   D OG    1 
ATOM   8229  N  N     . VAL   C 2  169 ? 19.346  -8.661  -33.149 1.00 59.48  ? 171 VAL   D N     1 
ATOM   8230  C  CA    . VAL   C 2  169 ? 18.360  -9.714  -33.382 1.00 47.43  ? 171 VAL   D CA    1 
ATOM   8231  C  C     . VAL   C 2  169 ? 19.004  -11.066 -33.122 1.00 46.77  ? 171 VAL   D C     1 
ATOM   8232  O  O     . VAL   C 2  169 ? 20.067  -11.369 -33.670 1.00 53.53  ? 171 VAL   D O     1 
ATOM   8233  C  CB    . VAL   C 2  169 ? 17.800  -9.646  -34.808 1.00 52.18  ? 171 VAL   D CB    1 
ATOM   8234  C  CG1   . VAL   C 2  169 ? 16.714  -10.685 -34.962 1.00 58.82  ? 171 VAL   D CG1   1 
ATOM   8235  C  CG2   . VAL   C 2  169 ? 17.274  -8.245  -35.131 1.00 44.65  ? 171 VAL   D CG2   1 
ATOM   8236  N  N     . MET   C 2  170 ? 18.342  -11.894 -32.289 1.00 53.08  ? 172 MET   D N     1 
ATOM   8237  C  CA    . MET   C 2  170 ? 18.818  -13.119 -31.665 1.00 62.12  ? 172 MET   D CA    1 
ATOM   8238  C  C     . MET   C 2  170 ? 18.349  -14.352 -32.430 1.00 63.53  ? 172 MET   D C     1 
ATOM   8239  O  O     . MET   C 2  170 ? 17.287  -14.330 -33.060 1.00 65.75  ? 172 MET   D O     1 
ATOM   8240  C  CB    . MET   C 2  170 ? 18.319  -13.217 -30.216 1.00 72.51  ? 172 MET   D CB    1 
ATOM   8241  C  CG    . MET   C 2  170 ? 18.727  -12.066 -29.283 1.00 68.57  ? 172 MET   D CG    1 
ATOM   8242  S  SD    . MET   C 2  170 ? 20.378  -12.252 -28.577 0.43 58.52  ? 172 MET   D SD    1 
ATOM   8243  C  CE    . MET   C 2  170 ? 20.427  -14.035 -28.336 0.87 51.67  ? 172 MET   D CE    1 
ATOM   8244  N  N     . PRO   C 2  171 ? 19.133  -15.435 -32.361 1.00 64.99  ? 173 PRO   D N     1 
ATOM   8245  C  CA    . PRO   C 2  171 ? 18.799  -16.670 -33.091 1.00 72.48  ? 173 PRO   D CA    1 
ATOM   8246  C  C     . PRO   C 2  171 ? 17.771  -17.561 -32.396 1.00 70.31  ? 173 PRO   D C     1 
ATOM   8247  O  O     . PRO   C 2  171 ? 17.872  -17.839 -31.196 1.00 67.23  ? 173 PRO   D O     1 
ATOM   8248  C  CB    . PRO   C 2  171 ? 20.150  -17.404 -33.171 1.00 58.47  ? 173 PRO   D CB    1 
ATOM   8249  C  CG    . PRO   C 2  171 ? 21.178  -16.432 -32.765 1.00 46.82  ? 173 PRO   D CG    1 
ATOM   8250  C  CD    . PRO   C 2  171 ? 20.519  -15.450 -31.868 1.00 64.95  ? 173 PRO   D CD    1 
ATOM   8251  N  N     . SER   C 2  172 ? 16.800  -18.054 -33.187 1.00 68.89  ? 174 SER   D N     1 
ATOM   8252  C  CA    . SER   C 2  172 ? 15.983  -19.221 -32.816 1.00 76.37  ? 174 SER   D CA    1 
ATOM   8253  C  C     . SER   C 2  172 ? 15.914  -20.221 -33.968 1.00 71.26  ? 174 SER   D C     1 
ATOM   8254  O  O     . SER   C 2  172 ? 15.485  -19.861 -35.083 1.00 58.88  ? 174 SER   D O     1 
ATOM   8255  C  CB    . SER   C 2  172 ? 14.557  -18.837 -32.400 1.00 71.55  ? 174 SER   D CB    1 
ATOM   8256  O  OG    . SER   C 2  172 ? 13.889  -19.973 -31.862 1.00 62.63  ? 174 SER   D OG    1 
ATOM   8257  N  N     . PRO   C 2  173 ? 16.273  -21.500 -33.733 1.00 63.45  ? 175 PRO   D N     1 
ATOM   8258  C  CA    . PRO   C 2  173 ? 16.193  -22.506 -34.804 1.00 75.51  ? 175 PRO   D CA    1 
ATOM   8259  C  C     . PRO   C 2  173 ? 14.812  -22.561 -35.438 1.00 67.24  ? 175 PRO   D C     1 
ATOM   8260  O  O     . PRO   C 2  173 ? 14.632  -23.122 -36.524 1.00 63.30  ? 175 PRO   D O     1 
ATOM   8261  C  CB    . PRO   C 2  173 ? 16.533  -23.819 -34.085 1.00 68.42  ? 175 PRO   D CB    1 
ATOM   8262  C  CG    . PRO   C 2  173 ? 17.287  -23.405 -32.867 1.00 62.59  ? 175 PRO   D CG    1 
ATOM   8263  C  CD    . PRO   C 2  173 ? 16.688  -22.091 -32.451 1.00 62.86  ? 175 PRO   D CD    1 
ATOM   8264  N  N     . LYS   C 2  174 ? 13.829  -21.975 -34.759 1.00 60.32  ? 176 LYS   D N     1 
ATOM   8265  C  CA    . LYS   C 2  174 ? 12.502  -21.823 -35.332 1.00 69.81  ? 176 LYS   D CA    1 
ATOM   8266  C  C     . LYS   C 2  174 ? 12.456  -20.834 -36.493 1.00 68.17  ? 176 LYS   D C     1 
ATOM   8267  O  O     . LYS   C 2  174 ? 11.423  -20.754 -37.163 1.00 73.21  ? 176 LYS   D O     1 
ATOM   8268  C  CB    . LYS   C 2  174 ? 11.515  -21.377 -34.249 1.00 72.74  ? 176 LYS   D CB    1 
ATOM   8269  C  CG    . LYS   C 2  174 ? 11.497  -22.251 -33.008 1.00 68.27  ? 176 LYS   D CG    1 
ATOM   8270  C  CD    . LYS   C 2  174 ? 10.469  -21.737 -32.002 1.00 70.54  ? 176 LYS   D CD    1 
ATOM   8271  C  CE    . LYS   C 2  174 ? 10.476  -22.576 -30.732 1.00 60.67  ? 176 LYS   D CE    1 
ATOM   8272  N  NZ    . LYS   C 2  174 ? 9.544   -22.042 -29.710 1.00 69.29  ? 176 LYS   D NZ    1 
ATOM   8273  N  N     . VAL   C 2  175 ? 13.522  -20.076 -36.748 1.00 70.32  ? 177 VAL   D N     1 
ATOM   8274  C  CA    . VAL   C 2  175 ? 13.459  -19.023 -37.761 1.00 72.95  ? 177 VAL   D CA    1 
ATOM   8275  C  C     . VAL   C 2  175 ? 14.568  -19.204 -38.789 1.00 72.56  ? 177 VAL   D C     1 
ATOM   8276  O  O     . VAL   C 2  175 ? 14.439  -18.768 -39.938 1.00 63.27  ? 177 VAL   D O     1 
ATOM   8277  C  CB    . VAL   C 2  175 ? 13.544  -17.624 -37.119 1.00 71.24  ? 177 VAL   D CB    1 
ATOM   8278  C  CG1   . VAL   C 2  175 ? 15.009  -17.192 -36.975 1.00 70.50  ? 177 VAL   D CG1   1 
ATOM   8279  C  CG2   . VAL   C 2  175 ? 12.737  -16.602 -37.920 1.00 56.63  ? 177 VAL   D CG2   1 
ATOM   8280  N  N     . SER   C 2  176 ? 15.668  -19.835 -38.380 1.00 71.24  ? 178 SER   D N     1 
ATOM   8281  C  CA    . SER   C 2  176 ? 16.815  -20.033 -39.251 1.00 64.00  ? 178 SER   D CA    1 
ATOM   8282  C  C     . SER   C 2  176 ? 17.550  -21.292 -38.819 1.00 75.73  ? 178 SER   D C     1 
ATOM   8283  O  O     . SER   C 2  176 ? 17.553  -21.661 -37.638 1.00 67.37  ? 178 SER   D O     1 
ATOM   8284  C  CB    . SER   C 2  176 ? 17.763  -18.825 -39.236 1.00 73.58  ? 178 SER   D CB    1 
ATOM   8285  O  OG    . SER   C 2  176 ? 18.979  -19.101 -39.922 1.00 75.63  ? 178 SER   D OG    1 
ATOM   8286  N  N     . ASP   C 2  177 ? 18.198  -21.927 -39.793 1.00 81.92  ? 179 ASP   D N     1 
ATOM   8287  C  CA    . ASP   C 2  177 ? 18.735  -23.272 -39.649 1.00 84.29  ? 179 ASP   D CA    1 
ATOM   8288  C  C     . ASP   C 2  177 ? 20.251  -23.311 -39.493 1.00 77.45  ? 179 ASP   D C     1 
ATOM   8289  O  O     . ASP   C 2  177 ? 20.808  -24.389 -39.245 1.00 67.60  ? 179 ASP   D O     1 
ATOM   8290  C  CB    . ASP   C 2  177 ? 18.315  -24.109 -40.867 1.00 86.30  ? 179 ASP   D CB    1 
ATOM   8291  C  CG    . ASP   C 2  177 ? 18.211  -25.580 -40.555 1.00 91.31  ? 179 ASP   D CG    1 
ATOM   8292  O  OD1   . ASP   C 2  177 ? 18.302  -25.914 -39.354 1.00 92.47  ? 179 ASP   D OD1   1 
ATOM   8293  O  OD2   . ASP   C 2  177 ? 18.042  -26.392 -41.500 1.00 83.55  ? 179 ASP   D OD2   1 
ATOM   8294  N  N     . THR   C 2  178 ? 20.928  -22.165 -39.589 1.00 71.96  ? 180 THR   D N     1 
ATOM   8295  C  CA    . THR   C 2  178 ? 22.342  -22.143 -39.948 1.00 65.89  ? 180 THR   D CA    1 
ATOM   8296  C  C     . THR   C 2  178 ? 23.266  -22.626 -38.830 1.00 66.99  ? 180 THR   D C     1 
ATOM   8297  O  O     . THR   C 2  178 ? 24.293  -22.002 -38.547 1.00 74.22  ? 180 THR   D O     1 
ATOM   8298  C  CB    . THR   C 2  178 ? 22.731  -20.734 -40.420 1.00 71.56  ? 180 THR   D CB    1 
ATOM   8299  O  OG1   . THR   C 2  178 ? 21.825  -20.304 -41.455 1.00 63.27  ? 180 THR   D OG1   1 
ATOM   8300  C  CG2   . THR   C 2  178 ? 24.157  -20.718 -40.971 1.00 60.52  ? 180 THR   D CG2   1 
ATOM   8301  N  N     . VAL   C 2  179 ? 22.897  -23.732 -38.184 1.00 68.11  ? 181 VAL   D N     1 
ATOM   8302  C  CA    . VAL   C 2  179 ? 23.813  -24.654 -37.504 1.00 74.77  ? 181 VAL   D CA    1 
ATOM   8303  C  C     . VAL   C 2  179 ? 24.769  -24.005 -36.496 1.00 68.43  ? 181 VAL   D C     1 
ATOM   8304  O  O     . VAL   C 2  179 ? 24.817  -24.422 -35.333 1.00 76.27  ? 181 VAL   D O     1 
ATOM   8305  C  CB    . VAL   C 2  179 ? 24.608  -25.473 -38.549 1.00 77.77  ? 181 VAL   D CB    1 
ATOM   8306  C  CG1   . VAL   C 2  179 ? 25.229  -26.727 -37.912 1.00 56.93  ? 181 VAL   D CG1   1 
ATOM   8307  C  CG2   . VAL   C 2  179 ? 23.715  -25.855 -39.741 1.00 68.46  ? 181 VAL   D CG2   1 
ATOM   8308  N  N     . VAL   C 2  180 ? 25.575  -23.026 -36.915 1.00 74.56  ? 182 VAL   D N     1 
ATOM   8309  C  CA    . VAL   C 2  180 ? 26.591  -22.486 -36.004 1.00 75.91  ? 182 VAL   D CA    1 
ATOM   8310  C  C     . VAL   C 2  180 ? 26.176  -21.137 -35.416 1.00 67.47  ? 182 VAL   D C     1 
ATOM   8311  O  O     . VAL   C 2  180 ? 27.021  -20.272 -35.172 1.00 65.15  ? 182 VAL   D O     1 
ATOM   8312  C  CB    . VAL   C 2  180 ? 27.967  -22.360 -36.695 1.00 70.16  ? 182 VAL   D CB    1 
ATOM   8313  C  CG1   . VAL   C 2  180 ? 28.479  -23.713 -37.132 1.00 71.04  ? 182 VAL   D CG1   1 
ATOM   8314  C  CG2   . VAL   C 2  180 ? 27.918  -21.372 -37.866 1.00 54.02  ? 182 VAL   D CG2   1 
ATOM   8315  N  N     . GLU   C 2  181 ? 24.891  -20.946 -35.159 1.00 65.21  ? 183 GLU   D N     1 
ATOM   8316  C  CA    . GLU   C 2  181 ? 24.483  -19.654 -34.623 1.00 70.51  ? 183 GLU   D CA    1 
ATOM   8317  C  C     . GLU   C 2  181 ? 24.734  -19.574 -33.112 1.00 65.42  ? 183 GLU   D C     1 
ATOM   8318  O  O     . GLU   C 2  181 ? 25.159  -18.525 -32.611 1.00 53.71  ? 183 GLU   D O     1 
ATOM   8319  C  CB    . GLU   C 2  181 ? 23.027  -19.388 -35.008 1.00 57.23  ? 183 GLU   D CB    1 
ATOM   8320  C  CG    . GLU   C 2  181 ? 22.852  -19.451 -36.524 1.00 55.98  ? 183 GLU   D CG    1 
ATOM   8321  C  CD    . GLU   C 2  181 ? 21.573  -18.800 -37.031 1.00 68.06  ? 183 GLU   D CD    1 
ATOM   8322  O  OE1   . GLU   C 2  181 ? 20.887  -18.120 -36.239 1.00 72.21  ? 183 GLU   D OE1   1 
ATOM   8323  O  OE2   . GLU   C 2  181 ? 21.253  -18.965 -38.232 1.00 64.99  ? 183 GLU   D OE2   1 
ATOM   8324  N  N     . PRO   C 2  182 ? 24.542  -20.656 -32.354 1.00 65.84  ? 184 PRO   D N     1 
ATOM   8325  C  CA    . PRO   C 2  182 ? 25.006  -20.654 -30.956 1.00 59.45  ? 184 PRO   D CA    1 
ATOM   8326  C  C     . PRO   C 2  182 ? 26.450  -20.204 -30.804 1.00 59.00  ? 184 PRO   D C     1 
ATOM   8327  O  O     . PRO   C 2  182 ? 26.877  -19.814 -29.715 1.00 65.21  ? 184 PRO   D O     1 
ATOM   8328  C  CB    . PRO   C 2  182 ? 24.839  -22.116 -30.532 1.00 55.71  ? 184 PRO   D CB    1 
ATOM   8329  C  CG    . PRO   C 2  182 ? 23.690  -22.595 -31.352 1.00 65.69  ? 184 PRO   D CG    1 
ATOM   8330  C  CD    . PRO   C 2  182 ? 23.776  -21.872 -32.680 1.00 62.77  ? 184 PRO   D CD    1 
ATOM   8331  N  N     . TYR   C 2  183 ? 27.227  -20.284 -31.876 1.00 61.11  ? 185 TYR   D N     1 
ATOM   8332  C  CA    . TYR   C 2  183 ? 28.592  -19.782 -31.834 1.00 67.64  ? 185 TYR   D CA    1 
ATOM   8333  C  C     . TYR   C 2  183 ? 28.637  -18.288 -32.136 1.00 62.24  ? 185 TYR   D C     1 
ATOM   8334  O  O     . TYR   C 2  183 ? 29.217  -17.514 -31.370 1.00 62.66  ? 185 TYR   D O     1 
ATOM   8335  C  CB    . TYR   C 2  183 ? 29.471  -20.549 -32.829 1.00 72.35  ? 185 TYR   D CB    1 
ATOM   8336  C  CG    . TYR   C 2  183 ? 29.801  -21.976 -32.443 1.00 73.65  ? 185 TYR   D CG    1 
ATOM   8337  C  CD1   . TYR   C 2  183 ? 30.110  -22.314 -31.133 1.00 67.05  ? 185 TYR   D CD1   1 
ATOM   8338  C  CD2   . TYR   C 2  183 ? 29.822  -22.985 -33.403 1.00 77.29  ? 185 TYR   D CD2   1 
ATOM   8339  C  CE1   . TYR   C 2  183 ? 30.421  -23.629 -30.784 1.00 76.53  ? 185 TYR   D CE1   1 
ATOM   8340  C  CE2   . TYR   C 2  183 ? 30.129  -24.294 -33.065 1.00 75.76  ? 185 TYR   D CE2   1 
ATOM   8341  C  CZ    . TYR   C 2  183 ? 30.428  -24.612 -31.756 1.00 74.19  ? 185 TYR   D CZ    1 
ATOM   8342  O  OH    . TYR   C 2  183 ? 30.732  -25.913 -31.424 1.00 61.86  ? 185 TYR   D OH    1 
ATOM   8343  N  N     . ASN   C 2  184 ? 28.028  -17.875 -33.249 1.00 54.72  ? 186 ASN   D N     1 
ATOM   8344  C  CA    . ASN   C 2  184 ? 28.049  -16.468 -33.633 1.00 59.42  ? 186 ASN   D CA    1 
ATOM   8345  C  C     . ASN   C 2  184 ? 27.401  -15.591 -32.578 1.00 58.33  ? 186 ASN   D C     1 
ATOM   8346  O  O     . ASN   C 2  184 ? 27.820  -14.445 -32.373 1.00 53.84  ? 186 ASN   D O     1 
ATOM   8347  C  CB    . ASN   C 2  184 ? 27.335  -16.277 -34.965 1.00 58.06  ? 186 ASN   D CB    1 
ATOM   8348  C  CG    . ASN   C 2  184 ? 27.965  -17.063 -36.055 1.00 57.55  ? 186 ASN   D CG    1 
ATOM   8349  O  OD1   . ASN   C 2  184 ? 29.172  -17.276 -36.050 1.00 53.62  ? 186 ASN   D OD1   1 
ATOM   8350  N  ND2   . ASN   C 2  184 ? 27.154  -17.530 -36.991 1.00 63.16  ? 186 ASN   D ND2   1 
ATOM   8351  N  N     . ALA   C 2  185 ? 26.354  -16.099 -31.924 1.00 62.65  ? 187 ALA   D N     1 
ATOM   8352  C  CA    . ALA   C 2  185 ? 25.625  -15.305 -30.947 1.00 49.76  ? 187 ALA   D CA    1 
ATOM   8353  C  C     . ALA   C 2  185 ? 26.409  -15.178 -29.642 1.00 55.12  ? 187 ALA   D C     1 
ATOM   8354  O  O     . ALA   C 2  185 ? 26.596  -14.072 -29.130 1.00 57.53  ? 187 ALA   D O     1 
ATOM   8355  C  CB    . ALA   C 2  185 ? 24.246  -15.913 -30.713 1.00 52.76  ? 187 ALA   D CB    1 
ATOM   8356  N  N     . THR   C 2  186 ? 26.905  -16.288 -29.100 1.00 50.60  ? 188 THR   D N     1 
ATOM   8357  C  CA    . THR   C 2  186 ? 27.737  -16.199 -27.906 1.00 47.42  ? 188 THR   D CA    1 
ATOM   8358  C  C     . THR   C 2  186 ? 28.933  -15.268 -28.126 1.00 57.46  ? 188 THR   D C     1 
ATOM   8359  O  O     . THR   C 2  186 ? 29.119  -14.293 -27.390 1.00 64.18  ? 188 THR   D O     1 
ATOM   8360  C  CB    . THR   C 2  186 ? 28.193  -17.590 -27.487 1.00 46.18  ? 188 THR   D CB    1 
ATOM   8361  O  OG1   . THR   C 2  186 ? 27.108  -18.261 -26.836 1.00 45.64  ? 188 THR   D OG1   1 
ATOM   8362  C  CG2   . THR   C 2  186 ? 29.386  -17.489 -26.545 1.00 52.16  ? 188 THR   D CG2   1 
ATOM   8363  N  N     . LEU   C 2  187 ? 29.758  -15.551 -29.137 1.00 57.27  ? 189 LEU   D N     1 
ATOM   8364  C  CA    . LEU   C 2  187 ? 30.877  -14.664 -29.447 1.00 57.13  ? 189 LEU   D CA    1 
ATOM   8365  C  C     . LEU   C 2  187 ? 30.428  -13.212 -29.594 1.00 59.51  ? 189 LEU   D C     1 
ATOM   8366  O  O     . LEU   C 2  187 ? 31.172  -12.290 -29.238 1.00 53.02  ? 189 LEU   D O     1 
ATOM   8367  C  CB    . LEU   C 2  187 ? 31.581  -15.126 -30.728 1.00 57.79  ? 189 LEU   D CB    1 
ATOM   8368  C  CG    . LEU   C 2  187 ? 32.254  -16.504 -30.758 1.00 57.64  ? 189 LEU   D CG    1 
ATOM   8369  C  CD1   . LEU   C 2  187 ? 32.685  -16.842 -32.178 1.00 57.25  ? 189 LEU   D CD1   1 
ATOM   8370  C  CD2   . LEU   C 2  187 ? 33.443  -16.576 -29.803 1.00 49.62  ? 189 LEU   D CD2   1 
ATOM   8371  N  N     . SER   C 2  188 ? 29.221  -12.983 -30.120 1.00 51.09  ? 190 SER   D N     1 
ATOM   8372  C  CA    . SER   C 2  188 ? 28.709  -11.618 -30.214 1.00 59.20  ? 190 SER   D CA    1 
ATOM   8373  C  C     . SER   C 2  188 ? 28.370  -11.055 -28.833 1.00 61.98  ? 190 SER   D C     1 
ATOM   8374  O  O     . SER   C 2  188 ? 28.716  -9.909  -28.517 1.00 50.04  ? 190 SER   D O     1 
ATOM   8375  C  CB    . SER   C 2  188 ? 27.476  -11.574 -31.121 1.00 59.69  ? 190 SER   D CB    1 
ATOM   8376  O  OG    . SER   C 2  188 ? 27.831  -11.446 -32.481 1.00 61.56  ? 190 SER   D OG    1 
ATOM   8377  N  N     . VAL   C 2  189 ? 27.678  -11.843 -28.003 1.00 54.72  ? 191 VAL   D N     1 
ATOM   8378  C  CA    . VAL   C 2  189 ? 27.234  -11.351 -26.703 1.00 54.21  ? 191 VAL   D CA    1 
ATOM   8379  C  C     . VAL   C 2  189 ? 28.429  -10.992 -25.832 1.00 55.21  ? 191 VAL   D C     1 
ATOM   8380  O  O     . VAL   C 2  189 ? 28.393  -10.002 -25.090 1.00 52.18  ? 191 VAL   D O     1 
ATOM   8381  C  CB    . VAL   C 2  189 ? 26.320  -12.381 -26.016 1.00 54.52  ? 191 VAL   D CB    1 
ATOM   8382  C  CG1   . VAL   C 2  189 ? 26.396  -12.226 -24.490 1.00 51.10  ? 191 VAL   D CG1   1 
ATOM   8383  C  CG2   . VAL   C 2  189 ? 24.902  -12.218 -26.502 1.00 39.50  ? 191 VAL   D CG2   1 
ATOM   8384  N  N     . HIS   C 2  190 ? 29.499  -11.796 -25.900 1.00 51.30  ? 192 HIS   D N     1 
ATOM   8385  C  CA    . HIS   C 2  190 ? 30.735  -11.478 -25.183 1.00 49.29  ? 192 HIS   D CA    1 
ATOM   8386  C  C     . HIS   C 2  190 ? 31.255  -10.101 -25.581 1.00 48.44  ? 192 HIS   D C     1 
ATOM   8387  O  O     . HIS   C 2  190 ? 31.665  -9.309  -24.727 1.00 49.29  ? 192 HIS   D O     1 
ATOM   8388  C  CB    . HIS   C 2  190 ? 31.767  -12.568 -25.463 1.00 45.38  ? 192 HIS   D CB    1 
ATOM   8389  C  CG    . HIS   C 2  190 ? 33.125  -12.308 -24.889 1.00 58.84  ? 192 HIS   D CG    1 
ATOM   8390  N  ND1   . HIS   C 2  190 ? 33.628  -13.020 -23.821 1.00 56.03  ? 192 HIS   D ND1   1 
ATOM   8391  C  CD2   . HIS   C 2  190 ? 34.109  -11.457 -25.268 1.00 66.59  ? 192 HIS   D CD2   1 
ATOM   8392  C  CE1   . HIS   C 2  190 ? 34.854  -12.608 -23.557 1.00 53.00  ? 192 HIS   D CE1   1 
ATOM   8393  N  NE2   . HIS   C 2  190 ? 35.170  -11.658 -24.418 1.00 60.88  ? 192 HIS   D NE2   1 
ATOM   8394  N  N     . GLN   C 2  191 ? 31.219  -9.790  -26.875 1.00 48.47  ? 193 GLN   D N     1 
ATOM   8395  C  CA    . GLN   C 2  191 ? 31.554  -8.447  -27.335 1.00 52.69  ? 193 GLN   D CA    1 
ATOM   8396  C  C     . GLN   C 2  191 ? 30.606  -7.408  -26.753 1.00 45.69  ? 193 GLN   D C     1 
ATOM   8397  O  O     . GLN   C 2  191 ? 31.030  -6.310  -26.383 1.00 37.30  ? 193 GLN   D O     1 
ATOM   8398  C  CB    . GLN   C 2  191 ? 31.510  -8.395  -28.864 1.00 58.21  ? 193 GLN   D CB    1 
ATOM   8399  C  CG    . GLN   C 2  191 ? 32.515  -9.296  -29.533 1.00 58.13  ? 193 GLN   D CG    1 
ATOM   8400  C  CD    . GLN   C 2  191 ? 33.922  -8.972  -29.093 1.00 59.02  ? 193 GLN   D CD    1 
ATOM   8401  O  OE1   . GLN   C 2  191 ? 34.310  -7.800  -29.041 1.00 61.42  ? 193 GLN   D OE1   1 
ATOM   8402  N  NE2   . GLN   C 2  191 ? 34.693  -10.005 -28.756 1.00 58.14  ? 193 GLN   D NE2   1 
ATOM   8403  N  N     . LEU   C 2  192 ? 29.313  -7.743  -26.675 1.00 50.92  ? 194 LEU   D N     1 
ATOM   8404  C  CA    . LEU   C 2  192 ? 28.276  -6.789  -26.304 1.00 41.67  ? 194 LEU   D CA    1 
ATOM   8405  C  C     . LEU   C 2  192 ? 28.256  -6.519  -24.800 1.00 46.67  ? 194 LEU   D C     1 
ATOM   8406  O  O     . LEU   C 2  192 ? 28.058  -5.374  -24.379 1.00 43.73  ? 194 LEU   D O     1 
ATOM   8407  C  CB    . LEU   C 2  192 ? 26.918  -7.297  -26.782 1.00 35.82  ? 194 LEU   D CB    1 
ATOM   8408  C  CG    . LEU   C 2  192 ? 26.632  -7.233  -28.282 1.00 37.73  ? 194 LEU   D CG    1 
ATOM   8409  C  CD1   . LEU   C 2  192 ? 25.180  -7.591  -28.555 1.00 48.63  ? 194 LEU   D CD1   1 
ATOM   8410  C  CD2   . LEU   C 2  192 ? 26.930  -5.875  -28.857 1.00 28.57  ? 194 LEU   D CD2   1 
ATOM   8411  N  N     . VAL   C 2  193 ? 28.462  -7.551  -23.976 1.00 41.04  ? 195 VAL   D N     1 
ATOM   8412  C  CA    . VAL   C 2  193 ? 28.518  -7.356  -22.529 1.00 39.14  ? 195 VAL   D CA    1 
ATOM   8413  C  C     . VAL   C 2  193 ? 29.491  -6.247  -22.176 1.00 48.43  ? 195 VAL   D C     1 
ATOM   8414  O  O     . VAL   C 2  193 ? 29.308  -5.546  -21.174 1.00 52.61  ? 195 VAL   D O     1 
ATOM   8415  C  CB    . VAL   C 2  193 ? 28.917  -8.668  -21.815 1.00 47.27  ? 195 VAL   D CB    1 
ATOM   8416  C  CG1   . VAL   C 2  193 ? 28.768  -8.529  -20.309 1.00 50.67  ? 195 VAL   D CG1   1 
ATOM   8417  C  CG2   . VAL   C 2  193 ? 28.115  -9.828  -22.320 1.00 52.75  ? 195 VAL   D CG2   1 
ATOM   8418  N  N     . GLU   C 2  194 ? 30.539  -6.067  -22.986 1.00 50.78  ? 196 GLU   D N     1 
ATOM   8419  C  CA    . GLU   C 2  194 ? 31.676  -5.234  -22.625 1.00 48.39  ? 196 GLU   D CA    1 
ATOM   8420  C  C     . GLU   C 2  194 ? 31.729  -3.899  -23.346 1.00 38.74  ? 196 GLU   D C     1 
ATOM   8421  O  O     . GLU   C 2  194 ? 32.350  -2.972  -22.826 1.00 45.09  ? 196 GLU   D O     1 
ATOM   8422  C  CB    . GLU   C 2  194 ? 32.994  -5.985  -22.885 1.00 35.63  ? 196 GLU   D CB    1 
ATOM   8423  C  CG    . GLU   C 2  194 ? 32.990  -7.400  -22.337 1.00 43.46  ? 196 GLU   D CG    1 
ATOM   8424  C  CD    . GLU   C 2  194 ? 33.642  -7.535  -20.962 1.00 50.52  ? 196 GLU   D CD    1 
ATOM   8425  O  OE1   . GLU   C 2  194 ? 34.533  -6.724  -20.632 1.00 73.41  ? 196 GLU   D OE1   1 
ATOM   8426  O  OE2   . GLU   C 2  194 ? 33.274  -8.466  -20.211 1.00 42.21  ? 196 GLU   D OE2   1 
ATOM   8427  N  N     . ASN   C 2  195 ? 31.097  -3.763  -24.509 1.00 37.94  ? 197 ASN   D N     1 
ATOM   8428  C  CA    . ASN   C 2  195 ? 31.334  -2.588  -25.341 1.00 43.63  ? 197 ASN   D CA    1 
ATOM   8429  C  C     . ASN   C 2  195 ? 30.071  -1.843  -25.760 1.00 41.86  ? 197 ASN   D C     1 
ATOM   8430  O  O     . ASN   C 2  195 ? 30.172  -0.901  -26.556 1.00 39.16  ? 197 ASN   D O     1 
ATOM   8431  C  CB    . ASN   C 2  195 ? 32.148  -2.973  -26.584 1.00 37.85  ? 197 ASN   D CB    1 
ATOM   8432  C  CG    . ASN   C 2  195 ? 33.591  -3.366  -26.234 1.00 51.71  ? 197 ASN   D CG    1 
ATOM   8433  O  OD1   . ASN   C 2  195 ? 34.182  -2.849  -25.282 1.00 43.28  ? 197 ASN   D OD1   1 
ATOM   8434  N  ND2   . ASN   C 2  195 ? 34.155  -4.288  -27.003 1.00 54.11  ? 197 ASN   D ND2   1 
ATOM   8435  N  N     . THR   C 2  196 ? 28.898  -2.210  -25.243 1.00 42.30  ? 198 THR   D N     1 
ATOM   8436  C  CA    . THR   C 2  196 ? 27.680  -1.432  -25.439 1.00 43.81  ? 198 THR   D CA    1 
ATOM   8437  C  C     . THR   C 2  196 ? 27.200  -0.811  -24.130 1.00 40.09  ? 198 THR   D C     1 
ATOM   8438  O  O     . THR   C 2  196 ? 27.430  -1.341  -23.040 1.00 39.91  ? 198 THR   D O     1 
ATOM   8439  C  CB    . THR   C 2  196 ? 26.547  -2.290  -26.019 1.00 44.73  ? 198 THR   D CB    1 
ATOM   8440  O  OG1   . THR   C 2  196 ? 26.711  -3.646  -25.587 1.00 50.40  ? 198 THR   D OG1   1 
ATOM   8441  C  CG2   . THR   C 2  196 ? 26.538  -2.220  -27.529 1.00 35.77  ? 198 THR   D CG2   1 
ATOM   8442  N  N     . ASP   C 2  197 ? 26.502  0.309   -24.258 1.00 37.76  ? 199 ASP   D N     1 
ATOM   8443  C  CA    . ASP   C 2  197 ? 25.806  0.916   -23.133 1.00 35.41  ? 199 ASP   D CA    1 
ATOM   8444  C  C     . ASP   C 2  197 ? 24.377  0.421   -23.008 1.00 45.90  ? 199 ASP   D C     1 
ATOM   8445  O  O     . ASP   C 2  197 ? 23.918  0.122   -21.897 1.00 39.91  ? 199 ASP   D O     1 
ATOM   8446  C  CB    . ASP   C 2  197 ? 25.802  2.429   -23.294 1.00 40.25  ? 199 ASP   D CB    1 
ATOM   8447  C  CG    . ASP   C 2  197 ? 27.178  2.970   -23.486 1.00 33.42  ? 199 ASP   D CG    1 
ATOM   8448  O  OD1   . ASP   C 2  197 ? 28.090  2.434   -22.836 1.00 25.73  ? 199 ASP   D OD1   1 
ATOM   8449  O  OD2   . ASP   C 2  197 ? 27.343  3.900   -24.295 1.00 35.18  ? 199 ASP   D OD2   1 
ATOM   8450  N  N     . GLU   C 2  198 ? 23.668  0.322   -24.133 1.00 51.16  ? 200 GLU   D N     1 
ATOM   8451  C  CA    . GLU   C 2  198 ? 22.283  -0.127  -24.119 1.00 54.38  ? 200 GLU   D CA    1 
ATOM   8452  C  C     . GLU   C 2  198 ? 21.975  -0.912  -25.389 1.00 50.18  ? 200 GLU   D C     1 
ATOM   8453  O  O     . GLU   C 2  198 ? 22.213  -0.425  -26.500 1.00 50.50  ? 200 GLU   D O     1 
ATOM   8454  C  CB    . GLU   C 2  198 ? 21.338  1.069   -23.957 1.00 45.35  ? 200 GLU   D CB    1 
ATOM   8455  C  CG    . GLU   C 2  198 ? 21.721  2.283   -24.780 1.00 44.38  ? 200 GLU   D CG    1 
ATOM   8456  C  CD    . GLU   C 2  198 ? 21.190  3.553   -24.167 1.00 48.20  ? 200 GLU   D CD    1 
ATOM   8457  O  OE1   . GLU   C 2  198 ? 20.945  3.565   -22.944 1.00 52.99  ? 200 GLU   D OE1   1 
ATOM   8458  O  OE2   . GLU   C 2  198 ? 21.001  4.539   -24.894 1.00 45.61  ? 200 GLU   D OE2   1 
ATOM   8459  N  N     . THR   C 2  199 ? 21.433  -2.120  -25.206 1.00 45.57  ? 201 THR   D N     1 
ATOM   8460  C  CA    . THR   C 2  199 ? 21.167  -3.077  -26.281 1.00 52.40  ? 201 THR   D CA    1 
ATOM   8461  C  C     . THR   C 2  199 ? 19.737  -3.595  -26.162 1.00 46.15  ? 201 THR   D C     1 
ATOM   8462  O  O     . THR   C 2  199 ? 19.389  -4.239  -25.164 1.00 35.40  ? 201 THR   D O     1 
ATOM   8463  C  CB    . THR   C 2  199 ? 22.154  -4.255  -26.213 1.00 54.69  ? 201 THR   D CB    1 
ATOM   8464  O  OG1   . THR   C 2  199 ? 23.473  -3.819  -26.576 1.00 56.01  ? 201 THR   D OG1   1 
ATOM   8465  C  CG2   . THR   C 2  199 ? 21.702  -5.387  -27.109 1.00 44.61  ? 201 THR   D CG2   1 
ATOM   8466  N  N     . TYR   C 2  200 ? 18.908  -3.313  -27.170 1.00 37.17  ? 202 TYR   D N     1 
ATOM   8467  C  CA    . TYR   C 2  200 ? 17.587  -3.932  -27.265 1.00 38.55  ? 202 TYR   D CA    1 
ATOM   8468  C  C     . TYR   C 2  200 ? 17.730  -5.360  -27.799 1.00 55.47  ? 202 TYR   D C     1 
ATOM   8469  O  O     . TYR   C 2  200 ? 18.130  -5.563  -28.953 1.00 47.51  ? 202 TYR   D O     1 
ATOM   8470  C  CB    . TYR   C 2  200 ? 16.679  -3.124  -28.177 1.00 31.40  ? 202 TYR   D CB    1 
ATOM   8471  C  CG    . TYR   C 2  200 ? 16.573  -1.675  -27.819 1.00 43.94  ? 202 TYR   D CG    1 
ATOM   8472  C  CD1   . TYR   C 2  200 ? 15.771  -1.251  -26.751 1.00 48.89  ? 202 TYR   D CD1   1 
ATOM   8473  C  CD2   . TYR   C 2  200 ? 17.240  -0.718  -28.561 1.00 37.42  ? 202 TYR   D CD2   1 
ATOM   8474  C  CE1   . TYR   C 2  200 ? 15.664  0.094   -26.421 1.00 42.37  ? 202 TYR   D CE1   1 
ATOM   8475  C  CE2   . TYR   C 2  200 ? 17.147  0.620   -28.245 1.00 39.77  ? 202 TYR   D CE2   1 
ATOM   8476  C  CZ    . TYR   C 2  200 ? 16.361  1.030   -27.179 1.00 51.45  ? 202 TYR   D CZ    1 
ATOM   8477  O  OH    . TYR   C 2  200 ? 16.282  2.385   -26.893 1.00 56.67  ? 202 TYR   D OH    1 
ATOM   8478  N  N     . CYS   C 2  201 ? 17.396  -6.352  -26.971 1.00 46.57  ? 203 CYS   D N     1 
ATOM   8479  C  CA    . CYS   C 2  201 ? 17.403  -7.754  -27.389 1.00 45.67  ? 203 CYS   D CA    1 
ATOM   8480  C  C     . CYS   C 2  201 ? 16.170  -8.056  -28.227 1.00 49.39  ? 203 CYS   D C     1 
ATOM   8481  O  O     . CYS   C 2  201 ? 15.093  -8.327  -27.698 1.00 57.16  ? 203 CYS   D O     1 
ATOM   8482  C  CB    . CYS   C 2  201 ? 17.457  -8.663  -26.178 1.00 38.14  ? 203 CYS   D CB    1 
ATOM   8483  S  SG    . CYS   C 2  201 ? 18.916  -8.304  -25.268 1.00 65.15  ? 203 CYS   D SG    1 
ATOM   8484  N  N     . ILE   C 2  202 ? 16.319  -8.014  -29.540 1.00 47.58  ? 204 ILE   D N     1 
ATOM   8485  C  CA    . ILE   C 2  202 ? 15.269  -8.455  -30.446 1.00 56.75  ? 204 ILE   D CA    1 
ATOM   8486  C  C     . ILE   C 2  202 ? 15.445  -9.955  -30.670 1.00 59.94  ? 204 ILE   D C     1 
ATOM   8487  O  O     . ILE   C 2  202 ? 16.475  -10.395 -31.192 1.00 57.88  ? 204 ILE   D O     1 
ATOM   8488  C  CB    . ILE   C 2  202 ? 15.323  -7.672  -31.761 1.00 46.38  ? 204 ILE   D CB    1 
ATOM   8489  C  CG1   . ILE   C 2  202 ? 14.827  -6.246  -31.507 1.00 41.65  ? 204 ILE   D CG1   1 
ATOM   8490  C  CG2   . ILE   C 2  202 ? 14.540  -8.406  -32.848 1.00 47.06  ? 204 ILE   D CG2   1 
ATOM   8491  C  CD1   . ILE   C 2  202 ? 15.490  -5.199  -32.359 1.00 47.58  ? 204 ILE   D CD1   1 
ATOM   8492  N  N     . ASP   C 2  203 ? 14.468  -10.750 -30.233 1.00 53.65  ? 205 ASP   D N     1 
ATOM   8493  C  CA    . ASP   C 2  203 ? 14.593  -12.206 -30.239 1.00 65.15  ? 205 ASP   D CA    1 
ATOM   8494  C  C     . ASP   C 2  203 ? 13.702  -12.788 -31.329 1.00 68.64  ? 205 ASP   D C     1 
ATOM   8495  O  O     . ASP   C 2  203 ? 12.478  -12.596 -31.311 1.00 65.03  ? 205 ASP   D O     1 
ATOM   8496  C  CB    . ASP   C 2  203 ? 14.249  -12.811 -28.875 1.00 64.43  ? 205 ASP   D CB    1 
ATOM   8497  C  CG    . ASP   C 2  203 ? 14.738  -14.251 -28.734 1.00 70.44  ? 205 ASP   D CG    1 
ATOM   8498  O  OD1   . ASP   C 2  203 ? 14.880  -14.927 -29.780 1.00 76.19  ? 205 ASP   D OD1   1 
ATOM   8499  O  OD2   . ASP   C 2  203 ? 14.979  -14.705 -27.586 1.00 63.82  ? 205 ASP   D OD2   1 
ATOM   8500  N  N     . ASN   C 2  204 ? 14.327  -13.484 -32.285 1.00 68.15  ? 206 ASN   D N     1 
ATOM   8501  C  CA    . ASN   C 2  204 ? 13.569  -14.113 -33.359 1.00 70.69  ? 206 ASN   D CA    1 
ATOM   8502  C  C     . ASN   C 2  204 ? 12.643  -15.187 -32.806 1.00 71.44  ? 206 ASN   D C     1 
ATOM   8503  O  O     . ASN   C 2  204 ? 11.492  -15.314 -33.249 1.00 55.23  ? 206 ASN   D O     1 
ATOM   8504  C  CB    . ASN   C 2  204 ? 14.523  -14.686 -34.409 1.00 62.14  ? 206 ASN   D CB    1 
ATOM   8505  C  CG    . ASN   C 2  204 ? 14.771  -13.723 -35.553 1.00 58.73  ? 206 ASN   D CG    1 
ATOM   8506  O  OD1   . ASN   C 2  204 ? 14.236  -12.616 -35.577 1.00 59.33  ? 206 ASN   D OD1   1 
ATOM   8507  N  ND2   . ASN   C 2  204 ? 15.575  -14.144 -36.513 1.00 61.05  ? 206 ASN   D ND2   1 
ATOM   8508  N  N     . GLU   C 2  205 ? 13.127  -15.959 -31.824 1.00 68.67  ? 207 GLU   D N     1 
ATOM   8509  C  CA    . GLU   C 2  205 ? 12.261  -16.892 -31.115 1.00 65.99  ? 207 GLU   D CA    1 
ATOM   8510  C  C     . GLU   C 2  205 ? 10.960  -16.213 -30.722 1.00 70.96  ? 207 GLU   D C     1 
ATOM   8511  O  O     . GLU   C 2  205 ? 9.865   -16.700 -31.027 1.00 68.73  ? 207 GLU   D O     1 
ATOM   8512  C  CB    . GLU   C 2  205 ? 12.971  -17.437 -29.877 1.00 60.52  ? 207 GLU   D CB    1 
ATOM   8513  C  CG    . GLU   C 2  205 ? 12.012  -18.029 -28.852 1.00 73.04  ? 207 GLU   D CG    1 
ATOM   8514  C  CD    . GLU   C 2  205 ? 11.927  -19.551 -28.906 1.00 78.95  ? 207 GLU   D CD    1 
ATOM   8515  O  OE1   . GLU   C 2  205 ? 12.955  -20.194 -29.212 1.00 72.60  ? 207 GLU   D OE1   1 
ATOM   8516  O  OE2   . GLU   C 2  205 ? 10.832  -20.101 -28.633 1.00 80.37  ? 207 GLU   D OE2   1 
ATOM   8517  N  N     . ALA   C 2  206 ? 11.062  -15.065 -30.062 1.00 62.85  ? 208 ALA   D N     1 
ATOM   8518  C  CA    . ALA   C 2  206 ? 9.851   -14.356 -29.688 1.00 63.33  ? 208 ALA   D CA    1 
ATOM   8519  C  C     . ALA   C 2  206 ? 9.149   -13.780 -30.912 1.00 63.74  ? 208 ALA   D C     1 
ATOM   8520  O  O     . ALA   C 2  206 ? 7.919   -13.856 -31.016 1.00 66.56  ? 208 ALA   D O     1 
ATOM   8521  C  CB    . ALA   C 2  206 ? 10.178  -13.268 -28.668 1.00 66.92  ? 208 ALA   D CB    1 
ATOM   8522  N  N     . LEU   C 2  207 ? 9.905   -13.199 -31.850 1.00 60.81  ? 209 LEU   D N     1 
ATOM   8523  C  CA    . LEU   C 2  207 ? 9.277   -12.666 -33.057 1.00 61.47  ? 209 LEU   D CA    1 
ATOM   8524  C  C     . LEU   C 2  207 ? 8.377   -13.710 -33.708 1.00 75.07  ? 209 LEU   D C     1 
ATOM   8525  O  O     . LEU   C 2  207 ? 7.271   -13.396 -34.161 1.00 76.36  ? 209 LEU   D O     1 
ATOM   8526  C  CB    . LEU   C 2  207 ? 10.343  -12.190 -34.042 1.00 68.03  ? 209 LEU   D CB    1 
ATOM   8527  C  CG    . LEU   C 2  207 ? 10.715  -10.708 -34.022 1.00 74.26  ? 209 LEU   D CG    1 
ATOM   8528  C  CD1   . LEU   C 2  207 ? 9.811   -9.887  -34.940 1.00 71.05  ? 209 LEU   D CD1   1 
ATOM   8529  C  CD2   . LEU   C 2  207 ? 10.618  -10.200 -32.615 1.00 60.54  ? 209 LEU   D CD2   1 
ATOM   8530  N  N     . TYR   C 2  208 ? 8.833   -14.964 -33.736 1.00 75.52  ? 210 TYR   D N     1 
ATOM   8531  C  CA    . TYR   C 2  208 ? 8.124   -16.076 -34.358 1.00 72.19  ? 210 TYR   D CA    1 
ATOM   8532  C  C     . TYR   C 2  208 ? 6.864   -16.436 -33.590 1.00 76.59  ? 210 TYR   D C     1 
ATOM   8533  O  O     . TYR   C 2  208 ? 5.752   -16.294 -34.107 1.00 79.49  ? 210 TYR   D O     1 
ATOM   8534  C  CB    . TYR   C 2  208 ? 9.039   -17.299 -34.431 1.00 78.96  ? 210 TYR   D CB    1 
ATOM   8535  C  CG    . TYR   C 2  208 ? 8.511   -18.440 -35.262 1.00 86.19  ? 210 TYR   D CG    1 
ATOM   8536  C  CD1   . TYR   C 2  208 ? 7.680   -18.206 -36.355 1.00 84.17  ? 210 TYR   D CD1   1 
ATOM   8537  C  CD2   . TYR   C 2  208 ? 8.846   -19.758 -34.957 1.00 86.77  ? 210 TYR   D CD2   1 
ATOM   8538  C  CE1   . TYR   C 2  208 ? 7.198   -19.255 -37.122 1.00 93.99  ? 210 TYR   D CE1   1 
ATOM   8539  C  CE2   . TYR   C 2  208 ? 8.367   -20.817 -35.718 1.00 94.17  ? 210 TYR   D CE2   1 
ATOM   8540  C  CZ    . TYR   C 2  208 ? 7.542   -20.559 -36.802 1.00 105.44 ? 210 TYR   D CZ    1 
ATOM   8541  O  OH    . TYR   C 2  208 ? 7.058   -21.598 -37.569 1.00 100.27 ? 210 TYR   D OH    1 
ATOM   8542  N  N     . ASP   C 2  209 ? 7.042   -16.921 -32.358 1.00 77.10  ? 211 ASP   D N     1 
ATOM   8543  C  CA    . ASP   C 2  209 ? 5.942   -17.328 -31.491 1.00 66.30  ? 211 ASP   D CA    1 
ATOM   8544  C  C     . ASP   C 2  209 ? 4.796   -16.329 -31.547 1.00 65.16  ? 211 ASP   D C     1 
ATOM   8545  O  O     . ASP   C 2  209 ? 3.628   -16.721 -31.610 1.00 73.88  ? 211 ASP   D O     1 
ATOM   8546  C  CB    . ASP   C 2  209 ? 6.440   -17.507 -30.055 1.00 48.88  ? 211 ASP   D CB    1 
ATOM   8547  C  CG    . ASP   C 2  209 ? 7.380   -18.705 -29.907 1.00 69.24  ? 211 ASP   D CG    1 
ATOM   8548  O  OD1   . ASP   C 2  209 ? 7.623   -19.392 -30.922 1.00 67.78  ? 211 ASP   D OD1   1 
ATOM   8549  O  OD2   . ASP   C 2  209 ? 7.874   -18.971 -28.783 1.00 68.69  ? 211 ASP   D OD2   1 
ATOM   8550  N  N     . ILE   C 2  210 ? 5.113   -15.036 -31.537 1.00 68.40  ? 212 ILE   D N     1 
ATOM   8551  C  CA    . ILE   C 2  210 ? 4.063   -14.029 -31.632 1.00 72.68  ? 212 ILE   D CA    1 
ATOM   8552  C  C     . ILE   C 2  210 ? 3.385   -14.101 -32.990 1.00 75.55  ? 212 ILE   D C     1 
ATOM   8553  O  O     . ILE   C 2  210 ? 2.164   -13.941 -33.103 1.00 76.34  ? 212 ILE   D O     1 
ATOM   8554  C  CB    . ILE   C 2  210 ? 4.641   -12.630 -31.352 1.00 79.04  ? 212 ILE   D CB    1 
ATOM   8555  C  CG1   . ILE   C 2  210 ? 5.033   -12.519 -29.872 1.00 81.44  ? 212 ILE   D CG1   1 
ATOM   8556  C  CG2   . ILE   C 2  210 ? 3.650   -11.535 -31.774 1.00 74.25  ? 212 ILE   D CG2   1 
ATOM   8557  C  CD1   . ILE   C 2  210 ? 5.778   -11.245 -29.507 1.00 74.33  ? 212 ILE   D CD1   1 
ATOM   8558  N  N     . CYS   C 2  211 ? 4.167   -14.350 -34.039 1.00 84.39  ? 213 CYS   D N     1 
ATOM   8559  C  CA    . CYS   C 2  211 ? 3.615   -14.502 -35.381 1.00 79.01  ? 213 CYS   D CA    1 
ATOM   8560  C  C     . CYS   C 2  211 ? 2.729   -15.740 -35.470 1.00 75.20  ? 213 CYS   D C     1 
ATOM   8561  O  O     . CYS   C 2  211 ? 1.551   -15.655 -35.839 1.00 71.44  ? 213 CYS   D O     1 
ATOM   8562  C  CB    . CYS   C 2  211 ? 4.757   -14.573 -36.395 1.00 72.40  ? 213 CYS   D CB    1 
ATOM   8563  S  SG    . CYS   C 2  211 ? 5.601   -13.009 -36.679 1.00 79.50  ? 213 CYS   D SG    1 
ATOM   8564  N  N     . PHE   C 2  212 ? 3.292   -16.904 -35.142 1.00 78.53  ? 214 PHE   D N     1 
ATOM   8565  C  CA    . PHE   C 2  212 ? 2.568   -18.168 -35.104 1.00 84.40  ? 214 PHE   D CA    1 
ATOM   8566  C  C     . PHE   C 2  212 ? 1.239   -17.970 -34.392 1.00 86.13  ? 214 PHE   D C     1 
ATOM   8567  O  O     . PHE   C 2  212 ? 0.191   -17.818 -35.033 1.00 81.17  ? 214 PHE   D O     1 
ATOM   8568  C  CB    . PHE   C 2  212 ? 3.405   -19.232 -34.386 1.00 83.56  ? 214 PHE   D CB    1 
ATOM   8569  C  CG    . PHE   C 2  212 ? 3.265   -20.617 -34.956 1.00 97.35  ? 214 PHE   D CG    1 
ATOM   8570  C  CD1   . PHE   C 2  212 ? 2.669   -20.823 -36.190 1.00 93.50  ? 214 PHE   D CD1   1 
ATOM   8571  C  CD2   . PHE   C 2  212 ? 3.731   -21.718 -34.248 1.00 96.82  ? 214 PHE   D CD2   1 
ATOM   8572  C  CE1   . PHE   C 2  212 ? 2.545   -22.101 -36.709 1.00 94.10  ? 214 PHE   D CE1   1 
ATOM   8573  C  CE2   . PHE   C 2  212 ? 3.609   -22.997 -34.761 1.00 88.34  ? 214 PHE   D CE2   1 
ATOM   8574  C  CZ    . PHE   C 2  212 ? 3.014   -23.189 -35.992 1.00 90.07  ? 214 PHE   D CZ    1 
ATOM   8575  N  N     . ARG   C 2  213 ? 1.297   -17.952 -33.058 1.00 88.93  ? 215 ARG   D N     1 
ATOM   8576  C  CA    . ARG   C 2  213 ? 0.154   -17.664 -32.203 1.00 76.99  ? 215 ARG   D CA    1 
ATOM   8577  C  C     . ARG   C 2  213 ? -0.397  -16.270 -32.456 1.00 79.97  ? 215 ARG   D C     1 
ATOM   8578  O  O     . ARG   C 2  213 ? -0.403  -15.784 -33.592 1.00 86.68  ? 215 ARG   D O     1 
ATOM   8579  C  CB    . ARG   C 2  213 ? 0.544   -17.792 -30.731 1.00 70.54  ? 215 ARG   D CB    1 
ATOM   8580  C  CG    . ARG   C 2  213 ? 0.833   -19.210 -30.287 1.00 79.20  ? 215 ARG   D CG    1 
ATOM   8581  C  CD    . ARG   C 2  213 ? 2.308   -19.441 -30.033 1.00 76.54  ? 215 ARG   D CD    1 
ATOM   8582  N  NE    . ARG   C 2  213 ? 2.523   -20.675 -29.285 1.00 82.34  ? 215 ARG   D NE    1 
ATOM   8583  C  CZ    . ARG   C 2  213 ? 2.864   -20.731 -28.003 1.00 90.05  ? 215 ARG   D CZ    1 
ATOM   8584  N  NH1   . ARG   C 2  213 ? 3.068   -19.635 -27.292 1.00 87.30  ? 215 ARG   D NH1   1 
ATOM   8585  N  NH2   . ARG   C 2  213 ? 3.016   -21.919 -27.423 1.00 97.23  ? 215 ARG   D NH2   1 
ATOM   8586  N  N     . THR   C 2  214 ? -0.874  -15.641 -31.387 1.00 87.44  ? 216 THR   D N     1 
ATOM   8587  C  CA    . THR   C 2  214 ? -1.331  -14.255 -31.347 1.00 87.86  ? 216 THR   D CA    1 
ATOM   8588  C  C     . THR   C 2  214 ? -1.671  -13.671 -32.718 1.00 79.85  ? 216 THR   D C     1 
ATOM   8589  O  O     . THR   C 2  214 ? -2.796  -13.208 -32.936 1.00 83.79  ? 216 THR   D O     1 
ATOM   8590  C  CB    . THR   C 2  214 ? -0.271  -13.403 -30.636 1.00 89.06  ? 216 THR   D CB    1 
ATOM   8591  O  OG1   . THR   C 2  214 ? 0.189   -14.092 -29.459 1.00 71.81  ? 216 THR   D OG1   1 
ATOM   8592  C  CG2   . THR   C 2  214 ? -0.851  -12.056 -30.229 1.00 87.57  ? 216 THR   D CG2   1 
ATOM   8593  N  N     . LEU   C 2  215 ? -0.727  -13.689 -33.656 1.00 88.66  ? 217 LEU   D N     1 
ATOM   8594  C  CA    . LEU   C 2  215 ? -0.964  -13.072 -34.955 1.00 90.17  ? 217 LEU   D CA    1 
ATOM   8595  C  C     . LEU   C 2  215 ? -1.531  -14.030 -36.001 1.00 88.15  ? 217 LEU   D C     1 
ATOM   8596  O  O     . LEU   C 2  215 ? -1.937  -13.570 -37.077 1.00 83.51  ? 217 LEU   D O     1 
ATOM   8597  C  CB    . LEU   C 2  215 ? 0.322   -12.423 -35.472 1.00 83.20  ? 217 LEU   D CB    1 
ATOM   8598  C  CG    . LEU   C 2  215 ? 0.309   -10.935 -35.126 1.00 75.14  ? 217 LEU   D CG    1 
ATOM   8599  C  CD1   . LEU   C 2  215 ? 1.349   -10.157 -35.912 1.00 68.21  ? 217 LEU   D CD1   1 
ATOM   8600  C  CD2   . LEU   C 2  215 ? -1.085  -10.381 -35.370 1.00 76.43  ? 217 LEU   D CD2   1 
ATOM   8601  N  N     . LYS   C 2  216 ? -1.568  -15.337 -35.724 1.00 85.29  ? 218 LYS   D N     1 
ATOM   8602  C  CA    . LYS   C 2  216 ? -2.424  -16.239 -36.490 1.00 92.96  ? 218 LYS   D CA    1 
ATOM   8603  C  C     . LYS   C 2  216 ? -1.828  -16.593 -37.847 1.00 93.14  ? 218 LYS   D C     1 
ATOM   8604  O  O     . LYS   C 2  216 ? -2.492  -16.426 -38.875 1.00 90.14  ? 218 LYS   D O     1 
ATOM   8605  C  CB    . LYS   C 2  216 ? -3.802  -15.588 -36.689 1.00 106.07 ? 218 LYS   D CB    1 
ATOM   8606  C  CG    . LYS   C 2  216 ? -5.035  -16.432 -36.339 1.00 108.68 ? 218 LYS   D CG    1 
ATOM   8607  C  CD    . LYS   C 2  216 ? -6.314  -15.670 -36.729 1.00 105.49 ? 218 LYS   D CD    1 
ATOM   8608  C  CE    . LYS   C 2  216 ? -7.579  -16.490 -36.525 1.00 99.39  ? 218 LYS   D CE    1 
ATOM   8609  N  NZ    . LYS   C 2  216 ? -8.779  -15.773 -37.048 1.00 90.16  ? 218 LYS   D NZ    1 
ATOM   8610  N  N     . LEU   C 2  217 ? -0.591  -17.085 -37.877 1.00 94.36  ? 219 LEU   D N     1 
ATOM   8611  C  CA    . LEU   C 2  217 ? 0.071   -17.371 -39.143 1.00 89.30  ? 219 LEU   D CA    1 
ATOM   8612  C  C     . LEU   C 2  217 ? 0.952   -18.599 -39.008 1.00 88.11  ? 219 LEU   D C     1 
ATOM   8613  O  O     . LEU   C 2  217 ? 1.727   -18.705 -38.055 1.00 81.24  ? 219 LEU   D O     1 
ATOM   8614  C  CB    . LEU   C 2  217 ? 0.931   -16.190 -39.613 1.00 85.11  ? 219 LEU   D CB    1 
ATOM   8615  C  CG    . LEU   C 2  217 ? 0.363   -14.770 -39.608 1.00 86.68  ? 219 LEU   D CG    1 
ATOM   8616  C  CD1   . LEU   C 2  217 ? 1.391   -13.814 -40.208 1.00 86.45  ? 219 LEU   D CD1   1 
ATOM   8617  C  CD2   . LEU   C 2  217 ? -0.964  -14.680 -40.349 1.00 76.90  ? 219 LEU   D CD2   1 
ATOM   8618  N  N     . THR   C 2  218 ? 0.826   -19.522 -39.958 1.00 91.26  ? 220 THR   D N     1 
ATOM   8619  C  CA    . THR   C 2  218 ? 1.841   -20.541 -40.168 1.00 87.27  ? 220 THR   D CA    1 
ATOM   8620  C  C     . THR   C 2  218 ? 2.840   -20.015 -41.179 1.00 85.28  ? 220 THR   D C     1 
ATOM   8621  O  O     . THR   C 2  218 ? 2.492   -19.223 -42.059 1.00 94.39  ? 220 THR   D O     1 
ATOM   8622  C  CB    . THR   C 2  218 ? 1.244   -21.853 -40.679 1.00 92.09  ? 220 THR   D CB    1 
ATOM   8623  O  OG1   . THR   C 2  218 ? -0.175  -21.715 -40.827 1.00 99.07  ? 220 THR   D OG1   1 
ATOM   8624  C  CG2   . THR   C 2  218 ? 1.570   -23.003 -39.724 1.00 78.34  ? 220 THR   D CG2   1 
ATOM   8625  N  N     . THR   C 2  219 ? 4.084   -20.463 -41.049 1.00 80.10  ? 221 THR   D N     1 
ATOM   8626  C  CA    . THR   C 2  219 ? 5.169   -19.982 -41.899 1.00 85.43  ? 221 THR   D CA    1 
ATOM   8627  C  C     . THR   C 2  219 ? 5.086   -18.465 -42.031 1.00 86.91  ? 221 THR   D C     1 
ATOM   8628  O  O     . THR   C 2  219 ? 4.541   -17.944 -43.017 1.00 73.49  ? 221 THR   D O     1 
ATOM   8629  C  CB    . THR   C 2  219 ? 5.143   -20.649 -43.280 1.00 72.17  ? 221 THR   D CB    1 
ATOM   8630  O  OG1   . THR   C 2  219 ? 3.884   -20.406 -43.923 1.00 72.16  ? 221 THR   D OG1   1 
ATOM   8631  C  CG2   . THR   C 2  219 ? 5.358   -22.148 -43.147 1.00 77.62  ? 221 THR   D CG2   1 
ATOM   8632  N  N     . PRO   C 2  220 ? 5.579   -17.730 -41.040 1.00 90.47  ? 222 PRO   D N     1 
ATOM   8633  C  CA    . PRO   C 2  220 ? 5.638   -16.271 -41.158 1.00 81.83  ? 222 PRO   D CA    1 
ATOM   8634  C  C     . PRO   C 2  220 ? 6.844   -15.831 -41.974 1.00 70.29  ? 222 PRO   D C     1 
ATOM   8635  O  O     . PRO   C 2  220 ? 7.884   -16.495 -42.008 1.00 66.97  ? 222 PRO   D O     1 
ATOM   8636  C  CB    . PRO   C 2  220 ? 5.746   -15.807 -39.701 1.00 83.43  ? 222 PRO   D CB    1 
ATOM   8637  C  CG    . PRO   C 2  220 ? 6.393   -16.960 -38.991 1.00 77.07  ? 222 PRO   D CG    1 
ATOM   8638  C  CD    . PRO   C 2  220 ? 5.964   -18.210 -39.699 1.00 74.45  ? 222 PRO   D CD    1 
ATOM   8639  N  N     . THR   C 2  221 ? 6.688   -14.697 -42.645 1.00 72.12  ? 223 THR   D N     1 
ATOM   8640  C  CA    . THR   C 2  221 ? 7.720   -14.180 -43.532 1.00 74.66  ? 223 THR   D CA    1 
ATOM   8641  C  C     . THR   C 2  221 ? 8.645   -13.215 -42.782 1.00 81.71  ? 223 THR   D C     1 
ATOM   8642  O  O     . THR   C 2  221 ? 8.249   -12.585 -41.794 1.00 75.76  ? 223 THR   D O     1 
ATOM   8643  C  CB    . THR   C 2  221 ? 7.078   -13.495 -44.752 1.00 67.79  ? 223 THR   D CB    1 
ATOM   8644  O  OG1   . THR   C 2  221 ? 8.079   -12.834 -45.540 1.00 84.74  ? 223 THR   D OG1   1 
ATOM   8645  C  CG2   . THR   C 2  221 ? 6.025   -12.481 -44.331 1.00 65.16  ? 223 THR   D CG2   1 
ATOM   8646  N  N     . TYR   C 2  222 ? 9.901   -13.130 -43.241 1.00 81.71  ? 224 TYR   D N     1 
ATOM   8647  C  CA    . TYR   C 2  222 ? 10.833  -12.171 -42.654 1.00 67.60  ? 224 TYR   D CA    1 
ATOM   8648  C  C     . TYR   C 2  222 ? 10.219  -10.784 -42.631 1.00 71.86  ? 224 TYR   D C     1 
ATOM   8649  O  O     . TYR   C 2  222 ? 10.159  -10.135 -41.581 1.00 76.20  ? 224 TYR   D O     1 
ATOM   8650  C  CB    . TYR   C 2  222 ? 12.162  -12.155 -43.415 1.00 62.31  ? 224 TYR   D CB    1 
ATOM   8651  C  CG    . TYR   C 2  222 ? 13.152  -13.176 -42.907 1.00 64.82  ? 224 TYR   D CG    1 
ATOM   8652  C  CD1   . TYR   C 2  222 ? 13.365  -13.337 -41.547 1.00 61.92  ? 224 TYR   D CD1   1 
ATOM   8653  C  CD2   . TYR   C 2  222 ? 13.858  -13.993 -43.781 1.00 58.12  ? 224 TYR   D CD2   1 
ATOM   8654  C  CE1   . TYR   C 2  222 ? 14.259  -14.280 -41.064 1.00 66.41  ? 224 TYR   D CE1   1 
ATOM   8655  C  CE2   . TYR   C 2  222 ? 14.760  -14.939 -43.308 1.00 65.37  ? 224 TYR   D CE2   1 
ATOM   8656  C  CZ    . TYR   C 2  222 ? 14.956  -15.081 -41.947 1.00 67.06  ? 224 TYR   D CZ    1 
ATOM   8657  O  OH    . TYR   C 2  222 ? 15.844  -16.019 -41.454 1.00 60.60  ? 224 TYR   D OH    1 
ATOM   8658  N  N     . GLY   C 2  223 ? 9.739   -10.319 -43.782 1.00 69.05  ? 225 GLY   D N     1 
ATOM   8659  C  CA    . GLY   C 2  223 ? 9.034   -9.052  -43.810 1.00 67.27  ? 225 GLY   D CA    1 
ATOM   8660  C  C     . GLY   C 2  223 ? 7.986   -8.945  -42.722 1.00 78.16  ? 225 GLY   D C     1 
ATOM   8661  O  O     . GLY   C 2  223 ? 7.662   -7.839  -42.277 1.00 81.50  ? 225 GLY   D O     1 
ATOM   8662  N  N     . ASP   C 2  224 ? 7.452   -10.088 -42.266 1.00 65.76  ? 226 ASP   D N     1 
ATOM   8663  C  CA    . ASP   C 2  224 ? 6.434   -10.081 -41.217 1.00 72.41  ? 226 ASP   D CA    1 
ATOM   8664  C  C     . ASP   C 2  224 ? 7.062   -9.943  -39.831 1.00 76.50  ? 226 ASP   D C     1 
ATOM   8665  O  O     . ASP   C 2  224 ? 6.666   -9.064  -39.053 1.00 66.18  ? 226 ASP   D O     1 
ATOM   8666  C  CB    . ASP   C 2  224 ? 5.570   -11.344 -41.304 1.00 81.97  ? 226 ASP   D CB    1 
ATOM   8667  C  CG    . ASP   C 2  224 ? 4.268   -11.120 -42.080 1.00 85.70  ? 226 ASP   D CG    1 
ATOM   8668  O  OD1   . ASP   C 2  224 ? 4.046   -9.997  -42.608 1.00 71.65  ? 226 ASP   D OD1   1 
ATOM   8669  O  OD2   . ASP   C 2  224 ? 3.465   -12.080 -42.152 1.00 86.02  ? 226 ASP   D OD2   1 
ATOM   8670  N  N     . LEU   C 2  225 ? 8.037   -10.805 -39.501 1.00 76.01  ? 227 LEU   D N     1 
ATOM   8671  C  CA    . LEU   C 2  225 ? 8.886   -10.551 -38.337 1.00 72.82  ? 227 LEU   D CA    1 
ATOM   8672  C  C     . LEU   C 2  225 ? 9.372   -9.108  -38.340 1.00 71.05  ? 227 LEU   D C     1 
ATOM   8673  O  O     . LEU   C 2  225 ? 9.182   -8.365  -37.369 1.00 67.24  ? 227 LEU   D O     1 
ATOM   8674  C  CB    . LEU   C 2  225 ? 10.082  -11.503 -38.316 1.00 57.02  ? 227 LEU   D CB    1 
ATOM   8675  C  CG    . LEU   C 2  225 ? 9.775   -12.995 -38.239 1.00 67.13  ? 227 LEU   D CG    1 
ATOM   8676  C  CD1   . LEU   C 2  225 ? 11.039  -13.813 -37.967 1.00 56.00  ? 227 LEU   D CD1   1 
ATOM   8677  C  CD2   . LEU   C 2  225 ? 8.731   -13.256 -37.185 1.00 67.91  ? 227 LEU   D CD2   1 
ATOM   8678  N  N     . ASN   C 2  226 ? 9.971   -8.687  -39.450 1.00 62.96  ? 228 ASN   D N     1 
ATOM   8679  C  CA    . ASN   C 2  226 ? 10.460  -7.325  -39.591 1.00 62.14  ? 228 ASN   D CA    1 
ATOM   8680  C  C     . ASN   C 2  226 ? 9.332   -6.308  -39.445 1.00 67.77  ? 228 ASN   D C     1 
ATOM   8681  O  O     . ASN   C 2  226 ? 9.575   -5.094  -39.460 1.00 72.74  ? 228 ASN   D O     1 
ATOM   8682  C  CB    . ASN   C 2  226 ? 11.185  -7.176  -40.928 1.00 61.26  ? 228 ASN   D CB    1 
ATOM   8683  C  CG    . ASN   C 2  226 ? 12.543  -7.885  -40.936 1.00 63.01  ? 228 ASN   D CG    1 
ATOM   8684  O  OD1   . ASN   C 2  226 ? 12.919  -8.577  -39.975 1.00 49.31  ? 228 ASN   D OD1   1 
ATOM   8685  N  ND2   . ASN   C 2  226 ? 13.282  -7.713  -42.022 1.00 59.62  ? 228 ASN   D ND2   1 
ATOM   8686  N  N     . HIS   C 2  227 ? 8.097   -6.777  -39.281 1.00 70.49  ? 229 HIS   D N     1 
ATOM   8687  C  CA    . HIS   C 2  227 ? 7.025   -5.845  -38.965 1.00 72.93  ? 229 HIS   D CA    1 
ATOM   8688  C  C     . HIS   C 2  227 ? 6.892   -5.615  -37.474 1.00 63.35  ? 229 HIS   D C     1 
ATOM   8689  O  O     . HIS   C 2  227 ? 6.495   -4.522  -37.049 1.00 51.11  ? 229 HIS   D O     1 
ATOM   8690  C  CB    . HIS   C 2  227 ? 5.687   -6.332  -39.505 1.00 62.05  ? 229 HIS   D CB    1 
ATOM   8691  C  CG    . HIS   C 2  227 ? 4.667   -5.248  -39.560 1.00 76.76  ? 229 HIS   D CG    1 
ATOM   8692  N  ND1   . HIS   C 2  227 ? 4.804   -4.150  -40.385 1.00 77.18  ? 229 HIS   D ND1   1 
ATOM   8693  C  CD2   . HIS   C 2  227 ? 3.523   -5.058  -38.861 1.00 74.84  ? 229 HIS   D CD2   1 
ATOM   8694  C  CE1   . HIS   C 2  227 ? 3.773   -3.343  -40.213 1.00 81.62  ? 229 HIS   D CE1   1 
ATOM   8695  N  NE2   . HIS   C 2  227 ? 2.982   -3.870  -39.293 1.00 93.28  ? 229 HIS   D NE2   1 
ATOM   8696  N  N     . LEU   C 2  228 ? 7.202   -6.639  -36.684 1.00 65.16  ? 230 LEU   D N     1 
ATOM   8697  C  CA    . LEU   C 2  228 ? 7.339   -6.457  -35.246 1.00 73.77  ? 230 LEU   D CA    1 
ATOM   8698  C  C     . LEU   C 2  228 ? 8.573   -5.619  -34.915 1.00 67.35  ? 230 LEU   D C     1 
ATOM   8699  O  O     . LEU   C 2  228 ? 8.519   -4.739  -34.047 1.00 61.26  ? 230 LEU   D O     1 
ATOM   8700  C  CB    . LEU   C 2  228 ? 7.401   -7.823  -34.555 1.00 71.84  ? 230 LEU   D CB    1 
ATOM   8701  C  CG    . LEU   C 2  228 ? 6.248   -8.787  -34.864 1.00 70.41  ? 230 LEU   D CG    1 
ATOM   8702  C  CD1   . LEU   C 2  228 ? 6.349   -10.069 -34.023 1.00 69.68  ? 230 LEU   D CD1   1 
ATOM   8703  C  CD2   . LEU   C 2  228 ? 4.882   -8.096  -34.689 1.00 58.85  ? 230 LEU   D CD2   1 
ATOM   8704  N  N     . VAL   C 2  229 ? 9.694   -5.872  -35.599 1.00 59.61  ? 231 VAL   D N     1 
ATOM   8705  C  CA    . VAL   C 2  229 ? 10.888  -5.074  -35.353 1.00 51.45  ? 231 VAL   D CA    1 
ATOM   8706  C  C     . VAL   C 2  229 ? 10.636  -3.626  -35.740 1.00 50.56  ? 231 VAL   D C     1 
ATOM   8707  O  O     . VAL   C 2  229 ? 11.055  -2.698  -35.042 1.00 47.79  ? 231 VAL   D O     1 
ATOM   8708  C  CB    . VAL   C 2  229 ? 12.093  -5.665  -36.104 1.00 59.04  ? 231 VAL   D CB    1 
ATOM   8709  C  CG1   . VAL   C 2  229 ? 13.359  -4.860  -35.800 1.00 52.93  ? 231 VAL   D CG1   1 
ATOM   8710  C  CG2   . VAL   C 2  229 ? 12.275  -7.132  -35.735 1.00 50.15  ? 231 VAL   D CG2   1 
ATOM   8711  N  N     . SER   C 2  230 ? 9.921   -3.410  -36.842 1.00 51.80  ? 232 SER   D N     1 
ATOM   8712  C  CA    . SER   C 2  230 ? 9.672   -2.050  -37.299 1.00 49.91  ? 232 SER   D CA    1 
ATOM   8713  C  C     . SER   C 2  230 ? 8.809   -1.264  -36.313 1.00 64.51  ? 232 SER   D C     1 
ATOM   8714  O  O     . SER   C 2  230 ? 8.954   -0.038  -36.203 1.00 65.38  ? 232 SER   D O     1 
ATOM   8715  C  CB    . SER   C 2  230 ? 9.025   -2.087  -38.680 1.00 51.39  ? 232 SER   D CB    1 
ATOM   8716  O  OG    . SER   C 2  230 ? 8.891   -0.782  -39.210 1.00 62.35  ? 232 SER   D OG    1 
ATOM   8717  N  N     . ALA   C 2  231 ? 7.908   -1.941  -35.592 1.00 62.60  ? 233 ALA   D N     1 
ATOM   8718  C  CA    . ALA   C 2  231 ? 7.038   -1.250  -34.645 1.00 61.33  ? 233 ALA   D CA    1 
ATOM   8719  C  C     . ALA   C 2  231 ? 7.793   -0.886  -33.369 1.00 59.01  ? 233 ALA   D C     1 
ATOM   8720  O  O     . ALA   C 2  231 ? 7.699   0.244   -32.874 1.00 50.02  ? 233 ALA   D O     1 
ATOM   8721  C  CB    . ALA   C 2  231 ? 5.824   -2.124  -34.322 1.00 49.15  ? 233 ALA   D CB    1 
ATOM   8722  N  N     . THR   C 2  232 ? 8.521   -1.847  -32.815 1.00 43.88  ? 234 THR   D N     1 
ATOM   8723  C  CA    . THR   C 2  232 ? 9.407   -1.598  -31.697 1.00 54.03  ? 234 THR   D CA    1 
ATOM   8724  C  C     . THR   C 2  232 ? 10.288  -0.388  -31.960 1.00 60.94  ? 234 THR   D C     1 
ATOM   8725  O  O     . THR   C 2  232 ? 10.122  0.655   -31.313 1.00 53.20  ? 234 THR   D O     1 
ATOM   8726  C  CB    . THR   C 2  232 ? 10.270  -2.822  -31.442 1.00 49.34  ? 234 THR   D CB    1 
ATOM   8727  O  OG1   . THR   C 2  232 ? 9.418   -3.965  -31.292 1.00 50.06  ? 234 THR   D OG1   1 
ATOM   8728  C  CG2   . THR   C 2  232 ? 11.103  -2.623  -30.198 1.00 46.11  ? 234 THR   D CG2   1 
ATOM   8729  N  N     . MET   C 2  233 ? 11.209  -0.523  -32.926 1.00 56.97  ? 235 MET   D N     1 
ATOM   8730  C  CA    . MET   C 2  233 ? 12.202  0.515   -33.185 1.00 49.09  ? 235 MET   D CA    1 
ATOM   8731  C  C     . MET   C 2  233 ? 11.566  1.897   -33.294 1.00 53.09  ? 235 MET   D C     1 
ATOM   8732  O  O     . MET   C 2  233 ? 12.150  2.896   -32.855 1.00 54.80  ? 235 MET   D O     1 
ATOM   8733  C  CB    . MET   C 2  233 ? 12.995  0.179   -34.448 1.00 49.15  ? 235 MET   D CB    1 
ATOM   8734  C  CG    . MET   C 2  233 ? 13.571  -1.230  -34.435 1.00 57.84  ? 235 MET   D CG    1 
ATOM   8735  S  SD    . MET   C 2  233 ? 15.226  -1.435  -35.141 1.00 62.10  ? 235 MET   D SD    1 
ATOM   8736  C  CE    . MET   C 2  233 ? 15.145  -0.375  -36.561 1.00 50.42  ? 235 MET   D CE    1 
ATOM   8737  N  N     . SER   C 2  234 ? 10.369  1.988   -33.865 1.00 51.61  ? 236 SER   D N     1 
ATOM   8738  C  CA    . SER   C 2  234 ? 9.703   3.286   -33.832 1.00 51.90  ? 236 SER   D CA    1 
ATOM   8739  C  C     . SER   C 2  234 ? 9.261   3.642   -32.424 1.00 58.82  ? 236 SER   D C     1 
ATOM   8740  O  O     . SER   C 2  234 ? 9.254   4.825   -32.053 1.00 58.79  ? 236 SER   D O     1 
ATOM   8741  C  CB    . SER   C 2  234 ? 8.498   3.307   -34.755 1.00 49.43  ? 236 SER   D CB    1 
ATOM   8742  O  OG    . SER   C 2  234 ? 7.859   4.560   -34.644 1.00 54.91  ? 236 SER   D OG    1 
ATOM   8743  N  N     . GLY   C 2  235 ? 8.888   2.637   -31.632 1.00 51.70  ? 237 GLY   D N     1 
ATOM   8744  C  CA    . GLY   C 2  235 ? 8.410   2.912   -30.288 1.00 57.37  ? 237 GLY   D CA    1 
ATOM   8745  C  C     . GLY   C 2  235 ? 9.528   3.318   -29.351 1.00 57.60  ? 237 GLY   D C     1 
ATOM   8746  O  O     . GLY   C 2  235 ? 9.436   4.334   -28.661 1.00 50.27  ? 237 GLY   D O     1 
ATOM   8747  N  N     . VAL   C 2  236 ? 10.614  2.536   -29.333 1.00 57.58  ? 238 VAL   D N     1 
ATOM   8748  C  CA    . VAL   C 2  236 ? 11.736  2.810   -28.441 1.00 54.85  ? 238 VAL   D CA    1 
ATOM   8749  C  C     . VAL   C 2  236 ? 12.602  3.978   -28.891 1.00 53.95  ? 238 VAL   D C     1 
ATOM   8750  O  O     . VAL   C 2  236 ? 13.592  4.290   -28.215 1.00 62.99  ? 238 VAL   D O     1 
ATOM   8751  C  CB    . VAL   C 2  236 ? 12.595  1.541   -28.287 1.00 51.45  ? 238 VAL   D CB    1 
ATOM   8752  C  CG1   . VAL   C 2  236 ? 11.702  0.336   -28.129 1.00 44.29  ? 238 VAL   D CG1   1 
ATOM   8753  C  CG2   . VAL   C 2  236 ? 13.502  1.391   -29.481 1.00 48.25  ? 238 VAL   D CG2   1 
ATOM   8754  N  N     . THR   C 2  237 ? 12.272  4.645   -29.996 1.00 50.73  ? 239 THR   D N     1 
ATOM   8755  C  CA    . THR   C 2  237 ? 12.983  5.866   -30.368 1.00 52.36  ? 239 THR   D CA    1 
ATOM   8756  C  C     . THR   C 2  237 ? 12.073  7.082   -30.409 1.00 52.70  ? 239 THR   D C     1 
ATOM   8757  O  O     . THR   C 2  237 ? 12.544  8.182   -30.737 1.00 46.24  ? 239 THR   D O     1 
ATOM   8758  C  CB    . THR   C 2  237 ? 13.709  5.718   -31.722 1.00 42.93  ? 239 THR   D CB    1 
ATOM   8759  O  OG1   . THR   C 2  237 ? 12.780  5.820   -32.816 1.00 39.68  ? 239 THR   D OG1   1 
ATOM   8760  C  CG2   . THR   C 2  237 ? 14.430  4.390   -31.782 1.00 40.30  ? 239 THR   D CG2   1 
ATOM   8761  N  N     . THR   C 2  238 ? 10.789  6.923   -30.074 1.00 49.25  ? 240 THR   D N     1 
ATOM   8762  C  CA    A THR   C 2  238 ? 9.885   8.068   -30.048 0.00 47.54  ? 240 THR   D CA    1 
ATOM   8763  C  CA    B THR   C 2  238 ? 9.889   8.070   -30.052 1.00 47.13  ? 240 THR   D CA    1 
ATOM   8764  C  C     . THR   C 2  238 ? 10.422  9.169   -29.142 1.00 52.46  ? 240 THR   D C     1 
ATOM   8765  O  O     . THR   C 2  238 ? 10.449  10.348  -29.523 1.00 54.24  ? 240 THR   D O     1 
ATOM   8766  C  CB    A THR   C 2  238 ? 8.494   7.626   -29.594 0.00 49.39  ? 240 THR   D CB    1 
ATOM   8767  C  CB    B THR   C 2  238 ? 8.500   7.633   -29.614 1.00 49.09  ? 240 THR   D CB    1 
ATOM   8768  O  OG1   A THR   C 2  238 ? 7.979   6.645   -30.503 0.00 55.60  ? 240 THR   D OG1   1 
ATOM   8769  O  OG1   B THR   C 2  238 ? 8.111   6.494   -30.381 1.00 56.56  ? 240 THR   D OG1   1 
ATOM   8770  C  CG2   A THR   C 2  238 ? 7.548   8.815   -29.550 0.00 53.73  ? 240 THR   D CG2   1 
ATOM   8771  C  CG2   B THR   C 2  238 ? 7.530   8.716   -29.888 1.00 53.46  ? 240 THR   D CG2   1 
ATOM   8772  N  N     . CYS   C 2  239 ? 10.866  8.801   -27.929 1.00 55.54  ? 241 CYS   D N     1 
ATOM   8773  C  CA    A CYS   C 2  239 ? 11.350  9.829   -27.012 0.63 46.12  ? 241 CYS   D CA    1 
ATOM   8774  C  CA    B CYS   C 2  239 ? 11.405  9.765   -26.970 0.37 46.16  ? 241 CYS   D CA    1 
ATOM   8775  C  C     . CYS   C 2  239 ? 12.612  10.522  -27.511 1.00 54.42  ? 241 CYS   D C     1 
ATOM   8776  O  O     . CYS   C 2  239 ? 12.966  11.578  -26.966 1.00 49.63  ? 241 CYS   D O     1 
ATOM   8777  C  CB    A CYS   C 2  239 ? 11.579  9.240   -25.622 0.63 42.39  ? 241 CYS   D CB    1 
ATOM   8778  C  CB    B CYS   C 2  239 ? 11.782  9.054   -25.663 0.37 42.72  ? 241 CYS   D CB    1 
ATOM   8779  S  SG    A CYS   C 2  239 ? 10.033  8.964   -24.717 0.63 40.43  ? 241 CYS   D SG    1 
ATOM   8780  S  SG    B CYS   C 2  239 ? 12.902  7.612   -25.819 0.37 48.78  ? 241 CYS   D SG    1 
ATOM   8781  N  N     . LEU   C 2  240 ? 13.270  10.000  -28.560 1.00 52.14  ? 242 LEU   D N     1 
ATOM   8782  C  CA    . LEU   C 2  240 ? 14.441  10.660  -29.125 1.00 42.61  ? 242 LEU   D CA    1 
ATOM   8783  C  C     . LEU   C 2  240 ? 14.114  11.560  -30.312 1.00 42.60  ? 242 LEU   D C     1 
ATOM   8784  O  O     . LEU   C 2  240 ? 14.934  12.417  -30.652 1.00 42.22  ? 242 LEU   D O     1 
ATOM   8785  C  CB    . LEU   C 2  240 ? 15.478  9.620   -29.549 1.00 40.06  ? 242 LEU   D CB    1 
ATOM   8786  C  CG    . LEU   C 2  240 ? 15.788  8.485   -28.566 1.00 36.28  ? 242 LEU   D CG    1 
ATOM   8787  C  CD1   . LEU   C 2  240 ? 16.696  7.453   -29.217 1.00 29.76  ? 242 LEU   D CD1   1 
ATOM   8788  C  CD2   . LEU   C 2  240 ? 16.395  8.994   -27.244 1.00 33.68  ? 242 LEU   D CD2   1 
ATOM   8789  N  N     . ARG   C 2  241 ? 12.935  11.406  -30.929 1.00 52.51  ? 243 ARG   D N     1 
ATOM   8790  C  CA    . ARG   C 2  241 ? 12.584  12.077  -32.183 1.00 50.71  ? 243 ARG   D CA    1 
ATOM   8791  C  C     . ARG   C 2  241 ? 11.478  13.112  -32.033 1.00 53.81  ? 243 ARG   D C     1 
ATOM   8792  O  O     . ARG   C 2  241 ? 11.285  13.930  -32.944 1.00 53.02  ? 243 ARG   D O     1 
ATOM   8793  C  CB    . ARG   C 2  241 ? 12.166  11.039  -33.240 1.00 40.56  ? 243 ARG   D CB    1 
ATOM   8794  C  CG    . ARG   C 2  241 ? 13.152  9.865   -33.321 1.00 56.84  ? 243 ARG   D CG    1 
ATOM   8795  C  CD    . ARG   C 2  241 ? 12.830  8.832   -34.407 1.00 56.15  ? 243 ARG   D CD    1 
ATOM   8796  N  NE    . ARG   C 2  241 ? 11.736  7.930   -34.056 1.00 48.74  ? 243 ARG   D NE    1 
ATOM   8797  C  CZ    . ARG   C 2  241 ? 10.495  8.061   -34.505 1.00 51.51  ? 243 ARG   D CZ    1 
ATOM   8798  N  NH1   . ARG   C 2  241 ? 10.160  9.044   -35.325 1.00 44.59  ? 243 ARG   D NH1   1 
ATOM   8799  N  NH2   . ARG   C 2  241 ? 9.568   7.182   -34.127 1.00 49.11  ? 243 ARG   D NH2   1 
ATOM   8800  N  N     . PHE   C 2  242 ? 10.754  13.099  -30.918 1.00 55.38  ? 244 PHE   D N     1 
ATOM   8801  C  CA    . PHE   C 2  242 ? 9.779   14.127  -30.604 1.00 56.65  ? 244 PHE   D CA    1 
ATOM   8802  C  C     . PHE   C 2  242 ? 10.094  14.756  -29.247 1.00 60.06  ? 244 PHE   D C     1 
ATOM   8803  O  O     . PHE   C 2  242 ? 10.664  14.098  -28.367 1.00 59.56  ? 244 PHE   D O     1 
ATOM   8804  C  CB    . PHE   C 2  242 ? 8.365   13.540  -30.595 1.00 61.39  ? 244 PHE   D CB    1 
ATOM   8805  C  CG    . PHE   C 2  242 ? 8.027   12.769  -31.837 1.00 56.29  ? 244 PHE   D CG    1 
ATOM   8806  C  CD1   . PHE   C 2  242 ? 7.556   13.418  -32.962 1.00 57.87  ? 244 PHE   D CD1   1 
ATOM   8807  C  CD2   . PHE   C 2  242 ? 8.192   11.400  -31.883 1.00 56.01  ? 244 PHE   D CD2   1 
ATOM   8808  C  CE1   . PHE   C 2  242 ? 7.249   12.721  -34.095 1.00 47.87  ? 244 PHE   D CE1   1 
ATOM   8809  C  CE2   . PHE   C 2  242 ? 7.883   10.697  -33.025 1.00 58.99  ? 244 PHE   D CE2   1 
ATOM   8810  C  CZ    . PHE   C 2  242 ? 7.408   11.365  -34.132 1.00 52.04  ? 244 PHE   D CZ    1 
ATOM   8811  N  N     . PRO   C 2  243 ? 9.733   16.024  -29.046 1.00 58.06  ? 245 PRO   D N     1 
ATOM   8812  C  CA    . PRO   C 2  243 ? 10.121  16.715  -27.808 1.00 59.73  ? 245 PRO   D CA    1 
ATOM   8813  C  C     . PRO   C 2  243 ? 9.478   16.075  -26.582 1.00 61.35  ? 245 PRO   D C     1 
ATOM   8814  O  O     . PRO   C 2  243 ? 8.429   15.434  -26.666 1.00 64.49  ? 245 PRO   D O     1 
ATOM   8815  C  CB    . PRO   C 2  243 ? 9.618   18.147  -28.032 1.00 54.42  ? 245 PRO   D CB    1 
ATOM   8816  C  CG    . PRO   C 2  243 ? 8.514   18.004  -29.019 1.00 57.30  ? 245 PRO   D CG    1 
ATOM   8817  C  CD    . PRO   C 2  243 ? 8.851   16.841  -29.896 1.00 56.20  ? 245 PRO   D CD    1 
ATOM   8818  N  N     . GLY   C 2  244 ? 10.126  16.236  -25.432 1.00 55.23  ? 246 GLY   D N     1 
ATOM   8819  C  CA    . GLY   C 2  244 ? 9.614   15.614  -24.225 1.00 51.17  ? 246 GLY   D CA    1 
ATOM   8820  C  C     . GLY   C 2  244 ? 10.634  15.620  -23.107 1.00 56.69  ? 246 GLY   D C     1 
ATOM   8821  O  O     . GLY   C 2  244 ? 11.823  15.888  -23.301 1.00 56.26  ? 246 GLY   D O     1 
ATOM   8822  N  N     . GLN   C 2  245 ? 10.137  15.301  -21.911 1.00 55.68  ? 247 GLN   D N     1 
ATOM   8823  C  CA    . GLN   C 2  245 ? 10.981  15.293  -20.721 1.00 55.44  ? 247 GLN   D CA    1 
ATOM   8824  C  C     . GLN   C 2  245 ? 11.763  13.994  -20.591 1.00 46.13  ? 247 GLN   D C     1 
ATOM   8825  O  O     . GLN   C 2  245 ? 12.985  14.017  -20.427 1.00 48.54  ? 247 GLN   D O     1 
ATOM   8826  C  CB    . GLN   C 2  245 ? 10.128  15.519  -19.471 1.00 58.81  ? 247 GLN   D CB    1 
ATOM   8827  C  CG    . GLN   C 2  245 ? 9.445   16.875  -19.418 1.00 45.07  ? 247 GLN   D CG    1 
ATOM   8828  C  CD    . GLN   C 2  245 ? 10.437  18.015  -19.533 1.00 54.05  ? 247 GLN   D CD    1 
ATOM   8829  O  OE1   . GLN   C 2  245 ? 10.876  18.588  -18.523 1.00 43.34  ? 247 GLN   D OE1   1 
ATOM   8830  N  NE2   . GLN   C 2  245 ? 10.809  18.346  -20.772 1.00 49.03  ? 247 GLN   D NE2   1 
ATOM   8831  N  N     . LEU   C 2  246 ? 11.078  12.855  -20.693 1.00 39.23  ? 248 LEU   D N     1 
ATOM   8832  C  CA    . LEU   C 2  246 ? 11.615  11.572  -20.249 1.00 43.17  ? 248 LEU   D CA    1 
ATOM   8833  C  C     . LEU   C 2  246 ? 12.469  10.915  -21.326 1.00 39.02  ? 248 LEU   D C     1 
ATOM   8834  O  O     . LEU   C 2  246 ? 12.023  10.741  -22.466 1.00 43.72  ? 248 LEU   D O     1 
ATOM   8835  C  CB    . LEU   C 2  246 ? 10.481  10.625  -19.838 1.00 38.77  ? 248 LEU   D CB    1 
ATOM   8836  C  CG    . LEU   C 2  246 ? 10.868  9.179   -19.505 1.00 39.42  ? 248 LEU   D CG    1 
ATOM   8837  C  CD1   . LEU   C 2  246 ? 11.643  9.077   -18.185 1.00 37.32  ? 248 LEU   D CD1   1 
ATOM   8838  C  CD2   . LEU   C 2  246 ? 9.651   8.280   -19.477 1.00 42.39  ? 248 LEU   D CD2   1 
ATOM   8839  N  N     . ASN   C 2  247 ? 13.693  10.548  -20.948 1.00 35.51  ? 249 ASN   D N     1 
ATOM   8840  C  CA    . ASN   C 2  247 ? 14.610  9.780   -21.785 1.00 35.63  ? 249 ASN   D CA    1 
ATOM   8841  C  C     . ASN   C 2  247 ? 14.705  10.331  -23.212 1.00 41.25  ? 249 ASN   D C     1 
ATOM   8842  O  O     . ASN   C 2  247 ? 14.553  9.605   -24.201 1.00 31.28  ? 249 ASN   D O     1 
ATOM   8843  C  CB    . ASN   C 2  247 ? 14.201  8.317   -21.776 1.00 39.70  ? 249 ASN   D CB    1 
ATOM   8844  C  CG    . ASN   C 2  247 ? 14.222  7.724   -20.371 1.00 48.29  ? 249 ASN   D CG    1 
ATOM   8845  O  OD1   . ASN   C 2  247 ? 15.222  7.832   -19.641 1.00 36.23  ? 249 ASN   D OD1   1 
ATOM   8846  N  ND2   . ASN   C 2  247 ? 13.113  7.102   -19.981 1.00 44.37  ? 249 ASN   D ND2   1 
ATOM   8847  N  N     . ALA   C 2  248 ? 15.011  11.632  -23.313 1.00 30.50  ? 250 ALA   D N     1 
ATOM   8848  C  CA    . ALA   C 2  248 ? 15.025  12.304  -24.599 1.00 34.33  ? 250 ALA   D CA    1 
ATOM   8849  C  C     . ALA   C 2  248 ? 16.356  12.176  -25.341 1.00 50.61  ? 250 ALA   D C     1 
ATOM   8850  O  O     . ALA   C 2  248 ? 16.435  12.582  -26.512 1.00 42.25  ? 250 ALA   D O     1 
ATOM   8851  C  CB    . ALA   C 2  248 ? 14.665  13.777  -24.434 1.00 29.94  ? 250 ALA   D CB    1 
ATOM   8852  N  N     . ASP   C 2  249 ? 17.393  11.612  -24.717 1.00 34.95  ? 251 ASP   D N     1 
ATOM   8853  C  CA    . ASP   C 2  249 ? 18.624  11.323  -25.438 1.00 35.71  ? 251 ASP   D CA    1 
ATOM   8854  C  C     . ASP   C 2  249 ? 19.200  10.003  -24.949 1.00 33.32  ? 251 ASP   D C     1 
ATOM   8855  O  O     . ASP   C 2  249 ? 18.847  9.498   -23.882 1.00 29.58  ? 251 ASP   D O     1 
ATOM   8856  C  CB    . ASP   C 2  249 ? 19.668  12.448  -25.288 1.00 29.93  ? 251 ASP   D CB    1 
ATOM   8857  C  CG    . ASP   C 2  249 ? 20.116  12.619  -23.862 1.00 37.03  ? 251 ASP   D CG    1 
ATOM   8858  O  OD1   . ASP   C 2  249 ? 20.855  11.738  -23.356 1.00 33.08  ? 251 ASP   D OD1   1 
ATOM   8859  O  OD2   . ASP   C 2  249 ? 19.707  13.619  -23.237 1.00 39.16  ? 251 ASP   D OD2   1 
ATOM   8860  N  N     . LEU   C 2  250 ? 20.129  9.472   -25.750 1.00 37.19  ? 252 LEU   D N     1 
ATOM   8861  C  CA    . LEU   C 2  250 ? 20.706  8.153   -25.508 1.00 37.24  ? 252 LEU   D CA    1 
ATOM   8862  C  C     . LEU   C 2  250 ? 21.341  7.999   -24.132 1.00 35.29  ? 252 LEU   D C     1 
ATOM   8863  O  O     . LEU   C 2  250 ? 21.481  6.861   -23.670 1.00 41.53  ? 252 LEU   D O     1 
ATOM   8864  C  CB    . LEU   C 2  250 ? 21.750  7.838   -26.584 1.00 36.50  ? 252 LEU   D CB    1 
ATOM   8865  C  CG    . LEU   C 2  250 ? 21.162  7.531   -27.962 1.00 37.52  ? 252 LEU   D CG    1 
ATOM   8866  C  CD1   . LEU   C 2  250 ? 22.243  7.616   -29.019 1.00 41.08  ? 252 LEU   D CD1   1 
ATOM   8867  C  CD2   . LEU   C 2  250 ? 20.479  6.166   -27.980 1.00 24.99  ? 252 LEU   D CD2   1 
ATOM   8868  N  N     . ARG   C 2  251 ? 21.751  9.093   -23.473 1.00 35.82  ? 253 ARG   D N     1 
ATOM   8869  C  CA    . ARG   C 2  251 ? 22.439  8.981   -22.184 1.00 42.91  ? 253 ARG   D CA    1 
ATOM   8870  C  C     . ARG   C 2  251 ? 21.515  9.148   -20.972 1.00 33.75  ? 253 ARG   D C     1 
ATOM   8871  O  O     . ARG   C 2  251 ? 21.685  8.441   -19.977 1.00 27.80  ? 253 ARG   D O     1 
ATOM   8872  C  CB    . ARG   C 2  251 ? 23.602  9.980   -22.075 1.00 27.65  ? 253 ARG   D CB    1 
ATOM   8873  C  CG    . ARG   C 2  251 ? 24.451  9.710   -20.808 1.00 26.30  ? 253 ARG   D CG    1 
ATOM   8874  C  CD    . ARG   C 2  251 ? 25.382  10.866  -20.465 1.00 25.71  ? 253 ARG   D CD    1 
ATOM   8875  N  NE    . ARG   C 2  251 ? 26.117  11.231  -21.656 1.00 38.03  ? 253 ARG   D NE    1 
ATOM   8876  C  CZ    . ARG   C 2  251 ? 27.093  10.496  -22.160 1.00 45.75  ? 253 ARG   D CZ    1 
ATOM   8877  N  NH1   . ARG   C 2  251 ? 27.608  9.481   -21.477 1.00 30.65  ? 253 ARG   D NH1   1 
ATOM   8878  N  NH2   . ARG   C 2  251 ? 27.539  10.767  -23.389 1.00 36.45  ? 253 ARG   D NH2   1 
ATOM   8879  N  N     . LYS   C 2  252 ? 20.554  10.070  -21.004 1.00 25.00  ? 254 LYS   D N     1 
ATOM   8880  C  CA    . LYS   C 2  252 ? 19.536  10.047  -19.965 1.00 28.03  ? 254 LYS   D CA    1 
ATOM   8881  C  C     . LYS   C 2  252 ? 18.816  8.706   -19.949 1.00 35.76  ? 254 LYS   D C     1 
ATOM   8882  O  O     . LYS   C 2  252 ? 18.557  8.142   -18.880 1.00 33.45  ? 254 LYS   D O     1 
ATOM   8883  C  CB    . LYS   C 2  252 ? 18.555  11.196  -20.153 1.00 30.59  ? 254 LYS   D CB    1 
ATOM   8884  C  CG    . LYS   C 2  252 ? 19.142  12.543  -19.804 1.00 23.23  ? 254 LYS   D CG    1 
ATOM   8885  C  CD    . LYS   C 2  252 ? 18.048  13.551  -19.767 1.00 22.32  ? 254 LYS   D CD    1 
ATOM   8886  C  CE    . LYS   C 2  252 ? 18.504  14.905  -19.240 1.00 22.80  ? 254 LYS   D CE    1 
ATOM   8887  N  NZ    . LYS   C 2  252 ? 17.781  15.945  -20.020 1.00 27.28  ? 254 LYS   D NZ    1 
ATOM   8888  N  N     . LEU   C 2  253 ? 18.527  8.156   -21.128 1.00 35.36  ? 255 LEU   D N     1 
ATOM   8889  C  CA    . LEU   C 2  253 ? 18.016  6.796   -21.198 1.00 34.32  ? 255 LEU   D CA    1 
ATOM   8890  C  C     . LEU   C 2  253 ? 18.933  5.811   -20.477 1.00 34.41  ? 255 LEU   D C     1 
ATOM   8891  O  O     . LEU   C 2  253 ? 18.477  4.973   -19.693 1.00 34.69  ? 255 LEU   D O     1 
ATOM   8892  C  CB    . LEU   C 2  253 ? 17.847  6.390   -22.657 1.00 45.97  ? 255 LEU   D CB    1 
ATOM   8893  C  CG    . LEU   C 2  253 ? 17.086  5.081   -22.844 1.00 43.04  ? 255 LEU   D CG    1 
ATOM   8894  C  CD1   . LEU   C 2  253 ? 15.656  5.332   -22.409 1.00 34.80  ? 255 LEU   D CD1   1 
ATOM   8895  C  CD2   . LEU   C 2  253 ? 17.176  4.605   -24.294 1.00 29.93  ? 255 LEU   D CD2   1 
ATOM   8896  N  N     . ALA   C 2  254 ? 20.236  5.882   -20.745 1.00 32.70  ? 256 ALA   D N     1 
ATOM   8897  C  CA    . ALA   C 2  254 ? 21.146  4.902   -20.163 1.00 28.96  ? 256 ALA   D CA    1 
ATOM   8898  C  C     . ALA   C 2  254 ? 21.229  5.051   -18.644 1.00 37.45  ? 256 ALA   D C     1 
ATOM   8899  O  O     . ALA   C 2  254 ? 21.278  4.048   -17.915 1.00 29.37  ? 256 ALA   D O     1 
ATOM   8900  C  CB    . ALA   C 2  254 ? 22.523  5.040   -20.810 1.00 30.03  ? 256 ALA   D CB    1 
ATOM   8901  N  N     . VAL   C 2  255 ? 21.243  6.300   -18.152 1.00 34.68  ? 257 VAL   D N     1 
ATOM   8902  C  CA    . VAL   C 2  255 ? 21.260  6.566   -16.715 1.00 31.27  ? 257 VAL   D CA    1 
ATOM   8903  C  C     . VAL   C 2  255 ? 19.965  6.126   -16.055 1.00 31.09  ? 257 VAL   D C     1 
ATOM   8904  O  O     . VAL   C 2  255 ? 19.958  5.779   -14.872 1.00 28.37  ? 257 VAL   D O     1 
ATOM   8905  C  CB    . VAL   C 2  255 ? 21.509  8.058   -16.443 1.00 34.11  ? 257 VAL   D CB    1 
ATOM   8906  C  CG1   . VAL   C 2  255 ? 21.375  8.329   -14.967 1.00 21.02  ? 257 VAL   D CG1   1 
ATOM   8907  C  CG2   . VAL   C 2  255 ? 22.874  8.469   -16.953 1.00 38.42  ? 257 VAL   D CG2   1 
ATOM   8908  N  N     . ASN   C 2  256 ? 18.850  6.145   -16.793 1.00 30.63  ? 258 ASN   D N     1 
ATOM   8909  C  CA    . ASN   C 2  256 ? 17.567  5.709   -16.248 1.00 35.51  ? 258 ASN   D CA    1 
ATOM   8910  C  C     . ASN   C 2  256 ? 17.382  4.191   -16.286 1.00 33.96  ? 258 ASN   D C     1 
ATOM   8911  O  O     . ASN   C 2  256 ? 16.664  3.637   -15.440 1.00 30.70  ? 258 ASN   D O     1 
ATOM   8912  C  CB    . ASN   C 2  256 ? 16.421  6.389   -17.006 1.00 32.65  ? 258 ASN   D CB    1 
ATOM   8913  C  CG    . ASN   C 2  256 ? 15.917  7.622   -16.308 1.00 30.58  ? 258 ASN   D CG    1 
ATOM   8914  O  OD1   . ASN   C 2  256 ? 16.170  7.819   -15.121 1.00 45.85  ? 258 ASN   D OD1   1 
ATOM   8915  N  ND2   . ASN   C 2  256 ? 15.195  8.457   -17.030 1.00 30.37  ? 258 ASN   D ND2   1 
ATOM   8916  N  N     . MET   C 2  257 ? 18.025  3.506   -17.240 1.00 33.94  ? 259 MET   D N     1 
ATOM   8917  C  CA    . MET   C 2  257 ? 17.727  2.111   -17.544 1.00 35.52  ? 259 MET   D CA    1 
ATOM   8918  C  C     . MET   C 2  257 ? 18.767  1.109   -17.075 1.00 31.75  ? 259 MET   D C     1 
ATOM   8919  O  O     . MET   C 2  257 ? 18.437  -0.070  -16.964 1.00 38.68  ? 259 MET   D O     1 
ATOM   8920  C  CB    . MET   C 2  257 ? 17.541  1.923   -19.058 1.00 34.19  ? 259 MET   D CB    1 
ATOM   8921  C  CG    . MET   C 2  257 ? 16.255  2.517   -19.577 1.00 37.59  ? 259 MET   D CG    1 
ATOM   8922  S  SD    . MET   C 2  257 ? 14.876  1.741   -18.723 1.00 42.45  ? 259 MET   D SD    1 
ATOM   8923  C  CE    . MET   C 2  257 ? 13.783  3.144   -18.568 1.00 37.57  ? 259 MET   D CE    1 
ATOM   8924  N  N     . VAL   C 2  258 ? 19.998  1.523   -16.815 1.00 33.00  ? 260 VAL   D N     1 
ATOM   8925  C  CA    . VAL   C 2  258 ? 21.103  0.603   -16.579 1.00 31.23  ? 260 VAL   D CA    1 
ATOM   8926  C  C     . VAL   C 2  258 ? 21.671  0.865   -15.192 1.00 37.44  ? 260 VAL   D C     1 
ATOM   8927  O  O     . VAL   C 2  258 ? 22.438  1.808   -14.988 1.00 30.84  ? 260 VAL   D O     1 
ATOM   8928  C  CB    . VAL   C 2  258 ? 22.193  0.741   -17.656 1.00 32.93  ? 260 VAL   D CB    1 
ATOM   8929  C  CG1   . VAL   C 2  258 ? 23.342  -0.207  -17.363 1.00 28.12  ? 260 VAL   D CG1   1 
ATOM   8930  C  CG2   . VAL   C 2  258 ? 21.597  0.492   -19.029 1.00 27.14  ? 260 VAL   D CG2   1 
ATOM   8931  N  N     . PRO   C 2  259 ? 21.315  0.040   -14.207 1.00 34.60  ? 261 PRO   D N     1 
ATOM   8932  C  CA    . PRO   C 2  259 ? 21.861  0.207   -12.855 1.00 32.88  ? 261 PRO   D CA    1 
ATOM   8933  C  C     . PRO   C 2  259 ? 23.256  -0.361  -12.672 1.00 32.60  ? 261 PRO   D C     1 
ATOM   8934  O  O     . PRO   C 2  259 ? 23.878  -0.102  -11.630 1.00 32.91  ? 261 PRO   D O     1 
ATOM   8935  C  CB    . PRO   C 2  259 ? 20.858  -0.557  -11.986 1.00 34.86  ? 261 PRO   D CB    1 
ATOM   8936  C  CG    . PRO   C 2  259 ? 20.340  -1.626  -12.910 1.00 38.73  ? 261 PRO   D CG    1 
ATOM   8937  C  CD    . PRO   C 2  259 ? 20.257  -0.979  -14.266 1.00 36.71  ? 261 PRO   D CD    1 
ATOM   8938  N  N     . PHE   C 2  260 ? 23.750  -1.156  -13.621 1.00 34.33  ? 262 PHE   D N     1 
ATOM   8939  C  CA    . PHE   C 2  260 ? 25.065  -1.784  -13.520 1.00 33.00  ? 262 PHE   D CA    1 
ATOM   8940  C  C     . PHE   C 2  260 ? 25.574  -1.893  -14.941 1.00 38.71  ? 262 PHE   D C     1 
ATOM   8941  O  O     . PHE   C 2  260 ? 24.796  -2.245  -15.844 1.00 42.99  ? 262 PHE   D O     1 
ATOM   8942  C  CB    . PHE   C 2  260 ? 25.035  -3.157  -12.846 1.00 21.88  ? 262 PHE   D CB    1 
ATOM   8943  C  CG    . PHE   C 2  260 ? 24.470  -3.113  -11.463 1.00 39.20  ? 262 PHE   D CG    1 
ATOM   8944  C  CD1   . PHE   C 2  260 ? 25.264  -2.712  -10.390 1.00 35.04  ? 262 PHE   D CD1   1 
ATOM   8945  C  CD2   . PHE   C 2  260 ? 23.128  -3.402  -11.237 1.00 41.08  ? 262 PHE   D CD2   1 
ATOM   8946  C  CE1   . PHE   C 2  260 ? 24.739  -2.631  -9.104  1.00 31.79  ? 262 PHE   D CE1   1 
ATOM   8947  C  CE2   . PHE   C 2  260 ? 22.599  -3.325  -9.959  1.00 40.76  ? 262 PHE   D CE2   1 
ATOM   8948  C  CZ    . PHE   C 2  260 ? 23.412  -2.938  -8.886  1.00 33.15  ? 262 PHE   D CZ    1 
ATOM   8949  N  N     . PRO   C 2  261 ? 26.842  -1.565  -15.175 1.00 38.07  ? 263 PRO   D N     1 
ATOM   8950  C  CA    . PRO   C 2  261 ? 27.337  -1.512  -16.559 1.00 38.02  ? 263 PRO   D CA    1 
ATOM   8951  C  C     . PRO   C 2  261 ? 26.984  -2.734  -17.402 1.00 39.23  ? 263 PRO   D C     1 
ATOM   8952  O  O     . PRO   C 2  261 ? 26.420  -2.565  -18.494 1.00 35.26  ? 263 PRO   D O     1 
ATOM   8953  C  CB    . PRO   C 2  261 ? 28.849  -1.326  -16.374 1.00 23.02  ? 263 PRO   D CB    1 
ATOM   8954  C  CG    . PRO   C 2  261 ? 29.106  -1.397  -14.903 1.00 33.31  ? 263 PRO   D CG    1 
ATOM   8955  C  CD    . PRO   C 2  261 ? 27.832  -1.062  -14.218 1.00 34.55  ? 263 PRO   D CD    1 
ATOM   8956  N  N     . ARG   C 2  262 ? 27.272  -3.954  -16.928 1.00 32.26  ? 264 ARG   D N     1 
ATOM   8957  C  CA    . ARG   C 2  262 ? 27.021  -5.137  -17.754 1.00 36.28  ? 264 ARG   D CA    1 
ATOM   8958  C  C     . ARG   C 2  262 ? 25.537  -5.306  -18.040 1.00 35.42  ? 264 ARG   D C     1 
ATOM   8959  O  O     . ARG   C 2  262 ? 25.131  -5.440  -19.196 1.00 49.33  ? 264 ARG   D O     1 
ATOM   8960  C  CB    . ARG   C 2  262 ? 27.583  -6.397  -17.091 1.00 32.27  ? 264 ARG   D CB    1 
ATOM   8961  C  CG    . ARG   C 2  262 ? 29.078  -6.462  -17.124 1.00 23.28  ? 264 ARG   D CG    1 
ATOM   8962  C  CD    . ARG   C 2  262 ? 29.648  -7.242  -15.970 1.00 36.87  ? 264 ARG   D CD    1 
ATOM   8963  N  NE    . ARG   C 2  262 ? 29.417  -8.678  -16.063 1.00 55.55  ? 264 ARG   D NE    1 
ATOM   8964  C  CZ    . ARG   C 2  262 ? 29.924  -9.464  -17.006 1.00 55.67  ? 264 ARG   D CZ    1 
ATOM   8965  N  NH1   . ARG   C 2  262 ? 30.622  -8.974  -18.019 1.00 42.60  ? 264 ARG   D NH1   1 
ATOM   8966  N  NH2   . ARG   C 2  262 ? 29.711  -10.775 -16.938 1.00 53.18  ? 264 ARG   D NH2   1 
ATOM   8967  N  N     . LEU   C 2  263 ? 24.706  -5.283  -17.006 1.00 34.75  ? 265 LEU   D N     1 
ATOM   8968  C  CA    . LEU   C 2  263 ? 23.287  -5.571  -17.192 1.00 40.23  ? 265 LEU   D CA    1 
ATOM   8969  C  C     . LEU   C 2  263 ? 22.590  -4.503  -18.017 1.00 41.76  ? 265 LEU   D C     1 
ATOM   8970  O  O     . LEU   C 2  263 ? 21.735  -3.785  -17.487 1.00 44.35  ? 265 LEU   D O     1 
ATOM   8971  C  CB    . LEU   C 2  263 ? 22.577  -5.702  -15.850 1.00 33.92  ? 265 LEU   D CB    1 
ATOM   8972  C  CG    . LEU   C 2  263 ? 23.405  -6.383  -14.775 1.00 32.76  ? 265 LEU   D CG    1 
ATOM   8973  C  CD1   . LEU   C 2  263 ? 22.574  -6.513  -13.530 1.00 39.29  ? 265 LEU   D CD1   1 
ATOM   8974  C  CD2   . LEU   C 2  263 ? 23.890  -7.741  -15.276 1.00 42.19  ? 265 LEU   D CD2   1 
ATOM   8975  N  N     . HIS   C 2  264 ? 22.919  -4.413  -19.311 1.00 40.11  ? 266 HIS   D N     1 
ATOM   8976  C  CA    . HIS   C 2  264 ? 22.361  -3.414  -20.218 1.00 41.83  ? 266 HIS   D CA    1 
ATOM   8977  C  C     . HIS   C 2  264 ? 21.608  -4.066  -21.382 1.00 48.97  ? 266 HIS   D C     1 
ATOM   8978  O  O     . HIS   C 2  264 ? 21.610  -3.561  -22.513 1.00 46.11  ? 266 HIS   D O     1 
ATOM   8979  C  CB    . HIS   C 2  264 ? 23.456  -2.481  -20.742 1.00 44.43  ? 266 HIS   D CB    1 
ATOM   8980  C  CG    . HIS   C 2  264 ? 24.512  -3.175  -21.556 1.00 49.42  ? 266 HIS   D CG    1 
ATOM   8981  N  ND1   . HIS   C 2  264 ? 25.702  -3.616  -21.016 1.00 40.65  ? 266 HIS   D ND1   1 
ATOM   8982  C  CD2   . HIS   C 2  264 ? 24.552  -3.506  -22.870 1.00 50.97  ? 266 HIS   D CD2   1 
ATOM   8983  C  CE1   . HIS   C 2  264 ? 26.425  -4.193  -21.958 1.00 43.58  ? 266 HIS   D CE1   1 
ATOM   8984  N  NE2   . HIS   C 2  264 ? 25.750  -4.141  -23.093 1.00 49.75  ? 266 HIS   D NE2   1 
ATOM   8985  N  N     . PHE   C 2  265 ? 20.928  -5.188  -21.123 1.00 54.46  ? 267 PHE   D N     1 
ATOM   8986  C  CA    . PHE   C 2  265 ? 20.211  -5.930  -22.161 1.00 46.79  ? 267 PHE   D CA    1 
ATOM   8987  C  C     . PHE   C 2  265 ? 18.721  -5.836  -21.875 1.00 43.99  ? 267 PHE   D C     1 
ATOM   8988  O  O     . PHE   C 2  265 ? 18.227  -6.422  -20.907 1.00 55.72  ? 267 PHE   D O     1 
ATOM   8989  C  CB    . PHE   C 2  265 ? 20.707  -7.373  -22.230 1.00 46.81  ? 267 PHE   D CB    1 
ATOM   8990  C  CG    . PHE   C 2  265 ? 22.155  -7.466  -22.599 1.00 43.19  ? 267 PHE   D CG    1 
ATOM   8991  C  CD1   . PHE   C 2  265 ? 22.551  -7.331  -23.916 1.00 42.63  ? 267 PHE   D CD1   1 
ATOM   8992  C  CD2   . PHE   C 2  265 ? 23.122  -7.611  -21.628 1.00 42.69  ? 267 PHE   D CD2   1 
ATOM   8993  C  CE1   . PHE   C 2  265 ? 23.874  -7.376  -24.255 1.00 44.94  ? 267 PHE   D CE1   1 
ATOM   8994  C  CE2   . PHE   C 2  265 ? 24.449  -7.653  -21.969 1.00 40.45  ? 267 PHE   D CE2   1 
ATOM   8995  C  CZ    . PHE   C 2  265 ? 24.822  -7.533  -23.278 1.00 37.77  ? 267 PHE   D CZ    1 
ATOM   8996  N  N     . PHE   C 2  266 ? 18.019  -5.068  -22.694 1.00 40.75  ? 268 PHE   D N     1 
ATOM   8997  C  CA    . PHE   C 2  266 ? 16.621  -4.758  -22.451 1.00 41.93  ? 268 PHE   D CA    1 
ATOM   8998  C  C     . PHE   C 2  266 ? 15.721  -5.763  -23.159 1.00 48.81  ? 268 PHE   D C     1 
ATOM   8999  O  O     . PHE   C 2  266 ? 16.107  -6.415  -24.132 1.00 50.41  ? 268 PHE   D O     1 
ATOM   9000  C  CB    . PHE   C 2  266 ? 16.269  -3.340  -22.926 1.00 35.36  ? 268 PHE   D CB    1 
ATOM   9001  C  CG    . PHE   C 2  266 ? 17.248  -2.279  -22.496 1.00 42.78  ? 268 PHE   D CG    1 
ATOM   9002  C  CD1   . PHE   C 2  266 ? 18.037  -2.445  -21.372 1.00 35.62  ? 268 PHE   D CD1   1 
ATOM   9003  C  CD2   . PHE   C 2  266 ? 17.372  -1.102  -23.226 1.00 44.02  ? 268 PHE   D CD2   1 
ATOM   9004  C  CE1   . PHE   C 2  266 ? 18.925  -1.468  -20.997 1.00 37.91  ? 268 PHE   D CE1   1 
ATOM   9005  C  CE2   . PHE   C 2  266 ? 18.265  -0.120  -22.848 1.00 36.84  ? 268 PHE   D CE2   1 
ATOM   9006  C  CZ    . PHE   C 2  266 ? 19.044  -0.307  -21.741 1.00 34.68  ? 268 PHE   D CZ    1 
ATOM   9007  N  N     . MET   C 2  267 ? 14.493  -5.861  -22.665 1.00 51.83  ? 269 MET   D N     1 
ATOM   9008  C  CA    . MET   C 2  267 ? 13.467  -6.696  -23.264 1.00 45.78  ? 269 MET   D CA    1 
ATOM   9009  C  C     . MET   C 2  267 ? 12.357  -5.789  -23.771 1.00 38.79  ? 269 MET   D C     1 
ATOM   9010  O  O     . MET   C 2  267 ? 11.627  -5.223  -22.951 1.00 47.62  ? 269 MET   D O     1 
ATOM   9011  C  CB    . MET   C 2  267 ? 12.946  -7.683  -22.213 1.00 50.33  ? 269 MET   D CB    1 
ATOM   9012  C  CG    . MET   C 2  267 ? 11.661  -8.425  -22.530 1.00 60.43  ? 269 MET   D CG    1 
ATOM   9013  S  SD    . MET   C 2  267 ? 11.205  -9.506  -21.141 1.00 70.12  ? 269 MET   D SD    1 
ATOM   9014  C  CE    . MET   C 2  267 ? 12.788  -10.269 -20.768 1.00 54.96  ? 269 MET   D CE    1 
ATOM   9015  N  N     . PRO   C 2  268 ? 12.204  -5.577  -25.081 1.00 43.73  ? 270 PRO   D N     1 
ATOM   9016  C  CA    . PRO   C 2  268 ? 11.188  -4.634  -25.571 1.00 40.26  ? 270 PRO   D CA    1 
ATOM   9017  C  C     . PRO   C 2  268 ? 9.800   -5.269  -25.595 1.00 45.98  ? 270 PRO   D C     1 
ATOM   9018  O  O     . PRO   C 2  268 ? 9.620   -6.474  -25.417 1.00 43.94  ? 270 PRO   D O     1 
ATOM   9019  C  CB    . PRO   C 2  268 ? 11.660  -4.276  -26.994 1.00 33.00  ? 270 PRO   D CB    1 
ATOM   9020  C  CG    . PRO   C 2  268 ? 12.812  -5.219  -27.292 1.00 37.59  ? 270 PRO   D CG    1 
ATOM   9021  C  CD    . PRO   C 2  268 ? 12.876  -6.254  -26.200 1.00 38.72  ? 270 PRO   D CD    1 
ATOM   9022  N  N     . GLY   C 2  269 ? 8.805   -4.419  -25.819 1.00 44.43  ? 271 GLY   D N     1 
ATOM   9023  C  CA    . GLY   C 2  269 ? 7.419   -4.833  -25.735 1.00 36.17  ? 271 GLY   D CA    1 
ATOM   9024  C  C     . GLY   C 2  269 ? 6.572   -3.839  -26.482 1.00 44.38  ? 271 GLY   D C     1 
ATOM   9025  O  O     . GLY   C 2  269 ? 6.945   -2.672  -26.626 1.00 52.06  ? 271 GLY   D O     1 
ATOM   9026  N  N     . PHE   C 2  270 ? 5.433   -4.308  -26.983 1.00 53.72  ? 272 PHE   D N     1 
ATOM   9027  C  CA    . PHE   C 2  270 ? 4.601   -3.486  -27.845 1.00 48.20  ? 272 PHE   D CA    1 
ATOM   9028  C  C     . PHE   C 2  270 ? 3.148   -3.936  -27.726 1.00 56.51  ? 272 PHE   D C     1 
ATOM   9029  O  O     . PHE   C 2  270 ? 2.847   -5.026  -27.225 1.00 47.23  ? 272 PHE   D O     1 
ATOM   9030  C  CB    . PHE   C 2  270 ? 5.086   -3.556  -29.299 1.00 48.83  ? 272 PHE   D CB    1 
ATOM   9031  C  CG    . PHE   C 2  270 ? 4.551   -2.455  -30.168 1.00 61.95  ? 272 PHE   D CG    1 
ATOM   9032  C  CD1   . PHE   C 2  270 ? 4.864   -1.125  -29.897 1.00 60.52  ? 272 PHE   D CD1   1 
ATOM   9033  C  CD2   . PHE   C 2  270 ? 3.741   -2.742  -31.264 1.00 61.31  ? 272 PHE   D CD2   1 
ATOM   9034  C  CE1   . PHE   C 2  270 ? 4.371   -0.085  -30.704 1.00 69.56  ? 272 PHE   D CE1   1 
ATOM   9035  C  CE2   . PHE   C 2  270 ? 3.244   -1.715  -32.076 1.00 68.28  ? 272 PHE   D CE2   1 
ATOM   9036  C  CZ    . PHE   C 2  270 ? 3.558   -0.383  -31.796 1.00 73.37  ? 272 PHE   D CZ    1 
ATOM   9037  N  N     . ALA   C 2  271 ? 2.245   -3.073  -28.203 1.00 55.95  ? 273 ALA   D N     1 
ATOM   9038  C  CA    . ALA   C 2  271 ? 0.803   -3.273  -28.151 1.00 54.58  ? 273 ALA   D CA    1 
ATOM   9039  C  C     . ALA   C 2  271 ? 0.122   -2.008  -28.651 1.00 60.34  ? 273 ALA   D C     1 
ATOM   9040  O  O     . ALA   C 2  271 ? 0.607   -0.897  -28.396 1.00 61.92  ? 273 ALA   D O     1 
ATOM   9041  C  CB    . ALA   C 2  271 ? 0.330   -3.619  -26.735 1.00 57.69  ? 273 ALA   D CB    1 
ATOM   9042  N  N     . PRO   C 2  272 ? -0.996  -2.130  -29.372 1.00 62.93  ? 274 PRO   D N     1 
ATOM   9043  C  CA    . PRO   C 2  272 ? -1.683  -3.379  -29.713 1.00 59.34  ? 274 PRO   D CA    1 
ATOM   9044  C  C     . PRO   C 2  272 ? -0.829  -4.226  -30.650 1.00 61.86  ? 274 PRO   D C     1 
ATOM   9045  O  O     . PRO   C 2  272 ? -0.101  -3.686  -31.473 1.00 58.43  ? 274 PRO   D O     1 
ATOM   9046  C  CB    . PRO   C 2  272 ? -2.983  -2.888  -30.355 1.00 62.27  ? 274 PRO   D CB    1 
ATOM   9047  C  CG    . PRO   C 2  272 ? -2.624  -1.560  -30.962 1.00 70.03  ? 274 PRO   D CG    1 
ATOM   9048  C  CD    . PRO   C 2  272 ? -1.607  -0.959  -30.031 1.00 63.02  ? 274 PRO   D CD    1 
ATOM   9049  N  N     . LEU   C 2  273 ? -0.906  -5.552  -30.516 1.00 63.76  ? 275 LEU   D N     1 
ATOM   9050  C  CA    . LEU   C 2  273 ? -0.100  -6.503  -31.283 1.00 63.07  ? 275 LEU   D CA    1 
ATOM   9051  C  C     . LEU   C 2  273 ? -0.868  -6.927  -32.531 1.00 73.41  ? 275 LEU   D C     1 
ATOM   9052  O  O     . LEU   C 2  273 ? -1.744  -7.795  -32.466 1.00 81.65  ? 275 LEU   D O     1 
ATOM   9053  C  CB    . LEU   C 2  273 ? 0.226   -7.721  -30.425 1.00 64.78  ? 275 LEU   D CB    1 
ATOM   9054  C  CG    . LEU   C 2  273 ? 1.667   -8.091  -30.105 1.00 66.86  ? 275 LEU   D CG    1 
ATOM   9055  C  CD1   . LEU   C 2  273 ? 1.712   -9.470  -29.421 1.00 65.59  ? 275 LEU   D CD1   1 
ATOM   9056  C  CD2   . LEU   C 2  273 ? 2.520   -8.055  -31.366 1.00 66.40  ? 275 LEU   D CD2   1 
ATOM   9057  N  N     . THR   C 2  274 ? -0.548  -6.319  -33.673 1.00 76.47  ? 276 THR   D N     1 
ATOM   9058  C  CA    . THR   C 2  274 ? -1.052  -6.790  -34.968 1.00 76.67  ? 276 THR   D CA    1 
ATOM   9059  C  C     . THR   C 2  274 ? -0.019  -6.524  -36.059 1.00 82.38  ? 276 THR   D C     1 
ATOM   9060  O  O     . THR   C 2  274 ? 0.778   -7.403  -36.401 1.00 85.30  ? 276 THR   D O     1 
ATOM   9061  C  CB    . THR   C 2  274 ? -2.394  -6.129  -35.369 1.00 68.21  ? 276 THR   D CB    1 
ATOM   9062  O  OG1   . THR   C 2  274 ? -2.288  -4.706  -35.257 1.00 64.30  ? 276 THR   D OG1   1 
ATOM   9063  C  CG2   . THR   C 2  274 ? -3.542  -6.642  -34.499 1.00 58.28  ? 276 THR   D CG2   1 
ATOM   9064  N  N     . ARG   C 2  282 ? -8.671  -3.357  -34.350 1.00 109.29 ? 284 ARG   D N     1 
ATOM   9065  C  CA    . ARG   C 2  282 ? -9.659  -2.963  -33.345 1.00 128.52 ? 284 ARG   D CA    1 
ATOM   9066  C  C     . ARG   C 2  282 ? -8.998  -2.295  -32.119 1.00 128.33 ? 284 ARG   D C     1 
ATOM   9067  O  O     . ARG   C 2  282 ? -8.141  -2.894  -31.465 1.00 123.23 ? 284 ARG   D O     1 
ATOM   9068  C  CB    . ARG   C 2  282 ? -10.485 -4.184  -32.931 1.00 122.19 ? 284 ARG   D CB    1 
ATOM   9069  C  CG    . ARG   C 2  282 ? -11.339 -4.752  -34.061 1.00 113.31 ? 284 ARG   D CG    1 
ATOM   9070  C  CD    . ARG   C 2  282 ? -12.275 -3.683  -34.591 1.00 116.27 ? 284 ARG   D CD    1 
ATOM   9071  N  NE    . ARG   C 2  282 ? -12.917 -2.972  -33.493 1.00 127.39 ? 284 ARG   D NE    1 
ATOM   9072  C  CZ    . ARG   C 2  282 ? -13.488 -1.779  -33.591 1.00 135.12 ? 284 ARG   D CZ    1 
ATOM   9073  N  NH1   . ARG   C 2  282 ? -13.536 -1.124  -34.742 1.00 116.89 ? 284 ARG   D NH1   1 
ATOM   9074  N  NH2   . ARG   C 2  282 ? -14.019 -1.224  -32.503 1.00 138.35 ? 284 ARG   D NH2   1 
ATOM   9075  N  N     . ALA   C 2  283 ? -9.407  -1.060  -31.814 1.00 120.36 ? 285 ALA   D N     1 
ATOM   9076  C  CA    . ALA   C 2  283 ? -8.690  -0.215  -30.862 1.00 114.66 ? 285 ALA   D CA    1 
ATOM   9077  C  C     . ALA   C 2  283 ? -9.085  -0.518  -29.416 1.00 114.77 ? 285 ALA   D C     1 
ATOM   9078  O  O     . ALA   C 2  283 ? -10.242 -0.830  -29.115 1.00 109.06 ? 285 ALA   D O     1 
ATOM   9079  C  CB    . ALA   C 2  283 ? -8.940  1.262   -31.170 1.00 105.55 ? 285 ALA   D CB    1 
ATOM   9080  N  N     . LEU   C 2  284 ? -8.107  -0.393  -28.514 1.00 109.12 ? 286 LEU   D N     1 
ATOM   9081  C  CA    . LEU   C 2  284 ? -8.215  -0.838  -27.125 1.00 94.63  ? 286 LEU   D CA    1 
ATOM   9082  C  C     . LEU   C 2  284 ? -8.049  0.338   -26.161 1.00 84.23  ? 286 LEU   D C     1 
ATOM   9083  O  O     . LEU   C 2  284 ? -7.786  1.473   -26.565 1.00 82.17  ? 286 LEU   D O     1 
ATOM   9084  C  CB    . LEU   C 2  284 ? -7.198  -1.945  -26.825 1.00 84.64  ? 286 LEU   D CB    1 
ATOM   9085  C  CG    . LEU   C 2  284 ? -5.708  -1.803  -27.153 1.00 79.86  ? 286 LEU   D CG    1 
ATOM   9086  C  CD1   . LEU   C 2  284 ? -4.958  -3.089  -26.745 1.00 54.80  ? 286 LEU   D CD1   1 
ATOM   9087  C  CD2   . LEU   C 2  284 ? -5.475  -1.477  -28.634 1.00 74.54  ? 286 LEU   D CD2   1 
ATOM   9088  N  N     . THR   C 2  285 ? -8.224  0.048   -24.870 1.00 82.09  ? 287 THR   D N     1 
ATOM   9089  C  CA    . THR   C 2  285 ? -8.275  1.053   -23.814 1.00 85.92  ? 287 THR   D CA    1 
ATOM   9090  C  C     . THR   C 2  285 ? -6.947  1.161   -23.082 1.00 70.47  ? 287 THR   D C     1 
ATOM   9091  O  O     . THR   C 2  285 ? -6.110  0.253   -23.117 1.00 66.98  ? 287 THR   D O     1 
ATOM   9092  C  CB    . THR   C 2  285 ? -9.368  0.739   -22.783 1.00 77.55  ? 287 THR   D CB    1 
ATOM   9093  O  OG1   . THR   C 2  285 ? -9.596  -0.677  -22.734 1.00 79.24  ? 287 THR   D OG1   1 
ATOM   9094  C  CG2   . THR   C 2  285 ? -10.660 1.490   -23.096 1.00 59.96  ? 287 THR   D CG2   1 
ATOM   9095  N  N     . VAL   C 2  286 ? -6.788  2.285   -22.371 1.00 62.87  ? 288 VAL   D N     1 
ATOM   9096  C  CA    . VAL   C 2  286 ? -5.538  2.531   -21.651 1.00 61.02  ? 288 VAL   D CA    1 
ATOM   9097  C  C     . VAL   C 2  286 ? -5.251  1.413   -20.666 1.00 59.34  ? 288 VAL   D C     1 
ATOM   9098  O  O     . VAL   C 2  286 ? -4.087  0.994   -20.556 1.00 58.51  ? 288 VAL   D O     1 
ATOM   9099  C  CB    . VAL   C 2  286 ? -5.562  3.922   -21.003 1.00 54.91  ? 288 VAL   D CB    1 
ATOM   9100  C  CG1   . VAL   C 2  286 ? -4.358  4.078   -20.072 1.00 46.24  ? 288 VAL   D CG1   1 
ATOM   9101  C  CG2   . VAL   C 2  286 ? -5.598  5.030   -22.082 1.00 37.06  ? 288 VAL   D CG2   1 
ATOM   9102  N  N     . PRO   C 2  287 ? -6.225  0.892   -19.920 1.00 58.85  ? 289 PRO   D N     1 
ATOM   9103  C  CA    . PRO   C 2  287 ? -5.959  -0.317  -19.127 1.00 52.11  ? 289 PRO   D CA    1 
ATOM   9104  C  C     . PRO   C 2  287 ? -5.461  -1.495  -19.952 1.00 67.11  ? 289 PRO   D C     1 
ATOM   9105  O  O     . PRO   C 2  287 ? -4.623  -2.265  -19.464 1.00 72.76  ? 289 PRO   D O     1 
ATOM   9106  C  CB    . PRO   C 2  287 ? -7.317  -0.596  -18.480 1.00 45.70  ? 289 PRO   D CB    1 
ATOM   9107  C  CG    . PRO   C 2  287 ? -7.920  0.786   -18.327 1.00 56.38  ? 289 PRO   D CG    1 
ATOM   9108  C  CD    . PRO   C 2  287 ? -7.492  1.546   -19.540 1.00 58.78  ? 289 PRO   D CD    1 
ATOM   9109  N  N     . GLU   C 2  288 ? -5.946  -1.667  -21.186 1.00 72.56  ? 290 GLU   D N     1 
ATOM   9110  C  CA    . GLU   C 2  288 ? -5.531  -2.819  -21.988 1.00 72.08  ? 290 GLU   D CA    1 
ATOM   9111  C  C     . GLU   C 2  288 ? -4.114  -2.643  -22.518 1.00 70.83  ? 290 GLU   D C     1 
ATOM   9112  O  O     . GLU   C 2  288 ? -3.274  -3.548  -22.402 1.00 68.38  ? 290 GLU   D O     1 
ATOM   9113  C  CB    . GLU   C 2  288 ? -6.505  -3.038  -23.139 1.00 73.49  ? 290 GLU   D CB    1 
ATOM   9114  C  CG    . GLU   C 2  288 ? -7.720  -3.862  -22.792 1.00 72.10  ? 290 GLU   D CG    1 
ATOM   9115  C  CD    . GLU   C 2  288 ? -8.842  -3.670  -23.806 1.00 83.33  ? 290 GLU   D CD    1 
ATOM   9116  O  OE1   . GLU   C 2  288 ? -8.979  -2.544  -24.335 1.00 79.07  ? 290 GLU   D OE1   1 
ATOM   9117  O  OE2   . GLU   C 2  288 ? -9.581  -4.641  -24.083 1.00 80.52  ? 290 GLU   D OE2   1 
ATOM   9118  N  N     . LEU   C 2  289 ? -3.834  -1.490  -23.128 1.00 68.89  ? 291 LEU   D N     1 
ATOM   9119  C  CA    . LEU   C 2  289 ? -2.458  -1.180  -23.491 1.00 62.90  ? 291 LEU   D CA    1 
ATOM   9120  C  C     . LEU   C 2  289 ? -1.523  -1.468  -22.332 1.00 67.73  ? 291 LEU   D C     1 
ATOM   9121  O  O     . LEU   C 2  289 ? -0.403  -1.954  -22.529 1.00 80.01  ? 291 LEU   D O     1 
ATOM   9122  C  CB    . LEU   C 2  289 ? -2.333  0.284   -23.900 1.00 54.80  ? 291 LEU   D CB    1 
ATOM   9123  C  CG    . LEU   C 2  289 ? -2.947  0.696   -25.229 1.00 62.70  ? 291 LEU   D CG    1 
ATOM   9124  C  CD1   . LEU   C 2  289 ? -2.876  2.207   -25.383 1.00 53.20  ? 291 LEU   D CD1   1 
ATOM   9125  C  CD2   . LEU   C 2  289 ? -2.224  -0.010  -26.369 1.00 61.25  ? 291 LEU   D CD2   1 
ATOM   9126  N  N     . THR   C 2  290 ? -1.982  -1.202  -21.109 1.00 61.31  ? 292 THR   D N     1 
ATOM   9127  C  CA    . THR   C 2  290 ? -1.082  -1.183  -19.964 1.00 62.97  ? 292 THR   D CA    1 
ATOM   9128  C  C     . THR   C 2  290 ? -0.799  -2.583  -19.441 1.00 60.55  ? 292 THR   D C     1 
ATOM   9129  O  O     . THR   C 2  290 ? 0.364   -2.941  -19.226 1.00 59.28  ? 292 THR   D O     1 
ATOM   9130  C  CB    . THR   C 2  290 ? -1.656  -0.299  -18.858 1.00 54.74  ? 292 THR   D CB    1 
ATOM   9131  O  OG1   . THR   C 2  290 ? -1.597  1.070   -19.270 1.00 49.49  ? 292 THR   D OG1   1 
ATOM   9132  C  CG2   . THR   C 2  290 ? -0.838  -0.450  -17.617 1.00 54.64  ? 292 THR   D CG2   1 
ATOM   9133  N  N     . GLN   C 2  291 ? -1.842  -3.386  -19.215 1.00 67.90  ? 293 GLN   D N     1 
ATOM   9134  C  CA    . GLN   C 2  291 ? -1.612  -4.745  -18.733 1.00 69.62  ? 293 GLN   D CA    1 
ATOM   9135  C  C     . GLN   C 2  291 ? -1.099  -5.653  -19.841 1.00 70.02  ? 293 GLN   D C     1 
ATOM   9136  O  O     . GLN   C 2  291 ? -0.418  -6.645  -19.556 1.00 56.81  ? 293 GLN   D O     1 
ATOM   9137  C  CB    . GLN   C 2  291 ? -2.887  -5.333  -18.127 1.00 73.82  ? 293 GLN   D CB    1 
ATOM   9138  C  CG    . GLN   C 2  291 ? -3.621  -6.286  -19.055 1.00 76.51  ? 293 GLN   D CG    1 
ATOM   9139  C  CD    . GLN   C 2  291 ? -4.974  -6.695  -18.511 1.00 91.62  ? 293 GLN   D CD    1 
ATOM   9140  O  OE1   . GLN   C 2  291 ? -5.074  -7.264  -17.416 1.00 71.25  ? 293 GLN   D OE1   1 
ATOM   9141  N  NE2   . GLN   C 2  291 ? -6.031  -6.401  -19.273 1.00 90.12  ? 293 GLN   D NE2   1 
ATOM   9142  N  N     . GLN   C 2  292 ? -1.400  -5.329  -21.103 1.00 69.36  ? 294 GLN   D N     1 
ATOM   9143  C  CA    . GLN   C 2  292 ? -0.883  -6.133  -22.204 1.00 67.48  ? 294 GLN   D CA    1 
ATOM   9144  C  C     . GLN   C 2  292 ? 0.636   -6.008  -22.315 1.00 75.42  ? 294 GLN   D C     1 
ATOM   9145  O  O     . GLN   C 2  292 ? 1.340   -7.014  -22.494 1.00 63.95  ? 294 GLN   D O     1 
ATOM   9146  C  CB    . GLN   C 2  292 ? -1.558  -5.719  -23.504 1.00 66.32  ? 294 GLN   D CB    1 
ATOM   9147  C  CG    . GLN   C 2  292 ? -2.214  -6.862  -24.258 1.00 71.77  ? 294 GLN   D CG    1 
ATOM   9148  C  CD    . GLN   C 2  292 ? -2.848  -6.396  -25.564 1.00 83.57  ? 294 GLN   D CD    1 
ATOM   9149  O  OE1   . GLN   C 2  292 ? -3.511  -5.352  -25.613 1.00 79.18  ? 294 GLN   D OE1   1 
ATOM   9150  N  NE2   . GLN   C 2  292 ? -2.627  -7.157  -26.634 1.00 72.73  ? 294 GLN   D NE2   1 
ATOM   9151  N  N     . MET   C 2  293 ? 1.165   -4.786  -22.189 1.00 70.84  ? 295 MET   D N     1 
ATOM   9152  C  CA    . MET   C 2  293 ? 2.600   -4.592  -22.363 1.00 67.69  ? 295 MET   D CA    1 
ATOM   9153  C  C     . MET   C 2  293 ? 3.425   -5.158  -21.209 1.00 67.78  ? 295 MET   D C     1 
ATOM   9154  O  O     . MET   C 2  293 ? 4.654   -5.201  -21.326 1.00 79.88  ? 295 MET   D O     1 
ATOM   9155  C  CB    . MET   C 2  293 ? 2.920   -3.106  -22.581 1.00 61.92  ? 295 MET   D CB    1 
ATOM   9156  C  CG    . MET   C 2  293 ? 2.873   -2.231  -21.336 1.00 71.49  ? 295 MET   D CG    1 
ATOM   9157  S  SD    . MET   C 2  293 ? 3.016   -0.469  -21.722 1.00 69.64  ? 295 MET   D SD    1 
ATOM   9158  C  CE    . MET   C 2  293 ? 4.601   -0.430  -22.523 1.00 53.10  ? 295 MET   D CE    1 
ATOM   9159  N  N     . PHE   C 2  294 ? 2.802   -5.600  -20.115 1.00 57.64  ? 296 PHE   D N     1 
ATOM   9160  C  CA    . PHE   C 2  294 ? 3.476   -6.410  -19.102 1.00 65.17  ? 296 PHE   D CA    1 
ATOM   9161  C  C     . PHE   C 2  294 ? 3.139   -7.894  -19.250 1.00 75.18  ? 296 PHE   D C     1 
ATOM   9162  O  O     . PHE   C 2  294 ? 3.177   -8.659  -18.271 1.00 65.88  ? 296 PHE   D O     1 
ATOM   9163  C  CB    . PHE   C 2  294 ? 3.124   -5.927  -17.695 1.00 62.82  ? 296 PHE   D CB    1 
ATOM   9164  C  CG    . PHE   C 2  294 ? 3.620   -4.551  -17.379 1.00 60.48  ? 296 PHE   D CG    1 
ATOM   9165  C  CD1   . PHE   C 2  294 ? 2.955   -3.437  -17.846 1.00 59.35  ? 296 PHE   D CD1   1 
ATOM   9166  C  CD2   . PHE   C 2  294 ? 4.747   -4.371  -16.603 1.00 58.11  ? 296 PHE   D CD2   1 
ATOM   9167  C  CE1   . PHE   C 2  294 ? 3.407   -2.177  -17.550 1.00 48.43  ? 296 PHE   D CE1   1 
ATOM   9168  C  CE2   . PHE   C 2  294 ? 5.197   -3.112  -16.308 1.00 48.79  ? 296 PHE   D CE2   1 
ATOM   9169  C  CZ    . PHE   C 2  294 ? 4.524   -2.016  -16.783 1.00 43.01  ? 296 PHE   D CZ    1 
ATOM   9170  N  N     . ASP   C 2  295 ? 2.794   -8.307  -20.467 1.00 77.97  ? 297 ASP   D N     1 
ATOM   9171  C  CA    . ASP   C 2  295 ? 2.337   -9.656  -20.764 1.00 73.66  ? 297 ASP   D CA    1 
ATOM   9172  C  C     . ASP   C 2  295 ? 3.435   -10.394 -21.511 1.00 69.95  ? 297 ASP   D C     1 
ATOM   9173  O  O     . ASP   C 2  295 ? 3.963   -9.885  -22.508 1.00 69.94  ? 297 ASP   D O     1 
ATOM   9174  C  CB    . ASP   C 2  295 ? 1.057   -9.610  -21.602 1.00 68.78  ? 297 ASP   D CB    1 
ATOM   9175  C  CG    . ASP   C 2  295 ? 0.458   -10.980 -21.836 1.00 78.56  ? 297 ASP   D CG    1 
ATOM   9176  O  OD1   . ASP   C 2  295 ? 0.843   -11.943 -21.124 1.00 71.61  ? 297 ASP   D OD1   1 
ATOM   9177  O  OD2   . ASP   C 2  295 ? -0.399  -11.082 -22.743 1.00 68.45  ? 297 ASP   D OD2   1 
ATOM   9178  N  N     . SER   C 2  296 ? 3.777   -11.591 -21.037 1.00 58.86  ? 298 SER   D N     1 
ATOM   9179  C  CA    . SER   C 2  296 ? 4.822   -12.351 -21.708 1.00 58.67  ? 298 SER   D CA    1 
ATOM   9180  C  C     . SER   C 2  296 ? 4.574   -12.450 -23.208 1.00 55.01  ? 298 SER   D C     1 
ATOM   9181  O  O     . SER   C 2  296 ? 5.523   -12.469 -23.996 1.00 55.06  ? 298 SER   D O     1 
ATOM   9182  C  CB    . SER   C 2  296 ? 4.936   -13.741 -21.089 1.00 45.76  ? 298 SER   D CB    1 
ATOM   9183  O  OG    . SER   C 2  296 ? 6.249   -14.245 -21.242 0.69 57.12  ? 298 SER   D OG    1 
ATOM   9184  N  N     . LYS   C 2  297 ? 3.319   -12.486 -23.625 1.00 56.56  ? 299 LYS   D N     1 
ATOM   9185  C  CA    . LYS   C 2  297 ? 2.981   -12.653 -25.032 1.00 64.62  ? 299 LYS   D CA    1 
ATOM   9186  C  C     . LYS   C 2  297 ? 3.043   -11.346 -25.828 1.00 73.32  ? 299 LYS   D C     1 
ATOM   9187  O  O     . LYS   C 2  297 ? 2.688   -11.348 -27.018 1.00 77.80  ? 299 LYS   D O     1 
ATOM   9188  C  CB    . LYS   C 2  297 ? 1.592   -13.288 -25.168 1.00 71.48  ? 299 LYS   D CB    1 
ATOM   9189  C  CG    . LYS   C 2  297 ? 1.499   -14.718 -24.613 1.00 69.90  ? 299 LYS   D CG    1 
ATOM   9190  C  CD    . LYS   C 2  297 ? 0.053   -15.157 -24.394 1.00 68.67  ? 299 LYS   D CD    1 
ATOM   9191  C  CE    . LYS   C 2  297 ? -0.661  -14.222 -23.421 1.00 69.73  ? 299 LYS   D CE    1 
ATOM   9192  N  NZ    . LYS   C 2  297 ? -2.029  -14.689 -23.093 1.00 60.99  ? 299 LYS   D NZ    1 
ATOM   9193  N  N     . ASN   C 2  298 ? 3.476   -10.237 -25.223 1.00 63.46  ? 300 ASN   D N     1 
ATOM   9194  C  CA    . ASN   C 2  298 ? 3.769   -9.032  -25.989 1.00 48.02  ? 300 ASN   D CA    1 
ATOM   9195  C  C     . ASN   C 2  298 ? 5.239   -8.650  -25.930 1.00 49.83  ? 300 ASN   D C     1 
ATOM   9196  O  O     . ASN   C 2  298 ? 5.604   -7.581  -26.435 1.00 49.25  ? 300 ASN   D O     1 
ATOM   9197  C  CB    . ASN   C 2  298 ? 2.913   -7.865  -25.523 1.00 45.82  ? 300 ASN   D CB    1 
ATOM   9198  C  CG    . ASN   C 2  298 ? 1.483   -8.030  -25.893 1.00 52.21  ? 300 ASN   D CG    1 
ATOM   9199  O  OD1   . ASN   C 2  298 ? 0.825   -8.950  -25.431 1.00 62.09  ? 300 ASN   D OD1   1 
ATOM   9200  N  ND2   . ASN   C 2  298 ? 0.973   -7.128  -26.714 1.00 58.30  ? 300 ASN   D ND2   1 
ATOM   9201  N  N     . MET   C 2  299 ? 6.091   -9.501  -25.353 1.00 48.72  ? 301 MET   D N     1 
ATOM   9202  C  CA    . MET   C 2  299 ? 7.526   -9.240  -25.278 1.00 54.65  ? 301 MET   D CA    1 
ATOM   9203  C  C     . MET   C 2  299 ? 8.238   -9.625  -26.580 1.00 64.89  ? 301 MET   D C     1 
ATOM   9204  O  O     . MET   C 2  299 ? 7.978   -10.685 -27.160 1.00 65.33  ? 301 MET   D O     1 
ATOM   9205  C  CB    . MET   C 2  299 ? 8.144   -10.011 -24.108 1.00 58.15  ? 301 MET   D CB    1 
ATOM   9206  C  CG    . MET   C 2  299 ? 7.529   -9.728  -22.720 1.00 60.13  ? 301 MET   D CG    1 
ATOM   9207  S  SD    . MET   C 2  299 ? 8.058   -8.182  -21.933 1.00 51.85  ? 301 MET   D SD    1 
ATOM   9208  C  CE    . MET   C 2  299 ? 6.867   -7.020  -22.602 1.00 43.35  ? 301 MET   D CE    1 
ATOM   9209  N  N     . MET   C 2  300 ? 9.146   -8.750  -27.042 1.00 64.33  ? 302 MET   D N     1 
ATOM   9210  C  CA    . MET   C 2  300 ? 9.938   -9.040  -28.234 1.00 54.75  ? 302 MET   D CA    1 
ATOM   9211  C  C     . MET   C 2  300 ? 11.158  -9.875  -27.933 1.00 48.35  ? 302 MET   D C     1 
ATOM   9212  O  O     . MET   C 2  300 ? 12.027  -9.989  -28.795 1.00 56.29  ? 302 MET   D O     1 
ATOM   9213  C  CB    . MET   C 2  300 ? 10.383  -7.760  -28.931 1.00 45.24  ? 302 MET   D CB    1 
ATOM   9214  C  CG    . MET   C 2  300 ? 9.251   -6.856  -29.369 1.00 57.43  ? 302 MET   D CG    1 
ATOM   9215  S  SD    . MET   C 2  300 ? 8.004   -7.642  -30.401 1.00 63.24  ? 302 MET   D SD    1 
ATOM   9216  C  CE    . MET   C 2  300 ? 6.888   -6.238  -30.655 1.00 51.13  ? 302 MET   D CE    1 
ATOM   9217  N  N     . ALA   C 2  301 ? 11.254  -10.439 -26.739 1.00 47.02  ? 303 ALA   D N     1 
ATOM   9218  C  CA    . ALA   C 2  301 ? 12.291  -11.402 -26.420 1.00 52.64  ? 303 ALA   D CA    1 
ATOM   9219  C  C     . ALA   C 2  301 ? 11.640  -12.532 -25.643 1.00 53.57  ? 303 ALA   D C     1 
ATOM   9220  O  O     . ALA   C 2  301 ? 10.970  -12.289 -24.637 1.00 53.60  ? 303 ALA   D O     1 
ATOM   9221  C  CB    . ALA   C 2  301 ? 13.428  -10.768 -25.613 1.00 45.60  ? 303 ALA   D CB    1 
ATOM   9222  N  N     . ALA   C 2  302 ? 11.811  -13.757 -26.127 1.00 55.89  ? 304 ALA   D N     1 
ATOM   9223  C  CA    . ALA   C 2  302 ? 11.187  -14.925 -25.515 1.00 60.60  ? 304 ALA   D CA    1 
ATOM   9224  C  C     . ALA   C 2  302 ? 11.593  -15.081 -24.056 1.00 56.75  ? 304 ALA   D C     1 
ATOM   9225  O  O     . ALA   C 2  302 ? 12.408  -15.950 -23.716 1.00 51.96  ? 304 ALA   D O     1 
ATOM   9226  C  CB    . ALA   C 2  302 ? 11.543  -16.193 -26.297 1.00 71.75  ? 304 ALA   D CB    1 
ATOM   9227  N  N     . CYS   C 2  303 ? 11.021  -14.245 -23.191 1.00 64.14  ? 305 CYS   D N     1 
ATOM   9228  C  CA    . CYS   C 2  303 ? 11.256  -14.300 -21.757 1.00 50.45  ? 305 CYS   D CA    1 
ATOM   9229  C  C     . CYS   C 2  303 ? 9.948   -14.025 -21.040 1.00 51.69  ? 305 CYS   D C     1 
ATOM   9230  O  O     . CYS   C 2  303 ? 9.098   -13.275 -21.529 1.00 52.41  ? 305 CYS   D O     1 
ATOM   9231  C  CB    . CYS   C 2  303 ? 12.320  -13.293 -21.316 1.00 56.76  ? 305 CYS   D CB    1 
ATOM   9232  S  SG    . CYS   C 2  303 ? 14.002  -13.705 -21.849 1.00 65.02  ? 305 CYS   D SG    1 
ATOM   9233  N  N     . ASP   C 2  304 ? 9.782   -14.664 -19.886 1.00 56.37  ? 306 ASP   D N     1 
ATOM   9234  C  CA    . ASP   C 2  304 ? 8.612   -14.425 -19.055 1.00 59.58  ? 306 ASP   D CA    1 
ATOM   9235  C  C     . ASP   C 2  304 ? 9.024   -13.508 -17.915 1.00 62.87  ? 306 ASP   D C     1 
ATOM   9236  O  O     . ASP   C 2  304 ? 9.816   -13.926 -17.045 1.00 56.01  ? 306 ASP   D O     1 
ATOM   9237  C  CB    . ASP   C 2  304 ? 8.039   -15.739 -18.513 1.00 56.99  ? 306 ASP   D CB    1 
ATOM   9238  C  CG    . ASP   C 2  304 ? 6.650   -15.574 -17.872 1.00 63.99  ? 306 ASP   D CG    1 
ATOM   9239  O  OD1   . ASP   C 2  304 ? 6.025   -14.482 -17.977 1.00 56.34  ? 306 ASP   D OD1   1 
ATOM   9240  O  OD2   . ASP   C 2  304 ? 6.183   -16.562 -17.259 1.00 68.52  ? 306 ASP   D OD2   1 
ATOM   9241  N  N     . PRO   C 2  305 ? 8.551   -12.260 -17.885 1.00 54.79  ? 307 PRO   D N     1 
ATOM   9242  C  CA    . PRO   C 2  305 ? 8.909   -11.371 -16.765 1.00 45.37  ? 307 PRO   D CA    1 
ATOM   9243  C  C     . PRO   C 2  305 ? 8.545   -11.942 -15.407 1.00 54.52  ? 307 PRO   D C     1 
ATOM   9244  O  O     . PRO   C 2  305 ? 9.248   -11.679 -14.421 1.00 55.16  ? 307 PRO   D O     1 
ATOM   9245  C  CB    . PRO   C 2  305 ? 8.135   -10.088 -17.069 1.00 38.46  ? 307 PRO   D CB    1 
ATOM   9246  C  CG    . PRO   C 2  305 ? 7.165   -10.449 -18.206 1.00 47.93  ? 307 PRO   D CG    1 
ATOM   9247  C  CD    . PRO   C 2  305 ? 7.740   -11.600 -18.920 1.00 45.48  ? 307 PRO   D CD    1 
ATOM   9248  N  N     . ARG   C 2  306 ? 7.487   -12.748 -15.327 1.00 52.24  ? 308 ARG   D N     1 
ATOM   9249  C  CA    . ARG   C 2  306 ? 7.101   -13.333 -14.051 1.00 45.80  ? 308 ARG   D CA    1 
ATOM   9250  C  C     . ARG   C 2  306 ? 8.096   -14.365 -13.549 1.00 54.21  ? 308 ARG   D C     1 
ATOM   9251  O  O     . ARG   C 2  306 ? 7.846   -14.980 -12.506 1.00 53.06  ? 308 ARG   D O     1 
ATOM   9252  C  CB    . ARG   C 2  306 ? 5.710   -13.949 -14.173 1.00 50.15  ? 308 ARG   D CB    1 
ATOM   9253  C  CG    . ARG   C 2  306 ? 4.646   -12.921 -14.444 1.00 51.03  ? 308 ARG   D CG    1 
ATOM   9254  C  CD    . ARG   C 2  306 ? 3.415   -13.503 -15.106 1.00 61.38  ? 308 ARG   D CD    1 
ATOM   9255  N  NE    . ARG   C 2  306 ? 2.218   -12.831 -14.611 1.00 68.83  ? 308 ARG   D NE    1 
ATOM   9256  C  CZ    . ARG   C 2  306 ? 2.021   -11.518 -14.646 1.00 73.73  ? 308 ARG   D CZ    1 
ATOM   9257  N  NH1   . ARG   C 2  306 ? 2.895   -10.696 -15.213 1.00 56.04  ? 308 ARG   D NH1   1 
ATOM   9258  N  NH2   . ARG   C 2  306 ? 0.923   -11.015 -14.086 1.00 81.99  ? 308 ARG   D NH2   1 
ATOM   9259  N  N     . HIS   C 2  307 ? 9.206   -14.585 -14.253 1.00 51.72  ? 309 HIS   D N     1 
ATOM   9260  C  CA    . HIS   C 2  307 ? 10.253  -15.458 -13.748 1.00 47.97  ? 309 HIS   D CA    1 
ATOM   9261  C  C     . HIS   C 2  307 ? 11.418  -14.680 -13.168 1.00 48.95  ? 309 HIS   D C     1 
ATOM   9262  O  O     . HIS   C 2  307 ? 12.302  -15.277 -12.545 1.00 52.27  ? 309 HIS   D O     1 
ATOM   9263  C  CB    . HIS   C 2  307 ? 10.750  -16.398 -14.857 1.00 59.06  ? 309 HIS   D CB    1 
ATOM   9264  C  CG    . HIS   C 2  307 ? 9.721   -17.392 -15.315 1.00 63.63  ? 309 HIS   D CG    1 
ATOM   9265  N  ND1   . HIS   C 2  307 ? 9.489   -17.669 -16.646 1.00 49.57  ? 309 HIS   D ND1   1 
ATOM   9266  C  CD2   . HIS   C 2  307 ? 8.861   -18.170 -14.615 1.00 65.55  ? 309 HIS   D CD2   1 
ATOM   9267  C  CE1   . HIS   C 2  307 ? 8.527   -18.569 -16.744 1.00 59.79  ? 309 HIS   D CE1   1 
ATOM   9268  N  NE2   . HIS   C 2  307 ? 8.130   -18.893 -15.526 1.00 62.19  ? 309 HIS   D NE2   1 
ATOM   9269  N  N     . GLY   C 2  308 ? 11.437  -13.369 -13.348 1.00 53.65  ? 310 GLY   D N     1 
ATOM   9270  C  CA    . GLY   C 2  308 ? 12.440  -12.547 -12.705 1.00 56.38  ? 310 GLY   D CA    1 
ATOM   9271  C  C     . GLY   C 2  308 ? 11.851  -11.259 -12.175 1.00 55.28  ? 310 GLY   D C     1 
ATOM   9272  O  O     . GLY   C 2  308 ? 10.631  -11.135 -12.015 1.00 54.22  ? 310 GLY   D O     1 
ATOM   9273  N  N     . ARG   C 2  309 ? 12.707  -10.281 -11.917 1.00 52.10  ? 311 ARG   D N     1 
ATOM   9274  C  CA    . ARG   C 2  309 ? 12.253  -8.994  -11.429 1.00 46.35  ? 311 ARG   D CA    1 
ATOM   9275  C  C     . ARG   C 2  309 ? 12.774  -7.887  -12.333 1.00 47.28  ? 311 ARG   D C     1 
ATOM   9276  O  O     . ARG   C 2  309 ? 13.943  -7.895  -12.737 1.00 43.39  ? 311 ARG   D O     1 
ATOM   9277  C  CB    . ARG   C 2  309 ? 12.696  -8.773  -9.969  1.00 42.73  ? 311 ARG   D CB    1 
ATOM   9278  C  CG    . ARG   C 2  309 ? 12.042  -9.734  -8.975  1.00 40.45  ? 311 ARG   D CG    1 
ATOM   9279  C  CD    . ARG   C 2  309 ? 11.982  -9.156  -7.578  1.00 42.62  ? 311 ARG   D CD    1 
ATOM   9280  N  NE    . ARG   C 2  309 ? 12.869  -9.863  -6.664  1.00 57.43  ? 311 ARG   D NE    1 
ATOM   9281  C  CZ    . ARG   C 2  309 ? 12.481  -10.791 -5.794  1.00 61.17  ? 311 ARG   D CZ    1 
ATOM   9282  N  NH1   . ARG   C 2  309 ? 11.206  -11.127 -5.655  1.00 48.50  ? 311 ARG   D NH1   1 
ATOM   9283  N  NH2   . ARG   C 2  309 ? 13.396  -11.394 -5.039  1.00 66.24  ? 311 ARG   D NH2   1 
ATOM   9284  N  N     . TYR   C 2  310 ? 11.881  -6.944  -12.650 1.00 47.28  ? 312 TYR   D N     1 
ATOM   9285  C  CA    . TYR   C 2  310 ? 12.201  -5.668  -13.285 1.00 45.41  ? 312 TYR   D CA    1 
ATOM   9286  C  C     . TYR   C 2  310 ? 13.131  -4.780  -12.452 1.00 43.53  ? 312 TYR   D C     1 
ATOM   9287  O  O     . TYR   C 2  310 ? 12.730  -4.298  -11.390 1.00 41.82  ? 312 TYR   D O     1 
ATOM   9288  C  CB    . TYR   C 2  310 ? 10.910  -4.907  -13.561 1.00 43.00  ? 312 TYR   D CB    1 
ATOM   9289  C  CG    . TYR   C 2  310 ? 10.102  -5.428  -14.731 1.00 44.53  ? 312 TYR   D CG    1 
ATOM   9290  C  CD1   . TYR   C 2  310 ? 10.694  -5.681  -15.959 1.00 48.10  ? 312 TYR   D CD1   1 
ATOM   9291  C  CD2   . TYR   C 2  310 ? 8.737   -5.652  -14.607 1.00 50.39  ? 312 TYR   D CD2   1 
ATOM   9292  C  CE1   . TYR   C 2  310 ? 9.944   -6.141  -17.040 1.00 48.50  ? 312 TYR   D CE1   1 
ATOM   9293  C  CE2   . TYR   C 2  310 ? 7.981   -6.110  -15.677 1.00 49.16  ? 312 TYR   D CE2   1 
ATOM   9294  C  CZ    . TYR   C 2  310 ? 8.590   -6.356  -16.885 1.00 49.73  ? 312 TYR   D CZ    1 
ATOM   9295  O  OH    . TYR   C 2  310 ? 7.832   -6.804  -17.939 1.00 53.75  ? 312 TYR   D OH    1 
ATOM   9296  N  N     . LEU   C 2  311 ? 14.374  -4.573  -12.928 1.00 46.15  ? 313 LEU   D N     1 
ATOM   9297  C  CA    . LEU   C 2  311 ? 15.282  -3.585  -12.342 1.00 33.91  ? 313 LEU   D CA    1 
ATOM   9298  C  C     . LEU   C 2  311 ? 14.873  -2.166  -12.720 1.00 38.73  ? 313 LEU   D C     1 
ATOM   9299  O  O     . LEU   C 2  311 ? 14.926  -1.253  -11.886 1.00 43.31  ? 313 LEU   D O     1 
ATOM   9300  C  CB    . LEU   C 2  311 ? 16.721  -3.838  -12.805 1.00 34.38  ? 313 LEU   D CB    1 
ATOM   9301  C  CG    . LEU   C 2  311 ? 17.414  -5.167  -12.526 1.00 38.09  ? 313 LEU   D CG    1 
ATOM   9302  C  CD1   . LEU   C 2  311 ? 18.685  -5.316  -13.366 1.00 34.41  ? 313 LEU   D CD1   1 
ATOM   9303  C  CD2   . LEU   C 2  311 ? 17.750  -5.257  -11.058 1.00 36.98  ? 313 LEU   D CD2   1 
ATOM   9304  N  N     . THR   C 2  312 ? 14.489  -1.957  -13.978 1.00 38.97  ? 314 THR   D N     1 
ATOM   9305  C  CA    . THR   C 2  312 ? 14.014  -0.668  -14.463 1.00 32.22  ? 314 THR   D CA    1 
ATOM   9306  C  C     . THR   C 2  312 ? 12.976  -0.892  -15.542 1.00 31.91  ? 314 THR   D C     1 
ATOM   9307  O  O     . THR   C 2  312 ? 12.974  -1.919  -16.224 1.00 43.03  ? 314 THR   D O     1 
ATOM   9308  C  CB    . THR   C 2  312 ? 15.133  0.155   -15.065 1.00 32.29  ? 314 THR   D CB    1 
ATOM   9309  O  OG1   . THR   C 2  312 ? 15.862  -0.695  -15.951 1.00 37.86  ? 314 THR   D OG1   1 
ATOM   9310  C  CG2   . THR   C 2  312 ? 16.046  0.697   -13.968 1.00 37.97  ? 314 THR   D CG2   1 
ATOM   9311  N  N     . VAL   C 2  313 ? 12.115  0.091   -15.731 1.00 24.51  ? 315 VAL   D N     1 
ATOM   9312  C  CA    . VAL   C 2  313 ? 11.149  0.027   -16.818 1.00 35.87  ? 315 VAL   D CA    1 
ATOM   9313  C  C     . VAL   C 2  313 ? 10.954  1.434   -17.346 1.00 30.47  ? 315 VAL   D C     1 
ATOM   9314  O  O     . VAL   C 2  313 ? 10.736  2.361   -16.563 1.00 35.04  ? 315 VAL   D O     1 
ATOM   9315  C  CB    . VAL   C 2  313 ? 9.806   -0.583  -16.353 1.00 33.43  ? 315 VAL   D CB    1 
ATOM   9316  C  CG1   . VAL   C 2  313 ? 8.739   -0.498  -17.444 1.00 26.39  ? 315 VAL   D CG1   1 
ATOM   9317  C  CG2   . VAL   C 2  313 ? 10.001  -2.025  -15.894 1.00 31.02  ? 315 VAL   D CG2   1 
ATOM   9318  N  N     . ALA   C 2  314 ? 11.054  1.602   -18.660 1.00 32.95  ? 316 ALA   D N     1 
ATOM   9319  C  CA    . ALA   C 2  314 ? 10.441  2.749   -19.317 1.00 31.00  ? 316 ALA   D CA    1 
ATOM   9320  C  C     . ALA   C 2  314 ? 9.084   2.339   -19.896 1.00 46.75  ? 316 ALA   D C     1 
ATOM   9321  O  O     . ALA   C 2  314 ? 8.748   1.152   -19.989 1.00 44.44  ? 316 ALA   D O     1 
ATOM   9322  C  CB    . ALA   C 2  314 ? 11.350  3.305   -20.409 1.00 22.45  ? 316 ALA   D CB    1 
ATOM   9323  N  N     . ALA   C 2  315 ? 8.295   3.338   -20.286 1.00 42.29  ? 317 ALA   D N     1 
ATOM   9324  C  CA    . ALA   C 2  315 ? 6.965   3.083   -20.841 1.00 32.87  ? 317 ALA   D CA    1 
ATOM   9325  C  C     . ALA   C 2  315 ? 6.547   4.322   -21.602 1.00 40.60  ? 317 ALA   D C     1 
ATOM   9326  O  O     . ALA   C 2  315 ? 6.512   5.413   -21.026 1.00 53.04  ? 317 ALA   D O     1 
ATOM   9327  C  CB    . ALA   C 2  315 ? 5.936   2.747   -19.742 1.00 29.89  ? 317 ALA   D CB    1 
ATOM   9328  N  N     . ILE   C 2  316 ? 6.224   4.155   -22.879 1.00 38.97  ? 318 ILE   D N     1 
ATOM   9329  C  CA    . ILE   C 2  316 ? 5.833   5.246   -23.761 1.00 35.28  ? 318 ILE   D CA    1 
ATOM   9330  C  C     . ILE   C 2  316 ? 4.410   4.985   -24.231 1.00 40.60  ? 318 ILE   D C     1 
ATOM   9331  O  O     . ILE   C 2  316 ? 4.095   3.879   -24.682 1.00 49.94  ? 318 ILE   D O     1 
ATOM   9332  C  CB    . ILE   C 2  316 ? 6.779   5.356   -24.972 1.00 36.23  ? 318 ILE   D CB    1 
ATOM   9333  C  CG1   . ILE   C 2  316 ? 8.168   4.819   -24.626 1.00 36.20  ? 318 ILE   D CG1   1 
ATOM   9334  C  CG2   . ILE   C 2  316 ? 6.813   6.780   -25.491 1.00 37.76  ? 318 ILE   D CG2   1 
ATOM   9335  C  CD1   . ILE   C 2  316 ? 8.877   5.606   -23.544 0.00 39.65  ? 318 ILE   D CD1   1 
ATOM   9336  N  N     . PHE   C 2  317 ? 3.555   5.995   -24.147 1.00 44.32  ? 319 PHE   D N     1 
ATOM   9337  C  CA    . PHE   C 2  317 ? 2.194   5.905   -24.657 1.00 44.94  ? 319 PHE   D CA    1 
ATOM   9338  C  C     . PHE   C 2  317 ? 2.044   6.915   -25.781 1.00 46.22  ? 319 PHE   D C     1 
ATOM   9339  O  O     . PHE   C 2  317 ? 2.291   8.106   -25.579 1.00 45.66  ? 319 PHE   D O     1 
ATOM   9340  C  CB    . PHE   C 2  317 ? 1.168   6.148   -23.550 1.00 36.95  ? 319 PHE   D CB    1 
ATOM   9341  C  CG    . PHE   C 2  317 ? 1.116   5.043   -22.525 1.00 41.75  ? 319 PHE   D CG    1 
ATOM   9342  C  CD1   . PHE   C 2  317 ? 2.095   4.931   -21.552 1.00 42.41  ? 319 PHE   D CD1   1 
ATOM   9343  C  CD2   . PHE   C 2  317 ? 0.088   4.125   -22.529 1.00 36.33  ? 319 PHE   D CD2   1 
ATOM   9344  C  CE1   . PHE   C 2  317 ? 2.048   3.915   -20.613 1.00 46.93  ? 319 PHE   D CE1   1 
ATOM   9345  C  CE2   . PHE   C 2  317 ? 0.031   3.119   -21.598 1.00 40.86  ? 319 PHE   D CE2   1 
ATOM   9346  C  CZ    . PHE   C 2  317 ? 1.016   3.007   -20.639 1.00 53.48  ? 319 PHE   D CZ    1 
ATOM   9347  N  N     . ARG   C 2  318 ? 1.658   6.436   -26.962 1.00 55.82  ? 320 ARG   D N     1 
ATOM   9348  C  CA    . ARG   C 2  318 ? 1.492   7.277   -28.140 1.00 59.54  ? 320 ARG   D CA    1 
ATOM   9349  C  C     . ARG   C 2  318 ? 0.025   7.309   -28.539 1.00 61.84  ? 320 ARG   D C     1 
ATOM   9350  O  O     . ARG   C 2  318 ? -0.607  6.256   -28.671 1.00 60.35  ? 320 ARG   D O     1 
ATOM   9351  C  CB    . ARG   C 2  318 ? 2.336   6.763   -29.305 1.00 57.86  ? 320 ARG   D CB    1 
ATOM   9352  C  CG    . ARG   C 2  318 ? 3.714   6.304   -28.901 1.00 58.64  ? 320 ARG   D CG    1 
ATOM   9353  C  CD    . ARG   C 2  318 ? 4.500   5.858   -30.110 1.00 61.52  ? 320 ARG   D CD    1 
ATOM   9354  N  NE    . ARG   C 2  318 ? 4.761   6.960   -31.028 1.00 62.63  ? 320 ARG   D NE    1 
ATOM   9355  C  CZ    . ARG   C 2  318 ? 5.286   6.804   -32.235 1.00 65.53  ? 320 ARG   D CZ    1 
ATOM   9356  N  NH1   . ARG   C 2  318 ? 5.583   5.601   -32.703 1.00 62.37  ? 320 ARG   D NH1   1 
ATOM   9357  N  NH2   . ARG   C 2  318 ? 5.522   7.878   -32.989 1.00 62.19  ? 320 ARG   D NH2   1 
ATOM   9358  N  N     . GLY   C 2  319 ? -0.500  8.514   -28.748 1.00 57.86  ? 321 GLY   D N     1 
ATOM   9359  C  CA    . GLY   C 2  319 ? -1.883  8.704   -29.140 1.00 59.43  ? 321 GLY   D CA    1 
ATOM   9360  C  C     . GLY   C 2  319 ? -2.551  9.765   -28.295 1.00 67.61  ? 321 GLY   D C     1 
ATOM   9361  O  O     . GLY   C 2  319 ? -2.042  10.117  -27.226 1.00 69.04  ? 321 GLY   D O     1 
ATOM   9362  N  N     . ARG   C 2  320 ? -3.672  10.309  -28.755 1.00 69.44  ? 322 ARG   D N     1 
ATOM   9363  C  CA    . ARG   C 2  320 ? -4.451  11.181  -27.887 1.00 73.34  ? 322 ARG   D CA    1 
ATOM   9364  C  C     . ARG   C 2  320 ? -5.151  10.324  -26.841 1.00 71.25  ? 322 ARG   D C     1 
ATOM   9365  O  O     . ARG   C 2  320 ? -5.736  9.288   -27.167 1.00 70.59  ? 322 ARG   D O     1 
ATOM   9366  C  CB    . ARG   C 2  320 ? -5.463  11.996  -28.689 1.00 70.25  ? 322 ARG   D CB    1 
ATOM   9367  C  CG    . ARG   C 2  320 ? -6.314  12.933  -27.839 1.00 83.60  ? 322 ARG   D CG    1 
ATOM   9368  C  CD    . ARG   C 2  320 ? -6.129  14.404  -28.234 1.00 96.43  ? 322 ARG   D CD    1 
ATOM   9369  N  NE    . ARG   C 2  320 ? -6.993  15.305  -27.474 1.00 94.02  ? 322 ARG   D NE    1 
ATOM   9370  C  CZ    . ARG   C 2  320 ? -6.653  15.892  -26.332 1.00 109.26 ? 322 ARG   D CZ    1 
ATOM   9371  N  NH1   . ARG   C 2  320 ? -5.465  15.690  -25.777 1.00 110.22 ? 322 ARG   D NH1   1 
ATOM   9372  N  NH2   . ARG   C 2  320 ? -7.523  16.702  -25.731 1.00 83.04  ? 322 ARG   D NH2   1 
ATOM   9373  N  N     . MET   C 2  321 ? -5.058  10.731  -25.579 1.00 70.02  ? 323 MET   D N     1 
ATOM   9374  C  CA    . MET   C 2  321 ? -5.598  9.933   -24.488 1.00 57.49  ? 323 MET   D CA    1 
ATOM   9375  C  C     . MET   C 2  321 ? -5.458  10.732  -23.205 1.00 64.18  ? 323 MET   D C     1 
ATOM   9376  O  O     . MET   C 2  321 ? -4.776  11.757  -23.161 1.00 74.70  ? 323 MET   D O     1 
ATOM   9377  C  CB    . MET   C 2  321 ? -4.890  8.587   -24.377 1.00 50.61  ? 323 MET   D CB    1 
ATOM   9378  C  CG    . MET   C 2  321 ? -3.459  8.690   -23.893 1.00 57.20  ? 323 MET   D CG    1 
ATOM   9379  S  SD    . MET   C 2  321 ? -2.536  7.172   -24.241 1.00 54.45  ? 323 MET   D SD    1 
ATOM   9380  C  CE    . MET   C 2  321 ? -1.986  7.503   -25.920 1.00 56.78  ? 323 MET   D CE    1 
ATOM   9381  N  N     . SER   C 2  322 ? -6.126  10.251  -22.160 1.00 67.53  ? 324 SER   D N     1 
ATOM   9382  C  CA    . SER   C 2  322 ? -6.124  10.912  -20.861 1.00 49.21  ? 324 SER   D CA    1 
ATOM   9383  C  C     . SER   C 2  322 ? -4.826  10.588  -20.139 1.00 55.47  ? 324 SER   D C     1 
ATOM   9384  O  O     . SER   C 2  322 ? -4.625  9.461   -19.664 1.00 44.83  ? 324 SER   D O     1 
ATOM   9385  C  CB    . SER   C 2  322 ? -7.323  10.470  -20.026 1.00 56.57  ? 324 SER   D CB    1 
ATOM   9386  O  OG    . SER   C 2  322 ? -7.267  11.028  -18.722 1.00 51.39  ? 324 SER   D OG    1 
ATOM   9387  N  N     . MET   C 2  323 ? -3.939  11.577  -20.047 1.00 58.03  ? 325 MET   D N     1 
ATOM   9388  C  CA    . MET   C 2  323 ? -2.774  11.411  -19.190 1.00 65.41  ? 325 MET   D CA    1 
ATOM   9389  C  C     . MET   C 2  323 ? -3.183  10.964  -17.789 1.00 61.22  ? 325 MET   D C     1 
ATOM   9390  O  O     . MET   C 2  323 ? -2.496  10.150  -17.161 1.00 57.43  ? 325 MET   D O     1 
ATOM   9391  C  CB    . MET   C 2  323 ? -1.971  12.708  -19.141 1.00 58.67  ? 325 MET   D CB    1 
ATOM   9392  C  CG    . MET   C 2  323 ? -0.866  12.769  -20.176 1.00 60.72  ? 325 MET   D CG    1 
ATOM   9393  S  SD    . MET   C 2  323 ? 0.648   13.344  -19.391 1.00 87.57  ? 325 MET   D SD    1 
ATOM   9394  C  CE    . MET   C 2  323 ? 0.051   14.835  -18.581 1.00 60.94  ? 325 MET   D CE    1 
ATOM   9395  N  N     . LYS   C 2  324 ? -4.311  11.471  -17.284 1.00 61.12  ? 326 LYS   D N     1 
ATOM   9396  C  CA    . LYS   C 2  324 ? -4.761  11.052  -15.962 1.00 53.48  ? 326 LYS   D CA    1 
ATOM   9397  C  C     . LYS   C 2  324 ? -5.006  9.548   -15.929 1.00 52.06  ? 326 LYS   D C     1 
ATOM   9398  O  O     . LYS   C 2  324 ? -4.541  8.850   -15.020 1.00 52.56  ? 326 LYS   D O     1 
ATOM   9399  C  CB    . LYS   C 2  324 ? -6.021  11.822  -15.566 1.00 56.61  ? 326 LYS   D CB    1 
ATOM   9400  C  CG    . LYS   C 2  324 ? -6.159  12.041  -14.071 1.00 54.19  ? 326 LYS   D CG    1 
ATOM   9401  C  CD    . LYS   C 2  324 ? -7.624  12.059  -13.636 1.00 55.03  ? 326 LYS   D CD    1 
ATOM   9402  C  CE    . LYS   C 2  324 ? -7.736  12.023  -12.110 1.00 65.61  ? 326 LYS   D CE    1 
ATOM   9403  N  NZ    . LYS   C 2  324 ? -9.125  11.786  -11.611 1.00 72.57  ? 326 LYS   D NZ    1 
ATOM   9404  N  N     . GLU   C 2  325 ? -5.731  9.028   -16.925 1.00 52.77  ? 327 GLU   D N     1 
ATOM   9405  C  CA    . GLU   C 2  325 ? -5.936  7.582   -17.024 1.00 47.81  ? 327 GLU   D CA    1 
ATOM   9406  C  C     . GLU   C 2  325 ? -4.600  6.838   -17.068 1.00 41.95  ? 327 GLU   D C     1 
ATOM   9407  O  O     . GLU   C 2  325 ? -4.431  5.812   -16.401 1.00 45.48  ? 327 GLU   D O     1 
ATOM   9408  C  CB    . GLU   C 2  325 ? -6.800  7.268   -18.259 1.00 48.02  ? 327 GLU   D CB    1 
ATOM   9409  C  CG    . GLU   C 2  325 ? -7.275  5.816   -18.429 1.00 39.71  ? 327 GLU   D CG    1 
ATOM   9410  C  CD    . GLU   C 2  325 ? -8.575  5.708   -19.246 1.00 54.14  ? 327 GLU   D CD    1 
ATOM   9411  O  OE1   . GLU   C 2  325 ? -9.473  6.560   -19.058 1.00 61.61  ? 327 GLU   D OE1   1 
ATOM   9412  O  OE2   . GLU   C 2  325 ? -8.706  4.777   -20.078 1.00 50.93  ? 327 GLU   D OE2   1 
ATOM   9413  N  N     . VAL   C 2  326 ? -3.630  7.355   -17.827 1.00 45.68  ? 328 VAL   D N     1 
ATOM   9414  C  CA    . VAL   C 2  326 ? -2.322  6.702   -17.916 1.00 46.69  ? 328 VAL   D CA    1 
ATOM   9415  C  C     . VAL   C 2  326 ? -1.686  6.596   -16.534 1.00 44.83  ? 328 VAL   D C     1 
ATOM   9416  O  O     . VAL   C 2  326 ? -1.267  5.514   -16.103 1.00 52.67  ? 328 VAL   D O     1 
ATOM   9417  C  CB    . VAL   C 2  326 ? -1.402  7.454   -18.900 1.00 48.77  ? 328 VAL   D CB    1 
ATOM   9418  C  CG1   . VAL   C 2  326 ? -0.084  6.698   -19.094 1.00 45.28  ? 328 VAL   D CG1   1 
ATOM   9419  C  CG2   . VAL   C 2  326 ? -2.091  7.683   -20.230 1.00 38.65  ? 328 VAL   D CG2   1 
ATOM   9420  N  N     . ASP   C 2  327 ? -1.588  7.723   -15.824 1.00 43.82  ? 329 ASP   D N     1 
ATOM   9421  C  CA    . ASP   C 2  327 ? -0.976  7.709   -14.497 1.00 43.30  ? 329 ASP   D CA    1 
ATOM   9422  C  C     . ASP   C 2  327 ? -1.635  6.665   -13.608 1.00 46.72  ? 329 ASP   D C     1 
ATOM   9423  O  O     . ASP   C 2  327 ? -0.962  5.784   -13.064 1.00 47.34  ? 329 ASP   D O     1 
ATOM   9424  C  CB    . ASP   C 2  327 ? -1.061  9.093   -13.858 1.00 36.46  ? 329 ASP   D CB    1 
ATOM   9425  C  CG    . ASP   C 2  327 ? -0.298  10.146  -14.645 1.00 46.31  ? 329 ASP   D CG    1 
ATOM   9426  O  OD1   . ASP   C 2  327 ? 0.628   9.763   -15.395 1.00 40.12  ? 329 ASP   D OD1   1 
ATOM   9427  O  OD2   . ASP   C 2  327 ? -0.621  11.353  -14.515 1.00 46.95  ? 329 ASP   D OD2   1 
ATOM   9428  N  N     . GLU   C 2  328 ? -2.963  6.742   -13.466 1.00 47.40  ? 330 GLU   D N     1 
ATOM   9429  C  CA    . GLU   C 2  328 ? -3.687  5.773   -12.650 1.00 41.81  ? 330 GLU   D CA    1 
ATOM   9430  C  C     . GLU   C 2  328 ? -3.395  4.347   -13.106 1.00 52.06  ? 330 GLU   D C     1 
ATOM   9431  O  O     . GLU   C 2  328 ? -3.188  3.442   -12.280 1.00 44.03  ? 330 GLU   D O     1 
ATOM   9432  C  CB    . GLU   C 2  328 ? -5.189  6.056   -12.711 1.00 45.78  ? 330 GLU   D CB    1 
ATOM   9433  C  CG    . GLU   C 2  328 ? -5.589  7.508   -12.483 1.00 50.52  ? 330 GLU   D CG    1 
ATOM   9434  C  CD    . GLU   C 2  328 ? -7.079  7.752   -12.699 1.00 61.22  ? 330 GLU   D CD    1 
ATOM   9435  O  OE1   . GLU   C 2  328 ? -7.814  6.783   -13.019 1.00 57.41  ? 330 GLU   D OE1   1 
ATOM   9436  O  OE2   . GLU   C 2  328 ? -7.511  8.919   -12.556 1.00 53.27  ? 330 GLU   D OE2   1 
ATOM   9437  N  N     . GLN   C 2  329 ? -3.366  4.127   -14.423 1.00 44.99  ? 331 GLN   D N     1 
ATOM   9438  C  CA    . GLN   C 2  329 ? -3.195  2.769   -14.914 1.00 52.48  ? 331 GLN   D CA    1 
ATOM   9439  C  C     . GLN   C 2  329 ? -1.759  2.289   -14.756 1.00 52.30  ? 331 GLN   D C     1 
ATOM   9440  O  O     . GLN   C 2  329 ? -1.543  1.097   -14.486 1.00 42.28  ? 331 GLN   D O     1 
ATOM   9441  C  CB    . GLN   C 2  329 ? -3.681  2.666   -16.367 1.00 47.88  ? 331 GLN   D CB    1 
ATOM   9442  C  CG    . GLN   C 2  329 ? -5.211  2.704   -16.489 1.00 44.25  ? 331 GLN   D CG    1 
ATOM   9443  C  CD    . GLN   C 2  329 ? -5.906  1.866   -15.392 1.00 65.59  ? 331 GLN   D CD    1 
ATOM   9444  O  OE1   . GLN   C 2  329 ? -5.655  0.650   -15.251 1.00 45.03  ? 331 GLN   D OE1   1 
ATOM   9445  N  NE2   . GLN   C 2  329 ? -6.764  2.528   -14.593 1.00 50.02  ? 331 GLN   D NE2   1 
ATOM   9446  N  N     . MET   C 2  330 ? -0.773  3.199   -14.872 1.00 43.57  ? 332 MET   D N     1 
ATOM   9447  C  CA    . MET   C 2  330 ? 0.604   2.807   -14.570 1.00 38.58  ? 332 MET   D CA    1 
ATOM   9448  C  C     . MET   C 2  330 ? 0.788   2.553   -13.077 1.00 43.51  ? 332 MET   D C     1 
ATOM   9449  O  O     . MET   C 2  330 ? 1.679   1.789   -12.681 1.00 38.30  ? 332 MET   D O     1 
ATOM   9450  C  CB    . MET   C 2  330 ? 1.599   3.864   -15.052 1.00 34.97  ? 332 MET   D CB    1 
ATOM   9451  C  CG    . MET   C 2  330 ? 1.954   3.797   -16.523 1.00 38.97  ? 332 MET   D CG    1 
ATOM   9452  S  SD    . MET   C 2  330 ? 2.340   2.137   -17.118 1.00 44.23  ? 332 MET   D SD    1 
ATOM   9453  C  CE    . MET   C 2  330 ? 3.937   1.786   -16.381 1.00 35.69  ? 332 MET   D CE    1 
ATOM   9454  N  N     . LEU   C 2  331 ? -0.045  3.178   -12.231 1.00 43.84  ? 333 LEU   D N     1 
ATOM   9455  C  CA    . LEU   C 2  331 ? 0.014   2.923   -10.795 1.00 38.37  ? 333 LEU   D CA    1 
ATOM   9456  C  C     . LEU   C 2  331 ? -0.594  1.574   -10.434 1.00 47.40  ? 333 LEU   D C     1 
ATOM   9457  O  O     . LEU   C 2  331 ? -0.087  0.887   -9.541  1.00 46.62  ? 333 LEU   D O     1 
ATOM   9458  C  CB    . LEU   C 2  331 ? -0.683  4.041   -10.032 1.00 42.80  ? 333 LEU   D CB    1 
ATOM   9459  C  CG    . LEU   C 2  331 ? 0.157   5.312   -9.955  1.00 48.77  ? 333 LEU   D CG    1 
ATOM   9460  C  CD1   . LEU   C 2  331 ? -0.655  6.463   -9.395  1.00 26.70  ? 333 LEU   D CD1   1 
ATOM   9461  C  CD2   . LEU   C 2  331 ? 1.441   5.045   -9.151  1.00 30.52  ? 333 LEU   D CD2   1 
ATOM   9462  N  N     . ASN   C 2  332 ? -1.670  1.160   -11.111 1.00 50.06  ? 334 ASN   D N     1 
ATOM   9463  C  CA    . ASN   C 2  332 ? -2.234  -0.148  -10.790 1.00 46.36  ? 334 ASN   D CA    1 
ATOM   9464  C  C     . ASN   C 2  332 ? -1.233  -1.253  -11.099 1.00 48.67  ? 334 ASN   D C     1 
ATOM   9465  O  O     . ASN   C 2  332 ? -1.022  -2.158  -10.279 1.00 44.99  ? 334 ASN   D O     1 
ATOM   9466  C  CB    . ASN   C 2  332 ? -3.551  -0.382  -11.533 1.00 40.79  ? 334 ASN   D CB    1 
ATOM   9467  C  CG    . ASN   C 2  332 ? -4.625  0.602   -11.136 0.00 55.29  ? 334 ASN   D CG    1 
ATOM   9468  O  OD1   . ASN   C 2  332 ? -4.337  1.743   -10.763 1.00 71.13  ? 334 ASN   D OD1   1 
ATOM   9469  N  ND2   . ASN   C 2  332 ? -5.879  0.164   -11.212 1.00 65.01  ? 334 ASN   D ND2   1 
ATOM   9470  N  N     . VAL   C 2  333 ? -0.584  -1.186  -12.270 1.00 38.52  ? 335 VAL   D N     1 
ATOM   9471  C  CA    . VAL   C 2  333 ? 0.304   -2.279  -12.658 1.00 39.81  ? 335 VAL   D CA    1 
ATOM   9472  C  C     . VAL   C 2  333 ? 1.363   -2.476  -11.593 1.00 43.52  ? 335 VAL   D C     1 
ATOM   9473  O  O     . VAL   C 2  333 ? 1.575   -3.587  -11.101 1.00 47.89  ? 335 VAL   D O     1 
ATOM   9474  C  CB    . VAL   C 2  333 ? 0.941   -2.031  -14.040 1.00 47.76  ? 335 VAL   D CB    1 
ATOM   9475  C  CG1   . VAL   C 2  333 ? 1.834   -3.193  -14.417 1.00 43.95  ? 335 VAL   D CG1   1 
ATOM   9476  C  CG2   . VAL   C 2  333 ? -0.120  -1.861  -15.103 1.00 49.77  ? 335 VAL   D CG2   1 
ATOM   9477  N  N     . GLN   C 2  334 ? 2.018   -1.389  -11.189 1.00 49.26  ? 336 GLN   D N     1 
ATOM   9478  C  CA    . GLN   C 2  334 ? 3.064   -1.499  -10.178 1.00 44.26  ? 336 GLN   D CA    1 
ATOM   9479  C  C     . GLN   C 2  334 ? 2.498   -2.035  -8.869  1.00 42.25  ? 336 GLN   D C     1 
ATOM   9480  O  O     . GLN   C 2  334 ? 3.017   -3.017  -8.321  1.00 36.73  ? 336 GLN   D O     1 
ATOM   9481  C  CB    . GLN   C 2  334 ? 3.744   -0.144  -9.985  1.00 29.67  ? 336 GLN   D CB    1 
ATOM   9482  C  CG    . GLN   C 2  334 ? 3.870   0.604   -11.265 1.00 34.39  ? 336 GLN   D CG    1 
ATOM   9483  C  CD    . GLN   C 2  334 ? 4.884   1.693   -11.204 1.00 38.26  ? 336 GLN   D CD    1 
ATOM   9484  O  OE1   . GLN   C 2  334 ? 6.038   1.469   -10.826 1.00 39.48  ? 336 GLN   D OE1   1 
ATOM   9485  N  NE2   . GLN   C 2  334 ? 4.470   2.895   -11.582 1.00 35.34  ? 336 GLN   D NE2   1 
ATOM   9486  N  N     . ASN   C 2  335 ? 1.416   -1.418  -8.365  1.00 39.50  ? 337 ASN   D N     1 
ATOM   9487  C  CA    . ASN   C 2  335 ? 0.729   -1.932  -7.176  1.00 49.82  ? 337 ASN   D CA    1 
ATOM   9488  C  C     . ASN   C 2  335 ? 0.437   -3.429  -7.295  1.00 47.45  ? 337 ASN   D C     1 
ATOM   9489  O  O     . ASN   C 2  335 ? 0.910   -4.235  -6.486  1.00 43.61  ? 337 ASN   D O     1 
ATOM   9490  C  CB    . ASN   C 2  335 ? -0.580  -1.167  -6.921  1.00 57.29  ? 337 ASN   D CB    1 
ATOM   9491  C  CG    . ASN   C 2  335 ? -0.362  0.315   -6.578  1.00 70.79  ? 337 ASN   D CG    1 
ATOM   9492  O  OD1   . ASN   C 2  335 ? 0.738   0.731   -6.190  1.00 61.97  ? 337 ASN   D OD1   1 
ATOM   9493  N  ND2   . ASN   C 2  335 ? -1.428  1.118   -6.721  0.78 53.51  ? 337 ASN   D ND2   1 
ATOM   9494  N  N     . LYS   C 2  336 ? -0.339  -3.828  -8.309  1.00 40.05  ? 338 LYS   D N     1 
ATOM   9495  C  CA    . LYS   C 2  336 ? -0.824  -5.204  -8.327  1.00 47.26  ? 338 LYS   D CA    1 
ATOM   9496  C  C     . LYS   C 2  336 ? 0.282   -6.217  -8.645  1.00 49.87  ? 338 LYS   D C     1 
ATOM   9497  O  O     . LYS   C 2  336 ? 0.140   -7.392  -8.291  1.00 58.72  ? 338 LYS   D O     1 
ATOM   9498  C  CB    . LYS   C 2  336 ? -2.014  -5.335  -9.298  1.00 40.53  ? 338 LYS   D CB    1 
ATOM   9499  N  N     . ASN   C 2  337 ? 1.390   -5.792  -9.257  1.00 49.75  ? 339 ASN   D N     1 
ATOM   9500  C  CA    . ASN   C 2  337 ? 2.541   -6.644  -9.564  1.00 45.90  ? 339 ASN   D CA    1 
ATOM   9501  C  C     . ASN   C 2  337 ? 3.793   -6.199  -8.807  1.00 50.72  ? 339 ASN   D C     1 
ATOM   9502  O  O     . ASN   C 2  337 ? 4.917   -6.273  -9.322  1.00 48.52  ? 339 ASN   D O     1 
ATOM   9503  C  CB    . ASN   C 2  337 ? 2.823   -6.663  -11.065 1.00 50.92  ? 339 ASN   D CB    1 
ATOM   9504  C  CG    . ASN   C 2  337 ? 1.742   -7.364  -11.851 1.00 56.19  ? 339 ASN   D CG    1 
ATOM   9505  O  OD1   . ASN   C 2  337 ? 1.742   -8.594  -11.976 1.00 62.72  ? 339 ASN   D OD1   1 
ATOM   9506  N  ND2   . ASN   C 2  337 ? 0.817   -6.590  -12.394 1.00 43.92  ? 339 ASN   D ND2   1 
ATOM   9507  N  N     . SER   C 2  338 ? 3.609   -5.747  -7.563  1.00 43.85  ? 340 SER   D N     1 
ATOM   9508  C  CA    . SER   C 2  338 ? 4.713   -5.206  -6.780  1.00 37.40  ? 340 SER   D CA    1 
ATOM   9509  C  C     . SER   C 2  338 ? 5.918   -6.144  -6.742  1.00 46.31  ? 340 SER   D C     1 
ATOM   9510  O  O     . SER   C 2  338 ? 7.068   -5.690  -6.805  1.00 49.78  ? 340 SER   D O     1 
ATOM   9511  C  CB    . SER   C 2  338 ? 4.224   -4.921  -5.367  1.00 39.74  ? 340 SER   D CB    1 
ATOM   9512  O  OG    . SER   C 2  338 ? 3.717   -6.116  -4.795  1.00 57.08  ? 340 SER   D OG    1 
ATOM   9513  N  N     . SER   C 2  339 ? 5.681   -7.454  -6.617  1.00 49.02  ? 341 SER   D N     1 
ATOM   9514  C  CA    . SER   C 2  339 ? 6.785   -8.407  -6.477  1.00 51.62  ? 341 SER   D CA    1 
ATOM   9515  C  C     . SER   C 2  339 ? 7.740   -8.377  -7.675  1.00 57.62  ? 341 SER   D C     1 
ATOM   9516  O  O     . SER   C 2  339 ? 8.939   -8.659  -7.527  1.00 48.61  ? 341 SER   D O     1 
ATOM   9517  C  CB    . SER   C 2  339 ? 6.237   -9.828  -6.290  1.00 47.53  ? 341 SER   D CB    1 
ATOM   9518  O  OG    . SER   C 2  339 ? 5.222   -9.869  -5.314  1.00 49.87  ? 341 SER   D OG    1 
ATOM   9519  N  N     . TYR   C 2  340 ? 7.240   -8.056  -8.866  1.00 49.95  ? 342 TYR   D N     1 
ATOM   9520  C  CA    . TYR   C 2  340 ? 8.049   -8.159  -10.069 1.00 49.25  ? 342 TYR   D CA    1 
ATOM   9521  C  C     . TYR   C 2  340 ? 8.892   -6.903  -10.339 1.00 56.75  ? 342 TYR   D C     1 
ATOM   9522  O  O     . TYR   C 2  340 ? 9.359   -6.710  -11.471 1.00 56.33  ? 342 TYR   D O     1 
ATOM   9523  C  CB    . TYR   C 2  340 ? 7.144   -8.491  -11.252 1.00 49.89  ? 342 TYR   D CB    1 
ATOM   9524  C  CG    . TYR   C 2  340 ? 6.329   -9.747  -11.024 1.00 57.29  ? 342 TYR   D CG    1 
ATOM   9525  C  CD1   . TYR   C 2  340 ? 6.935   -10.999 -11.000 1.00 52.02  ? 342 TYR   D CD1   1 
ATOM   9526  C  CD2   . TYR   C 2  340 ? 4.956   -9.682  -10.820 1.00 57.46  ? 342 TYR   D CD2   1 
ATOM   9527  C  CE1   . TYR   C 2  340 ? 6.195   -12.145 -10.788 1.00 47.88  ? 342 TYR   D CE1   1 
ATOM   9528  C  CE2   . TYR   C 2  340 ? 4.204   -10.832 -10.610 1.00 49.38  ? 342 TYR   D CE2   1 
ATOM   9529  C  CZ    . TYR   C 2  340 ? 4.828   -12.060 -10.600 1.00 49.75  ? 342 TYR   D CZ    1 
ATOM   9530  O  OH    . TYR   C 2  340 ? 4.081   -13.205 -10.387 1.00 51.29  ? 342 TYR   D OH    1 
ATOM   9531  N  N     . PHE   C 2  341 ? 9.099   -6.052  -9.326  1.00 52.64  ? 343 PHE   D N     1 
ATOM   9532  C  CA    . PHE   C 2  341 ? 9.998   -4.904  -9.412  1.00 49.08  ? 343 PHE   D CA    1 
ATOM   9533  C  C     . PHE   C 2  341 ? 10.904  -4.910  -8.186  1.00 46.78  ? 343 PHE   D C     1 
ATOM   9534  O  O     . PHE   C 2  341 ? 10.414  -5.023  -7.059  1.00 48.47  ? 343 PHE   D O     1 
ATOM   9535  C  CB    . PHE   C 2  341 ? 9.234   -3.569  -9.469  1.00 42.78  ? 343 PHE   D CB    1 
ATOM   9536  C  CG    . PHE   C 2  341 ? 8.160   -3.490  -10.533 1.00 39.26  ? 343 PHE   D CG    1 
ATOM   9537  C  CD1   . PHE   C 2  341 ? 6.898   -4.012  -10.306 1.00 40.19  ? 343 PHE   D CD1   1 
ATOM   9538  C  CD2   . PHE   C 2  341 ? 8.397   -2.842  -11.729 1.00 44.16  ? 343 PHE   D CD2   1 
ATOM   9539  C  CE1   . PHE   C 2  341 ? 5.908   -3.911  -11.260 1.00 38.95  ? 343 PHE   D CE1   1 
ATOM   9540  C  CE2   . PHE   C 2  341 ? 7.404   -2.744  -12.700 1.00 44.75  ? 343 PHE   D CE2   1 
ATOM   9541  C  CZ    . PHE   C 2  341 ? 6.159   -3.275  -12.457 1.00 41.94  ? 343 PHE   D CZ    1 
ATOM   9542  N  N     . VAL   C 2  342 ? 12.218  -4.786  -8.397  1.00 33.49  ? 344 VAL   D N     1 
ATOM   9543  C  CA    . VAL   C 2  342 ? 13.137  -4.759  -7.265  1.00 41.96  ? 344 VAL   D CA    1 
ATOM   9544  C  C     . VAL   C 2  342 ? 12.731  -3.656  -6.294  1.00 39.84  ? 344 VAL   D C     1 
ATOM   9545  O  O     . VAL   C 2  342 ? 12.586  -2.484  -6.662  1.00 39.85  ? 344 VAL   D O     1 
ATOM   9546  C  CB    . VAL   C 2  342 ? 14.591  -4.588  -7.735  1.00 40.45  ? 344 VAL   D CB    1 
ATOM   9547  C  CG1   . VAL   C 2  342 ? 15.122  -5.896  -8.251  1.00 42.17  ? 344 VAL   D CG1   1 
ATOM   9548  C  CG2   . VAL   C 2  342 ? 14.705  -3.501  -8.804  1.00 32.68  ? 344 VAL   D CG2   1 
ATOM   9549  N  N     . GLU   C 2  343 ? 12.546  -4.030  -5.036  1.00 41.83  ? 345 GLU   D N     1 
ATOM   9550  C  CA    . GLU   C 2  343 ? 12.151  -3.067  -4.022  1.00 33.91  ? 345 GLU   D CA    1 
ATOM   9551  C  C     . GLU   C 2  343 ? 13.263  -2.068  -3.721  1.00 41.05  ? 345 GLU   D C     1 
ATOM   9552  O  O     . GLU   C 2  343 ? 12.979  -0.977  -3.217  1.00 42.27  ? 345 GLU   D O     1 
ATOM   9553  C  CB    . GLU   C 2  343 ? 11.753  -3.814  -2.741  1.00 30.59  ? 345 GLU   D CB    1 
ATOM   9554  C  CG    . GLU   C 2  343 ? 12.936  -4.635  -2.182  1.00 55.50  ? 345 GLU   D CG    1 
ATOM   9555  C  CD    . GLU   C 2  343 ? 12.669  -5.311  -0.845  1.00 56.57  ? 345 GLU   D CD    1 
ATOM   9556  O  OE1   . GLU   C 2  343 ? 11.577  -5.106  -0.276  1.00 59.04  ? 345 GLU   D OE1   1 
ATOM   9557  O  OE2   . GLU   C 2  343 ? 13.562  -6.051  -0.365  1.00 63.71  ? 345 GLU   D OE2   1 
ATOM   9558  N  N     . TRP   C 2  344 ? 14.517  -2.411  -4.005  1.00 33.59  ? 346 TRP   D N     1 
ATOM   9559  C  CA    . TRP   C 2  344 ? 15.637  -1.557  -3.631  1.00 40.88  ? 346 TRP   D CA    1 
ATOM   9560  C  C     . TRP   C 2  344 ? 16.053  -0.585  -4.738  1.00 45.51  ? 346 TRP   D C     1 
ATOM   9561  O  O     . TRP   C 2  344 ? 17.126  0.028   -4.636  1.00 40.17  ? 346 TRP   D O     1 
ATOM   9562  C  CB    . TRP   C 2  344 ? 16.833  -2.411  -3.190  1.00 46.14  ? 346 TRP   D CB    1 
ATOM   9563  C  CG    . TRP   C 2  344 ? 17.104  -3.527  -4.104  1.00 43.03  ? 346 TRP   D CG    1 
ATOM   9564  C  CD1   . TRP   C 2  344 ? 16.552  -4.763  -4.059  1.00 42.68  ? 346 TRP   D CD1   1 
ATOM   9565  C  CD2   . TRP   C 2  344 ? 17.981  -3.514  -5.230  1.00 48.40  ? 346 TRP   D CD2   1 
ATOM   9566  N  NE1   . TRP   C 2  344 ? 17.031  -5.533  -5.088  1.00 45.08  ? 346 TRP   D NE1   1 
ATOM   9567  C  CE2   . TRP   C 2  344 ? 17.914  -4.792  -5.823  1.00 45.38  ? 346 TRP   D CE2   1 
ATOM   9568  C  CE3   . TRP   C 2  344 ? 18.820  -2.547  -5.796  1.00 46.10  ? 346 TRP   D CE3   1 
ATOM   9569  C  CZ2   . TRP   C 2  344 ? 18.645  -5.130  -6.949  1.00 37.08  ? 346 TRP   D CZ2   1 
ATOM   9570  C  CZ3   . TRP   C 2  344 ? 19.548  -2.880  -6.914  1.00 39.92  ? 346 TRP   D CZ3   1 
ATOM   9571  C  CH2   . TRP   C 2  344 ? 19.456  -4.164  -7.481  1.00 47.88  ? 346 TRP   D CH2   1 
ATOM   9572  N  N     . ILE   C 2  345 ? 15.229  -0.421  -5.772  1.00 37.82  ? 347 ILE   D N     1 
ATOM   9573  C  CA    . ILE   C 2  345 ? 15.349  0.709   -6.692  1.00 35.18  ? 347 ILE   D CA    1 
ATOM   9574  C  C     . ILE   C 2  345 ? 14.015  1.444   -6.758  1.00 37.98  ? 347 ILE   D C     1 
ATOM   9575  O  O     . ILE   C 2  345 ? 13.114  1.043   -7.509  1.00 38.81  ? 347 ILE   D O     1 
ATOM   9576  C  CB    . ILE   C 2  345 ? 15.786  0.270   -8.092  1.00 33.77  ? 347 ILE   D CB    1 
ATOM   9577  C  CG1   . ILE   C 2  345 ? 17.206  -0.296  -8.068  1.00 31.55  ? 347 ILE   D CG1   1 
ATOM   9578  C  CG2   . ILE   C 2  345 ? 15.698  1.449   -9.015  1.00 35.05  ? 347 ILE   D CG2   1 
ATOM   9579  C  CD1   . ILE   C 2  345 ? 17.673  -0.820  -9.430  1.00 31.34  ? 347 ILE   D CD1   1 
ATOM   9580  N  N     . PRO   C 2  346 ? 13.835  2.515   -6.003  1.00 33.02  ? 348 PRO   D N     1 
ATOM   9581  C  CA    . PRO   C 2  346 ? 12.524  3.167   -5.973  1.00 31.31  ? 348 PRO   D CA    1 
ATOM   9582  C  C     . PRO   C 2  346 ? 12.214  3.887   -7.270  1.00 29.57  ? 348 PRO   D C     1 
ATOM   9583  O  O     . PRO   C 2  346 ? 13.095  4.403   -7.958  1.00 33.27  ? 348 PRO   D O     1 
ATOM   9584  C  CB    . PRO   C 2  346 ? 12.639  4.160   -4.811  1.00 20.56  ? 348 PRO   D CB    1 
ATOM   9585  C  CG    . PRO   C 2  346 ? 13.801  3.679   -4.018  1.00 34.61  ? 348 PRO   D CG    1 
ATOM   9586  C  CD    . PRO   C 2  346 ? 14.747  3.053   -4.988  1.00 33.62  ? 348 PRO   D CD    1 
ATOM   9587  N  N     . ASN   C 2  347 ? 10.930  3.922   -7.592  1.00 29.70  ? 349 ASN   D N     1 
ATOM   9588  C  CA    . ASN   C 2  347 ? 10.428  4.712   -8.703  1.00 28.24  ? 349 ASN   D CA    1 
ATOM   9589  C  C     . ASN   C 2  347 ? 11.162  4.374   -9.991  1.00 35.46  ? 349 ASN   D C     1 
ATOM   9590  O  O     . ASN   C 2  347 ? 11.565  5.251   -10.758 1.00 37.09  ? 349 ASN   D O     1 
ATOM   9591  C  CB    . ASN   C 2  347 ? 10.531  6.193   -8.383  1.00 23.73  ? 349 ASN   D CB    1 
ATOM   9592  C  CG    . ASN   C 2  347 ? 10.028  6.513   -6.992  1.00 34.66  ? 349 ASN   D CG    1 
ATOM   9593  O  OD1   . ASN   C 2  347 ? 10.818  6.731   -6.070  1.00 26.06  ? 349 ASN   D OD1   1 
ATOM   9594  N  ND2   . ASN   C 2  347 ? 8.706   6.539   -6.830  1.00 28.97  ? 349 ASN   D ND2   1 
ATOM   9595  N  N     . ASN   C 2  348 ? 11.320  3.074   -10.234 1.00 37.80  ? 350 ASN   D N     1 
ATOM   9596  C  CA    . ASN   C 2  348 ? 12.169  2.599   -11.310 1.00 30.88  ? 350 ASN   D CA    1 
ATOM   9597  C  C     . ASN   C 2  348 ? 11.407  2.424   -12.607 1.00 26.70  ? 350 ASN   D C     1 
ATOM   9598  O  O     . ASN   C 2  348 ? 11.948  1.859   -13.553 1.00 33.96  ? 350 ASN   D O     1 
ATOM   9599  C  CB    . ASN   C 2  348 ? 12.842  1.291   -10.904 1.00 34.46  ? 350 ASN   D CB    1 
ATOM   9600  C  CG    . ASN   C 2  348 ? 11.841  0.197   -10.621 1.00 40.41  ? 350 ASN   D CG    1 
ATOM   9601  O  OD1   . ASN   C 2  348 ? 10.635  0.414   -10.720 1.00 45.64  ? 350 ASN   D OD1   1 
ATOM   9602  N  ND2   . ASN   C 2  348 ? 12.330  -0.989  -10.295 1.00 34.33  ? 350 ASN   D ND2   1 
ATOM   9603  N  N     . VAL   C 2  349 ? 10.172  2.900   -12.675 1.00 31.40  ? 351 VAL   D N     1 
ATOM   9604  C  CA    . VAL   C 2  349 ? 9.325   2.759   -13.855 1.00 32.67  ? 351 VAL   D CA    1 
ATOM   9605  C  C     . VAL   C 2  349 ? 8.923   4.162   -14.282 1.00 36.55  ? 351 VAL   D C     1 
ATOM   9606  O  O     . VAL   C 2  349 ? 8.030   4.782   -13.685 1.00 32.70  ? 351 VAL   D O     1 
ATOM   9607  C  CB    . VAL   C 2  349 ? 8.083   1.896   -13.593 1.00 29.69  ? 351 VAL   D CB    1 
ATOM   9608  C  CG1   . VAL   C 2  349 ? 7.236   1.827   -14.842 1.00 26.04  ? 351 VAL   D CG1   1 
ATOM   9609  C  CG2   . VAL   C 2  349 ? 8.465   0.510   -13.092 1.00 28.47  ? 351 VAL   D CG2   1 
ATOM   9610  N  N     . LYS   C 2  350 ? 9.554   4.656   -15.331 1.00 36.76  ? 352 LYS   D N     1 
ATOM   9611  C  CA    . LYS   C 2  350 ? 9.214   5.948   -15.899 1.00 37.72  ? 352 LYS   D CA    1 
ATOM   9612  C  C     . LYS   C 2  350 ? 8.241   5.771   -17.063 1.00 39.24  ? 352 LYS   D C     1 
ATOM   9613  O  O     . LYS   C 2  350 ? 8.262   4.755   -17.762 1.00 41.64  ? 352 LYS   D O     1 
ATOM   9614  C  CB    . LYS   C 2  350 ? 10.489  6.668   -16.340 1.00 40.48  ? 352 LYS   D CB    1 
ATOM   9615  C  CG    . LYS   C 2  350 ? 11.426  6.945   -15.171 1.00 33.05  ? 352 LYS   D CG    1 
ATOM   9616  C  CD    . LYS   C 2  350 ? 10.632  7.585   -14.041 1.00 32.88  ? 352 LYS   D CD    1 
ATOM   9617  C  CE    . LYS   C 2  350 ? 11.522  8.261   -13.017 1.00 41.66  ? 352 LYS   D CE    1 
ATOM   9618  N  NZ    . LYS   C 2  350 ? 11.562  7.554   -11.689 1.00 37.37  ? 352 LYS   D NZ    1 
ATOM   9619  N  N     . THR   C 2  351 ? 7.359   6.757   -17.240 1.00 37.80  ? 353 THR   D N     1 
ATOM   9620  C  CA    . THR   C 2  351 ? 6.364   6.766   -18.302 1.00 36.60  ? 353 THR   D CA    1 
ATOM   9621  C  C     . THR   C 2  351 ? 6.484   8.058   -19.081 1.00 36.50  ? 353 THR   D C     1 
ATOM   9622  O  O     . THR   C 2  351 ? 6.688   9.121   -18.488 1.00 42.33  ? 353 THR   D O     1 
ATOM   9623  C  CB    . THR   C 2  351 ? 4.909   6.695   -17.770 1.00 39.89  ? 353 THR   D CB    1 
ATOM   9624  O  OG1   . THR   C 2  351 ? 4.696   5.524   -16.973 1.00 34.74  ? 353 THR   D OG1   1 
ATOM   9625  C  CG2   . THR   C 2  351 ? 3.922   6.713   -18.938 1.00 34.53  ? 353 THR   D CG2   1 
ATOM   9626  N  N     . ALA   C 2  352 ? 6.305   7.974   -20.398 1.00 37.50  ? 354 ALA   D N     1 
ATOM   9627  C  CA    . ALA   C 2  352 ? 6.154   9.147   -21.254 1.00 38.39  ? 354 ALA   D CA    1 
ATOM   9628  C  C     . ALA   C 2  352 ? 4.956   8.961   -22.181 1.00 46.11  ? 354 ALA   D C     1 
ATOM   9629  O  O     . ALA   C 2  352 ? 4.746   7.869   -22.714 1.00 55.08  ? 354 ALA   D O     1 
ATOM   9630  C  CB    . ALA   C 2  352 ? 7.422   9.393   -22.077 1.00 41.61  ? 354 ALA   D CB    1 
ATOM   9631  N  N     . VAL   C 2  353 ? 4.164   10.014  -22.372 1.00 40.10  ? 355 VAL   D N     1 
ATOM   9632  C  CA    . VAL   C 2  353 ? 3.080   10.009  -23.352 1.00 43.41  ? 355 VAL   D CA    1 
ATOM   9633  C  C     . VAL   C 2  353 ? 3.457   10.959  -24.478 1.00 50.54  ? 355 VAL   D C     1 
ATOM   9634  O  O     . VAL   C 2  353 ? 3.629   12.162  -24.246 1.00 53.70  ? 355 VAL   D O     1 
ATOM   9635  C  CB    . VAL   C 2  353 ? 1.724   10.405  -22.741 1.00 47.63  ? 355 VAL   D CB    1 
ATOM   9636  C  CG1   . VAL   C 2  353 ? 1.375   9.522   -21.535 1.00 49.77  ? 355 VAL   D CG1   1 
ATOM   9637  C  CG2   . VAL   C 2  353 ? 1.677   11.881  -22.393 1.00 52.52  ? 355 VAL   D CG2   1 
ATOM   9638  N  N     . CYS   C 2  354 ? 3.599   10.413  -25.690 1.00 55.81  ? 356 CYS   D N     1 
ATOM   9639  C  CA    . CYS   C 2  354 ? 3.757   11.185  -26.923 1.00 58.65  ? 356 CYS   D CA    1 
ATOM   9640  C  C     . CYS   C 2  354 ? 2.477   11.077  -27.743 1.00 58.71  ? 356 CYS   D C     1 
ATOM   9641  O  O     . CYS   C 2  354 ? 2.018   9.967   -28.042 1.00 55.27  ? 356 CYS   D O     1 
ATOM   9642  C  CB    . CYS   C 2  354 ? 4.948   10.685  -27.745 1.00 56.67  ? 356 CYS   D CB    1 
ATOM   9643  S  SG    . CYS   C 2  354 ? 4.994   11.354  -29.419 1.00 69.39  ? 356 CYS   D SG    1 
ATOM   9644  N  N     . ASP   C 2  355 ? 1.896   12.216  -28.108 1.00 54.69  ? 357 ASP   D N     1 
ATOM   9645  C  CA    . ASP   C 2  355 ? 0.521   12.165  -28.588 1.00 70.70  ? 357 ASP   D CA    1 
ATOM   9646  C  C     . ASP   C 2  355 ? 0.401   11.966  -30.098 1.00 67.22  ? 357 ASP   D C     1 
ATOM   9647  O  O     . ASP   C 2  355 ? -0.723  11.917  -30.607 1.00 74.33  ? 357 ASP   D O     1 
ATOM   9648  C  CB    . ASP   C 2  355 ? -0.257  13.413  -28.136 1.00 68.86  ? 357 ASP   D CB    1 
ATOM   9649  C  CG    . ASP   C 2  355 ? 0.175   14.680  -28.841 1.00 77.29  ? 357 ASP   D CG    1 
ATOM   9650  O  OD1   . ASP   C 2  355 ? 0.939   14.610  -29.830 1.00 79.38  ? 357 ASP   D OD1   1 
ATOM   9651  O  OD2   . ASP   C 2  355 ? -0.265  15.762  -28.393 1.00 73.84  ? 357 ASP   D OD2   1 
ATOM   9652  N  N     . ILE   C 2  356 ? 1.511   11.820  -30.816 1.00 64.01  ? 358 ILE   D N     1 
ATOM   9653  C  CA    . ILE   C 2  356 ? 1.491   11.484  -32.239 1.00 60.22  ? 358 ILE   D CA    1 
ATOM   9654  C  C     . ILE   C 2  356 ? 1.543   9.963   -32.352 1.00 57.60  ? 358 ILE   D C     1 
ATOM   9655  O  O     . ILE   C 2  356 ? 2.610   9.373   -32.106 1.00 60.61  ? 358 ILE   D O     1 
ATOM   9656  C  CB    . ILE   C 2  356 ? 2.661   12.134  -32.990 1.00 68.80  ? 358 ILE   D CB    1 
ATOM   9657  C  CG1   . ILE   C 2  356 ? 2.285   13.539  -33.468 1.00 59.24  ? 358 ILE   D CG1   1 
ATOM   9658  C  CG2   . ILE   C 2  356 ? 3.118   11.253  -34.157 1.00 70.97  ? 358 ILE   D CG2   1 
ATOM   9659  C  CD1   . ILE   C 2  356 ? 3.479   14.406  -33.832 1.00 60.51  ? 358 ILE   D CD1   1 
ATOM   9660  N  N     . PRO   C 2  357 ? 0.446   9.296   -32.695 1.00 56.89  ? 359 PRO   D N     1 
ATOM   9661  C  CA    . PRO   C 2  357 ? 0.470   7.837   -32.764 1.00 62.09  ? 359 PRO   D CA    1 
ATOM   9662  C  C     . PRO   C 2  357 ? 1.223   7.383   -33.997 1.00 64.76  ? 359 PRO   D C     1 
ATOM   9663  O  O     . PRO   C 2  357 ? 1.459   8.179   -34.919 1.00 55.11  ? 359 PRO   D O     1 
ATOM   9664  C  CB    . PRO   C 2  357 ? -1.016  7.452   -32.835 1.00 64.05  ? 359 PRO   D CB    1 
ATOM   9665  C  CG    . PRO   C 2  357 ? -1.685  8.649   -33.413 1.00 64.15  ? 359 PRO   D CG    1 
ATOM   9666  C  CD    . PRO   C 2  357 ? -0.875  9.856   -33.032 1.00 54.94  ? 359 PRO   D CD    1 
ATOM   9667  N  N     . PRO   C 2  358 ? 1.637   6.123   -34.042 1.00 64.62  ? 360 PRO   D N     1 
ATOM   9668  C  CA    . PRO   C 2  358 ? 2.327   5.622   -35.230 1.00 69.27  ? 360 PRO   D CA    1 
ATOM   9669  C  C     . PRO   C 2  358 ? 1.348   5.487   -36.387 1.00 85.17  ? 360 PRO   D C     1 
ATOM   9670  O  O     . PRO   C 2  358 ? 0.128   5.565   -36.220 1.00 81.53  ? 360 PRO   D O     1 
ATOM   9671  C  CB    . PRO   C 2  358 ? 2.882   4.266   -34.784 1.00 61.36  ? 360 PRO   D CB    1 
ATOM   9672  C  CG    . PRO   C 2  358 ? 2.039   3.855   -33.663 1.00 55.03  ? 360 PRO   D CG    1 
ATOM   9673  C  CD    . PRO   C 2  358 ? 1.497   5.093   -33.001 1.00 59.37  ? 360 PRO   D CD    1 
ATOM   9674  N  N     . ARG   C 2  359 ? 1.908   5.305   -37.585 1.00 93.19  ? 369 ARG   D N     1 
ATOM   9675  C  CA    . ARG   C 2  359 ? 1.099   5.048   -38.772 1.00 79.32  ? 369 ARG   D CA    1 
ATOM   9676  C  C     . ARG   C 2  359 ? 0.207   3.832   -38.534 1.00 81.56  ? 369 ARG   D C     1 
ATOM   9677  O  O     . ARG   C 2  359 ? 0.699   2.715   -38.330 1.00 72.05  ? 369 ARG   D O     1 
ATOM   9678  C  CB    . ARG   C 2  359 ? 2.012   4.825   -39.978 1.00 81.41  ? 369 ARG   D CB    1 
ATOM   9679  C  CG    . ARG   C 2  359 ? 1.395   5.113   -41.347 1.00 84.56  ? 369 ARG   D CG    1 
ATOM   9680  C  CD    . ARG   C 2  359 ? 2.332   4.610   -42.449 1.00 92.25  ? 369 ARG   D CD    1 
ATOM   9681  N  NE    . ARG   C 2  359 ? 1.934   5.021   -43.793 1.00 102.37 ? 369 ARG   D NE    1 
ATOM   9682  C  CZ    . ARG   C 2  359 ? 2.458   4.536   -44.915 1.00 102.20 ? 369 ARG   D CZ    1 
ATOM   9683  N  NH1   . ARG   C 2  359 ? 3.393   3.600   -44.895 1.00 98.95  ? 369 ARG   D NH1   1 
ATOM   9684  N  NH2   . ARG   C 2  359 ? 2.031   5.000   -46.087 1.00 97.74  ? 369 ARG   D NH2   1 
ATOM   9685  N  N     . GLY   C 2  360 ? -1.104  4.053   -38.533 1.00 66.30  ? 370 GLY   D N     1 
ATOM   9686  C  CA    . GLY   C 2  360 ? -2.026  2.959   -38.313 1.00 74.93  ? 370 GLY   D CA    1 
ATOM   9687  C  C     . GLY   C 2  360 ? -2.828  3.090   -37.035 1.00 79.68  ? 370 GLY   D C     1 
ATOM   9688  O  O     . GLY   C 2  360 ? -3.922  3.666   -37.036 1.00 75.00  ? 370 GLY   D O     1 
ATOM   9689  N  N     . LEU   C 2  361 ? -2.286  2.562   -35.938 1.00 75.63  ? 371 LEU   D N     1 
ATOM   9690  C  CA    . LEU   C 2  361 ? -2.988  2.569   -34.664 1.00 49.34  ? 371 LEU   D CA    1 
ATOM   9691  C  C     . LEU   C 2  361 ? -3.357  3.988   -34.250 1.00 60.39  ? 371 LEU   D C     1 
ATOM   9692  O  O     . LEU   C 2  361 ? -2.685  4.962   -34.603 1.00 66.29  ? 371 LEU   D O     1 
ATOM   9693  C  CB    . LEU   C 2  361 ? -2.125  1.919   -33.592 1.00 54.60  ? 371 LEU   D CB    1 
ATOM   9694  C  CG    . LEU   C 2  361 ? -1.093  0.922   -34.128 1.00 58.81  ? 371 LEU   D CG    1 
ATOM   9695  C  CD1   . LEU   C 2  361 ? 0.302   1.360   -33.724 1.00 60.61  ? 371 LEU   D CD1   1 
ATOM   9696  C  CD2   . LEU   C 2  361 ? -1.355  -0.518  -33.666 1.00 55.18  ? 371 LEU   D CD2   1 
ATOM   9697  N  N     . LYS   C 2  362 ? -4.449  4.102   -33.495 1.00 64.50  ? 372 LYS   D N     1 
ATOM   9698  C  CA    . LYS   C 2  362 ? -4.877  5.385   -32.950 1.00 72.13  ? 372 LYS   D CA    1 
ATOM   9699  C  C     . LYS   C 2  362 ? -4.226  5.688   -31.604 1.00 72.93  ? 372 LYS   D C     1 
ATOM   9700  O  O     . LYS   C 2  362 ? -4.279  6.839   -31.145 1.00 59.36  ? 372 LYS   D O     1 
ATOM   9701  C  CB    . LYS   C 2  362 ? -6.404  5.409   -32.819 1.00 66.96  ? 372 LYS   D CB    1 
ATOM   9702  C  CG    . LYS   C 2  362 ? -7.026  6.785   -32.964 1.00 62.96  ? 372 LYS   D CG    1 
ATOM   9703  C  CD    . LYS   C 2  362 ? -8.555  6.695   -32.969 1.00 82.95  ? 372 LYS   D CD    1 
ATOM   9704  C  CE    . LYS   C 2  362 ? -9.195  8.068   -33.142 1.00 87.74  ? 372 LYS   D CE    1 
ATOM   9705  N  NZ    . LYS   C 2  362 ? -10.579 8.119   -32.587 1.00 73.07  ? 372 LYS   D NZ    1 
ATOM   9706  N  N     . MET   C 2  363 ? -3.627  4.675   -30.968 1.00 71.22  ? 373 MET   D N     1 
ATOM   9707  C  CA    . MET   C 2  363 ? -2.800  4.844   -29.780 1.00 69.57  ? 373 MET   D CA    1 
ATOM   9708  C  C     . MET   C 2  363 ? -2.234  3.498   -29.326 1.00 61.47  ? 373 MET   D C     1 
ATOM   9709  O  O     . MET   C 2  363 ? -2.952  2.492   -29.326 1.00 49.59  ? 373 MET   D O     1 
ATOM   9710  C  CB    . MET   C 2  363 ? -3.606  5.524   -28.669 1.00 80.31  ? 373 MET   D CB    1 
ATOM   9711  C  CG    . MET   C 2  363 ? -4.715  4.690   -28.032 1.00 76.64  ? 373 MET   D CG    1 
ATOM   9712  S  SD    . MET   C 2  363 ? -5.631  5.696   -26.834 1.00 75.33  ? 373 MET   D SD    1 
ATOM   9713  C  CE    . MET   C 2  363 ? -6.579  6.742   -27.955 1.00 64.70  ? 373 MET   D CE    1 
ATOM   9714  N  N     . SER   C 2  364 ? -0.949  3.473   -28.941 1.00 55.62  ? 374 SER   D N     1 
ATOM   9715  C  CA    . SER   C 2  364 ? -0.221  2.239   -28.652 1.00 54.45  ? 374 SER   D CA    1 
ATOM   9716  C  C     . SER   C 2  364 ? 0.761   2.458   -27.506 1.00 57.71  ? 374 SER   D C     1 
ATOM   9717  O  O     . SER   C 2  364 ? 0.950   3.576   -27.018 1.00 56.99  ? 374 SER   D O     1 
ATOM   9718  C  CB    . SER   C 2  364 ? 0.541   1.734   -29.881 1.00 56.40  ? 374 SER   D CB    1 
ATOM   9719  O  OG    . SER   C 2  364 ? 1.348   2.767   -30.414 1.00 52.43  ? 374 SER   D OG    1 
ATOM   9720  N  N     . ALA   C 2  365 ? 1.418   1.372   -27.108 1.00 48.51  ? 375 ALA   D N     1 
ATOM   9721  C  CA    . ALA   C 2  365 ? 2.336   1.359   -25.985 1.00 42.81  ? 375 ALA   D CA    1 
ATOM   9722  C  C     . ALA   C 2  365 ? 3.600   0.608   -26.372 1.00 53.51  ? 375 ALA   D C     1 
ATOM   9723  O  O     . ALA   C 2  365 ? 3.525   -0.542  -26.809 1.00 57.54  ? 375 ALA   D O     1 
ATOM   9724  C  CB    . ALA   C 2  365 ? 1.689   0.691   -24.765 1.00 50.91  ? 375 ALA   D CB    1 
ATOM   9725  N  N     . THR   C 2  366 ? 4.758   1.244   -26.203 1.00 50.46  ? 376 THR   D N     1 
ATOM   9726  C  CA    . THR   C 2  366 ? 6.039   0.558   -26.280 1.00 38.97  ? 376 THR   D CA    1 
ATOM   9727  C  C     . THR   C 2  366 ? 6.623   0.380   -24.885 1.00 45.06  ? 376 THR   D C     1 
ATOM   9728  O  O     . THR   C 2  366 ? 6.460   1.233   -24.007 1.00 43.10  ? 376 THR   D O     1 
ATOM   9729  C  CB    . THR   C 2  366 ? 7.044   1.323   -27.137 1.00 46.41  ? 376 THR   D CB    1 
ATOM   9730  O  OG1   . THR   C 2  366 ? 6.558   1.435   -28.469 1.00 38.32  ? 376 THR   D OG1   1 
ATOM   9731  C  CG2   . THR   C 2  366 ? 8.377   0.597   -27.150 1.00 42.51  ? 376 THR   D CG2   1 
ATOM   9732  N  N     . PHE   C 2  367 ? 7.368   -0.704  -24.710 1.00 40.90  ? 377 PHE   D N     1 
ATOM   9733  C  CA    . PHE   C 2  367 ? 7.810   -1.150  -23.399 1.00 34.44  ? 377 PHE   D CA    1 
ATOM   9734  C  C     . PHE   C 2  367 ? 9.296   -1.460  -23.467 1.00 33.69  ? 377 PHE   D C     1 
ATOM   9735  O  O     . PHE   C 2  367 ? 9.695   -2.443  -24.087 1.00 41.66  ? 377 PHE   D O     1 
ATOM   9736  C  CB    . PHE   C 2  367 ? 7.009   -2.381  -22.965 1.00 41.63  ? 377 PHE   D CB    1 
ATOM   9737  C  CG    . PHE   C 2  367 ? 7.637   -3.167  -21.855 1.00 38.79  ? 377 PHE   D CG    1 
ATOM   9738  C  CD1   . PHE   C 2  367 ? 7.380   -2.853  -20.539 1.00 44.72  ? 377 PHE   D CD1   1 
ATOM   9739  C  CD2   . PHE   C 2  367 ? 8.479   -4.222  -22.127 1.00 42.33  ? 377 PHE   D CD2   1 
ATOM   9740  C  CE1   . PHE   C 2  367 ? 7.948   -3.581  -19.506 1.00 46.57  ? 377 PHE   D CE1   1 
ATOM   9741  C  CE2   . PHE   C 2  367 ? 9.057   -4.954  -21.104 1.00 54.06  ? 377 PHE   D CE2   1 
ATOM   9742  C  CZ    . PHE   C 2  367 ? 8.789   -4.635  -19.788 1.00 52.21  ? 377 PHE   D CZ    1 
ATOM   9743  N  N     . ILE   C 2  368 ? 10.118  -0.656  -22.814 1.00 31.94  ? 378 ILE   D N     1 
ATOM   9744  C  CA    . ILE   C 2  368 ? 11.518  -1.008  -22.612 1.00 34.22  ? 378 ILE   D CA    1 
ATOM   9745  C  C     . ILE   C 2  368 ? 11.678  -1.489  -21.176 1.00 39.21  ? 378 ILE   D C     1 
ATOM   9746  O  O     . ILE   C 2  368 ? 11.527  -0.706  -20.224 1.00 45.23  ? 378 ILE   D O     1 
ATOM   9747  C  CB    . ILE   C 2  368 ? 12.455  0.163   -22.916 1.00 30.67  ? 378 ILE   D CB    1 
ATOM   9748  C  CG1   . ILE   C 2  368 ? 12.108  0.773   -24.276 1.00 40.63  ? 378 ILE   D CG1   1 
ATOM   9749  C  CG2   . ILE   C 2  368 ? 13.878  -0.315  -22.904 1.00 29.14  ? 378 ILE   D CG2   1 
ATOM   9750  C  CD1   . ILE   C 2  368 ? 11.662  2.232   -24.229 1.00 33.63  ? 378 ILE   D CD1   1 
ATOM   9751  N  N     . GLY   C 2  369 ? 11.977  -2.771  -21.015 1.00 26.57  ? 379 GLY   D N     1 
ATOM   9752  C  CA    . GLY   C 2  369 ? 12.175  -3.366  -19.701 1.00 35.51  ? 379 GLY   D CA    1 
ATOM   9753  C  C     . GLY   C 2  369 ? 13.548  -3.992  -19.544 1.00 30.61  ? 379 GLY   D C     1 
ATOM   9754  O  O     . GLY   C 2  369 ? 14.047  -4.644  -20.457 1.00 38.32  ? 379 GLY   D O     1 
ATOM   9755  N  N     . ASN   C 2  370 ? 14.151  -3.787  -18.378 1.00 33.50  ? 380 ASN   D N     1 
ATOM   9756  C  CA    . ASN   C 2  370 ? 15.417  -4.403  -17.997 1.00 30.16  ? 380 ASN   D CA    1 
ATOM   9757  C  C     . ASN   C 2  370 ? 15.077  -5.402  -16.891 1.00 44.25  ? 380 ASN   D C     1 
ATOM   9758  O  O     . ASN   C 2  370 ? 15.267  -5.143  -15.702 1.00 41.83  ? 380 ASN   D O     1 
ATOM   9759  C  CB    . ASN   C 2  370 ? 16.415  -3.345  -17.557 1.00 22.99  ? 380 ASN   D CB    1 
ATOM   9760  C  CG    . ASN   C 2  370 ? 17.789  -3.915  -17.229 1.00 44.35  ? 380 ASN   D CG    1 
ATOM   9761  O  OD1   . ASN   C 2  370 ? 17.947  -5.118  -17.036 1.00 46.15  ? 380 ASN   D OD1   1 
ATOM   9762  N  ND2   . ASN   C 2  370 ? 18.793  -3.037  -17.135 1.00 38.38  ? 380 ASN   D ND2   1 
ATOM   9763  N  N     . SER   C 2  371 ? 14.529  -6.546  -17.295 1.00 44.93  ? 381 SER   D N     1 
ATOM   9764  C  CA    . SER   C 2  371 ? 14.142  -7.598  -16.361 1.00 49.47  ? 381 SER   D CA    1 
ATOM   9765  C  C     . SER   C 2  371 ? 15.278  -8.592  -16.148 1.00 46.12  ? 381 SER   D C     1 
ATOM   9766  O  O     . SER   C 2  371 ? 15.950  -8.990  -17.100 1.00 50.68  ? 381 SER   D O     1 
ATOM   9767  C  CB    . SER   C 2  371 ? 12.909  -8.337  -16.882 1.00 45.75  ? 381 SER   D CB    1 
ATOM   9768  O  OG    . SER   C 2  371 ? 12.874  -9.647  -16.358 1.00 49.22  ? 381 SER   D OG    1 
ATOM   9769  N  N     . THR   C 2  372 ? 15.489  -9.005  -14.894 1.00 47.83  ? 382 THR   D N     1 
ATOM   9770  C  CA    . THR   C 2  372 ? 16.473  -10.060 -14.649 1.00 51.01  ? 382 THR   D CA    1 
ATOM   9771  C  C     . THR   C 2  372 ? 16.092  -11.369 -15.333 1.00 54.30  ? 382 THR   D C     1 
ATOM   9772  O  O     . THR   C 2  372 ? 16.906  -12.303 -15.338 1.00 47.56  ? 382 THR   D O     1 
ATOM   9773  C  CB    . THR   C 2  372 ? 16.670  -10.326 -13.142 1.00 46.01  ? 382 THR   D CB    1 
ATOM   9774  O  OG1   . THR   C 2  372 ? 15.497  -10.935 -12.588 1.00 46.61  ? 382 THR   D OG1   1 
ATOM   9775  C  CG2   . THR   C 2  372 ? 16.955  -9.049  -12.402 1.00 45.72  ? 382 THR   D CG2   1 
ATOM   9776  N  N     . ALA   C 2  373 ? 14.875  -11.454 -15.894 1.00 49.05  ? 383 ALA   D N     1 
ATOM   9777  C  CA    . ALA   C 2  373 ? 14.431  -12.644 -16.608 1.00 45.55  ? 383 ALA   D CA    1 
ATOM   9778  C  C     . ALA   C 2  373 ? 15.105  -12.799 -17.965 1.00 56.13  ? 383 ALA   D C     1 
ATOM   9779  O  O     . ALA   C 2  373 ? 15.108  -13.904 -18.520 1.00 58.97  ? 383 ALA   D O     1 
ATOM   9780  C  CB    . ALA   C 2  373 ? 12.913  -12.615 -16.795 1.00 39.26  ? 383 ALA   D CB    1 
ATOM   9781  N  N     . ILE   C 2  374 ? 15.685  -11.732 -18.516 1.00 54.45  ? 384 ILE   D N     1 
ATOM   9782  C  CA    A ILE   C 2  374 ? 16.268  -11.838 -19.845 1.00 53.51  ? 384 ILE   D CA    1 
ATOM   9783  C  CA    B ILE   C 2  374 ? 16.329  -11.778 -19.826 0.00 53.23  ? 384 ILE   D CA    1 
ATOM   9784  C  C     . ILE   C 2  374 ? 17.346  -12.913 -19.899 1.00 52.26  ? 384 ILE   D C     1 
ATOM   9785  O  O     . ILE   C 2  374 ? 17.836  -13.244 -20.983 1.00 44.68  ? 384 ILE   D O     1 
ATOM   9786  C  CB    A ILE   C 2  374 ? 16.812  -10.472 -20.313 1.00 51.04  ? 384 ILE   D CB    1 
ATOM   9787  C  CB    B ILE   C 2  374 ? 16.995  -10.429 -20.155 0.00 51.08  ? 384 ILE   D CB    1 
ATOM   9788  C  CG1   A ILE   C 2  374 ? 16.745  -10.380 -21.841 1.00 45.98  ? 384 ILE   D CG1   1 
ATOM   9789  C  CG1   B ILE   C 2  374 ? 17.553  -10.440 -21.580 0.00 50.16  ? 384 ILE   D CG1   1 
ATOM   9790  C  CG2   A ILE   C 2  374 ? 18.220  -10.244 -19.775 1.00 49.60  ? 384 ILE   D CG2   1 
ATOM   9791  C  CG2   B ILE   C 2  374 ? 18.094  -10.119 -19.150 0.00 50.78  ? 384 ILE   D CG2   1 
ATOM   9792  C  CD1   A ILE   C 2  374 ? 17.355  -9.150  -22.404 1.00 44.58  ? 384 ILE   D CD1   1 
ATOM   9793  C  CD1   B ILE   C 2  374 ? 16.502  -10.669 -22.645 0.00 50.08  ? 384 ILE   D CD1   1 
ATOM   9794  N  N     . GLN   C 2  375 ? 17.694  -13.493 -18.747 1.00 45.90  ? 385 GLN   D N     1 
ATOM   9795  C  CA    . GLN   C 2  375 ? 18.579  -14.647 -18.711 1.00 51.92  ? 385 GLN   D CA    1 
ATOM   9796  C  C     . GLN   C 2  375 ? 17.932  -15.888 -19.315 1.00 61.26  ? 385 GLN   D C     1 
ATOM   9797  O  O     . GLN   C 2  375 ? 18.649  -16.801 -19.734 1.00 55.24  ? 385 GLN   D O     1 
ATOM   9798  C  CB    . GLN   C 2  375 ? 18.971  -14.945 -17.276 1.00 47.98  ? 385 GLN   D CB    1 
ATOM   9799  C  CG    . GLN   C 2  375 ? 17.747  -15.038 -16.380 1.00 48.69  ? 385 GLN   D CG    1 
ATOM   9800  C  CD    . GLN   C 2  375 ? 18.025  -15.793 -15.098 1.00 57.02  ? 385 GLN   D CD    1 
ATOM   9801  O  OE1   . GLN   C 2  375 ? 18.376  -16.983 -15.124 1.00 49.16  ? 385 GLN   D OE1   1 
ATOM   9802  N  NE2   . GLN   C 2  375 ? 17.879  -15.104 -13.959 1.00 46.56  ? 385 GLN   D NE2   1 
ATOM   9803  N  N     . GLU   C 2  376 ? 16.597  -15.962 -19.335 1.00 57.17  ? 386 GLU   D N     1 
ATOM   9804  C  CA    . GLU   C 2  376 ? 15.937  -17.045 -20.056 1.00 56.86  ? 386 GLU   D CA    1 
ATOM   9805  C  C     . GLU   C 2  376 ? 16.456  -17.130 -21.488 1.00 69.19  ? 386 GLU   D C     1 
ATOM   9806  O  O     . GLU   C 2  376 ? 16.692  -18.228 -22.012 1.00 71.11  ? 386 GLU   D O     1 
ATOM   9807  C  CB    . GLU   C 2  376 ? 14.416  -16.842 -20.043 1.00 56.95  ? 386 GLU   D CB    1 
ATOM   9808  C  CG    . GLU   C 2  376 ? 13.751  -17.166 -18.701 1.00 54.97  ? 386 GLU   D CG    1 
ATOM   9809  C  CD    . GLU   C 2  376 ? 12.223  -17.102 -18.737 1.00 54.35  ? 386 GLU   D CD    1 
ATOM   9810  O  OE1   . GLU   C 2  376 ? 11.635  -16.326 -19.532 1.00 44.21  ? 386 GLU   D OE1   1 
ATOM   9811  O  OE2   . GLU   C 2  376 ? 11.610  -17.842 -17.941 1.00 64.05  ? 386 GLU   D OE2   1 
ATOM   9812  N  N     . LEU   C 2  377 ? 16.645  -15.972 -22.129 1.00 66.17  ? 387 LEU   D N     1 
ATOM   9813  C  CA    . LEU   C 2  377 ? 17.190  -15.914 -23.482 1.00 53.30  ? 387 LEU   D CA    1 
ATOM   9814  C  C     . LEU   C 2  377 ? 18.655  -16.343 -23.504 1.00 54.52  ? 387 LEU   D C     1 
ATOM   9815  O  O     . LEU   C 2  377 ? 19.037  -17.259 -24.240 1.00 62.33  ? 387 LEU   D O     1 
ATOM   9816  C  CB    . LEU   C 2  377 ? 17.011  -14.500 -24.034 1.00 50.55  ? 387 LEU   D CB    1 
ATOM   9817  C  CG    . LEU   C 2  377 ? 17.754  -14.006 -25.271 1.00 54.38  ? 387 LEU   D CG    1 
ATOM   9818  C  CD1   . LEU   C 2  377 ? 17.210  -12.634 -25.655 1.00 56.08  ? 387 LEU   D CD1   1 
ATOM   9819  C  CD2   . LEU   C 2  377 ? 19.267  -13.931 -25.044 1.00 54.16  ? 387 LEU   D CD2   1 
ATOM   9820  N  N     . PHE   C 2  378 ? 19.498  -15.696 -22.701 1.00 45.27  ? 388 PHE   D N     1 
ATOM   9821  C  CA    . PHE   C 2  378 ? 20.897  -16.105 -22.648 1.00 55.91  ? 388 PHE   D CA    1 
ATOM   9822  C  C     . PHE   C 2  378 ? 21.050  -17.553 -22.222 1.00 55.88  ? 388 PHE   D C     1 
ATOM   9823  O  O     . PHE   C 2  378 ? 22.090  -18.158 -22.491 1.00 61.21  ? 388 PHE   D O     1 
ATOM   9824  C  CB    . PHE   C 2  378 ? 21.701  -15.199 -21.709 1.00 52.77  ? 388 PHE   D CB    1 
ATOM   9825  C  CG    . PHE   C 2  378 ? 21.794  -13.775 -22.188 1.00 59.99  ? 388 PHE   D CG    1 
ATOM   9826  C  CD1   . PHE   C 2  378 ? 22.332  -13.487 -23.437 1.00 54.28  ? 388 PHE   D CD1   1 
ATOM   9827  C  CD2   . PHE   C 2  378 ? 21.329  -12.729 -21.399 1.00 54.43  ? 388 PHE   D CD2   1 
ATOM   9828  C  CE1   . PHE   C 2  378 ? 22.415  -12.195 -23.893 1.00 49.35  ? 388 PHE   D CE1   1 
ATOM   9829  C  CE2   . PHE   C 2  378 ? 21.404  -11.430 -21.846 1.00 53.02  ? 388 PHE   D CE2   1 
ATOM   9830  C  CZ    . PHE   C 2  378 ? 21.952  -11.161 -23.098 1.00 63.55  ? 388 PHE   D CZ    1 
ATOM   9831  N  N     . LYS   C 2  379 ? 20.049  -18.120 -21.553 1.00 63.33  ? 389 LYS   D N     1 
ATOM   9832  C  CA    . LYS   C 2  379 ? 20.105  -19.539 -21.220 1.00 63.02  ? 389 LYS   D CA    1 
ATOM   9833  C  C     . LYS   C 2  379 ? 19.886  -20.385 -22.462 1.00 61.61  ? 389 LYS   D C     1 
ATOM   9834  O  O     . LYS   C 2  379 ? 20.584  -21.384 -22.676 1.00 55.32  ? 389 LYS   D O     1 
ATOM   9835  C  CB    . LYS   C 2  379 ? 19.057  -19.873 -20.158 1.00 55.83  ? 389 LYS   D CB    1 
ATOM   9836  C  CG    . LYS   C 2  379 ? 19.594  -20.055 -18.762 1.00 55.53  ? 389 LYS   D CG    1 
ATOM   9837  C  CD    . LYS   C 2  379 ? 18.480  -19.839 -17.747 1.00 60.29  ? 389 LYS   D CD    1 
ATOM   9838  C  CE    . LYS   C 2  379 ? 18.946  -20.143 -16.333 1.00 55.72  ? 389 LYS   D CE    1 
ATOM   9839  N  NZ    . LYS   C 2  379 ? 20.395  -19.866 -16.185 1.00 57.49  ? 389 LYS   D NZ    1 
ATOM   9840  N  N     . ARG   C 2  380 ? 18.912  -19.992 -23.287 1.00 62.59  ? 390 ARG   D N     1 
ATOM   9841  C  CA    . ARG   C 2  380 ? 18.613  -20.731 -24.507 1.00 60.89  ? 390 ARG   D CA    1 
ATOM   9842  C  C     . ARG   C 2  380 ? 19.814  -20.745 -25.444 1.00 67.02  ? 390 ARG   D C     1 
ATOM   9843  O  O     . ARG   C 2  380 ? 20.155  -21.787 -26.016 1.00 67.95  ? 390 ARG   D O     1 
ATOM   9844  C  CB    . ARG   C 2  380 ? 17.389  -20.120 -25.195 1.00 54.35  ? 390 ARG   D CB    1 
ATOM   9845  C  CG    . ARG   C 2  380 ? 16.869  -20.924 -26.360 1.00 50.78  ? 390 ARG   D CG    1 
ATOM   9846  C  CD    . ARG   C 2  380 ? 15.573  -20.347 -26.879 1.00 53.85  ? 390 ARG   D CD    1 
ATOM   9847  N  NE    . ARG   C 2  380 ? 15.783  -19.263 -27.828 1.00 61.36  ? 390 ARG   D NE    1 
ATOM   9848  C  CZ    . ARG   C 2  380 ? 15.776  -17.976 -27.513 1.00 71.13  ? 390 ARG   D CZ    1 
ATOM   9849  N  NH1   . ARG   C 2  380 ? 15.600  -17.571 -26.263 1.00 78.28  ? 390 ARG   D NH1   1 
ATOM   9850  N  NH2   . ARG   C 2  380 ? 15.944  -17.072 -28.475 1.00 61.85  ? 390 ARG   D NH2   1 
ATOM   9851  N  N     . ILE   C 2  381 ? 20.476  -19.598 -25.609 1.00 66.78  ? 391 ILE   D N     1 
ATOM   9852  C  CA    . ILE   C 2  381 ? 21.681  -19.559 -26.430 1.00 55.45  ? 391 ILE   D CA    1 
ATOM   9853  C  C     . ILE   C 2  381 ? 22.767  -20.431 -25.818 1.00 57.26  ? 391 ILE   D C     1 
ATOM   9854  O  O     . ILE   C 2  381 ? 23.408  -21.229 -26.508 1.00 64.75  ? 391 ILE   D O     1 
ATOM   9855  C  CB    . ILE   C 2  381 ? 22.172  -18.117 -26.611 1.00 48.30  ? 391 ILE   D CB    1 
ATOM   9856  C  CG1   . ILE   C 2  381 ? 21.464  -17.453 -27.792 1.00 51.59  ? 391 ILE   D CG1   1 
ATOM   9857  C  CG2   . ILE   C 2  381 ? 23.690  -18.123 -26.798 1.00 55.33  ? 391 ILE   D CG2   1 
ATOM   9858  C  CD1   . ILE   C 2  381 ? 19.998  -17.747 -27.865 1.00 51.39  ? 391 ILE   D CD1   1 
ATOM   9859  N  N     . SER   C 2  382 ? 22.989  -20.294 -24.511 1.00 50.09  ? 392 SER   D N     1 
ATOM   9860  C  CA    . SER   C 2  382 ? 24.143  -20.936 -23.905 1.00 53.30  ? 392 SER   D CA    1 
ATOM   9861  C  C     . SER   C 2  382 ? 24.060  -22.454 -23.962 1.00 65.48  ? 392 SER   D C     1 
ATOM   9862  O  O     . SER   C 2  382 ? 25.079  -23.122 -23.756 1.00 66.62  ? 392 SER   D O     1 
ATOM   9863  C  CB    . SER   C 2  382 ? 24.311  -20.482 -22.465 1.00 56.39  ? 392 SER   D CB    1 
ATOM   9864  O  OG    . SER   C 2  382 ? 25.590  -20.858 -21.990 1.00 64.13  ? 392 SER   D OG    1 
ATOM   9865  N  N     . GLU   C 2  383 ? 22.882  -23.015 -24.233 1.00 68.74  ? 393 GLU   D N     1 
ATOM   9866  C  CA    . GLU   C 2  383 ? 22.758  -24.461 -24.397 1.00 71.63  ? 393 GLU   D CA    1 
ATOM   9867  C  C     . GLU   C 2  383 ? 23.059  -24.860 -25.838 1.00 70.38  ? 393 GLU   D C     1 
ATOM   9868  O  O     . GLU   C 2  383 ? 24.026  -25.582 -26.101 1.00 74.33  ? 393 GLU   D O     1 
ATOM   9869  C  CB    . GLU   C 2  383 ? 21.363  -24.930 -23.980 1.00 69.25  ? 393 GLU   D CB    1 
ATOM   9870  C  CG    . GLU   C 2  383 ? 21.372  -26.269 -23.271 1.00 74.60  ? 393 GLU   D CG    1 
ATOM   9871  C  CD    . GLU   C 2  383 ? 20.104  -26.504 -22.483 1.00 87.67  ? 393 GLU   D CD    1 
ATOM   9872  O  OE1   . GLU   C 2  383 ? 19.115  -25.771 -22.731 1.00 83.90  ? 393 GLU   D OE1   1 
ATOM   9873  O  OE2   . GLU   C 2  383 ? 20.100  -27.411 -21.616 1.00 90.76  ? 393 GLU   D OE2   1 
ATOM   9874  N  N     . GLN   C 2  384 ? 22.245  -24.380 -26.777 1.00 64.02  ? 394 GLN   D N     1 
ATOM   9875  C  CA    . GLN   C 2  384 ? 22.551  -24.447 -28.201 1.00 61.27  ? 394 GLN   D CA    1 
ATOM   9876  C  C     . GLN   C 2  384 ? 24.051  -24.279 -28.471 1.00 68.27  ? 394 GLN   D C     1 
ATOM   9877  O  O     . GLN   C 2  384 ? 24.606  -24.937 -29.356 1.00 70.34  ? 394 GLN   D O     1 
ATOM   9878  C  CB    . GLN   C 2  384 ? 21.729  -23.388 -28.938 1.00 46.42  ? 394 GLN   D CB    1 
ATOM   9879  C  CG    . GLN   C 2  384 ? 20.260  -23.461 -28.589 1.00 49.46  ? 394 GLN   D CG    1 
ATOM   9880  C  CD    . GLN   C 2  384 ? 19.424  -22.389 -29.269 1.00 64.23  ? 394 GLN   D CD    1 
ATOM   9881  O  OE1   . GLN   C 2  384 ? 18.345  -22.666 -29.798 1.00 60.12  ? 394 GLN   D OE1   1 
ATOM   9882  N  NE2   . GLN   C 2  384 ? 19.906  -21.156 -29.240 1.00 66.41  ? 394 GLN   D NE2   1 
ATOM   9883  N  N     . PHE   C 2  385 ? 24.718  -23.404 -27.714 1.00 65.77  ? 395 PHE   D N     1 
ATOM   9884  C  CA    . PHE   C 2  385 ? 26.170  -23.290 -27.805 1.00 66.54  ? 395 PHE   D CA    1 
ATOM   9885  C  C     . PHE   C 2  385 ? 26.854  -24.526 -27.220 1.00 72.74  ? 395 PHE   D C     1 
ATOM   9886  O  O     . PHE   C 2  385 ? 27.762  -25.097 -27.839 1.00 72.50  ? 395 PHE   D O     1 
ATOM   9887  C  CB    . PHE   C 2  385 ? 26.633  -22.007 -27.093 1.00 60.84  ? 395 PHE   D CB    1 
ATOM   9888  C  CG    . PHE   C 2  385 ? 28.137  -21.878 -26.939 1.00 51.70  ? 395 PHE   D CG    1 
ATOM   9889  C  CD1   . PHE   C 2  385 ? 28.809  -22.548 -25.923 1.00 45.69  ? 395 PHE   D CD1   1 
ATOM   9890  C  CD2   . PHE   C 2  385 ? 28.870  -21.061 -27.796 1.00 48.85  ? 395 PHE   D CD2   1 
ATOM   9891  C  CE1   . PHE   C 2  385 ? 30.186  -22.419 -25.776 1.00 58.32  ? 395 PHE   D CE1   1 
ATOM   9892  C  CE2   . PHE   C 2  385 ? 30.244  -20.924 -27.652 1.00 43.20  ? 395 PHE   D CE2   1 
ATOM   9893  C  CZ    . PHE   C 2  385 ? 30.903  -21.607 -26.640 1.00 54.47  ? 395 PHE   D CZ    1 
ATOM   9894  N  N     . THR   C 2  386 ? 26.427  -24.956 -26.023 1.00 69.19  ? 396 THR   D N     1 
ATOM   9895  C  CA    . THR   C 2  386 ? 27.087  -26.046 -25.309 1.00 71.82  ? 396 THR   D CA    1 
ATOM   9896  C  C     . THR   C 2  386 ? 26.713  -27.430 -25.842 1.00 78.94  ? 396 THR   D C     1 
ATOM   9897  O  O     . THR   C 2  386 ? 27.407  -28.406 -25.527 1.00 84.38  ? 396 THR   D O     1 
ATOM   9898  C  CB    . THR   C 2  386 ? 26.765  -25.955 -23.812 1.00 76.67  ? 396 THR   D CB    1 
ATOM   9899  O  OG1   . THR   C 2  386 ? 27.664  -26.787 -23.062 1.00 71.02  ? 396 THR   D OG1   1 
ATOM   9900  C  CG2   . THR   C 2  386 ? 25.325  -26.390 -23.551 1.00 73.34  ? 396 THR   D CG2   1 
ATOM   9901  N  N     . ALA   C 2  387 ? 25.635  -27.543 -26.630 1.00 71.03  ? 397 ALA   D N     1 
ATOM   9902  C  CA    . ALA   C 2  387 ? 25.316  -28.753 -27.386 1.00 70.79  ? 397 ALA   D CA    1 
ATOM   9903  C  C     . ALA   C 2  387 ? 26.110  -28.854 -28.684 1.00 81.31  ? 397 ALA   D C     1 
ATOM   9904  O  O     . ALA   C 2  387 ? 25.702  -29.570 -29.610 1.00 82.33  ? 397 ALA   D O     1 
ATOM   9905  C  CB    . ALA   C 2  387 ? 23.817  -28.815 -27.694 1.00 72.10  ? 397 ALA   D CB    1 
ATOM   9906  N  N     . MET   C 2  388 ? 27.219  -28.123 -28.769 1.00 77.04  ? 398 MET   D N     1 
ATOM   9907  C  CA    . MET   C 2  388 ? 28.106  -28.150 -29.917 1.00 71.64  ? 398 MET   D CA    1 
ATOM   9908  C  C     . MET   C 2  388 ? 29.538  -28.105 -29.413 1.00 81.81  ? 398 MET   D C     1 
ATOM   9909  O  O     . MET   C 2  388 ? 30.380  -28.902 -29.837 1.00 85.90  ? 398 MET   D O     1 
ATOM   9910  C  CB    . MET   C 2  388 ? 27.841  -26.974 -30.857 1.00 63.63  ? 398 MET   D CB    1 
ATOM   9911  C  CG    . MET   C 2  388 ? 26.411  -26.839 -31.314 1.00 60.87  ? 398 MET   D CG    1 
ATOM   9912  S  SD    . MET   C 2  388 ? 26.302  -25.943 -32.871 1.00 82.39  ? 398 MET   D SD    1 
ATOM   9913  C  CE    . MET   C 2  388 ? 24.526  -25.961 -33.124 1.00 69.87  ? 398 MET   D CE    1 
ATOM   9914  N  N     . PHE   C 2  389 ? 29.815  -27.186 -28.486 1.00 76.79  ? 399 PHE   D N     1 
ATOM   9915  C  CA    . PHE   C 2  389 ? 31.191  -26.965 -28.057 1.00 82.66  ? 399 PHE   D CA    1 
ATOM   9916  C  C     . PHE   C 2  389 ? 31.759  -28.171 -27.312 1.00 85.36  ? 399 PHE   D C     1 
ATOM   9917  O  O     . PHE   C 2  389 ? 32.982  -28.359 -27.279 1.00 79.75  ? 399 PHE   D O     1 
ATOM   9918  C  CB    . PHE   C 2  389 ? 31.270  -25.705 -27.199 1.00 69.84  ? 399 PHE   D CB    1 
ATOM   9919  C  CG    . PHE   C 2  389 ? 32.663  -25.322 -26.823 1.00 70.06  ? 399 PHE   D CG    1 
ATOM   9920  C  CD1   . PHE   C 2  389 ? 33.526  -24.794 -27.771 1.00 70.85  ? 399 PHE   D CD1   1 
ATOM   9921  C  CD2   . PHE   C 2  389 ? 33.114  -25.483 -25.519 1.00 75.83  ? 399 PHE   D CD2   1 
ATOM   9922  C  CE1   . PHE   C 2  389 ? 34.815  -24.434 -27.428 1.00 69.09  ? 399 PHE   D CE1   1 
ATOM   9923  C  CE2   . PHE   C 2  389 ? 34.406  -25.123 -25.160 1.00 73.43  ? 399 PHE   D CE2   1 
ATOM   9924  C  CZ    . PHE   C 2  389 ? 35.258  -24.595 -26.117 1.00 76.16  ? 399 PHE   D CZ    1 
ATOM   9925  N  N     . ARG   C 2  390 ? 30.903  -28.993 -26.703 1.00 83.82  ? 400 ARG   D N     1 
ATOM   9926  C  CA    . ARG   C 2  390 ? 31.356  -30.294 -26.224 1.00 88.24  ? 400 ARG   D CA    1 
ATOM   9927  C  C     . ARG   C 2  390 ? 31.997  -31.092 -27.358 1.00 97.21  ? 400 ARG   D C     1 
ATOM   9928  O  O     . ARG   C 2  390 ? 33.172  -31.481 -27.285 1.00 88.04  ? 400 ARG   D O     1 
ATOM   9929  C  CB    . ARG   C 2  390 ? 30.179  -31.061 -25.625 1.00 88.79  ? 400 ARG   D CB    1 
ATOM   9930  C  CG    . ARG   C 2  390 ? 30.245  -31.232 -24.131 1.00 95.00  ? 400 ARG   D CG    1 
ATOM   9931  C  CD    . ARG   C 2  390 ? 29.613  -30.063 -23.423 1.00 103.38 ? 400 ARG   D CD    1 
ATOM   9932  N  NE    . ARG   C 2  390 ? 28.934  -30.495 -22.205 1.00 118.24 ? 400 ARG   D NE    1 
ATOM   9933  C  CZ    . ARG   C 2  390 ? 27.680  -30.926 -22.158 1.00 108.35 ? 400 ARG   D CZ    1 
ATOM   9934  N  NH1   . ARG   C 2  390 ? 26.929  -30.992 -23.246 1.00 98.61  ? 400 ARG   D NH1   1 
ATOM   9935  N  NH2   . ARG   C 2  390 ? 27.165  -31.299 -20.989 1.00 100.21 ? 400 ARG   D NH2   1 
ATOM   9936  N  N     . ARG   C 2  391 ? 31.218  -31.324 -28.428 1.00 98.21  ? 401 ARG   D N     1 
ATOM   9937  C  CA    . ARG   C 2  391 ? 31.536  -32.052 -29.652 1.00 84.26  ? 401 ARG   D CA    1 
ATOM   9938  C  C     . ARG   C 2  391 ? 32.524  -31.334 -30.565 1.00 87.41  ? 401 ARG   D C     1 
ATOM   9939  O  O     . ARG   C 2  391 ? 32.766  -31.827 -31.667 1.00 94.83  ? 401 ARG   D O     1 
ATOM   9940  C  CB    . ARG   C 2  391 ? 30.250  -32.291 -30.460 1.00 88.03  ? 401 ARG   D CB    1 
ATOM   9941  C  CG    . ARG   C 2  391 ? 29.124  -32.972 -29.694 1.00 91.70  ? 401 ARG   D CG    1 
ATOM   9942  C  CD    . ARG   C 2  391 ? 27.772  -32.464 -30.167 1.00 84.16  ? 401 ARG   D CD    1 
ATOM   9943  N  NE    . ARG   C 2  391 ? 27.735  -32.291 -31.613 1.00 75.19  ? 401 ARG   D NE    1 
ATOM   9944  C  CZ    . ARG   C 2  391 ? 26.722  -31.754 -32.278 1.00 84.61  ? 401 ARG   D CZ    1 
ATOM   9945  N  NH1   . ARG   C 2  391 ? 25.651  -31.291 -31.652 1.00 88.66  ? 401 ARG   D NH1   1 
ATOM   9946  N  NH2   . ARG   C 2  391 ? 26.782  -31.680 -33.605 1.00 80.34  ? 401 ARG   D NH2   1 
ATOM   9947  N  N     . LYS   C 2  392 ? 33.068  -30.185 -30.160 1.00 83.23  ? 402 LYS   D N     1 
ATOM   9948  C  CA    . LYS   C 2  392 ? 33.912  -29.363 -31.034 1.00 74.17  ? 402 LYS   D CA    1 
ATOM   9949  C  C     . LYS   C 2  392 ? 33.301  -29.195 -32.431 1.00 69.16  ? 402 LYS   D C     1 
ATOM   9950  O  O     . LYS   C 2  392 ? 33.991  -28.812 -33.380 1.00 78.51  ? 402 LYS   D O     1 
ATOM   9951  C  CB    . LYS   C 2  392 ? 35.327  -29.941 -31.124 1.00 77.78  ? 402 LYS   D CB    1 
ATOM   9952  C  CG    . LYS   C 2  392 ? 36.281  -29.151 -32.013 1.00 94.21  ? 402 LYS   D CG    1 
ATOM   9953  C  CD    . LYS   C 2  392 ? 37.373  -30.050 -32.590 1.00 95.73  ? 402 LYS   D CD    1 
ATOM   9954  C  CE    . LYS   C 2  392 ? 38.064  -29.400 -33.773 1.00 80.77  ? 402 LYS   D CE    1 
ATOM   9955  N  NZ    . LYS   C 2  392 ? 38.953  -30.376 -34.450 1.00 95.67  ? 402 LYS   D NZ    1 
ATOM   9956  N  N     . ALA   C 2  393 ? 31.998  -29.437 -32.565 1.00 64.39  ? 403 ALA   D N     1 
ATOM   9957  C  CA    . ALA   C 2  393 ? 31.334  -29.413 -33.866 1.00 82.30  ? 403 ALA   D CA    1 
ATOM   9958  C  C     . ALA   C 2  393 ? 31.623  -28.129 -34.636 1.00 78.19  ? 403 ALA   D C     1 
ATOM   9959  O  O     . ALA   C 2  393 ? 31.457  -27.023 -34.116 1.00 78.33  ? 403 ALA   D O     1 
ATOM   9960  C  CB    . ALA   C 2  393 ? 29.822  -29.581 -33.679 1.00 80.59  ? 403 ALA   D CB    1 
ATOM   9961  N  N     . PHE   C 2  394 ? 32.044  -28.279 -35.888 1.00 76.09  ? 404 PHE   D N     1 
ATOM   9962  C  CA    . PHE   C 2  394 ? 32.253  -27.159 -36.795 1.00 76.74  ? 404 PHE   D CA    1 
ATOM   9963  C  C     . PHE   C 2  394 ? 33.206  -26.122 -36.222 1.00 71.71  ? 404 PHE   D C     1 
ATOM   9964  O  O     . PHE   C 2  394 ? 33.335  -25.024 -36.784 1.00 72.11  ? 404 PHE   D O     1 
ATOM   9965  C  CB    . PHE   C 2  394 ? 30.921  -26.502 -37.178 1.00 79.36  ? 404 PHE   D CB    1 
ATOM   9966  C  CG    . PHE   C 2  394 ? 29.818  -27.485 -37.503 1.00 76.13  ? 404 PHE   D CG    1 
ATOM   9967  C  CD1   . PHE   C 2  394 ? 29.102  -28.119 -36.491 1.00 74.00  ? 404 PHE   D CD1   1 
ATOM   9968  C  CD2   . PHE   C 2  394 ? 29.473  -27.741 -38.822 1.00 74.05  ? 404 PHE   D CD2   1 
ATOM   9969  C  CE1   . PHE   C 2  394 ? 28.083  -29.005 -36.785 1.00 76.19  ? 404 PHE   D CE1   1 
ATOM   9970  C  CE2   . PHE   C 2  394 ? 28.453  -28.629 -39.128 1.00 82.22  ? 404 PHE   D CE2   1 
ATOM   9971  C  CZ    . PHE   C 2  394 ? 27.754  -29.261 -38.106 1.00 85.55  ? 404 PHE   D CZ    1 
ATOM   9972  N  N     . LEU   C 2  395 ? 33.874  -26.433 -35.115 1.00 61.33  ? 405 LEU   D N     1 
ATOM   9973  C  CA    . LEU   C 2  395 ? 34.811  -25.546 -34.433 1.00 75.91  ? 405 LEU   D CA    1 
ATOM   9974  C  C     . LEU   C 2  395 ? 36.116  -25.294 -35.228 1.00 80.80  ? 405 LEU   D C     1 
ATOM   9975  O  O     . LEU   C 2  395 ? 37.055  -24.675 -34.705 1.00 75.61  ? 405 LEU   D O     1 
ATOM   9976  C  CB    . LEU   C 2  395 ? 35.152  -26.113 -33.056 1.00 76.46  ? 405 LEU   D CB    1 
ATOM   9977  C  CG    . LEU   C 2  395 ? 35.630  -25.080 -32.042 1.00 74.13  ? 405 LEU   D CG    1 
ATOM   9978  C  CD1   . LEU   C 2  395 ? 34.436  -24.419 -31.366 1.00 72.60  ? 405 LEU   D CD1   1 
ATOM   9979  C  CD2   . LEU   C 2  395 ? 36.559  -25.725 -31.030 1.00 68.11  ? 405 LEU   D CD2   1 
ATOM   9980  N  N     . HIS   C 2  396 ? 36.198  -25.777 -36.465 1.00 82.93  ? 406 HIS   D N     1 
ATOM   9981  C  CA    . HIS   C 2  396 ? 37.322  -25.507 -37.347 1.00 76.87  ? 406 HIS   D CA    1 
ATOM   9982  C  C     . HIS   C 2  396 ? 37.052  -24.345 -38.287 1.00 77.48  ? 406 HIS   D C     1 
ATOM   9983  O  O     . HIS   C 2  396 ? 38.001  -23.682 -38.721 1.00 73.07  ? 406 HIS   D O     1 
ATOM   9984  C  CB    . HIS   C 2  396 ? 37.671  -26.763 -38.161 1.00 86.80  ? 406 HIS   D CB    1 
ATOM   9985  C  CG    . HIS   C 2  396 ? 36.514  -27.331 -38.933 1.00 87.99  ? 406 HIS   D CG    1 
ATOM   9986  N  ND1   . HIS   C 2  396 ? 36.029  -26.750 -40.088 1.00 90.54  ? 406 HIS   D ND1   1 
ATOM   9987  C  CD2   . HIS   C 2  396 ? 35.747  -28.427 -38.714 1.00 76.45  ? 406 HIS   D CD2   1 
ATOM   9988  C  CE1   . HIS   C 2  396 ? 35.013  -27.461 -40.545 1.00 86.45  ? 406 HIS   D CE1   1 
ATOM   9989  N  NE2   . HIS   C 2  396 ? 34.820  -28.482 -39.728 1.00 86.47  ? 406 HIS   D NE2   1 
ATOM   9990  N  N     . TRP   C 2  397 ? 35.777  -24.074 -38.605 1.00 67.78  ? 407 TRP   D N     1 
ATOM   9991  C  CA    . TRP   C 2  397 ? 35.440  -22.819 -39.266 1.00 74.31  ? 407 TRP   D CA    1 
ATOM   9992  C  C     . TRP   C 2  397 ? 36.065  -21.635 -38.553 1.00 74.18  ? 407 TRP   D C     1 
ATOM   9993  O  O     . TRP   C 2  397 ? 36.157  -20.550 -39.140 1.00 71.53  ? 407 TRP   D O     1 
ATOM   9994  C  CB    . TRP   C 2  397 ? 33.925  -22.572 -39.308 1.00 75.87  ? 407 TRP   D CB    1 
ATOM   9995  C  CG    . TRP   C 2  397 ? 33.111  -23.306 -40.340 1.00 80.59  ? 407 TRP   D CG    1 
ATOM   9996  C  CD1   . TRP   C 2  397 ? 33.480  -24.397 -41.068 1.00 77.75  ? 407 TRP   D CD1   1 
ATOM   9997  C  CD2   . TRP   C 2  397 ? 31.763  -22.993 -40.739 1.00 83.97  ? 407 TRP   D CD2   1 
ATOM   9998  N  NE1   . TRP   C 2  397 ? 32.448  -24.783 -41.895 1.00 78.58  ? 407 TRP   D NE1   1 
ATOM   9999  C  CE2   . TRP   C 2  397 ? 31.384  -23.936 -41.711 1.00 82.43  ? 407 TRP   D CE2   1 
ATOM   10000 C  CE3   . TRP   C 2  397 ? 30.843  -22.003 -40.368 1.00 77.98  ? 407 TRP   D CE3   1 
ATOM   10001 C  CZ2   . TRP   C 2  397 ? 30.120  -23.916 -42.322 1.00 81.79  ? 407 TRP   D CZ2   1 
ATOM   10002 C  CZ3   . TRP   C 2  397 ? 29.584  -21.988 -40.979 1.00 70.25  ? 407 TRP   D CZ3   1 
ATOM   10003 C  CH2   . TRP   C 2  397 ? 29.238  -22.936 -41.940 1.00 55.96  ? 407 TRP   D CH2   1 
ATOM   10004 N  N     . TYR   C 2  398 ? 36.470  -21.811 -37.292 1.00 73.81  ? 408 TYR   D N     1 
ATOM   10005 C  CA    . TYR   C 2  398 ? 36.922  -20.716 -36.443 1.00 72.59  ? 408 TYR   D CA    1 
ATOM   10006 C  C     . TYR   C 2  398 ? 38.407  -20.755 -36.131 1.00 61.65  ? 408 TYR   D C     1 
ATOM   10007 O  O     . TYR   C 2  398 ? 39.036  -19.696 -36.084 1.00 61.83  ? 408 TYR   D O     1 
ATOM   10008 C  CB    . TYR   C 2  398 ? 36.122  -20.688 -35.129 1.00 74.91  ? 408 TYR   D CB    1 
ATOM   10009 C  CG    . TYR   C 2  398 ? 34.651  -20.411 -35.344 1.00 67.00  ? 408 TYR   D CG    1 
ATOM   10010 C  CD1   . TYR   C 2  398 ? 34.229  -19.215 -35.900 1.00 63.57  ? 408 TYR   D CD1   1 
ATOM   10011 C  CD2   . TYR   C 2  398 ? 33.690  -21.354 -35.013 1.00 68.58  ? 408 TYR   D CD2   1 
ATOM   10012 C  CE1   . TYR   C 2  398 ? 32.888  -18.964 -36.116 1.00 71.56  ? 408 TYR   D CE1   1 
ATOM   10013 C  CE2   . TYR   C 2  398 ? 32.348  -21.113 -35.223 1.00 70.00  ? 408 TYR   D CE2   1 
ATOM   10014 C  CZ    . TYR   C 2  398 ? 31.952  -19.918 -35.776 1.00 69.88  ? 408 TYR   D CZ    1 
ATOM   10015 O  OH    . TYR   C 2  398 ? 30.616  -19.672 -35.984 1.00 63.02  ? 408 TYR   D OH    1 
ATOM   10016 N  N     . THR   C 2  399 ? 38.999  -21.930 -35.906 1.00 63.36  ? 409 THR   D N     1 
ATOM   10017 C  CA    . THR   C 2  399 ? 40.454  -21.970 -35.805 1.00 60.42  ? 409 THR   D CA    1 
ATOM   10018 C  C     . THR   C 2  399 ? 41.088  -21.676 -37.153 1.00 65.90  ? 409 THR   D C     1 
ATOM   10019 O  O     . THR   C 2  399 ? 42.141  -21.029 -37.223 1.00 58.54  ? 409 THR   D O     1 
ATOM   10020 C  CB    . THR   C 2  399 ? 40.933  -23.322 -35.300 1.00 61.48  ? 409 THR   D CB    1 
ATOM   10021 O  OG1   . THR   C 2  399 ? 39.898  -23.933 -34.530 1.00 65.83  ? 409 THR   D OG1   1 
ATOM   10022 C  CG2   . THR   C 2  399 ? 42.179  -23.147 -34.440 1.00 59.48  ? 409 THR   D CG2   1 
ATOM   10023 N  N     . GLY   C 2  400 ? 40.442  -22.132 -38.234 1.00 67.91  ? 410 GLY   D N     1 
ATOM   10024 C  CA    . GLY   C 2  400 ? 40.978  -21.932 -39.570 1.00 67.66  ? 410 GLY   D CA    1 
ATOM   10025 C  C     . GLY   C 2  400 ? 41.111  -20.474 -39.955 1.00 65.45  ? 410 GLY   D C     1 
ATOM   10026 O  O     . GLY   C 2  400 ? 42.028  -20.103 -40.699 1.00 63.44  ? 410 GLY   D O     1 
ATOM   10027 N  N     . GLU   C 2  401 ? 40.196  -19.633 -39.473 1.00 72.65  ? 411 GLU   D N     1 
ATOM   10028 C  CA    . GLU   C 2  401 ? 40.299  -18.189 -39.628 1.00 59.44  ? 411 GLU   D CA    1 
ATOM   10029 C  C     . GLU   C 2  401 ? 41.191  -17.543 -38.579 1.00 57.75  ? 411 GLU   D C     1 
ATOM   10030 O  O     . GLU   C 2  401 ? 41.404  -16.330 -38.644 1.00 57.92  ? 411 GLU   D O     1 
ATOM   10031 C  CB    . GLU   C 2  401 ? 38.913  -17.566 -39.592 1.00 60.56  ? 411 GLU   D CB    1 
ATOM   10032 C  CG    . GLU   C 2  401 ? 38.128  -17.812 -40.862 1.00 69.92  ? 411 GLU   D CG    1 
ATOM   10033 C  CD    . GLU   C 2  401 ? 38.959  -17.564 -42.100 1.00 73.03  ? 411 GLU   D CD    1 
ATOM   10034 O  OE1   . GLU   C 2  401 ? 39.853  -18.390 -42.368 1.00 83.00  ? 411 GLU   D OE1   1 
ATOM   10035 O  OE2   . GLU   C 2  401 ? 38.734  -16.548 -42.798 1.00 70.06  ? 411 GLU   D OE2   1 
ATOM   10036 N  N     . GLY   C 2  402 ? 41.710  -18.316 -37.623 1.00 58.72  ? 412 GLY   D N     1 
ATOM   10037 C  CA    . GLY   C 2  402 ? 42.772  -17.851 -36.752 1.00 66.41  ? 412 GLY   D CA    1 
ATOM   10038 C  C     . GLY   C 2  402 ? 42.591  -18.063 -35.259 1.00 67.76  ? 412 GLY   D C     1 
ATOM   10039 O  O     . GLY   C 2  402 ? 43.525  -17.819 -34.490 1.00 63.63  ? 412 GLY   D O     1 
ATOM   10040 N  N     . MET   C 2  403 ? 41.418  -18.522 -34.828 1.00 61.09  ? 413 MET   D N     1 
ATOM   10041 C  CA    . MET   C 2  403 ? 41.068  -18.457 -33.416 1.00 68.54  ? 413 MET   D CA    1 
ATOM   10042 C  C     . MET   C 2  403 ? 41.580  -19.662 -32.628 1.00 71.22  ? 413 MET   D C     1 
ATOM   10043 O  O     . MET   C 2  403 ? 42.225  -20.573 -33.158 1.00 76.58  ? 413 MET   D O     1 
ATOM   10044 C  CB    . MET   C 2  403 ? 39.560  -18.331 -33.241 1.00 63.18  ? 413 MET   D CB    1 
ATOM   10045 C  CG    . MET   C 2  403 ? 39.041  -16.923 -33.255 1.00 55.80  ? 413 MET   D CG    1 
ATOM   10046 S  SD    . MET   C 2  403 ? 37.280  -17.021 -33.001 1.00 63.47  ? 413 MET   D SD    1 
ATOM   10047 C  CE    . MET   C 2  403 ? 36.646  -16.640 -34.632 1.00 40.17  ? 413 MET   D CE    1 
ATOM   10048 N  N     . ASP   C 2  404 ? 41.250  -19.669 -31.335 1.00 68.39  ? 414 ASP   D N     1 
ATOM   10049 C  CA    . ASP   C 2  404 ? 41.801  -20.586 -30.347 1.00 66.55  ? 414 ASP   D CA    1 
ATOM   10050 C  C     . ASP   C 2  404 ? 40.682  -21.202 -29.521 1.00 67.96  ? 414 ASP   D C     1 
ATOM   10051 O  O     . ASP   C 2  404 ? 39.503  -20.851 -29.638 1.00 64.94  ? 414 ASP   D O     1 
ATOM   10052 C  CB    . ASP   C 2  404 ? 42.793  -19.871 -29.425 1.00 71.28  ? 414 ASP   D CB    1 
ATOM   10053 C  CG    . ASP   C 2  404 ? 42.274  -18.506 -28.945 1.00 88.68  ? 414 ASP   D CG    1 
ATOM   10054 O  OD1   . ASP   C 2  404 ? 41.895  -17.652 -29.794 1.00 74.13  ? 414 ASP   D OD1   1 
ATOM   10055 O  OD2   . ASP   C 2  404 ? 42.238  -18.290 -27.710 1.00 90.56  ? 414 ASP   D OD2   1 
ATOM   10056 N  N     . GLU   C 2  405 ? 41.077  -22.130 -28.660 1.00 74.66  ? 415 GLU   D N     1 
ATOM   10057 C  CA    . GLU   C 2  405 ? 40.115  -22.778 -27.779 1.00 83.19  ? 415 GLU   D CA    1 
ATOM   10058 C  C     . GLU   C 2  405 ? 39.515  -21.779 -26.790 1.00 81.66  ? 415 GLU   D C     1 
ATOM   10059 O  O     . GLU   C 2  405 ? 38.294  -21.756 -26.585 1.00 71.58  ? 415 GLU   D O     1 
ATOM   10060 C  CB    . GLU   C 2  405 ? 40.801  -23.937 -27.045 1.00 87.54  ? 415 GLU   D CB    1 
ATOM   10061 C  CG    . GLU   C 2  405 ? 42.025  -23.503 -26.201 1.00 92.46  ? 415 GLU   D CG    1 
ATOM   10062 C  CD    . GLU   C 2  405 ? 43.346  -24.172 -26.607 1.00 98.89  ? 415 GLU   D CD    1 
ATOM   10063 O  OE1   . GLU   C 2  405 ? 43.617  -25.293 -26.122 1.00 100.52 ? 415 GLU   D OE1   1 
ATOM   10064 O  OE2   . GLU   C 2  405 ? 44.117  -23.574 -27.400 1.00 98.88  ? 415 GLU   D OE2   1 
ATOM   10065 N  N     . MET   C 2  406 ? 40.359  -20.932 -26.190 1.00 70.63  ? 416 MET   D N     1 
ATOM   10066 C  CA    . MET   C 2  406 ? 39.918  -20.039 -25.121 1.00 73.94  ? 416 MET   D CA    1 
ATOM   10067 C  C     . MET   C 2  406 ? 38.728  -19.190 -25.551 1.00 74.99  ? 416 MET   D C     1 
ATOM   10068 O  O     . MET   C 2  406 ? 37.706  -19.117 -24.853 1.00 63.25  ? 416 MET   D O     1 
ATOM   10069 C  CB    . MET   C 2  406 ? 41.076  -19.135 -24.698 1.00 81.56  ? 416 MET   D CB    1 
ATOM   10070 C  CG    . MET   C 2  406 ? 42.358  -19.871 -24.384 1.00 92.62  ? 416 MET   D CG    1 
ATOM   10071 S  SD    . MET   C 2  406 ? 42.240  -20.851 -22.878 1.00 94.76  ? 416 MET   D SD    1 
ATOM   10072 C  CE    . MET   C 2  406 ? 43.731  -21.844 -23.029 1.00 90.08  ? 416 MET   D CE    1 
ATOM   10073 N  N     . GLU   C 2  407 ? 38.857  -18.527 -26.703 1.00 72.83  ? 417 GLU   D N     1 
ATOM   10074 C  CA    . GLU   C 2  407 ? 37.852  -17.571 -27.151 1.00 67.26  ? 417 GLU   D CA    1 
ATOM   10075 C  C     . GLU   C 2  407 ? 36.448  -18.131 -27.026 1.00 62.60  ? 417 GLU   D C     1 
ATOM   10076 O  O     . GLU   C 2  407 ? 35.484  -17.377 -26.867 1.00 60.89  ? 417 GLU   D O     1 
ATOM   10077 C  CB    . GLU   C 2  407 ? 38.134  -17.170 -28.595 1.00 69.15  ? 417 GLU   D CB    1 
ATOM   10078 C  CG    . GLU   C 2  407 ? 37.537  -15.851 -29.006 1.00 62.38  ? 417 GLU   D CG    1 
ATOM   10079 C  CD    . GLU   C 2  407 ? 38.575  -14.949 -29.615 1.00 66.05  ? 417 GLU   D CD    1 
ATOM   10080 O  OE1   . GLU   C 2  407 ? 39.779  -15.283 -29.500 1.00 69.17  ? 417 GLU   D OE1   1 
ATOM   10081 O  OE2   . GLU   C 2  407 ? 38.189  -13.916 -30.201 1.00 60.76  ? 417 GLU   D OE2   1 
ATOM   10082 N  N     . PHE   C 2  408 ? 36.305  -19.445 -27.103 1.00 66.49  ? 418 PHE   D N     1 
ATOM   10083 C  CA    . PHE   C 2  408 ? 34.979  -19.986 -26.879 1.00 70.21  ? 418 PHE   D CA    1 
ATOM   10084 C  C     . PHE   C 2  408 ? 34.717  -20.189 -25.388 1.00 61.42  ? 418 PHE   D C     1 
ATOM   10085 O  O     . PHE   C 2  408 ? 33.726  -19.669 -24.870 1.00 60.77  ? 418 PHE   D O     1 
ATOM   10086 C  CB    . PHE   C 2  408 ? 34.796  -21.273 -27.690 1.00 72.34  ? 418 PHE   D CB    1 
ATOM   10087 C  CG    . PHE   C 2  408 ? 34.630  -21.031 -29.177 1.00 69.71  ? 418 PHE   D CG    1 
ATOM   10088 C  CD1   . PHE   C 2  408 ? 35.711  -20.653 -29.961 1.00 73.45  ? 418 PHE   D CD1   1 
ATOM   10089 C  CD2   . PHE   C 2  408 ? 33.400  -21.184 -29.788 1.00 64.47  ? 418 PHE   D CD2   1 
ATOM   10090 C  CE1   . PHE   C 2  408 ? 35.558  -20.431 -31.321 1.00 66.84  ? 418 PHE   D CE1   1 
ATOM   10091 C  CE2   . PHE   C 2  408 ? 33.248  -20.960 -31.148 1.00 67.90  ? 418 PHE   D CE2   1 
ATOM   10092 C  CZ    . PHE   C 2  408 ? 34.326  -20.582 -31.910 1.00 61.83  ? 418 PHE   D CZ    1 
ATOM   10093 N  N     . THR   C 2  409 ? 35.597  -20.898 -24.673 1.00 57.19  ? 419 THR   D N     1 
ATOM   10094 C  CA    . THR   C 2  409 ? 35.427  -20.989 -23.224 1.00 66.10  ? 419 THR   D CA    1 
ATOM   10095 C  C     . THR   C 2  409 ? 35.191  -19.603 -22.626 1.00 69.83  ? 419 THR   D C     1 
ATOM   10096 O  O     . THR   C 2  409 ? 34.275  -19.409 -21.817 1.00 60.49  ? 419 THR   D O     1 
ATOM   10097 C  CB    . THR   C 2  409 ? 36.638  -21.652 -22.546 1.00 47.40  ? 419 THR   D CB    1 
ATOM   10098 O  OG1   . THR   C 2  409 ? 37.823  -20.898 -22.826 1.00 56.16  ? 419 THR   D OG1   1 
ATOM   10099 C  CG2   . THR   C 2  409 ? 36.808  -23.095 -22.980 1.00 48.00  ? 419 THR   D CG2   1 
ATOM   10100 N  N     . GLU   C 2  410 ? 35.996  -18.618 -23.041 1.00 69.67  ? 420 GLU   D N     1 
ATOM   10101 C  CA    . GLU   C 2  410 ? 35.890  -17.273 -22.480 1.00 63.80  ? 420 GLU   D CA    1 
ATOM   10102 C  C     . GLU   C 2  410 ? 34.502  -16.685 -22.710 1.00 57.14  ? 420 GLU   D C     1 
ATOM   10103 O  O     . GLU   C 2  410 ? 33.801  -16.329 -21.759 1.00 60.26  ? 420 GLU   D O     1 
ATOM   10104 C  CB    . GLU   C 2  410 ? 36.982  -16.378 -23.070 1.00 60.24  ? 420 GLU   D CB    1 
ATOM   10105 C  CG    . GLU   C 2  410 ? 38.376  -16.789 -22.608 1.00 68.56  ? 420 GLU   D CG    1 
ATOM   10106 C  CD    . GLU   C 2  410 ? 39.479  -15.952 -23.222 1.00 71.63  ? 420 GLU   D CD    1 
ATOM   10107 O  OE1   . GLU   C 2  410 ? 39.169  -15.089 -24.065 1.00 78.30  ? 420 GLU   D OE1   1 
ATOM   10108 O  OE2   . GLU   C 2  410 ? 40.657  -16.156 -22.861 1.00 75.58  ? 420 GLU   D OE2   1 
ATOM   10109 N  N     . ALA   C 2  411 ? 34.082  -16.580 -23.971 1.00 61.21  ? 421 ALA   D N     1 
ATOM   10110 C  CA    . ALA   C 2  411 ? 32.713  -16.163 -24.256 1.00 59.40  ? 421 ALA   D CA    1 
ATOM   10111 C  C     . ALA   C 2  411 ? 31.724  -16.981 -23.438 1.00 59.80  ? 421 ALA   D C     1 
ATOM   10112 O  O     . ALA   C 2  411 ? 30.812  -16.435 -22.811 1.00 58.86  ? 421 ALA   D O     1 
ATOM   10113 C  CB    . ALA   C 2  411 ? 32.420  -16.293 -25.752 1.00 51.14  ? 421 ALA   D CB    1 
ATOM   10114 N  N     . GLU   C 2  412 ? 31.911  -18.301 -23.422 1.00 67.57  ? 422 GLU   D N     1 
ATOM   10115 C  CA    . GLU   C 2  412 ? 31.055  -19.195 -22.648 1.00 66.12  ? 422 GLU   D CA    1 
ATOM   10116 C  C     . GLU   C 2  412 ? 30.906  -18.714 -21.210 1.00 64.60  ? 422 GLU   D C     1 
ATOM   10117 O  O     . GLU   C 2  412 ? 29.797  -18.428 -20.747 1.00 65.20  ? 422 GLU   D O     1 
ATOM   10118 C  CB    . GLU   C 2  412 ? 31.637  -20.609 -22.690 1.00 64.52  ? 422 GLU   D CB    1 
ATOM   10119 C  CG    . GLU   C 2  412 ? 30.743  -21.696 -22.151 1.00 60.80  ? 422 GLU   D CG    1 
ATOM   10120 C  CD    . GLU   C 2  412 ? 31.349  -23.075 -22.350 1.00 73.17  ? 422 GLU   D CD    1 
ATOM   10121 O  OE1   . GLU   C 2  412 ? 32.493  -23.300 -21.886 1.00 68.13  ? 422 GLU   D OE1   1 
ATOM   10122 O  OE2   . GLU   C 2  412 ? 30.689  -23.927 -22.987 1.00 76.65  ? 422 GLU   D OE2   1 
ATOM   10123 N  N     . SER   C 2  413 ? 32.026  -18.613 -20.490 1.00 60.41  ? 423 SER   D N     1 
ATOM   10124 C  CA    . SER   C 2  413 ? 32.013  -18.253 -19.079 1.00 63.14  ? 423 SER   D CA    1 
ATOM   10125 C  C     . SER   C 2  413 ? 31.749  -16.774 -18.835 1.00 67.02  ? 423 SER   D C     1 
ATOM   10126 O  O     . SER   C 2  413 ? 31.492  -16.392 -17.686 1.00 63.85  ? 423 SER   D O     1 
ATOM   10127 C  CB    . SER   C 2  413 ? 33.340  -18.632 -18.423 1.00 65.60  ? 423 SER   D CB    1 
ATOM   10128 O  OG    . SER   C 2  413 ? 34.388  -17.842 -18.953 1.00 76.72  ? 423 SER   D OG    1 
ATOM   10129 N  N     . ASN   C 2  414 ? 31.829  -15.934 -19.868 1.00 62.23  ? 424 ASN   D N     1 
ATOM   10130 C  CA    . ASN   C 2  414 ? 31.449  -14.535 -19.715 1.00 55.89  ? 424 ASN   D CA    1 
ATOM   10131 C  C     . ASN   C 2  414 ? 29.941  -14.374 -19.785 1.00 51.02  ? 424 ASN   D C     1 
ATOM   10132 O  O     . ASN   C 2  414 ? 29.364  -13.579 -19.041 1.00 57.37  ? 424 ASN   D O     1 
ATOM   10133 C  CB    . ASN   C 2  414 ? 32.118  -13.677 -20.793 1.00 63.05  ? 424 ASN   D CB    1 
ATOM   10134 C  CG    . ASN   C 2  414 ? 31.935  -12.177 -20.561 1.00 59.86  ? 424 ASN   D CG    1 
ATOM   10135 O  OD1   . ASN   C 2  414 ? 31.536  -11.750 -19.481 1.00 54.95  ? 424 ASN   D OD1   1 
ATOM   10136 N  ND2   . ASN   C 2  414 ? 32.245  -11.373 -21.582 1.00 59.88  ? 424 ASN   D ND2   1 
ATOM   10137 N  N     . MET   C 2  415 ? 29.288  -15.112 -20.676 1.00 53.65  ? 425 MET   D N     1 
ATOM   10138 C  CA    . MET   C 2  415 ? 27.841  -15.036 -20.763 1.00 46.10  ? 425 MET   D CA    1 
ATOM   10139 C  C     . MET   C 2  415 ? 27.173  -15.808 -19.636 1.00 51.91  ? 425 MET   D C     1 
ATOM   10140 O  O     . MET   C 2  415 ? 26.051  -15.479 -19.247 1.00 53.34  ? 425 MET   D O     1 
ATOM   10141 C  CB    . MET   C 2  415 ? 27.374  -15.554 -22.114 1.00 52.49  ? 425 MET   D CB    1 
ATOM   10142 C  CG    . MET   C 2  415 ? 25.922  -15.292 -22.413 1.00 49.53  ? 425 MET   D CG    1 
ATOM   10143 S  SD    . MET   C 2  415 ? 25.488  -16.245 -23.878 1.00 69.15  ? 425 MET   D SD    1 
ATOM   10144 C  CE    . MET   C 2  415 ? 24.988  -14.944 -25.000 1.00 50.05  ? 425 MET   D CE    1 
ATOM   10145 N  N     . ASN   C 2  416 ? 27.839  -16.820 -19.081 1.00 50.79  ? 426 ASN   D N     1 
ATOM   10146 C  CA    . ASN   C 2  416 ? 27.294  -17.446 -17.884 1.00 54.14  ? 426 ASN   D CA    1 
ATOM   10147 C  C     . ASN   C 2  416 ? 27.441  -16.520 -16.677 1.00 63.47  ? 426 ASN   D C     1 
ATOM   10148 O  O     . ASN   C 2  416 ? 26.558  -16.472 -15.808 1.00 59.49  ? 426 ASN   D O     1 
ATOM   10149 C  CB    . ASN   C 2  416 ? 27.962  -18.804 -17.652 1.00 67.92  ? 426 ASN   D CB    1 
ATOM   10150 C  CG    . ASN   C 2  416 ? 27.575  -19.841 -18.720 1.00 77.33  ? 426 ASN   D CG    1 
ATOM   10151 O  OD1   . ASN   C 2  416 ? 26.443  -19.850 -19.218 1.00 65.41  ? 426 ASN   D OD1   1 
ATOM   10152 N  ND2   . ASN   C 2  416 ? 28.520  -20.712 -19.077 1.00 75.99  ? 426 ASN   D ND2   1 
ATOM   10153 N  N     . ASP   C 2  417 ? 28.549  -15.774 -16.612 1.00 61.65  ? 427 ASP   D N     1 
ATOM   10154 C  CA    . ASP   C 2  417 ? 28.661  -14.640 -15.701 1.00 47.93  ? 427 ASP   D CA    1 
ATOM   10155 C  C     . ASP   C 2  417 ? 27.451  -13.720 -15.815 1.00 47.93  ? 427 ASP   D C     1 
ATOM   10156 O  O     . ASP   C 2  417 ? 26.778  -13.420 -14.826 1.00 52.58  ? 427 ASP   D O     1 
ATOM   10157 C  CB    . ASP   C 2  417 ? 29.935  -13.855 -16.010 1.00 54.19  ? 427 ASP   D CB    1 
ATOM   10158 C  CG    . ASP   C 2  417 ? 31.176  -14.520 -15.486 1.00 55.29  ? 427 ASP   D CG    1 
ATOM   10159 O  OD1   . ASP   C 2  417 ? 31.038  -15.485 -14.705 1.00 45.97  ? 427 ASP   D OD1   1 
ATOM   10160 O  OD2   . ASP   C 2  417 ? 32.285  -14.068 -15.867 1.00 51.08  ? 427 ASP   D OD2   1 
ATOM   10161 N  N     . LEU   C 2  418 ? 27.174  -13.242 -17.024 1.00 47.99  ? 428 LEU   D N     1 
ATOM   10162 C  CA    . LEU   C 2  418 ? 26.077  -12.302 -17.210 1.00 52.21  ? 428 LEU   D CA    1 
ATOM   10163 C  C     . LEU   C 2  418 ? 24.764  -12.844 -16.671 1.00 55.26  ? 428 LEU   D C     1 
ATOM   10164 O  O     . LEU   C 2  418 ? 23.848  -12.067 -16.380 1.00 55.23  ? 428 LEU   D O     1 
ATOM   10165 C  CB    . LEU   C 2  418 ? 25.925  -11.962 -18.693 1.00 47.66  ? 428 LEU   D CB    1 
ATOM   10166 C  CG    . LEU   C 2  418 ? 24.752  -11.023 -18.963 1.00 56.24  ? 428 LEU   D CG    1 
ATOM   10167 C  CD1   . LEU   C 2  418 ? 24.937  -9.767  -18.150 1.00 47.32  ? 428 LEU   D CD1   1 
ATOM   10168 C  CD2   . LEU   C 2  418 ? 24.602  -10.695 -20.450 1.00 55.16  ? 428 LEU   D CD2   1 
ATOM   10169 N  N     . VAL   C 2  419 ? 24.649  -14.159 -16.545 1.00 53.80  ? 429 VAL   D N     1 
ATOM   10170 C  CA    . VAL   C 2  419 ? 23.417  -14.777 -16.085 1.00 51.25  ? 429 VAL   D CA    1 
ATOM   10171 C  C     . VAL   C 2  419 ? 23.429  -14.977 -14.577 1.00 46.00  ? 429 VAL   D C     1 
ATOM   10172 O  O     . VAL   C 2  419 ? 22.404  -14.808 -13.918 1.00 45.12  ? 429 VAL   D O     1 
ATOM   10173 C  CB    . VAL   C 2  419 ? 23.211  -16.100 -16.850 1.00 55.21  ? 429 VAL   D CB    1 
ATOM   10174 C  CG1   . VAL   C 2  419 ? 22.183  -17.027 -16.141 1.00 30.12  ? 429 VAL   D CG1   1 
ATOM   10175 C  CG2   . VAL   C 2  419 ? 22.814  -15.790 -18.290 1.00 47.47  ? 429 VAL   D CG2   1 
ATOM   10176 N  N     . SER   C 2  420 ? 24.575  -15.344 -14.003 1.00 50.31  ? 430 SER   D N     1 
ATOM   10177 C  CA    . SER   C 2  420 ? 24.689  -15.344 -12.547 1.00 52.67  ? 430 SER   D CA    1 
ATOM   10178 C  C     . SER   C 2  420 ? 24.368  -13.968 -11.978 1.00 58.25  ? 430 SER   D C     1 
ATOM   10179 O  O     . SER   C 2  420 ? 23.738  -13.855 -10.920 1.00 57.56  ? 430 SER   D O     1 
ATOM   10180 C  CB    . SER   C 2  420 ? 26.092  -15.775 -12.120 1.00 49.27  ? 430 SER   D CB    1 
ATOM   10181 O  OG    . SER   C 2  420 ? 26.446  -17.019 -12.700 1.00 67.51  ? 430 SER   D OG    1 
ATOM   10182 N  N     . GLU   C 2  421 ? 24.800  -12.907 -12.668 1.00 59.47  ? 431 GLU   D N     1 
ATOM   10183 C  CA    . GLU   C 2  421 ? 24.572  -11.551 -12.180 1.00 56.68  ? 431 GLU   D CA    1 
ATOM   10184 C  C     . GLU   C 2  421 ? 23.088  -11.201 -12.206 1.00 48.79  ? 431 GLU   D C     1 
ATOM   10185 O  O     . GLU   C 2  421 ? 22.538  -10.748 -11.199 1.00 57.76  ? 431 GLU   D O     1 
ATOM   10186 C  CB    . GLU   C 2  421 ? 25.403  -10.554 -12.998 1.00 52.71  ? 431 GLU   D CB    1 
ATOM   10187 C  CG    . GLU   C 2  421 ? 26.916  -10.667 -12.737 1.00 43.26  ? 431 GLU   D CG    1 
ATOM   10188 C  CD    . GLU   C 2  421 ? 27.780  -10.262 -13.934 1.00 53.53  ? 431 GLU   D CD    1 
ATOM   10189 O  OE1   . GLU   C 2  421 ? 27.335  -9.437  -14.776 1.00 41.57  ? 431 GLU   D OE1   1 
ATOM   10190 O  OE2   . GLU   C 2  421 ? 28.920  -10.778 -14.026 1.00 52.41  ? 431 GLU   D OE2   1 
ATOM   10191 N  N     . TYR   C 2  422 ? 22.416  -11.413 -13.342 1.00 48.33  ? 432 TYR   D N     1 
ATOM   10192 C  CA    . TYR   C 2  422 ? 20.973  -11.195 -13.391 1.00 48.14  ? 432 TYR   D CA    1 
ATOM   10193 C  C     . TYR   C 2  422 ? 20.266  -11.957 -12.281 1.00 48.98  ? 432 TYR   D C     1 
ATOM   10194 O  O     . TYR   C 2  422 ? 19.241  -11.499 -11.760 1.00 51.62  ? 432 TYR   D O     1 
ATOM   10195 C  CB    . TYR   C 2  422 ? 20.412  -11.609 -14.755 1.00 48.02  ? 432 TYR   D CB    1 
ATOM   10196 C  CG    . TYR   C 2  422 ? 20.462  -10.502 -15.769 1.00 49.89  ? 432 TYR   D CG    1 
ATOM   10197 C  CD1   . TYR   C 2  422 ? 19.659  -9.392  -15.614 1.00 48.00  ? 432 TYR   D CD1   1 
ATOM   10198 C  CD2   . TYR   C 2  422 ? 21.304  -10.564 -16.881 1.00 47.51  ? 432 TYR   D CD2   1 
ATOM   10199 C  CE1   . TYR   C 2  422 ? 19.679  -8.364  -16.517 1.00 48.11  ? 432 TYR   D CE1   1 
ATOM   10200 C  CE2   . TYR   C 2  422 ? 21.341  -9.523  -17.803 1.00 48.93  ? 432 TYR   D CE2   1 
ATOM   10201 C  CZ    . TYR   C 2  422 ? 20.518  -8.416  -17.606 1.00 51.73  ? 432 TYR   D CZ    1 
ATOM   10202 O  OH    . TYR   C 2  422 ? 20.493  -7.340  -18.481 1.00 55.13  ? 432 TYR   D OH    1 
ATOM   10203 N  N     . GLN   C 2  423 ? 20.802  -13.117 -11.903 1.00 50.83  ? 433 GLN   D N     1 
ATOM   10204 C  CA    . GLN   C 2  423 ? 20.202  -13.888 -10.821 1.00 50.24  ? 433 GLN   D CA    1 
ATOM   10205 C  C     . GLN   C 2  423 ? 20.481  -13.241 -9.476  1.00 48.10  ? 433 GLN   D C     1 
ATOM   10206 O  O     . GLN   C 2  423 ? 19.607  -13.215 -8.604  1.00 56.46  ? 433 GLN   D O     1 
ATOM   10207 C  CB    . GLN   C 2  423 ? 20.725  -15.326 -10.841 1.00 41.78  ? 433 GLN   D CB    1 
ATOM   10208 C  CG    . GLN   C 2  423 ? 19.961  -16.266 -9.923  1.00 41.02  ? 433 GLN   D CG    1 
ATOM   10209 C  CD    . GLN   C 2  423 ? 18.506  -16.402 -10.322 1.00 46.02  ? 433 GLN   D CD    1 
ATOM   10210 O  OE1   . GLN   C 2  423 ? 18.167  -16.308 -11.505 1.00 40.08  ? 433 GLN   D OE1   1 
ATOM   10211 N  NE2   . GLN   C 2  423 ? 17.635  -16.613 -9.338  1.00 41.24  ? 433 GLN   D NE2   1 
ATOM   10212 N  N     . GLN   C 2  424 ? 21.690  -12.703 -9.299  1.00 43.00  ? 434 GLN   D N     1 
ATOM   10213 C  CA    . GLN   C 2  424 ? 22.081  -12.118 -8.023  1.00 40.11  ? 434 GLN   D CA    1 
ATOM   10214 C  C     . GLN   C 2  424 ? 21.186  -10.948 -7.654  1.00 47.27  ? 434 GLN   D C     1 
ATOM   10215 O  O     . GLN   C 2  424 ? 20.800  -10.797 -6.489  1.00 50.47  ? 434 GLN   D O     1 
ATOM   10216 C  CB    . GLN   C 2  424 ? 23.540  -11.675 -8.084  1.00 51.17  ? 434 GLN   D CB    1 
ATOM   10217 C  CG    . GLN   C 2  424 ? 23.954  -10.700 -7.004  1.00 55.42  ? 434 GLN   D CG    1 
ATOM   10218 C  CD    . GLN   C 2  424 ? 25.327  -10.085 -7.261  1.00 64.56  ? 434 GLN   D CD    1 
ATOM   10219 O  OE1   . GLN   C 2  424 ? 26.236  -10.746 -7.768  1.00 70.10  ? 434 GLN   D OE1   1 
ATOM   10220 N  NE2   . GLN   C 2  424 ? 25.476  -8.808  -6.919  1.00 61.72  ? 434 GLN   D NE2   1 
ATOM   10221 N  N     . TYR   C 2  425 ? 20.837  -10.111 -8.632  1.00 42.45  ? 435 TYR   D N     1 
ATOM   10222 C  CA    . TYR   C 2  425 ? 19.988  -8.967  -8.337  1.00 46.38  ? 435 TYR   D CA    1 
ATOM   10223 C  C     . TYR   C 2  425 ? 18.527  -9.366  -8.249  1.00 43.48  ? 435 TYR   D C     1 
ATOM   10224 O  O     . TYR   C 2  425 ? 17.763  -8.773  -7.474  1.00 44.94  ? 435 TYR   D O     1 
ATOM   10225 C  CB    . TYR   C 2  425 ? 20.216  -7.870  -9.380  1.00 41.18  ? 435 TYR   D CB    1 
ATOM   10226 C  CG    . TYR   C 2  425 ? 21.587  -7.284  -9.217  1.00 36.73  ? 435 TYR   D CG    1 
ATOM   10227 C  CD1   . TYR   C 2  425 ? 21.862  -6.394  -8.190  1.00 39.93  ? 435 TYR   D CD1   1 
ATOM   10228 C  CD2   . TYR   C 2  425 ? 22.621  -7.661  -10.042 1.00 44.84  ? 435 TYR   D CD2   1 
ATOM   10229 C  CE1   . TYR   C 2  425 ? 23.127  -5.879  -8.008  1.00 39.83  ? 435 TYR   D CE1   1 
ATOM   10230 C  CE2   . TYR   C 2  425 ? 23.889  -7.143  -9.874  1.00 45.54  ? 435 TYR   D CE2   1 
ATOM   10231 C  CZ    . TYR   C 2  425 ? 24.139  -6.255  -8.862  1.00 39.98  ? 435 TYR   D CZ    1 
ATOM   10232 O  OH    . TYR   C 2  425 ? 25.408  -5.755  -8.704  1.00 36.71  ? 435 TYR   D OH    1 
ATOM   10233 N  N     . GLN   C 2  426 ? 18.134  -10.377 -9.015  1.00 41.00  ? 436 GLN   D N     1 
ATOM   10234 C  CA    . GLN   C 2  426 ? 16.798  -10.934 -8.879  1.00 44.55  ? 436 GLN   D CA    1 
ATOM   10235 C  C     . GLN   C 2  426 ? 16.537  -11.377 -7.445  1.00 38.86  ? 436 GLN   D C     1 
ATOM   10236 O  O     . GLN   C 2  426 ? 15.493  -11.067 -6.866  1.00 51.08  ? 436 GLN   D O     1 
ATOM   10237 C  CB    . GLN   C 2  426 ? 16.655  -12.094 -9.855  1.00 53.23  ? 436 GLN   D CB    1 
ATOM   10238 C  CG    . GLN   C 2  426 ? 15.452  -12.968 -9.660  1.00 51.12  ? 436 GLN   D CG    1 
ATOM   10239 C  CD    . GLN   C 2  426 ? 15.081  -13.628 -10.950 1.00 50.48  ? 436 GLN   D CD    1 
ATOM   10240 O  OE1   . GLN   C 2  426 ? 15.104  -12.992 -12.001 1.00 50.39  ? 436 GLN   D OE1   1 
ATOM   10241 N  NE2   . GLN   C 2  426 ? 14.759  -14.909 -10.894 1.00 55.37  ? 436 GLN   D NE2   1 
ATOM   10242 N  N     . ASP   C 2  427 ? 17.494  -12.077 -6.849  1.00 37.34  ? 437 ASP   D N     1 
ATOM   10243 C  CA    . ASP   C 2  427 ? 17.372  -12.630 -5.506  1.00 47.14  ? 437 ASP   D CA    1 
ATOM   10244 C  C     . ASP   C 2  427 ? 17.635  -11.613 -4.398  1.00 53.41  ? 437 ASP   D C     1 
ATOM   10245 O  O     . ASP   C 2  427 ? 17.353  -11.906 -3.226  1.00 41.79  ? 437 ASP   D O     1 
ATOM   10246 C  CB    . ASP   C 2  427 ? 18.349  -13.803 -5.334  1.00 42.90  ? 437 ASP   D CB    1 
ATOM   10247 C  CG    . ASP   C 2  427 ? 17.999  -14.999 -6.201  1.00 55.42  ? 437 ASP   D CG    1 
ATOM   10248 O  OD1   . ASP   C 2  427 ? 16.793  -15.180 -6.545  1.00 38.83  ? 437 ASP   D OD1   1 
ATOM   10249 O  OD2   . ASP   C 2  427 ? 18.948  -15.758 -6.526  1.00 48.38  ? 437 ASP   D OD2   1 
ATOM   10250 N  N     . ALA   C 2  428 ? 18.200  -10.453 -4.717  1.00 45.18  ? 438 ALA   D N     1 
ATOM   10251 C  CA    . ALA   C 2  428 ? 18.519  -9.510  -3.662  1.00 46.33  ? 438 ALA   D CA    1 
ATOM   10252 C  C     . ALA   C 2  428 ? 17.244  -8.905  -3.079  1.00 51.47  ? 438 ALA   D C     1 
ATOM   10253 O  O     . ALA   C 2  428 ? 16.185  -8.859  -3.722  1.00 47.90  ? 438 ALA   D O     1 
ATOM   10254 C  CB    . ALA   C 2  428 ? 19.443  -8.408  -4.179  1.00 37.70  ? 438 ALA   D CB    1 
ATOM   10255 N  N     . THR   C 2  429 ? 17.360  -8.446  -1.833  1.00 50.42  ? 439 THR   D N     1 
ATOM   10256 C  CA    . THR   C 2  429 ? 16.319  -7.674  -1.174  1.00 52.67  ? 439 THR   D CA    1 
ATOM   10257 C  C     . THR   C 2  429 ? 16.968  -6.564  -0.371  1.00 55.22  ? 439 THR   D C     1 
ATOM   10258 O  O     . THR   C 2  429 ? 18.159  -6.618  -0.055  1.00 62.87  ? 439 THR   D O     1 
ATOM   10259 C  CB    . THR   C 2  429 ? 15.487  -8.521  -0.219  1.00 55.91  ? 439 THR   D CB    1 
ATOM   10260 O  OG1   . THR   C 2  429 ? 16.365  -9.099  0.757   1.00 49.48  ? 439 THR   D OG1   1 
ATOM   10261 C  CG2   . THR   C 2  429 ? 14.746  -9.611  -0.979  1.00 52.03  ? 439 THR   D CG2   1 
ATOM   10262 N  N     . ALA   C 2  430 ? 16.162  -5.561  -0.022  1.00 61.45  ? 440 ALA   D N     1 
ATOM   10263 C  CA    . ALA   C 2  430 ? 16.590  -4.604  0.992   1.00 56.28  ? 440 ALA   D CA    1 
ATOM   10264 C  C     . ALA   C 2  430 ? 16.901  -5.311  2.308   1.00 63.50  ? 440 ALA   D C     1 
ATOM   10265 O  O     . ALA   C 2  430 ? 17.873  -4.970  2.994   1.00 64.32  ? 440 ALA   D O     1 
ATOM   10266 C  CB    . ALA   C 2  430 ? 15.514  -3.542  1.179   1.00 51.33  ? 440 ALA   D CB    1 
ATOM   10267 N  N     . ASP   C 2  431 ? 16.095  -6.309  2.664   1.00 77.86  ? 441 ASP   D N     1 
ATOM   10268 C  CA    . ASP   C 2  431 ? 16.394  -7.222  3.765   1.00 70.81  ? 441 ASP   D CA    1 
ATOM   10269 C  C     . ASP   C 2  431 ? 15.754  -8.592  3.520   1.00 76.65  ? 441 ASP   D C     1 
ATOM   10270 O  O     . ASP   C 2  431 ? 15.041  -9.130  4.368   1.00 80.07  ? 441 ASP   D O     1 
ATOM   10271 C  CB    . ASP   C 2  431 ? 15.916  -6.632  5.080   1.00 67.38  ? 441 ASP   D CB    1 
ATOM   10272 C  CG    . ASP   C 2  431 ? 16.557  -5.305  5.367   1.00 85.62  ? 441 ASP   D CG    1 
ATOM   10273 O  OD1   . ASP   C 2  431 ? 17.801  -5.274  5.529   1.00 84.54  ? 441 ASP   D OD1   1 
ATOM   10274 O  OD2   . ASP   C 2  431 ? 15.827  -4.289  5.378   1.00 85.81  ? 441 ASP   D OD2   1 
ATOM   10275 N  N     . MET   D 3  4   ? 20.935  89.155  91.732  1.00 84.24  ? 6   MET   E N     1 
ATOM   10276 C  CA    . MET   D 3  4   ? 20.484  90.068  92.775  1.00 79.79  ? 6   MET   E CA    1 
ATOM   10277 C  C     . MET   D 3  4   ? 21.391  91.296  92.808  1.00 77.44  ? 6   MET   E C     1 
ATOM   10278 O  O     . MET   D 3  4   ? 20.941  92.400  93.125  1.00 84.11  ? 6   MET   E O     1 
ATOM   10279 C  CB    . MET   D 3  4   ? 20.467  89.363  94.140  1.00 71.47  ? 6   MET   E CB    1 
ATOM   10280 C  CG    . MET   D 3  4   ? 19.769  90.132  95.256  1.00 69.64  ? 6   MET   E CG    1 
ATOM   10281 S  SD    . MET   D 3  4   ? 19.718  89.186  96.799  1.00 101.50 ? 6   MET   E SD    1 
ATOM   10282 C  CE    . MET   D 3  4   ? 21.467  89.098  97.208  1.00 88.09  ? 6   MET   E CE    1 
ATOM   10283 N  N     . GLU   D 3  5   ? 22.660  91.100  92.451  1.00 61.18  ? 7   GLU   E N     1 
ATOM   10284 C  CA    . GLU   D 3  5   ? 23.693  92.122  92.583  1.00 68.19  ? 7   GLU   E CA    1 
ATOM   10285 C  C     . GLU   D 3  5   ? 24.101  92.635  91.204  1.00 70.05  ? 7   GLU   E C     1 
ATOM   10286 O  O     . GLU   D 3  5   ? 24.556  91.850  90.361  1.00 60.63  ? 7   GLU   E O     1 
ATOM   10287 C  CB    . GLU   D 3  5   ? 24.899  91.555  93.327  1.00 68.44  ? 7   GLU   E CB    1 
ATOM   10288 C  CG    . GLU   D 3  5   ? 25.962  92.569  93.679  1.00 73.03  ? 7   GLU   E CG    1 
ATOM   10289 C  CD    . GLU   D 3  5   ? 27.255  91.895  94.087  1.00 86.44  ? 7   GLU   E CD    1 
ATOM   10290 O  OE1   . GLU   D 3  5   ? 27.281  90.642  94.090  1.00 79.50  ? 7   GLU   E OE1   1 
ATOM   10291 O  OE2   . GLU   D 3  5   ? 28.239  92.611  94.390  1.00 90.05  ? 7   GLU   E OE2   1 
ATOM   10292 N  N     . VAL   D 3  6   ? 23.956  93.946  90.989  1.00 66.00  ? 8   VAL   E N     1 
ATOM   10293 C  CA    . VAL   D 3  6   ? 24.276  94.591  89.715  1.00 54.91  ? 8   VAL   E CA    1 
ATOM   10294 C  C     . VAL   D 3  6   ? 25.729  95.052  89.756  1.00 54.67  ? 8   VAL   E C     1 
ATOM   10295 O  O     . VAL   D 3  6   ? 26.071  95.971  90.500  1.00 61.66  ? 8   VAL   E O     1 
ATOM   10296 C  CB    . VAL   D 3  6   ? 23.343  95.775  89.419  1.00 45.80  ? 8   VAL   E CB    1 
ATOM   10297 C  CG1   . VAL   D 3  6   ? 23.984  96.697  88.393  1.00 56.20  ? 8   VAL   E CG1   1 
ATOM   10298 C  CG2   . VAL   D 3  6   ? 22.006  95.309  88.891  1.00 35.09  ? 8   VAL   E CG2   1 
ATOM   10299 N  N     . ILE   D 3  7   ? 26.577  94.442  88.922  1.00 67.34  ? 9   ILE   E N     1 
ATOM   10300 C  CA    . ILE   D 3  7   ? 27.989  94.808  88.812  1.00 55.10  ? 9   ILE   E CA    1 
ATOM   10301 C  C     . ILE   D 3  7   ? 28.227  95.611  87.539  1.00 61.87  ? 9   ILE   E C     1 
ATOM   10302 O  O     . ILE   D 3  7   ? 27.306  95.825  86.737  1.00 52.55  ? 9   ILE   E O     1 
ATOM   10303 C  CB    . ILE   D 3  7   ? 28.902  93.567  88.822  1.00 65.74  ? 9   ILE   E CB    1 
ATOM   10304 C  CG1   . ILE   D 3  7   ? 28.278  92.444  89.647  1.00 62.64  ? 9   ILE   E CG1   1 
ATOM   10305 C  CG2   . ILE   D 3  7   ? 30.296  93.924  89.342  1.00 70.91  ? 9   ILE   E CG2   1 
ATOM   10306 C  CD1   . ILE   D 3  7   ? 27.816  92.863  91.011  1.00 53.78  ? 9   ILE   E CD1   1 
ATOM   10307 N  N     . GLU   D 3  8   ? 29.469  96.082  87.383  1.00 54.80  ? 10  GLU   E N     1 
ATOM   10308 C  CA    . GLU   D 3  8   ? 30.025  96.695  86.179  1.00 59.53  ? 10  GLU   E CA    1 
ATOM   10309 C  C     . GLU   D 3  8   ? 29.080  97.557  85.341  1.00 56.68  ? 10  GLU   E C     1 
ATOM   10310 O  O     . GLU   D 3  8   ? 29.203  97.569  84.111  1.00 51.90  ? 10  GLU   E O     1 
ATOM   10311 C  CB    . GLU   D 3  8   ? 30.606  95.602  85.275  1.00 66.18  ? 10  GLU   E CB    1 
ATOM   10312 C  CG    . GLU   D 3  8   ? 32.117  95.708  85.025  1.00 74.03  ? 10  GLU   E CG    1 
ATOM   10313 C  CD    . GLU   D 3  8   ? 32.943  94.908  86.030  1.00 75.80  ? 10  GLU   E CD    1 
ATOM   10314 O  OE1   . GLU   D 3  8   ? 32.368  94.412  87.027  1.00 68.13  ? 10  GLU   E OE1   1 
ATOM   10315 O  OE2   . GLU   D 3  8   ? 34.169  94.770  85.816  1.00 79.64  ? 10  GLU   E OE2   1 
ATOM   10316 N  N     . LEU   D 3  9   ? 28.174  98.312  85.957  1.00 41.28  ? 11  LEU   E N     1 
ATOM   10317 C  CA    . LEU   D 3  9   ? 27.295  99.148  85.148  1.00 50.56  ? 11  LEU   E CA    1 
ATOM   10318 C  C     . LEU   D 3  9   ? 28.084  100.209 84.372  1.00 53.75  ? 11  LEU   E C     1 
ATOM   10319 O  O     . LEU   D 3  9   ? 28.862  100.965 84.957  1.00 53.47  ? 11  LEU   E O     1 
ATOM   10320 C  CB    . LEU   D 3  9   ? 26.250  99.821  86.019  1.00 42.48  ? 11  LEU   E CB    1 
ATOM   10321 C  CG    . LEU   D 3  9   ? 25.449  100.706 85.075  1.00 43.52  ? 11  LEU   E CG    1 
ATOM   10322 C  CD1   . LEU   D 3  9   ? 24.598  99.831  84.165  1.00 36.21  ? 11  LEU   E CD1   1 
ATOM   10323 C  CD2   . LEU   D 3  9   ? 24.615  101.716 85.828  1.00 42.14  ? 11  LEU   E CD2   1 
ATOM   10324 N  N     . ASN   D 3  10  ? 27.864  100.263 83.048  1.00 53.52  ? 12  ASN   E N     1 
ATOM   10325 C  CA    . ASN   D 3  10  ? 28.465  101.236 82.129  1.00 45.23  ? 12  ASN   E CA    1 
ATOM   10326 C  C     . ASN   D 3  10  ? 27.384  101.843 81.239  1.00 49.21  ? 12  ASN   E C     1 
ATOM   10327 O  O     . ASN   D 3  10  ? 26.550  101.113 80.687  1.00 47.91  ? 12  ASN   E O     1 
ATOM   10328 C  CB    . ASN   D 3  10  ? 29.546  100.600 81.234  1.00 40.05  ? 12  ASN   E CB    1 
ATOM   10329 C  CG    . ASN   D 3  10  ? 30.875  100.362 81.969  1.00 59.91  ? 12  ASN   E CG    1 
ATOM   10330 O  OD1   . ASN   D 3  10  ? 31.667  101.289 82.150  1.00 74.12  ? 12  ASN   E OD1   1 
ATOM   10331 N  ND2   . ASN   D 3  10  ? 31.126  99.116  82.378  1.00 52.68  ? 12  ASN   E ND2   1 
ATOM   10332 N  N     . LYS   D 3  11  ? 27.410  103.169 81.073  1.00 45.25  ? 13  LYS   E N     1 
ATOM   10333 C  CA    . LYS   D 3  11  ? 26.404  103.863 80.277  1.00 52.46  ? 13  LYS   E CA    1 
ATOM   10334 C  C     . LYS   D 3  11  ? 27.062  104.736 79.214  1.00 65.01  ? 13  LYS   E C     1 
ATOM   10335 O  O     . LYS   D 3  11  ? 27.975  105.510 79.520  1.00 66.74  ? 13  LYS   E O     1 
ATOM   10336 C  CB    . LYS   D 3  11  ? 25.493  104.710 81.167  1.00 55.26  ? 13  LYS   E CB    1 
ATOM   10337 C  CG    . LYS   D 3  11  ? 24.780  103.911 82.246  1.00 54.40  ? 13  LYS   E CG    1 
ATOM   10338 C  CD    . LYS   D 3  11  ? 24.275  104.820 83.346  1.00 51.27  ? 13  LYS   E CD    1 
ATOM   10339 C  CE    . LYS   D 3  11  ? 23.193  105.752 82.846  1.00 39.22  ? 13  LYS   E CE    1 
ATOM   10340 N  NZ    . LYS   D 3  11  ? 22.819  106.694 83.929  1.00 36.63  ? 13  LYS   E NZ    1 
ATOM   10341 N  N     . CYS   D 3  12  ? 26.604  104.585 77.963  1.00 73.50  ? 14  CYS   E N     1 
ATOM   10342 C  CA    . CYS   D 3  12  ? 26.902  105.425 76.806  1.00 62.14  ? 14  CYS   E CA    1 
ATOM   10343 C  C     . CYS   D 3  12  ? 25.675  106.276 76.523  1.00 62.92  ? 14  CYS   E C     1 
ATOM   10344 O  O     . CYS   D 3  12  ? 24.724  106.308 77.309  1.00 70.41  ? 14  CYS   E O     1 
ATOM   10345 C  CB    . CYS   D 3  12  ? 27.260  104.576 75.569  1.00 55.00  ? 14  CYS   E CB    1 
ATOM   10346 S  SG    . CYS   D 3  12  ? 28.342  103.128 75.884  1.00 84.93  ? 14  CYS   E SG    1 
ATOM   10347 N  N     . THR   D 3  13  ? 25.679  106.942 75.379  1.00 59.77  ? 15  THR   E N     1 
ATOM   10348 C  CA    . THR   D 3  13  ? 24.471  107.547 74.839  1.00 60.53  ? 15  THR   E CA    1 
ATOM   10349 C  C     . THR   D 3  13  ? 23.733  106.606 73.888  1.00 67.34  ? 15  THR   E C     1 
ATOM   10350 O  O     . THR   D 3  13  ? 22.653  106.955 73.398  1.00 67.15  ? 15  THR   E O     1 
ATOM   10351 C  CB    . THR   D 3  13  ? 24.821  108.861 74.126  1.00 70.02  ? 15  THR   E CB    1 
ATOM   10352 O  OG1   . THR   D 3  13  ? 25.574  109.692 75.017  1.00 69.58  ? 15  THR   E OG1   1 
ATOM   10353 C  CG2   . THR   D 3  13  ? 23.563  109.605 73.688  1.00 60.53  ? 15  THR   E CG2   1 
ATOM   10354 N  N     . SER   D 3  14  ? 24.291  105.424 73.619  1.00 59.30  ? 16  SER   E N     1 
ATOM   10355 C  CA    . SER   D 3  14  ? 23.625  104.413 72.814  1.00 50.34  ? 16  SER   E CA    1 
ATOM   10356 C  C     . SER   D 3  14  ? 22.896  103.354 73.640  1.00 61.39  ? 16  SER   E C     1 
ATOM   10357 O  O     . SER   D 3  14  ? 22.039  102.647 73.088  1.00 57.25  ? 16  SER   E O     1 
ATOM   10358 C  CB    . SER   D 3  14  ? 24.637  103.723 71.897  1.00 56.99  ? 16  SER   E CB    1 
ATOM   10359 O  OG    . SER   D 3  14  ? 25.261  104.661 71.042  1.00 69.25  ? 16  SER   E OG    1 
ATOM   10360 N  N     . GLY   D 3  15  ? 23.202  103.231 74.928  1.00 63.05  ? 17  GLY   E N     1 
ATOM   10361 C  CA    . GLY   D 3  15  ? 22.567  102.240 75.778  1.00 56.30  ? 17  GLY   E CA    1 
ATOM   10362 C  C     . GLY   D 3  15  ? 23.406  102.015 77.022  1.00 57.81  ? 17  GLY   E C     1 
ATOM   10363 O  O     . GLY   D 3  15  ? 24.338  102.766 77.302  1.00 64.57  ? 17  GLY   E O     1 
ATOM   10364 N  N     . GLN   D 3  16  ? 23.064  100.955 77.759  1.00 55.09  ? 18  GLN   E N     1 
ATOM   10365 C  CA    . GLN   D 3  16  ? 23.797  100.602 78.973  1.00 52.38  ? 18  GLN   E CA    1 
ATOM   10366 C  C     . GLN   D 3  16  ? 24.230  99.147  78.932  1.00 40.73  ? 18  GLN   E C     1 
ATOM   10367 O  O     . GLN   D 3  16  ? 23.656  98.330  78.204  1.00 32.79  ? 18  GLN   E O     1 
ATOM   10368 C  CB    . GLN   D 3  16  ? 22.961  100.832 80.231  1.00 44.08  ? 18  GLN   E CB    1 
ATOM   10369 C  CG    . GLN   D 3  16  ? 22.293  102.190 80.286  1.00 46.38  ? 18  GLN   E CG    1 
ATOM   10370 C  CD    . GLN   D 3  16  ? 21.365  102.314 81.471  1.00 42.77  ? 18  GLN   E CD    1 
ATOM   10371 O  OE1   . GLN   D 3  16  ? 21.603  101.726 82.527  1.00 44.32  ? 18  GLN   E OE1   1 
ATOM   10372 N  NE2   . GLN   D 3  16  ? 20.289  103.067 81.297  1.00 43.44  ? 18  GLN   E NE2   1 
ATOM   10373 N  N     . SER   D 3  17  ? 25.239  98.835  79.754  1.00 36.19  ? 19  SER   E N     1 
ATOM   10374 C  CA    . SER   D 3  17  ? 25.761  97.479  79.921  1.00 39.98  ? 19  SER   E CA    1 
ATOM   10375 C  C     . SER   D 3  17  ? 25.998  97.199  81.401  1.00 37.72  ? 19  SER   E C     1 
ATOM   10376 O  O     . SER   D 3  17  ? 26.387  98.090  82.158  1.00 47.02  ? 19  SER   E O     1 
ATOM   10377 C  CB    . SER   D 3  17  ? 27.082  97.277  79.142  1.00 44.96  ? 19  SER   E CB    1 
ATOM   10378 O  OG    . SER   D 3  17  ? 28.198  97.072  80.025  1.00 49.21  ? 19  SER   E OG    1 
ATOM   10379 N  N     . PHE   D 3  18  ? 25.798  95.949  81.811  1.00 37.76  ? 20  PHE   E N     1 
ATOM   10380 C  CA    . PHE   D 3  18  ? 26.009  95.573  83.211  1.00 37.36  ? 20  PHE   E CA    1 
ATOM   10381 C  C     . PHE   D 3  18  ? 25.833  94.067  83.377  1.00 35.22  ? 20  PHE   E C     1 
ATOM   10382 O  O     . PHE   D 3  18  ? 25.271  93.382  82.519  1.00 42.65  ? 20  PHE   E O     1 
ATOM   10383 C  CB    . PHE   D 3  18  ? 25.047  96.319  84.158  1.00 34.67  ? 20  PHE   E CB    1 
ATOM   10384 C  CG    . PHE   D 3  18  ? 23.613  95.919  83.995  1.00 31.72  ? 20  PHE   E CG    1 
ATOM   10385 C  CD1   . PHE   D 3  18  ? 22.822  96.498  82.998  1.00 37.86  ? 20  PHE   E CD1   1 
ATOM   10386 C  CD2   . PHE   D 3  18  ? 23.058  94.939  84.794  1.00 28.38  ? 20  PHE   E CD2   1 
ATOM   10387 C  CE1   . PHE   D 3  18  ? 21.496  96.120  82.824  1.00 33.62  ? 20  PHE   E CE1   1 
ATOM   10388 C  CE2   . PHE   D 3  18  ? 21.733  94.551  84.616  1.00 37.74  ? 20  PHE   E CE2   1 
ATOM   10389 C  CZ    . PHE   D 3  18  ? 20.953  95.144  83.627  1.00 32.14  ? 20  PHE   E CZ    1 
ATOM   10390 N  N     . GLU   D 3  19  ? 26.307  93.566  84.503  1.00 40.73  ? 21  GLU   E N     1 
ATOM   10391 C  CA    . GLU   D 3  19  ? 26.159  92.170  84.864  1.00 39.95  ? 21  GLU   E CA    1 
ATOM   10392 C  C     . GLU   D 3  19  ? 25.193  92.057  86.038  1.00 46.63  ? 21  GLU   E C     1 
ATOM   10393 O  O     . GLU   D 3  19  ? 25.072  92.972  86.857  1.00 56.68  ? 21  GLU   E O     1 
ATOM   10394 C  CB    . GLU   D 3  19  ? 27.522  91.576  85.216  1.00 39.43  ? 21  GLU   E CB    1 
ATOM   10395 C  CG    . GLU   D 3  19  ? 27.606  90.072  85.203  1.00 34.32  ? 21  GLU   E CG    1 
ATOM   10396 C  CD    . GLU   D 3  19  ? 29.046  89.595  85.054  1.00 54.63  ? 21  GLU   E CD    1 
ATOM   10397 O  OE1   . GLU   D 3  19  ? 29.911  90.401  84.614  1.00 47.11  ? 21  GLU   E OE1   1 
ATOM   10398 O  OE2   . GLU   D 3  19  ? 29.317  88.413  85.374  1.00 59.49  ? 21  GLU   E OE2   1 
ATOM   10399 N  N     . VAL   D 3  20  ? 24.475  90.947  86.108  1.00 35.72  ? 22  VAL   E N     1 
ATOM   10400 C  CA    . VAL   D 3  20  ? 23.594  90.684  87.238  1.00 46.04  ? 22  VAL   E CA    1 
ATOM   10401 C  C     . VAL   D 3  20  ? 23.760  89.215  87.594  1.00 49.24  ? 22  VAL   E C     1 
ATOM   10402 O  O     . VAL   D 3  20  ? 23.362  88.339  86.821  1.00 50.55  ? 22  VAL   E O     1 
ATOM   10403 C  CB    . VAL   D 3  20  ? 22.121  91.014  86.943  1.00 47.23  ? 22  VAL   E CB    1 
ATOM   10404 C  CG1   . VAL   D 3  20  ? 21.781  90.728  85.502  1.00 49.40  ? 22  VAL   E CG1   1 
ATOM   10405 C  CG2   . VAL   D 3  20  ? 21.208  90.206  87.846  1.00 52.71  ? 22  VAL   E CG2   1 
ATOM   10406 N  N     . ILE   D 3  21  ? 24.346  88.940  88.757  1.00 59.20  ? 23  ILE   E N     1 
ATOM   10407 C  CA    . ILE   D 3  21  ? 24.602  87.577  89.204  1.00 58.68  ? 23  ILE   E CA    1 
ATOM   10408 C  C     . ILE   D 3  21  ? 23.707  87.275  90.403  1.00 53.31  ? 23  ILE   E C     1 
ATOM   10409 O  O     . ILE   D 3  21  ? 23.608  88.077  91.335  1.00 59.75  ? 23  ILE   E O     1 
ATOM   10410 C  CB    . ILE   D 3  21  ? 26.096  87.370  89.509  1.00 52.18  ? 23  ILE   E CB    1 
ATOM   10411 C  CG1   . ILE   D 3  21  ? 26.345  87.130  90.983  1.00 55.77  ? 23  ILE   E CG1   1 
ATOM   10412 C  CG2   . ILE   D 3  21  ? 26.913  88.564  89.034  1.00 43.34  ? 23  ILE   E CG2   1 
ATOM   10413 C  CD1   . ILE   D 3  21  ? 27.827  87.195  91.311  1.00 65.13  ? 23  ILE   E CD1   1 
ATOM   10414 N  N     . LEU   D 3  22  ? 23.033  86.127  90.356  1.00 59.15  ? 24  LEU   E N     1 
ATOM   10415 C  CA    . LEU   D 3  22  ? 22.023  85.741  91.335  1.00 62.82  ? 24  LEU   E CA    1 
ATOM   10416 C  C     . LEU   D 3  22  ? 22.523  84.688  92.319  1.00 60.79  ? 24  LEU   E C     1 
ATOM   10417 O  O     . LEU   D 3  22  ? 21.724  84.154  93.092  1.00 57.26  ? 24  LEU   E O     1 
ATOM   10418 C  CB    . LEU   D 3  22  ? 20.773  85.208  90.624  1.00 49.42  ? 24  LEU   E CB    1 
ATOM   10419 C  CG    . LEU   D 3  22  ? 19.905  86.106  89.739  1.00 65.10  ? 24  LEU   E CG    1 
ATOM   10420 C  CD1   . LEU   D 3  22  ? 20.695  87.286  89.170  1.00 65.90  ? 24  LEU   E CD1   1 
ATOM   10421 C  CD2   . LEU   D 3  22  ? 19.268  85.290  88.609  1.00 52.41  ? 24  LEU   E CD2   1 
ATOM   10422 N  N     . LYS   D 3  23  ? 23.818  84.381  92.312  1.00 63.51  ? 25  LYS   E N     1 
ATOM   10423 C  CA    . LYS   D 3  23  ? 24.342  83.231  93.042  1.00 63.07  ? 25  LYS   E CA    1 
ATOM   10424 C  C     . LYS   D 3  23  ? 25.763  82.936  92.564  1.00 66.36  ? 25  LYS   E C     1 
ATOM   10425 O  O     . LYS   D 3  23  ? 26.007  82.890  91.350  1.00 67.08  ? 25  LYS   E O     1 
ATOM   10426 C  CB    . LYS   D 3  23  ? 23.414  82.029  92.830  1.00 60.17  ? 25  LYS   E CB    1 
ATOM   10427 C  CG    . LYS   D 3  23  ? 23.753  80.763  93.602  1.00 67.83  ? 25  LYS   E CG    1 
ATOM   10428 C  CD    . LYS   D 3  23  ? 22.524  79.861  93.699  1.00 62.33  ? 25  LYS   E CD    1 
ATOM   10429 C  CE    . LYS   D 3  23  ? 21.812  79.731  92.357  1.00 63.72  ? 25  LYS   E CE    1 
ATOM   10430 N  NZ    . LYS   D 3  23  ? 20.342  79.481  92.514  1.00 70.71  ? 25  LYS   E NZ    1 
ATOM   10431 N  N     . PRO   D 3  24  ? 26.730  82.762  93.462  1.00 69.16  ? 26  PRO   E N     1 
ATOM   10432 C  CA    . PRO   D 3  24  ? 28.104  82.443  93.022  1.00 72.04  ? 26  PRO   E CA    1 
ATOM   10433 C  C     . PRO   D 3  24  ? 28.232  80.965  92.688  1.00 67.08  ? 26  PRO   E C     1 
ATOM   10434 O  O     . PRO   D 3  24  ? 27.320  80.176  92.983  1.00 61.44  ? 26  PRO   E O     1 
ATOM   10435 C  CB    . PRO   D 3  24  ? 28.970  82.823  94.238  1.00 59.61  ? 26  PRO   E CB    1 
ATOM   10436 C  CG    . PRO   D 3  24  ? 28.029  83.502  95.216  1.00 64.98  ? 26  PRO   E CG    1 
ATOM   10437 C  CD    . PRO   D 3  24  ? 26.659  82.975  94.914  1.00 58.25  ? 26  PRO   E CD    1 
ATOM   10438 N  N     . PRO   D 3  25  ? 29.361  80.539  92.067  1.00 64.92  ? 27  PRO   E N     1 
ATOM   10439 C  CA    . PRO   D 3  25  ? 29.525  79.116  91.710  1.00 67.13  ? 27  PRO   E CA    1 
ATOM   10440 C  C     . PRO   D 3  25  ? 29.483  78.124  92.880  1.00 64.63  ? 27  PRO   E C     1 
ATOM   10441 O  O     . PRO   D 3  25  ? 28.465  78.032  93.584  1.00 47.13  ? 27  PRO   E O     1 
ATOM   10442 C  CB    . PRO   D 3  25  ? 30.894  79.088  91.003  1.00 60.72  ? 27  PRO   E CB    1 
ATOM   10443 C  CG    . PRO   D 3  25  ? 31.540  80.398  91.292  1.00 51.11  ? 27  PRO   E CG    1 
ATOM   10444 C  CD    . PRO   D 3  25  ? 30.433  81.376  91.500  1.00 57.70  ? 27  PRO   E CD    1 
ATOM   10445 N  N     . SER   D 3  26  ? 30.574  77.358  93.049  1.00 62.01  ? 28  SER   E N     1 
ATOM   10446 C  CA    . SER   D 3  26  ? 30.729  76.242  94.015  1.00 55.11  ? 28  SER   E CA    1 
ATOM   10447 C  C     . SER   D 3  26  ? 31.245  74.986  93.310  1.00 55.48  ? 28  SER   E C     1 
ATOM   10448 O  O     . SER   D 3  26  ? 32.454  74.783  93.162  1.00 50.53  ? 28  SER   E O     1 
ATOM   10449 C  CB    . SER   D 3  26  ? 29.421  75.901  94.753  1.00 43.17  ? 28  SER   E CB    1 
ATOM   10450 O  OG    . SER   D 3  26  ? 28.416  75.419  93.874  1.00 50.81  ? 28  SER   E OG    1 
ATOM   10451 N  N     . ASP   D 3  42  ? 47.279  71.737  66.042  1.00 59.75  ? 44  ASP   E N     1 
ATOM   10452 C  CA    . ASP   D 3  42  ? 46.932  72.737  65.032  1.00 84.24  ? 44  ASP   E CA    1 
ATOM   10453 C  C     . ASP   D 3  42  ? 47.868  72.612  63.823  1.00 87.76  ? 44  ASP   E C     1 
ATOM   10454 O  O     . ASP   D 3  42  ? 49.075  72.857  63.934  1.00 87.50  ? 44  ASP   E O     1 
ATOM   10455 C  CB    . ASP   D 3  42  ? 46.986  74.153  65.635  1.00 95.33  ? 44  ASP   E CB    1 
ATOM   10456 C  CG    . ASP   D 3  42  ? 46.138  75.171  64.857  1.00 94.31  ? 44  ASP   E CG    1 
ATOM   10457 O  OD1   . ASP   D 3  42  ? 46.640  75.731  63.850  1.00 74.76  ? 44  ASP   E OD1   1 
ATOM   10458 O  OD2   . ASP   D 3  42  ? 44.969  75.409  65.260  1.00 81.48  ? 44  ASP   E OD2   1 
ATOM   10459 N  N     . PRO   D 3  43  ? 47.310  72.241  62.671  1.00 86.07  ? 45  PRO   E N     1 
ATOM   10460 C  CA    . PRO   D 3  43  ? 48.146  71.893  61.516  1.00 84.56  ? 45  PRO   E CA    1 
ATOM   10461 C  C     . PRO   D 3  43  ? 48.760  73.125  60.865  1.00 79.59  ? 45  PRO   E C     1 
ATOM   10462 O  O     . PRO   D 3  43  ? 48.358  74.269  61.095  1.00 75.23  ? 45  PRO   E O     1 
ATOM   10463 C  CB    . PRO   D 3  43  ? 47.177  71.182  60.560  1.00 79.33  ? 45  PRO   E CB    1 
ATOM   10464 C  CG    . PRO   D 3  43  ? 45.820  71.187  61.250  1.00 80.46  ? 45  PRO   E CG    1 
ATOM   10465 C  CD    . PRO   D 3  43  ? 45.879  72.218  62.332  1.00 78.94  ? 45  PRO   E CD    1 
ATOM   10466 N  N     . SER   D 3  44  ? 49.748  72.857  60.014  1.00 74.28  ? 46  SER   E N     1 
ATOM   10467 C  CA    . SER   D 3  44  ? 50.560  73.877  59.373  1.00 74.63  ? 46  SER   E CA    1 
ATOM   10468 C  C     . SER   D 3  44  ? 50.461  73.762  57.857  1.00 72.34  ? 46  SER   E C     1 
ATOM   10469 O  O     . SER   D 3  44  ? 50.131  72.704  57.315  1.00 73.92  ? 46  SER   E O     1 
ATOM   10470 C  CB    . SER   D 3  44  ? 52.016  73.744  59.809  1.00 74.20  ? 46  SER   E CB    1 
ATOM   10471 O  OG    . SER   D 3  44  ? 52.357  72.370  59.891  1.00 81.31  ? 46  SER   E OG    1 
ATOM   10472 N  N     . LEU   D 3  45  ? 50.767  74.865  57.166  1.00 73.61  ? 47  LEU   E N     1 
ATOM   10473 C  CA    . LEU   D 3  45  ? 50.703  74.857  55.706  1.00 73.27  ? 47  LEU   E CA    1 
ATOM   10474 C  C     . LEU   D 3  45  ? 51.469  73.686  55.111  1.00 76.00  ? 47  LEU   E C     1 
ATOM   10475 O  O     . LEU   D 3  45  ? 51.182  73.272  53.983  1.00 78.07  ? 47  LEU   E O     1 
ATOM   10476 C  CB    . LEU   D 3  45  ? 51.246  76.167  55.140  1.00 64.43  ? 47  LEU   E CB    1 
ATOM   10477 C  CG    . LEU   D 3  45  ? 51.310  76.212  53.617  1.00 70.59  ? 47  LEU   E CG    1 
ATOM   10478 C  CD1   . LEU   D 3  45  ? 49.971  75.766  53.031  1.00 63.45  ? 47  LEU   E CD1   1 
ATOM   10479 C  CD2   . LEU   D 3  45  ? 51.697  77.610  53.133  1.00 56.93  ? 47  LEU   E CD2   1 
ATOM   10480 N  N     . GLU   D 3  46  ? 52.437  73.146  55.845  1.00 72.90  ? 48  GLU   E N     1 
ATOM   10481 C  CA    . GLU   D 3  46  ? 53.150  71.949  55.430  1.00 79.13  ? 48  GLU   E CA    1 
ATOM   10482 C  C     . GLU   D 3  46  ? 52.219  70.746  55.458  1.00 63.58  ? 48  GLU   E C     1 
ATOM   10483 O  O     . GLU   D 3  46  ? 51.893  70.187  54.410  1.00 66.83  ? 48  GLU   E O     1 
ATOM   10484 C  CB    . GLU   D 3  46  ? 54.356  71.715  56.340  1.00 86.50  ? 48  GLU   E CB    1 
ATOM   10485 C  CG    . GLU   D 3  46  ? 55.348  70.681  55.854  1.00 71.70  ? 48  GLU   E CG    1 
ATOM   10486 C  CD    . GLU   D 3  46  ? 56.422  70.424  56.891  1.00 98.53  ? 48  GLU   E CD    1 
ATOM   10487 O  OE1   . GLU   D 3  46  ? 56.083  70.368  58.095  1.00 93.69  ? 48  GLU   E OE1   1 
ATOM   10488 O  OE2   . GLU   D 3  46  ? 57.605  70.298  56.509  1.00 110.32 ? 48  GLU   E OE2   1 
ATOM   10489 N  N     . GLU   D 3  47  ? 51.778  70.353  56.654  1.00 64.77  ? 49  GLU   E N     1 
ATOM   10490 C  CA    . GLU   D 3  47  ? 50.920  69.180  56.789  1.00 64.75  ? 49  GLU   E CA    1 
ATOM   10491 C  C     . GLU   D 3  47  ? 49.652  69.302  55.958  1.00 69.72  ? 49  GLU   E C     1 
ATOM   10492 O  O     . GLU   D 3  47  ? 49.056  68.283  55.594  1.00 68.94  ? 49  GLU   E O     1 
ATOM   10493 C  CB    . GLU   D 3  47  ? 50.546  68.962  58.253  1.00 72.51  ? 49  GLU   E CB    1 
ATOM   10494 C  CG    . GLU   D 3  47  ? 51.717  68.843  59.210  1.00 77.74  ? 49  GLU   E CG    1 
ATOM   10495 C  CD    . GLU   D 3  47  ? 51.324  69.238  60.616  1.00 82.31  ? 49  GLU   E CD    1 
ATOM   10496 O  OE1   . GLU   D 3  47  ? 50.868  70.393  60.777  1.00 76.56  ? 49  GLU   E OE1   1 
ATOM   10497 O  OE2   . GLU   D 3  47  ? 51.450  68.398  61.543  1.00 79.02  ? 49  GLU   E OE2   1 
ATOM   10498 N  N     . ILE   D 3  48  ? 49.218  70.533  55.661  1.00 67.04  ? 50  ILE   E N     1 
ATOM   10499 C  CA    . ILE   D 3  48  ? 48.010  70.732  54.863  1.00 65.20  ? 50  ILE   E CA    1 
ATOM   10500 C  C     . ILE   D 3  48  ? 48.247  70.308  53.417  1.00 66.48  ? 50  ILE   E C     1 
ATOM   10501 O  O     . ILE   D 3  48  ? 47.353  69.748  52.766  1.00 56.58  ? 50  ILE   E O     1 
ATOM   10502 C  CB    . ILE   D 3  48  ? 47.538  72.199  54.966  1.00 66.02  ? 50  ILE   E CB    1 
ATOM   10503 C  CG1   . ILE   D 3  48  ? 47.023  72.506  56.375  1.00 67.30  ? 50  ILE   E CG1   1 
ATOM   10504 C  CG2   . ILE   D 3  48  ? 46.442  72.518  53.958  1.00 54.52  ? 50  ILE   E CG2   1 
ATOM   10505 C  CD1   . ILE   D 3  48  ? 46.496  73.912  56.535  1.00 54.73  ? 50  ILE   E CD1   1 
ATOM   10506 N  N     . GLN   D 3  49  ? 49.454  70.563  52.891  1.00 67.65  ? 51  GLN   E N     1 
ATOM   10507 C  CA    . GLN   D 3  49  ? 49.766  70.170  51.518  1.00 67.06  ? 51  GLN   E CA    1 
ATOM   10508 C  C     . GLN   D 3  49  ? 49.876  68.659  51.389  1.00 59.70  ? 51  GLN   E C     1 
ATOM   10509 O  O     . GLN   D 3  49  ? 49.360  68.073  50.435  1.00 63.23  ? 51  GLN   E O     1 
ATOM   10510 C  CB    . GLN   D 3  49  ? 51.057  70.833  51.051  1.00 73.41  ? 51  GLN   E CB    1 
ATOM   10511 C  CG    . GLN   D 3  49  ? 51.101  72.337  51.245  1.00 77.62  ? 51  GLN   E CG    1 
ATOM   10512 C  CD    . GLN   D 3  49  ? 50.006  73.060  50.486  1.00 87.82  ? 51  GLN   E CD    1 
ATOM   10513 O  OE1   . GLN   D 3  49  ? 48.825  72.719  50.593  1.00 85.37  ? 51  GLN   E OE1   1 
ATOM   10514 N  NE2   . GLN   D 3  49  ? 50.392  74.071  49.715  1.00 79.46  ? 51  GLN   E NE2   1 
ATOM   10515 N  N     . LYS   D 3  50  ? 50.542  68.009  52.339  1.00 62.23  ? 52  LYS   E N     1 
ATOM   10516 C  CA    . LYS   D 3  50  ? 50.613  66.554  52.309  1.00 66.53  ? 52  LYS   E CA    1 
ATOM   10517 C  C     . LYS   D 3  50  ? 49.225  65.929  52.378  1.00 69.45  ? 52  LYS   E C     1 
ATOM   10518 O  O     . LYS   D 3  50  ? 48.995  64.858  51.804  1.00 64.69  ? 52  LYS   E O     1 
ATOM   10519 C  CB    . LYS   D 3  50  ? 51.491  66.050  53.454  1.00 53.98  ? 52  LYS   E CB    1 
ATOM   10520 C  CG    . LYS   D 3  50  ? 51.808  64.574  53.383  1.00 66.47  ? 52  LYS   E CG    1 
ATOM   10521 C  CD    . LYS   D 3  50  ? 53.117  64.253  54.109  1.00 91.00  ? 52  LYS   E CD    1 
ATOM   10522 C  CE    . LYS   D 3  50  ? 53.286  62.749  54.342  1.00 80.00  ? 52  LYS   E CE    1 
ATOM   10523 N  NZ    . LYS   D 3  50  ? 52.330  62.226  55.364  1.00 47.90  ? 52  LYS   E NZ    1 
ATOM   10524 N  N     . LYS   D 3  51  ? 48.290  66.579  53.073  1.00 71.61  ? 53  LYS   E N     1 
ATOM   10525 C  CA    . LYS   D 3  51  ? 46.925  66.073  53.140  1.00 66.03  ? 53  LYS   E CA    1 
ATOM   10526 C  C     . LYS   D 3  51  ? 46.228  66.206  51.788  1.00 61.22  ? 53  LYS   E C     1 
ATOM   10527 O  O     . LYS   D 3  51  ? 45.691  65.228  51.250  1.00 53.37  ? 53  LYS   E O     1 
ATOM   10528 C  CB    . LYS   D 3  51  ? 46.160  66.819  54.238  1.00 63.89  ? 53  LYS   E CB    1 
ATOM   10529 C  CG    . LYS   D 3  51  ? 44.767  66.298  54.529  1.00 73.59  ? 53  LYS   E CG    1 
ATOM   10530 C  CD    . LYS   D 3  51  ? 44.488  66.267  56.035  1.00 91.39  ? 53  LYS   E CD    1 
ATOM   10531 C  CE    . LYS   D 3  51  ? 45.387  65.249  56.751  1.00 82.59  ? 53  LYS   E CE    1 
ATOM   10532 N  NZ    . LYS   D 3  51  ? 44.925  64.934  58.138  1.00 76.62  ? 53  LYS   E NZ    1 
ATOM   10533 N  N     . LEU   D 3  52  ? 46.244  67.410  51.216  1.00 50.26  ? 54  LEU   E N     1 
ATOM   10534 C  CA    . LEU   D 3  52  ? 45.569  67.634  49.946  1.00 50.01  ? 54  LEU   E CA    1 
ATOM   10535 C  C     . LEU   D 3  52  ? 46.197  66.805  48.832  1.00 60.21  ? 54  LEU   E C     1 
ATOM   10536 O  O     . LEU   D 3  52  ? 45.499  66.083  48.110  1.00 62.84  ? 54  LEU   E O     1 
ATOM   10537 C  CB    . LEU   D 3  52  ? 45.598  69.120  49.601  1.00 49.59  ? 54  LEU   E CB    1 
ATOM   10538 C  CG    . LEU   D 3  52  ? 44.841  69.992  50.597  1.00 50.84  ? 54  LEU   E CG    1 
ATOM   10539 C  CD1   . LEU   D 3  52  ? 44.923  71.458  50.220  1.00 48.69  ? 54  LEU   E CD1   1 
ATOM   10540 C  CD2   . LEU   D 3  52  ? 43.387  69.533  50.669  1.00 46.23  ? 54  LEU   E CD2   1 
ATOM   10541 N  N     . GLU   D 3  53  ? 47.522  66.890  48.680  1.00 61.31  ? 55  GLU   E N     1 
ATOM   10542 C  CA    . GLU   D 3  53  ? 48.195  66.174  47.600  1.00 59.36  ? 55  GLU   E CA    1 
ATOM   10543 C  C     . GLU   D 3  53  ? 47.945  64.669  47.681  1.00 55.28  ? 55  GLU   E C     1 
ATOM   10544 O  O     . GLU   D 3  53  ? 47.644  64.026  46.671  1.00 55.54  ? 55  GLU   E O     1 
ATOM   10545 C  CB    . GLU   D 3  53  ? 49.691  66.486  47.619  1.00 52.74  ? 55  GLU   E CB    1 
ATOM   10546 C  CG    . GLU   D 3  53  ? 50.056  67.673  46.759  1.00 60.33  ? 55  GLU   E CG    1 
ATOM   10547 C  CD    . GLU   D 3  53  ? 51.362  68.302  47.166  1.00 74.64  ? 55  GLU   E CD    1 
ATOM   10548 O  OE1   . GLU   D 3  53  ? 52.040  67.735  48.054  1.00 78.52  ? 55  GLU   E OE1   1 
ATOM   10549 O  OE2   . GLU   D 3  53  ? 51.703  69.368  46.605  1.00 80.60  ? 55  GLU   E OE2   1 
ATOM   10550 N  N     . ALA   D 3  54  ? 48.075  64.085  48.874  1.00 43.52  ? 56  ALA   E N     1 
ATOM   10551 C  CA    . ALA   D 3  54  ? 47.714  62.681  49.037  1.00 51.70  ? 56  ALA   E CA    1 
ATOM   10552 C  C     . ALA   D 3  54  ? 46.325  62.378  48.481  1.00 59.24  ? 56  ALA   E C     1 
ATOM   10553 O  O     . ALA   D 3  54  ? 46.082  61.280  47.966  1.00 52.61  ? 56  ALA   E O     1 
ATOM   10554 C  CB    . ALA   D 3  54  ? 47.771  62.291  50.511  1.00 31.95  ? 56  ALA   E CB    1 
ATOM   10555 N  N     . ALA   D 3  55  ? 45.402  63.335  48.587  1.00 63.86  ? 57  ALA   E N     1 
ATOM   10556 C  CA    . ALA   D 3  55  ? 44.036  63.130  48.132  1.00 50.36  ? 57  ALA   E CA    1 
ATOM   10557 C  C     . ALA   D 3  55  ? 43.957  63.187  46.612  1.00 50.74  ? 57  ALA   E C     1 
ATOM   10558 O  O     . ALA   D 3  55  ? 43.491  62.240  45.969  1.00 57.02  ? 57  ALA   E O     1 
ATOM   10559 C  CB    . ALA   D 3  55  ? 43.115  64.171  48.770  1.00 49.41  ? 57  ALA   E CB    1 
ATOM   10560 N  N     . GLU   D 3  56  ? 44.410  64.293  46.016  1.00 54.52  ? 58  GLU   E N     1 
ATOM   10561 C  CA    . GLU   D 3  56  ? 44.490  64.355  44.557  1.00 60.03  ? 58  GLU   E CA    1 
ATOM   10562 C  C     . GLU   D 3  56  ? 45.352  63.231  43.991  1.00 56.83  ? 58  GLU   E C     1 
ATOM   10563 O  O     . GLU   D 3  56  ? 45.188  62.847  42.830  1.00 54.78  ? 58  GLU   E O     1 
ATOM   10564 C  CB    . GLU   D 3  56  ? 45.045  65.700  44.116  1.00 49.13  ? 58  GLU   E CB    1 
ATOM   10565 C  CG    . GLU   D 3  56  ? 46.380  65.589  43.455  1.00 51.09  ? 58  GLU   E CG    1 
ATOM   10566 C  CD    . GLU   D 3  56  ? 47.037  66.943  43.322  1.00 75.13  ? 58  GLU   E CD    1 
ATOM   10567 O  OE1   . GLU   D 3  56  ? 46.459  67.810  42.621  1.00 63.12  ? 58  GLU   E OE1   1 
ATOM   10568 O  OE2   . GLU   D 3  56  ? 48.111  67.149  43.941  1.00 70.06  ? 58  GLU   E OE2   1 
ATOM   10569 N  N     . GLU   D 3  57  ? 46.289  62.718  44.788  1.00 68.13  ? 59  GLU   E N     1 
ATOM   10570 C  CA    . GLU   D 3  57  ? 46.978  61.474  44.467  1.00 61.74  ? 59  GLU   E CA    1 
ATOM   10571 C  C     . GLU   D 3  57  ? 46.003  60.308  44.407  1.00 57.79  ? 59  GLU   E C     1 
ATOM   10572 O  O     . GLU   D 3  57  ? 45.877  59.634  43.380  1.00 62.85  ? 59  GLU   E O     1 
ATOM   10573 C  CB    . GLU   D 3  57  ? 48.050  61.194  45.519  1.00 66.27  ? 59  GLU   E CB    1 
ATOM   10574 C  CG    . GLU   D 3  57  ? 49.018  60.121  45.107  1.00 71.84  ? 59  GLU   E CG    1 
ATOM   10575 C  CD    . GLU   D 3  57  ? 49.753  60.521  43.850  1.00 98.52  ? 59  GLU   E CD    1 
ATOM   10576 O  OE1   . GLU   D 3  57  ? 49.609  61.700  43.444  1.00 90.36  ? 59  GLU   E OE1   1 
ATOM   10577 O  OE2   . GLU   D 3  57  ? 50.464  59.668  43.268  1.00 106.87 ? 59  GLU   E OE2   1 
ATOM   10578 N  N     . ARG   D 3  58  ? 45.326  60.037  45.526  1.00 55.02  ? 60  ARG   E N     1 
ATOM   10579 C  CA    . ARG   D 3  58  ? 44.399  58.916  45.587  1.00 51.48  ? 60  ARG   E CA    1 
ATOM   10580 C  C     . ARG   D 3  58  ? 43.392  58.964  44.450  1.00 58.45  ? 60  ARG   E C     1 
ATOM   10581 O  O     . ARG   D 3  58  ? 42.897  57.920  44.011  1.00 61.17  ? 60  ARG   E O     1 
ATOM   10582 C  CB    . ARG   D 3  58  ? 43.686  58.900  46.942  1.00 53.95  ? 60  ARG   E CB    1 
ATOM   10583 C  CG    . ARG   D 3  58  ? 44.486  58.238  48.060  1.00 47.20  ? 60  ARG   E CG    1 
ATOM   10584 C  CD    . ARG   D 3  58  ? 43.650  57.985  49.326  1.00 59.04  ? 60  ARG   E CD    1 
ATOM   10585 N  NE    . ARG   D 3  58  ? 43.128  59.218  49.902  1.00 52.15  ? 60  ARG   E NE    1 
ATOM   10586 C  CZ    . ARG   D 3  58  ? 43.889  60.196  50.373  1.00 57.78  ? 60  ARG   E CZ    1 
ATOM   10587 N  NH1   . ARG   D 3  58  ? 45.206  60.099  50.383  1.00 53.43  ? 60  ARG   E NH1   1 
ATOM   10588 N  NH2   . ARG   D 3  58  ? 43.315  61.311  50.820  1.00 56.02  ? 60  ARG   E NH2   1 
ATOM   10589 N  N     . ARG   D 3  59  ? 43.095  60.156  43.941  1.00 53.49  ? 61  ARG   E N     1 
ATOM   10590 C  CA    . ARG   D 3  59  ? 42.100  60.271  42.891  1.00 48.65  ? 61  ARG   E CA    1 
ATOM   10591 C  C     . ARG   D 3  59  ? 42.729  60.073  41.513  1.00 54.35  ? 61  ARG   E C     1 
ATOM   10592 O  O     . ARG   D 3  59  ? 42.251  59.245  40.732  1.00 62.93  ? 61  ARG   E O     1 
ATOM   10593 C  CB    . ARG   D 3  59  ? 41.343  61.615  43.028  1.00 42.06  ? 61  ARG   E CB    1 
ATOM   10594 C  CG    . ARG   D 3  59  ? 41.500  62.627  41.909  1.00 44.40  ? 61  ARG   E CG    1 
ATOM   10595 C  CD    . ARG   D 3  59  ? 40.565  63.818  42.105  1.00 38.48  ? 61  ARG   E CD    1 
ATOM   10596 N  NE    . ARG   D 3  59  ? 40.626  64.343  43.467  1.00 63.14  ? 61  ARG   E NE    1 
ATOM   10597 C  CZ    . ARG   D 3  59  ? 41.232  65.470  43.839  1.00 57.87  ? 61  ARG   E CZ    1 
ATOM   10598 N  NH1   . ARG   D 3  59  ? 41.828  66.267  42.962  1.00 60.20  ? 61  ARG   E NH1   1 
ATOM   10599 N  NH2   . ARG   D 3  59  ? 41.241  65.806  45.126  1.00 47.25  ? 61  ARG   E NH2   1 
ATOM   10600 N  N     . LYS   D 3  60  ? 43.823  60.778  41.207  1.00 60.47  ? 62  LYS   E N     1 
ATOM   10601 C  CA    . LYS   D 3  60  ? 44.462  60.596  39.902  1.00 53.82  ? 62  LYS   E CA    1 
ATOM   10602 C  C     . LYS   D 3  60  ? 44.777  59.128  39.636  1.00 54.22  ? 62  LYS   E C     1 
ATOM   10603 O  O     . LYS   D 3  60  ? 44.724  58.680  38.483  1.00 50.79  ? 62  LYS   E O     1 
ATOM   10604 C  CB    . LYS   D 3  60  ? 45.745  61.434  39.792  1.00 45.43  ? 62  LYS   E CB    1 
ATOM   10605 C  CG    . LYS   D 3  60  ? 45.507  62.929  39.717  1.00 50.60  ? 62  LYS   E CG    1 
ATOM   10606 C  CD    . LYS   D 3  60  ? 46.603  63.649  38.943  1.00 46.48  ? 62  LYS   E CD    1 
ATOM   10607 C  CE    . LYS   D 3  60  ? 47.973  63.417  39.536  1.00 60.05  ? 62  LYS   E CE    1 
ATOM   10608 N  NZ    . LYS   D 3  60  ? 48.955  64.262  38.818  1.00 62.50  ? 62  LYS   E NZ    1 
ATOM   10609 N  N     . TYR   D 3  61  ? 45.106  58.366  40.685  1.00 41.90  ? 63  TYR   E N     1 
ATOM   10610 C  CA    . TYR   D 3  61  ? 45.344  56.939  40.507  1.00 49.36  ? 63  TYR   E CA    1 
ATOM   10611 C  C     . TYR   D 3  61  ? 44.047  56.217  40.168  1.00 53.09  ? 63  TYR   E C     1 
ATOM   10612 O  O     . TYR   D 3  61  ? 44.000  55.407  39.234  1.00 54.82  ? 63  TYR   E O     1 
ATOM   10613 C  CB    . TYR   D 3  61  ? 46.003  56.355  41.759  1.00 39.99  ? 63  TYR   E CB    1 
ATOM   10614 C  CG    . TYR   D 3  61  ? 45.926  54.846  41.904  1.00 45.05  ? 63  TYR   E CG    1 
ATOM   10615 C  CD1   . TYR   D 3  61  ? 46.856  54.009  41.288  1.00 52.67  ? 63  TYR   E CD1   1 
ATOM   10616 C  CD2   . TYR   D 3  61  ? 44.939  54.255  42.686  1.00 52.75  ? 63  TYR   E CD2   1 
ATOM   10617 C  CE1   . TYR   D 3  61  ? 46.795  52.620  41.439  1.00 44.88  ? 63  TYR   E CE1   1 
ATOM   10618 C  CE2   . TYR   D 3  61  ? 44.867  52.875  42.844  1.00 43.51  ? 63  TYR   E CE2   1 
ATOM   10619 C  CZ    . TYR   D 3  61  ? 45.797  52.059  42.221  1.00 51.68  ? 63  TYR   E CZ    1 
ATOM   10620 O  OH    . TYR   D 3  61  ? 45.714  50.685  42.388  1.00 46.88  ? 63  TYR   E OH    1 
ATOM   10621 N  N     . GLN   D 3  62  ? 42.972  56.524  40.890  1.00 55.85  ? 64  GLN   E N     1 
ATOM   10622 C  CA    . GLN   D 3  62  ? 41.695  55.880  40.598  1.00 59.09  ? 64  GLN   E CA    1 
ATOM   10623 C  C     . GLN   D 3  62  ? 41.243  56.165  39.168  1.00 50.58  ? 64  GLN   E C     1 
ATOM   10624 O  O     . GLN   D 3  62  ? 40.749  55.267  38.474  1.00 41.50  ? 64  GLN   E O     1 
ATOM   10625 C  CB    . GLN   D 3  62  ? 40.646  56.325  41.620  1.00 55.73  ? 64  GLN   E CB    1 
ATOM   10626 C  CG    . GLN   D 3  62  ? 40.884  55.688  43.001  1.00 67.33  ? 64  GLN   E CG    1 
ATOM   10627 C  CD    . GLN   D 3  62  ? 40.390  56.538  44.163  1.00 60.71  ? 64  GLN   E CD    1 
ATOM   10628 O  OE1   . GLN   D 3  62  ? 39.928  57.670  43.972  1.00 56.06  ? 64  GLN   E OE1   1 
ATOM   10629 N  NE2   . GLN   D 3  62  ? 40.489  55.994  45.377  1.00 40.57  ? 64  GLN   E NE2   1 
ATOM   10630 N  N     . GLU   D 3  63  ? 41.425  57.399  38.700  1.00 40.37  ? 65  GLU   E N     1 
ATOM   10631 C  CA    . GLU   D 3  63  ? 41.039  57.720  37.332  1.00 45.27  ? 65  GLU   E CA    1 
ATOM   10632 C  C     . GLU   D 3  63  ? 41.877  56.939  36.330  1.00 55.55  ? 65  GLU   E C     1 
ATOM   10633 O  O     . GLU   D 3  63  ? 41.355  56.428  35.331  1.00 55.66  ? 65  GLU   E O     1 
ATOM   10634 C  CB    . GLU   D 3  63  ? 41.170  59.222  37.083  1.00 37.86  ? 65  GLU   E CB    1 
ATOM   10635 C  CG    . GLU   D 3  63  ? 41.578  59.556  35.668  1.00 45.14  ? 65  GLU   E CG    1 
ATOM   10636 C  CD    . GLU   D 3  63  ? 41.142  60.950  35.218  1.00 57.52  ? 65  GLU   E CD    1 
ATOM   10637 O  OE1   . GLU   D 3  63  ? 40.049  61.416  35.631  1.00 49.24  ? 65  GLU   E OE1   1 
ATOM   10638 O  OE2   . GLU   D 3  63  ? 41.898  61.574  34.435  1.00 49.15  ? 65  GLU   E OE2   1 
ATOM   10639 N  N     . ALA   D 3  64  ? 43.184  56.837  36.587  1.00 61.18  ? 66  ALA   E N     1 
ATOM   10640 C  CA    . ALA   D 3  64  ? 44.092  56.130  35.692  1.00 51.57  ? 66  ALA   E CA    1 
ATOM   10641 C  C     . ALA   D 3  64  ? 43.833  54.628  35.705  1.00 50.31  ? 66  ALA   E C     1 
ATOM   10642 O  O     . ALA   D 3  64  ? 44.047  53.952  34.692  1.00 50.48  ? 66  ALA   E O     1 
ATOM   10643 C  CB    . ALA   D 3  64  ? 45.543  56.439  36.083  1.00 48.32  ? 66  ALA   E CB    1 
ATOM   10644 N  N     . GLU   D 3  65  ? 43.399  54.084  36.838  1.00 48.89  ? 67  GLU   E N     1 
ATOM   10645 C  CA    . GLU   D 3  65  ? 42.907  52.716  36.831  1.00 50.15  ? 67  GLU   E CA    1 
ATOM   10646 C  C     . GLU   D 3  65  ? 41.737  52.576  35.863  1.00 60.51  ? 67  GLU   E C     1 
ATOM   10647 O  O     . GLU   D 3  65  ? 41.584  51.535  35.209  1.00 58.66  ? 67  GLU   E O     1 
ATOM   10648 C  CB    . GLU   D 3  65  ? 42.502  52.307  38.245  1.00 43.12  ? 67  GLU   E CB    1 
ATOM   10649 C  CG    . GLU   D 3  65  ? 42.813  50.862  38.588  1.00 56.20  ? 67  GLU   E CG    1 
ATOM   10650 C  CD    . GLU   D 3  65  ? 44.275  50.535  38.392  1.00 65.41  ? 67  GLU   E CD    1 
ATOM   10651 O  OE1   . GLU   D 3  65  ? 45.122  51.378  38.765  1.00 70.12  ? 67  GLU   E OE1   1 
ATOM   10652 O  OE2   . GLU   D 3  65  ? 44.577  49.449  37.848  1.00 65.82  ? 67  GLU   E OE2   1 
ATOM   10653 N  N     . LEU   D 3  66  ? 40.924  53.632  35.744  1.00 53.17  ? 68  LEU   E N     1 
ATOM   10654 C  CA    . LEU   D 3  66  ? 39.765  53.608  34.863  1.00 44.69  ? 68  LEU   E CA    1 
ATOM   10655 C  C     . LEU   D 3  66  ? 40.182  53.711  33.407  1.00 50.71  ? 68  LEU   E C     1 
ATOM   10656 O  O     . LEU   D 3  66  ? 39.697  52.957  32.559  1.00 55.16  ? 68  LEU   E O     1 
ATOM   10657 C  CB    . LEU   D 3  66  ? 38.812  54.749  35.207  1.00 49.19  ? 68  LEU   E CB    1 
ATOM   10658 C  CG    . LEU   D 3  66  ? 37.889  55.005  34.014  1.00 50.63  ? 68  LEU   E CG    1 
ATOM   10659 C  CD1   . LEU   D 3  66  ? 36.931  53.837  33.872  1.00 42.96  ? 68  LEU   E CD1   1 
ATOM   10660 C  CD2   . LEU   D 3  66  ? 37.141  56.329  34.080  1.00 36.94  ? 68  LEU   E CD2   1 
ATOM   10661 N  N     . LEU   D 3  67  ? 41.055  54.667  33.086  1.00 54.44  ? 69  LEU   E N     1 
ATOM   10662 C  CA    . LEU   D 3  67  ? 41.531  54.781  31.712  1.00 48.45  ? 69  LEU   E CA    1 
ATOM   10663 C  C     . LEU   D 3  67  ? 42.270  53.522  31.273  1.00 56.37  ? 69  LEU   E C     1 
ATOM   10664 O  O     . LEU   D 3  67  ? 42.282  53.196  30.076  1.00 51.89  ? 69  LEU   E O     1 
ATOM   10665 C  CB    . LEU   D 3  67  ? 42.418  56.015  31.564  1.00 30.31  ? 69  LEU   E CB    1 
ATOM   10666 C  CG    . LEU   D 3  67  ? 41.640  57.336  31.627  1.00 41.94  ? 69  LEU   E CG    1 
ATOM   10667 C  CD1   . LEU   D 3  67  ? 42.565  58.531  31.609  1.00 40.72  ? 69  LEU   E CD1   1 
ATOM   10668 C  CD2   . LEU   D 3  67  ? 40.639  57.455  30.478  1.00 43.16  ? 69  LEU   E CD2   1 
ATOM   10669 N  N     . LYS   D 3  68  ? 42.879  52.795  32.222  1.00 52.43  ? 70  LYS   E N     1 
ATOM   10670 C  CA    . LYS   D 3  68  ? 43.618  51.586  31.865  1.00 49.38  ? 70  LYS   E CA    1 
ATOM   10671 C  C     . LYS   D 3  68  ? 42.664  50.456  31.528  1.00 54.74  ? 70  LYS   E C     1 
ATOM   10672 O  O     . LYS   D 3  68  ? 42.891  49.700  30.573  1.00 49.20  ? 70  LYS   E O     1 
ATOM   10673 C  CB    . LYS   D 3  68  ? 44.553  51.170  33.002  1.00 49.09  ? 70  LYS   E CB    1 
ATOM   10674 C  CG    . LYS   D 3  68  ? 45.030  49.711  32.931  1.00 55.23  ? 70  LYS   E CG    1 
ATOM   10675 C  CD    . LYS   D 3  68  ? 44.537  48.842  34.118  1.00 65.74  ? 70  LYS   E CD    1 
ATOM   10676 C  CE    . LYS   D 3  68  ? 43.019  48.541  34.058  1.00 73.56  ? 70  LYS   E CE    1 
ATOM   10677 N  NZ    . LYS   D 3  68  ? 42.434  47.827  35.255  1.00 74.96  ? 70  LYS   E NZ    1 
ATOM   10678 N  N     . HIS   D 3  69  ? 41.595  50.329  32.315  1.00 54.47  ? 71  HIS   E N     1 
ATOM   10679 C  CA    . HIS   D 3  69  ? 40.560  49.346  32.028  1.00 51.43  ? 71  HIS   E CA    1 
ATOM   10680 C  C     . HIS   D 3  69  ? 39.859  49.666  30.713  1.00 49.89  ? 71  HIS   E C     1 
ATOM   10681 O  O     . HIS   D 3  69  ? 39.608  48.766  29.899  1.00 43.18  ? 71  HIS   E O     1 
ATOM   10682 C  CB    . HIS   D 3  69  ? 39.577  49.304  33.198  1.00 56.64  ? 71  HIS   E CB    1 
ATOM   10683 C  CG    . HIS   D 3  69  ? 38.433  48.361  33.008  1.00 65.45  ? 71  HIS   E CG    1 
ATOM   10684 N  ND1   . HIS   D 3  69  ? 37.402  48.607  32.124  1.00 61.06  ? 71  HIS   E ND1   1 
ATOM   10685 C  CD2   . HIS   D 3  69  ? 38.140  47.186  33.613  1.00 68.96  ? 71  HIS   E CD2   1 
ATOM   10686 C  CE1   . HIS   D 3  69  ? 36.528  47.619  32.187  1.00 69.26  ? 71  HIS   E CE1   1 
ATOM   10687 N  NE2   . HIS   D 3  69  ? 36.951  46.744  33.084  1.00 64.03  ? 71  HIS   E NE2   1 
ATOM   10688 N  N     . LEU   D 3  70  ? 39.582  50.955  30.465  1.00 47.77  ? 72  LEU   E N     1 
ATOM   10689 C  CA    . LEU   D 3  70  ? 39.000  51.370  29.189  1.00 38.58  ? 72  LEU   E CA    1 
ATOM   10690 C  C     . LEU   D 3  70  ? 39.923  51.090  28.007  1.00 40.87  ? 72  LEU   E C     1 
ATOM   10691 O  O     . LEU   D 3  70  ? 39.442  50.902  26.888  1.00 47.56  ? 72  LEU   E O     1 
ATOM   10692 C  CB    . LEU   D 3  70  ? 38.639  52.851  29.223  1.00 39.71  ? 72  LEU   E CB    1 
ATOM   10693 C  CG    . LEU   D 3  70  ? 37.340  53.242  29.934  1.00 45.29  ? 72  LEU   E CG    1 
ATOM   10694 C  CD1   . LEU   D 3  70  ? 37.044  54.728  29.711  1.00 35.53  ? 72  LEU   E CD1   1 
ATOM   10695 C  CD2   . LEU   D 3  70  ? 36.160  52.363  29.499  1.00 39.11  ? 72  LEU   E CD2   1 
ATOM   10696 N  N     . ALA   D 3  71  ? 41.240  51.074  28.207  1.00 44.48  ? 73  ALA   E N     1 
ATOM   10697 C  CA    . ALA   D 3  71  ? 42.112  50.713  27.095  1.00 37.79  ? 73  ALA   E CA    1 
ATOM   10698 C  C     . ALA   D 3  71  ? 42.219  49.204  26.905  1.00 39.66  ? 73  ALA   E C     1 
ATOM   10699 O  O     . ALA   D 3  71  ? 42.515  48.748  25.798  1.00 33.31  ? 73  ALA   E O     1 
ATOM   10700 C  CB    . ALA   D 3  71  ? 43.500  51.317  27.278  1.00 33.43  ? 73  ALA   E CB    1 
ATOM   10701 N  N     . GLU   D 3  72  ? 41.990  48.408  27.946  1.00 42.65  ? 74  GLU   E N     1 
ATOM   10702 C  CA    . GLU   D 3  72  ? 41.790  46.986  27.706  1.00 38.89  ? 74  GLU   E CA    1 
ATOM   10703 C  C     . GLU   D 3  72  ? 40.553  46.754  26.837  1.00 45.49  ? 74  GLU   E C     1 
ATOM   10704 O  O     . GLU   D 3  72  ? 40.543  45.847  25.998  1.00 48.08  ? 74  GLU   E O     1 
ATOM   10705 C  CB    . GLU   D 3  72  ? 41.671  46.222  29.021  1.00 40.27  ? 74  GLU   E CB    1 
ATOM   10706 C  CG    . GLU   D 3  72  ? 42.866  46.333  29.954  1.00 49.12  ? 74  GLU   E CG    1 
ATOM   10707 C  CD    . GLU   D 3  72  ? 42.567  45.749  31.338  1.00 58.23  ? 74  GLU   E CD    1 
ATOM   10708 O  OE1   . GLU   D 3  72  ? 41.370  45.543  31.649  1.00 55.72  ? 74  GLU   E OE1   1 
ATOM   10709 O  OE2   . GLU   D 3  72  ? 43.523  45.492  32.111  1.00 60.32  ? 74  GLU   E OE2   1 
ATOM   10710 N  N     . LYS   D 3  73  ? 39.500  47.565  27.014  1.00 47.17  ? 75  LYS   E N     1 
ATOM   10711 C  CA    . LYS   D 3  73  ? 38.305  47.389  26.187  1.00 46.45  ? 75  LYS   E CA    1 
ATOM   10712 C  C     . LYS   D 3  73  ? 38.564  47.822  24.754  1.00 42.76  ? 75  LYS   E C     1 
ATOM   10713 O  O     . LYS   D 3  73  ? 37.902  47.327  23.835  1.00 45.33  ? 75  LYS   E O     1 
ATOM   10714 C  CB    . LYS   D 3  73  ? 37.101  48.153  26.769  1.00 41.22  ? 75  LYS   E CB    1 
ATOM   10715 C  CG    . LYS   D 3  73  ? 36.467  47.508  28.026  1.00 48.37  ? 75  LYS   E CG    1 
ATOM   10716 C  CD    . LYS   D 3  73  ? 35.598  46.278  27.692  1.00 67.22  ? 75  LYS   E CD    1 
ATOM   10717 C  CE    . LYS   D 3  73  ? 34.533  45.947  28.787  1.00 67.46  ? 75  LYS   E CE    1 
ATOM   10718 N  NZ    . LYS   D 3  73  ? 33.360  45.110  28.270  1.00 38.00  ? 75  LYS   E NZ    1 
ATOM   10719 N  N     . ARG   D 3  74  ? 39.524  48.727  24.542  1.00 40.25  ? 76  ARG   E N     1 
ATOM   10720 C  CA    . ARG   D 3  74  ? 39.909  49.109  23.182  1.00 41.34  ? 76  ARG   E CA    1 
ATOM   10721 C  C     . ARG   D 3  74  ? 40.673  47.998  22.488  1.00 37.49  ? 76  ARG   E C     1 
ATOM   10722 O  O     . ARG   D 3  74  ? 40.588  47.853  21.268  1.00 41.54  ? 76  ARG   E O     1 
ATOM   10723 C  CB    . ARG   D 3  74  ? 40.791  50.355  23.188  1.00 40.55  ? 76  ARG   E CB    1 
ATOM   10724 C  CG    . ARG   D 3  74  ? 40.168  51.578  23.727  1.00 40.50  ? 76  ARG   E CG    1 
ATOM   10725 C  CD    . ARG   D 3  74  ? 39.064  52.101  22.837  1.00 39.59  ? 76  ARG   E CD    1 
ATOM   10726 N  NE    . ARG   D 3  74  ? 38.246  52.978  23.656  1.00 49.90  ? 76  ARG   E NE    1 
ATOM   10727 C  CZ    . ARG   D 3  74  ? 37.130  52.610  24.267  1.00 48.74  ? 76  ARG   E CZ    1 
ATOM   10728 N  NH1   . ARG   D 3  74  ? 36.518  51.470  23.977  1.00 35.92  ? 76  ARG   E NH1   1 
ATOM   10729 N  NH2   . ARG   D 3  74  ? 36.616  53.407  25.196  1.00 57.50  ? 76  ARG   E NH2   1 
ATOM   10730 N  N     . GLU   D 3  75  ? 41.486  47.257  23.238  1.00 39.49  ? 77  GLU   E N     1 
ATOM   10731 C  CA    . GLU   D 3  75  ? 42.259  46.183  22.640  1.00 43.22  ? 77  GLU   E CA    1 
ATOM   10732 C  C     . GLU   D 3  75  ? 41.350  45.020  22.267  1.00 44.24  ? 77  GLU   E C     1 
ATOM   10733 O  O     . GLU   D 3  75  ? 41.480  44.432  21.186  1.00 43.12  ? 77  GLU   E O     1 
ATOM   10734 C  CB    . GLU   D 3  75  ? 43.373  45.747  23.605  1.00 45.30  ? 77  GLU   E CB    1 
ATOM   10735 C  CG    . GLU   D 3  75  ? 44.592  45.159  22.900  1.00 59.98  ? 77  GLU   E CG    1 
ATOM   10736 C  CD    . GLU   D 3  75  ? 45.016  45.980  21.663  1.00 74.38  ? 77  GLU   E CD    1 
ATOM   10737 O  OE1   . GLU   D 3  75  ? 44.905  47.232  21.700  1.00 64.70  ? 77  GLU   E OE1   1 
ATOM   10738 O  OE2   . GLU   D 3  75  ? 45.447  45.372  20.651  1.00 65.50  ? 77  GLU   E OE2   1 
ATOM   10739 N  N     . HIS   D 3  76  ? 40.403  44.696  23.143  1.00 45.30  ? 78  HIS   E N     1 
ATOM   10740 C  CA    . HIS   D 3  76  ? 39.425  43.661  22.843  1.00 37.04  ? 78  HIS   E CA    1 
ATOM   10741 C  C     . HIS   D 3  76  ? 38.584  44.012  21.620  1.00 38.89  ? 78  HIS   E C     1 
ATOM   10742 O  O     . HIS   D 3  76  ? 38.149  43.117  20.891  1.00 36.87  ? 78  HIS   E O     1 
ATOM   10743 C  CB    . HIS   D 3  76  ? 38.536  43.445  24.058  1.00 26.91  ? 78  HIS   E CB    1 
ATOM   10744 C  CG    . HIS   D 3  76  ? 37.413  42.507  23.802  1.00 38.80  ? 78  HIS   E CG    1 
ATOM   10745 N  ND1   . HIS   D 3  76  ? 37.608  41.156  23.626  1.00 40.57  ? 78  HIS   E ND1   1 
ATOM   10746 C  CD2   . HIS   D 3  76  ? 36.086  42.723  23.640  1.00 37.40  ? 78  HIS   E CD2   1 
ATOM   10747 C  CE1   . HIS   D 3  76  ? 36.444  40.574  23.396  1.00 34.26  ? 78  HIS   E CE1   1 
ATOM   10748 N  NE2   . HIS   D 3  76  ? 35.505  41.502  23.399  1.00 35.70  ? 78  HIS   E NE2   1 
ATOM   10749 N  N     . GLU   D 3  77  ? 38.335  45.300  21.382  1.00 31.54  ? 79  GLU   E N     1 
ATOM   10750 C  CA    . GLU   D 3  77  ? 37.542  45.683  20.225  1.00 28.67  ? 79  GLU   E CA    1 
ATOM   10751 C  C     . GLU   D 3  77  ? 38.298  45.417  18.929  1.00 38.05  ? 79  GLU   E C     1 
ATOM   10752 O  O     . GLU   D 3  77  ? 37.717  44.907  17.963  1.00 32.40  ? 79  GLU   E O     1 
ATOM   10753 C  CB    . GLU   D 3  77  ? 37.142  47.150  20.338  1.00 29.62  ? 79  GLU   E CB    1 
ATOM   10754 C  CG    . GLU   D 3  77  ? 36.369  47.448  21.626  1.00 40.09  ? 79  GLU   E CG    1 
ATOM   10755 C  CD    . GLU   D 3  77  ? 36.127  48.938  21.896  1.00 39.26  ? 79  GLU   E CD    1 
ATOM   10756 O  OE1   . GLU   D 3  77  ? 36.687  49.810  21.187  1.00 36.03  ? 79  GLU   E OE1   1 
ATOM   10757 O  OE2   . GLU   D 3  77  ? 35.362  49.226  22.839  1.00 44.88  ? 79  GLU   E OE2   1 
ATOM   10758 N  N     . ARG   D 3  78  ? 39.584  45.786  18.884  1.00 34.28  ? 80  ARG   E N     1 
ATOM   10759 C  CA    . ARG   D 3  78  ? 40.456  45.424  17.772  1.00 36.04  ? 80  ARG   E CA    1 
ATOM   10760 C  C     . ARG   D 3  78  ? 40.414  43.917  17.525  1.00 39.61  ? 80  ARG   E C     1 
ATOM   10761 O  O     . ARG   D 3  78  ? 40.095  43.455  16.424  1.00 35.33  ? 80  ARG   E O     1 
ATOM   10762 C  CB    . ARG   D 3  78  ? 41.899  45.871  18.072  1.00 40.29  ? 80  ARG   E CB    1 
ATOM   10763 C  CG    . ARG   D 3  78  ? 42.246  47.323  17.727  1.00 61.05  ? 80  ARG   E CG    1 
ATOM   10764 C  CD    . ARG   D 3  78  ? 43.304  47.412  16.616  1.00 65.75  ? 80  ARG   E CD    1 
ATOM   10765 N  NE    . ARG   D 3  78  ? 43.632  48.791  16.257  1.00 74.29  ? 80  ARG   E NE    1 
ATOM   10766 C  CZ    . ARG   D 3  78  ? 42.844  49.603  15.558  1.00 77.34  ? 80  ARG   E CZ    1 
ATOM   10767 N  NH1   . ARG   D 3  78  ? 41.645  49.221  15.144  1.00 79.21  ? 80  ARG   E NH1   1 
ATOM   10768 N  NH2   . ARG   D 3  78  ? 43.271  50.829  15.264  1.00 65.15  ? 80  ARG   E NH2   1 
ATOM   10769 N  N     . GLU   D 3  79  ? 40.742  43.139  18.562  1.00 26.21  ? 81  GLU   E N     1 
ATOM   10770 C  CA    . GLU   D 3  79  ? 40.756  41.688  18.456  1.00 30.23  ? 81  GLU   E CA    1 
ATOM   10771 C  C     . GLU   D 3  79  ? 39.470  41.147  17.836  1.00 37.83  ? 81  GLU   E C     1 
ATOM   10772 O  O     . GLU   D 3  79  ? 39.519  40.349  16.887  1.00 38.76  ? 81  GLU   E O     1 
ATOM   10773 C  CB    . GLU   D 3  79  ? 41.007  41.062  19.830  1.00 23.00  ? 81  GLU   E CB    1 
ATOM   10774 C  CG    . GLU   D 3  79  ? 42.415  41.299  20.344  1.00 33.15  ? 81  GLU   E CG    1 
ATOM   10775 C  CD    . GLU   D 3  79  ? 42.682  40.642  21.698  1.00 54.71  ? 81  GLU   E CD    1 
ATOM   10776 O  OE1   . GLU   D 3  79  ? 41.826  39.840  22.147  1.00 43.66  ? 81  GLU   E OE1   1 
ATOM   10777 O  OE2   . GLU   D 3  79  ? 43.747  40.931  22.309  1.00 47.98  ? 81  GLU   E OE2   1 
ATOM   10778 N  N     . VAL   D 3  80  ? 38.303  41.564  18.351  1.00 33.10  ? 82  VAL   E N     1 
ATOM   10779 C  CA    . VAL   D 3  80  ? 37.048  40.998  17.852  1.00 33.36  ? 82  VAL   E CA    1 
ATOM   10780 C  C     . VAL   D 3  80  ? 36.968  41.139  16.339  1.00 29.38  ? 82  VAL   E C     1 
ATOM   10781 O  O     . VAL   D 3  80  ? 36.742  40.150  15.634  1.00 35.29  ? 82  VAL   E O     1 
ATOM   10782 C  CB    . VAL   D 3  80  ? 35.826  41.629  18.550  1.00 34.27  ? 82  VAL   E CB    1 
ATOM   10783 C  CG1   . VAL   D 3  80  ? 34.544  41.412  17.732  1.00 24.97  ? 82  VAL   E CG1   1 
ATOM   10784 C  CG2   . VAL   D 3  80  ? 35.643  41.011  19.913  1.00 33.75  ? 82  VAL   E CG2   1 
ATOM   10785 N  N     . ILE   D 3  81  ? 37.168  42.360  15.817  1.00 20.31  ? 83  ILE   E N     1 
ATOM   10786 C  CA    . ILE   D 3  81  ? 37.043  42.594  14.375  1.00 24.14  ? 83  ILE   E CA    1 
ATOM   10787 C  C     . ILE   D 3  81  ? 38.158  41.893  13.616  1.00 33.18  ? 83  ILE   E C     1 
ATOM   10788 O  O     . ILE   D 3  81  ? 38.006  41.553  12.433  1.00 32.18  ? 83  ILE   E O     1 
ATOM   10789 C  CB    . ILE   D 3  81  ? 37.018  44.094  14.020  1.00 25.82  ? 83  ILE   E CB    1 
ATOM   10790 C  CG1   . ILE   D 3  81  ? 36.943  44.259  12.499  1.00 30.76  ? 83  ILE   E CG1   1 
ATOM   10791 C  CG2   . ILE   D 3  81  ? 38.271  44.794  14.523  1.00 24.38  ? 83  ILE   E CG2   1 
ATOM   10792 C  CD1   . ILE   D 3  81  ? 36.241  45.512  12.068  1.00 34.14  ? 83  ILE   E CD1   1 
ATOM   10793 N  N     . GLN   D 3  82  ? 39.293  41.672  14.263  1.00 28.08  ? 84  GLN   E N     1 
ATOM   10794 C  CA    . GLN   D 3  82  ? 40.306  40.851  13.630  1.00 36.17  ? 84  GLN   E CA    1 
ATOM   10795 C  C     . GLN   D 3  82  ? 39.852  39.397  13.558  1.00 29.97  ? 84  GLN   E C     1 
ATOM   10796 O  O     . GLN   D 3  82  ? 40.060  38.732  12.540  1.00 41.53  ? 84  GLN   E O     1 
ATOM   10797 C  CB    . GLN   D 3  82  ? 41.634  41.000  14.375  1.00 37.49  ? 84  GLN   E CB    1 
ATOM   10798 C  CG    . GLN   D 3  82  ? 42.494  42.151  13.882  1.00 42.59  ? 84  GLN   E CG    1 
ATOM   10799 C  CD    . GLN   D 3  82  ? 43.882  42.140  14.531  1.00 77.82  ? 84  GLN   E CD    1 
ATOM   10800 O  OE1   . GLN   D 3  82  ? 44.049  41.626  15.645  1.00 71.60  ? 84  GLN   E OE1   1 
ATOM   10801 N  NE2   . GLN   D 3  82  ? 44.884  42.691  13.832  1.00 67.11  ? 84  GLN   E NE2   1 
ATOM   10802 N  N     . LYS   D 3  83  ? 39.217  38.894  14.619  1.00 26.42  ? 85  LYS   E N     1 
ATOM   10803 C  CA    . LYS   D 3  83  ? 38.674  37.537  14.607  1.00 31.57  ? 85  LYS   E CA    1 
ATOM   10804 C  C     . LYS   D 3  83  ? 37.682  37.348  13.453  1.00 36.48  ? 85  LYS   E C     1 
ATOM   10805 O  O     . LYS   D 3  83  ? 37.852  36.458  12.613  1.00 37.69  ? 85  LYS   E O     1 
ATOM   10806 C  CB    . LYS   D 3  83  ? 38.017  37.221  15.963  1.00 34.27  ? 85  LYS   E CB    1 
ATOM   10807 C  CG    . LYS   D 3  83  ? 38.408  35.857  16.595  1.00 33.89  ? 85  LYS   E CG    1 
ATOM   10808 C  CD    . LYS   D 3  83  ? 37.240  35.178  17.359  1.00 48.83  ? 85  LYS   E CD    1 
ATOM   10809 C  CE    . LYS   D 3  83  ? 36.148  34.608  16.395  1.00 58.02  ? 85  LYS   E CE    1 
ATOM   10810 N  NZ    . LYS   D 3  83  ? 34.775  34.255  16.981  1.00 40.93  ? 85  LYS   E NZ    1 
ATOM   10811 N  N     . ALA   D 3  84  ? 36.642  38.185  13.389  1.00 26.28  ? 86  ALA   E N     1 
ATOM   10812 C  CA    . ALA   D 3  84  ? 35.691  38.119  12.285  1.00 34.06  ? 86  ALA   E CA    1 
ATOM   10813 C  C     . ALA   D 3  84  ? 36.416  38.048  10.941  1.00 37.14  ? 86  ALA   E C     1 
ATOM   10814 O  O     . ALA   D 3  84  ? 36.180  37.132  10.143  1.00 37.67  ? 86  ALA   E O     1 
ATOM   10815 C  CB    . ALA   D 3  84  ? 34.723  39.316  12.320  1.00 28.44  ? 86  ALA   E CB    1 
ATOM   10816 N  N     . ILE   D 3  85  ? 37.302  39.013  10.669  1.00 31.84  ? 87  ILE   E N     1 
ATOM   10817 C  CA    . ILE   D 3  85  ? 38.029  38.998  9.398   1.00 34.64  ? 87  ILE   E CA    1 
ATOM   10818 C  C     . ILE   D 3  85  ? 38.739  37.665  9.221   1.00 35.40  ? 87  ILE   E C     1 
ATOM   10819 O  O     . ILE   D 3  85  ? 38.634  37.020  8.173   1.00 34.17  ? 87  ILE   E O     1 
ATOM   10820 C  CB    . ILE   D 3  85  ? 39.022  40.171  9.312   1.00 38.19  ? 87  ILE   E CB    1 
ATOM   10821 C  CG1   . ILE   D 3  85  ? 38.311  41.512  9.217   1.00 30.08  ? 87  ILE   E CG1   1 
ATOM   10822 C  CG2   . ILE   D 3  85  ? 39.854  40.051  8.092   1.00 25.13  ? 87  ILE   E CG2   1 
ATOM   10823 C  CD1   . ILE   D 3  85  ? 39.282  42.631  9.351   1.00 34.34  ? 87  ILE   E CD1   1 
ATOM   10824 N  N     . GLU   D 3  86  ? 39.454  37.218  10.259  1.00 32.52  ? 88  GLU   E N     1 
ATOM   10825 C  CA    . GLU   D 3  86  ? 40.272  36.019  10.119  1.00 34.38  ? 88  GLU   E CA    1 
ATOM   10826 C  C     . GLU   D 3  86  ? 39.426  34.773  9.894   1.00 42.28  ? 88  GLU   E C     1 
ATOM   10827 O  O     . GLU   D 3  86  ? 39.891  33.820  9.261   1.00 48.76  ? 88  GLU   E O     1 
ATOM   10828 C  CB    . GLU   D 3  86  ? 41.162  35.846  11.343  1.00 29.24  ? 88  GLU   E CB    1 
ATOM   10829 C  CG    . GLU   D 3  86  ? 41.993  34.558  11.360  1.00 51.48  ? 88  GLU   E CG    1 
ATOM   10830 C  CD    . GLU   D 3  86  ? 42.895  34.374  10.123  1.00 68.75  ? 88  GLU   E CD    1 
ATOM   10831 O  OE1   . GLU   D 3  86  ? 43.202  35.377  9.430   1.00 63.00  ? 88  GLU   E OE1   1 
ATOM   10832 O  OE2   . GLU   D 3  86  ? 43.298  33.214  9.848   1.00 62.92  ? 88  GLU   E OE2   1 
ATOM   10833 N  N     . GLU   D 3  87  ? 38.193  34.754  10.397  1.00 41.22  ? 89  GLU   E N     1 
ATOM   10834 C  CA    . GLU   D 3  87  ? 37.332  33.604  10.154  1.00 43.42  ? 89  GLU   E CA    1 
ATOM   10835 C  C     . GLU   D 3  87  ? 36.702  33.658  8.765   1.00 35.74  ? 89  GLU   E C     1 
ATOM   10836 O  O     . GLU   D 3  87  ? 36.553  32.620  8.113   1.00 32.70  ? 89  GLU   E O     1 
ATOM   10837 C  CB    . GLU   D 3  87  ? 36.266  33.501  11.248  1.00 34.94  ? 89  GLU   E CB    1 
ATOM   10838 C  CG    . GLU   D 3  87  ? 36.776  32.768  12.481  1.00 42.01  ? 89  GLU   E CG    1 
ATOM   10839 C  CD    . GLU   D 3  87  ? 35.914  32.980  13.719  1.00 58.13  ? 89  GLU   E CD    1 
ATOM   10840 O  OE1   . GLU   D 3  87  ? 35.040  33.889  13.728  1.00 62.78  ? 89  GLU   E OE1   1 
ATOM   10841 O  OE2   . GLU   D 3  87  ? 36.124  32.234  14.698  1.00 48.69  ? 89  GLU   E OE2   1 
ATOM   10842 N  N     . ASN   D 3  88  ? 36.336  34.850  8.292   1.00 38.22  ? 90  ASN   E N     1 
ATOM   10843 C  CA    . ASN   D 3  88  ? 35.831  34.972  6.929   1.00 41.00  ? 90  ASN   E CA    1 
ATOM   10844 C  C     . ASN   D 3  88  ? 36.926  34.675  5.903   1.00 41.75  ? 90  ASN   E C     1 
ATOM   10845 O  O     . ASN   D 3  88  ? 36.641  34.149  4.819   1.00 43.38  ? 90  ASN   E O     1 
ATOM   10846 C  CB    . ASN   D 3  88  ? 35.231  36.370  6.710   1.00 33.76  ? 90  ASN   E CB    1 
ATOM   10847 C  CG    . ASN   D 3  88  ? 34.469  36.483  5.386   1.00 57.44  ? 90  ASN   E CG    1 
ATOM   10848 O  OD1   . ASN   D 3  88  ? 33.663  35.608  5.042   1.00 59.91  ? 90  ASN   E OD1   1 
ATOM   10849 N  ND2   . ASN   D 3  88  ? 34.734  37.553  4.629   1.00 53.58  ? 90  ASN   E ND2   1 
ATOM   10850 N  N     . ASN   D 3  89  ? 38.176  34.988  6.228   1.00 32.33  ? 91  ASN   E N     1 
ATOM   10851 C  CA    . ASN   D 3  89  ? 39.258  34.662  5.317   1.00 35.79  ? 91  ASN   E CA    1 
ATOM   10852 C  C     . ASN   D 3  89  ? 39.510  33.163  5.275   1.00 46.72  ? 91  ASN   E C     1 
ATOM   10853 O  O     . ASN   D 3  89  ? 39.726  32.602  4.191   1.00 53.26  ? 91  ASN   E O     1 
ATOM   10854 C  CB    . ASN   D 3  89  ? 40.523  35.433  5.691   1.00 34.62  ? 91  ASN   E CB    1 
ATOM   10855 C  CG    . ASN   D 3  89  ? 40.471  36.876  5.203   1.00 39.10  ? 91  ASN   E CG    1 
ATOM   10856 O  OD1   . ASN   D 3  89  ? 39.590  37.231  4.413   1.00 36.25  ? 91  ASN   E OD1   1 
ATOM   10857 N  ND2   . ASN   D 3  89  ? 41.409  37.709  5.659   1.00 41.21  ? 91  ASN   E ND2   1 
ATOM   10858 N  N     . ASN   D 3  90  ? 39.469  32.482  6.426   1.00 41.71  ? 92  ASN   E N     1 
ATOM   10859 C  CA    . ASN   D 3  90  ? 39.708  31.041  6.384   1.00 47.19  ? 92  ASN   E CA    1 
ATOM   10860 C  C     . ASN   D 3  90  ? 38.565  30.308  5.701   1.00 42.41  ? 92  ASN   E C     1 
ATOM   10861 O  O     . ASN   D 3  90  ? 38.785  29.271  5.069   1.00 44.97  ? 92  ASN   E O     1 
ATOM   10862 C  CB    . ASN   D 3  90  ? 39.957  30.485  7.785   1.00 41.01  ? 92  ASN   E CB    1 
ATOM   10863 C  CG    . ASN   D 3  90  ? 41.390  30.695  8.230   1.00 68.13  ? 92  ASN   E CG    1 
ATOM   10864 O  OD1   . ASN   D 3  90  ? 42.300  30.872  7.399   1.00 61.32  ? 92  ASN   E OD1   1 
ATOM   10865 N  ND2   . ASN   D 3  90  ? 41.607  30.689  9.544   1.00 78.25  ? 92  ASN   E ND2   1 
ATOM   10866 N  N     . PHE   D 3  91  ? 37.353  30.845  5.784   1.00 37.06  ? 93  PHE   E N     1 
ATOM   10867 C  CA    . PHE   D 3  91  ? 36.237  30.208  5.104   1.00 51.21  ? 93  PHE   E CA    1 
ATOM   10868 C  C     . PHE   D 3  91  ? 36.327  30.364  3.582   1.00 50.24  ? 93  PHE   E C     1 
ATOM   10869 O  O     . PHE   D 3  91  ? 35.855  29.491  2.841   1.00 40.28  ? 93  PHE   E O     1 
ATOM   10870 C  CB    . PHE   D 3  91  ? 34.919  30.761  5.629   1.00 39.12  ? 93  PHE   E CB    1 
ATOM   10871 C  CG    . PHE   D 3  91  ? 33.750  30.276  4.872   1.00 45.29  ? 93  PHE   E CG    1 
ATOM   10872 C  CD1   . PHE   D 3  91  ? 33.259  29.001  5.100   1.00 35.35  ? 93  PHE   E CD1   1 
ATOM   10873 C  CD2   . PHE   D 3  91  ? 33.172  31.069  3.892   1.00 39.37  ? 93  PHE   E CD2   1 
ATOM   10874 C  CE1   . PHE   D 3  91  ? 32.196  28.528  4.382   1.00 34.65  ? 93  PHE   E CE1   1 
ATOM   10875 C  CE2   . PHE   D 3  91  ? 32.113  30.603  3.164   1.00 48.47  ? 93  PHE   E CE2   1 
ATOM   10876 C  CZ    . PHE   D 3  91  ? 31.613  29.326  3.411   1.00 40.53  ? 93  PHE   E CZ    1 
ATOM   10877 N  N     . ILE   D 3  92  ? 36.899  31.463  3.095   1.00 40.01  ? 94  ILE   E N     1 
ATOM   10878 C  CA    . ILE   D 3  92  ? 37.202  31.547  1.673   1.00 44.41  ? 94  ILE   E CA    1 
ATOM   10879 C  C     . ILE   D 3  92  ? 38.360  30.617  1.319   1.00 50.50  ? 94  ILE   E C     1 
ATOM   10880 O  O     . ILE   D 3  92  ? 38.314  29.896  0.311   1.00 46.25  ? 94  ILE   E O     1 
ATOM   10881 C  CB    . ILE   D 3  92  ? 37.501  33.002  1.279   1.00 42.45  ? 94  ILE   E CB    1 
ATOM   10882 C  CG1   . ILE   D 3  92  ? 36.258  33.870  1.491   1.00 45.53  ? 94  ILE   E CG1   1 
ATOM   10883 C  CG2   . ILE   D 3  92  ? 37.993  33.077  -0.150  1.00 38.75  ? 94  ILE   E CG2   1 
ATOM   10884 C  CD1   . ILE   D 3  92  ? 36.573  35.345  1.613   1.00 50.60  ? 94  ILE   E CD1   1 
ATOM   10885 N  N     . LYS   D 3  93  ? 39.405  30.603  2.150   1.00 40.31  ? 95  LYS   E N     1 
ATOM   10886 C  CA    . LYS   D 3  93  ? 40.608  29.848  1.823   1.00 41.79  ? 95  LYS   E CA    1 
ATOM   10887 C  C     . LYS   D 3  93  ? 40.336  28.343  1.790   1.00 50.17  ? 95  LYS   E C     1 
ATOM   10888 O  O     . LYS   D 3  93  ? 40.712  27.661  0.831   1.00 52.23  ? 95  LYS   E O     1 
ATOM   10889 C  CB    . LYS   D 3  93  ? 41.722  30.185  2.815   1.00 38.27  ? 95  LYS   E CB    1 
ATOM   10890 C  CG    . LYS   D 3  93  ? 43.046  29.481  2.550   1.00 39.93  ? 95  LYS   E CG    1 
ATOM   10891 C  CD    . LYS   D 3  93  ? 43.916  29.456  3.813   1.00 52.40  ? 95  LYS   E CD    1 
ATOM   10892 C  CE    . LYS   D 3  93  ? 45.214  28.649  3.631   1.00 64.72  ? 95  LYS   E CE    1 
ATOM   10893 N  NZ    . LYS   D 3  93  ? 46.378  29.431  3.085   1.00 49.85  ? 95  LYS   E NZ    1 
ATOM   10894 N  N     . MET   D 3  94  ? 39.692  27.797  2.829   1.00 47.96  ? 96  MET   E N     1 
ATOM   10895 C  CA    . MET   D 3  94  ? 39.405  26.362  2.824   1.00 47.98  ? 96  MET   E CA    1 
ATOM   10896 C  C     . MET   D 3  94  ? 38.445  26.003  1.702   1.00 38.92  ? 96  MET   E C     1 
ATOM   10897 O  O     . MET   D 3  94  ? 38.577  24.951  1.072   1.00 47.94  ? 96  MET   E O     1 
ATOM   10898 C  CB    . MET   D 3  94  ? 38.830  25.908  4.170   1.00 55.43  ? 96  MET   E CB    1 
ATOM   10899 C  CG    . MET   D 3  94  ? 39.851  25.728  5.316   1.00 62.56  ? 96  MET   E CG    1 
ATOM   10900 S  SD    . MET   D 3  94  ? 41.399  24.876  4.884   1.00 82.47  ? 96  MET   E SD    1 
ATOM   10901 C  CE    . MET   D 3  94  ? 40.814  23.412  4.017   1.00 60.85  ? 96  MET   E CE    1 
ATOM   10902 N  N     . ALA   D 3  95  ? 37.469  26.862  1.440   1.00 35.67  ? 97  ALA   E N     1 
ATOM   10903 C  CA    . ALA   D 3  95  ? 36.557  26.608  0.339   1.00 35.78  ? 97  ALA   E CA    1 
ATOM   10904 C  C     . ALA   D 3  95  ? 37.314  26.564  -0.979  1.00 48.86  ? 97  ALA   E C     1 
ATOM   10905 O  O     . ALA   D 3  95  ? 37.146  25.631  -1.774  1.00 42.44  ? 97  ALA   E O     1 
ATOM   10906 C  CB    . ALA   D 3  95  ? 35.463  27.674  0.299   1.00 31.46  ? 97  ALA   E CB    1 
ATOM   10907 N  N     . LYS   D 3  96  ? 38.146  27.579  -1.228  1.00 48.67  ? 98  LYS   E N     1 
ATOM   10908 C  CA    . LYS   D 3  96  ? 38.977  27.587  -2.423  1.00 42.05  ? 98  LYS   E CA    1 
ATOM   10909 C  C     . LYS   D 3  96  ? 39.853  26.351  -2.495  1.00 45.56  ? 98  LYS   E C     1 
ATOM   10910 O  O     . LYS   D 3  96  ? 40.127  25.849  -3.591  1.00 47.96  ? 98  LYS   E O     1 
ATOM   10911 C  CB    . LYS   D 3  96  ? 39.843  28.838  -2.448  1.00 44.23  ? 98  LYS   E CB    1 
ATOM   10912 C  CG    . LYS   D 3  96  ? 40.204  29.308  -3.841  1.00 45.64  ? 98  LYS   E CG    1 
ATOM   10913 C  CD    . LYS   D 3  96  ? 40.914  30.640  -3.782  1.00 47.44  ? 98  LYS   E CD    1 
ATOM   10914 C  CE    . LYS   D 3  96  ? 41.027  31.306  -5.133  1.00 52.33  ? 98  LYS   E CE    1 
ATOM   10915 N  NZ    . LYS   D 3  96  ? 41.484  32.711  -4.906  1.00 59.29  ? 98  LYS   E NZ    1 
ATOM   10916 N  N     . GLU   D 3  97  ? 40.295  25.844  -1.344  1.00 44.82  ? 99  GLU   E N     1 
ATOM   10917 C  CA    . GLU   D 3  97  ? 41.170  24.674  -1.330  1.00 43.83  ? 99  GLU   E CA    1 
ATOM   10918 C  C     . GLU   D 3  97  ? 40.385  23.418  -1.652  1.00 45.92  ? 99  GLU   E C     1 
ATOM   10919 O  O     . GLU   D 3  97  ? 40.669  22.732  -2.637  1.00 55.63  ? 99  GLU   E O     1 
ATOM   10920 C  CB    . GLU   D 3  97  ? 41.863  24.535  0.031   1.00 42.86  ? 99  GLU   E CB    1 
ATOM   10921 C  CG    . GLU   D 3  97  ? 43.310  24.995  0.046   1.00 51.04  ? 99  GLU   E CG    1 
ATOM   10922 C  CD    . GLU   D 3  97  ? 43.812  25.332  1.450   1.00 69.24  ? 99  GLU   E CD    1 
ATOM   10923 O  OE1   . GLU   D 3  97  ? 43.525  24.548  2.396   1.00 56.64  ? 99  GLU   E OE1   1 
ATOM   10924 O  OE2   . GLU   D 3  97  ? 44.486  26.390  1.598   1.00 51.07  ? 99  GLU   E OE2   1 
ATOM   10925 N  N     . LYS   D 3  98  ? 39.385  23.103  -0.821  1.00 53.95  ? 100 LYS   E N     1 
ATOM   10926 C  CA    . LYS   D 3  98  ? 38.505  21.970  -1.086  1.00 54.34  ? 100 LYS   E CA    1 
ATOM   10927 C  C     . LYS   D 3  98  ? 38.036  21.956  -2.542  1.00 45.71  ? 100 LYS   E C     1 
ATOM   10928 O  O     . LYS   D 3  98  ? 37.846  20.891  -3.128  1.00 41.74  ? 100 LYS   E O     1 
ATOM   10929 C  CB    . LYS   D 3  98  ? 37.314  22.012  -0.113  1.00 41.08  ? 100 LYS   E CB    1 
ATOM   10930 C  CG    . LYS   D 3  98  ? 36.425  20.763  -0.134  1.00 58.03  ? 100 LYS   E CG    1 
ATOM   10931 C  CD    . LYS   D 3  98  ? 35.185  20.906  0.752   1.00 67.60  ? 100 LYS   E CD    1 
ATOM   10932 C  CE    . LYS   D 3  98  ? 34.213  19.733  0.572   1.00 73.20  ? 100 LYS   E CE    1 
ATOM   10933 N  NZ    . LYS   D 3  98  ? 33.134  19.708  1.617   1.00 75.96  ? 100 LYS   E NZ    1 
ATOM   10934 N  N     . LEU   D 3  99  ? 37.888  23.124  -3.153  1.00 44.06  ? 101 LEU   E N     1 
ATOM   10935 C  CA    . LEU   D 3  99  ? 37.354  23.174  -4.504  1.00 43.10  ? 101 LEU   E CA    1 
ATOM   10936 C  C     . LEU   D 3  99  ? 38.366  22.659  -5.512  1.00 50.84  ? 101 LEU   E C     1 
ATOM   10937 O  O     . LEU   D 3  99  ? 37.998  22.018  -6.503  1.00 58.41  ? 101 LEU   E O     1 
ATOM   10938 C  CB    . LEU   D 3  99  ? 36.938  24.603  -4.843  1.00 41.14  ? 101 LEU   E CB    1 
ATOM   10939 C  CG    . LEU   D 3  99  ? 35.933  24.726  -5.980  1.00 35.46  ? 101 LEU   E CG    1 
ATOM   10940 C  CD1   . LEU   D 3  99  ? 35.032  23.495  -5.994  1.00 35.33  ? 101 LEU   E CD1   1 
ATOM   10941 C  CD2   . LEU   D 3  99  ? 35.144  26.046  -5.846  1.00 43.04  ? 101 LEU   E CD2   1 
ATOM   10942 N  N     . ALA   D 3  100 ? 39.642  22.926  -5.275  1.00 49.92  ? 102 ALA   E N     1 
ATOM   10943 C  CA    . ALA   D 3  100 ? 40.680  22.566  -6.223  1.00 43.36  ? 102 ALA   E CA    1 
ATOM   10944 C  C     . ALA   D 3  100 ? 41.204  21.153  -5.985  1.00 42.45  ? 102 ALA   E C     1 
ATOM   10945 O  O     . ALA   D 3  100 ? 41.494  20.435  -6.943  1.00 45.15  ? 102 ALA   E O     1 
ATOM   10946 C  CB    . ALA   D 3  100 ? 41.808  23.599  -6.165  1.00 34.57  ? 102 ALA   E CB    1 
ATOM   10947 N  N     . GLN   D 3  101 ? 41.316  20.705  -4.736  1.00 51.36  ? 103 GLN   E N     1 
ATOM   10948 C  CA    . GLN   D 3  101 ? 41.558  19.280  -4.539  1.00 60.91  ? 103 GLN   E CA    1 
ATOM   10949 C  C     . GLN   D 3  101 ? 40.417  18.466  -5.143  1.00 57.09  ? 103 GLN   E C     1 
ATOM   10950 O  O     . GLN   D 3  101 ? 40.647  17.436  -5.788  1.00 49.31  ? 103 GLN   E O     1 
ATOM   10951 C  CB    . GLN   D 3  101 ? 41.754  18.956  -3.052  1.00 44.50  ? 103 GLN   E CB    1 
ATOM   10952 C  CG    . GLN   D 3  101 ? 40.486  18.913  -2.197  1.00 71.98  ? 103 GLN   E CG    1 
ATOM   10953 C  CD    . GLN   D 3  101 ? 39.785  17.549  -2.214  1.00 87.88  ? 103 GLN   E CD    1 
ATOM   10954 O  OE1   . GLN   D 3  101 ? 40.284  16.583  -2.803  1.00 81.31  ? 103 GLN   E OE1   1 
ATOM   10955 N  NE2   . GLN   D 3  101 ? 38.616  17.473  -1.568  1.00 85.44  ? 103 GLN   E NE2   1 
ATOM   10956 N  N     . LYS   D 3  102 ? 39.181  18.948  -4.979  1.00 57.76  ? 104 LYS   E N     1 
ATOM   10957 C  CA    . LYS   D 3  102 ? 38.020  18.259  -5.528  1.00 60.21  ? 104 LYS   E CA    1 
ATOM   10958 C  C     . LYS   D 3  102 ? 38.106  18.138  -7.048  1.00 51.70  ? 104 LYS   E C     1 
ATOM   10959 O  O     . LYS   D 3  102 ? 37.750  17.099  -7.606  1.00 49.78  ? 104 LYS   E O     1 
ATOM   10960 C  CB    . LYS   D 3  102 ? 36.737  18.993  -5.115  1.00 67.68  ? 104 LYS   E CB    1 
ATOM   10961 C  CG    . LYS   D 3  102 ? 35.757  18.162  -4.277  1.00 56.88  ? 104 LYS   E CG    1 
ATOM   10962 C  CD    . LYS   D 3  102 ? 34.712  19.037  -3.566  1.00 51.55  ? 104 LYS   E CD    1 
ATOM   10963 C  CE    . LYS   D 3  102 ? 33.531  19.437  -4.457  1.00 54.13  ? 104 LYS   E CE    1 
ATOM   10964 N  NZ    . LYS   D 3  102 ? 32.207  19.355  -3.725  1.00 41.17  ? 104 LYS   E NZ    1 
ATOM   10965 N  N     . MET   D 3  103 ? 38.586  19.182  -7.733  1.00 51.14  ? 105 MET   E N     1 
ATOM   10966 C  CA    . MET   D 3  103 ? 38.610  19.204  -9.195  1.00 50.90  ? 105 MET   E CA    1 
ATOM   10967 C  C     . MET   D 3  103 ? 39.814  18.491  -9.805  1.00 60.95  ? 105 MET   E C     1 
ATOM   10968 O  O     . MET   D 3  103 ? 39.731  18.066  -10.967 1.00 58.34  ? 105 MET   E O     1 
ATOM   10969 C  CB    . MET   D 3  103 ? 38.575  20.644  -9.717  1.00 47.49  ? 105 MET   E CB    1 
ATOM   10970 C  CG    . MET   D 3  103 ? 37.217  21.323  -9.542  1.00 70.40  ? 105 MET   E CG    1 
ATOM   10971 S  SD    . MET   D 3  103 ? 35.854  20.415  -10.323 1.00 77.37  ? 105 MET   E SD    1 
ATOM   10972 C  CE    . MET   D 3  103 ? 34.452  21.241  -9.596  1.00 66.85  ? 105 MET   E CE    1 
ATOM   10973 N  N     . GLU   D 3  104 ? 40.927  18.359  -9.076  1.00 49.37  ? 106 GLU   E N     1 
ATOM   10974 C  CA    . GLU   D 3  104 ? 42.043  17.610  -9.637  1.00 48.58  ? 106 GLU   E CA    1 
ATOM   10975 C  C     . GLU   D 3  104 ? 41.899  16.112  -9.372  1.00 52.99  ? 106 GLU   E C     1 
ATOM   10976 O  O     . GLU   D 3  104 ? 42.078  15.304  -10.287 1.00 60.27  ? 106 GLU   E O     1 
ATOM   10977 C  CB    . GLU   D 3  104 ? 43.382  18.146  -9.115  1.00 48.86  ? 106 GLU   E CB    1 
ATOM   10978 C  CG    . GLU   D 3  104 ? 43.996  19.297  -9.985  1.00 68.39  ? 106 GLU   E CG    1 
ATOM   10979 C  CD    . GLU   D 3  104 ? 44.466  18.875  -11.417 1.00 79.30  ? 106 GLU   E CD    1 
ATOM   10980 O  OE1   . GLU   D 3  104 ? 44.735  17.676  -11.656 1.00 73.16  ? 106 GLU   E OE1   1 
ATOM   10981 O  OE2   . GLU   D 3  104 ? 44.574  19.756  -12.313 1.00 79.93  ? 106 GLU   E OE2   1 
ATOM   10982 N  N     . SER   D 3  105 ? 41.559  15.723  -8.144  1.00 45.31  ? 107 SER   E N     1 
ATOM   10983 C  CA    . SER   D 3  105 ? 41.169  14.339  -7.890  1.00 48.14  ? 107 SER   E CA    1 
ATOM   10984 C  C     . SER   D 3  105 ? 40.151  13.847  -8.924  1.00 53.73  ? 107 SER   E C     1 
ATOM   10985 O  O     . SER   D 3  105 ? 40.309  12.770  -9.517  1.00 49.49  ? 107 SER   E O     1 
ATOM   10986 C  CB    . SER   D 3  105 ? 40.606  14.220  -6.470  1.00 54.35  ? 107 SER   E CB    1 
ATOM   10987 O  OG    . SER   D 3  105 ? 39.288  13.687  -6.465  1.00 56.15  ? 107 SER   E OG    1 
ATOM   10988 N  N     . ASN   D 3  106 ? 39.095  14.632  -9.150  1.00 50.20  ? 108 ASN   E N     1 
ATOM   10989 C  CA    . ASN   D 3  106 ? 38.084  14.275  -10.141 1.00 46.52  ? 108 ASN   E CA    1 
ATOM   10990 C  C     . ASN   D 3  106 ? 38.708  14.035  -11.511 1.00 55.94  ? 108 ASN   E C     1 
ATOM   10991 O  O     . ASN   D 3  106 ? 38.270  13.144  -12.248 1.00 58.81  ? 108 ASN   E O     1 
ATOM   10992 C  CB    . ASN   D 3  106 ? 37.021  15.377  -10.214 1.00 43.49  ? 108 ASN   E CB    1 
ATOM   10993 C  CG    . ASN   D 3  106 ? 35.982  15.129  -11.294 1.00 53.01  ? 108 ASN   E CG    1 
ATOM   10994 O  OD1   . ASN   D 3  106 ? 36.106  15.609  -12.437 1.00 60.39  ? 108 ASN   E OD1   1 
ATOM   10995 N  ND2   . ASN   D 3  106 ? 34.933  14.400  -10.933 1.00 48.31  ? 108 ASN   E ND2   1 
ATOM   10996 N  N     . LYS   D 3  107 ? 39.737  14.817  -11.867 1.00 56.29  ? 109 LYS   E N     1 
ATOM   10997 C  CA    . LYS   D 3  107 ? 40.306  14.786  -13.214 1.00 50.43  ? 109 LYS   E CA    1 
ATOM   10998 C  C     . LYS   D 3  107 ? 41.212  13.578  -13.422 1.00 54.54  ? 109 LYS   E C     1 
ATOM   10999 O  O     . LYS   D 3  107 ? 41.154  12.927  -14.472 1.00 59.65  ? 109 LYS   E O     1 
ATOM   11000 C  CB    . LYS   D 3  107 ? 41.072  16.085  -13.485 1.00 60.16  ? 109 LYS   E CB    1 
ATOM   11001 C  CG    . LYS   D 3  107 ? 41.742  16.182  -14.854 1.00 59.52  ? 109 LYS   E CG    1 
ATOM   11002 C  CD    . LYS   D 3  107 ? 42.179  17.621  -15.155 1.00 55.69  ? 109 LYS   E CD    1 
ATOM   11003 C  CE    . LYS   D 3  107 ? 43.177  17.684  -16.293 1.00 49.96  ? 109 LYS   E CE    1 
ATOM   11004 N  NZ    . LYS   D 3  107 ? 44.494  17.115  -15.900 1.00 55.15  ? 109 LYS   E NZ    1 
ATOM   11005 N  N     . GLU   D 3  108 ? 42.059  13.266  -12.448 1.00 51.07  ? 110 GLU   E N     1 
ATOM   11006 C  CA    . GLU   D 3  108 ? 42.870  12.064  -12.545 1.00 47.99  ? 110 GLU   E CA    1 
ATOM   11007 C  C     . GLU   D 3  108 ? 42.070  10.805  -12.276 1.00 55.61  ? 110 GLU   E C     1 
ATOM   11008 O  O     . GLU   D 3  108 ? 42.609  9.704   -12.420 1.00 63.30  ? 110 GLU   E O     1 
ATOM   11009 C  CB    . GLU   D 3  108 ? 44.044  12.128  -11.576 1.00 42.48  ? 110 GLU   E CB    1 
ATOM   11010 C  CG    . GLU   D 3  108 ? 43.780  12.949  -10.348 1.00 55.80  ? 110 GLU   E CG    1 
ATOM   11011 C  CD    . GLU   D 3  108 ? 44.501  12.404  -9.146  1.00 66.93  ? 110 GLU   E CD    1 
ATOM   11012 O  OE1   . GLU   D 3  108 ? 43.964  11.458  -8.523  1.00 59.55  ? 110 GLU   E OE1   1 
ATOM   11013 O  OE2   . GLU   D 3  108 ? 45.609  12.905  -8.845  1.00 68.38  ? 110 GLU   E OE2   1 
ATOM   11014 N  N     . ASN   D 3  109 ? 40.817  10.942  -11.859 1.00 54.38  ? 111 ASN   E N     1 
ATOM   11015 C  CA    . ASN   D 3  109 ? 39.947  9.792   -11.705 1.00 44.07  ? 111 ASN   E CA    1 
ATOM   11016 C  C     . ASN   D 3  109 ? 39.287  9.446   -13.033 1.00 49.78  ? 111 ASN   E C     1 
ATOM   11017 O  O     . ASN   D 3  109 ? 39.416  8.316   -13.518 1.00 40.04  ? 111 ASN   E O     1 
ATOM   11018 C  CB    . ASN   D 3  109 ? 38.913  10.072  -10.609 1.00 33.80  ? 111 ASN   E CB    1 
ATOM   11019 C  CG    . ASN   D 3  109 ? 39.431  9.738   -9.211  1.00 41.74  ? 111 ASN   E CG    1 
ATOM   11020 O  OD1   . ASN   D 3  109 ? 40.549  9.263   -9.065  1.00 52.27  ? 111 ASN   E OD1   1 
ATOM   11021 N  ND2   . ASN   D 3  109 ? 38.611  9.977   -8.179  1.00 35.90  ? 111 ASN   E ND2   1 
ATOM   11022 N  N     . ARG   D 3  110 ? 38.617  10.430  -13.647 1.00 50.67  ? 112 ARG   E N     1 
ATOM   11023 C  CA    . ARG   D 3  110 ? 37.931  10.236  -14.917 1.00 45.35  ? 112 ARG   E CA    1 
ATOM   11024 C  C     . ARG   D 3  110 ? 38.889  9.970   -16.070 1.00 52.96  ? 112 ARG   E C     1 
ATOM   11025 O  O     . ARG   D 3  110 ? 38.477  9.383   -17.080 1.00 57.41  ? 112 ARG   E O     1 
ATOM   11026 C  CB    . ARG   D 3  110 ? 37.071  11.459  -15.254 1.00 51.49  ? 112 ARG   E CB    1 
ATOM   11027 C  CG    . ARG   D 3  110 ? 36.263  11.294  -16.555 1.00 49.56  ? 112 ARG   E CG    1 
ATOM   11028 C  CD    . ARG   D 3  110 ? 35.684  12.605  -17.076 1.00 43.13  ? 112 ARG   E CD    1 
ATOM   11029 N  NE    . ARG   D 3  110 ? 34.653  12.334  -18.072 1.00 58.79  ? 112 ARG   E NE    1 
ATOM   11030 C  CZ    . ARG   D 3  110 ? 34.786  12.503  -19.383 1.00 62.81  ? 112 ARG   E CZ    1 
ATOM   11031 N  NH1   . ARG   D 3  110 ? 35.888  13.017  -19.911 1.00 44.48  ? 112 ARG   E NH1   1 
ATOM   11032 N  NH2   . ARG   D 3  110 ? 33.780  12.160  -20.184 1.00 55.69  ? 112 ARG   E NH2   1 
ATOM   11033 N  N     . GLU   D 3  111 ? 40.143  10.403  -15.968 1.00 46.97  ? 113 GLU   E N     1 
ATOM   11034 C  CA    . GLU   D 3  111 ? 41.089  10.053  -17.018 1.00 52.46  ? 113 GLU   E CA    1 
ATOM   11035 C  C     . GLU   D 3  111 ? 41.657  8.653   -16.811 1.00 56.48  ? 113 GLU   E C     1 
ATOM   11036 O  O     . GLU   D 3  111 ? 41.764  7.881   -17.769 1.00 57.50  ? 113 GLU   E O     1 
ATOM   11037 C  CB    . GLU   D 3  111 ? 42.193  11.099  -17.093 1.00 54.71  ? 113 GLU   E CB    1 
ATOM   11038 C  CG    . GLU   D 3  111 ? 41.837  12.236  -18.026 1.00 57.25  ? 113 GLU   E CG    1 
ATOM   11039 C  CD    . GLU   D 3  111 ? 42.615  13.499  -17.731 1.00 75.67  ? 113 GLU   E CD    1 
ATOM   11040 O  OE1   . GLU   D 3  111 ? 43.699  13.404  -17.110 1.00 70.85  ? 113 GLU   E OE1   1 
ATOM   11041 O  OE2   . GLU   D 3  111 ? 42.133  14.591  -18.110 1.00 77.21  ? 113 GLU   E OE2   1 
ATOM   11042 N  N     . ALA   D 3  112 ? 41.994  8.295   -15.570 1.00 58.58  ? 114 ALA   E N     1 
ATOM   11043 C  CA    . ALA   D 3  112 ? 42.391  6.918   -15.282 1.00 60.67  ? 114 ALA   E CA    1 
ATOM   11044 C  C     . ALA   D 3  112 ? 41.291  5.928   -15.667 1.00 61.48  ? 114 ALA   E C     1 
ATOM   11045 O  O     . ALA   D 3  112 ? 41.583  4.838   -16.181 1.00 60.23  ? 114 ALA   E O     1 
ATOM   11046 C  CB    . ALA   D 3  112 ? 42.770  6.768   -13.803 1.00 28.85  ? 114 ALA   E CB    1 
ATOM   11047 N  N     . HIS   D 3  113 ? 40.019  6.280   -15.423 1.00 56.73  ? 115 HIS   E N     1 
ATOM   11048 C  CA    . HIS   D 3  113 ? 38.927  5.409   -15.859 1.00 65.77  ? 115 HIS   E CA    1 
ATOM   11049 C  C     . HIS   D 3  113 ? 38.881  5.326   -17.376 1.00 63.66  ? 115 HIS   E C     1 
ATOM   11050 O  O     . HIS   D 3  113 ? 38.707  4.241   -17.945 1.00 48.68  ? 115 HIS   E O     1 
ATOM   11051 C  CB    . HIS   D 3  113 ? 37.577  5.899   -15.313 1.00 65.47  ? 115 HIS   E CB    1 
ATOM   11052 C  CG    . HIS   D 3  113 ? 36.381  5.290   -16.000 1.00 79.83  ? 115 HIS   E CG    1 
ATOM   11053 N  ND1   . HIS   D 3  113 ? 35.816  5.830   -17.140 1.00 72.04  ? 115 HIS   E ND1   1 
ATOM   11054 C  CD2   . HIS   D 3  113 ? 35.637  4.194   -15.701 1.00 76.38  ? 115 HIS   E CD2   1 
ATOM   11055 C  CE1   . HIS   D 3  113 ? 34.784  5.090   -17.517 1.00 60.89  ? 115 HIS   E CE1   1 
ATOM   11056 N  NE2   . HIS   D 3  113 ? 34.655  4.090   -16.662 1.00 62.07  ? 115 HIS   E NE2   1 
ATOM   11057 N  N     . LEU   D 3  114 ? 39.052  6.468   -18.042 1.00 65.57  ? 116 LEU   E N     1 
ATOM   11058 C  CA    . LEU   D 3  114 ? 39.041  6.498   -19.498 1.00 60.23  ? 116 LEU   E CA    1 
ATOM   11059 C  C     . LEU   D 3  114 ? 40.267  5.791   -20.084 1.00 63.01  ? 116 LEU   E C     1 
ATOM   11060 O  O     . LEU   D 3  114 ? 40.141  5.038   -21.060 1.00 65.18  ? 116 LEU   E O     1 
ATOM   11061 C  CB    . LEU   D 3  114 ? 38.959  7.949   -19.970 1.00 54.87  ? 116 LEU   E CB    1 
ATOM   11062 C  CG    . LEU   D 3  114 ? 38.158  8.266   -21.228 1.00 68.59  ? 116 LEU   E CG    1 
ATOM   11063 C  CD1   . LEU   D 3  114 ? 36.956  9.135   -20.878 1.00 61.31  ? 116 LEU   E CD1   1 
ATOM   11064 C  CD2   . LEU   D 3  114 ? 39.044  8.947   -22.280 1.00 66.39  ? 116 LEU   E CD2   1 
ATOM   11065 N  N     . ALA   D 3  115 ? 41.461  6.013   -19.506 1.00 57.21  ? 117 ALA   E N     1 
ATOM   11066 C  CA    . ALA   D 3  115 ? 42.672  5.379   -20.036 1.00 52.03  ? 117 ALA   E CA    1 
ATOM   11067 C  C     . ALA   D 3  115 ? 42.548  3.865   -20.036 1.00 51.19  ? 117 ALA   E C     1 
ATOM   11068 O  O     . ALA   D 3  115 ? 42.931  3.200   -21.008 1.00 63.44  ? 117 ALA   E O     1 
ATOM   11069 C  CB    . ALA   D 3  115 ? 43.911  5.796   -19.237 1.00 35.78  ? 117 ALA   E CB    1 
ATOM   11070 N  N     . ALA   D 3  116 ? 42.025  3.303   -18.949 1.00 45.79  ? 118 ALA   E N     1 
ATOM   11071 C  CA    . ALA   D 3  116 ? 41.831  1.862   -18.883 1.00 49.86  ? 118 ALA   E CA    1 
ATOM   11072 C  C     . ALA   D 3  116 ? 40.948  1.380   -20.030 1.00 53.01  ? 118 ALA   E C     1 
ATOM   11073 O  O     . ALA   D 3  116 ? 41.276  0.406   -20.717 1.00 54.30  ? 118 ALA   E O     1 
ATOM   11074 C  CB    . ALA   D 3  116 ? 41.232  1.488   -17.525 1.00 46.16  ? 118 ALA   E CB    1 
ATOM   11075 N  N     . MET   D 3  117 ? 39.834  2.077   -20.270 1.00 42.10  ? 119 MET   E N     1 
ATOM   11076 C  CA    . MET   D 3  117 ? 38.903  1.679   -21.317 1.00 48.02  ? 119 MET   E CA    1 
ATOM   11077 C  C     . MET   D 3  117 ? 39.547  1.723   -22.696 1.00 68.71  ? 119 MET   E C     1 
ATOM   11078 O  O     . MET   D 3  117 ? 39.125  0.992   -23.604 1.00 66.21  ? 119 MET   E O     1 
ATOM   11079 C  CB    . MET   D 3  117 ? 37.669  2.573   -21.287 1.00 48.41  ? 119 MET   E CB    1 
ATOM   11080 C  CG    . MET   D 3  117 ? 36.661  2.285   -22.364 1.00 45.69  ? 119 MET   E CG    1 
ATOM   11081 S  SD    . MET   D 3  117 ? 35.808  3.793   -22.850 1.00 53.87  ? 119 MET   E SD    1 
ATOM   11082 C  CE    . MET   D 3  117 ? 35.436  4.451   -21.221 1.00 59.32  ? 119 MET   E CE    1 
ATOM   11083 N  N     . LEU   D 3  118 ? 40.553  2.575   -22.889 1.00 61.35  ? 120 LEU   E N     1 
ATOM   11084 C  CA    . LEU   D 3  118 ? 41.301  2.493   -24.131 1.00 63.63  ? 120 LEU   E CA    1 
ATOM   11085 C  C     . LEU   D 3  118 ? 42.441  1.492   -24.045 1.00 61.85  ? 120 LEU   E C     1 
ATOM   11086 O  O     . LEU   D 3  118 ? 42.902  1.011   -25.084 1.00 57.57  ? 120 LEU   E O     1 
ATOM   11087 C  CB    . LEU   D 3  118 ? 41.828  3.872   -24.548 1.00 54.50  ? 120 LEU   E CB    1 
ATOM   11088 C  CG    . LEU   D 3  118 ? 40.794  4.823   -25.170 1.00 56.66  ? 120 LEU   E CG    1 
ATOM   11089 C  CD1   . LEU   D 3  118 ? 39.793  5.294   -24.123 1.00 63.92  ? 120 LEU   E CD1   1 
ATOM   11090 C  CD2   . LEU   D 3  118 ? 41.457  6.021   -25.833 1.00 62.37  ? 120 LEU   E CD2   1 
ATOM   11091 N  N     . GLU   D 3  119 ? 42.886  1.136   -22.843 1.00 57.17  ? 121 GLU   E N     1 
ATOM   11092 C  CA    . GLU   D 3  119 ? 43.945  0.136   -22.756 1.00 69.69  ? 121 GLU   E CA    1 
ATOM   11093 C  C     . GLU   D 3  119 ? 43.427  -1.277  -23.022 1.00 69.42  ? 121 GLU   E C     1 
ATOM   11094 O  O     . GLU   D 3  119 ? 44.177  -2.122  -23.524 1.00 70.47  ? 121 GLU   E O     1 
ATOM   11095 C  CB    . GLU   D 3  119 ? 44.632  0.198   -21.391 1.00 62.52  ? 121 GLU   E CB    1 
ATOM   11096 C  CG    . GLU   D 3  119 ? 45.547  -0.988  -21.119 1.00 67.00  ? 121 GLU   E CG    1 
ATOM   11097 C  CD    . GLU   D 3  119 ? 46.890  -0.574  -20.550 1.00 83.23  ? 121 GLU   E CD    1 
ATOM   11098 O  OE1   . GLU   D 3  119 ? 47.145  0.650   -20.465 1.00 89.53  ? 121 GLU   E OE1   1 
ATOM   11099 O  OE2   . GLU   D 3  119 ? 47.688  -1.472  -20.194 1.00 80.30  ? 121 GLU   E OE2   1 
ATOM   11100 N  N     . ARG   D 3  120 ? 42.170  -1.562  -22.684 1.00 60.14  ? 122 ARG   E N     1 
ATOM   11101 C  CA    . ARG   D 3  120 ? 41.606  -2.860  -23.027 1.00 61.09  ? 122 ARG   E CA    1 
ATOM   11102 C  C     . ARG   D 3  120 ? 41.323  -2.941  -24.523 1.00 74.11  ? 122 ARG   E C     1 
ATOM   11103 O  O     . ARG   D 3  120 ? 41.705  -3.913  -25.186 1.00 76.55  ? 122 ARG   E O     1 
ATOM   11104 C  CB    . ARG   D 3  120 ? 40.332  -3.118  -22.222 1.00 71.49  ? 122 ARG   E CB    1 
ATOM   11105 C  CG    . ARG   D 3  120 ? 40.492  -3.146  -20.712 1.00 68.80  ? 122 ARG   E CG    1 
ATOM   11106 C  CD    . ARG   D 3  120 ? 39.205  -3.658  -20.079 1.00 82.51  ? 122 ARG   E CD    1 
ATOM   11107 N  NE    . ARG   D 3  120 ? 39.000  -3.188  -18.713 1.00 104.56 ? 122 ARG   E NE    1 
ATOM   11108 C  CZ    . ARG   D 3  120 ? 38.051  -3.644  -17.902 1.00 102.90 ? 122 ARG   E CZ    1 
ATOM   11109 N  NH1   . ARG   D 3  120 ? 37.213  -4.597  -18.283 1.00 89.63  ? 122 ARG   E NH1   1 
ATOM   11110 N  NH2   . ARG   D 3  120 ? 37.942  -3.134  -16.677 1.00 91.40  ? 122 ARG   E NH2   1 
ATOM   11111 N  N     . LEU   D 3  121 ? 40.644  -1.923  -25.072 1.00 71.62  ? 123 LEU   E N     1 
ATOM   11112 C  CA    . LEU   D 3  121 ? 40.466  -1.834  -26.519 1.00 70.99  ? 123 LEU   E CA    1 
ATOM   11113 C  C     . LEU   D 3  121 ? 41.793  -2.006  -27.247 1.00 70.26  ? 123 LEU   E C     1 
ATOM   11114 O  O     . LEU   D 3  121 ? 41.874  -2.726  -28.248 1.00 79.53  ? 123 LEU   E O     1 
ATOM   11115 C  CB    . LEU   D 3  121 ? 39.821  -0.497  -26.898 1.00 61.47  ? 123 LEU   E CB    1 
ATOM   11116 C  CG    . LEU   D 3  121 ? 38.372  -0.321  -26.454 1.00 49.06  ? 123 LEU   E CG    1 
ATOM   11117 C  CD1   . LEU   D 3  121 ? 37.589  0.498   -27.454 1.00 51.14  ? 123 LEU   E CD1   1 
ATOM   11118 C  CD2   . LEU   D 3  121 ? 37.726  -1.665  -26.265 1.00 56.62  ? 123 LEU   E CD2   1 
ATOM   11119 N  N     . GLN   D 3  122 ? 42.849  -1.359  -26.754 1.00 66.71  ? 124 GLN   E N     1 
ATOM   11120 C  CA    . GLN   D 3  122 ? 44.162  -1.529  -27.356 1.00 68.15  ? 124 GLN   E CA    1 
ATOM   11121 C  C     . GLN   D 3  122 ? 44.700  -2.942  -27.195 1.00 78.84  ? 124 GLN   E C     1 
ATOM   11122 O  O     . GLN   D 3  122 ? 45.778  -3.235  -27.726 1.00 86.37  ? 124 GLN   E O     1 
ATOM   11123 C  CB    . GLN   D 3  122 ? 45.141  -0.515  -26.769 1.00 66.55  ? 124 GLN   E CB    1 
ATOM   11124 C  CG    . GLN   D 3  122 ? 44.966  0.883   -27.358 1.00 69.91  ? 124 GLN   E CG    1 
ATOM   11125 C  CD    . GLN   D 3  122 ? 45.470  2.010   -26.443 1.00 73.22  ? 124 GLN   E CD    1 
ATOM   11126 O  OE1   . GLN   D 3  122 ? 46.087  1.774   -25.391 1.00 59.82  ? 124 GLN   E OE1   1 
ATOM   11127 N  NE2   . GLN   D 3  122 ? 45.200  3.246   -26.850 1.00 60.37  ? 124 GLN   E NE2   1 
ATOM   11128 N  N     . GLU   D 3  123 ? 43.988  -3.820  -26.486 1.00 79.86  ? 125 GLU   E N     1 
ATOM   11129 C  CA    . GLU   D 3  123 ? 44.338  -5.232  -26.453 1.00 75.29  ? 125 GLU   E CA    1 
ATOM   11130 C  C     . GLU   D 3  123 ? 43.443  -6.082  -27.339 1.00 70.42  ? 125 GLU   E C     1 
ATOM   11131 O  O     . GLU   D 3  123 ? 43.829  -7.197  -27.693 1.00 71.98  ? 125 GLU   E O     1 
ATOM   11132 C  CB    . GLU   D 3  123 ? 44.307  -5.761  -25.017 1.00 59.03  ? 125 GLU   E CB    1 
ATOM   11133 C  CG    . GLU   D 3  123 ? 45.510  -5.298  -24.221 1.00 74.15  ? 125 GLU   E CG    1 
ATOM   11134 C  CD    . GLU   D 3  123 ? 46.787  -5.286  -25.059 1.00 80.24  ? 125 GLU   E CD    1 
ATOM   11135 O  OE1   . GLU   D 3  123 ? 47.035  -6.269  -25.789 1.00 86.73  ? 125 GLU   E OE1   1 
ATOM   11136 O  OE2   . GLU   D 3  123 ? 47.540  -4.290  -25.001 1.00 76.09  ? 125 GLU   E OE2   1 
ATOM   11137 N  N     . LYS   D 3  124 ? 42.272  -5.586  -27.723 1.00 67.87  ? 126 LYS   E N     1 
ATOM   11138 C  CA    . LYS   D 3  124 ? 41.568  -6.224  -28.825 1.00 79.81  ? 126 LYS   E CA    1 
ATOM   11139 C  C     . LYS   D 3  124 ? 42.424  -6.204  -30.087 1.00 86.77  ? 126 LYS   E C     1 
ATOM   11140 O  O     . LYS   D 3  124 ? 42.456  -7.186  -30.841 1.00 79.77  ? 126 LYS   E O     1 
ATOM   11141 C  CB    . LYS   D 3  124 ? 40.217  -5.541  -29.055 1.00 71.00  ? 126 LYS   E CB    1 
ATOM   11142 C  CG    . LYS   D 3  124 ? 39.213  -5.757  -27.922 1.00 66.38  ? 126 LYS   E CG    1 
ATOM   11143 C  CD    . LYS   D 3  124 ? 39.069  -7.241  -27.557 1.00 76.16  ? 126 LYS   E CD    1 
ATOM   11144 C  CE    . LYS   D 3  124 ? 40.193  -7.722  -26.627 1.00 72.69  ? 126 LYS   E CE    1 
ATOM   11145 N  NZ    . LYS   D 3  124 ? 40.269  -9.207  -26.513 1.00 60.16  ? 126 LYS   E NZ    1 
ATOM   11146 N  N     . ASP   D 3  125 ? 43.158  -5.105  -30.308 1.00 82.85  ? 127 ASP   E N     1 
ATOM   11147 C  CA    . ASP   D 3  125 ? 43.966  -4.976  -31.517 1.00 73.14  ? 127 ASP   E CA    1 
ATOM   11148 C  C     . ASP   D 3  125 ? 45.195  -5.871  -31.462 1.00 74.62  ? 127 ASP   E C     1 
ATOM   11149 O  O     . ASP   D 3  125 ? 45.623  -6.411  -32.489 1.00 79.27  ? 127 ASP   E O     1 
ATOM   11150 C  CB    . ASP   D 3  125 ? 44.367  -3.519  -31.735 1.00 72.31  ? 127 ASP   E CB    1 
ATOM   11151 C  CG    . ASP   D 3  125 ? 43.182  -2.640  -32.089 1.00 77.67  ? 127 ASP   E CG    1 
ATOM   11152 O  OD1   . ASP   D 3  125 ? 42.032  -3.101  -31.943 1.00 73.45  ? 127 ASP   E OD1   1 
ATOM   11153 O  OD2   . ASP   D 3  125 ? 43.399  -1.488  -32.522 1.00 80.69  ? 127 ASP   E OD2   1 
ATOM   11154 N  N     . LYS   D 3  126 ? 45.784  -6.043  -30.281 1.00 75.48  ? 128 LYS   E N     1 
ATOM   11155 C  CA    . LYS   D 3  126 ? 46.892  -6.984  -30.170 1.00 81.91  ? 128 LYS   E CA    1 
ATOM   11156 C  C     . LYS   D 3  126 ? 46.421  -8.399  -30.490 1.00 78.66  ? 128 LYS   E C     1 
ATOM   11157 O  O     . LYS   D 3  126 ? 46.904  -9.031  -31.434 1.00 82.45  ? 128 LYS   E O     1 
ATOM   11158 C  CB    . LYS   D 3  126 ? 47.517  -6.915  -28.777 1.00 72.08  ? 128 LYS   E CB    1 
ATOM   11159 C  CG    . LYS   D 3  126 ? 48.600  -7.953  -28.571 1.00 75.00  ? 128 LYS   E CG    1 
ATOM   11160 C  CD    . LYS   D 3  126 ? 49.456  -7.642  -27.364 1.00 83.56  ? 128 LYS   E CD    1 
ATOM   11161 C  CE    . LYS   D 3  126 ? 50.394  -6.485  -27.630 1.00 74.49  ? 128 LYS   E CE    1 
ATOM   11162 N  NZ    . LYS   D 3  126 ? 51.512  -6.483  -26.652 1.00 70.14  ? 128 LYS   E NZ    1 
ATOM   11163 N  N     . HIS   D 3  127 ? 45.455  -8.899  -29.716 1.00 79.64  ? 129 HIS   E N     1 
ATOM   11164 C  CA    . HIS   D 3  127 ? 44.861  -10.207 -29.976 1.00 73.19  ? 129 HIS   E CA    1 
ATOM   11165 C  C     . HIS   D 3  127 ? 44.484  -10.361 -31.447 1.00 72.26  ? 129 HIS   E C     1 
ATOM   11166 O  O     . HIS   D 3  127 ? 44.844  -11.351 -32.092 1.00 69.23  ? 129 HIS   E O     1 
ATOM   11167 C  CB    . HIS   D 3  127 ? 43.644  -10.392 -29.065 1.00 63.24  ? 129 HIS   E CB    1 
ATOM   11168 C  CG    . HIS   D 3  127 ? 42.908  -11.680 -29.265 1.00 70.57  ? 129 HIS   E CG    1 
ATOM   11169 N  ND1   . HIS   D 3  127 ? 43.380  -12.890 -28.802 1.00 66.23  ? 129 HIS   E ND1   1 
ATOM   11170 C  CD2   . HIS   D 3  127 ? 41.715  -11.941 -29.853 1.00 62.49  ? 129 HIS   E CD2   1 
ATOM   11171 C  CE1   . HIS   D 3  127 ? 42.514  -13.841 -29.104 1.00 67.22  ? 129 HIS   E CE1   1 
ATOM   11172 N  NE2   . HIS   D 3  127 ? 41.496  -13.291 -29.744 1.00 58.47  ? 129 HIS   E NE2   1 
ATOM   11173 N  N     . ALA   D 3  128 ? 43.777  -9.376  -32.003 1.00 76.06  ? 130 ALA   E N     1 
ATOM   11174 C  CA    . ALA   D 3  128 ? 43.325  -9.493  -33.386 1.00 67.09  ? 130 ALA   E CA    1 
ATOM   11175 C  C     . ALA   D 3  128 ? 44.491  -9.746  -34.327 1.00 78.61  ? 130 ALA   E C     1 
ATOM   11176 O  O     . ALA   D 3  128 ? 44.365  -10.515 -35.287 1.00 77.73  ? 130 ALA   E O     1 
ATOM   11177 C  CB    . ALA   D 3  128 ? 42.571  -8.235  -33.808 1.00 72.53  ? 130 ALA   E CB    1 
ATOM   11178 N  N     . GLU   D 3  129 ? 45.634  -9.101  -34.080 1.00 84.67  ? 131 GLU   E N     1 
ATOM   11179 C  CA    . GLU   D 3  129 ? 46.810  -9.377  -34.899 1.00 84.78  ? 131 GLU   E CA    1 
ATOM   11180 C  C     . GLU   D 3  129 ? 47.256  -10.824 -34.731 1.00 78.90  ? 131 GLU   E C     1 
ATOM   11181 O  O     . GLU   D 3  129 ? 47.580  -11.501 -35.716 1.00 77.61  ? 131 GLU   E O     1 
ATOM   11182 C  CB    . GLU   D 3  129 ? 47.948  -8.409  -34.554 1.00 70.12  ? 131 GLU   E CB    1 
ATOM   11183 C  CG    . GLU   D 3  129 ? 47.717  -6.973  -35.018 1.00 76.09  ? 131 GLU   E CG    1 
ATOM   11184 C  CD    . GLU   D 3  129 ? 47.624  -6.843  -36.536 1.00 96.27  ? 131 GLU   E CD    1 
ATOM   11185 O  OE1   . GLU   D 3  129 ? 48.089  -7.764  -37.242 1.00 105.99 ? 131 GLU   E OE1   1 
ATOM   11186 O  OE2   . GLU   D 3  129 ? 47.081  -5.825  -37.029 1.00 85.32  ? 131 GLU   E OE2   1 
ATOM   11187 N  N     . GLU   D 3  130 ? 47.253  -11.325 -33.492 1.00 73.32  ? 132 GLU   E N     1 
ATOM   11188 C  CA    . GLU   D 3  130 ? 47.661  -12.702 -33.248 1.00 71.88  ? 132 GLU   E CA    1 
ATOM   11189 C  C     . GLU   D 3  130 ? 46.687  -13.707 -33.839 1.00 74.00  ? 132 GLU   E C     1 
ATOM   11190 O  O     . GLU   D 3  130 ? 47.086  -14.842 -34.120 1.00 78.29  ? 132 GLU   E O     1 
ATOM   11191 C  CB    . GLU   D 3  130 ? 47.812  -12.955 -31.757 1.00 69.64  ? 132 GLU   E CB    1 
ATOM   11192 C  CG    . GLU   D 3  130 ? 49.038  -12.326 -31.157 1.00 75.21  ? 132 GLU   E CG    1 
ATOM   11193 C  CD    . GLU   D 3  130 ? 49.118  -12.547 -29.661 1.00 89.65  ? 132 GLU   E CD    1 
ATOM   11194 O  OE1   . GLU   D 3  130 ? 49.413  -13.688 -29.241 1.00 92.21  ? 132 GLU   E OE1   1 
ATOM   11195 O  OE2   . GLU   D 3  130 ? 48.869  -11.580 -28.906 1.00 89.83  ? 132 GLU   E OE2   1 
ATOM   11196 N  N     . VAL   D 3  131 ? 45.425  -13.324 -34.032 1.00 71.97  ? 133 VAL   E N     1 
ATOM   11197 C  CA    . VAL   D 3  131 ? 44.487  -14.219 -34.700 1.00 71.43  ? 133 VAL   E CA    1 
ATOM   11198 C  C     . VAL   D 3  131 ? 44.817  -14.312 -36.186 1.00 73.11  ? 133 VAL   E C     1 
ATOM   11199 O  O     . VAL   D 3  131 ? 44.862  -15.409 -36.755 1.00 72.16  ? 133 VAL   E O     1 
ATOM   11200 C  CB    . VAL   D 3  131 ? 43.034  -13.765 -34.445 1.00 66.87  ? 133 VAL   E CB    1 
ATOM   11201 C  CG1   . VAL   D 3  131 ? 42.071  -14.452 -35.394 1.00 61.87  ? 133 VAL   E CG1   1 
ATOM   11202 C  CG2   . VAL   D 3  131 ? 42.635  -14.065 -33.005 1.00 66.33  ? 133 VAL   E CG2   1 
ATOM   11203 N  N     . ARG   D 3  132 ? 45.088  -13.171 -36.831 1.00 66.95  ? 134 ARG   E N     1 
ATOM   11204 C  CA    . ARG   D 3  132 ? 45.419  -13.191 -38.253 1.00 69.91  ? 134 ARG   E CA    1 
ATOM   11205 C  C     . ARG   D 3  132 ? 46.812  -13.766 -38.492 1.00 77.94  ? 134 ARG   E C     1 
ATOM   11206 O  O     . ARG   D 3  132 ? 47.032  -14.497 -39.467 1.00 75.91  ? 134 ARG   E O     1 
ATOM   11207 C  CB    . ARG   D 3  132 ? 45.301  -11.788 -38.843 1.00 68.35  ? 134 ARG   E CB    1 
ATOM   11208 C  CG    . ARG   D 3  132 ? 43.872  -11.267 -38.943 1.00 61.13  ? 134 ARG   E CG    1 
ATOM   11209 C  CD    . ARG   D 3  132 ? 43.820  -9.882  -39.604 1.00 56.96  ? 134 ARG   E CD    1 
ATOM   11210 N  NE    . ARG   D 3  132 ? 44.512  -8.837  -38.852 1.00 79.80  ? 134 ARG   E NE    1 
ATOM   11211 C  CZ    . ARG   D 3  132 ? 43.985  -8.163  -37.834 1.00 86.51  ? 134 ARG   E CZ    1 
ATOM   11212 N  NH1   . ARG   D 3  132 ? 42.763  -8.417  -37.390 1.00 76.93  ? 134 ARG   E NH1   1 
ATOM   11213 N  NH2   . ARG   D 3  132 ? 44.704  -7.212  -37.241 1.00 79.93  ? 134 ARG   E NH2   1 
ATOM   11214 N  N     . LYS   D 3  133 ? 47.761  -13.463 -37.606 1.00 73.73  ? 135 LYS   E N     1 
ATOM   11215 C  CA    . LYS   D 3  133 ? 49.083  -14.079 -37.637 1.00 72.10  ? 135 LYS   E CA    1 
ATOM   11216 C  C     . LYS   D 3  133 ? 49.010  -15.571 -37.301 1.00 78.52  ? 135 LYS   E C     1 
ATOM   11217 O  O     . LYS   D 3  133 ? 49.982  -16.163 -36.816 1.00 69.84  ? 135 LYS   E O     1 
ATOM   11218 C  CB    . LYS   D 3  133 ? 50.013  -13.346 -36.668 1.00 72.87  ? 135 LYS   E CB    1 
ATOM   11219 C  CG    . LYS   D 3  133 ? 51.466  -13.809 -36.690 1.00 90.49  ? 135 LYS   E CG    1 
ATOM   11220 C  CD    . LYS   D 3  133 ? 52.206  -13.343 -35.440 1.00 89.47  ? 135 LYS   E CD    1 
ATOM   11221 C  CE    . LYS   D 3  133 ? 53.471  -14.154 -35.200 1.00 90.78  ? 135 LYS   E CE    1 
ATOM   11222 N  NZ    . LYS   D 3  133 ? 54.119  -13.802 -33.909 1.00 93.60  ? 135 LYS   E NZ    1 
ATOM   11223 N  N     . ASN   D 3  134 ? 47.859  -16.193 -37.553 1.00 80.53  ? 136 ASN   E N     1 
ATOM   11224 C  CA    . ASN   D 3  134 ? 47.684  -17.620 -37.305 1.00 81.75  ? 136 ASN   E CA    1 
ATOM   11225 C  C     . ASN   D 3  134 ? 46.948  -18.279 -38.458 1.00 72.58  ? 136 ASN   E C     1 
ATOM   11226 O  O     . ASN   D 3  134 ? 47.273  -19.406 -38.848 1.00 72.35  ? 136 ASN   E O     1 
ATOM   11227 C  CB    . ASN   D 3  134 ? 46.933  -17.853 -35.998 1.00 75.71  ? 136 ASN   E CB    1 
ATOM   11228 C  CG    . ASN   D 3  134 ? 47.859  -17.990 -34.830 1.00 81.93  ? 136 ASN   E CG    1 
ATOM   11229 O  OD1   . ASN   D 3  134 ? 48.988  -17.489 -34.859 1.00 76.53  ? 136 ASN   E OD1   1 
ATOM   11230 N  ND2   . ASN   D 3  134 ? 47.405  -18.688 -33.794 1.00 92.97  ? 136 ASN   E ND2   1 
ATOM   11231 N  N     . LYS   D 3  135 ? 45.932  -17.589 -38.985 1.00 69.78  ? 137 LYS   E N     1 
ATOM   11232 C  CA    . LYS   D 3  135 ? 45.368  -17.969 -40.268 1.00 75.25  ? 137 LYS   E CA    1 
ATOM   11233 C  C     . LYS   D 3  135 ? 46.368  -17.806 -41.383 1.00 84.84  ? 137 LYS   E C     1 
ATOM   11234 O  O     . LYS   D 3  135 ? 46.050  -18.043 -42.556 1.00 89.15  ? 137 LYS   E O     1 
ATOM   11235 C  CB    . LYS   D 3  135 ? 44.097  -17.152 -40.546 1.00 64.93  ? 137 LYS   E CB    1 
ATOM   11236 C  CG    . LYS   D 3  135 ? 43.440  -17.440 -41.877 1.00 60.53  ? 137 LYS   E CG    1 
ATOM   11237 C  CD    . LYS   D 3  135 ? 42.336  -16.455 -42.177 1.00 65.56  ? 137 LYS   E CD    1 
ATOM   11238 C  CE    . LYS   D 3  135 ? 41.798  -16.676 -43.572 1.00 69.32  ? 137 LYS   E CE    1 
ATOM   11239 N  NZ    . LYS   D 3  135 ? 42.860  -16.450 -44.590 1.00 96.95  ? 137 LYS   E NZ    1 
ATOM   11240 N  N     . GLU   D 3  136 ? 47.581  -17.383 -41.036 1.00 83.86  ? 138 GLU   E N     1 
ATOM   11241 C  CA    . GLU   D 3  136 ? 48.691  -17.428 -41.968 1.00 86.78  ? 138 GLU   E CA    1 
ATOM   11242 C  C     . GLU   D 3  136 ? 49.690  -18.485 -41.527 1.00 90.15  ? 138 GLU   E C     1 
ATOM   11243 O  O     . GLU   D 3  136 ? 50.862  -18.181 -41.286 1.00 94.07  ? 138 GLU   E O     1 
ATOM   11244 C  CB    . GLU   D 3  136 ? 49.365  -16.070 -42.088 1.00 81.56  ? 138 GLU   E CB    1 
ATOM   11245 C  CG    . GLU   D 3  136 ? 50.381  -16.068 -43.196 1.00 90.75  ? 138 GLU   E CG    1 
ATOM   11246 C  CD    . GLU   D 3  136 ? 50.441  -14.754 -43.927 1.00 102.49 ? 138 GLU   E CD    1 
ATOM   11247 O  OE1   . GLU   D 3  136 ? 50.793  -13.734 -43.295 1.00 98.36  ? 138 GLU   E OE1   1 
ATOM   11248 O  OE2   . GLU   D 3  136 ? 50.130  -14.742 -45.137 1.00 112.19 ? 138 GLU   E OE2   1 
ATOM   11249 N  N     . LEU   D 3  137 ? 49.218  -19.729 -41.409 1.00 92.74  ? 139 LEU   E N     1 
ATOM   11250 C  CA    . LEU   D 3  137 ? 50.038  -20.897 -41.075 1.00 89.16  ? 139 LEU   E CA    1 
ATOM   11251 C  C     . LEU   D 3  137 ? 49.540  -22.045 -41.953 1.00 94.02  ? 139 LEU   E C     1 
ATOM   11252 O  O     . LEU   D 3  137 ? 48.592  -22.750 -41.592 1.00 87.46  ? 139 LEU   E O     1 
ATOM   11253 C  CB    . LEU   D 3  137 ? 49.956  -21.237 -39.594 1.00 87.88  ? 139 LEU   E CB    1 
ATOM   11254 C  CG    . LEU   D 3  137 ? 51.013  -20.621 -38.680 1.00 75.35  ? 139 LEU   E CG    1 
ATOM   11255 C  CD1   . LEU   D 3  137 ? 51.016  -19.100 -38.750 1.00 64.69  ? 139 LEU   E CD1   1 
ATOM   11256 C  CD2   . LEU   D 3  137 ? 50.780  -21.107 -37.264 1.00 67.48  ? 139 LEU   E CD2   1 
ATOM   11257 N  N     . LYS   D 3  138 ? 50.180  -22.211 -43.111 1.00 107.26 ? 140 LYS   E N     1 
ATOM   11258 C  CA    . LYS   D 3  138 ? 49.847  -23.267 -44.061 1.00 102.14 ? 140 LYS   E CA    1 
ATOM   11259 C  C     . LYS   D 3  138 ? 50.822  -24.429 -43.902 1.00 89.89  ? 140 LYS   E C     1 
ATOM   11260 O  O     . LYS   D 3  138 ? 51.984  -24.219 -43.549 1.00 75.58  ? 140 LYS   E O     1 
ATOM   11261 C  CB    . LYS   D 3  138 ? 49.885  -22.734 -45.498 1.00 91.12  ? 140 LYS   E CB    1 
ATOM   11262 C  CG    . LYS   D 3  138 ? 49.455  -21.288 -45.632 1.00 74.16  ? 140 LYS   E CG    1 
ATOM   11263 C  CD    . LYS   D 3  138 ? 48.076  -21.080 -45.032 1.00 90.36  ? 140 LYS   E CD    1 
ATOM   11264 C  CE    . LYS   D 3  138 ? 47.621  -19.635 -45.162 1.00 90.06  ? 140 LYS   E CE    1 
ATOM   11265 N  NZ    . LYS   D 3  138 ? 46.180  -19.465 -44.807 1.00 74.44  ? 140 LYS   E NZ    1 
ATOM   11266 N  N     . MET   E 4  1   ? -5.563  56.786  59.580  1.00 48.04  ? 1   MET   F N     1 
ATOM   11267 C  CA    . MET   E 4  1   ? -4.411  55.936  59.871  1.00 65.91  ? 1   MET   F CA    1 
ATOM   11268 C  C     . MET   E 4  1   ? -3.389  56.712  60.691  1.00 56.99  ? 1   MET   F C     1 
ATOM   11269 O  O     . MET   E 4  1   ? -3.049  57.845  60.351  1.00 48.73  ? 1   MET   F O     1 
ATOM   11270 C  CB    . MET   E 4  1   ? -3.764  55.411  58.570  1.00 81.14  ? 1   MET   F CB    1 
ATOM   11271 C  CG    . MET   E 4  1   ? -2.841  54.164  58.728  1.00 80.74  ? 1   MET   F CG    1 
ATOM   11272 S  SD    . MET   E 4  1   ? -3.724  52.562  58.786  1.00 109.63 ? 1   MET   F SD    1 
ATOM   11273 C  CE    . MET   E 4  1   ? -2.387  51.355  58.619  1.00 75.19  ? 1   MET   F CE    1 
ATOM   11274 N  N     . TYR   E 4  2   ? -2.916  56.103  61.777  1.00 54.29  ? 2   TYR   F N     1 
ATOM   11275 C  CA    . TYR   E 4  2   ? -1.772  56.604  62.523  1.00 47.48  ? 2   TYR   F CA    1 
ATOM   11276 C  C     . TYR   E 4  2   ? -0.738  55.500  62.637  1.00 50.00  ? 2   TYR   F C     1 
ATOM   11277 O  O     . TYR   E 4  2   ? -1.064  54.312  62.549  1.00 53.58  ? 2   TYR   F O     1 
ATOM   11278 C  CB    . TYR   E 4  2   ? -2.164  57.070  63.907  1.00 46.96  ? 2   TYR   F CB    1 
ATOM   11279 C  CG    . TYR   E 4  2   ? -3.297  58.060  63.916  1.00 49.17  ? 2   TYR   F CG    1 
ATOM   11280 C  CD1   . TYR   E 4  2   ? -3.161  59.292  63.317  1.00 37.02  ? 2   TYR   F CD1   1 
ATOM   11281 C  CD2   . TYR   E 4  2   ? -4.494  57.771  64.565  1.00 49.03  ? 2   TYR   F CD2   1 
ATOM   11282 C  CE1   . TYR   E 4  2   ? -4.182  60.203  63.352  1.00 48.26  ? 2   TYR   F CE1   1 
ATOM   11283 C  CE2   . TYR   E 4  2   ? -5.521  58.674  64.605  1.00 43.22  ? 2   TYR   F CE2   1 
ATOM   11284 C  CZ    . TYR   E 4  2   ? -5.366  59.891  63.996  1.00 46.26  ? 2   TYR   F CZ    1 
ATOM   11285 O  OH    . TYR   E 4  2   ? -6.392  60.811  64.017  1.00 46.06  ? 2   TYR   F OH    1 
ATOM   11286 N  N     . THR   E 4  3   ? 0.516   55.893  62.842  1.00 41.91  ? 3   THR   F N     1 
ATOM   11287 C  CA    . THR   E 4  3   ? 1.589   54.921  63.011  1.00 54.02  ? 3   THR   F CA    1 
ATOM   11288 C  C     . THR   E 4  3   ? 2.229   55.025  64.395  1.00 48.34  ? 3   THR   F C     1 
ATOM   11289 O  O     . THR   E 4  3   ? 2.204   56.075  65.045  1.00 38.28  ? 3   THR   F O     1 
ATOM   11290 C  CB    . THR   E 4  3   ? 2.655   55.110  61.943  1.00 46.55  ? 3   THR   F CB    1 
ATOM   11291 O  OG1   . THR   E 4  3   ? 3.196   56.427  62.077  1.00 46.46  ? 3   THR   F OG1   1 
ATOM   11292 C  CG2   . THR   E 4  3   ? 2.034   54.985  60.589  1.00 43.13  ? 3   THR   F CG2   1 
ATOM   11293 N  N     . PHE   E 4  4   ? 2.833   53.922  64.830  1.00 46.39  ? 4   PHE   F N     1 
ATOM   11294 C  CA    . PHE   E 4  4   ? 3.519   53.896  66.113  1.00 46.54  ? 4   PHE   F CA    1 
ATOM   11295 C  C     . PHE   E 4  4   ? 4.616   52.838  66.087  1.00 49.91  ? 4   PHE   F C     1 
ATOM   11296 O  O     . PHE   E 4  4   ? 4.510   51.838  65.376  1.00 47.69  ? 4   PHE   F O     1 
ATOM   11297 C  CB    . PHE   E 4  4   ? 2.538   53.631  67.258  1.00 45.11  ? 4   PHE   F CB    1 
ATOM   11298 C  CG    . PHE   E 4  4   ? 2.063   52.205  67.351  1.00 45.91  ? 4   PHE   F CG    1 
ATOM   11299 C  CD1   . PHE   E 4  4   ? 0.902   51.803  66.703  1.00 50.31  ? 4   PHE   F CD1   1 
ATOM   11300 C  CD2   . PHE   E 4  4   ? 2.757   51.275  68.119  1.00 50.63  ? 4   PHE   F CD2   1 
ATOM   11301 C  CE1   . PHE   E 4  4   ? 0.449   50.500  66.799  1.00 53.19  ? 4   PHE   F CE1   1 
ATOM   11302 C  CE2   . PHE   E 4  4   ? 2.314   49.964  68.221  1.00 50.23  ? 4   PHE   F CE2   1 
ATOM   11303 C  CZ    . PHE   E 4  4   ? 1.157   49.578  67.559  1.00 56.35  ? 4   PHE   F CZ    1 
ATOM   11304 N  N     . VAL   E 4  5   ? 5.675   53.073  66.873  1.00 48.23  ? 5   VAL   F N     1 
ATOM   11305 C  CA    . VAL   E 4  5   ? 6.769   52.121  67.034  1.00 46.86  ? 5   VAL   F CA    1 
ATOM   11306 C  C     . VAL   E 4  5   ? 6.824   51.675  68.488  1.00 50.17  ? 5   VAL   F C     1 
ATOM   11307 O  O     . VAL   E 4  5   ? 6.419   52.405  69.395  1.00 50.32  ? 5   VAL   F O     1 
ATOM   11308 C  CB    . VAL   E 4  5   ? 8.136   52.696  66.608  1.00 47.81  ? 5   VAL   F CB    1 
ATOM   11309 C  CG1   . VAL   E 4  5   ? 8.076   53.221  65.178  1.00 51.78  ? 5   VAL   F CG1   1 
ATOM   11310 C  CG2   . VAL   E 4  5   ? 8.593   53.778  67.585  1.00 47.10  ? 5   VAL   F CG2   1 
ATOM   11311 N  N     . VAL   E 4  6   ? 7.347   50.469  68.702  1.00 52.44  ? 6   VAL   F N     1 
ATOM   11312 C  CA    . VAL   E 4  6   ? 7.431   49.842  70.016  1.00 39.29  ? 6   VAL   F CA    1 
ATOM   11313 C  C     . VAL   E 4  6   ? 8.905   49.613  70.329  1.00 47.04  ? 6   VAL   F C     1 
ATOM   11314 O  O     . VAL   E 4  6   ? 9.592   48.878  69.612  1.00 51.70  ? 6   VAL   F O     1 
ATOM   11315 C  CB    . VAL   E 4  6   ? 6.641   48.524  70.062  1.00 41.91  ? 6   VAL   F CB    1 
ATOM   11316 C  CG1   . VAL   E 4  6   ? 6.952   47.753  71.340  1.00 45.37  ? 6   VAL   F CG1   1 
ATOM   11317 C  CG2   . VAL   E 4  6   ? 5.136   48.789  69.924  1.00 41.67  ? 6   VAL   F CG2   1 
ATOM   11318 N  N     . ARG   E 4  7   ? 9.395   50.236  71.398  1.00 49.93  ? 7   ARG   F N     1 
ATOM   11319 C  CA    . ARG   E 4  7   ? 10.823  50.220  71.682  1.00 43.93  ? 7   ARG   F CA    1 
ATOM   11320 C  C     . ARG   E 4  7   ? 11.139  49.765  73.105  1.00 55.37  ? 7   ARG   F C     1 
ATOM   11321 O  O     . ARG   E 4  7   ? 12.257  49.993  73.590  1.00 55.07  ? 7   ARG   F O     1 
ATOM   11322 C  CB    . ARG   E 4  7   ? 11.417  51.598  71.406  1.00 46.29  ? 7   ARG   F CB    1 
ATOM   11323 C  CG    . ARG   E 4  7   ? 11.305  51.989  69.960  1.00 40.13  ? 7   ARG   F CG    1 
ATOM   11324 C  CD    . ARG   E 4  7   ? 11.695  53.424  69.751  1.00 48.80  ? 7   ARG   F CD    1 
ATOM   11325 N  NE    . ARG   E 4  7   ? 13.038  53.729  70.227  1.00 41.97  ? 7   ARG   F NE    1 
ATOM   11326 C  CZ    . ARG   E 4  7   ? 14.108  53.760  69.445  1.00 51.99  ? 7   ARG   F CZ    1 
ATOM   11327 N  NH1   . ARG   E 4  7   ? 14.036  53.404  68.168  1.00 44.40  ? 7   ARG   F NH1   1 
ATOM   11328 N  NH2   . ARG   E 4  7   ? 15.272  54.175  69.950  1.00 40.97  ? 7   ARG   F NH2   1 
ATOM   11329 N  N     . ASP   E 4  8   ? 10.185  49.108  73.777  1.00 55.14  ? 8   ASP   F N     1 
ATOM   11330 C  CA    . ASP   E 4  8   ? 10.403  48.469  75.081  1.00 56.09  ? 8   ASP   F CA    1 
ATOM   11331 C  C     . ASP   E 4  8   ? 9.576   47.182  75.081  1.00 63.05  ? 8   ASP   F C     1 
ATOM   11332 O  O     . ASP   E 4  8   ? 8.399   47.188  75.456  1.00 57.72  ? 8   ASP   F O     1 
ATOM   11333 C  CB    . ASP   E 4  8   ? 10.020  49.398  76.222  1.00 47.94  ? 8   ASP   F CB    1 
ATOM   11334 C  CG    . ASP   E 4  8   ? 10.062  48.723  77.570  1.00 48.77  ? 8   ASP   F CG    1 
ATOM   11335 O  OD1   . ASP   E 4  8   ? 10.405  47.525  77.644  1.00 55.81  ? 8   ASP   F OD1   1 
ATOM   11336 O  OD2   . ASP   E 4  8   ? 9.749   49.405  78.568  1.00 61.37  ? 8   ASP   F OD2   1 
ATOM   11337 N  N     . GLU   E 4  9   ? 10.208  46.078  74.665  1.00 70.66  ? 9   GLU   F N     1 
ATOM   11338 C  CA    . GLU   E 4  9   ? 9.498   44.820  74.434  1.00 66.74  ? 9   GLU   F CA    1 
ATOM   11339 C  C     . GLU   E 4  9   ? 9.108   44.104  75.721  1.00 63.76  ? 9   GLU   F C     1 
ATOM   11340 O  O     . GLU   E 4  9   ? 8.416   43.081  75.652  1.00 65.30  ? 9   GLU   F O     1 
ATOM   11341 C  CB    . GLU   E 4  9   ? 10.356  43.888  73.576  1.00 61.77  ? 9   GLU   F CB    1 
ATOM   11342 C  CG    . GLU   E 4  9   ? 9.544   43.019  72.631  1.00 73.99  ? 9   GLU   F CG    1 
ATOM   11343 C  CD    . GLU   E 4  9   ? 9.198   43.737  71.345  1.00 57.41  ? 9   GLU   F CD    1 
ATOM   11344 O  OE1   . GLU   E 4  9   ? 9.998   44.595  70.925  1.00 61.34  ? 9   GLU   F OE1   1 
ATOM   11345 O  OE2   . GLU   E 4  9   ? 8.136   43.443  70.751  1.00 55.45  ? 9   GLU   F OE2   1 
ATOM   11346 N  N     . ASN   E 4  10  ? 9.522   44.610  76.884  1.00 61.91  ? 10  ASN   F N     1 
ATOM   11347 C  CA    . ASN   E 4  10  ? 9.228   43.980  78.164  1.00 55.67  ? 10  ASN   F CA    1 
ATOM   11348 C  C     . ASN   E 4  10  ? 8.209   44.772  78.979  1.00 63.51  ? 10  ASN   F C     1 
ATOM   11349 O  O     . ASN   E 4  10  ? 8.242   44.755  80.212  1.00 73.08  ? 10  ASN   F O     1 
ATOM   11350 C  CB    . ASN   E 4  10  ? 10.514  43.790  78.958  1.00 55.70  ? 10  ASN   F CB    1 
ATOM   11351 C  CG    . ASN   E 4  10  ? 11.572  43.065  78.165  1.00 69.18  ? 10  ASN   F CG    1 
ATOM   11352 O  OD1   . ASN   E 4  10  ? 11.272  42.392  77.172  1.00 63.45  ? 10  ASN   F OD1   1 
ATOM   11353 N  ND2   . ASN   E 4  10  ? 12.822  43.191  78.597  1.00 80.05  ? 10  ASN   F ND2   1 
ATOM   11354 N  N     . SER   E 4  11  ? 7.296   45.463  78.305  1.00 57.72  ? 11  SER   F N     1 
ATOM   11355 C  CA    . SER   E 4  11  ? 6.250   46.244  78.954  1.00 50.72  ? 11  SER   F CA    1 
ATOM   11356 C  C     . SER   E 4  11  ? 4.926   45.529  78.727  1.00 51.83  ? 11  SER   F C     1 
ATOM   11357 O  O     . SER   E 4  11  ? 4.321   45.638  77.657  1.00 55.91  ? 11  SER   F O     1 
ATOM   11358 C  CB    . SER   E 4  11  ? 6.212   47.671  78.415  1.00 56.20  ? 11  SER   F CB    1 
ATOM   11359 O  OG    . SER   E 4  11  ? 5.052   48.360  78.850  1.00 53.11  ? 11  SER   F OG    1 
ATOM   11360 N  N     . SER   E 4  12  ? 4.489   44.782  79.735  1.00 52.04  ? 12  SER   F N     1 
ATOM   11361 C  CA    . SER   E 4  12  ? 3.137   44.242  79.715  1.00 57.50  ? 12  SER   F CA    1 
ATOM   11362 C  C     . SER   E 4  12  ? 2.114   45.325  79.387  1.00 56.25  ? 12  SER   F C     1 
ATOM   11363 O  O     . SER   E 4  12  ? 1.197   45.110  78.585  1.00 50.33  ? 12  SER   F O     1 
ATOM   11364 C  CB    . SER   E 4  12  ? 2.829   43.615  81.070  1.00 54.67  ? 12  SER   F CB    1 
ATOM   11365 O  OG    . SER   E 4  12  ? 3.108   44.539  82.108  1.00 61.97  ? 12  SER   F OG    1 
ATOM   11366 N  N     . VAL   E 4  13  ? 2.271   46.500  79.999  1.00 56.99  ? 13  VAL   F N     1 
ATOM   11367 C  CA    . VAL   E 4  13  ? 1.306   47.582  79.842  1.00 52.04  ? 13  VAL   F CA    1 
ATOM   11368 C  C     . VAL   E 4  13  ? 1.212   48.015  78.386  1.00 56.00  ? 13  VAL   F C     1 
ATOM   11369 O  O     . VAL   E 4  13  ? 0.115   48.186  77.843  1.00 59.29  ? 13  VAL   F O     1 
ATOM   11370 C  CB    . VAL   E 4  13  ? 1.682   48.762  80.754  1.00 53.44  ? 13  VAL   F CB    1 
ATOM   11371 C  CG1   . VAL   E 4  13  ? 0.972   50.030  80.301  1.00 48.81  ? 13  VAL   F CG1   1 
ATOM   11372 C  CG2   . VAL   E 4  13  ? 1.348   48.441  82.195  1.00 48.09  ? 13  VAL   F CG2   1 
ATOM   11373 N  N     . TYR   E 4  14  ? 2.357   48.204  77.726  1.00 58.04  ? 14  TYR   F N     1 
ATOM   11374 C  CA    . TYR   E 4  14  ? 2.328   48.734  76.366  1.00 60.30  ? 14  TYR   F CA    1 
ATOM   11375 C  C     . TYR   E 4  14  ? 2.279   47.663  75.289  1.00 53.94  ? 14  TYR   F C     1 
ATOM   11376 O  O     . TYR   E 4  14  ? 1.979   47.987  74.137  1.00 53.96  ? 14  TYR   F O     1 
ATOM   11377 C  CB    . TYR   E 4  14  ? 3.504   49.688  76.154  1.00 47.54  ? 14  TYR   F CB    1 
ATOM   11378 C  CG    . TYR   E 4  14  ? 3.204   50.964  76.896  1.00 52.74  ? 14  TYR   F CG    1 
ATOM   11379 C  CD1   . TYR   E 4  14  ? 2.321   51.902  76.366  1.00 44.87  ? 14  TYR   F CD1   1 
ATOM   11380 C  CD2   . TYR   E 4  14  ? 3.719   51.187  78.169  1.00 44.45  ? 14  TYR   F CD2   1 
ATOM   11381 C  CE1   . TYR   E 4  14  ? 2.005   53.047  77.059  1.00 49.05  ? 14  TYR   F CE1   1 
ATOM   11382 C  CE2   . TYR   E 4  14  ? 3.417   52.325  78.863  1.00 42.32  ? 14  TYR   F CE2   1 
ATOM   11383 C  CZ    . TYR   E 4  14  ? 2.556   53.259  78.307  1.00 49.90  ? 14  TYR   F CZ    1 
ATOM   11384 O  OH    . TYR   E 4  14  ? 2.248   54.406  79.008  1.00 42.73  ? 14  TYR   F OH    1 
ATOM   11385 N  N     . ALA   E 4  15  ? 2.532   46.403  75.636  1.00 52.27  ? 15  ALA   F N     1 
ATOM   11386 C  CA    . ALA   E 4  15  ? 2.080   45.313  74.784  1.00 52.94  ? 15  ALA   F CA    1 
ATOM   11387 C  C     . ALA   E 4  15  ? 0.567   45.362  74.604  1.00 56.87  ? 15  ALA   F C     1 
ATOM   11388 O  O     . ALA   E 4  15  ? 0.054   45.254  73.482  1.00 53.82  ? 15  ALA   F O     1 
ATOM   11389 C  CB    . ALA   E 4  15  ? 2.512   43.979  75.381  1.00 52.11  ? 15  ALA   F CB    1 
ATOM   11390 N  N     . GLU   E 4  16  ? -0.171  45.540  75.703  1.00 57.72  ? 16  GLU   F N     1 
ATOM   11391 C  CA    . GLU   E 4  16  ? -1.624  45.617  75.587  1.00 63.31  ? 16  GLU   F CA    1 
ATOM   11392 C  C     . GLU   E 4  16  ? -2.049  46.878  74.847  1.00 59.18  ? 16  GLU   F C     1 
ATOM   11393 O  O     . GLU   E 4  16  ? -3.011  46.851  74.070  1.00 61.40  ? 16  GLU   F O     1 
ATOM   11394 C  CB    . GLU   E 4  16  ? -2.280  45.553  76.970  1.00 68.10  ? 16  GLU   F CB    1 
ATOM   11395 C  CG    . GLU   E 4  16  ? -3.820  45.446  76.946  1.00 62.33  ? 16  GLU   F CG    1 
ATOM   11396 C  CD    . GLU   E 4  16  ? -4.330  44.216  76.195  1.00 70.06  ? 16  GLU   F CD    1 
ATOM   11397 O  OE1   . GLU   E 4  16  ? -3.514  43.338  75.836  1.00 65.43  ? 16  GLU   F OE1   1 
ATOM   11398 O  OE2   . GLU   E 4  16  ? -5.557  44.131  75.956  1.00 77.42  ? 16  GLU   F OE2   1 
ATOM   11399 N  N     . VAL   E 4  17  ? -1.343  47.990  75.067  1.00 61.75  ? 17  VAL   F N     1 
ATOM   11400 C  CA    . VAL   E 4  17  ? -1.652  49.221  74.339  1.00 62.03  ? 17  VAL   F CA    1 
ATOM   11401 C  C     . VAL   E 4  17  ? -1.514  48.994  72.836  1.00 53.91  ? 17  VAL   F C     1 
ATOM   11402 O  O     . VAL   E 4  17  ? -2.462  49.187  72.069  1.00 54.34  ? 17  VAL   F O     1 
ATOM   11403 C  CB    . VAL   E 4  17  ? -0.762  50.383  74.823  1.00 61.34  ? 17  VAL   F CB    1 
ATOM   11404 C  CG1   . VAL   E 4  17  ? -0.896  51.591  73.886  1.00 53.47  ? 17  VAL   F CG1   1 
ATOM   11405 C  CG2   . VAL   E 4  17  ? -1.125  50.779  76.257  1.00 59.41  ? 17  VAL   F CG2   1 
ATOM   11406 N  N     . SER   E 4  18  ? -0.330  48.579  72.388  1.00 53.73  ? 18  SER   F N     1 
ATOM   11407 C  CA    . SER   E 4  18  ? -0.170  48.343  70.959  1.00 52.59  ? 18  SER   F CA    1 
ATOM   11408 C  C     . SER   E 4  18  ? -1.133  47.272  70.461  1.00 58.46  ? 18  SER   F C     1 
ATOM   11409 O  O     . SER   E 4  18  ? -1.608  47.350  69.323  1.00 62.39  ? 18  SER   F O     1 
ATOM   11410 C  CB    . SER   E 4  18  ? 1.272   47.968  70.639  1.00 55.86  ? 18  SER   F CB    1 
ATOM   11411 O  OG    . SER   E 4  18  ? 1.804   47.122  71.639  1.00 71.27  ? 18  SER   F OG    1 
ATOM   11412 N  N     . ARG   E 4  19  ? -1.451  46.277  71.294  1.00 52.97  ? 19  ARG   F N     1 
ATOM   11413 C  CA    . ARG   E 4  19  ? -2.464  45.297  70.915  1.00 52.38  ? 19  ARG   F CA    1 
ATOM   11414 C  C     . ARG   E 4  19  ? -3.795  45.985  70.624  1.00 51.36  ? 19  ARG   F C     1 
ATOM   11415 O  O     . ARG   E 4  19  ? -4.364  45.845  69.537  1.00 53.01  ? 19  ARG   F O     1 
ATOM   11416 C  CB    . ARG   E 4  19  ? -2.616  44.248  72.021  1.00 66.07  ? 19  ARG   F CB    1 
ATOM   11417 C  CG    . ARG   E 4  19  ? -3.253  42.934  71.574  1.00 63.54  ? 19  ARG   F CG    1 
ATOM   11418 C  CD    . ARG   E 4  19  ? -3.681  42.073  72.770  1.00 76.01  ? 19  ARG   F CD    1 
ATOM   11419 N  NE    . ARG   E 4  19  ? -4.851  42.622  73.454  1.00 83.16  ? 19  ARG   F NE    1 
ATOM   11420 C  CZ    . ARG   E 4  19  ? -6.112  42.384  73.107  1.00 88.35  ? 19  ARG   F CZ    1 
ATOM   11421 N  NH1   . ARG   E 4  19  ? -6.416  41.551  72.121  1.00 81.11  ? 19  ARG   F NH1   1 
ATOM   11422 N  NH2   . ARG   E 4  19  ? -7.093  43.007  73.756  1.00 71.75  ? 19  ARG   F NH2   1 
ATOM   11423 N  N     . LEU   E 4  20  ? -4.301  46.751  71.588  1.00 54.13  ? 20  LEU   F N     1 
ATOM   11424 C  CA    . LEU   E 4  20  ? -5.532  47.501  71.364  1.00 49.32  ? 20  LEU   F CA    1 
ATOM   11425 C  C     . LEU   E 4  20  ? -5.433  48.381  70.120  1.00 56.53  ? 20  LEU   F C     1 
ATOM   11426 O  O     . LEU   E 4  20  ? -6.286  48.308  69.227  1.00 60.99  ? 20  LEU   F O     1 
ATOM   11427 C  CB    . LEU   E 4  20  ? -5.853  48.344  72.597  1.00 52.84  ? 20  LEU   F CB    1 
ATOM   11428 C  CG    . LEU   E 4  20  ? -6.333  47.641  73.860  1.00 55.11  ? 20  LEU   F CG    1 
ATOM   11429 C  CD1   . LEU   E 4  20  ? -6.169  48.565  75.042  1.00 49.18  ? 20  LEU   F CD1   1 
ATOM   11430 C  CD2   . LEU   E 4  20  ? -7.791  47.248  73.701  1.00 41.80  ? 20  LEU   F CD2   1 
ATOM   11431 N  N     . LEU   E 4  21  ? -4.404  49.236  70.050  1.00 47.66  ? 21  LEU   F N     1 
ATOM   11432 C  CA    . LEU   E 4  21  ? -4.281  50.160  68.925  1.00 53.14  ? 21  LEU   F CA    1 
ATOM   11433 C  C     . LEU   E 4  21  ? -4.363  49.419  67.594  1.00 53.04  ? 21  LEU   F C     1 
ATOM   11434 O  O     . LEU   E 4  21  ? -5.156  49.777  66.717  1.00 50.20  ? 21  LEU   F O     1 
ATOM   11435 C  CB    . LEU   E 4  21  ? -2.971  50.943  69.021  1.00 63.36  ? 21  LEU   F CB    1 
ATOM   11436 C  CG    . LEU   E 4  21  ? -2.773  51.921  70.184  1.00 62.05  ? 21  LEU   F CG    1 
ATOM   11437 C  CD1   . LEU   E 4  21  ? -1.286  52.245  70.344  1.00 50.94  ? 21  LEU   F CD1   1 
ATOM   11438 C  CD2   . LEU   E 4  21  ? -3.585  53.196  69.975  1.00 48.24  ? 21  LEU   F CD2   1 
ATOM   11439 N  N     . LEU   E 4  22  ? -3.548  48.376  67.429  1.00 51.81  ? 22  LEU   F N     1 
ATOM   11440 C  CA    . LEU   E 4  22  ? -3.647  47.549  66.232  1.00 55.36  ? 22  LEU   F CA    1 
ATOM   11441 C  C     . LEU   E 4  22  ? -5.064  47.025  66.045  1.00 54.69  ? 22  LEU   F C     1 
ATOM   11442 O  O     . LEU   E 4  22  ? -5.606  47.042  64.931  1.00 47.32  ? 22  LEU   F O     1 
ATOM   11443 C  CB    . LEU   E 4  22  ? -2.647  46.391  66.306  1.00 54.69  ? 22  LEU   F CB    1 
ATOM   11444 C  CG    . LEU   E 4  22  ? -1.194  46.790  66.029  1.00 67.01  ? 22  LEU   F CG    1 
ATOM   11445 C  CD1   . LEU   E 4  22  ? -0.245  45.620  66.211  1.00 55.18  ? 22  LEU   F CD1   1 
ATOM   11446 C  CD2   . LEU   E 4  22  ? -1.059  47.398  64.622  1.00 63.08  ? 22  LEU   F CD2   1 
ATOM   11447 N  N     . ALA   E 4  23  ? -5.696  46.584  67.132  1.00 59.88  ? 23  ALA   F N     1 
ATOM   11448 C  CA    . ALA   E 4  23  ? -7.007  45.949  67.036  1.00 59.59  ? 23  ALA   F CA    1 
ATOM   11449 C  C     . ALA   E 4  23  ? -8.101  46.933  66.619  1.00 59.00  ? 23  ALA   F C     1 
ATOM   11450 O  O     . ALA   E 4  23  ? -9.291  46.656  66.795  1.00 60.26  ? 23  ALA   F O     1 
ATOM   11451 C  CB    . ALA   E 4  23  ? -7.354  45.280  68.366  1.00 40.83  ? 23  ALA   F CB    1 
ATOM   11452 N  N     . THR   E 4  24  ? -7.716  48.075  66.048  1.00 56.71  ? 24  THR   F N     1 
ATOM   11453 C  CA    . THR   E 4  24  ? -8.656  49.129  65.708  1.00 46.20  ? 24  THR   F CA    1 
ATOM   11454 C  C     . THR   E 4  24  ? -8.729  49.419  64.215  1.00 66.16  ? 24  THR   F C     1 
ATOM   11455 O  O     . THR   E 4  24  ? -9.643  50.139  63.788  1.00 66.60  ? 24  THR   F O     1 
ATOM   11456 C  CB    . THR   E 4  24  ? -8.291  50.428  66.448  1.00 55.28  ? 24  THR   F CB    1 
ATOM   11457 O  OG1   . THR   E 4  24  ? -7.102  50.987  65.867  1.00 62.30  ? 24  THR   F OG1   1 
ATOM   11458 C  CG2   . THR   E 4  24  ? -8.037  50.158  67.940  1.00 47.05  ? 24  THR   F CG2   1 
ATOM   11459 N  N     . GLY   E 4  25  ? -7.800  48.896  63.413  1.00 47.61  ? 25  GLY   F N     1 
ATOM   11460 C  CA    . GLY   E 4  25  ? -7.797  49.168  61.991  1.00 63.42  ? 25  GLY   F CA    1 
ATOM   11461 C  C     . GLY   E 4  25  ? -7.375  50.568  61.597  1.00 70.65  ? 25  GLY   F C     1 
ATOM   11462 O  O     . GLY   E 4  25  ? -7.266  50.853  60.396  1.00 68.51  ? 25  GLY   F O     1 
ATOM   11463 N  N     . GLN   E 4  26  ? -7.123  51.445  62.564  1.00 61.17  ? 26  GLN   F N     1 
ATOM   11464 C  CA    . GLN   E 4  26  ? -6.702  52.805  62.284  1.00 64.23  ? 26  GLN   F CA    1 
ATOM   11465 C  C     . GLN   E 4  26  ? -5.266  53.092  62.707  1.00 57.22  ? 26  GLN   F C     1 
ATOM   11466 O  O     . GLN   E 4  26  ? -4.824  54.239  62.583  1.00 57.93  ? 26  GLN   F O     1 
ATOM   11467 C  CB    . GLN   E 4  26  ? -7.648  53.797  62.975  1.00 72.71  ? 26  GLN   F CB    1 
ATOM   11468 C  CG    . GLN   E 4  26  ? -9.136  53.571  62.723  1.00 59.16  ? 26  GLN   F CG    1 
ATOM   11469 C  CD    . GLN   E 4  26  ? -9.981  54.747  63.189  1.00 69.64  ? 26  GLN   F CD    1 
ATOM   11470 O  OE1   . GLN   E 4  26  ? -9.535  55.895  63.161  1.00 77.27  ? 26  GLN   F OE1   1 
ATOM   11471 N  NE2   . GLN   E 4  26  ? -11.203 54.466  63.635  1.00 73.44  ? 26  GLN   F NE2   1 
ATOM   11472 N  N     . TRP   E 4  27  ? -4.533  52.100  63.220  1.00 51.42  ? 27  TRP   F N     1 
ATOM   11473 C  CA    . TRP   E 4  27  ? -3.149  52.276  63.650  1.00 48.17  ? 27  TRP   F CA    1 
ATOM   11474 C  C     . TRP   E 4  27  ? -2.310  51.191  63.001  1.00 55.44  ? 27  TRP   F C     1 
ATOM   11475 O  O     . TRP   E 4  27  ? -2.705  50.022  63.014  1.00 67.26  ? 27  TRP   F O     1 
ATOM   11476 C  CB    . TRP   E 4  27  ? -2.995  52.219  65.191  1.00 43.69  ? 27  TRP   F CB    1 
ATOM   11477 C  CG    . TRP   E 4  27  ? -3.320  53.527  65.886  1.00 52.20  ? 27  TRP   F CG    1 
ATOM   11478 C  CD1   . TRP   E 4  27  ? -4.567  54.029  66.158  1.00 55.93  ? 27  TRP   F CD1   1 
ATOM   11479 C  CD2   . TRP   E 4  27  ? -2.385  54.508  66.369  1.00 52.01  ? 27  TRP   F CD2   1 
ATOM   11480 N  NE1   . TRP   E 4  27  ? -4.464  55.257  66.779  1.00 47.75  ? 27  TRP   F NE1   1 
ATOM   11481 C  CE2   . TRP   E 4  27  ? -3.137  55.574  66.914  1.00 52.96  ? 27  TRP   F CE2   1 
ATOM   11482 C  CE3   . TRP   E 4  27  ? -0.990  54.588  66.392  1.00 41.24  ? 27  TRP   F CE3   1 
ATOM   11483 C  CZ2   . TRP   E 4  27  ? -2.536  56.700  67.474  1.00 48.94  ? 27  TRP   F CZ2   1 
ATOM   11484 C  CZ3   . TRP   E 4  27  ? -0.403  55.698  66.941  1.00 47.42  ? 27  TRP   F CZ3   1 
ATOM   11485 C  CH2   . TRP   E 4  27  ? -1.171  56.743  67.478  1.00 46.01  ? 27  TRP   F CH2   1 
ATOM   11486 N  N     . LYS   E 4  28  ? -1.167  51.575  62.427  1.00 51.43  ? 28  LYS   F N     1 
ATOM   11487 C  CA    . LYS   E 4  28  ? -0.168  50.629  61.937  1.00 58.81  ? 28  LYS   F CA    1 
ATOM   11488 C  C     . LYS   E 4  28  ? 1.096   50.708  62.787  1.00 55.92  ? 28  LYS   F C     1 
ATOM   11489 O  O     . LYS   E 4  28  ? 1.504   51.797  63.199  1.00 70.29  ? 28  LYS   F O     1 
ATOM   11490 C  CB    . LYS   E 4  28  ? 0.191   50.894  60.466  1.00 59.87  ? 28  LYS   F CB    1 
ATOM   11491 C  CG    . LYS   E 4  28  ? 1.308   49.967  59.923  1.00 66.83  ? 28  LYS   F CG    1 
ATOM   11492 C  CD    . LYS   E 4  28  ? 1.707   50.286  58.463  1.00 69.33  ? 28  LYS   F CD    1 
ATOM   11493 C  CE    . LYS   E 4  28  ? 2.571   49.172  57.825  1.00 79.92  ? 28  LYS   F CE    1 
ATOM   11494 N  NZ    . LYS   E 4  28  ? 3.999   49.108  58.303  1.00 53.11  ? 28  LYS   F NZ    1 
ATOM   11495 N  N     . ARG   E 4  29  ? 1.718   49.557  63.039  1.00 49.89  ? 29  ARG   F N     1 
ATOM   11496 C  CA    . ARG   E 4  29  ? 3.020   49.495  63.698  1.00 44.96  ? 29  ARG   F CA    1 
ATOM   11497 C  C     . ARG   E 4  29  ? 4.142   49.515  62.661  1.00 46.44  ? 29  ARG   F C     1 
ATOM   11498 O  O     . ARG   E 4  29  ? 4.059   48.856  61.624  1.00 60.79  ? 29  ARG   F O     1 
ATOM   11499 C  CB    . ARG   E 4  29  ? 3.134   48.234  64.565  1.00 49.70  ? 29  ARG   F CB    1 
ATOM   11500 C  CG    . ARG   E 4  29  ? 4.454   48.136  65.331  1.00 52.15  ? 29  ARG   F CG    1 
ATOM   11501 C  CD    . ARG   E 4  29  ? 4.635   46.814  66.089  1.00 44.88  ? 29  ARG   F CD    1 
ATOM   11502 N  NE    . ARG   E 4  29  ? 5.994   46.679  66.614  1.00 45.63  ? 29  ARG   F NE    1 
ATOM   11503 C  CZ    . ARG   E 4  29  ? 6.336   45.924  67.652  1.00 53.18  ? 29  ARG   F CZ    1 
ATOM   11504 N  NH1   . ARG   E 4  29  ? 5.447   45.181  68.288  1.00 48.31  ? 29  ARG   F NH1   1 
ATOM   11505 N  NH2   . ARG   E 4  29  ? 7.603   45.924  68.071  1.00 52.01  ? 29  ARG   F NH2   1 
ATOM   11506 N  N     . LEU   E 4  30  ? 5.193   50.269  62.946  1.00 48.22  ? 30  LEU   F N     1 
ATOM   11507 C  CA    . LEU   E 4  30  ? 6.324   50.429  62.043  1.00 47.25  ? 30  LEU   F CA    1 
ATOM   11508 C  C     . LEU   E 4  30  ? 7.541   49.713  62.614  1.00 52.29  ? 30  LEU   F C     1 
ATOM   11509 O  O     . LEU   E 4  30  ? 7.569   49.329  63.784  1.00 43.97  ? 30  LEU   F O     1 
ATOM   11510 C  CB    . LEU   E 4  30  ? 6.639   51.922  61.810  1.00 41.13  ? 30  LEU   F CB    1 
ATOM   11511 C  CG    . LEU   E 4  30  ? 5.581   52.899  61.244  1.00 41.11  ? 30  LEU   F CG    1 
ATOM   11512 C  CD1   . LEU   E 4  30  ? 6.091   54.319  61.168  1.00 34.00  ? 30  LEU   F CD1   1 
ATOM   11513 C  CD2   . LEU   E 4  30  ? 5.083   52.503  59.881  1.00 35.61  ? 30  LEU   F CD2   1 
ATOM   11514 N  N     . ARG   E 4  31  ? 8.560   49.533  61.772  1.00 59.94  ? 31  ARG   F N     1 
ATOM   11515 C  CA    . ARG   E 4  31  ? 9.876   49.154  62.274  1.00 62.90  ? 31  ARG   F CA    1 
ATOM   11516 C  C     . ARG   E 4  31  ? 10.316  50.140  63.349  1.00 62.82  ? 31  ARG   F C     1 
ATOM   11517 O  O     . ARG   E 4  31  ? 10.194  51.355  63.176  1.00 66.37  ? 31  ARG   F O     1 
ATOM   11518 C  CB    . ARG   E 4  31  ? 10.907  49.148  61.143  1.00 73.38  ? 31  ARG   F CB    1 
ATOM   11519 C  CG    . ARG   E 4  31  ? 10.428  48.554  59.827  1.00 95.05  ? 31  ARG   F CG    1 
ATOM   11520 C  CD    . ARG   E 4  31  ? 10.287  47.051  59.936  1.00 103.30 ? 31  ARG   F CD    1 
ATOM   11521 N  NE    . ARG   E 4  31  ? 11.532  46.405  60.336  1.00 93.05  ? 31  ARG   F NE    1 
ATOM   11522 C  CZ    . ARG   E 4  31  ? 12.160  45.483  59.621  1.00 98.24  ? 31  ARG   F CZ    1 
ATOM   11523 N  NH1   . ARG   E 4  31  ? 11.700  45.089  58.443  1.00 105.08 ? 31  ARG   F NH1   1 
ATOM   11524 N  NH2   . ARG   E 4  31  ? 13.268  44.930  60.105  1.00 95.40  ? 31  ARG   F NH2   1 
ATOM   11525 N  N     . LYS   E 4  32  ? 10.864  49.619  64.449  1.00 60.38  ? 32  LYS   F N     1 
ATOM   11526 C  CA    . LYS   E 4  32  ? 11.180  50.472  65.597  1.00 61.60  ? 32  LYS   F CA    1 
ATOM   11527 C  C     . LYS   E 4  32  ? 12.027  51.679  65.196  1.00 57.43  ? 32  LYS   F C     1 
ATOM   11528 O  O     . LYS   E 4  32  ? 11.868  52.774  65.755  1.00 53.05  ? 32  LYS   F O     1 
ATOM   11529 C  CB    . LYS   E 4  32  ? 11.887  49.654  66.689  1.00 60.08  ? 32  LYS   F CB    1 
ATOM   11530 C  CG    . LYS   E 4  32  ? 13.355  49.325  66.393  1.00 65.32  ? 32  LYS   F CG    1 
ATOM   11531 C  CD    . LYS   E 4  32  ? 13.914  48.274  67.353  1.00 75.72  ? 32  LYS   F CD    1 
ATOM   11532 C  CE    . LYS   E 4  32  ? 13.675  48.634  68.820  1.00 74.44  ? 32  LYS   F CE    1 
ATOM   11533 N  NZ    . LYS   E 4  32  ? 14.155  47.564  69.758  1.00 64.43  ? 32  LYS   F NZ    1 
ATOM   11534 N  N     . ASP   E 4  33  ? 12.925  51.507  64.226  1.00 52.37  ? 33  ASP   F N     1 
ATOM   11535 C  CA    . ASP   E 4  33  ? 13.839  52.566  63.818  1.00 53.83  ? 33  ASP   F CA    1 
ATOM   11536 C  C     . ASP   E 4  33  ? 13.356  53.332  62.593  1.00 53.95  ? 33  ASP   F C     1 
ATOM   11537 O  O     . ASP   E 4  33  ? 14.131  54.082  61.985  1.00 48.21  ? 33  ASP   F O     1 
ATOM   11538 C  CB    . ASP   E 4  33  ? 15.229  51.985  63.577  1.00 66.43  ? 33  ASP   F CB    1 
ATOM   11539 C  CG    . ASP   E 4  33  ? 16.088  52.035  64.823  1.00 76.99  ? 33  ASP   F CG    1 
ATOM   11540 O  OD1   . ASP   E 4  33  ? 16.587  53.149  65.126  1.00 63.16  ? 33  ASP   F OD1   1 
ATOM   11541 O  OD2   . ASP   E 4  33  ? 16.229  50.983  65.508  1.00 67.15  ? 33  ASP   F OD2   1 
ATOM   11542 N  N     . ASN   E 4  34  ? 12.098  53.168  62.223  1.00 56.92  ? 34  ASN   F N     1 
ATOM   11543 C  CA    . ASN   E 4  34  ? 11.521  53.993  61.180  1.00 51.04  ? 34  ASN   F CA    1 
ATOM   11544 C  C     . ASN   E 4  34  ? 11.084  55.326  61.778  1.00 46.92  ? 34  ASN   F C     1 
ATOM   11545 O  O     . ASN   E 4  34  ? 10.240  55.343  62.683  1.00 47.06  ? 34  ASN   F O     1 
ATOM   11546 C  CB    . ASN   E 4  34  ? 10.350  53.284  60.531  1.00 39.50  ? 34  ASN   F CB    1 
ATOM   11547 C  CG    . ASN   E 4  34  ? 9.534   54.209  59.674  1.00 42.10  ? 34  ASN   F CG    1 
ATOM   11548 O  OD1   . ASN   E 4  34  ? 10.007  55.268  59.251  1.00 59.32  ? 34  ASN   F OD1   1 
ATOM   11549 N  ND2   . ASN   E 4  34  ? 8.301   53.830  59.412  1.00 39.77  ? 34  ASN   F ND2   1 
ATOM   11550 N  N     . PRO   E 4  35  ? 11.607  56.455  61.297  1.00 48.37  ? 35  PRO   F N     1 
ATOM   11551 C  CA    . PRO   E 4  35  ? 11.371  57.730  61.987  1.00 37.27  ? 35  PRO   F CA    1 
ATOM   11552 C  C     . PRO   E 4  35  ? 9.953   58.249  61.858  1.00 42.59  ? 35  PRO   F C     1 
ATOM   11553 O  O     . PRO   E 4  35  ? 9.573   59.153  62.607  1.00 45.04  ? 35  PRO   F O     1 
ATOM   11554 C  CB    . PRO   E 4  35  ? 12.354  58.671  61.292  1.00 25.25  ? 35  PRO   F CB    1 
ATOM   11555 C  CG    . PRO   E 4  35  ? 12.409  58.145  59.916  1.00 40.04  ? 35  PRO   F CG    1 
ATOM   11556 C  CD    . PRO   E 4  35  ? 12.353  56.651  60.043  1.00 44.07  ? 35  PRO   F CD    1 
ATOM   11557 N  N     . ARG   E 4  36  ? 9.168   57.741  60.916  1.00 45.29  ? 36  ARG   F N     1 
ATOM   11558 C  CA    . ARG   E 4  36  ? 7.915   58.390  60.554  1.00 40.97  ? 36  ARG   F CA    1 
ATOM   11559 C  C     . ARG   E 4  36  ? 6.755   57.798  61.348  1.00 45.64  ? 36  ARG   F C     1 
ATOM   11560 O  O     . ARG   E 4  36  ? 5.823   57.227  60.788  1.00 53.15  ? 36  ARG   F O     1 
ATOM   11561 C  CB    . ARG   E 4  36  ? 7.688   58.270  59.053  1.00 40.30  ? 36  ARG   F CB    1 
ATOM   11562 C  CG    . ARG   E 4  36  ? 8.867   58.785  58.295  1.00 42.43  ? 36  ARG   F CG    1 
ATOM   11563 C  CD    . ARG   E 4  36  ? 8.678   58.821  56.804  1.00 51.52  ? 36  ARG   F CD    1 
ATOM   11564 N  NE    . ARG   E 4  36  ? 9.696   59.691  56.231  1.00 42.77  ? 36  ARG   F NE    1 
ATOM   11565 C  CZ    . ARG   E 4  36  ? 9.504   60.975  55.954  1.00 48.51  ? 36  ARG   F CZ    1 
ATOM   11566 N  NH1   . ARG   E 4  36  ? 8.306   61.530  56.047  1.00 41.88  ? 36  ARG   F NH1   1 
ATOM   11567 N  NH2   . ARG   E 4  36  ? 10.540  61.720  55.572  1.00 50.78  ? 36  ARG   F NH2   1 
ATOM   11568 N  N     . PHE   E 4  37  ? 6.833   57.946  62.674  1.00 39.82  ? 37  PHE   F N     1 
ATOM   11569 C  CA    . PHE   E 4  37  ? 5.779   57.521  63.585  1.00 44.43  ? 37  PHE   F CA    1 
ATOM   11570 C  C     . PHE   E 4  37  ? 4.980   58.717  64.107  1.00 47.95  ? 37  PHE   F C     1 
ATOM   11571 O  O     . PHE   E 4  37  ? 5.403   59.874  64.014  1.00 39.37  ? 37  PHE   F O     1 
ATOM   11572 C  CB    . PHE   E 4  37  ? 6.364   56.747  64.768  1.00 41.69  ? 37  PHE   F CB    1 
ATOM   11573 C  CG    . PHE   E 4  37  ? 7.395   57.517  65.543  1.00 45.45  ? 37  PHE   F CG    1 
ATOM   11574 C  CD1   . PHE   E 4  37  ? 7.014   58.395  66.554  1.00 43.02  ? 37  PHE   F CD1   1 
ATOM   11575 C  CD2   . PHE   E 4  37  ? 8.752   57.364  65.264  1.00 48.04  ? 37  PHE   F CD2   1 
ATOM   11576 C  CE1   . PHE   E 4  37  ? 7.965   59.111  67.271  1.00 38.89  ? 37  PHE   F CE1   1 
ATOM   11577 C  CE2   . PHE   E 4  37  ? 9.716   58.072  65.984  1.00 36.95  ? 37  PHE   F CE2   1 
ATOM   11578 C  CZ    . PHE   E 4  37  ? 9.314   58.947  66.989  1.00 42.57  ? 37  PHE   F CZ    1 
ATOM   11579 N  N     . ASN   E 4  38  ? 3.803   58.417  64.661  1.00 43.99  ? 38  ASN   F N     1 
ATOM   11580 C  CA    . ASN   E 4  38  ? 3.093   59.370  65.506  1.00 41.95  ? 38  ASN   F CA    1 
ATOM   11581 C  C     . ASN   E 4  38  ? 3.306   59.105  66.984  1.00 43.87  ? 38  ASN   F C     1 
ATOM   11582 O  O     . ASN   E 4  38  ? 3.323   60.043  67.786  1.00 51.19  ? 38  ASN   F O     1 
ATOM   11583 C  CB    . ASN   E 4  38  ? 1.587   59.333  65.236  1.00 43.75  ? 38  ASN   F CB    1 
ATOM   11584 C  CG    . ASN   E 4  38  ? 1.236   59.728  63.836  1.00 47.12  ? 38  ASN   F CG    1 
ATOM   11585 O  OD1   . ASN   E 4  38  ? 0.724   58.911  63.066  1.00 56.11  ? 38  ASN   F OD1   1 
ATOM   11586 N  ND2   . ASN   E 4  38  ? 1.498   60.985  63.488  1.00 38.43  ? 38  ASN   F ND2   1 
ATOM   11587 N  N     . LEU   E 4  39  ? 3.470   57.847  67.355  1.00 45.01  ? 39  LEU   F N     1 
ATOM   11588 C  CA    . LEU   E 4  39  ? 3.513   57.436  68.743  1.00 36.42  ? 39  LEU   F CA    1 
ATOM   11589 C  C     . LEU   E 4  39  ? 4.775   56.624  68.952  1.00 40.86  ? 39  LEU   F C     1 
ATOM   11590 O  O     . LEU   E 4  39  ? 4.989   55.620  68.267  1.00 45.49  ? 39  LEU   F O     1 
ATOM   11591 C  CB    . LEU   E 4  39  ? 2.270   56.618  69.091  1.00 35.11  ? 39  LEU   F CB    1 
ATOM   11592 C  CG    . LEU   E 4  39  ? 2.226   55.894  70.435  1.00 38.95  ? 39  LEU   F CG    1 
ATOM   11593 C  CD1   . LEU   E 4  39  ? 2.660   56.803  71.566  1.00 38.16  ? 39  LEU   F CD1   1 
ATOM   11594 C  CD2   . LEU   E 4  39  ? 0.812   55.407  70.671  1.00 43.92  ? 39  LEU   F CD2   1 
ATOM   11595 N  N     . MET   E 4  40  ? 5.622   57.068  69.864  1.00 36.31  ? 40  MET   F N     1 
ATOM   11596 C  CA    . MET   E 4  40  ? 6.716   56.243  70.352  1.00 36.20  ? 40  MET   F CA    1 
ATOM   11597 C  C     . MET   E 4  40  ? 6.327   55.747  71.734  1.00 43.13  ? 40  MET   F C     1 
ATOM   11598 O  O     . MET   E 4  40  ? 6.191   56.543  72.671  1.00 43.46  ? 40  MET   F O     1 
ATOM   11599 C  CB    . MET   E 4  40  ? 8.039   57.000  70.399  1.00 36.40  ? 40  MET   F CB    1 
ATOM   11600 C  CG    . MET   E 4  40  ? 9.139   56.236  71.112  1.00 35.50  ? 40  MET   F CG    1 
ATOM   11601 S  SD    . MET   E 4  40  ? 10.715  57.100  71.040  1.00 40.87  ? 40  MET   F SD    1 
ATOM   11602 C  CE    . MET   E 4  40  ? 10.824  57.367  69.289  1.00 35.17  ? 40  MET   F CE    1 
ATOM   11603 N  N     . LEU   E 4  41  ? 6.086   54.443  71.834  1.00 40.08  ? 41  LEU   F N     1 
ATOM   11604 C  CA    . LEU   E 4  41  ? 6.151   53.717  73.096  1.00 41.99  ? 41  LEU   F CA    1 
ATOM   11605 C  C     . LEU   E 4  41  ? 7.627   53.441  73.330  1.00 43.99  ? 41  LEU   F C     1 
ATOM   11606 O  O     . LEU   E 4  41  ? 8.190   52.471  72.827  1.00 54.12  ? 41  LEU   F O     1 
ATOM   11607 C  CB    . LEU   E 4  41  ? 5.323   52.445  73.026  1.00 36.13  ? 41  LEU   F CB    1 
ATOM   11608 C  CG    . LEU   E 4  41  ? 3.992   52.785  72.379  1.00 38.60  ? 41  LEU   F CG    1 
ATOM   11609 C  CD1   . LEU   E 4  41  ? 3.138   51.543  72.191  1.00 45.44  ? 41  LEU   F CD1   1 
ATOM   11610 C  CD2   . LEU   E 4  41  ? 3.289   53.822  73.231  1.00 39.23  ? 41  LEU   F CD2   1 
ATOM   11611 N  N     . GLY   E 4  42  ? 8.265   54.322  74.082  1.00 42.21  ? 42  GLY   F N     1 
ATOM   11612 C  CA    . GLY   E 4  42  ? 9.708   54.413  74.079  1.00 44.24  ? 42  GLY   F CA    1 
ATOM   11613 C  C     . GLY   E 4  42  ? 10.388  53.445  75.016  1.00 47.33  ? 42  GLY   F C     1 
ATOM   11614 O  O     . GLY   E 4  42  ? 9.765   52.777  75.838  1.00 48.93  ? 42  GLY   F O     1 
ATOM   11615 N  N     . GLU   E 4  43  ? 11.707  53.374  74.869  1.00 50.73  ? 43  GLU   F N     1 
ATOM   11616 C  CA    . GLU   E 4  43  ? 12.502  52.509  75.714  1.00 47.66  ? 43  GLU   F CA    1 
ATOM   11617 C  C     . GLU   E 4  43  ? 12.462  53.008  77.156  1.00 52.08  ? 43  GLU   F C     1 
ATOM   11618 O  O     . GLU   E 4  43  ? 11.885  54.052  77.470  1.00 51.11  ? 43  GLU   F O     1 
ATOM   11619 C  CB    . GLU   E 4  43  ? 13.934  52.430  75.189  1.00 45.44  ? 43  GLU   F CB    1 
ATOM   11620 C  CG    . GLU   E 4  43  ? 14.536  53.763  74.757  1.00 46.47  ? 43  GLU   F CG    1 
ATOM   11621 C  CD    . GLU   E 4  43  ? 14.736  53.886  73.250  1.00 48.27  ? 43  GLU   F CD    1 
ATOM   11622 O  OE1   . GLU   E 4  43  ? 13.713  53.896  72.528  1.00 43.61  ? 43  GLU   F OE1   1 
ATOM   11623 O  OE2   . GLU   E 4  43  ? 15.915  53.984  72.799  1.00 38.88  ? 43  GLU   F OE2   1 
ATOM   11624 N  N     . ARG   E 4  44  ? 13.064  52.226  78.051  1.00 62.65  ? 44  ARG   F N     1 
ATOM   11625 C  CA    . ARG   E 4  44  ? 13.141  52.610  79.454  1.00 55.54  ? 44  ARG   F CA    1 
ATOM   11626 C  C     . ARG   E 4  44  ? 14.400  53.395  79.763  1.00 52.75  ? 44  ARG   F C     1 
ATOM   11627 O  O     . ARG   E 4  44  ? 14.463  54.080  80.790  1.00 64.53  ? 44  ARG   F O     1 
ATOM   11628 C  CB    . ARG   E 4  44  ? 13.088  51.370  80.362  1.00 58.93  ? 44  ARG   F CB    1 
ATOM   11629 C  CG    . ARG   E 4  44  ? 11.703  50.749  80.540  1.00 62.93  ? 44  ARG   F CG    1 
ATOM   11630 C  CD    . ARG   E 4  44  ? 11.410  50.447  82.013  1.00 78.09  ? 44  ARG   F CD    1 
ATOM   11631 N  NE    . ARG   E 4  44  ? 12.113  49.272  82.525  1.00 100.52 ? 44  ARG   F NE    1 
ATOM   11632 C  CZ    . ARG   E 4  44  ? 12.199  48.952  83.812  1.00 103.79 ? 44  ARG   F CZ    1 
ATOM   11633 N  NH1   . ARG   E 4  44  ? 11.687  49.730  84.753  1.00 100.40 ? 44  ARG   F NH1   1 
ATOM   11634 N  NH2   . ARG   E 4  44  ? 12.815  47.824  84.165  1.00 93.62  ? 44  ARG   F NH2   1 
ATOM   11635 N  N     . ASN   E 4  45  ? 15.395  53.330  78.893  1.00 57.58  ? 45  ASN   F N     1 
ATOM   11636 C  CA    . ASN   E 4  45  ? 16.719  53.824  79.226  1.00 59.72  ? 45  ASN   F CA    1 
ATOM   11637 C  C     . ASN   E 4  45  ? 17.254  54.634  78.059  1.00 51.08  ? 45  ASN   F C     1 
ATOM   11638 O  O     . ASN   E 4  45  ? 17.391  54.108  76.951  1.00 47.53  ? 45  ASN   F O     1 
ATOM   11639 C  CB    . ASN   E 4  45  ? 17.645  52.652  79.557  1.00 66.93  ? 45  ASN   F CB    1 
ATOM   11640 C  CG    . ASN   E 4  45  ? 18.490  52.913  80.771  1.00 75.51  ? 45  ASN   F CG    1 
ATOM   11641 O  OD1   . ASN   E 4  45  ? 19.719  52.807  80.719  1.00 78.58  ? 45  ASN   F OD1   1 
ATOM   11642 N  ND2   . ASN   E 4  45  ? 17.842  53.275  81.877  1.00 69.84  ? 45  ASN   F ND2   1 
ATOM   11643 N  N     . ARG   E 4  46  ? 17.561  55.907  78.310  1.00 59.26  ? 46  ARG   F N     1 
ATOM   11644 C  CA    . ARG   E 4  46  ? 18.146  56.791  77.299  1.00 49.18  ? 46  ARG   F CA    1 
ATOM   11645 C  C     . ARG   E 4  46  ? 17.233  56.904  76.078  1.00 52.36  ? 46  ARG   F C     1 
ATOM   11646 O  O     . ARG   E 4  46  ? 17.675  56.837  74.928  1.00 45.68  ? 46  ARG   F O     1 
ATOM   11647 C  CB    . ARG   E 4  46  ? 19.548  56.323  76.904  1.00 54.60  ? 46  ARG   F CB    1 
ATOM   11648 C  CG    . ARG   E 4  46  ? 20.181  55.384  77.924  1.00 69.92  ? 46  ARG   F CG    1 
ATOM   11649 C  CD    . ARG   E 4  46  ? 21.668  55.222  77.719  1.00 71.35  ? 46  ARG   F CD    1 
ATOM   11650 N  NE    . ARG   E 4  46  ? 22.413  56.404  78.134  1.00 77.63  ? 46  ARG   F NE    1 
ATOM   11651 C  CZ    . ARG   E 4  46  ? 22.690  57.435  77.347  1.00 77.80  ? 46  ARG   F CZ    1 
ATOM   11652 N  NH1   . ARG   E 4  46  ? 22.259  57.486  76.095  1.00 74.74  ? 46  ARG   F NH1   1 
ATOM   11653 N  NH2   . ARG   E 4  46  ? 23.426  58.436  77.827  1.00 74.50  ? 46  ARG   F NH2   1 
ATOM   11654 N  N     . LEU   E 4  47  ? 15.941  57.064  76.339  1.00 51.00  ? 47  LEU   F N     1 
ATOM   11655 C  CA    . LEU   E 4  47  ? 14.991  57.322  75.273  1.00 41.63  ? 47  LEU   F CA    1 
ATOM   11656 C  C     . LEU   E 4  47  ? 15.431  58.564  74.508  1.00 36.26  ? 47  LEU   F C     1 
ATOM   11657 O  O     . LEU   E 4  47  ? 15.721  59.596  75.128  1.00 45.10  ? 47  LEU   F O     1 
ATOM   11658 C  CB    . LEU   E 4  47  ? 13.603  57.505  75.872  1.00 36.31  ? 47  LEU   F CB    1 
ATOM   11659 C  CG    . LEU   E 4  47  ? 12.365  57.649  75.016  1.00 38.83  ? 47  LEU   F CG    1 
ATOM   11660 C  CD1   . LEU   E 4  47  ? 11.167  57.510  75.942  1.00 37.93  ? 47  LEU   F CD1   1 
ATOM   11661 C  CD2   . LEU   E 4  47  ? 12.358  58.995  74.293  1.00 34.27  ? 47  LEU   F CD2   1 
ATOM   11662 N  N     . PRO   E 4  48  ? 15.513  58.512  73.200  1.00 37.28  ? 48  PRO   F N     1 
ATOM   11663 C  CA    . PRO   E 4  48  ? 16.157  59.609  72.444  1.00 40.78  ? 48  PRO   F CA    1 
ATOM   11664 C  C     . PRO   E 4  48  ? 15.270  60.849  72.293  1.00 42.40  ? 48  PRO   F C     1 
ATOM   11665 O  O     . PRO   E 4  48  ? 14.930  61.291  71.180  1.00 48.24  ? 48  PRO   F O     1 
ATOM   11666 C  CB    . PRO   E 4  48  ? 16.482  58.930  71.104  1.00 36.84  ? 48  PRO   F CB    1 
ATOM   11667 C  CG    . PRO   E 4  48  ? 15.455  57.844  70.972  1.00 42.37  ? 48  PRO   F CG    1 
ATOM   11668 C  CD    . PRO   E 4  48  ? 15.122  57.374  72.349  1.00 33.62  ? 48  PRO   F CD    1 
ATOM   11669 N  N     . PHE   E 4  49  ? 14.927  61.462  73.430  1.00 38.57  ? 49  PHE   F N     1 
ATOM   11670 C  CA    . PHE   E 4  49  ? 13.966  62.565  73.445  1.00 33.33  ? 49  PHE   F CA    1 
ATOM   11671 C  C     . PHE   E 4  49  ? 14.312  63.634  72.418  1.00 42.07  ? 49  PHE   F C     1 
ATOM   11672 O  O     . PHE   E 4  49  ? 13.440  64.121  71.691  1.00 41.72  ? 49  PHE   F O     1 
ATOM   11673 C  CB    . PHE   E 4  49  ? 13.896  63.172  74.847  1.00 36.90  ? 49  PHE   F CB    1 
ATOM   11674 C  CG    . PHE   E 4  49  ? 12.995  62.423  75.779  1.00 35.89  ? 49  PHE   F CG    1 
ATOM   11675 C  CD1   . PHE   E 4  49  ? 11.616  62.542  75.670  1.00 35.54  ? 49  PHE   F CD1   1 
ATOM   11676 C  CD2   . PHE   E 4  49  ? 13.518  61.583  76.740  1.00 29.78  ? 49  PHE   F CD2   1 
ATOM   11677 C  CE1   . PHE   E 4  49  ? 10.780  61.838  76.506  1.00 31.75  ? 49  PHE   F CE1   1 
ATOM   11678 C  CE2   . PHE   E 4  49  ? 12.688  60.870  77.583  1.00 33.76  ? 49  PHE   F CE2   1 
ATOM   11679 C  CZ    . PHE   E 4  49  ? 11.318  61.005  77.475  1.00 33.31  ? 49  PHE   F CZ    1 
ATOM   11680 N  N     . GLY   E 4  50  ? 15.587  64.012  72.347  1.00 42.92  ? 50  GLY   F N     1 
ATOM   11681 C  CA    . GLY   E 4  50  ? 16.015  65.041  71.422  1.00 33.93  ? 50  GLY   F CA    1 
ATOM   11682 C  C     . GLY   E 4  50  ? 15.766  64.722  69.962  1.00 34.25  ? 50  GLY   F C     1 
ATOM   11683 O  O     . GLY   E 4  50  ? 15.918  65.618  69.118  1.00 33.09  ? 50  GLY   F O     1 
ATOM   11684 N  N     . ARG   E 4  51  ? 15.394  63.486  69.639  1.00 29.94  ? 51  ARG   F N     1 
ATOM   11685 C  CA    . ARG   E 4  51  ? 15.072  63.168  68.254  1.00 43.50  ? 51  ARG   F CA    1 
ATOM   11686 C  C     . ARG   E 4  51  ? 13.586  63.317  67.933  1.00 35.76  ? 51  ARG   F C     1 
ATOM   11687 O  O     . ARG   E 4  51  ? 13.210  63.174  66.766  1.00 33.63  ? 51  ARG   F O     1 
ATOM   11688 C  CB    . ARG   E 4  51  ? 15.546  61.738  67.897  1.00 35.64  ? 51  ARG   F CB    1 
ATOM   11689 C  CG    . ARG   E 4  51  ? 17.087  61.527  67.957  1.00 42.94  ? 51  ARG   F CG    1 
ATOM   11690 C  CD    . ARG   E 4  51  ? 17.623  60.437  66.981  1.00 43.02  ? 51  ARG   F CD    1 
ATOM   11691 N  NE    . ARG   E 4  51  ? 16.809  59.221  66.959  1.00 45.36  ? 51  ARG   F NE    1 
ATOM   11692 C  CZ    . ARG   E 4  51  ? 17.117  58.080  67.565  1.00 36.61  ? 51  ARG   F CZ    1 
ATOM   11693 N  NH1   . ARG   E 4  51  ? 18.275  57.911  68.184  1.00 30.09  ? 51  ARG   F NH1   1 
ATOM   11694 N  NH2   . ARG   E 4  51  ? 16.237  57.079  67.548  1.00 47.94  ? 51  ARG   F NH2   1 
ATOM   11695 N  N     . LEU   E 4  52  ? 12.742  63.615  68.919  1.00 29.80  ? 52  LEU   F N     1 
ATOM   11696 C  CA    . LEU   E 4  52  ? 11.298  63.706  68.722  1.00 31.12  ? 52  LEU   F CA    1 
ATOM   11697 C  C     . LEU   E 4  52  ? 10.893  65.129  68.333  1.00 30.63  ? 52  LEU   F C     1 
ATOM   11698 O  O     . LEU   E 4  52  ? 11.558  66.108  68.677  1.00 33.86  ? 52  LEU   F O     1 
ATOM   11699 C  CB    . LEU   E 4  52  ? 10.536  63.269  69.988  1.00 27.03  ? 52  LEU   F CB    1 
ATOM   11700 C  CG    . LEU   E 4  52  ? 10.839  61.851  70.492  1.00 38.33  ? 52  LEU   F CG    1 
ATOM   11701 C  CD1   . LEU   E 4  52  ? 10.252  61.554  71.858  1.00 29.10  ? 52  LEU   F CD1   1 
ATOM   11702 C  CD2   . LEU   E 4  52  ? 10.364  60.831  69.482  1.00 37.97  ? 52  LEU   F CD2   1 
ATOM   11703 N  N     . GLY   E 4  53  ? 9.793   65.233  67.598  1.00 26.31  ? 53  GLY   F N     1 
ATOM   11704 C  CA    . GLY   E 4  53  ? 9.311   66.538  67.236  1.00 28.19  ? 53  GLY   F CA    1 
ATOM   11705 C  C     . GLY   E 4  53  ? 10.089  67.245  66.154  1.00 29.75  ? 53  GLY   F C     1 
ATOM   11706 O  O     . GLY   E 4  53  ? 9.985   68.465  66.049  1.00 31.93  ? 53  GLY   F O     1 
ATOM   11707 N  N     . HIS   E 4  54  ? 10.862  66.526  65.336  1.00 33.65  ? 54  HIS   F N     1 
ATOM   11708 C  CA    . HIS   E 4  54  ? 11.488  67.126  64.161  1.00 39.83  ? 54  HIS   F CA    1 
ATOM   11709 C  C     . HIS   E 4  54  ? 11.132  66.393  62.862  1.00 47.30  ? 54  HIS   F C     1 
ATOM   11710 O  O     . HIS   E 4  54  ? 11.964  66.307  61.951  1.00 53.71  ? 54  HIS   F O     1 
ATOM   11711 C  CB    . HIS   E 4  54  ? 13.006  67.188  64.312  1.00 28.78  ? 54  HIS   F CB    1 
ATOM   11712 C  CG    . HIS   E 4  54  ? 13.468  67.786  65.604  1.00 35.15  ? 54  HIS   F CG    1 
ATOM   11713 N  ND1   . HIS   E 4  54  ? 13.843  69.106  65.722  1.00 34.52  ? 54  HIS   F ND1   1 
ATOM   11714 C  CD2   . HIS   E 4  54  ? 13.643  67.237  66.828  1.00 36.38  ? 54  HIS   F CD2   1 
ATOM   11715 C  CE1   . HIS   E 4  54  ? 14.211  69.348  66.968  1.00 32.23  ? 54  HIS   F CE1   1 
ATOM   11716 N  NE2   . HIS   E 4  54  ? 14.105  68.229  67.659  1.00 33.66  ? 54  HIS   F NE2   1 
ATOM   11717 N  N     . GLU   E 4  55  ? 9.915   65.863  62.748  1.00 34.11  ? 55  GLU   F N     1 
ATOM   11718 C  CA    . GLU   E 4  55  ? 9.455   65.219  61.513  1.00 38.98  ? 55  GLU   F CA    1 
ATOM   11719 C  C     . GLU   E 4  55  ? 8.269   65.990  60.960  1.00 36.71  ? 55  GLU   F C     1 
ATOM   11720 O  O     . GLU   E 4  55  ? 7.139   65.822  61.449  1.00 46.82  ? 55  GLU   F O     1 
ATOM   11721 C  CB    . GLU   E 4  55  ? 9.058   63.763  61.761  1.00 31.97  ? 55  GLU   F CB    1 
ATOM   11722 C  CG    . GLU   E 4  55  ? 10.188  62.792  61.775  1.00 26.62  ? 55  GLU   F CG    1 
ATOM   11723 C  CD    . GLU   E 4  55  ? 10.959  62.780  60.474  1.00 44.33  ? 55  GLU   F CD    1 
ATOM   11724 O  OE1   . GLU   E 4  55  ? 10.635  63.591  59.567  1.00 48.40  ? 55  GLU   F OE1   1 
ATOM   11725 O  OE2   . GLU   E 4  55  ? 11.896  61.952  60.357  1.00 49.33  ? 55  GLU   F OE2   1 
ATOM   11726 N  N     . PRO   E 4  56  ? 8.446   66.839  59.959  1.00 38.06  ? 56  PRO   F N     1 
ATOM   11727 C  CA    . PRO   E 4  56  ? 7.290   67.615  59.462  1.00 39.83  ? 56  PRO   F CA    1 
ATOM   11728 C  C     . PRO   E 4  56  ? 6.177   66.720  58.893  1.00 42.18  ? 56  PRO   F C     1 
ATOM   11729 O  O     . PRO   E 4  56  ? 6.389   65.578  58.461  1.00 34.20  ? 56  PRO   F O     1 
ATOM   11730 C  CB    . PRO   E 4  56  ? 7.900   68.545  58.394  1.00 26.92  ? 56  PRO   F CB    1 
ATOM   11731 C  CG    . PRO   E 4  56  ? 9.281   68.003  58.106  1.00 31.43  ? 56  PRO   F CG    1 
ATOM   11732 C  CD    . PRO   E 4  56  ? 9.717   67.197  59.303  1.00 34.10  ? 56  PRO   F CD    1 
ATOM   11733 N  N     . GLY   E 4  57  ? 4.962   67.247  58.917  1.00 30.33  ? 57  GLY   F N     1 
ATOM   11734 C  CA    . GLY   E 4  57  ? 3.807   66.440  58.633  1.00 32.57  ? 57  GLY   F CA    1 
ATOM   11735 C  C     . GLY   E 4  57  ? 3.388   65.514  59.752  1.00 35.61  ? 57  GLY   F C     1 
ATOM   11736 O  O     . GLY   E 4  57  ? 2.299   64.933  59.680  1.00 34.28  ? 57  GLY   F O     1 
ATOM   11737 N  N     . LEU   E 4  58  ? 4.185   65.383  60.803  1.00 38.02  ? 58  LEU   F N     1 
ATOM   11738 C  CA    . LEU   E 4  58  ? 3.913   64.424  61.865  1.00 44.94  ? 58  LEU   F CA    1 
ATOM   11739 C  C     . LEU   E 4  58  ? 3.752   65.140  63.196  1.00 43.45  ? 58  LEU   F C     1 
ATOM   11740 O  O     . LEU   E 4  58  ? 4.646   65.881  63.620  1.00 50.86  ? 58  LEU   F O     1 
ATOM   11741 C  CB    . LEU   E 4  58  ? 5.029   63.386  61.956  1.00 39.31  ? 58  LEU   F CB    1 
ATOM   11742 C  CG    . LEU   E 4  58  ? 5.070   62.452  60.765  1.00 33.73  ? 58  LEU   F CG    1 
ATOM   11743 C  CD1   . LEU   E 4  58  ? 6.043   61.325  61.023  1.00 37.89  ? 58  LEU   F CD1   1 
ATOM   11744 C  CD2   . LEU   E 4  58  ? 3.667   61.933  60.561  1.00 43.84  ? 58  LEU   F CD2   1 
ATOM   11745 N  N     . VAL   E 4  59  ? 2.605   64.941  63.836  1.00 41.27  ? 59  VAL   F N     1 
ATOM   11746 C  CA    . VAL   E 4  59  ? 2.486   65.194  65.262  1.00 27.75  ? 59  VAL   F CA    1 
ATOM   11747 C  C     . VAL   E 4  59  ? 3.037   63.977  65.973  1.00 38.72  ? 59  VAL   F C     1 
ATOM   11748 O  O     . VAL   E 4  59  ? 2.603   62.852  65.704  1.00 47.68  ? 59  VAL   F O     1 
ATOM   11749 C  CB    . VAL   E 4  59  ? 1.022   65.445  65.660  1.00 31.92  ? 59  VAL   F CB    1 
ATOM   11750 C  CG1   . VAL   E 4  59  ? 0.927   65.673  67.166  1.00 24.82  ? 59  VAL   F CG1   1 
ATOM   11751 C  CG2   . VAL   E 4  59  ? 0.411   66.597  64.860  1.00 18.97  ? 59  VAL   F CG2   1 
ATOM   11752 N  N     . GLN   E 4  60  ? 4.004   64.181  66.857  1.00 36.46  ? 60  GLN   F N     1 
ATOM   11753 C  CA    . GLN   E 4  60  ? 4.623   63.065  67.553  1.00 32.45  ? 60  GLN   F CA    1 
ATOM   11754 C  C     . GLN   E 4  60  ? 4.328   63.112  69.043  1.00 31.68  ? 60  GLN   F C     1 
ATOM   11755 O  O     . GLN   E 4  60  ? 4.352   64.179  69.669  1.00 38.61  ? 60  GLN   F O     1 
ATOM   11756 C  CB    . GLN   E 4  60  ? 6.119   63.042  67.301  1.00 24.46  ? 60  GLN   F CB    1 
ATOM   11757 C  CG    . GLN   E 4  60  ? 6.418   62.729  65.862  1.00 29.06  ? 60  GLN   F CG    1 
ATOM   11758 C  CD    . GLN   E 4  60  ? 7.886   62.481  65.644  1.00 42.27  ? 60  GLN   F CD    1 
ATOM   11759 O  OE1   . GLN   E 4  60  ? 8.733   63.265  66.097  1.00 39.99  ? 60  GLN   F OE1   1 
ATOM   11760 N  NE2   . GLN   E 4  60  ? 8.210   61.373  64.976  1.00 38.86  ? 60  GLN   F NE2   1 
ATOM   11761 N  N     . LEU   E 4  61  ? 4.052   61.944  69.597  1.00 30.17  ? 61  LEU   F N     1 
ATOM   11762 C  CA    . LEU   E 4  61  ? 3.651   61.787  70.983  1.00 32.05  ? 61  LEU   F CA    1 
ATOM   11763 C  C     . LEU   E 4  61  ? 4.409   60.591  71.525  1.00 32.87  ? 61  LEU   F C     1 
ATOM   11764 O  O     . LEU   E 4  61  ? 4.557   59.589  70.823  1.00 46.91  ? 61  LEU   F O     1 
ATOM   11765 C  CB    . LEU   E 4  61  ? 2.130   61.583  71.094  1.00 30.90  ? 61  LEU   F CB    1 
ATOM   11766 C  CG    . LEU   E 4  61  ? 1.491   61.338  72.460  1.00 41.26  ? 61  LEU   F CG    1 
ATOM   11767 C  CD1   . LEU   E 4  61  ? 1.670   62.562  73.397  1.00 43.73  ? 61  LEU   F CD1   1 
ATOM   11768 C  CD2   . LEU   E 4  61  ? 0.021   60.974  72.298  1.00 29.98  ? 61  LEU   F CD2   1 
ATOM   11769 N  N     . VAL   E 4  62  ? 4.921   60.705  72.748  1.00 26.79  ? 62  VAL   F N     1 
ATOM   11770 C  CA    . VAL   E 4  62  ? 5.748   59.670  73.347  1.00 27.64  ? 62  VAL   F CA    1 
ATOM   11771 C  C     . VAL   E 4  62  ? 5.204   59.398  74.742  1.00 37.28  ? 62  VAL   F C     1 
ATOM   11772 O  O     . VAL   E 4  62  ? 4.531   60.238  75.344  1.00 32.83  ? 62  VAL   F O     1 
ATOM   11773 C  CB    . VAL   E 4  62  ? 7.243   60.076  73.383  1.00 32.38  ? 62  VAL   F CB    1 
ATOM   11774 C  CG1   . VAL   E 4  62  ? 7.443   61.385  74.166  1.00 26.75  ? 62  VAL   F CG1   1 
ATOM   11775 C  CG2   . VAL   E 4  62  ? 8.114   58.943  73.910  1.00 29.70  ? 62  VAL   F CG2   1 
ATOM   11776 N  N     . ASN   E 4  63  ? 5.470   58.189  75.243  1.00 41.73  ? 63  ASN   F N     1 
ATOM   11777 C  CA    . ASN   E 4  63  ? 4.834   57.702  76.463  1.00 41.14  ? 63  ASN   F CA    1 
ATOM   11778 C  C     . ASN   E 4  63  ? 5.724   57.873  77.690  1.00 40.79  ? 63  ASN   F C     1 
ATOM   11779 O  O     . ASN   E 4  63  ? 5.613   57.106  78.657  1.00 46.14  ? 63  ASN   F O     1 
ATOM   11780 C  CB    . ASN   E 4  63  ? 4.404   56.239  76.307  1.00 40.58  ? 63  ASN   F CB    1 
ATOM   11781 C  CG    . ASN   E 4  63  ? 5.583   55.280  76.283  1.00 46.95  ? 63  ASN   F CG    1 
ATOM   11782 O  OD1   . ASN   E 4  63  ? 6.697   55.665  75.924  1.00 38.16  ? 63  ASN   F OD1   1 
ATOM   11783 N  ND2   . ASN   E 4  63  ? 5.343   54.023  76.664  1.00 45.73  ? 63  ASN   F ND2   1 
ATOM   11784 N  N     . TYR   E 4  64  ? 6.596   58.874  77.675  1.00 31.76  ? 64  TYR   F N     1 
ATOM   11785 C  CA    . TYR   E 4  64  ? 7.369   59.222  78.852  1.00 36.28  ? 64  TYR   F CA    1 
ATOM   11786 C  C     . TYR   E 4  64  ? 7.560   60.724  78.918  1.00 35.66  ? 64  TYR   F C     1 
ATOM   11787 O  O     . TYR   E 4  64  ? 7.780   61.371  77.895  1.00 33.03  ? 64  TYR   F O     1 
ATOM   11788 C  CB    . TYR   E 4  64  ? 8.734   58.540  78.867  1.00 26.72  ? 64  TYR   F CB    1 
ATOM   11789 C  CG    . TYR   E 4  64  ? 8.644   57.097  79.213  1.00 29.70  ? 64  TYR   F CG    1 
ATOM   11790 C  CD1   . TYR   E 4  64  ? 8.627   56.682  80.540  1.00 40.18  ? 64  TYR   F CD1   1 
ATOM   11791 C  CD2   . TYR   E 4  64  ? 8.571   56.137  78.220  1.00 35.00  ? 64  TYR   F CD2   1 
ATOM   11792 C  CE1   . TYR   E 4  64  ? 8.542   55.327  80.869  1.00 40.58  ? 64  TYR   F CE1   1 
ATOM   11793 C  CE2   . TYR   E 4  64  ? 8.492   54.800  78.523  1.00 38.67  ? 64  TYR   F CE2   1 
ATOM   11794 C  CZ    . TYR   E 4  64  ? 8.475   54.394  79.848  1.00 47.64  ? 64  TYR   F CZ    1 
ATOM   11795 O  OH    . TYR   E 4  64  ? 8.390   53.054  80.137  1.00 60.07  ? 64  TYR   F OH    1 
ATOM   11796 N  N     . TYR   E 4  65  ? 7.477   61.261  80.134  1.00 33.98  ? 65  TYR   F N     1 
ATOM   11797 C  CA    . TYR   E 4  65  ? 7.885   62.630  80.424  1.00 29.53  ? 65  TYR   F CA    1 
ATOM   11798 C  C     . TYR   E 4  65  ? 9.378   62.665  80.721  1.00 25.48  ? 65  TYR   F C     1 
ATOM   11799 O  O     . TYR   E 4  65  ? 9.821   62.235  81.790  1.00 27.53  ? 65  TYR   F O     1 
ATOM   11800 C  CB    . TYR   E 4  65  ? 7.099   63.191  81.602  1.00 33.97  ? 65  TYR   F CB    1 
ATOM   11801 C  CG    . TYR   E 4  65  ? 5.778   63.773  81.223  1.00 31.55  ? 65  TYR   F CG    1 
ATOM   11802 C  CD1   . TYR   E 4  65  ? 5.695   65.064  80.723  1.00 30.70  ? 65  TYR   F CD1   1 
ATOM   11803 C  CD2   . TYR   E 4  65  ? 4.610   63.041  81.366  1.00 32.39  ? 65  TYR   F CD2   1 
ATOM   11804 C  CE1   . TYR   E 4  65  ? 4.487   65.617  80.375  1.00 31.52  ? 65  TYR   F CE1   1 
ATOM   11805 C  CE2   . TYR   E 4  65  ? 3.388   63.584  81.009  1.00 36.33  ? 65  TYR   F CE2   1 
ATOM   11806 C  CZ    . TYR   E 4  65  ? 3.340   64.876  80.516  1.00 29.92  ? 65  TYR   F CZ    1 
ATOM   11807 O  OH    . TYR   E 4  65  ? 2.145   65.432  80.164  1.00 32.50  ? 65  TYR   F OH    1 
ATOM   11808 N  N     . ARG   E 4  66  ? 10.152  63.180  79.780  1.00 29.79  ? 66  ARG   F N     1 
ATOM   11809 C  CA    . ARG   E 4  66  ? 11.525  63.547  80.072  1.00 27.03  ? 66  ARG   F CA    1 
ATOM   11810 C  C     . ARG   E 4  66  ? 11.580  64.339  81.371  1.00 33.60  ? 66  ARG   F C     1 
ATOM   11811 O  O     . ARG   E 4  66  ? 10.703  65.155  81.659  1.00 42.57  ? 66  ARG   F O     1 
ATOM   11812 C  CB    . ARG   E 4  66  ? 12.076  64.370  78.920  1.00 32.35  ? 66  ARG   F CB    1 
ATOM   11813 C  CG    . ARG   E 4  66  ? 13.515  64.725  79.037  1.00 32.68  ? 66  ARG   F CG    1 
ATOM   11814 C  CD    . ARG   E 4  66  ? 13.943  65.211  77.701  1.00 34.33  ? 66  ARG   F CD    1 
ATOM   11815 N  NE    . ARG   E 4  66  ? 15.384  65.317  77.576  1.00 40.60  ? 66  ARG   F NE    1 
ATOM   11816 C  CZ    . ARG   E 4  66  ? 15.968  66.119  76.704  1.00 33.58  ? 66  ARG   F CZ    1 
ATOM   11817 N  NH1   . ARG   E 4  66  ? 15.255  66.880  75.894  1.00 23.85  ? 66  ARG   F NH1   1 
ATOM   11818 N  NH2   . ARG   E 4  66  ? 17.295  66.170  76.656  1.00 31.92  ? 66  ARG   F NH2   1 
ATOM   11819 N  N     . GLY   E 4  67  ? 12.600  64.078  82.173  1.00 31.84  ? 67  GLY   F N     1 
ATOM   11820 C  CA    . GLY   E 4  67  ? 12.684  64.670  83.479  1.00 33.57  ? 67  GLY   F CA    1 
ATOM   11821 C  C     . GLY   E 4  67  ? 11.887  63.979  84.558  1.00 37.97  ? 67  GLY   F C     1 
ATOM   11822 O  O     . GLY   E 4  67  ? 12.205  64.154  85.736  1.00 48.21  ? 67  GLY   F O     1 
ATOM   11823 N  N     . ALA   E 4  68  ? 10.857  63.201  84.208  1.00 38.14  ? 68  ALA   F N     1 
ATOM   11824 C  CA    . ALA   E 4  68  ? 10.036  62.549  85.230  1.00 43.81  ? 68  ALA   F CA    1 
ATOM   11825 C  C     . ALA   E 4  68  ? 10.814  61.537  86.067  1.00 47.12  ? 68  ALA   F C     1 
ATOM   11826 O  O     . ALA   E 4  68  ? 10.285  61.054  87.074  1.00 51.50  ? 68  ALA   F O     1 
ATOM   11827 C  CB    . ALA   E 4  68  ? 8.821   61.858  84.604  1.00 33.22  ? 68  ALA   F CB    1 
ATOM   11828 N  N     . ASP   E 4  69  ? 12.050  61.214  85.694  1.00 45.20  ? 69  ASP   F N     1 
ATOM   11829 C  CA    . ASP   E 4  69  ? 12.854  60.310  86.504  1.00 47.97  ? 69  ASP   F CA    1 
ATOM   11830 C  C     . ASP   E 4  69  ? 13.245  60.927  87.836  1.00 50.45  ? 69  ASP   F C     1 
ATOM   11831 O  O     . ASP   E 4  69  ? 13.590  60.187  88.761  1.00 61.79  ? 69  ASP   F O     1 
ATOM   11832 C  CB    . ASP   E 4  69  ? 14.113  59.904  85.747  1.00 38.76  ? 69  ASP   F CB    1 
ATOM   11833 C  CG    . ASP   E 4  69  ? 14.971  61.103  85.395  1.00 56.38  ? 69  ASP   F CG    1 
ATOM   11834 O  OD1   . ASP   E 4  69  ? 15.699  61.601  86.283  1.00 55.47  ? 69  ASP   F OD1   1 
ATOM   11835 O  OD2   . ASP   E 4  69  ? 14.890  61.573  84.237  1.00 61.57  ? 69  ASP   F OD2   1 
ATOM   11836 N  N     . LYS   E 4  70  ? 13.226  62.259  87.952  1.00 47.09  ? 70  LYS   F N     1 
ATOM   11837 C  CA    . LYS   E 4  70  ? 13.543  62.890  89.233  1.00 50.28  ? 70  LYS   F CA    1 
ATOM   11838 C  C     . LYS   E 4  70  ? 12.549  62.469  90.313  1.00 59.30  ? 70  LYS   F C     1 
ATOM   11839 O  O     . LYS   E 4  70  ? 12.883  62.442  91.506  1.00 60.94  ? 70  LYS   F O     1 
ATOM   11840 C  CB    . LYS   E 4  70  ? 13.542  64.422  89.105  1.00 46.60  ? 70  LYS   F CB    1 
ATOM   11841 C  CG    . LYS   E 4  70  ? 14.087  65.013  87.803  1.00 63.43  ? 70  LYS   F CG    1 
ATOM   11842 C  CD    . LYS   E 4  70  ? 13.568  66.462  87.603  1.00 73.03  ? 70  LYS   F CD    1 
ATOM   11843 C  CE    . LYS   E 4  70  ? 13.951  67.058  86.232  1.00 77.74  ? 70  LYS   F CE    1 
ATOM   11844 N  NZ    . LYS   E 4  70  ? 15.423  67.320  86.044  1.00 77.70  ? 70  LYS   F NZ    1 
ATOM   11845 N  N     . LEU   E 4  71  ? 11.327  62.146  89.913  1.00 53.63  ? 71  LEU   F N     1 
ATOM   11846 C  CA    . LEU   E 4  71  ? 10.262  61.761  90.821  1.00 49.28  ? 71  LEU   F CA    1 
ATOM   11847 C  C     . LEU   E 4  71  ? 10.222  60.258  91.074  1.00 54.26  ? 71  LEU   F C     1 
ATOM   11848 O  O     . LEU   E 4  71  ? 9.542   59.813  92.003  1.00 53.98  ? 71  LEU   F O     1 
ATOM   11849 C  CB    . LEU   E 4  71  ? 8.931   62.238  90.226  1.00 42.67  ? 71  LEU   F CB    1 
ATOM   11850 C  CG    . LEU   E 4  71  ? 7.644   62.315  91.028  1.00 41.07  ? 71  LEU   F CG    1 
ATOM   11851 C  CD1   . LEU   E 4  71  ? 7.835   63.166  92.269  1.00 47.06  ? 71  LEU   F CD1   1 
ATOM   11852 C  CD2   . LEU   E 4  71  ? 6.594   62.914  90.132  1.00 46.87  ? 71  LEU   F CD2   1 
ATOM   11853 N  N     . CYS   E 4  72  ? 10.943  59.471  90.274  1.00 59.79  ? 72  CYS   F N     1 
ATOM   11854 C  CA    . CYS   E 4  72  ? 10.774  58.027  90.210  1.00 44.91  ? 72  CYS   F CA    1 
ATOM   11855 C  C     . CYS   E 4  72  ? 12.044  57.277  90.597  1.00 45.17  ? 72  CYS   F C     1 
ATOM   11856 O  O     . CYS   E 4  72  ? 12.089  56.050  90.477  1.00 43.85  ? 72  CYS   F O     1 
ATOM   11857 C  CB    . CYS   E 4  72  ? 10.312  57.634  88.797  1.00 44.60  ? 72  CYS   F CB    1 
ATOM   11858 S  SG    . CYS   E 4  72  ? 8.720   58.404  88.247  1.00 45.46  ? 72  CYS   F SG    1 
ATOM   11859 N  N     . ARG   E 4  73  ? 13.073  57.987  91.053  1.00 56.40  ? 73  ARG   F N     1 
ATOM   11860 C  CA    . ARG   E 4  73  ? 14.309  57.402  91.556  1.00 58.47  ? 73  ARG   F CA    1 
ATOM   11861 C  C     . ARG   E 4  73  ? 14.459  57.764  93.028  1.00 56.70  ? 73  ARG   F C     1 
ATOM   11862 O  O     . ARG   E 4  73  ? 14.281  58.926  93.405  1.00 56.43  ? 73  ARG   F O     1 
ATOM   11863 C  CB    . ARG   E 4  73  ? 15.520  57.903  90.761  1.00 64.51  ? 73  ARG   F CB    1 
ATOM   11864 C  CG    . ARG   E 4  73  ? 15.805  57.153  89.453  1.00 62.05  ? 73  ARG   F CG    1 
ATOM   11865 C  CD    . ARG   E 4  73  ? 17.048  57.741  88.788  1.00 88.04  ? 73  ARG   F CD    1 
ATOM   11866 N  NE    . ARG   E 4  73  ? 18.091  58.008  89.776  1.00 89.43  ? 73  ARG   F NE    1 
ATOM   11867 C  CZ    . ARG   E 4  73  ? 19.296  58.495  89.508  1.00 87.20  ? 73  ARG   F CZ    1 
ATOM   11868 N  NH1   . ARG   E 4  73  ? 19.670  58.791  88.269  1.00 68.38  ? 73  ARG   F NH1   1 
ATOM   11869 N  NH2   . ARG   E 4  73  ? 20.151  58.687  90.510  1.00 103.24 ? 73  ARG   F NH2   1 
ATOM   11870 N  N     . LYS   E 4  74  ? 14.806  56.776  93.854  1.00 58.93  ? 74  LYS   F N     1 
ATOM   11871 C  CA    . LYS   E 4  74  ? 14.722  56.961  95.300  1.00 63.64  ? 74  LYS   F CA    1 
ATOM   11872 C  C     . LYS   E 4  74  ? 15.699  58.025  95.794  1.00 65.64  ? 74  LYS   F C     1 
ATOM   11873 O  O     . LYS   E 4  74  ? 15.348  58.853  96.644  1.00 57.49  ? 74  LYS   F O     1 
ATOM   11874 C  CB    . LYS   E 4  74  ? 14.955  55.624  96.001  1.00 62.37  ? 74  LYS   F CB    1 
ATOM   11875 C  CG    . LYS   E 4  74  ? 14.104  54.516  95.397  1.00 66.68  ? 74  LYS   F CG    1 
ATOM   11876 C  CD    . LYS   E 4  74  ? 13.755  53.400  96.375  1.00 49.87  ? 74  LYS   F CD    1 
ATOM   11877 C  CE    . LYS   E 4  74  ? 12.873  52.359  95.684  1.00 62.45  ? 74  LYS   F CE    1 
ATOM   11878 N  NZ    . LYS   E 4  74  ? 11.594  52.941  95.155  1.00 59.91  ? 74  LYS   F NZ    1 
ATOM   11879 N  N     . ALA   E 4  75  ? 16.926  58.022  95.280  1.00 64.88  ? 75  ALA   F N     1 
ATOM   11880 C  CA    . ALA   E 4  75  ? 17.851  59.094  95.624  1.00 60.12  ? 75  ALA   F CA    1 
ATOM   11881 C  C     . ALA   E 4  75  ? 17.284  60.457  95.235  1.00 60.97  ? 75  ALA   F C     1 
ATOM   11882 O  O     . ALA   E 4  75  ? 17.437  61.438  95.972  1.00 63.45  ? 75  ALA   F O     1 
ATOM   11883 C  CB    . ALA   E 4  75  ? 19.197  58.852  94.939  1.00 69.68  ? 75  ALA   F CB    1 
ATOM   11884 N  N     . SER   E 4  76  ? 16.623  60.537  94.080  1.00 56.70  ? 76  SER   F N     1 
ATOM   11885 C  CA    . SER   E 4  76  ? 16.177  61.820  93.550  1.00 56.04  ? 76  SER   F CA    1 
ATOM   11886 C  C     . SER   E 4  76  ? 14.910  62.306  94.243  1.00 58.09  ? 76  SER   F C     1 
ATOM   11887 O  O     . SER   E 4  76  ? 14.848  63.453  94.699  1.00 65.62  ? 76  SER   F O     1 
ATOM   11888 C  CB    . SER   E 4  76  ? 15.958  61.699  92.047  1.00 59.78  ? 76  SER   F CB    1 
ATOM   11889 O  OG    . SER   E 4  76  ? 17.081  61.090  91.448  1.00 63.48  ? 76  SER   F OG    1 
ATOM   11890 N  N     . LEU   E 4  77  ? 13.892  61.444  94.327  1.00 51.12  ? 77  LEU   F N     1 
ATOM   11891 C  CA    . LEU   E 4  77  ? 12.662  61.759  95.048  1.00 51.43  ? 77  LEU   F CA    1 
ATOM   11892 C  C     . LEU   E 4  77  ? 12.927  62.452  96.378  1.00 55.28  ? 77  LEU   F C     1 
ATOM   11893 O  O     . LEU   E 4  77  ? 12.289  63.454  96.712  1.00 57.10  ? 77  LEU   F O     1 
ATOM   11894 C  CB    . LEU   E 4  77  ? 11.869  60.471  95.276  1.00 59.41  ? 77  LEU   F CB    1 
ATOM   11895 C  CG    . LEU   E 4  77  ? 10.600  60.527  96.127  1.00 53.28  ? 77  LEU   F CG    1 
ATOM   11896 C  CD1   . LEU   E 4  77  ? 9.625   61.554  95.580  1.00 56.58  ? 77  LEU   F CD1   1 
ATOM   11897 C  CD2   . LEU   E 4  77  ? 9.971   59.152  96.150  1.00 55.91  ? 77  LEU   F CD2   1 
ATOM   11898 N  N     . VAL   E 4  78  ? 13.866  61.922  97.159  1.00 58.69  ? 78  VAL   F N     1 
ATOM   11899 C  CA    . VAL   E 4  78  ? 14.225  62.565  98.420  1.00 64.85  ? 78  VAL   F CA    1 
ATOM   11900 C  C     . VAL   E 4  78  ? 14.763  63.971  98.172  1.00 63.57  ? 78  VAL   F C     1 
ATOM   11901 O  O     . VAL   E 4  78  ? 14.316  64.949  98.785  1.00 61.49  ? 78  VAL   F O     1 
ATOM   11902 C  CB    . VAL   E 4  78  ? 15.241  61.702  99.187  1.00 62.70  ? 78  VAL   F CB    1 
ATOM   11903 C  CG1   . VAL   E 4  78  ? 15.748  62.455  100.422 1.00 60.59  ? 78  VAL   F CG1   1 
ATOM   11904 C  CG2   . VAL   E 4  78  ? 14.616  60.365  99.548  1.00 53.33  ? 78  VAL   F CG2   1 
ATOM   11905 N  N     . LYS   E 4  79  ? 15.750  64.090  97.283  1.00 63.07  ? 79  LYS   F N     1 
ATOM   11906 C  CA    . LYS   E 4  79  ? 16.299  65.404  96.985  1.00 68.35  ? 79  LYS   F CA    1 
ATOM   11907 C  C     . LYS   E 4  79  ? 15.222  66.329  96.437  1.00 65.94  ? 79  LYS   F C     1 
ATOM   11908 O  O     . LYS   E 4  79  ? 15.236  67.538  96.712  1.00 61.06  ? 79  LYS   F O     1 
ATOM   11909 C  CB    . LYS   E 4  79  ? 17.465  65.265  96.003  1.00 66.82  ? 79  LYS   F CB    1 
ATOM   11910 C  CG    . LYS   E 4  79  ? 18.222  66.555  95.715  1.00 67.63  ? 79  LYS   F CG    1 
ATOM   11911 C  CD    . LYS   E 4  79  ? 19.353  66.321  94.716  1.00 72.06  ? 79  LYS   F CD    1 
ATOM   11912 C  CE    . LYS   E 4  79  ? 19.790  67.619  94.045  1.00 73.82  ? 79  LYS   F CE    1 
ATOM   11913 N  NZ    . LYS   E 4  79  ? 20.368  68.619  94.991  1.00 57.37  ? 79  LYS   F NZ    1 
ATOM   11914 N  N     . LEU   E 4  80  ? 14.262  65.778  95.692  1.00 46.25  ? 80  LEU   F N     1 
ATOM   11915 C  CA    . LEU   E 4  80  ? 13.205  66.613  95.130  1.00 58.05  ? 80  LEU   F CA    1 
ATOM   11916 C  C     . LEU   E 4  80  ? 12.336  67.205  96.232  1.00 62.21  ? 80  LEU   F C     1 
ATOM   11917 O  O     . LEU   E 4  80  ? 12.021  68.401  96.210  1.00 59.51  ? 80  LEU   F O     1 
ATOM   11918 C  CB    . LEU   E 4  80  ? 12.356  65.808  94.145  1.00 50.73  ? 80  LEU   F CB    1 
ATOM   11919 C  CG    . LEU   E 4  80  ? 11.114  66.494  93.576  1.00 44.06  ? 80  LEU   F CG    1 
ATOM   11920 C  CD1   . LEU   E 4  80  ? 11.505  67.704  92.756  1.00 41.68  ? 80  LEU   F CD1   1 
ATOM   11921 C  CD2   . LEU   E 4  80  ? 10.275  65.503  92.762  1.00 39.08  ? 80  LEU   F CD2   1 
ATOM   11922 N  N     . ILE   E 4  81  ? 11.949  66.381  97.211  1.00 66.82  ? 81  ILE   F N     1 
ATOM   11923 C  CA    . ILE   E 4  81  ? 11.089  66.848  98.295  1.00 65.28  ? 81  ILE   F CA    1 
ATOM   11924 C  C     . ILE   E 4  81  ? 11.832  67.845  99.177  1.00 64.94  ? 81  ILE   F C     1 
ATOM   11925 O  O     . ILE   E 4  81  ? 11.355  68.959  99.420  1.00 63.61  ? 81  ILE   F O     1 
ATOM   11926 C  CB    . ILE   E 4  81  ? 10.564  65.659  99.118  1.00 51.19  ? 81  ILE   F CB    1 
ATOM   11927 C  CG1   . ILE   E 4  81  ? 9.981   64.596  98.195  1.00 52.90  ? 81  ILE   F CG1   1 
ATOM   11928 C  CG2   . ILE   E 4  81  ? 9.507   66.126  100.094 1.00 57.18  ? 81  ILE   F CG2   1 
ATOM   11929 C  CD1   . ILE   E 4  81  ? 9.324   63.448  98.919  1.00 47.45  ? 81  ILE   F CD1   1 
ATOM   11930 N  N     . LYS   E 4  82  ? 13.006  67.459  99.675  1.00 61.12  ? 82  LYS   F N     1 
ATOM   11931 C  CA    . LYS   E 4  82  ? 13.726  68.333  100.595 1.00 67.07  ? 82  LYS   F CA    1 
ATOM   11932 C  C     . LYS   E 4  82  ? 13.999  69.693  99.964  1.00 71.60  ? 82  LYS   F C     1 
ATOM   11933 O  O     . LYS   E 4  82  ? 13.668  70.735  100.541 1.00 78.60  ? 82  LYS   F O     1 
ATOM   11934 C  CB    . LYS   E 4  82  ? 15.040  67.683  101.037 1.00 70.78  ? 82  LYS   F CB    1 
ATOM   11935 C  CG    . LYS   E 4  82  ? 14.904  66.327  101.709 1.00 70.79  ? 82  LYS   F CG    1 
ATOM   11936 C  CD    . LYS   E 4  82  ? 16.176  65.973  102.464 1.00 68.47  ? 82  LYS   F CD    1 
ATOM   11937 C  CE    . LYS   E 4  82  ? 16.194  64.509  102.867 1.00 72.09  ? 82  LYS   F CE    1 
ATOM   11938 N  NZ    . LYS   E 4  82  ? 17.422  64.169  103.641 1.00 68.22  ? 82  LYS   F NZ    1 
ATOM   11939 N  N     . THR   E 4  83  ? 14.597  69.700  98.774  1.00 71.75  ? 83  THR   F N     1 
ATOM   11940 C  CA    . THR   E 4  83  ? 15.112  70.921  98.154  1.00 72.54  ? 83  THR   F CA    1 
ATOM   11941 C  C     . THR   E 4  83  ? 14.090  71.609  97.261  1.00 72.20  ? 83  THR   F C     1 
ATOM   11942 O  O     . THR   E 4  83  ? 14.451  72.115  96.197  1.00 76.79  ? 83  THR   F O     1 
ATOM   11943 C  CB    . THR   E 4  83  ? 16.368  70.592  97.358  1.00 68.72  ? 83  THR   F CB    1 
ATOM   11944 O  OG1   . THR   E 4  83  ? 15.987  70.038  96.095  1.00 61.57  ? 83  THR   F OG1   1 
ATOM   11945 C  CG2   . THR   E 4  83  ? 17.224  69.580  98.110  1.00 72.08  ? 83  THR   F CG2   1 
ATOM   11946 N  N     . SER   E 4  84  ? 12.824  71.659  97.654  1.00 55.40  ? 84  SER   F N     1 
ATOM   11947 C  CA    . SER   E 4  84  ? 11.818  72.227  96.774  1.00 55.51  ? 84  SER   F CA    1 
ATOM   11948 C  C     . SER   E 4  84  ? 10.729  72.930  97.575  1.00 71.89  ? 84  SER   F C     1 
ATOM   11949 O  O     . SER   E 4  84  ? 9.915   72.268  98.231  1.00 74.47  ? 84  SER   F O     1 
ATOM   11950 C  CB    . SER   E 4  84  ? 11.222  71.129  95.897  1.00 55.83  ? 84  SER   F CB    1 
ATOM   11951 O  OG    . SER   E 4  84  ? 9.960   71.517  95.408  1.00 59.42  ? 84  SER   F OG    1 
ATOM   11952 N  N     . PRO   E 4  85  ? 10.663  74.264  97.527  1.00 78.74  ? 85  PRO   F N     1 
ATOM   11953 C  CA    . PRO   E 4  85  ? 9.734   74.984  98.415  1.00 65.25  ? 85  PRO   F CA    1 
ATOM   11954 C  C     . PRO   E 4  85  ? 8.343   74.391  98.475  1.00 58.57  ? 85  PRO   F C     1 
ATOM   11955 O  O     . PRO   E 4  85  ? 7.726   74.409  99.545  1.00 72.21  ? 85  PRO   F O     1 
ATOM   11956 C  CB    . PRO   E 4  85  ? 9.718   76.411  97.834  1.00 64.94  ? 85  PRO   F CB    1 
ATOM   11957 C  CG    . PRO   E 4  85  ? 10.508  76.363  96.551  1.00 69.80  ? 85  PRO   F CG    1 
ATOM   11958 C  CD    . PRO   E 4  85  ? 11.424  75.183  96.665  1.00 75.24  ? 85  PRO   F CD    1 
ATOM   11959 N  N     . GLU   E 4  86  ? 7.825   73.859  97.369  1.00 63.18  ? 86  GLU   F N     1 
ATOM   11960 C  CA    . GLU   E 4  86  ? 6.431   73.421  97.361  1.00 67.32  ? 86  GLU   F CA    1 
ATOM   11961 C  C     . GLU   E 4  86  ? 6.191   72.194  98.228  1.00 69.90  ? 86  GLU   F C     1 
ATOM   11962 O  O     . GLU   E 4  86  ? 5.030   71.816  98.422  1.00 57.32  ? 86  GLU   F O     1 
ATOM   11963 C  CB    . GLU   E 4  86  ? 5.963   73.125  95.934  1.00 59.62  ? 86  GLU   F CB    1 
ATOM   11964 C  CG    . GLU   E 4  86  ? 6.100   74.282  94.962  1.00 61.78  ? 86  GLU   F CG    1 
ATOM   11965 C  CD    . GLU   E 4  86  ? 7.408   74.236  94.177  1.00 79.47  ? 86  GLU   F CD    1 
ATOM   11966 O  OE1   . GLU   E 4  86  ? 8.425   74.809  94.639  1.00 72.28  ? 86  GLU   F OE1   1 
ATOM   11967 O  OE2   . GLU   E 4  86  ? 7.418   73.615  93.091  1.00 85.47  ? 86  GLU   F OE2   1 
ATOM   11968 N  N     . LEU   E 4  87  ? 7.252   71.564  98.740  1.00 71.39  ? 87  LEU   F N     1 
ATOM   11969 C  CA    . LEU   E 4  87  ? 7.140   70.330  99.506  1.00 63.88  ? 87  LEU   F CA    1 
ATOM   11970 C  C     . LEU   E 4  87  ? 7.948   70.450  100.792 1.00 75.04  ? 87  LEU   F C     1 
ATOM   11971 O  O     . LEU   E 4  87  ? 7.377   70.517  101.885 1.00 85.17  ? 87  LEU   F O     1 
ATOM   11972 C  CB    . LEU   E 4  87  ? 7.611   69.135  98.667  1.00 64.52  ? 87  LEU   F CB    1 
ATOM   11973 C  CG    . LEU   E 4  87  ? 7.019   68.989  97.255  1.00 54.52  ? 87  LEU   F CG    1 
ATOM   11974 C  CD1   . LEU   E 4  87  ? 7.461   67.707  96.589  1.00 48.01  ? 87  LEU   F CD1   1 
ATOM   11975 C  CD2   . LEU   E 4  87  ? 5.512   69.058  97.279  1.00 46.40  ? 87  LEU   F CD2   1 
ATOM   11976 N  N     . SER   E 4  88  ? 9.278   70.472  100.671 1.00 73.81  ? 88  SER   F N     1 
ATOM   11977 C  CA    . SER   E 4  88  ? 10.162  70.823  101.785 1.00 91.25  ? 88  SER   F CA    1 
ATOM   11978 C  C     . SER   E 4  88  ? 9.863   70.032  103.054 1.00 100.97 ? 88  SER   F C     1 
ATOM   11979 O  O     . SER   E 4  88  ? 9.222   68.978  102.990 1.00 104.77 ? 88  SER   F O     1 
ATOM   11980 C  CB    . SER   E 4  88  ? 10.044  72.320  102.091 1.00 95.59  ? 88  SER   F CB    1 
ATOM   11981 O  OG    . SER   E 4  88  ? 8.852   72.598  102.820 1.00 83.98  ? 88  SER   F OG    1 
ATOM   11982 N  N     . GLU   E 4  89  ? 10.325  70.535  104.197 1.00 99.12  ? 89  GLU   F N     1 
ATOM   11983 C  CA    . GLU   E 4  89  ? 9.729   70.231  105.507 1.00 106.68 ? 89  GLU   F CA    1 
ATOM   11984 C  C     . GLU   E 4  89  ? 8.292   70.721  105.655 1.00 111.64 ? 89  GLU   F C     1 
ATOM   11985 O  O     . GLU   E 4  89  ? 7.669   70.511  106.699 1.00 105.42 ? 89  GLU   F O     1 
ATOM   11986 C  CB    . GLU   E 4  89  ? 10.646  70.792  106.625 1.00 113.72 ? 89  GLU   F CB    1 
ATOM   11987 C  CG    . GLU   E 4  89  ? 9.975   70.920  107.997 1.00 111.52 ? 89  GLU   F CG    1 
ATOM   11988 C  CD    . GLU   E 4  89  ? 9.410   69.599  108.527 1.00 120.82 ? 89  GLU   F CD    1 
ATOM   11989 O  OE1   . GLU   E 4  89  ? 9.100   68.695  107.716 1.00 124.26 ? 89  GLU   F OE1   1 
ATOM   11990 O  OE2   . GLU   E 4  89  ? 9.273   69.470  109.763 1.00 106.30 ? 89  GLU   F OE2   1 
ATOM   11991 N  N     . SER   E 4  90  ? 7.723   71.356  104.617 1.00 103.13 ? 90  SER   F N     1 
ATOM   11992 C  CA    . SER   E 4  90  ? 6.263   71.562  104.514 1.00 106.63 ? 90  SER   F CA    1 
ATOM   11993 C  C     . SER   E 4  90  ? 5.497   70.252  104.396 1.00 103.75 ? 90  SER   F C     1 
ATOM   11994 O  O     . SER   E 4  90  ? 4.261   70.225  104.270 1.00 94.55  ? 90  SER   F O     1 
ATOM   11995 C  CB    . SER   E 4  90  ? 5.974   72.497  103.309 1.00 96.90  ? 90  SER   F CB    1 
ATOM   11996 O  OG    . SER   E 4  90  ? 4.681   73.099  103.342 1.00 81.85  ? 90  SER   F OG    1 
ATOM   11997 N  N     . CYS   E 4  91  ? 6.220   69.124  104.498 1.00 97.38  ? 91  CYS   F N     1 
ATOM   11998 C  CA    . CYS   E 4  91  ? 5.759   67.784  104.117 1.00 90.69  ? 91  CYS   F CA    1 
ATOM   11999 C  C     . CYS   E 4  91  ? 5.437   66.929  105.340 1.00 77.22  ? 91  CYS   F C     1 
ATOM   12000 O  O     . CYS   E 4  91  ? 6.278   66.757  106.229 1.00 81.12  ? 91  CYS   F O     1 
ATOM   12001 C  CB    . CYS   E 4  91  ? 6.818   67.072  103.265 1.00 78.43  ? 91  CYS   F CB    1 
ATOM   12002 S  SG    . CYS   E 4  91  ? 6.141   65.751  102.235 1.00 77.31  ? 91  CYS   F SG    1 
ATOM   12003 N  N     . THR   E 4  92  ? 4.225   66.376  105.357 1.00 60.37  ? 92  THR   F N     1 
ATOM   12004 C  CA    . THR   E 4  92  ? 3.755   65.492  106.413 1.00 66.81  ? 92  THR   F CA    1 
ATOM   12005 C  C     . THR   E 4  92  ? 3.491   64.072  105.925 1.00 64.77  ? 92  THR   F C     1 
ATOM   12006 O  O     . THR   E 4  92  ? 3.100   63.222  106.729 1.00 54.21  ? 92  THR   F O     1 
ATOM   12007 C  CB    . THR   E 4  92  ? 2.468   66.053  107.037 1.00 59.69  ? 92  THR   F CB    1 
ATOM   12008 O  OG1   . THR   E 4  92  ? 1.316   65.483  106.389 1.00 48.88  ? 92  THR   F OG1   1 
ATOM   12009 C  CG2   . THR   E 4  92  ? 2.423   67.552  106.878 1.00 51.17  ? 92  THR   F CG2   1 
ATOM   12010 N  N     . TRP   E 4  93  ? 3.681   63.792  104.632 1.00 63.48  ? 93  TRP   F N     1 
ATOM   12011 C  CA    . TRP   E 4  93  ? 3.286   62.518  104.041 1.00 51.42  ? 93  TRP   F CA    1 
ATOM   12012 C  C     . TRP   E 4  93  ? 4.466   61.731  103.477 1.00 53.67  ? 93  TRP   F C     1 
ATOM   12013 O  O     . TRP   E 4  93  ? 4.250   60.752  102.745 1.00 50.10  ? 93  TRP   F O     1 
ATOM   12014 C  CB    . TRP   E 4  93  ? 2.221   62.738  102.949 1.00 53.84  ? 93  TRP   F CB    1 
ATOM   12015 C  CG    . TRP   E 4  93  ? 2.479   63.918  102.004 1.00 59.00  ? 93  TRP   F CG    1 
ATOM   12016 C  CD1   . TRP   E 4  93  ? 1.813   65.110  101.986 1.00 57.36  ? 93  TRP   F CD1   1 
ATOM   12017 C  CD2   . TRP   E 4  93  ? 3.459   63.997  100.950 1.00 60.86  ? 93  TRP   F CD2   1 
ATOM   12018 N  NE1   . TRP   E 4  93  ? 2.314   65.925  100.993 1.00 59.12  ? 93  TRP   F NE1   1 
ATOM   12019 C  CE2   . TRP   E 4  93  ? 3.330   65.268  100.350 1.00 65.02  ? 93  TRP   F CE2   1 
ATOM   12020 C  CE3   . TRP   E 4  93  ? 4.435   63.122  100.461 1.00 55.18  ? 93  TRP   F CE3   1 
ATOM   12021 C  CZ2   . TRP   E 4  93  ? 4.139   65.681  99.294  1.00 59.22  ? 93  TRP   F CZ2   1 
ATOM   12022 C  CZ3   . TRP   E 4  93  ? 5.238   63.539  99.412  1.00 61.04  ? 93  TRP   F CZ3   1 
ATOM   12023 C  CH2   . TRP   E 4  93  ? 5.083   64.804  98.840  1.00 50.32  ? 93  TRP   F CH2   1 
ATOM   12024 N  N     . PHE   E 4  94  ? 5.701   62.110  103.803 1.00 47.12  ? 94  PHE   F N     1 
ATOM   12025 C  CA    . PHE   E 4  94  ? 6.881   61.414  103.294 1.00 53.87  ? 94  PHE   F CA    1 
ATOM   12026 C  C     . PHE   E 4  94  ? 7.763   61.021  104.472 1.00 59.64  ? 94  PHE   F C     1 
ATOM   12027 O  O     . PHE   E 4  94  ? 8.164   61.901  105.261 1.00 55.63  ? 94  PHE   F O     1 
ATOM   12028 C  CB    . PHE   E 4  94  ? 7.643   62.286  102.292 1.00 56.28  ? 94  PHE   F CB    1 
ATOM   12029 C  CG    . PHE   E 4  94  ? 8.799   61.586  101.620 1.00 52.49  ? 94  PHE   F CG    1 
ATOM   12030 C  CD1   . PHE   E 4  94  ? 8.573   60.559  100.713 1.00 49.26  ? 94  PHE   F CD1   1 
ATOM   12031 C  CD2   . PHE   E 4  94  ? 10.108  61.969  101.883 1.00 44.71  ? 94  PHE   F CD2   1 
ATOM   12032 C  CE1   . PHE   E 4  94  ? 9.621   59.923  100.090 1.00 45.12  ? 94  PHE   F CE1   1 
ATOM   12033 C  CE2   . PHE   E 4  94  ? 11.162  61.333  101.266 1.00 49.22  ? 94  PHE   F CE2   1 
ATOM   12034 C  CZ    . PHE   E 4  94  ? 10.919  60.312  100.365 1.00 52.45  ? 94  PHE   F CZ    1 
ATOM   12035 N  N     . PRO   E 4  95  ? 8.085   59.734  104.644 1.00 64.98  ? 95  PRO   F N     1 
ATOM   12036 C  CA    . PRO   E 4  95  ? 8.916   59.331  105.780 1.00 61.65  ? 95  PRO   F CA    1 
ATOM   12037 C  C     . PRO   E 4  95  ? 10.259  60.041  105.756 1.00 62.41  ? 95  PRO   F C     1 
ATOM   12038 O  O     . PRO   E 4  95  ? 10.773  60.407  104.699 1.00 55.69  ? 95  PRO   F O     1 
ATOM   12039 C  CB    . PRO   E 4  95  ? 9.077   57.818  105.582 1.00 53.56  ? 95  PRO   F CB    1 
ATOM   12040 C  CG    . PRO   E 4  95  ? 7.901   57.414  104.806 1.00 53.33  ? 95  PRO   F CG    1 
ATOM   12041 C  CD    . PRO   E 4  95  ? 7.654   58.564  103.857 1.00 66.42  ? 95  PRO   F CD    1 
ATOM   12042 N  N     . GLU   E 4  96  ? 10.822  60.244  106.944 1.00 67.69  ? 96  GLU   F N     1 
ATOM   12043 C  CA    . GLU   E 4  96  ? 12.106  60.921  107.049 1.00 73.68  ? 96  GLU   F CA    1 
ATOM   12044 C  C     . GLU   E 4  96  ? 13.172  60.135  106.297 1.00 77.98  ? 96  GLU   F C     1 
ATOM   12045 O  O     . GLU   E 4  96  ? 13.348  58.937  106.528 1.00 85.57  ? 96  GLU   F O     1 
ATOM   12046 C  CB    . GLU   E 4  96  ? 12.497  61.075  108.514 1.00 75.94  ? 96  GLU   F CB    1 
ATOM   12047 C  CG    . GLU   E 4  96  ? 12.927  62.464  108.890 1.00 72.31  ? 96  GLU   F CG    1 
ATOM   12048 C  CD    . GLU   E 4  96  ? 14.024  62.455  109.928 1.00 83.96  ? 96  GLU   F CD    1 
ATOM   12049 O  OE1   . GLU   E 4  96  ? 14.917  61.583  109.835 1.00 81.21  ? 96  GLU   F OE1   1 
ATOM   12050 O  OE2   . GLU   E 4  96  ? 13.992  63.317  110.835 1.00 79.07  ? 96  GLU   F OE2   1 
ATOM   12051 N  N     . SER   E 4  97  ? 13.891  60.812  105.401 1.00 74.39  ? 97  SER   F N     1 
ATOM   12052 C  CA    . SER   E 4  97  ? 14.826  60.141  104.508 1.00 69.63  ? 97  SER   F CA    1 
ATOM   12053 C  C     . SER   E 4  97  ? 16.121  60.935  104.387 1.00 66.87  ? 97  SER   F C     1 
ATOM   12054 O  O     . SER   E 4  97  ? 16.172  62.140  104.641 1.00 69.02  ? 97  SER   F O     1 
ATOM   12055 C  CB    . SER   E 4  97  ? 14.225  59.938  103.108 1.00 60.79  ? 97  SER   F CB    1 
ATOM   12056 O  OG    . SER   E 4  97  ? 13.121  59.057  103.130 1.00 55.30  ? 97  SER   F OG    1 
ATOM   12057 N  N     . TYR   E 4  98  ? 17.171  60.237  103.973 1.00 69.27  ? 98  TYR   F N     1 
ATOM   12058 C  CA    . TYR   E 4  98  ? 18.450  60.858  103.671 1.00 71.04  ? 98  TYR   F CA    1 
ATOM   12059 C  C     . TYR   E 4  98  ? 19.111  60.031  102.583 1.00 71.57  ? 98  TYR   F C     1 
ATOM   12060 O  O     . TYR   E 4  98  ? 18.920  58.815  102.521 1.00 69.61  ? 98  TYR   F O     1 
ATOM   12061 C  CB    . TYR   E 4  98  ? 19.354  60.940  104.908 1.00 75.03  ? 98  TYR   F CB    1 
ATOM   12062 C  CG    . TYR   E 4  98  ? 18.716  61.599  106.104 1.00 71.04  ? 98  TYR   F CG    1 
ATOM   12063 C  CD1   . TYR   E 4  98  ? 18.795  62.972  106.287 1.00 76.90  ? 98  TYR   F CD1   1 
ATOM   12064 C  CD2   . TYR   E 4  98  ? 18.033  60.854  107.050 1.00 74.94  ? 98  TYR   F CD2   1 
ATOM   12065 C  CE1   . TYR   E 4  98  ? 18.213  63.580  107.377 1.00 70.66  ? 98  TYR   F CE1   1 
ATOM   12066 C  CE2   . TYR   E 4  98  ? 17.445  61.457  108.147 1.00 71.39  ? 98  TYR   F CE2   1 
ATOM   12067 C  CZ    . TYR   E 4  98  ? 17.539  62.818  108.304 1.00 71.99  ? 98  TYR   F CZ    1 
ATOM   12068 O  OH    . TYR   E 4  98  ? 16.959  63.427  109.392 1.00 86.36  ? 98  TYR   F OH    1 
ATOM   12069 N  N     . VAL   E 4  99  ? 19.885  60.706  101.704 1.00 88.11  ? 99  VAL   F N     1 
ATOM   12070 C  CA    . VAL   E 4  99  ? 20.647  60.024  100.660 1.00 84.37  ? 99  VAL   F CA    1 
ATOM   12071 C  C     . VAL   E 4  99  ? 22.024  59.697  101.214 1.00 87.92  ? 99  VAL   F C     1 
ATOM   12072 O  O     . VAL   E 4  99  ? 22.565  60.415  102.062 1.00 86.79  ? 99  VAL   F O     1 
ATOM   12073 C  CB    . VAL   E 4  99  ? 20.744  60.863  99.369  1.00 68.88  ? 99  VAL   F CB    1 
ATOM   12074 C  CG1   . VAL   E 4  99  ? 19.380  61.381  98.974  1.00 69.05  ? 99  VAL   F CG1   1 
ATOM   12075 C  CG2   . VAL   E 4  99  ? 21.739  62.006  99.536  1.00 86.75  ? 99  VAL   F CG2   1 
ATOM   12076 N  N     . ILE   E 4  100 ? 22.603  58.600  100.737 1.00 87.34  ? 100 ILE   F N     1 
ATOM   12077 C  CA    . ILE   E 4  100 ? 23.836  58.100  101.330 1.00 100.16 ? 100 ILE   F CA    1 
ATOM   12078 C  C     . ILE   E 4  100 ? 24.658  57.384  100.263 1.00 106.99 ? 100 ILE   F C     1 
ATOM   12079 O  O     . ILE   E 4  100 ? 24.115  56.705  99.387  1.00 103.31 ? 100 ILE   F O     1 
ATOM   12080 C  CB    . ILE   E 4  100 ? 23.516  57.208  102.548 1.00 92.92  ? 100 ILE   F CB    1 
ATOM   12081 C  CG1   . ILE   E 4  100 ? 23.742  58.005  103.836 1.00 96.58  ? 100 ILE   F CG1   1 
ATOM   12082 C  CG2   . ILE   E 4  100 ? 24.314  55.917  102.509 1.00 98.57  ? 100 ILE   F CG2   1 
ATOM   12083 C  CD1   . ILE   E 4  100 ? 23.066  57.425  105.051 1.00 104.06 ? 100 ILE   F CD1   1 
ATOM   12084 N  N     . TYR   E 4  101 ? 25.980  57.549  100.344 1.00 111.59 ? 101 TYR   F N     1 
ATOM   12085 C  CA    . TYR   E 4  101 ? 26.914  57.051  99.350  1.00 113.03 ? 101 TYR   F CA    1 
ATOM   12086 C  C     . TYR   E 4  101 ? 27.837  55.991  99.942  1.00 110.06 ? 101 TYR   F C     1 
ATOM   12087 O  O     . TYR   E 4  101 ? 28.462  56.230  100.987 1.00 101.38 ? 101 TYR   F O     1 
ATOM   12088 C  CB    . TYR   E 4  101 ? 27.752  58.200  98.785  1.00 111.11 ? 101 TYR   F CB    1 
ATOM   12089 C  CG    . TYR   E 4  101 ? 26.972  59.194  97.963  1.00 105.17 ? 101 TYR   F CG    1 
ATOM   12090 C  CD1   . TYR   E 4  101 ? 26.294  58.801  96.817  1.00 102.70 ? 101 TYR   F CD1   1 
ATOM   12091 C  CD2   . TYR   E 4  101 ? 26.942  60.532  98.314  1.00 107.23 ? 101 TYR   F CD2   1 
ATOM   12092 C  CE1   . TYR   E 4  101 ? 25.596  59.714  96.058  1.00 100.09 ? 101 TYR   F CE1   1 
ATOM   12093 C  CE2   . TYR   E 4  101 ? 26.244  61.452  97.565  1.00 102.67 ? 101 TYR   F CE2   1 
ATOM   12094 C  CZ    . TYR   E 4  101 ? 25.574  61.039  96.439  1.00 103.50 ? 101 TYR   F CZ    1 
ATOM   12095 O  OH    . TYR   E 4  101 ? 24.881  61.960  95.694  1.00 105.10 ? 101 TYR   F OH    1 
ATOM   12096 N  N     . PRO   E 4  102 ? 27.972  54.826  99.298  1.00 110.90 ? 102 PRO   F N     1 
ATOM   12097 C  CA    . PRO   E 4  102 ? 28.899  53.796  99.793  1.00 112.55 ? 102 PRO   F CA    1 
ATOM   12098 C  C     . PRO   E 4  102 ? 30.363  54.202  99.707  1.00 116.58 ? 102 PRO   F C     1 
ATOM   12099 O  O     . PRO   E 4  102 ? 31.000  54.015  98.665  1.00 121.43 ? 102 PRO   F O     1 
ATOM   12100 C  CB    . PRO   E 4  102 ? 28.609  52.602  98.876  1.00 113.03 ? 102 PRO   F CB    1 
ATOM   12101 C  CG    . PRO   E 4  102 ? 28.057  53.211  97.638  1.00 115.04 ? 102 PRO   F CG    1 
ATOM   12102 C  CD    . PRO   E 4  102 ? 27.253  54.389  98.090  1.00 113.51 ? 102 PRO   F CD    1 
ATOM   12103 N  N     . THR   E 4  103 ? 30.901  54.737  100.801 1.00 115.48 ? 103 THR   F N     1 
ATOM   12104 C  CA    . THR   E 4  103 ? 32.291  55.182  100.878 1.00 107.60 ? 103 THR   F CA    1 
ATOM   12105 C  C     . THR   E 4  103 ? 33.234  54.371  99.988  1.00 105.52 ? 103 THR   F C     1 
ATOM   12106 O  O     . THR   E 4  103 ? 33.598  54.806  98.894  1.00 105.57 ? 103 THR   F O     1 
ATOM   12107 C  CB    . THR   E 4  103 ? 32.810  55.119  102.333 1.00 106.63 ? 103 THR   F CB    1 
ATOM   12108 O  OG1   . THR   E 4  103 ? 34.192  55.484  102.364 1.00 106.88 ? 103 THR   F OG1   1 
ATOM   12109 C  CG2   . THR   E 4  103 ? 32.664  53.718  102.901 1.00 107.77 ? 103 THR   F CG2   1 
ATOM   12110 N  N     . THR   E 4  125 ? 28.201  65.572  99.097  1.00 113.54 ? 125 THR   F N     1 
ATOM   12111 C  CA    . THR   E 4  125 ? 26.861  66.142  98.976  1.00 121.56 ? 125 THR   F CA    1 
ATOM   12112 C  C     . THR   E 4  125 ? 25.781  65.129  99.366  1.00 119.19 ? 125 THR   F C     1 
ATOM   12113 O  O     . THR   E 4  125 ? 24.662  65.170  98.845  1.00 107.71 ? 125 THR   F O     1 
ATOM   12114 C  CB    . THR   E 4  125 ? 26.580  66.647  97.541  1.00 119.86 ? 125 THR   F CB    1 
ATOM   12115 O  OG1   . THR   E 4  125 ? 26.556  65.539  96.632  1.00 119.79 ? 125 THR   F OG1   1 
ATOM   12116 C  CG2   . THR   E 4  125 ? 27.649  67.638  97.096  1.00 112.02 ? 125 THR   F CG2   1 
ATOM   12117 N  N     . ASP   E 4  126 ? 26.120  64.213  100.275 1.00 111.53 ? 126 ASP   F N     1 
ATOM   12118 C  CA    . ASP   E 4  126 ? 25.140  63.298  100.832 1.00 109.53 ? 126 ASP   F CA    1 
ATOM   12119 C  C     . ASP   E 4  126 ? 24.821  63.715  102.269 1.00 104.57 ? 126 ASP   F C     1 
ATOM   12120 O  O     . ASP   E 4  126 ? 25.057  64.869  102.660 1.00 99.41  ? 126 ASP   F O     1 
ATOM   12121 C  CB    . ASP   E 4  126 ? 25.636  61.852  100.726 1.00 107.66 ? 126 ASP   F CB    1 
ATOM   12122 C  CG    . ASP   E 4  126 ? 26.865  61.584  101.564 1.00 104.76 ? 126 ASP   F CG    1 
ATOM   12123 O  OD1   . ASP   E 4  126 ? 27.438  62.548  102.109 1.00 113.99 ? 126 ASP   F OD1   1 
ATOM   12124 O  OD2   . ASP   E 4  126 ? 27.259  60.402  101.674 1.00 96.40  ? 126 ASP   F OD2   1 
ATOM   12125 N  N     . GLU   E 4  127 ? 24.280  62.777  103.055 1.00 99.91  ? 127 GLU   F N     1 
ATOM   12126 C  CA    . GLU   E 4  127 ? 23.720  63.120  104.358 1.00 102.44 ? 127 GLU   F CA    1 
ATOM   12127 C  C     . GLU   E 4  127 ? 23.984  62.028  105.393 1.00 105.36 ? 127 GLU   F C     1 
ATOM   12128 O  O     . GLU   E 4  127 ? 23.210  61.872  106.344 1.00 100.15 ? 127 GLU   F O     1 
ATOM   12129 C  CB    . GLU   E 4  127 ? 22.211  63.389  104.250 1.00 90.64  ? 127 GLU   F CB    1 
ATOM   12130 C  CG    . GLU   E 4  127 ? 21.752  63.912  102.878 1.00 83.83  ? 127 GLU   F CG    1 
ATOM   12131 C  CD    . GLU   E 4  127 ? 20.258  64.219  102.808 1.00 76.86  ? 127 GLU   F CD    1 
ATOM   12132 O  OE1   . GLU   E 4  127 ? 19.842  65.316  103.235 1.00 53.05  ? 127 GLU   F OE1   1 
ATOM   12133 O  OE2   . GLU   E 4  127 ? 19.490  63.359  102.324 1.00 80.19  ? 127 GLU   F OE2   1 
ATOM   12134 N  N     . ARG   E 4  128 ? 25.070  61.267  105.229 1.00 106.20 ? 128 ARG   F N     1 
ATOM   12135 C  CA    . ARG   E 4  128 ? 25.407  60.239  106.211 1.00 106.81 ? 128 ARG   F CA    1 
ATOM   12136 C  C     . ARG   E 4  128 ? 25.708  60.844  107.579 1.00 96.07  ? 128 ARG   F C     1 
ATOM   12137 O  O     . ARG   E 4  128 ? 25.497  60.191  108.608 1.00 89.37  ? 128 ARG   F O     1 
ATOM   12138 C  CB    . ARG   E 4  128 ? 26.603  59.423  105.722 1.00 107.24 ? 128 ARG   F CB    1 
ATOM   12139 C  CG    . ARG   E 4  128 ? 27.928  59.886  106.309 1.00 111.79 ? 128 ARG   F CG    1 
ATOM   12140 C  CD    . ARG   E 4  128 ? 29.116  59.322  105.553 1.00 104.74 ? 128 ARG   F CD    1 
ATOM   12141 N  NE    . ARG   E 4  128 ? 28.989  57.889  105.332 1.00 99.52  ? 128 ARG   F NE    1 
ATOM   12142 C  CZ    . ARG   E 4  128 ? 28.548  57.348  104.207 1.00 104.81 ? 128 ARG   F CZ    1 
ATOM   12143 N  NH1   . ARG   E 4  128 ? 28.187  58.097  103.177 1.00 107.87 ? 128 ARG   F NH1   1 
ATOM   12144 N  NH2   . ARG   E 4  128 ? 28.474  56.024  104.109 1.00 106.81 ? 128 ARG   F NH2   1 
ATOM   12145 N  N     . GLU   E 4  129 ? 26.216  62.083  107.600 1.00 92.94  ? 129 GLU   F N     1 
ATOM   12146 C  CA    . GLU   E 4  129 ? 26.475  62.809  108.841 1.00 101.91 ? 129 GLU   F CA    1 
ATOM   12147 C  C     . GLU   E 4  129 ? 25.219  63.516  109.338 1.00 106.67 ? 129 GLU   F C     1 
ATOM   12148 O  O     . GLU   E 4  129 ? 24.881  63.439  110.526 1.00 108.27 ? 129 GLU   F O     1 
ATOM   12149 C  CB    . GLU   E 4  129 ? 27.602  63.820  108.628 1.00 108.68 ? 129 GLU   F CB    1 
ATOM   12150 C  CG    . GLU   E 4  129 ? 27.865  64.731  109.822 1.00 120.32 ? 129 GLU   F CG    1 
ATOM   12151 C  CD    . GLU   E 4  129 ? 28.287  66.137  109.412 1.00 123.16 ? 129 GLU   F CD    1 
ATOM   12152 O  OE1   . GLU   E 4  129 ? 28.009  66.531  108.257 1.00 118.14 ? 129 GLU   F OE1   1 
ATOM   12153 O  OE2   . GLU   E 4  129 ? 28.895  66.847  110.246 1.00 113.64 ? 129 GLU   F OE2   1 
ATOM   12154 N  N     . VAL   E 4  130 ? 24.520  64.231  108.448 1.00 106.36 ? 130 VAL   F N     1 
ATOM   12155 C  CA    . VAL   E 4  130 ? 23.244  64.836  108.819 1.00 100.93 ? 130 VAL   F CA    1 
ATOM   12156 C  C     . VAL   E 4  130 ? 22.229  63.765  109.197 1.00 98.36  ? 130 VAL   F C     1 
ATOM   12157 O  O     . VAL   E 4  130 ? 21.239  64.058  109.880 1.00 94.05  ? 130 VAL   F O     1 
ATOM   12158 C  CB    . VAL   E 4  130 ? 22.716  65.731  107.672 1.00 93.22  ? 130 VAL   F CB    1 
ATOM   12159 C  CG1   . VAL   E 4  130 ? 21.574  66.618  108.152 1.00 55.28  ? 130 VAL   F CG1   1 
ATOM   12160 C  CG2   . VAL   E 4  130 ? 23.846  66.577  107.080 1.00 103.00 ? 130 VAL   F CG2   1 
ATOM   12161 N  N     . PHE   E 4  131 ? 22.462  62.515  108.772 1.00 102.54 ? 131 PHE   F N     1 
ATOM   12162 C  CA    . PHE   E 4  131 ? 21.566  61.411  109.114 1.00 99.76  ? 131 PHE   F CA    1 
ATOM   12163 C  C     . PHE   E 4  131 ? 21.721  60.999  110.572 1.00 102.85 ? 131 PHE   F C     1 
ATOM   12164 O  O     . PHE   E 4  131 ? 20.727  60.760  111.269 1.00 100.18 ? 131 PHE   F O     1 
ATOM   12165 C  CB    . PHE   E 4  131 ? 21.833  60.214  108.198 1.00 93.24  ? 131 PHE   F CB    1 
ATOM   12166 C  CG    . PHE   E 4  131 ? 21.512  58.883  108.830 1.00 108.07 ? 131 PHE   F CG    1 
ATOM   12167 C  CD1   . PHE   E 4  131 ? 20.215  58.388  108.826 1.00 106.39 ? 131 PHE   F CD1   1 
ATOM   12168 C  CD2   . PHE   E 4  131 ? 22.506  58.127  109.428 1.00 107.75 ? 131 PHE   F CD2   1 
ATOM   12169 C  CE1   . PHE   E 4  131 ? 19.917  57.169  109.403 1.00 89.52  ? 131 PHE   F CE1   1 
ATOM   12170 C  CE2   . PHE   E 4  131 ? 22.210  56.909  110.005 1.00 103.43 ? 131 PHE   F CE2   1 
ATOM   12171 C  CZ    . PHE   E 4  131 ? 20.914  56.432  109.990 1.00 97.54  ? 131 PHE   F CZ    1 
ATOM   12172 N  N     . LEU   E 4  132 ? 22.964  60.887  111.042 1.00 102.63 ? 132 LEU   F N     1 
ATOM   12173 C  CA    . LEU   E 4  132 ? 23.192  60.555  112.441 1.00 97.68  ? 132 LEU   F CA    1 
ATOM   12174 C  C     . LEU   E 4  132 ? 22.563  61.597  113.355 1.00 96.31  ? 132 LEU   F C     1 
ATOM   12175 O  O     . LEU   E 4  132 ? 21.994  61.254  114.396 1.00 106.57 ? 132 LEU   F O     1 
ATOM   12176 C  CB    . LEU   E 4  132 ? 24.691  60.428  112.700 1.00 88.43  ? 132 LEU   F CB    1 
ATOM   12177 C  CG    . LEU   E 4  132 ? 25.403  59.516  111.695 1.00 97.26  ? 132 LEU   F CG    1 
ATOM   12178 C  CD1   . LEU   E 4  132 ? 26.911  59.648  111.820 1.00 92.94  ? 132 LEU   F CD1   1 
ATOM   12179 C  CD2   . LEU   E 4  132 ? 24.961  58.061  111.859 1.00 82.79  ? 132 LEU   F CD2   1 
ATOM   12180 N  N     . ALA   E 4  133 ? 22.637  62.871  112.967 1.00 103.05 ? 133 ALA   F N     1 
ATOM   12181 C  CA    . ALA   E 4  133 ? 22.101  63.985  113.746 1.00 106.62 ? 133 ALA   F CA    1 
ATOM   12182 C  C     . ALA   E 4  133 ? 20.723  63.682  114.327 1.00 110.57 ? 133 ALA   F C     1 
ATOM   12183 O  O     . ALA   E 4  133 ? 20.596  63.410  115.526 1.00 110.82 ? 133 ALA   F O     1 
ATOM   12184 C  CB    . ALA   E 4  133 ? 22.041  65.249  112.885 1.00 100.08 ? 133 ALA   F CB    1 
ATOM   12185 N  N     . ALA   E 4  134 ? 19.682  63.728  113.490 1.00 110.21 ? 134 ALA   F N     1 
ATOM   12186 C  CA    . ALA   E 4  134 ? 18.332  63.431  113.954 1.00 106.64 ? 134 ALA   F CA    1 
ATOM   12187 C  C     . ALA   E 4  134 ? 18.173  61.989  114.430 1.00 108.04 ? 134 ALA   F C     1 
ATOM   12188 O  O     . ALA   E 4  134 ? 17.145  61.668  115.041 1.00 104.59 ? 134 ALA   F O     1 
ATOM   12189 C  CB    . ALA   E 4  134 ? 17.323  63.733  112.843 1.00 99.10  ? 134 ALA   F CB    1 
ATOM   12190 N  N     . TYR   E 4  135 ? 19.158  61.121  114.170 1.00 107.42 ? 135 TYR   F N     1 
ATOM   12191 C  CA    . TYR   E 4  135 ? 19.087  59.737  114.637 1.00 103.11 ? 135 TYR   F CA    1 
ATOM   12192 C  C     . TYR   E 4  135 ? 19.099  59.664  116.163 1.00 105.64 ? 135 TYR   F C     1 
ATOM   12193 O  O     . TYR   E 4  135 ? 18.399  58.836  116.758 1.00 102.24 ? 135 TYR   F O     1 
ATOM   12194 C  CB    . TYR   E 4  135 ? 20.241  58.932  114.033 1.00 102.85 ? 135 TYR   F CB    1 
ATOM   12195 C  CG    . TYR   E 4  135 ? 20.269  57.460  114.397 1.00 103.96 ? 135 TYR   F CG    1 
ATOM   12196 C  CD1   . TYR   E 4  135 ? 19.170  56.836  114.972 1.00 100.76 ? 135 TYR   F CD1   1 
ATOM   12197 C  CD2   . TYR   E 4  135 ? 21.405  56.698  114.171 1.00 106.38 ? 135 TYR   F CD2   1 
ATOM   12198 C  CE1   . TYR   E 4  135 ? 19.206  55.504  115.310 1.00 101.28 ? 135 TYR   F CE1   1 
ATOM   12199 C  CE2   . TYR   E 4  135 ? 21.448  55.364  114.506 1.00 100.91 ? 135 TYR   F CE2   1 
ATOM   12200 C  CZ    . TYR   E 4  135 ? 20.347  54.774  115.073 1.00 101.70 ? 135 TYR   F CZ    1 
ATOM   12201 O  OH    . TYR   E 4  135 ? 20.387  53.445  115.407 1.00 96.20  ? 135 TYR   F OH    1 
ATOM   12202 N  N     . ASN   E 4  136 ? 19.883  60.523  116.817 1.00 107.19 ? 136 ASN   F N     1 
ATOM   12203 C  CA    . ASN   E 4  136 ? 19.821  60.629  118.271 1.00 99.16  ? 136 ASN   F CA    1 
ATOM   12204 C  C     . ASN   E 4  136 ? 18.410  60.969  118.731 1.00 98.17  ? 136 ASN   F C     1 
ATOM   12205 O  O     . ASN   E 4  136 ? 18.030  62.143  118.813 1.00 78.98  ? 136 ASN   F O     1 
ATOM   12206 C  CB    . ASN   E 4  136 ? 20.815  61.669  118.776 1.00 100.00 ? 136 ASN   F CB    1 
ATOM   12207 C  CG    . ASN   E 4  136 ? 22.237  61.210  118.625 1.00 98.00  ? 136 ASN   F CG    1 
ATOM   12208 O  OD1   . ASN   E 4  136 ? 22.548  60.417  117.734 1.00 90.69  ? 136 ASN   F OD1   1 
ATOM   12209 N  ND2   . ASN   E 4  136 ? 23.110  61.683  119.507 1.00 97.02  ? 136 ASN   F ND2   1 
ATOM   12210 N  N     . ARG   E 4  137 ? 17.634  59.932  119.030 1.00 100.94 ? 137 ARG   F N     1 
ATOM   12211 C  CA    . ARG   E 4  137 ? 16.254  60.083  119.439 1.00 93.96  ? 137 ARG   F CA    1 
ATOM   12212 C  C     . ARG   E 4  137 ? 15.730  58.732  119.906 1.00 91.35  ? 137 ARG   F C     1 
ATOM   12213 O  O     . ARG   E 4  137 ? 16.516  57.857  120.277 1.00 90.61  ? 137 ARG   F O     1 
ATOM   12214 C  CB    . ARG   E 4  137 ? 15.416  60.632  118.287 1.00 100.74 ? 137 ARG   F CB    1 
ATOM   12215 C  CG    . ARG   E 4  137 ? 14.442  61.724  118.691 1.00 106.54 ? 137 ARG   F CG    1 
ATOM   12216 C  CD    . ARG   E 4  137 ? 13.048  61.173  118.963 1.00 108.29 ? 137 ARG   F CD    1 
ATOM   12217 N  NE    . ARG   E 4  137 ? 12.113  62.234  119.316 1.00 110.12 ? 137 ARG   F NE    1 
ATOM   12218 C  CZ    . ARG   E 4  137 ? 10.808  62.065  119.483 1.00 113.60 ? 137 ARG   F CZ    1 
ATOM   12219 N  NH1   . ARG   E 4  137 ? 10.236  60.882  119.322 1.00 106.71 ? 137 ARG   F NH1   1 
ATOM   12220 N  NH2   . ARG   E 4  137 ? 10.058  63.110  119.820 1.00 119.15 ? 137 ARG   F NH2   1 
ATOM   12221 N  N     . GLY   E 4  144 ? 12.773  55.934  119.421 1.00 66.02  ? 144 GLY   F N     1 
ATOM   12222 C  CA    . GLY   E 4  144 ? 12.516  54.600  118.898 1.00 83.73  ? 144 GLY   F CA    1 
ATOM   12223 C  C     . GLY   E 4  144 ? 12.896  54.407  117.437 1.00 83.80  ? 144 GLY   F C     1 
ATOM   12224 O  O     . GLY   E 4  144 ? 12.041  54.203  116.579 1.00 72.22  ? 144 GLY   F O     1 
ATOM   12225 N  N     . ASN   E 4  145 ? 14.196  54.425  117.159 1.00 92.02  ? 145 ASN   F N     1 
ATOM   12226 C  CA    . ASN   E 4  145 ? 14.709  54.603  115.803 1.00 91.93  ? 145 ASN   F CA    1 
ATOM   12227 C  C     . ASN   E 4  145 ? 14.789  53.269  115.065 1.00 86.61  ? 145 ASN   F C     1 
ATOM   12228 O  O     . ASN   E 4  145 ? 15.599  52.406  115.413 1.00 97.53  ? 145 ASN   F O     1 
ATOM   12229 C  CB    . ASN   E 4  145 ? 16.079  55.276  115.859 1.00 92.76  ? 145 ASN   F CB    1 
ATOM   12230 C  CG    . ASN   E 4  145 ? 16.049  56.583  116.628 1.00 101.69 ? 145 ASN   F CG    1 
ATOM   12231 O  OD1   . ASN   E 4  145 ? 15.799  56.603  117.837 1.00 105.58 ? 145 ASN   F OD1   1 
ATOM   12232 N  ND2   . ASN   E 4  145 ? 16.298  57.686  115.930 1.00 108.57 ? 145 ASN   F ND2   1 
ATOM   12233 N  N     . VAL   E 4  146 ? 13.966  53.112  114.031 1.00 81.21  ? 146 VAL   F N     1 
ATOM   12234 C  CA    . VAL   E 4  146 ? 14.091  52.023  113.066 1.00 84.68  ? 146 VAL   F CA    1 
ATOM   12235 C  C     . VAL   E 4  146 ? 14.109  52.625  111.664 1.00 84.71  ? 146 VAL   F C     1 
ATOM   12236 O  O     . VAL   E 4  146 ? 13.336  53.541  111.364 1.00 83.34  ? 146 VAL   F O     1 
ATOM   12237 C  CB    . VAL   E 4  146 ? 12.946  50.997  113.198 1.00 83.48  ? 146 VAL   F CB    1 
ATOM   12238 C  CG1   . VAL   E 4  146 ? 13.073  49.911  112.135 1.00 76.19  ? 146 VAL   F CG1   1 
ATOM   12239 C  CG2   . VAL   E 4  146 ? 12.939  50.392  114.580 1.00 80.53  ? 146 VAL   F CG2   1 
ATOM   12240 N  N     . TRP   E 4  147 ? 14.992  52.112  110.804 1.00 84.46  ? 147 TRP   F N     1 
ATOM   12241 C  CA    . TRP   E 4  147 ? 15.145  52.657  109.458 1.00 80.47  ? 147 TRP   F CA    1 
ATOM   12242 C  C     . TRP   E 4  147 ? 15.165  51.532  108.424 1.00 79.59  ? 147 TRP   F C     1 
ATOM   12243 O  O     . TRP   E 4  147 ? 14.915  50.374  108.773 1.00 82.13  ? 147 TRP   F O     1 
ATOM   12244 C  CB    . TRP   E 4  147 ? 16.406  53.529  109.388 1.00 80.12  ? 147 TRP   F CB    1 
ATOM   12245 C  CG    . TRP   E 4  147 ? 16.384  54.655  110.406 1.00 88.09  ? 147 TRP   F CG    1 
ATOM   12246 C  CD1   . TRP   E 4  147 ? 16.622  54.551  111.748 1.00 94.94  ? 147 TRP   F CD1   1 
ATOM   12247 C  CD2   . TRP   E 4  147 ? 16.090  56.037  110.164 1.00 94.01  ? 147 TRP   F CD2   1 
ATOM   12248 N  NE1   . TRP   E 4  147 ? 16.498  55.778  112.355 1.00 85.71  ? 147 TRP   F NE1   1 
ATOM   12249 C  CE2   . TRP   E 4  147 ? 16.174  56.707  111.405 1.00 88.68  ? 147 TRP   F CE2   1 
ATOM   12250 C  CE3   . TRP   E 4  147 ? 15.769  56.773  109.021 1.00 89.93  ? 147 TRP   F CE3   1 
ATOM   12251 C  CZ2   . TRP   E 4  147 ? 15.948  58.073  111.532 1.00 83.82  ? 147 TRP   F CZ2   1 
ATOM   12252 C  CZ3   . TRP   E 4  147 ? 15.544  58.129  109.151 1.00 88.11  ? 147 TRP   F CZ3   1 
ATOM   12253 C  CH2   . TRP   E 4  147 ? 15.637  58.766  110.400 1.00 82.20  ? 147 TRP   F CH2   1 
ATOM   12254 N  N     . ILE   E 4  148 ? 15.427  51.855  107.152 1.00 86.82  ? 148 ILE   F N     1 
ATOM   12255 C  CA    . ILE   E 4  148 ? 15.395  50.873  106.068 1.00 77.84  ? 148 ILE   F CA    1 
ATOM   12256 C  C     . ILE   E 4  148 ? 16.301  51.345  104.933 1.00 77.49  ? 148 ILE   F C     1 
ATOM   12257 O  O     . ILE   E 4  148 ? 16.484  52.546  104.717 1.00 83.52  ? 148 ILE   F O     1 
ATOM   12258 C  CB    . ILE   E 4  148 ? 13.949  50.619  105.567 1.00 69.58  ? 148 ILE   F CB    1 
ATOM   12259 C  CG1   . ILE   E 4  148 ? 13.949  49.595  104.423 1.00 77.68  ? 148 ILE   F CG1   1 
ATOM   12260 C  CG2   . ILE   E 4  148 ? 13.300  51.912  105.125 1.00 69.13  ? 148 ILE   F CG2   1 
ATOM   12261 C  CD1   . ILE   E 4  148 ? 12.608  48.925  104.155 1.00 57.67  ? 148 ILE   F CD1   1 
ATOM   12262 N  N     . ALA   E 4  149 ? 16.864  50.381  104.199 1.00 86.28  ? 149 ALA   F N     1 
ATOM   12263 C  CA    . ALA   E 4  149 ? 17.809  50.642  103.101 1.00 80.34  ? 149 ALA   F CA    1 
ATOM   12264 C  C     . ALA   E 4  149 ? 17.137  51.218  101.851 1.00 86.62  ? 149 ALA   F C     1 
ATOM   12265 O  O     . ALA   E 4  149 ? 17.725  51.259  100.764 1.00 76.25  ? 149 ALA   F O     1 
ATOM   12266 C  CB    . ALA   E 4  149 ? 18.544  49.369  102.747 1.00 79.38  ? 149 ALA   F CB    1 
ATOM   12267 N  N     . GLY   E 4  159 ? 17.143  42.886  98.503  1.00 81.32  ? 159 GLY   F N     1 
ATOM   12268 C  CA    . GLY   E 4  159 ? 18.012  43.990  98.140  1.00 79.69  ? 159 GLY   F CA    1 
ATOM   12269 C  C     . GLY   E 4  159 ? 17.970  45.161  99.105  1.00 91.13  ? 159 GLY   F C     1 
ATOM   12270 O  O     . GLY   E 4  159 ? 18.789  46.075  99.003  1.00 89.22  ? 159 GLY   F O     1 
ATOM   12271 N  N     . ILE   E 4  160 ? 17.019  45.135  100.033 1.00 100.26 ? 160 ILE   F N     1 
ATOM   12272 C  CA    . ILE   E 4  160 ? 16.887  46.171  101.057 1.00 103.81 ? 160 ILE   F CA    1 
ATOM   12273 C  C     . ILE   E 4  160 ? 17.425  45.640  102.381 1.00 99.08  ? 160 ILE   F C     1 
ATOM   12274 O  O     . ILE   E 4  160 ? 17.751  44.463  102.517 1.00 100.89 ? 160 ILE   F O     1 
ATOM   12275 C  CB    . ILE   E 4  160 ? 15.415  46.659  101.219 1.00 97.82  ? 160 ILE   F CB    1 
ATOM   12276 C  CG1   . ILE   E 4  160 ? 14.425  45.735  100.490 1.00 94.87  ? 160 ILE   F CG1   1 
ATOM   12277 C  CG2   . ILE   E 4  160 ? 15.269  48.118  100.784 1.00 95.30  ? 160 ILE   F CG2   1 
ATOM   12278 C  CD1   . ILE   E 4  160 ? 14.399  45.883  98.974  1.00 81.79  ? 160 ILE   F CD1   1 
ATOM   12279 N  N     . LEU   E 4  161 ? 17.501  46.513  103.386 1.00 89.94  ? 161 LEU   F N     1 
ATOM   12280 C  CA    . LEU   E 4  161 ? 17.963  46.066  104.698 1.00 93.84  ? 161 LEU   F CA    1 
ATOM   12281 C  C     . LEU   E 4  161 ? 17.485  47.028  105.776 1.00 97.93  ? 161 LEU   F C     1 
ATOM   12282 O  O     . LEU   E 4  161 ? 17.840  48.212  105.747 1.00 99.46  ? 161 LEU   F O     1 
ATOM   12283 C  CB    . LEU   E 4  161 ? 19.482  45.944  104.717 1.00 97.09  ? 161 LEU   F CB    1 
ATOM   12284 C  CG    . LEU   E 4  161 ? 20.002  44.913  105.719 1.00 95.83  ? 161 LEU   F CG    1 
ATOM   12285 C  CD1   . LEU   E 4  161 ? 19.768  45.381  107.146 1.00 74.30  ? 161 LEU   F CD1   1 
ATOM   12286 C  CD2   . LEU   E 4  161 ? 19.339  43.558  105.476 1.00 87.67  ? 161 LEU   F CD2   1 
ATOM   12287 N  N     . ILE   E 4  162 ? 16.706  46.502  106.748 1.00 92.93  ? 162 ILE   F N     1 
ATOM   12288 C  CA    . ILE   E 4  162 ? 16.128  47.262  107.857 1.00 92.74  ? 162 ILE   F CA    1 
ATOM   12289 C  C     . ILE   E 4  162 ? 16.910  46.976  109.136 1.00 99.12  ? 162 ILE   F C     1 
ATOM   12290 O  O     . ILE   E 4  162 ? 17.502  45.903  109.296 1.00 105.69 ? 162 ILE   F O     1 
ATOM   12291 C  CB    . ILE   E 4  162 ? 14.633  46.912  108.034 1.00 85.43  ? 162 ILE   F CB    1 
ATOM   12292 C  CG1   . ILE   E 4  162 ? 14.418  45.398  107.941 1.00 101.73 ? 162 ILE   F CG1   1 
ATOM   12293 C  CG2   . ILE   E 4  162 ? 13.801  47.569  106.975 1.00 82.49  ? 162 ILE   F CG2   1 
ATOM   12294 C  CD1   . ILE   E 4  162 ? 14.933  44.614  109.134 1.00 112.17 ? 162 ILE   F CD1   1 
ATOM   12295 N  N     . SER   E 4  163 ? 16.905  47.929  110.066 1.00 92.63  ? 163 SER   F N     1 
ATOM   12296 C  CA    . SER   E 4  163 ? 17.569  47.734  111.352 1.00 91.54  ? 163 SER   F CA    1 
ATOM   12297 C  C     . SER   E 4  163 ? 17.066  48.767  112.355 1.00 95.13  ? 163 SER   F C     1 
ATOM   12298 O  O     . SER   E 4  163 ? 16.126  49.522  112.086 1.00 95.20  ? 163 SER   F O     1 
ATOM   12299 C  CB    . SER   E 4  163 ? 19.089  47.817  111.220 1.00 105.23 ? 163 SER   F CB    1 
ATOM   12300 O  OG    . SER   E 4  163 ? 19.678  48.043  112.493 1.00 110.65 ? 163 SER   F OG    1 
ATOM   12301 N  N     . SER   E 4  164 ? 17.717  48.803  113.519 1.00 98.44  ? 164 SER   F N     1 
ATOM   12302 C  CA    . SER   E 4  164 ? 17.316  49.661  114.625 1.00 97.10  ? 164 SER   F CA    1 
ATOM   12303 C  C     . SER   E 4  164 ? 18.479  50.536  115.082 1.00 98.49  ? 164 SER   F C     1 
ATOM   12304 O  O     . SER   E 4  164 ? 18.275  51.662  115.546 1.00 99.00  ? 164 SER   F O     1 
ATOM   12305 C  CB    . SER   E 4  164 ? 16.789  48.808  115.782 1.00 99.05  ? 164 SER   F CB    1 
ATOM   12306 O  OG    . SER   E 4  164 ? 16.553  49.595  116.936 1.00 102.08 ? 164 SER   F OG    1 
ATOM   12307 N  N     . GLU   E 4  165 ? 19.702  50.028  114.972 1.00 98.30  ? 165 GLU   F N     1 
ATOM   12308 C  CA    . GLU   E 4  165 ? 20.894  50.822  115.226 1.00 104.61 ? 165 GLU   F CA    1 
ATOM   12309 C  C     . GLU   E 4  165 ? 21.673  50.941  113.924 1.00 111.51 ? 165 GLU   F C     1 
ATOM   12310 O  O     . GLU   E 4  165 ? 21.756  49.979  113.152 1.00 107.47 ? 165 GLU   F O     1 
ATOM   12311 C  CB    . GLU   E 4  165 ? 21.772  50.220  116.345 1.00 104.78 ? 165 GLU   F CB    1 
ATOM   12312 C  CG    . GLU   E 4  165 ? 22.822  51.199  116.905 1.00 108.20 ? 165 GLU   F CG    1 
ATOM   12313 C  CD    . GLU   E 4  165 ? 23.246  50.897  118.344 1.00 110.06 ? 165 GLU   F CD    1 
ATOM   12314 O  OE1   . GLU   E 4  165 ? 23.056  49.745  118.794 1.00 109.42 ? 165 GLU   F OE1   1 
ATOM   12315 O  OE2   . GLU   E 4  165 ? 23.769  51.817  119.025 1.00 95.15  ? 165 GLU   F OE2   1 
ATOM   12316 N  N     . ALA   E 4  166 ? 22.214  52.137  113.677 1.00 113.32 ? 166 ALA   F N     1 
ATOM   12317 C  CA    . ALA   E 4  166 ? 22.863  52.471  112.412 1.00 109.27 ? 166 ALA   F CA    1 
ATOM   12318 C  C     . ALA   E 4  166 ? 23.921  51.444  112.029 1.00 116.78 ? 166 ALA   F C     1 
ATOM   12319 O  O     . ALA   E 4  166 ? 23.587  50.327  111.619 1.00 115.36 ? 166 ALA   F O     1 
ATOM   12320 C  CB    . ALA   E 4  166 ? 23.488  53.865  112.490 1.00 95.18  ? 166 ALA   F CB    1 
ATOM   12321 N  N     . SER   E 4  167 ? 25.194  51.831  112.137 1.00 112.79 ? 167 SER   F N     1 
ATOM   12322 C  CA    . SER   E 4  167 ? 26.326  50.932  111.937 1.00 117.43 ? 167 SER   F CA    1 
ATOM   12323 C  C     . SER   E 4  167 ? 26.041  49.881  110.868 1.00 115.05 ? 167 SER   F C     1 
ATOM   12324 O  O     . SER   E 4  167 ? 26.482  50.010  109.722 1.00 110.48 ? 167 SER   F O     1 
ATOM   12325 C  CB    . SER   E 4  167 ? 26.698  50.253  113.261 1.00 118.00 ? 167 SER   F CB    1 
ATOM   12326 O  OG    . SER   E 4  167 ? 26.917  51.203  114.294 1.00 105.72 ? 167 SER   F OG    1 
ATOM   12327 N  N     . GLU   E 4  168 ? 25.287  48.843  111.244 1.00 120.08 ? 168 GLU   F N     1 
ATOM   12328 C  CA    . GLU   E 4  168 ? 24.959  47.772  110.310 1.00 115.52 ? 168 GLU   F CA    1 
ATOM   12329 C  C     . GLU   E 4  168 ? 24.329  48.317  109.036 1.00 116.01 ? 168 GLU   F C     1 
ATOM   12330 O  O     . GLU   E 4  168 ? 24.680  47.890  107.931 1.00 116.83 ? 168 GLU   F O     1 
ATOM   12331 C  CB    . GLU   E 4  168 ? 24.028  46.763  110.985 1.00 109.15 ? 168 GLU   F CB    1 
ATOM   12332 C  CG    . GLU   E 4  168 ? 23.107  47.382  112.024 1.00 115.51 ? 168 GLU   F CG    1 
ATOM   12333 C  CD    . GLU   E 4  168 ? 22.067  46.409  112.548 1.00 115.95 ? 168 GLU   F CD    1 
ATOM   12334 O  OE1   . GLU   E 4  168 ? 21.832  45.374  111.891 1.00 111.89 ? 168 GLU   F OE1   1 
ATOM   12335 O  OE2   . GLU   E 4  168 ? 21.480  46.683  113.616 1.00 112.57 ? 168 GLU   F OE2   1 
ATOM   12336 N  N     . LEU   E 4  169 ? 23.396  49.263  109.168 1.00 121.94 ? 169 LEU   F N     1 
ATOM   12337 C  CA    . LEU   E 4  169 ? 22.773  49.865  107.992 1.00 118.21 ? 169 LEU   F CA    1 
ATOM   12338 C  C     . LEU   E 4  169 ? 23.806  50.593  107.137 1.00 115.74 ? 169 LEU   F C     1 
ATOM   12339 O  O     . LEU   E 4  169 ? 24.009  50.258  105.963 1.00 107.96 ? 169 LEU   F O     1 
ATOM   12340 C  CB    . LEU   E 4  169 ? 21.645  50.813  108.416 1.00 112.67 ? 169 LEU   F CB    1 
ATOM   12341 C  CG    . LEU   E 4  169 ? 20.280  50.170  108.689 1.00 103.27 ? 169 LEU   F CG    1 
ATOM   12342 C  CD1   . LEU   E 4  169 ? 19.172  51.212  108.738 1.00 77.27  ? 169 LEU   F CD1   1 
ATOM   12343 C  CD2   . LEU   E 4  169 ? 19.974  49.094  107.651 1.00 97.35  ? 169 LEU   F CD2   1 
ATOM   12344 N  N     . LEU   E 4  170 ? 24.466  51.606  107.713 1.00 115.81 ? 170 LEU   F N     1 
ATOM   12345 C  CA    . LEU   E 4  170 ? 25.528  52.308  106.997 1.00 112.58 ? 170 LEU   F CA    1 
ATOM   12346 C  C     . LEU   E 4  170 ? 26.562  51.332  106.450 1.00 115.14 ? 170 LEU   F C     1 
ATOM   12347 O  O     . LEU   E 4  170 ? 27.073  51.514  105.338 1.00 110.41 ? 170 LEU   F O     1 
ATOM   12348 C  CB    . LEU   E 4  170 ? 26.197  53.332  107.916 1.00 112.79 ? 170 LEU   F CB    1 
ATOM   12349 C  CG    . LEU   E 4  170 ? 25.471  54.652  108.182 1.00 108.04 ? 170 LEU   F CG    1 
ATOM   12350 C  CD1   . LEU   E 4  170 ? 26.055  55.335  109.406 1.00 103.54 ? 170 LEU   F CD1   1 
ATOM   12351 C  CD2   . LEU   E 4  170 ? 25.565  55.566  106.972 1.00 105.55 ? 170 LEU   F CD2   1 
ATOM   12352 N  N     . ASP   E 4  171 ? 26.884  50.288  107.222 1.00 115.93 ? 171 ASP   F N     1 
ATOM   12353 C  CA    . ASP   E 4  171 ? 27.792  49.253  106.734 1.00 119.25 ? 171 ASP   F CA    1 
ATOM   12354 C  C     . ASP   E 4  171 ? 27.250  48.590  105.468 1.00 118.99 ? 171 ASP   F C     1 
ATOM   12355 O  O     . ASP   E 4  171 ? 28.003  48.335  104.519 1.00 112.98 ? 171 ASP   F O     1 
ATOM   12356 C  CB    . ASP   E 4  171 ? 28.032  48.207  107.827 1.00 116.45 ? 171 ASP   F CB    1 
ATOM   12357 C  CG    . ASP   E 4  171 ? 28.790  48.764  109.021 1.00 113.21 ? 171 ASP   F CG    1 
ATOM   12358 O  OD1   . ASP   E 4  171 ? 29.594  49.705  108.843 1.00 103.54 ? 171 ASP   F OD1   1 
ATOM   12359 O  OD2   . ASP   E 4  171 ? 28.577  48.255  110.142 1.00 106.77 ? 171 ASP   F OD2   1 
ATOM   12360 N  N     . PHE   E 4  172 ? 25.943  48.307  105.436 1.00 120.30 ? 172 PHE   F N     1 
ATOM   12361 C  CA    . PHE   E 4  172 ? 25.352  47.636  104.280 1.00 113.97 ? 172 PHE   F CA    1 
ATOM   12362 C  C     . PHE   E 4  172 ? 25.557  48.450  103.010 1.00 111.21 ? 172 PHE   F C     1 
ATOM   12363 O  O     . PHE   E 4  172 ? 26.069  47.941  102.006 1.00 105.02 ? 172 PHE   F O     1 
ATOM   12364 C  CB    . PHE   E 4  172 ? 23.861  47.378  104.521 1.00 106.28 ? 172 PHE   F CB    1 
ATOM   12365 C  CG    . PHE   E 4  172 ? 23.162  46.726  103.355 1.00 106.15 ? 172 PHE   F CG    1 
ATOM   12366 C  CD1   . PHE   E 4  172 ? 23.594  45.503  102.866 1.00 106.95 ? 172 PHE   F CD1   1 
ATOM   12367 C  CD2   . PHE   E 4  172 ? 22.071  47.334  102.752 1.00 103.35 ? 172 PHE   F CD2   1 
ATOM   12368 C  CE1   . PHE   E 4  172 ? 22.956  44.903  101.793 1.00 107.58 ? 172 PHE   F CE1   1 
ATOM   12369 C  CE2   . PHE   E 4  172 ? 21.429  46.738  101.681 1.00 101.42 ? 172 PHE   F CE2   1 
ATOM   12370 C  CZ    . PHE   E 4  172 ? 21.872  45.522  101.201 1.00 103.64 ? 172 PHE   F CZ    1 
ATOM   12371 N  N     . ILE   E 4  173 ? 25.155  49.723  103.035 1.00 113.21 ? 173 ILE   F N     1 
ATOM   12372 C  CA    . ILE   E 4  173 ? 25.320  50.570  101.861 1.00 106.13 ? 173 ILE   F CA    1 
ATOM   12373 C  C     . ILE   E 4  173 ? 26.784  50.650  101.461 1.00 112.83 ? 173 ILE   F C     1 
ATOM   12374 O  O     . ILE   E 4  173 ? 27.106  50.739  100.271 1.00 114.42 ? 173 ILE   F O     1 
ATOM   12375 C  CB    . ILE   E 4  173 ? 24.728  51.966  102.122 1.00 100.65 ? 173 ILE   F CB    1 
ATOM   12376 C  CG1   . ILE   E 4  173 ? 23.249  51.856  102.487 1.00 97.14  ? 173 ILE   F CG1   1 
ATOM   12377 C  CG2   . ILE   E 4  173 ? 24.916  52.855  100.906 1.00 107.71 ? 173 ILE   F CG2   1 
ATOM   12378 C  CD1   . ILE   E 4  173 ? 22.569  53.196  102.689 1.00 99.55  ? 173 ILE   F CD1   1 
ATOM   12379 N  N     . ASP   E 4  174 ? 27.695  50.615  102.438 1.00 114.86 ? 174 ASP   F N     1 
ATOM   12380 C  CA    . ASP   E 4  174 ? 29.118  50.594  102.122 1.00 110.42 ? 174 ASP   F CA    1 
ATOM   12381 C  C     . ASP   E 4  174 ? 29.532  49.302  101.432 1.00 109.69 ? 174 ASP   F C     1 
ATOM   12382 O  O     . ASP   E 4  174 ? 30.539  49.294  100.716 1.00 102.57 ? 174 ASP   F O     1 
ATOM   12383 C  CB    . ASP   E 4  174 ? 29.939  50.806  103.392 1.00 110.71 ? 174 ASP   F CB    1 
ATOM   12384 C  CG    . ASP   E 4  174 ? 29.803  52.210  103.944 1.00 99.77  ? 174 ASP   F CG    1 
ATOM   12385 O  OD1   . ASP   E 4  174 ? 29.991  53.179  103.182 1.00 96.17  ? 174 ASP   F OD1   1 
ATOM   12386 O  OD2   . ASP   E 4  174 ? 29.498  52.346  105.142 1.00 107.31 ? 174 ASP   F OD2   1 
ATOM   12387 N  N     . GLU   E 4  175 ? 28.777  48.219  101.631 1.00 115.57 ? 175 GLU   F N     1 
ATOM   12388 C  CA    . GLU   E 4  175 ? 28.963  46.981  100.883 1.00 108.67 ? 175 GLU   F CA    1 
ATOM   12389 C  C     . GLU   E 4  175 ? 28.795  47.218  99.386  1.00 106.05 ? 175 GLU   F C     1 
ATOM   12390 O  O     . GLU   E 4  175 ? 29.775  47.165  98.639  1.00 111.62 ? 175 GLU   F O     1 
ATOM   12391 C  CB    . GLU   E 4  175 ? 27.983  45.909  101.364 1.00 112.24 ? 175 GLU   F CB    1 
ATOM   12392 C  CG    . GLU   E 4  175 ? 28.490  45.086  102.533 1.00 116.97 ? 175 GLU   F CG    1 
ATOM   12393 C  CD    . GLU   E 4  175 ? 28.489  43.600  102.230 1.00 120.29 ? 175 GLU   F CD    1 
ATOM   12394 O  OE1   . GLU   E 4  175 ? 27.429  43.078  101.821 1.00 111.44 ? 175 GLU   F OE1   1 
ATOM   12395 O  OE2   . GLU   E 4  175 ? 29.552  42.958  102.384 1.00 116.62 ? 175 GLU   F OE2   1 
ATOM   12396 N  N     . GLN   E 4  176 ? 27.565  47.470  98.934  1.00 111.13 ? 176 GLN   F N     1 
ATOM   12397 C  CA    . GLN   E 4  176 ? 27.342  47.813  97.535  1.00 114.50 ? 176 GLN   F CA    1 
ATOM   12398 C  C     . GLN   E 4  176 ? 27.881  49.214  97.250  1.00 113.95 ? 176 GLN   F C     1 
ATOM   12399 O  O     . GLN   E 4  176 ? 28.445  49.885  98.119  1.00 110.05 ? 176 GLN   F O     1 
ATOM   12400 C  CB    . GLN   E 4  176 ? 25.860  47.721  97.176  1.00 110.67 ? 176 GLN   F CB    1 
ATOM   12401 C  CG    . GLN   E 4  176 ? 25.272  46.330  97.262  1.00 97.55  ? 176 GLN   F CG    1 
ATOM   12402 C  CD    . GLN   E 4  176 ? 24.225  46.227  98.342  1.00 98.33  ? 176 GLN   F CD    1 
ATOM   12403 O  OE1   . GLN   E 4  176 ? 23.027  46.232  98.060  1.00 103.42 ? 176 GLN   F OE1   1 
ATOM   12404 N  NE2   . GLN   E 4  176 ? 24.668  46.145  99.591  1.00 92.75  ? 176 GLN   F NE2   1 
ATOM   12405 N  N     . GLY   E 4  177 ? 27.694  49.668  96.014  1.00 124.44 ? 177 GLY   F N     1 
ATOM   12406 C  CA    . GLY   E 4  177 ? 28.324  50.899  95.577  1.00 127.33 ? 177 GLY   F CA    1 
ATOM   12407 C  C     . GLY   E 4  177 ? 27.407  51.940  94.965  1.00 130.21 ? 177 GLY   F C     1 
ATOM   12408 O  O     . GLY   E 4  177 ? 27.847  53.056  94.672  1.00 132.04 ? 177 GLY   F O     1 
ATOM   12409 N  N     . GLN   E 4  178 ? 26.138  51.603  94.766  1.00 128.32 ? 178 GLN   F N     1 
ATOM   12410 C  CA    . GLN   E 4  178 ? 25.178  52.550  94.220  1.00 124.52 ? 178 GLN   F CA    1 
ATOM   12411 C  C     . GLN   E 4  178 ? 24.577  53.380  95.348  1.00 119.08 ? 178 GLN   F C     1 
ATOM   12412 O  O     . GLN   E 4  178 ? 24.404  52.897  96.472  1.00 115.85 ? 178 GLN   F O     1 
ATOM   12413 C  CB    . GLN   E 4  178 ? 24.075  51.827  93.442  1.00 118.54 ? 178 GLN   F CB    1 
ATOM   12414 C  CG    . GLN   E 4  178 ? 24.583  50.909  92.332  1.00 122.75 ? 178 GLN   F CG    1 
ATOM   12415 C  CD    . GLN   E 4  178 ? 25.283  49.666  92.864  1.00 122.57 ? 178 GLN   F CD    1 
ATOM   12416 O  OE1   . GLN   E 4  178 ? 25.402  49.478  94.074  1.00 117.99 ? 178 GLN   F OE1   1 
ATOM   12417 N  NE2   . GLN   E 4  178 ? 25.753  48.817  91.959  1.00 128.92 ? 178 GLN   F NE2   1 
ATOM   12418 N  N     . VAL   E 4  179 ? 24.274  54.647  95.043  1.00 112.67 ? 179 VAL   F N     1 
ATOM   12419 C  CA    . VAL   E 4  179 ? 23.742  55.543  96.062  1.00 107.40 ? 179 VAL   F CA    1 
ATOM   12420 C  C     . VAL   E 4  179 ? 22.516  54.909  96.695  1.00 106.72 ? 179 VAL   F C     1 
ATOM   12421 O  O     . VAL   E 4  179 ? 21.727  54.234  96.025  1.00 107.79 ? 179 VAL   F O     1 
ATOM   12422 C  CB    . VAL   E 4  179 ? 23.407  56.924  95.469  1.00 101.65 ? 179 VAL   F CB    1 
ATOM   12423 C  CG1   . VAL   E 4  179 ? 22.266  56.812  94.464  1.00 98.41  ? 179 VAL   F CG1   1 
ATOM   12424 C  CG2   . VAL   E 4  179 ? 23.051  57.903  96.581  1.00 90.63  ? 179 VAL   F CG2   1 
ATOM   12425 N  N     . HIS   E 4  180 ? 22.357  55.122  97.999  1.00 104.88 ? 180 HIS   F N     1 
ATOM   12426 C  CA    . HIS   E 4  180 ? 21.287  54.497  98.759  1.00 97.76  ? 180 HIS   F CA    1 
ATOM   12427 C  C     . HIS   E 4  180 ? 20.608  55.510  99.671  1.00 86.39  ? 180 HIS   F C     1 
ATOM   12428 O  O     . HIS   E 4  180 ? 21.197  56.522  100.068 1.00 76.17  ? 180 HIS   F O     1 
ATOM   12429 C  CB    . HIS   E 4  180 ? 21.812  53.310  99.578  1.00 99.43  ? 180 HIS   F CB    1 
ATOM   12430 C  CG    . HIS   E 4  180 ? 21.387  51.979  99.044  1.00 91.40  ? 180 HIS   F CG    1 
ATOM   12431 N  ND1   . HIS   E 4  180 ? 22.065  50.813  99.322  1.00 89.18  ? 180 HIS   F ND1   1 
ATOM   12432 C  CD2   . HIS   E 4  180 ? 20.344  51.629  98.254  1.00 99.68  ? 180 HIS   F CD2   1 
ATOM   12433 C  CE1   . HIS   E 4  180 ? 21.460  49.802  98.725  1.00 95.56  ? 180 HIS   F CE1   1 
ATOM   12434 N  NE2   . HIS   E 4  180 ? 20.413  50.270  98.069  1.00 102.18 ? 180 HIS   F NE2   1 
ATOM   12435 N  N     . VAL   E 4  181 ? 19.358  55.218  99.995  1.00 80.76  ? 181 VAL   F N     1 
ATOM   12436 C  CA    . VAL   E 4  181 ? 18.528  56.106  100.791 1.00 79.12  ? 181 VAL   F CA    1 
ATOM   12437 C  C     . VAL   E 4  181 ? 18.081  55.358  102.040 1.00 83.40  ? 181 VAL   F C     1 
ATOM   12438 O  O     . VAL   E 4  181 ? 17.873  54.139  102.014 1.00 85.18  ? 181 VAL   F O     1 
ATOM   12439 C  CB    . VAL   E 4  181 ? 17.332  56.616  99.959  1.00 69.59  ? 181 VAL   F CB    1 
ATOM   12440 C  CG1   . VAL   E 4  181 ? 16.485  55.450  99.484  1.00 71.43  ? 181 VAL   F CG1   1 
ATOM   12441 C  CG2   . VAL   E 4  181 ? 16.510  57.615  100.743 1.00 70.01  ? 181 VAL   F CG2   1 
ATOM   12442 N  N     . ILE   E 4  182 ? 17.950  56.096  103.143 1.00 81.31  ? 182 ILE   F N     1 
ATOM   12443 C  CA    . ILE   E 4  182 ? 17.693  55.522  104.467 1.00 81.93  ? 182 ILE   F CA    1 
ATOM   12444 C  C     . ILE   E 4  182 ? 16.515  56.280  105.073 1.00 84.74  ? 182 ILE   F C     1 
ATOM   12445 O  O     . ILE   E 4  182 ? 16.697  57.274  105.787 1.00 82.89  ? 182 ILE   F O     1 
ATOM   12446 C  CB    . ILE   E 4  182 ? 18.917  55.594  105.387 1.00 89.86  ? 182 ILE   F CB    1 
ATOM   12447 C  CG1   . ILE   E 4  182 ? 20.090  54.808  104.787 1.00 100.00 ? 182 ILE   F CG1   1 
ATOM   12448 C  CG2   . ILE   E 4  182 ? 18.557  55.114  106.798 1.00 88.44  ? 182 ILE   F CG2   1 
ATOM   12449 C  CD1   . ILE   E 4  182 ? 21.343  54.802  105.644 1.00 97.84  ? 182 ILE   F CD1   1 
ATOM   12450 N  N     . GLN   E 4  183 ? 15.298  55.804  104.815 1.00 82.33  ? 183 GLN   F N     1 
ATOM   12451 C  CA    . GLN   E 4  183 ? 14.096  56.399  105.384 1.00 79.29  ? 183 GLN   F CA    1 
ATOM   12452 C  C     . GLN   E 4  183 ? 13.681  55.648  106.644 1.00 81.01  ? 183 GLN   F C     1 
ATOM   12453 O  O     . GLN   E 4  183 ? 13.890  54.439  106.765 1.00 77.03  ? 183 GLN   F O     1 
ATOM   12454 C  CB    . GLN   E 4  183 ? 12.934  56.382  104.392 1.00 57.87  ? 183 GLN   F CB    1 
ATOM   12455 C  CG    . GLN   E 4  183 ? 12.426  54.971  104.135 1.00 72.39  ? 183 GLN   F CG    1 
ATOM   12456 C  CD    . GLN   E 4  183 ? 11.068  54.943  103.479 1.00 65.00  ? 183 GLN   F CD    1 
ATOM   12457 O  OE1   . GLN   E 4  183 ? 10.761  55.784  102.636 1.00 58.15  ? 183 GLN   F OE1   1 
ATOM   12458 N  NE2   . GLN   E 4  183 ? 10.239  53.974  103.871 1.00 62.07  ? 183 GLN   F NE2   1 
ATOM   12459 N  N     . LYS   E 4  184 ? 13.082  56.382  107.580 1.00 82.98  ? 184 LYS   F N     1 
ATOM   12460 C  CA    . LYS   E 4  184 ? 12.528  55.766  108.774 1.00 76.53  ? 184 LYS   F CA    1 
ATOM   12461 C  C     . LYS   E 4  184 ? 11.583  54.644  108.383 1.00 71.60  ? 184 LYS   F C     1 
ATOM   12462 O  O     . LYS   E 4  184 ? 10.727  54.813  107.512 1.00 68.66  ? 184 LYS   F O     1 
ATOM   12463 C  CB    . LYS   E 4  184 ? 11.793  56.816  109.616 1.00 80.59  ? 184 LYS   F CB    1 
ATOM   12464 C  CG    . LYS   E 4  184 ? 10.863  56.238  110.688 1.00 89.54  ? 184 LYS   F CG    1 
ATOM   12465 C  CD    . LYS   E 4  184 ? 11.617  55.706  111.916 1.00 84.24  ? 184 LYS   F CD    1 
ATOM   12466 C  CE    . LYS   E 4  184 ? 10.751  54.755  112.747 1.00 63.77  ? 184 LYS   F CE    1 
ATOM   12467 N  NZ    . LYS   E 4  184 ? 9.375   55.300  113.004 1.00 61.11  ? 184 LYS   F NZ    1 
ATOM   12468 N  N     . TYR   E 4  185 ? 11.752  53.485  109.012 1.00 79.34  ? 185 TYR   F N     1 
ATOM   12469 C  CA    . TYR   E 4  185 ? 10.794  52.406  108.840 1.00 76.45  ? 185 TYR   F CA    1 
ATOM   12470 C  C     . TYR   E 4  185 ? 9.532   52.720  109.634 1.00 73.76  ? 185 TYR   F C     1 
ATOM   12471 O  O     . TYR   E 4  185 ? 9.596   53.285  110.730 1.00 62.06  ? 185 TYR   F O     1 
ATOM   12472 C  CB    . TYR   E 4  185 ? 11.385  51.068  109.276 1.00 70.15  ? 185 TYR   F CB    1 
ATOM   12473 C  CG    . TYR   E 4  185 ? 10.536  49.886  108.860 1.00 71.88  ? 185 TYR   F CG    1 
ATOM   12474 C  CD1   . TYR   E 4  185 ? 10.587  49.391  107.564 1.00 63.68  ? 185 TYR   F CD1   1 
ATOM   12475 C  CD2   . TYR   E 4  185 ? 9.677   49.268  109.764 1.00 71.79  ? 185 TYR   F CD2   1 
ATOM   12476 C  CE1   . TYR   E 4  185 ? 9.810   48.308  107.182 1.00 68.32  ? 185 TYR   F CE1   1 
ATOM   12477 C  CE2   . TYR   E 4  185 ? 8.897   48.192  109.391 1.00 65.59  ? 185 TYR   F CE2   1 
ATOM   12478 C  CZ    . TYR   E 4  185 ? 8.968   47.714  108.102 1.00 71.84  ? 185 TYR   F CZ    1 
ATOM   12479 O  OH    . TYR   E 4  185 ? 8.186   46.644  107.724 1.00 76.72  ? 185 TYR   F OH    1 
ATOM   12480 N  N     . LEU   E 4  186 ? 8.382   52.371  109.064 1.00 72.63  ? 186 LEU   F N     1 
ATOM   12481 C  CA    . LEU   E 4  186 ? 7.089   52.732  109.639 1.00 75.41  ? 186 LEU   F CA    1 
ATOM   12482 C  C     . LEU   E 4  186 ? 6.713   51.664  110.658 1.00 81.45  ? 186 LEU   F C     1 
ATOM   12483 O  O     . LEU   E 4  186 ? 6.158   50.619  110.305 1.00 74.00  ? 186 LEU   F O     1 
ATOM   12484 C  CB    . LEU   E 4  186 ? 6.035   52.874  108.547 1.00 73.19  ? 186 LEU   F CB    1 
ATOM   12485 C  CG    . LEU   E 4  186 ? 5.162   54.134  108.590 1.00 77.23  ? 186 LEU   F CG    1 
ATOM   12486 C  CD1   . LEU   E 4  186 ? 5.974   55.431  108.401 1.00 62.07  ? 186 LEU   F CD1   1 
ATOM   12487 C  CD2   . LEU   E 4  186 ? 4.055   54.029  107.550 1.00 80.25  ? 186 LEU   F CD2   1 
ATOM   12488 N  N     . GLU   E 4  187 ? 7.001   51.943  111.935 1.00 78.77  ? 187 GLU   F N     1 
ATOM   12489 C  CA    . GLU   E 4  187 ? 6.917   50.904  112.958 1.00 79.60  ? 187 GLU   F CA    1 
ATOM   12490 C  C     . GLU   E 4  187 ? 5.478   50.446  113.194 1.00 80.77  ? 187 GLU   F C     1 
ATOM   12491 O  O     . GLU   E 4  187 ? 5.221   49.240  113.289 1.00 76.93  ? 187 GLU   F O     1 
ATOM   12492 C  CB    . GLU   E 4  187 ? 7.566   51.394  114.251 1.00 71.77  ? 187 GLU   F CB    1 
ATOM   12493 C  CG    . GLU   E 4  187 ? 9.077   51.163  114.285 1.00 75.20  ? 187 GLU   F CG    1 
ATOM   12494 C  CD    . GLU   E 4  187 ? 9.802   52.044  115.296 1.00 77.41  ? 187 GLU   F CD    1 
ATOM   12495 O  OE1   . GLU   E 4  187 ? 9.151   52.564  116.231 1.00 70.29  ? 187 GLU   F OE1   1 
ATOM   12496 O  OE2   . GLU   E 4  187 ? 11.030  52.225  115.145 1.00 78.67  ? 187 GLU   F OE2   1 
ATOM   12497 N  N     . LYS   E 4  188 ? 4.525   51.383  113.290 1.00 76.02  ? 188 LYS   F N     1 
ATOM   12498 C  CA    . LYS   E 4  188 ? 3.141   50.997  113.560 1.00 75.20  ? 188 LYS   F CA    1 
ATOM   12499 C  C     . LYS   E 4  188 ? 2.290   51.063  112.297 1.00 69.54  ? 188 LYS   F C     1 
ATOM   12500 O  O     . LYS   E 4  188 ? 1.504   52.004  112.128 1.00 68.29  ? 188 LYS   F O     1 
ATOM   12501 C  CB    . LYS   E 4  188 ? 2.514   51.875  114.656 1.00 72.47  ? 188 LYS   F CB    1 
ATOM   12502 C  CG    . LYS   E 4  188 ? 3.344   53.071  115.112 1.00 78.77  ? 188 LYS   F CG    1 
ATOM   12503 C  CD    . LYS   E 4  188 ? 4.233   52.746  116.314 1.00 76.53  ? 188 LYS   F CD    1 
ATOM   12504 C  CE    . LYS   E 4  188 ? 5.135   53.933  116.663 1.00 80.94  ? 188 LYS   F CE    1 
ATOM   12505 N  NZ    . LYS   E 4  188 ? 6.174   53.614  117.694 1.00 74.67  ? 188 LYS   F NZ    1 
ATOM   12506 N  N     . PRO   E 4  189 ? 2.399   50.088  111.400 1.00 64.75  ? 189 PRO   F N     1 
ATOM   12507 C  CA    . PRO   E 4  189 ? 1.530   50.075  110.220 1.00 65.45  ? 189 PRO   F CA    1 
ATOM   12508 C  C     . PRO   E 4  189 ? 0.101   49.693  110.575 1.00 71.16  ? 189 PRO   F C     1 
ATOM   12509 O  O     . PRO   E 4  189 ? -0.179  49.085  111.610 1.00 74.69  ? 189 PRO   F O     1 
ATOM   12510 C  CB    . PRO   E 4  189 ? 2.167   49.006  109.332 1.00 60.79  ? 189 PRO   F CB    1 
ATOM   12511 C  CG    . PRO   E 4  189 ? 2.735   48.043  110.333 1.00 62.64  ? 189 PRO   F CG    1 
ATOM   12512 C  CD    . PRO   E 4  189 ? 3.286   48.915  111.432 1.00 62.23  ? 189 PRO   F CD    1 
ATOM   12513 N  N     . LEU   E 4  190 ? -0.811  50.061  109.684 1.00 62.92  ? 190 LEU   F N     1 
ATOM   12514 C  CA    . LEU   E 4  190 ? -2.165  49.535  109.743 1.00 64.03  ? 190 LEU   F CA    1 
ATOM   12515 C  C     . LEU   E 4  190 ? -2.153  48.070  109.335 1.00 64.52  ? 190 LEU   F C     1 
ATOM   12516 O  O     . LEU   E 4  190 ? -1.615  47.716  108.278 1.00 62.38  ? 190 LEU   F O     1 
ATOM   12517 C  CB    . LEU   E 4  190 ? -3.085  50.327  108.820 1.00 61.99  ? 190 LEU   F CB    1 
ATOM   12518 C  CG    . LEU   E 4  190 ? -4.574  50.074  109.005 1.00 47.62  ? 190 LEU   F CG    1 
ATOM   12519 C  CD1   . LEU   E 4  190 ? -5.152  51.116  109.944 1.00 59.70  ? 190 LEU   F CD1   1 
ATOM   12520 C  CD2   . LEU   E 4  190 ? -5.279  50.086  107.681 1.00 53.31  ? 190 LEU   F CD2   1 
ATOM   12521 N  N     . LEU   E 4  191 ? -2.761  47.220  110.161 1.00 68.51  ? 191 LEU   F N     1 
ATOM   12522 C  CA    . LEU   E 4  191 ? -2.709  45.774  109.976 1.00 70.29  ? 191 LEU   F CA    1 
ATOM   12523 C  C     . LEU   E 4  191 ? -4.093  45.239  109.628 1.00 66.99  ? 191 LEU   F C     1 
ATOM   12524 O  O     . LEU   E 4  191 ? -5.049  45.431  110.393 1.00 65.61  ? 191 LEU   F O     1 
ATOM   12525 C  CB    . LEU   E 4  191 ? -2.156  45.093  111.227 1.00 63.65  ? 191 LEU   F CB    1 
ATOM   12526 C  CG    . LEU   E 4  191 ? -0.731  45.538  111.550 1.00 70.31  ? 191 LEU   F CG    1 
ATOM   12527 C  CD1   . LEU   E 4  191 ? -0.087  44.605  112.551 1.00 72.11  ? 191 LEU   F CD1   1 
ATOM   12528 C  CD2   . LEU   E 4  191 ? 0.107   45.635  110.278 1.00 61.54  ? 191 LEU   F CD2   1 
ATOM   12529 N  N     . LEU   E 4  192 ? -4.191  44.571  108.476 1.00 57.60  ? 192 LEU   F N     1 
ATOM   12530 C  CA    . LEU   E 4  192 ? -5.429  43.922  108.071 1.00 63.10  ? 192 LEU   F CA    1 
ATOM   12531 C  C     . LEU   E 4  192 ? -5.762  42.766  109.004 1.00 76.51  ? 192 LEU   F C     1 
ATOM   12532 O  O     . LEU   E 4  192 ? -4.877  42.129  109.586 1.00 68.87  ? 192 LEU   F O     1 
ATOM   12533 C  CB    . LEU   E 4  192 ? -5.328  43.392  106.643 1.00 63.81  ? 192 LEU   F CB    1 
ATOM   12534 C  CG    . LEU   E 4  192 ? -5.128  44.398  105.514 1.00 69.34  ? 192 LEU   F CG    1 
ATOM   12535 C  CD1   . LEU   E 4  192 ? -4.874  43.650  104.229 1.00 56.87  ? 192 LEU   F CD1   1 
ATOM   12536 C  CD2   . LEU   E 4  192 ? -6.336  45.304  105.378 1.00 63.65  ? 192 LEU   F CD2   1 
ATOM   12537 N  N     . GLU   E 4  193 ? -7.064  42.490  109.124 1.00 78.79  ? 193 GLU   F N     1 
ATOM   12538 C  CA    . GLU   E 4  193 ? -7.619  41.413  109.926 1.00 67.58  ? 193 GLU   F CA    1 
ATOM   12539 C  C     . GLU   E 4  193 ? -8.721  40.757  109.107 1.00 71.05  ? 193 GLU   F C     1 
ATOM   12540 O  O     . GLU   E 4  193 ? -9.532  41.461  108.492 1.00 76.95  ? 193 GLU   F O     1 
ATOM   12541 C  CB    . GLU   E 4  193 ? -8.192  41.922  111.250 1.00 59.77  ? 193 GLU   F CB    1 
ATOM   12542 C  CG    . GLU   E 4  193 ? -7.220  42.724  112.096 1.00 67.59  ? 193 GLU   F CG    1 
ATOM   12543 C  CD    . GLU   E 4  193 ? -6.075  41.890  112.609 1.00 67.10  ? 193 GLU   F CD    1 
ATOM   12544 O  OE1   . GLU   E 4  193 ? -5.984  40.708  112.204 1.00 68.43  ? 193 GLU   F OE1   1 
ATOM   12545 O  OE2   . GLU   E 4  193 ? -5.271  42.421  113.410 1.00 54.74  ? 193 GLU   F OE2   1 
ATOM   12546 N  N     . PRO   E 4  194 ? -8.789  39.424  109.084 1.00 85.00  ? 194 PRO   F N     1 
ATOM   12547 C  CA    . PRO   E 4  194 ? -7.992  38.464  109.856 1.00 81.50  ? 194 PRO   F CA    1 
ATOM   12548 C  C     . PRO   E 4  194 ? -6.559  38.358  109.341 1.00 79.97  ? 194 PRO   F C     1 
ATOM   12549 O  O     . PRO   E 4  194 ? -6.319  38.487  108.141 1.00 78.44  ? 194 PRO   F O     1 
ATOM   12550 C  CB    . PRO   E 4  194 ? -8.768  37.159  109.649 1.00 84.39  ? 194 PRO   F CB    1 
ATOM   12551 C  CG    . PRO   E 4  194 ? -9.260  37.277  108.220 1.00 72.39  ? 194 PRO   F CG    1 
ATOM   12552 C  CD    . PRO   E 4  194 ? -9.602  38.745  108.052 1.00 86.58  ? 194 PRO   F CD    1 
ATOM   12553 N  N     . GLY   E 4  195 ? -5.583  38.131  110.218 1.00 76.81  ? 195 GLY   F N     1 
ATOM   12554 C  CA    . GLY   E 4  195 ? -4.228  37.896  109.765 1.00 72.48  ? 195 GLY   F CA    1 
ATOM   12555 C  C     . GLY   E 4  195 ? -3.182  38.769  110.420 1.00 69.47  ? 195 GLY   F C     1 
ATOM   12556 O  O     . GLY   E 4  195 ? -2.031  38.353  110.569 1.00 77.71  ? 195 GLY   F O     1 
ATOM   12557 N  N     . HIS   E 4  196 ? -3.549  39.984  110.808 1.00 71.61  ? 196 HIS   F N     1 
ATOM   12558 C  CA    . HIS   E 4  196 ? -2.592  40.896  111.422 1.00 69.32  ? 196 HIS   F CA    1 
ATOM   12559 C  C     . HIS   E 4  196 ? -1.395  41.115  110.495 1.00 74.07  ? 196 HIS   F C     1 
ATOM   12560 O  O     . HIS   E 4  196 ? -0.242  40.918  110.880 1.00 83.48  ? 196 HIS   F O     1 
ATOM   12561 C  CB    . HIS   E 4  196 ? -2.144  40.356  112.778 1.00 64.74  ? 196 HIS   F CB    1 
ATOM   12562 C  CG    . HIS   E 4  196 ? -1.815  41.417  113.776 1.00 68.34  ? 196 HIS   F CG    1 
ATOM   12563 N  ND1   . HIS   E 4  196 ? -2.780  42.194  114.379 1.00 75.91  ? 196 HIS   F ND1   1 
ATOM   12564 C  CD2   . HIS   E 4  196 ? -0.628  41.823  114.289 1.00 73.11  ? 196 HIS   F CD2   1 
ATOM   12565 C  CE1   . HIS   E 4  196 ? -2.201  43.038  115.217 1.00 78.01  ? 196 HIS   F CE1   1 
ATOM   12566 N  NE2   . HIS   E 4  196 ? -0.895  42.835  115.180 1.00 68.49  ? 196 HIS   F NE2   1 
ATOM   12567 N  N     . ARG   E 4  197 ? -1.681  41.523  109.256 1.00 78.06  ? 197 ARG   F N     1 
ATOM   12568 C  CA    . ARG   E 4  197 ? -0.687  41.571  108.187 1.00 81.98  ? 197 ARG   F CA    1 
ATOM   12569 C  C     . ARG   E 4  197 ? -0.563  42.965  107.571 1.00 75.50  ? 197 ARG   F C     1 
ATOM   12570 O  O     . ARG   E 4  197 ? -1.534  43.724  107.476 1.00 65.92  ? 197 ARG   F O     1 
ATOM   12571 C  CB    . ARG   E 4  197 ? -1.020  40.544  107.082 1.00 82.02  ? 197 ARG   F CB    1 
ATOM   12572 C  CG    . ARG   E 4  197 ? -2.480  40.506  106.684 1.00 66.07  ? 197 ARG   F CG    1 
ATOM   12573 C  CD    . ARG   E 4  197 ? -2.820  39.273  105.887 1.00 62.15  ? 197 ARG   F CD    1 
ATOM   12574 N  NE    . ARG   E 4  197 ? -4.263  39.098  105.881 1.00 74.94  ? 197 ARG   F NE    1 
ATOM   12575 C  CZ    . ARG   E 4  197 ? -5.056  39.391  104.861 1.00 73.21  ? 197 ARG   F CZ    1 
ATOM   12576 N  NH1   . ARG   E 4  197 ? -4.562  39.768  103.691 1.00 63.72  ? 197 ARG   F NH1   1 
ATOM   12577 N  NH2   . ARG   E 4  197 ? -6.377  39.298  105.018 1.00 62.21  ? 197 ARG   F NH2   1 
ATOM   12578 N  N     . LYS   E 4  198 ? 0.649   43.275  107.123 1.00 85.56  ? 198 LYS   F N     1 
ATOM   12579 C  CA    . LYS   E 4  198 ? 0.999   44.561  106.539 1.00 77.85  ? 198 LYS   F CA    1 
ATOM   12580 C  C     . LYS   E 4  198 ? 0.666   44.594  105.050 1.00 73.65  ? 198 LYS   F C     1 
ATOM   12581 O  O     . LYS   E 4  198 ? 0.654   43.562  104.377 1.00 75.01  ? 198 LYS   F O     1 
ATOM   12582 C  CB    . LYS   E 4  198 ? 2.487   44.828  106.759 1.00 72.21  ? 198 LYS   F CB    1 
ATOM   12583 C  CG    . LYS   E 4  198 ? 3.030   46.082  106.140 1.00 74.87  ? 198 LYS   F CG    1 
ATOM   12584 C  CD    . LYS   E 4  198 ? 4.535   46.092  106.306 1.00 78.77  ? 198 LYS   F CD    1 
ATOM   12585 C  CE    . LYS   E 4  198 ? 5.135   47.456  106.050 1.00 82.32  ? 198 LYS   F CE    1 
ATOM   12586 N  NZ    . LYS   E 4  198 ? 6.580   47.468  106.396 1.00 79.28  ? 198 LYS   F NZ    1 
ATOM   12587 N  N     . PHE   E 4  199 ? 0.397   45.800  104.543 1.00 74.31  ? 199 PHE   F N     1 
ATOM   12588 C  CA    . PHE   E 4  199 ? 0.058   46.003  103.139 1.00 58.48  ? 199 PHE   F CA    1 
ATOM   12589 C  C     . PHE   E 4  199 ? 0.585   47.356  102.683 1.00 58.32  ? 199 PHE   F C     1 
ATOM   12590 O  O     . PHE   E 4  199 ? 0.746   48.272  103.490 1.00 63.03  ? 199 PHE   F O     1 
ATOM   12591 C  CB    . PHE   E 4  199 ? -1.453  45.951  102.916 1.00 60.83  ? 199 PHE   F CB    1 
ATOM   12592 C  CG    . PHE   E 4  199 ? -2.185  47.137  103.491 1.00 64.17  ? 199 PHE   F CG    1 
ATOM   12593 C  CD1   . PHE   E 4  199 ? -2.357  48.293  102.748 1.00 64.90  ? 199 PHE   F CD1   1 
ATOM   12594 C  CD2   . PHE   E 4  199 ? -2.691  47.100  104.778 1.00 70.87  ? 199 PHE   F CD2   1 
ATOM   12595 C  CE1   . PHE   E 4  199 ? -3.020  49.382  103.275 1.00 58.99  ? 199 PHE   F CE1   1 
ATOM   12596 C  CE2   . PHE   E 4  199 ? -3.361  48.192  105.307 1.00 68.51  ? 199 PHE   F CE2   1 
ATOM   12597 C  CZ    . PHE   E 4  199 ? -3.521  49.331  104.552 1.00 58.26  ? 199 PHE   F CZ    1 
ATOM   12598 N  N     . ASP   E 4  200 ? 0.841   47.478  101.379 1.00 63.76  ? 200 ASP   F N     1 
ATOM   12599 C  CA    . ASP   E 4  200 ? 1.037   48.769  100.727 1.00 52.94  ? 200 ASP   F CA    1 
ATOM   12600 C  C     . ASP   E 4  200 ? -0.048  48.962  99.668  1.00 61.37  ? 200 ASP   F C     1 
ATOM   12601 O  O     . ASP   E 4  200 ? -0.834  48.053  99.379  1.00 65.57  ? 200 ASP   F O     1 
ATOM   12602 C  CB    . ASP   E 4  200 ? 2.448   48.904  100.126 1.00 47.82  ? 200 ASP   F CB    1 
ATOM   12603 C  CG    . ASP   E 4  200 ? 2.651   48.088  98.851  1.00 65.61  ? 200 ASP   F CG    1 
ATOM   12604 O  OD1   . ASP   E 4  200 ? 2.012   48.391  97.814  1.00 58.16  ? 200 ASP   F OD1   1 
ATOM   12605 O  OD2   . ASP   E 4  200 ? 3.492   47.158  98.877  1.00 60.24  ? 200 ASP   F OD2   1 
ATOM   12606 N  N     . ILE   E 4  201 ? -0.118  50.173  99.110  1.00 58.56  ? 201 ILE   F N     1 
ATOM   12607 C  CA    . ILE   E 4  201 ? -1.161  50.536  98.152  1.00 57.62  ? 201 ILE   F CA    1 
ATOM   12608 C  C     . ILE   E 4  201 ? -0.510  51.099  96.897  1.00 51.55  ? 201 ILE   F C     1 
ATOM   12609 O  O     . ILE   E 4  201 ? 0.368   51.962  96.979  1.00 56.02  ? 201 ILE   F O     1 
ATOM   12610 C  CB    . ILE   E 4  201 ? -2.167  51.555  98.730  1.00 55.20  ? 201 ILE   F CB    1 
ATOM   12611 C  CG1   . ILE   E 4  201 ? -2.999  50.936  99.852  1.00 55.20  ? 201 ILE   F CG1   1 
ATOM   12612 C  CG2   . ILE   E 4  201 ? -3.099  52.045  97.635  1.00 60.77  ? 201 ILE   F CG2   1 
ATOM   12613 C  CD1   . ILE   E 4  201 ? -3.986  51.893  100.468 1.00 57.08  ? 201 ILE   F CD1   1 
ATOM   12614 N  N     . ARG   E 4  202 ? -0.952  50.619  95.742  1.00 49.65  ? 202 ARG   F N     1 
ATOM   12615 C  CA    . ARG   E 4  202 ? -0.458  51.040  94.442  1.00 43.40  ? 202 ARG   F CA    1 
ATOM   12616 C  C     . ARG   E 4  202 ? -1.591  51.739  93.714  1.00 51.21  ? 202 ARG   F C     1 
ATOM   12617 O  O     . ARG   E 4  202 ? -2.662  51.151  93.528  1.00 53.84  ? 202 ARG   F O     1 
ATOM   12618 C  CB    . ARG   E 4  202 ? 0.028   49.841  93.633  1.00 52.73  ? 202 ARG   F CB    1 
ATOM   12619 C  CG    . ARG   E 4  202 ? -0.113  49.995  92.124  1.00 53.97  ? 202 ARG   F CG    1 
ATOM   12620 C  CD    . ARG   E 4  202 ? 0.824   51.068  91.607  1.00 53.30  ? 202 ARG   F CD    1 
ATOM   12621 N  NE    . ARG   E 4  202 ? 2.208   50.784  91.964  1.00 52.17  ? 202 ARG   F NE    1 
ATOM   12622 C  CZ    . ARG   E 4  202 ? 2.986   49.937  91.303  1.00 52.68  ? 202 ARG   F CZ    1 
ATOM   12623 N  NH1   . ARG   E 4  202 ? 2.544   49.282  90.239  1.00 55.78  ? 202 ARG   F NH1   1 
ATOM   12624 N  NH2   . ARG   E 4  202 ? 4.231   49.734  91.727  1.00 44.16  ? 202 ARG   F NH2   1 
ATOM   12625 N  N     . SER   E 4  203 ? -1.363  52.990  93.317  1.00 53.51  ? 203 SER   F N     1 
ATOM   12626 C  CA    . SER   E 4  203 ? -2.285  53.731  92.467  1.00 54.09  ? 203 SER   F CA    1 
ATOM   12627 C  C     . SER   E 4  203 ? -1.578  54.091  91.167  1.00 48.74  ? 203 SER   F C     1 
ATOM   12628 O  O     . SER   E 4  203 ? -0.404  54.467  91.170  1.00 47.43  ? 203 SER   F O     1 
ATOM   12629 C  CB    . SER   E 4  203 ? -2.808  54.992  93.164  1.00 44.27  ? 203 SER   F CB    1 
ATOM   12630 O  OG    . SER   E 4  203 ? -3.829  54.673  94.093  1.00 49.82  ? 203 SER   F OG    1 
ATOM   12631 N  N     . TRP   E 4  204 ? -2.278  53.933  90.056  1.00 48.57  ? 204 TRP   F N     1 
ATOM   12632 C  CA    . TRP   E 4  204 ? -1.736  54.245  88.741  1.00 53.69  ? 204 TRP   F CA    1 
ATOM   12633 C  C     . TRP   E 4  204 ? -2.258  55.620  88.353  1.00 50.10  ? 204 TRP   F C     1 
ATOM   12634 O  O     . TRP   E 4  204 ? -3.472  55.852  88.369  1.00 45.46  ? 204 TRP   F O     1 
ATOM   12635 C  CB    . TRP   E 4  204 ? -2.129  53.174  87.712  1.00 59.57  ? 204 TRP   F CB    1 
ATOM   12636 C  CG    . TRP   E 4  204 ? -1.641  51.789  88.099  1.00 57.53  ? 204 TRP   F CG    1 
ATOM   12637 C  CD1   . TRP   E 4  204 ? -0.407  51.256  87.850  1.00 60.74  ? 204 TRP   F CD1   1 
ATOM   12638 C  CD2   . TRP   E 4  204 ? -2.362  50.793  88.842  1.00 57.55  ? 204 TRP   F CD2   1 
ATOM   12639 N  NE1   . TRP   E 4  204 ? -0.317  49.991  88.388  1.00 65.14  ? 204 TRP   F NE1   1 
ATOM   12640 C  CE2   . TRP   E 4  204 ? -1.504  49.684  89.000  1.00 63.55  ? 204 TRP   F CE2   1 
ATOM   12641 C  CE3   . TRP   E 4  204 ? -3.647  50.731  89.391  1.00 63.33  ? 204 TRP   F CE3   1 
ATOM   12642 C  CZ2   . TRP   E 4  204 ? -1.893  48.529  89.678  1.00 60.63  ? 204 TRP   F CZ2   1 
ATOM   12643 C  CZ3   . TRP   E 4  204 ? -4.032  49.577  90.061  1.00 56.32  ? 204 TRP   F CZ3   1 
ATOM   12644 C  CH2   . TRP   E 4  204 ? -3.157  48.496  90.198  1.00 58.15  ? 204 TRP   F CH2   1 
ATOM   12645 N  N     . VAL   E 4  205 ? -1.347  56.546  88.066  1.00 46.03  ? 205 VAL   F N     1 
ATOM   12646 C  CA    . VAL   E 4  205 ? -1.717  57.896  87.661  1.00 46.11  ? 205 VAL   F CA    1 
ATOM   12647 C  C     . VAL   E 4  205 ? -1.222  58.100  86.236  1.00 42.34  ? 205 VAL   F C     1 
ATOM   12648 O  O     . VAL   E 4  205 ? -0.030  57.935  85.960  1.00 51.50  ? 205 VAL   F O     1 
ATOM   12649 C  CB    . VAL   E 4  205 ? -1.152  58.972  88.607  1.00 49.87  ? 205 VAL   F CB    1 
ATOM   12650 C  CG1   . VAL   E 4  205 ? -1.810  60.326  88.313  1.00 41.60  ? 205 VAL   F CG1   1 
ATOM   12651 C  CG2   . VAL   E 4  205 ? -1.370  58.590  90.070  1.00 49.24  ? 205 VAL   F CG2   1 
ATOM   12652 N  N     . LEU   E 4  206 ? -2.138  58.431  85.335  1.00 35.56  ? 206 LEU   F N     1 
ATOM   12653 C  CA    . LEU   E 4  206 ? -1.823  58.811  83.966  1.00 39.54  ? 206 LEU   F CA    1 
ATOM   12654 C  C     . LEU   E 4  206 ? -1.807  60.331  83.872  1.00 37.82  ? 206 LEU   F C     1 
ATOM   12655 O  O     . LEU   E 4  206 ? -2.705  60.992  84.393  1.00 36.27  ? 206 LEU   F O     1 
ATOM   12656 C  CB    . LEU   E 4  206 ? -2.857  58.225  83.002  1.00 37.83  ? 206 LEU   F CB    1 
ATOM   12657 C  CG    . LEU   E 4  206 ? -2.861  58.561  81.514  1.00 43.72  ? 206 LEU   F CG    1 
ATOM   12658 C  CD1   . LEU   E 4  206 ? -1.662  57.979  80.821  1.00 38.97  ? 206 LEU   F CD1   1 
ATOM   12659 C  CD2   . LEU   E 4  206 ? -4.148  58.039  80.871  1.00 53.06  ? 206 LEU   F CD2   1 
ATOM   12660 N  N     . VAL   E 4  207 ? -0.789  60.882  83.219  1.00 44.88  ? 207 VAL   F N     1 
ATOM   12661 C  CA    . VAL   E 4  207 ? -0.701  62.311  82.936  1.00 37.10  ? 207 VAL   F CA    1 
ATOM   12662 C  C     . VAL   E 4  207 ? -0.605  62.474  81.428  1.00 36.22  ? 207 VAL   F C     1 
ATOM   12663 O  O     . VAL   E 4  207 ? 0.347   61.974  80.816  1.00 44.30  ? 207 VAL   F O     1 
ATOM   12664 C  CB    . VAL   E 4  207 ? 0.504   62.959  83.631  1.00 38.19  ? 207 VAL   F CB    1 
ATOM   12665 C  CG1   . VAL   E 4  207 ? 0.515   64.459  83.368  1.00 36.63  ? 207 VAL   F CG1   1 
ATOM   12666 C  CG2   . VAL   E 4  207 ? 0.479   62.652  85.120  1.00 31.80  ? 207 VAL   F CG2   1 
ATOM   12667 N  N     . ASP   E 4  208 ? -1.589  63.163  80.828  1.00 37.61  ? 208 ASP   F N     1 
ATOM   12668 C  CA    . ASP   E 4  208 ? -1.639  63.352  79.380  1.00 46.77  ? 208 ASP   F CA    1 
ATOM   12669 C  C     . ASP   E 4  208 ? -0.840  64.595  78.967  1.00 43.55  ? 208 ASP   F C     1 
ATOM   12670 O  O     . ASP   E 4  208 ? -0.195  65.250  79.789  1.00 35.77  ? 208 ASP   F O     1 
ATOM   12671 C  CB    . ASP   E 4  208 ? -3.089  63.405  78.865  1.00 37.25  ? 208 ASP   F CB    1 
ATOM   12672 C  CG    . ASP   E 4  208 ? -3.859  64.671  79.297  1.00 44.61  ? 208 ASP   F CG    1 
ATOM   12673 O  OD1   . ASP   E 4  208 ? -3.256  65.617  79.841  1.00 35.04  ? 208 ASP   F OD1   1 
ATOM   12674 O  OD2   . ASP   E 4  208 ? -5.099  64.712  79.079  1.00 44.82  ? 208 ASP   F OD2   1 
ATOM   12675 N  N     . HIS   E 4  209 ? -0.870  64.905  77.663  1.00 41.69  ? 209 HIS   F N     1 
ATOM   12676 C  CA    . HIS   E 4  209 ? -0.074  66.010  77.125  1.00 42.88  ? 209 HIS   F CA    1 
ATOM   12677 C  C     . HIS   E 4  209 ? -0.501  67.367  77.700  1.00 45.71  ? 209 HIS   F C     1 
ATOM   12678 O  O     . HIS   E 4  209 ? 0.348   68.225  77.976  1.00 45.65  ? 209 HIS   F O     1 
ATOM   12679 C  CB    . HIS   E 4  209 ? -0.166  66.011  75.602  1.00 41.54  ? 209 HIS   F CB    1 
ATOM   12680 C  CG    . HIS   E 4  209 ? -1.568  65.923  75.091  1.00 45.91  ? 209 HIS   F CG    1 
ATOM   12681 N  ND1   . HIS   E 4  209 ? -2.413  64.882  75.412  1.00 50.38  ? 209 HIS   F ND1   1 
ATOM   12682 C  CD2   . HIS   E 4  209 ? -2.279  66.752  74.291  1.00 41.75  ? 209 HIS   F CD2   1 
ATOM   12683 C  CE1   . HIS   E 4  209 ? -3.588  65.079  74.838  1.00 51.85  ? 209 HIS   F CE1   1 
ATOM   12684 N  NE2   . HIS   E 4  209 ? -3.531  66.205  74.148  1.00 48.07  ? 209 HIS   F NE2   1 
ATOM   12685 N  N     . LEU   E 4  210 ? -1.807  67.583  77.893  1.00 42.31  ? 210 LEU   F N     1 
ATOM   12686 C  CA    . LEU   E 4  210 ? -2.287  68.792  78.570  1.00 41.96  ? 210 LEU   F CA    1 
ATOM   12687 C  C     . LEU   E 4  210 ? -1.897  68.867  80.050  1.00 42.12  ? 210 LEU   F C     1 
ATOM   12688 O  O     . LEU   E 4  210 ? -2.211  69.871  80.692  1.00 46.46  ? 210 LEU   F O     1 
ATOM   12689 C  CB    . LEU   E 4  210 ? -3.808  68.897  78.470  1.00 31.84  ? 210 LEU   F CB    1 
ATOM   12690 C  CG    . LEU   E 4  210 ? -4.494  68.488  77.157  1.00 42.73  ? 210 LEU   F CG    1 
ATOM   12691 C  CD1   . LEU   E 4  210 ? -5.983  68.271  77.391  1.00 31.80  ? 210 LEU   F CD1   1 
ATOM   12692 C  CD2   . LEU   E 4  210 ? -4.262  69.486  76.029  1.00 26.75  ? 210 LEU   F CD2   1 
ATOM   12693 N  N     . TYR   E 4  211 ? -1.230  67.857  80.608  1.00 37.99  ? 211 TYR   F N     1 
ATOM   12694 C  CA    . TYR   E 4  211 ? -0.955  67.767  82.048  1.00 37.88  ? 211 TYR   F CA    1 
ATOM   12695 C  C     . TYR   E 4  211 ? -2.221  67.648  82.891  1.00 42.55  ? 211 TYR   F C     1 
ATOM   12696 O  O     . TYR   E 4  211 ? -2.246  68.103  84.036  1.00 45.13  ? 211 TYR   F O     1 
ATOM   12697 C  CB    . TYR   E 4  211 ? -0.126  68.937  82.559  1.00 27.46  ? 211 TYR   F CB    1 
ATOM   12698 C  CG    . TYR   E 4  211 ? 0.962   68.490  83.496  1.00 39.97  ? 211 TYR   F CG    1 
ATOM   12699 C  CD1   . TYR   E 4  211 ? 2.202   68.105  83.005  1.00 35.34  ? 211 TYR   F CD1   1 
ATOM   12700 C  CD2   . TYR   E 4  211 ? 0.753   68.422  84.872  1.00 39.19  ? 211 TYR   F CD2   1 
ATOM   12701 C  CE1   . TYR   E 4  211 ? 3.212   67.686  83.848  1.00 32.41  ? 211 TYR   F CE1   1 
ATOM   12702 C  CE2   . TYR   E 4  211 ? 1.771   67.994  85.729  1.00 33.93  ? 211 TYR   F CE2   1 
ATOM   12703 C  CZ    . TYR   E 4  211 ? 2.994   67.624  85.203  1.00 32.92  ? 211 TYR   F CZ    1 
ATOM   12704 O  OH    . TYR   E 4  211 ? 4.024   67.201  86.017  1.00 33.51  ? 211 TYR   F OH    1 
ATOM   12705 N  N     . ASN   E 4  212 ? -3.285  67.074  82.333  1.00 34.55  ? 212 ASN   F N     1 
ATOM   12706 C  CA    . ASN   E 4  212 ? -4.322  66.483  83.163  1.00 39.69  ? 212 ASN   F CA    1 
ATOM   12707 C  C     . ASN   E 4  212 ? -3.699  65.381  84.022  1.00 47.67  ? 212 ASN   F C     1 
ATOM   12708 O  O     . ASN   E 4  212 ? -2.855  64.614  83.552  1.00 45.61  ? 212 ASN   F O     1 
ATOM   12709 C  CB    . ASN   E 4  212 ? -5.434  65.891  82.290  1.00 46.63  ? 212 ASN   F CB    1 
ATOM   12710 C  CG    . ASN   E 4  212 ? -6.237  66.943  81.558  1.00 49.19  ? 212 ASN   F CG    1 
ATOM   12711 O  OD1   . ASN   E 4  212 ? -6.709  67.899  82.165  1.00 50.40  ? 212 ASN   F OD1   1 
ATOM   12712 N  ND2   . ASN   E 4  212 ? -6.405  66.767  80.244  1.00 40.85  ? 212 ASN   F ND2   1 
ATOM   12713 N  N     . ILE   E 4  213 ? -4.106  65.304  85.286  1.00 41.00  ? 213 ILE   F N     1 
ATOM   12714 C  CA    . ILE   E 4  213 ? -3.639  64.267  86.200  1.00 42.49  ? 213 ILE   F CA    1 
ATOM   12715 C  C     . ILE   E 4  213 ? -4.816  63.334  86.480  1.00 44.92  ? 213 ILE   F C     1 
ATOM   12716 O  O     . ILE   E 4  213 ? -5.803  63.740  87.106  1.00 46.34  ? 213 ILE   F O     1 
ATOM   12717 C  CB    . ILE   E 4  213 ? -3.073  64.861  87.497  1.00 40.54  ? 213 ILE   F CB    1 
ATOM   12718 C  CG1   . ILE   E 4  213 ? -2.094  65.986  87.178  1.00 38.03  ? 213 ILE   F CG1   1 
ATOM   12719 C  CG2   . ILE   E 4  213 ? -2.374  63.802  88.288  1.00 37.88  ? 213 ILE   F CG2   1 
ATOM   12720 C  CD1   . ILE   E 4  213 ? -1.396  66.550  88.367  1.00 35.74  ? 213 ILE   F CD1   1 
ATOM   12721 N  N     . TYR   E 4  214 ? -4.712  62.086  86.019  1.00 41.15  ? 214 TYR   F N     1 
ATOM   12722 C  CA    . TYR   E 4  214 ? -5.797  61.111  86.068  1.00 39.20  ? 214 TYR   F CA    1 
ATOM   12723 C  C     . TYR   E 4  214 ? -5.470  59.992  87.048  1.00 50.07  ? 214 TYR   F C     1 
ATOM   12724 O  O     . TYR   E 4  214 ? -4.399  59.375  86.971  1.00 39.17  ? 214 TYR   F O     1 
ATOM   12725 C  CB    . TYR   E 4  214 ? -6.072  60.528  84.679  1.00 46.10  ? 214 TYR   F CB    1 
ATOM   12726 C  CG    . TYR   E 4  214 ? -6.679  61.540  83.730  1.00 49.86  ? 214 TYR   F CG    1 
ATOM   12727 C  CD1   . TYR   E 4  214 ? -7.933  62.066  83.978  1.00 45.88  ? 214 TYR   F CD1   1 
ATOM   12728 C  CD2   . TYR   E 4  214 ? -5.993  61.987  82.607  1.00 54.31  ? 214 TYR   F CD2   1 
ATOM   12729 C  CE1   . TYR   E 4  214 ? -8.495  62.986  83.154  1.00 47.21  ? 214 TYR   F CE1   1 
ATOM   12730 C  CE2   . TYR   E 4  214 ? -6.562  62.937  81.758  1.00 55.58  ? 214 TYR   F CE2   1 
ATOM   12731 C  CZ    . TYR   E 4  214 ? -7.823  63.422  82.044  1.00 48.70  ? 214 TYR   F CZ    1 
ATOM   12732 O  OH    . TYR   E 4  214 ? -8.439  64.354  81.240  1.00 50.29  ? 214 TYR   F OH    1 
ATOM   12733 N  N     . LEU   E 4  215 ? -6.399  59.737  87.969  1.00 56.97  ? 215 LEU   F N     1 
ATOM   12734 C  CA    . LEU   E 4  215 ? -6.306  58.644  88.929  1.00 45.32  ? 215 LEU   F CA    1 
ATOM   12735 C  C     . LEU   E 4  215 ? -7.290  57.559  88.507  1.00 54.75  ? 215 LEU   F C     1 
ATOM   12736 O  O     . LEU   E 4  215 ? -8.507  57.766  88.558  1.00 59.21  ? 215 LEU   F O     1 
ATOM   12737 C  CB    . LEU   E 4  215 ? -6.603  59.146  90.335  1.00 45.07  ? 215 LEU   F CB    1 
ATOM   12738 C  CG    . LEU   E 4  215 ? -6.590  58.109  91.450  1.00 52.59  ? 215 LEU   F CG    1 
ATOM   12739 C  CD1   . LEU   E 4  215 ? -5.240  57.363  91.507  1.00 42.83  ? 215 LEU   F CD1   1 
ATOM   12740 C  CD2   . LEU   E 4  215 ? -6.930  58.780  92.795  1.00 36.76  ? 215 LEU   F CD2   1 
ATOM   12741 N  N     . TYR   E 4  216 ? -6.764  56.429  88.039  1.00 48.51  ? 216 TYR   F N     1 
ATOM   12742 C  CA    . TYR   E 4  216 ? -7.574  55.239  87.827  1.00 47.27  ? 216 TYR   F CA    1 
ATOM   12743 C  C     . TYR   E 4  216 ? -8.357  54.923  89.096  1.00 59.88  ? 216 TYR   F C     1 
ATOM   12744 O  O     . TYR   E 4  216 ? -7.802  54.938  90.198  1.00 57.78  ? 216 TYR   F O     1 
ATOM   12745 C  CB    . TYR   E 4  216 ? -6.649  54.084  87.459  1.00 54.59  ? 216 TYR   F CB    1 
ATOM   12746 C  CG    . TYR   E 4  216 ? -7.303  52.776  87.106  1.00 59.71  ? 216 TYR   F CG    1 
ATOM   12747 C  CD1   . TYR   E 4  216 ? -8.630  52.716  86.685  1.00 59.54  ? 216 TYR   F CD1   1 
ATOM   12748 C  CD2   . TYR   E 4  216 ? -6.578  51.586  87.196  1.00 53.93  ? 216 TYR   F CD2   1 
ATOM   12749 C  CE1   . TYR   E 4  216 ? -9.215  51.495  86.353  1.00 64.50  ? 216 TYR   F CE1   1 
ATOM   12750 C  CE2   . TYR   E 4  216 ? -7.148  50.369  86.875  1.00 63.69  ? 216 TYR   F CE2   1 
ATOM   12751 C  CZ    . TYR   E 4  216 ? -8.465  50.322  86.452  1.00 64.57  ? 216 TYR   F CZ    1 
ATOM   12752 O  OH    . TYR   E 4  216 ? -9.018  49.101  86.131  1.00 49.38  ? 216 TYR   F OH    1 
ATOM   12753 N  N     . ARG   E 4  217 ? -9.661  54.658  88.953  1.00 61.02  ? 217 ARG   F N     1 
ATOM   12754 C  CA    . ARG   E 4  217 ? -10.476 54.505  90.159  1.00 55.67  ? 217 ARG   F CA    1 
ATOM   12755 C  C     . ARG   E 4  217 ? -10.178 53.197  90.883  1.00 62.16  ? 217 ARG   F C     1 
ATOM   12756 O  O     . ARG   E 4  217 ? -10.324 53.127  92.108  1.00 63.64  ? 217 ARG   F O     1 
ATOM   12757 C  CB    . ARG   E 4  217 ? -11.963 54.614  89.831  1.00 48.05  ? 217 ARG   F CB    1 
ATOM   12758 C  CG    . ARG   E 4  217 ? -12.425 53.851  88.626  1.00 50.73  ? 217 ARG   F CG    1 
ATOM   12759 C  CD    . ARG   E 4  217 ? -13.940 53.887  88.574  1.00 55.00  ? 217 ARG   F CD    1 
ATOM   12760 N  NE    . ARG   E 4  217 ? -14.515 53.388  87.324  1.00 68.00  ? 217 ARG   F NE    1 
ATOM   12761 C  CZ    . ARG   E 4  217 ? -14.376 52.155  86.847  1.00 59.27  ? 217 ARG   F CZ    1 
ATOM   12762 N  NH1   . ARG   E 4  217 ? -13.566 51.272  87.420  1.00 63.18  ? 217 ARG   F NH1   1 
ATOM   12763 N  NH2   . ARG   E 4  217 ? -15.064 51.801  85.764  1.00 49.75  ? 217 ARG   F NH2   1 
ATOM   12764 N  N     . GLU   E 4  218 ? -9.733  52.172  90.157  1.00 58.47  ? 218 GLU   F N     1 
ATOM   12765 C  CA    . GLU   E 4  218 ? -9.327  50.905  90.748  1.00 51.70  ? 218 GLU   F CA    1 
ATOM   12766 C  C     . GLU   E 4  218 ? -7.873  50.956  91.199  1.00 46.27  ? 218 GLU   F C     1 
ATOM   12767 O  O     . GLU   E 4  218 ? -6.986  51.287  90.413  1.00 50.27  ? 218 GLU   F O     1 
ATOM   12768 C  CB    . GLU   E 4  218 ? -9.520  49.770  89.745  1.00 56.16  ? 218 GLU   F CB    1 
ATOM   12769 C  CG    . GLU   E 4  218 ? -10.990 49.476  89.419  1.00 66.61  ? 218 GLU   F CG    1 
ATOM   12770 C  CD    . GLU   E 4  218 ? -11.720 48.736  90.534  1.00 67.37  ? 218 GLU   F CD    1 
ATOM   12771 O  OE1   . GLU   E 4  218 ? -11.207 48.680  91.682  1.00 71.54  ? 218 GLU   F OE1   1 
ATOM   12772 O  OE2   . GLU   E 4  218 ? -12.811 48.200  90.248  1.00 66.07  ? 218 GLU   F OE2   1 
ATOM   12773 N  N     . GLY   E 4  219 ? -7.637  50.630  92.464  1.00 55.91  ? 219 GLY   F N     1 
ATOM   12774 C  CA    . GLY   E 4  219 ? -6.290  50.476  92.986  1.00 48.30  ? 219 GLY   F CA    1 
ATOM   12775 C  C     . GLY   E 4  219 ? -6.096  49.077  93.533  1.00 53.05  ? 219 GLY   F C     1 
ATOM   12776 O  O     . GLY   E 4  219 ? -6.999  48.241  93.394  1.00 50.60  ? 219 GLY   F O     1 
ATOM   12777 N  N     . VAL   E 4  220 ? -4.944  48.796  94.150  1.00 48.86  ? 220 VAL   F N     1 
ATOM   12778 C  CA    . VAL   E 4  220 ? -4.687  47.491  94.759  1.00 59.81  ? 220 VAL   F CA    1 
ATOM   12779 C  C     . VAL   E 4  220 ? -3.896  47.681  96.039  1.00 66.42  ? 220 VAL   F C     1 
ATOM   12780 O  O     . VAL   E 4  220 ? -3.020  48.552  96.116  1.00 60.80  ? 220 VAL   F O     1 
ATOM   12781 C  CB    . VAL   E 4  220 ? -3.913  46.518  93.833  1.00 60.17  ? 220 VAL   F CB    1 
ATOM   12782 C  CG1   . VAL   E 4  220 ? -4.703  46.199  92.569  1.00 68.59  ? 220 VAL   F CG1   1 
ATOM   12783 C  CG2   . VAL   E 4  220 ? -2.533  47.062  93.507  1.00 50.70  ? 220 VAL   F CG2   1 
ATOM   12784 N  N     . LEU   E 4  221 ? -4.199  46.851  97.038  1.00 67.80  ? 221 LEU   F N     1 
ATOM   12785 C  CA    . LEU   E 4  221 ? -3.322  46.654  98.185  1.00 63.32  ? 221 LEU   F CA    1 
ATOM   12786 C  C     . LEU   E 4  221 ? -2.529  45.376  97.948  1.00 70.98  ? 221 LEU   F C     1 
ATOM   12787 O  O     . LEU   E 4  221 ? -3.112  44.323  97.662  1.00 71.37  ? 221 LEU   F O     1 
ATOM   12788 C  CB    . LEU   E 4  221 ? -4.106  46.560  99.499  1.00 68.60  ? 221 LEU   F CB    1 
ATOM   12789 C  CG    . LEU   E 4  221 ? -4.893  47.746  100.076 1.00 64.72  ? 221 LEU   F CG    1 
ATOM   12790 C  CD1   . LEU   E 4  221 ? -6.193  47.987  99.322  1.00 56.53  ? 221 LEU   F CD1   1 
ATOM   12791 C  CD2   . LEU   E 4  221 ? -5.181  47.522  101.557 1.00 59.63  ? 221 LEU   F CD2   1 
ATOM   12792 N  N     . ARG   E 4  222 ? -1.203  45.480  98.026  1.00 74.41  ? 222 ARG   F N     1 
ATOM   12793 C  CA    . ARG   E 4  222 ? -0.313  44.322  97.941  1.00 74.77  ? 222 ARG   F CA    1 
ATOM   12794 C  C     . ARG   E 4  222 ? -0.088  43.824  99.363  1.00 69.21  ? 222 ARG   F C     1 
ATOM   12795 O  O     . ARG   E 4  222 ? 0.745   44.366  100.095 1.00 66.57  ? 222 ARG   F O     1 
ATOM   12796 C  CB    . ARG   E 4  222 ? 1.005   44.691  97.262  1.00 75.16  ? 222 ARG   F CB    1 
ATOM   12797 C  CG    . ARG   E 4  222 ? 1.001   44.623  95.737  1.00 61.74  ? 222 ARG   F CG    1 
ATOM   12798 C  CD    . ARG   E 4  222 ? 0.851   46.002  95.114  1.00 74.65  ? 222 ARG   F CD    1 
ATOM   12799 N  NE    . ARG   E 4  222 ? 1.874   46.942  95.564  1.00 66.51  ? 222 ARG   F NE    1 
ATOM   12800 C  CZ    . ARG   E 4  222 ? 2.912   47.340  94.836  1.00 63.15  ? 222 ARG   F CZ    1 
ATOM   12801 N  NH1   . ARG   E 4  222 ? 3.118   46.885  93.608  1.00 49.97  ? 222 ARG   F NH1   1 
ATOM   12802 N  NH2   . ARG   E 4  222 ? 3.762   48.224  95.352  1.00 61.17  ? 222 ARG   F NH2   1 
ATOM   12803 N  N     . THR   E 4  223 ? -0.828  42.785  99.756  1.00 70.87  ? 223 THR   F N     1 
ATOM   12804 C  CA    . THR   E 4  223 ? -0.899  42.381  101.156 1.00 73.59  ? 223 THR   F CA    1 
ATOM   12805 C  C     . THR   E 4  223 ? 0.304   41.519  101.528 1.00 76.13  ? 223 THR   F C     1 
ATOM   12806 O  O     . THR   E 4  223 ? 1.290   41.424  100.793 1.00 77.34  ? 223 THR   F O     1 
ATOM   12807 C  CB    . THR   E 4  223 ? -2.208  41.650  101.450 1.00 71.03  ? 223 THR   F CB    1 
ATOM   12808 O  OG1   . THR   E 4  223 ? -2.286  40.454  100.664 1.00 67.94  ? 223 THR   F OG1   1 
ATOM   12809 C  CG2   . THR   E 4  223 ? -3.410  42.549  101.158 1.00 71.82  ? 223 THR   F CG2   1 
ATOM   12810 N  N     . SER   E 4  224 ? 0.234   40.902  102.706 1.00 83.80  ? 224 SER   F N     1 
ATOM   12811 C  CA    . SER   E 4  224 ? 1.250   39.987  103.202 1.00 83.18  ? 224 SER   F CA    1 
ATOM   12812 C  C     . SER   E 4  224 ? 0.557   38.715  103.659 1.00 88.31  ? 224 SER   F C     1 
ATOM   12813 O  O     . SER   E 4  224 ? -0.513  38.771  104.274 1.00 88.99  ? 224 SER   F O     1 
ATOM   12814 C  CB    . SER   E 4  224 ? 2.053   40.598  104.360 1.00 77.54  ? 224 SER   F CB    1 
ATOM   12815 O  OG    . SER   E 4  224 ? 3.129   39.758  104.734 1.00 74.50  ? 224 SER   F OG    1 
ATOM   12816 N  N     . SER   E 4  225 ? 1.155   37.568  103.328 1.00 95.28  ? 225 SER   F N     1 
ATOM   12817 C  CA    . SER   E 4  225 ? 0.589   36.294  103.760 1.00 89.59  ? 225 SER   F CA    1 
ATOM   12818 C  C     . SER   E 4  225 ? 0.845   36.058  105.243 1.00 89.99  ? 225 SER   F C     1 
ATOM   12819 O  O     . SER   E 4  225 ? -0.033  35.562  105.958 1.00 87.59  ? 225 SER   F O     1 
ATOM   12820 C  CB    . SER   E 4  225 ? 1.164   35.145  102.925 1.00 90.85  ? 225 SER   F CB    1 
ATOM   12821 O  OG    . SER   E 4  225 ? 0.526   35.045  101.662 1.00 90.82  ? 225 SER   F OG    1 
ATOM   12822 N  N     . GLU   E 4  226 ? 2.032   36.427  105.726 1.00 89.69  ? 226 GLU   F N     1 
ATOM   12823 C  CA    . GLU   E 4  226 ? 2.383   36.094  107.100 1.00 96.23  ? 226 GLU   F CA    1 
ATOM   12824 C  C     . GLU   E 4  226 ? 2.283   37.323  108.004 1.00 95.72  ? 226 GLU   F C     1 
ATOM   12825 O  O     . GLU   E 4  226 ? 2.595   38.439  107.571 1.00 95.46  ? 226 GLU   F O     1 
ATOM   12826 C  CB    . GLU   E 4  226 ? 3.794   35.503  107.160 1.00 91.39  ? 226 GLU   F CB    1 
ATOM   12827 C  CG    . GLU   E 4  226 ? 3.839   33.970  106.970 1.00 99.20  ? 226 GLU   F CG    1 
ATOM   12828 C  CD    . GLU   E 4  226 ? 3.271   33.495  105.627 1.00 102.14 ? 226 GLU   F CD    1 
ATOM   12829 O  OE1   . GLU   E 4  226 ? 3.654   34.069  104.583 1.00 93.50  ? 226 GLU   F OE1   1 
ATOM   12830 O  OE2   . GLU   E 4  226 ? 2.444   32.547  105.618 1.00 96.76  ? 226 GLU   F OE2   1 
ATOM   12831 N  N     . PRO   E 4  227 ? 1.860   37.146  109.260 1.00 95.48  ? 227 PRO   F N     1 
ATOM   12832 C  CA    . PRO   E 4  227 ? 1.465   38.298  110.076 1.00 82.19  ? 227 PRO   F CA    1 
ATOM   12833 C  C     . PRO   E 4  227 ? 2.656   39.150  110.458 1.00 85.32  ? 227 PRO   F C     1 
ATOM   12834 O  O     . PRO   E 4  227 ? 3.772   38.658  110.636 1.00 90.32  ? 227 PRO   F O     1 
ATOM   12835 C  CB    . PRO   E 4  227 ? 0.836   37.655  111.313 1.00 82.58  ? 227 PRO   F CB    1 
ATOM   12836 C  CG    . PRO   E 4  227 ? 1.594   36.392  111.464 1.00 87.90  ? 227 PRO   F CG    1 
ATOM   12837 C  CD    . PRO   E 4  227 ? 1.876   35.904  110.052 1.00 89.69  ? 227 PRO   F CD    1 
ATOM   12838 N  N     . TYR   E 4  228 ? 2.393   40.446  110.604 1.00 91.45  ? 228 TYR   F N     1 
ATOM   12839 C  CA    . TYR   E 4  228 ? 3.459   41.405  110.852 1.00 89.83  ? 228 TYR   F CA    1 
ATOM   12840 C  C     . TYR   E 4  228 ? 4.220   41.042  112.122 1.00 88.99  ? 228 TYR   F C     1 
ATOM   12841 O  O     . TYR   E 4  228 ? 3.642   40.562  113.099 1.00 88.73  ? 228 TYR   F O     1 
ATOM   12842 C  CB    . TYR   E 4  228 ? 2.883   42.820  110.944 1.00 79.48  ? 228 TYR   F CB    1 
ATOM   12843 C  CG    . TYR   E 4  228 ? 3.928   43.882  111.160 1.00 79.05  ? 228 TYR   F CG    1 
ATOM   12844 C  CD1   . TYR   E 4  228 ? 4.940   44.091  110.231 1.00 79.96  ? 228 TYR   F CD1   1 
ATOM   12845 C  CD2   . TYR   E 4  228 ? 3.905   44.679  112.295 1.00 79.27  ? 228 TYR   F CD2   1 
ATOM   12846 C  CE1   . TYR   E 4  228 ? 5.903   45.061  110.431 1.00 75.12  ? 228 TYR   F CE1   1 
ATOM   12847 C  CE2   . TYR   E 4  228 ? 4.863   45.650  112.505 1.00 77.60  ? 228 TYR   F CE2   1 
ATOM   12848 C  CZ    . TYR   E 4  228 ? 5.857   45.840  111.571 1.00 75.57  ? 228 TYR   F CZ    1 
ATOM   12849 O  OH    . TYR   E 4  228 ? 6.802   46.813  111.789 1.00 72.72  ? 228 TYR   F OH    1 
ATOM   12850 N  N     . ASN   E 4  229 ? 5.529   41.271  112.098 1.00 92.02  ? 229 ASN   F N     1 
ATOM   12851 C  CA    . ASN   E 4  229 ? 6.450   40.809  113.132 1.00 94.01  ? 229 ASN   F CA    1 
ATOM   12852 C  C     . ASN   E 4  229 ? 6.902   42.011  113.959 1.00 97.60  ? 229 ASN   F C     1 
ATOM   12853 O  O     . ASN   E 4  229 ? 7.977   42.569  113.737 1.00 96.88  ? 229 ASN   F O     1 
ATOM   12854 C  CB    . ASN   E 4  229 ? 7.653   40.080  112.476 1.00 105.13 ? 229 ASN   F CB    1 
ATOM   12855 C  CG    . ASN   E 4  229 ? 7.881   38.685  113.036 1.00 105.50 ? 229 ASN   F CG    1 
ATOM   12856 O  OD1   . ASN   E 4  229 ? 8.425   38.525  114.128 1.00 105.69 ? 229 ASN   F OD1   1 
ATOM   12857 N  ND2   . ASN   E 4  229 ? 7.492   37.666  112.272 1.00 93.11  ? 229 ASN   F ND2   1 
ATOM   12858 N  N     . SER   E 4  230 ? 6.067   42.409  114.925 1.00 97.17  ? 230 SER   F N     1 
ATOM   12859 C  CA    . SER   E 4  230 ? 6.414   43.505  115.826 1.00 104.05 ? 230 SER   F CA    1 
ATOM   12860 C  C     . SER   E 4  230 ? 7.876   43.399  116.245 1.00 107.87 ? 230 SER   F C     1 
ATOM   12861 O  O     . SER   E 4  230 ? 8.744   44.052  115.658 1.00 94.92  ? 230 SER   F O     1 
ATOM   12862 C  CB    . SER   E 4  230 ? 5.506   43.514  117.062 1.00 110.34 ? 230 SER   F CB    1 
ATOM   12863 O  OG    . SER   E 4  230 ? 4.175   43.884  116.736 1.00 102.14 ? 230 SER   F OG    1 
ATOM   12864 N  N     . ALA   E 4  231 ? 8.163   42.565  117.241 1.00 120.92 ? 231 ALA   F N     1 
ATOM   12865 C  CA    . ALA   E 4  231 ? 9.543   42.347  117.655 1.00 127.06 ? 231 ALA   F CA    1 
ATOM   12866 C  C     . ALA   E 4  231 ? 10.296  41.561  116.584 1.00 118.97 ? 231 ALA   F C     1 
ATOM   12867 O  O     . ALA   E 4  231 ? 9.802   40.548  116.079 1.00 115.11 ? 231 ALA   F O     1 
ATOM   12868 C  CB    . ALA   E 4  231 ? 9.590   41.612  118.996 1.00 111.73 ? 231 ALA   F CB    1 
ATOM   12869 N  N     . ASN   E 4  232 ? 11.491  42.038  116.230 1.00 118.51 ? 232 ASN   F N     1 
ATOM   12870 C  CA    . ASN   E 4  232 ? 12.316  41.374  115.227 1.00 121.86 ? 232 ASN   F CA    1 
ATOM   12871 C  C     . ASN   E 4  232 ? 11.757  41.567  113.821 1.00 116.75 ? 232 ASN   F C     1 
ATOM   12872 O  O     . ASN   E 4  232 ? 10.673  41.066  113.507 1.00 117.26 ? 232 ASN   F O     1 
ATOM   12873 C  CB    . ASN   E 4  232 ? 12.438  39.882  115.550 1.00 122.59 ? 232 ASN   F CB    1 
ATOM   12874 C  CG    . ASN   E 4  232 ? 12.499  39.016  114.303 1.00 131.04 ? 232 ASN   F CG    1 
ATOM   12875 O  OD1   . ASN   E 4  232 ? 11.467  38.635  113.747 1.00 128.44 ? 232 ASN   F OD1   1 
ATOM   12876 N  ND2   . ASN   E 4  232 ? 13.711  38.698  113.861 1.00 132.08 ? 232 ASN   F ND2   1 
ATOM   12877 N  N     . PHE   E 4  233 ? 12.483  42.294  112.964 1.00 115.04 ? 233 PHE   F N     1 
ATOM   12878 C  CA    . PHE   E 4  233 ? 12.081  42.452  111.571 1.00 120.76 ? 233 PHE   F CA    1 
ATOM   12879 C  C     . PHE   E 4  233 ? 13.124  42.014  110.554 1.00 127.24 ? 233 PHE   F C     1 
ATOM   12880 O  O     . PHE   E 4  233 ? 12.761  41.813  109.389 1.00 129.01 ? 233 PHE   F O     1 
ATOM   12881 C  CB    . PHE   E 4  233 ? 11.693  43.908  111.241 1.00 110.17 ? 233 PHE   F CB    1 
ATOM   12882 C  CG    . PHE   E 4  233 ? 12.143  44.931  112.249 1.00 104.34 ? 233 PHE   F CG    1 
ATOM   12883 C  CD1   . PHE   E 4  233 ? 13.467  45.018  112.641 1.00 102.24 ? 233 PHE   F CD1   1 
ATOM   12884 C  CD2   . PHE   E 4  233 ? 11.236  45.845  112.761 1.00 88.99  ? 233 PHE   F CD2   1 
ATOM   12885 C  CE1   . PHE   E 4  233 ? 13.865  45.968  113.558 1.00 98.91  ? 233 PHE   F CE1   1 
ATOM   12886 C  CE2   . PHE   E 4  233 ? 11.631  46.800  113.667 1.00 84.14  ? 233 PHE   F CE2   1 
ATOM   12887 C  CZ    . PHE   E 4  233 ? 12.945  46.862  114.069 1.00 88.08  ? 233 PHE   F CZ    1 
ATOM   12888 N  N     . GLN   E 4  234 ? 14.390  41.855  110.939 1.00 127.52 ? 234 GLN   F N     1 
ATOM   12889 C  CA    . GLN   E 4  234 ? 15.414  41.509  109.957 1.00 123.26 ? 234 GLN   F CA    1 
ATOM   12890 C  C     . GLN   E 4  234 ? 15.188  40.117  109.375 1.00 130.64 ? 234 GLN   F C     1 
ATOM   12891 O  O     . GLN   E 4  234 ? 16.117  39.305  109.325 1.00 134.86 ? 234 GLN   F O     1 
ATOM   12892 C  CB    . GLN   E 4  234 ? 16.811  41.602  110.574 1.00 119.11 ? 234 GLN   F CB    1 
ATOM   12893 C  CG    . GLN   E 4  234 ? 17.220  43.009  110.996 1.00 128.61 ? 234 GLN   F CG    1 
ATOM   12894 C  CD    . GLN   E 4  234 ? 18.694  43.107  111.375 1.00 130.18 ? 234 GLN   F CD    1 
ATOM   12895 O  OE1   . GLN   E 4  234 ? 19.476  42.192  111.106 1.00 137.49 ? 234 GLN   F OE1   1 
ATOM   12896 N  NE2   . GLN   E 4  234 ? 19.078  44.222  111.999 1.00 110.92 ? 234 GLN   F NE2   1 
ATOM   12897 N  N     . ASP   E 4  235 ? 13.963  39.829  108.929 1.00 130.45 ? 235 ASP   F N     1 
ATOM   12898 C  CA    . ASP   E 4  235 ? 13.654  38.586  108.228 1.00 128.87 ? 235 ASP   F CA    1 
ATOM   12899 C  C     . ASP   E 4  235 ? 12.961  38.822  106.893 1.00 127.72 ? 235 ASP   F C     1 
ATOM   12900 O  O     . ASP   E 4  235 ? 13.314  38.169  105.906 1.00 130.84 ? 235 ASP   F O     1 
ATOM   12901 C  CB    . ASP   E 4  235 ? 12.789  37.655  109.113 1.00 126.69 ? 235 ASP   F CB    1 
ATOM   12902 C  CG    . ASP   E 4  235 ? 11.317  38.031  109.107 1.00 118.82 ? 235 ASP   F CG    1 
ATOM   12903 O  OD1   . ASP   E 4  235 ? 10.964  39.104  109.638 1.00 119.07 ? 235 ASP   F OD1   1 
ATOM   12904 O  OD2   . ASP   E 4  235 ? 10.512  37.251  108.558 1.00 112.55 ? 235 ASP   F OD2   1 
ATOM   12905 N  N     . LYS   E 4  236 ? 11.988  39.738  106.838 1.00 117.17 ? 236 LYS   F N     1 
ATOM   12906 C  CA    . LYS   E 4  236 ? 11.319  40.118  105.598 1.00 106.28 ? 236 LYS   F CA    1 
ATOM   12907 C  C     . LYS   E 4  236 ? 10.195  39.147  105.251 1.00 108.00 ? 236 LYS   F C     1 
ATOM   12908 O  O     . LYS   E 4  236 ? 9.856   38.274  106.056 1.00 114.78 ? 236 LYS   F O     1 
ATOM   12909 C  CB    . LYS   E 4  236 ? 12.344  40.221  104.464 1.00 113.43 ? 236 LYS   F CB    1 
ATOM   12910 C  CG    . LYS   E 4  236 ? 13.455  41.224  104.777 1.00 113.73 ? 236 LYS   F CG    1 
ATOM   12911 C  CD    . LYS   E 4  236 ? 14.623  41.145  103.809 1.00 99.96  ? 236 LYS   F CD    1 
ATOM   12912 C  CE    . LYS   E 4  236 ? 15.662  42.203  104.151 1.00 96.36  ? 236 LYS   F CE    1 
ATOM   12913 N  NZ    . LYS   E 4  236 ? 16.870  42.110  103.288 1.00 100.72 ? 236 LYS   F NZ    1 
ATOM   12914 N  N     . THR   E 4  237 ? 9.604   39.302  104.064 1.00 101.06 ? 237 THR   F N     1 
ATOM   12915 C  CA    . THR   E 4  237 ? 8.406   38.571  103.653 1.00 95.84  ? 237 THR   F CA    1 
ATOM   12916 C  C     . THR   E 4  237 ? 7.160   39.134  104.328 1.00 94.86  ? 237 THR   F C     1 
ATOM   12917 O  O     . THR   E 4  237 ? 6.184   39.472  103.651 1.00 94.36  ? 237 THR   F O     1 
ATOM   12918 C  CB    . THR   E 4  237 ? 8.515   37.070  103.951 1.00 97.12  ? 237 THR   F CB    1 
ATOM   12919 O  OG1   . THR   E 4  237 ? 8.449   36.852  105.363 1.00 103.56 ? 237 THR   F OG1   1 
ATOM   12920 C  CG2   . THR   E 4  237 ? 9.815   36.499  103.413 1.00 111.00 ? 237 THR   F CG2   1 
ATOM   12921 N  N     . CYS   E 4  238 ? 7.172   39.236  105.660 1.00 103.28 ? 238 CYS   F N     1 
ATOM   12922 C  CA    . CYS   E 4  238 ? 6.022   39.763  106.387 1.00 96.77  ? 238 CYS   F CA    1 
ATOM   12923 C  C     . CYS   E 4  238 ? 6.054   41.278  106.540 1.00 94.65  ? 238 CYS   F C     1 
ATOM   12924 O  O     . CYS   E 4  238 ? 4.994   41.885  106.740 1.00 90.28  ? 238 CYS   F O     1 
ATOM   12925 C  CB    . CYS   E 4  238 ? 5.924   39.129  107.776 1.00 89.94  ? 238 CYS   F CB    1 
ATOM   12926 S  SG    . CYS   E 4  238 ? 6.904   39.981  109.033 1.00 90.41  ? 238 CYS   F SG    1 
ATOM   12927 N  N     . HIS   E 4  239 ? 7.237   41.898  106.470 1.00 93.44  ? 239 HIS   F N     1 
ATOM   12928 C  CA    . HIS   E 4  239 ? 7.344   43.364  106.404 1.00 97.28  ? 239 HIS   F CA    1 
ATOM   12929 C  C     . HIS   E 4  239 ? 7.264   43.836  104.954 1.00 96.50  ? 239 HIS   F C     1 
ATOM   12930 O  O     . HIS   E 4  239 ? 6.300   44.497  104.556 1.00 95.69  ? 239 HIS   F O     1 
ATOM   12931 C  CB    . HIS   E 4  239 ? 8.645   43.846  107.045 1.00 90.52  ? 239 HIS   F CB    1 
ATOM   12932 C  CG    . HIS   E 4  239 ? 8.705   43.646  108.523 1.00 94.60  ? 239 HIS   F CG    1 
ATOM   12933 N  ND1   . HIS   E 4  239 ? 8.525   42.416  109.115 1.00 106.90 ? 239 HIS   F ND1   1 
ATOM   12934 C  CD2   . HIS   E 4  239 ? 8.951   44.517  109.528 1.00 93.52  ? 239 HIS   F CD2   1 
ATOM   12935 C  CE1   . HIS   E 4  239 ? 8.650   42.539  110.424 1.00 103.55 ? 239 HIS   F CE1   1 
ATOM   12936 N  NE2   . HIS   E 4  239 ? 8.904   43.805  110.701 1.00 97.93  ? 239 HIS   F NE2   1 
ATOM   12937 N  N     . LEU   E 4  240 ? 8.283   43.511  104.160 1.00 90.69  ? 240 LEU   F N     1 
ATOM   12938 C  CA    . LEU   E 4  240 ? 8.328   43.935  102.766 1.00 84.38  ? 240 LEU   F CA    1 
ATOM   12939 C  C     . LEU   E 4  240 ? 7.244   43.205  101.985 1.00 81.56  ? 240 LEU   F C     1 
ATOM   12940 O  O     . LEU   E 4  240 ? 7.285   41.980  101.841 1.00 86.68  ? 240 LEU   F O     1 
ATOM   12941 C  CB    . LEU   E 4  240 ? 9.720   43.688  102.194 1.00 82.61  ? 240 LEU   F CB    1 
ATOM   12942 C  CG    . LEU   E 4  240 ? 10.723  44.697  102.776 1.00 79.49  ? 240 LEU   F CG    1 
ATOM   12943 C  CD1   . LEU   E 4  240 ? 11.861  44.047  103.555 1.00 79.08  ? 240 LEU   F CD1   1 
ATOM   12944 C  CD2   . LEU   E 4  240 ? 11.262  45.605  101.683 1.00 96.74  ? 240 LEU   F CD2   1 
ATOM   12945 N  N     . THR   E 4  241 ? 6.265   43.963  101.491 1.00 84.65  ? 241 THR   F N     1 
ATOM   12946 C  CA    . THR   E 4  241 ? 5.047   43.424  100.900 1.00 80.68  ? 241 THR   F CA    1 
ATOM   12947 C  C     . THR   E 4  241 ? 5.124   43.312  99.384  1.00 80.89  ? 241 THR   F C     1 
ATOM   12948 O  O     . THR   E 4  241 ? 4.083   43.175  98.727  1.00 78.14  ? 241 THR   F O     1 
ATOM   12949 C  CB    . THR   E 4  241 ? 3.855   44.292  101.299 1.00 75.44  ? 241 THR   F CB    1 
ATOM   12950 O  OG1   . THR   E 4  241 ? 4.278   45.657  101.382 1.00 71.25  ? 241 THR   F OG1   1 
ATOM   12951 C  CG2   . THR   E 4  241 ? 3.306   43.863  102.649 1.00 80.30  ? 241 THR   F CG2   1 
ATOM   12952 N  N     . ASN   E 4  242 ? 6.330   43.363  98.819  1.00 80.56  ? 242 ASN   F N     1 
ATOM   12953 C  CA    . ASN   E 4  242 ? 6.486   43.323  97.371  1.00 94.37  ? 242 ASN   F CA    1 
ATOM   12954 C  C     . ASN   E 4  242 ? 6.002   41.989  96.819  1.00 96.08  ? 242 ASN   F C     1 
ATOM   12955 O  O     . ASN   E 4  242 ? 6.345   40.927  97.343  1.00 104.06 ? 242 ASN   F O     1 
ATOM   12956 C  CB    . ASN   E 4  242 ? 7.947   43.562  96.995  1.00 96.02  ? 242 ASN   F CB    1 
ATOM   12957 C  CG    . ASN   E 4  242 ? 8.432   44.938  97.407  1.00 92.30  ? 242 ASN   F CG    1 
ATOM   12958 O  OD1   . ASN   E 4  242 ? 8.409   45.881  96.615  1.00 94.02  ? 242 ASN   F OD1   1 
ATOM   12959 N  ND2   . ASN   E 4  242 ? 8.867   45.062  98.656  1.00 96.65  ? 242 ASN   F ND2   1 
ATOM   12960 N  N     . HIS   E 4  243 ? 5.208   42.053  95.748  1.00 84.14  ? 243 HIS   F N     1 
ATOM   12961 C  CA    . HIS   E 4  243 ? 4.553   40.858  95.222  1.00 91.80  ? 243 HIS   F CA    1 
ATOM   12962 C  C     . HIS   E 4  243 ? 5.526   39.696  95.031  1.00 104.79 ? 243 HIS   F C     1 
ATOM   12963 O  O     . HIS   E 4  243 ? 5.161   38.533  95.238  1.00 104.25 ? 243 HIS   F O     1 
ATOM   12964 C  CB    . HIS   E 4  243 ? 3.860   41.189  93.903  1.00 88.92  ? 243 HIS   F CB    1 
ATOM   12965 C  CG    . HIS   E 4  243 ? 2.855   40.169  93.479  1.00 84.06  ? 243 HIS   F CG    1 
ATOM   12966 N  ND1   . HIS   E 4  243 ? 1.588   40.507  93.055  1.00 81.26  ? 243 HIS   F ND1   1 
ATOM   12967 C  CD2   . HIS   E 4  243 ? 2.927   38.819  93.410  1.00 88.62  ? 243 HIS   F CD2   1 
ATOM   12968 C  CE1   . HIS   E 4  243 ? 0.923   39.409  92.744  1.00 89.42  ? 243 HIS   F CE1   1 
ATOM   12969 N  NE2   . HIS   E 4  243 ? 1.712   38.370  92.951  1.00 94.60  ? 243 HIS   F NE2   1 
ATOM   12970 N  N     . CYS   E 4  244 ? 6.767   39.982  94.631  1.00 107.36 ? 244 CYS   F N     1 
ATOM   12971 C  CA    . CYS   E 4  244 ? 7.707   38.896  94.366  1.00 105.81 ? 244 CYS   F CA    1 
ATOM   12972 C  C     . CYS   E 4  244 ? 8.124   38.193  95.656  1.00 106.25 ? 244 CYS   F C     1 
ATOM   12973 O  O     . CYS   E 4  244 ? 8.051   36.963  95.754  1.00 109.38 ? 244 CYS   F O     1 
ATOM   12974 C  CB    . CYS   E 4  244 ? 8.925   39.427  93.606  1.00 112.67 ? 244 CYS   F CB    1 
ATOM   12975 S  SG    . CYS   E 4  244 ? 9.853   40.724  94.451  1.00 126.12 ? 244 CYS   F SG    1 
ATOM   12976 N  N     . ILE   E 4  245 ? 8.542   38.958  96.668  1.00 107.01 ? 245 ILE   F N     1 
ATOM   12977 C  CA    . ILE   E 4  245 ? 8.988   38.402  97.947  1.00 113.34 ? 245 ILE   F CA    1 
ATOM   12978 C  C     . ILE   E 4  245 ? 7.786   37.889  98.742  1.00 109.27 ? 245 ILE   F C     1 
ATOM   12979 O  O     . ILE   E 4  245 ? 7.843   37.747  99.969  1.00 105.74 ? 245 ILE   F O     1 
ATOM   12980 C  CB    . ILE   E 4  245 ? 9.804   39.448  98.740  1.00 106.91 ? 245 ILE   F CB    1 
ATOM   12981 C  CG1   . ILE   E 4  245 ? 11.067  39.827  97.964  1.00 117.65 ? 245 ILE   F CG1   1 
ATOM   12982 C  CG2   . ILE   E 4  245 ? 10.220  38.930  100.111 1.00 100.55 ? 245 ILE   F CG2   1 
ATOM   12983 C  CD1   . ILE   E 4  245 ? 12.035  38.670  97.760  1.00 115.89 ? 245 ILE   F CD1   1 
ATOM   12984 N  N     . GLN   E 4  246 ? 6.691   37.593  98.046  1.00 101.42 ? 246 GLN   F N     1 
ATOM   12985 C  CA    . GLN   E 4  246 ? 5.518   37.006  98.684  1.00 93.67  ? 246 GLN   F CA    1 
ATOM   12986 C  C     . GLN   E 4  246 ? 4.848   35.924  97.859  1.00 99.98  ? 246 GLN   F C     1 
ATOM   12987 O  O     . GLN   E 4  246 ? 4.084   35.133  98.425  1.00 94.74  ? 246 GLN   F O     1 
ATOM   12988 C  CB    . GLN   E 4  246 ? 4.492   38.088  99.018  1.00 88.45  ? 246 GLN   F CB    1 
ATOM   12989 C  CG    . GLN   E 4  246 ? 4.886   38.932  100.213 1.00 89.11  ? 246 GLN   F CG    1 
ATOM   12990 C  CD    . GLN   E 4  246 ? 3.880   38.837  101.338 1.00 79.36  ? 246 GLN   F CD    1 
ATOM   12991 O  OE1   . GLN   E 4  246 ? 2.786   38.299  101.162 1.00 76.36  ? 246 GLN   F OE1   1 
ATOM   12992 N  NE2   . GLN   E 4  246 ? 4.240   39.363  102.501 1.00 83.96  ? 246 GLN   F NE2   1 
ATOM   12993 N  N     . LYS   E 4  247 ? 5.068   35.873  96.546  1.00 107.01 ? 247 LYS   F N     1 
ATOM   12994 C  CA    . LYS   E 4  247 ? 4.838   34.658  95.769  1.00 103.47 ? 247 LYS   F CA    1 
ATOM   12995 C  C     . LYS   E 4  247 ? 6.107   33.808  95.809  1.00 109.30 ? 247 LYS   F C     1 
ATOM   12996 O  O     . LYS   E 4  247 ? 6.754   33.522  94.801  1.00 104.95 ? 247 LYS   F O     1 
ATOM   12997 C  CB    . LYS   E 4  247 ? 4.422   34.997  94.343  1.00 91.90  ? 247 LYS   F CB    1 
ATOM   12998 C  CG    . LYS   E 4  247 ? 2.916   34.936  94.102  1.00 99.01  ? 247 LYS   F CG    1 
ATOM   12999 C  CD    . LYS   E 4  247 ? 2.610   35.285  92.657  1.00 103.96 ? 247 LYS   F CD    1 
ATOM   13000 C  CE    . LYS   E 4  247 ? 1.192   34.931  92.255  1.00 96.08  ? 247 LYS   F CE    1 
ATOM   13001 N  NZ    . LYS   E 4  247 ? 1.059   34.992  90.767  1.00 91.73  ? 247 LYS   F NZ    1 
ATOM   13002 N  N     . GLU   E 4  248 ? 6.464   33.436  97.039  1.00 107.64 ? 248 GLU   F N     1 
ATOM   13003 C  CA    . GLU   E 4  248 ? 7.705   32.734  97.323  1.00 100.84 ? 248 GLU   F CA    1 
ATOM   13004 C  C     . GLU   E 4  248 ? 7.817   32.441  98.817  1.00 103.50 ? 248 GLU   F C     1 
ATOM   13005 O  O     . GLU   E 4  248 ? 8.889   32.054  99.289  1.00 105.72 ? 248 GLU   F O     1 
ATOM   13006 C  CB    . GLU   E 4  248 ? 8.898   33.563  96.839  1.00 102.17 ? 248 GLU   F CB    1 
ATOM   13007 C  CG    . GLU   E 4  248 ? 10.244  32.867  96.923  1.00 105.13 ? 248 GLU   F CG    1 
ATOM   13008 C  CD    . GLU   E 4  248 ? 11.401  33.848  96.957  1.00 106.50 ? 248 GLU   F CD    1 
ATOM   13009 O  OE1   . GLU   E 4  248 ? 11.149  35.067  96.868  1.00 107.02 ? 248 GLU   F OE1   1 
ATOM   13010 O  OE2   . GLU   E 4  248 ? 12.561  33.404  97.083  1.00 97.18  ? 248 GLU   F OE2   1 
ATOM   13011 N  N     . TYR   E 4  249 ? 6.727   32.642  99.573  1.00 104.68 ? 249 TYR   F N     1 
ATOM   13012 C  CA    . TYR   E 4  249 ? 6.693   32.317  101.002 1.00 105.62 ? 249 TYR   F CA    1 
ATOM   13013 C  C     . TYR   E 4  249 ? 5.274   32.111  101.539 1.00 100.72 ? 249 TYR   F C     1 
ATOM   13014 O  O     . TYR   E 4  249 ? 5.114   31.621  102.661 1.00 103.94 ? 249 TYR   F O     1 
ATOM   13015 C  CB    . TYR   E 4  249 ? 7.374   33.408  101.847 1.00 105.77 ? 249 TYR   F CB    1 
ATOM   13016 C  CG    . TYR   E 4  249 ? 8.813   33.727  101.484 1.00 115.79 ? 249 TYR   F CG    1 
ATOM   13017 C  CD1   . TYR   E 4  249 ? 9.106   34.698  100.532 1.00 123.15 ? 249 TYR   F CD1   1 
ATOM   13018 C  CD2   . TYR   E 4  249 ? 9.875   33.069  102.095 1.00 112.79 ? 249 TYR   F CD2   1 
ATOM   13019 C  CE1   . TYR   E 4  249 ? 10.416  35.002  100.187 1.00 124.98 ? 249 TYR   F CE1   1 
ATOM   13020 C  CE2   . TYR   E 4  249 ? 11.193  33.369  101.758 1.00 119.33 ? 249 TYR   F CE2   1 
ATOM   13021 C  CZ    . TYR   E 4  249 ? 11.456  34.337  100.801 1.00 126.21 ? 249 TYR   F CZ    1 
ATOM   13022 O  OH    . TYR   E 4  249 ? 12.754  34.649  100.452 1.00 119.37 ? 249 TYR   F OH    1 
ATOM   13023 N  N     . SER   E 4  250 ? 4.244   32.475  100.768 1.00 102.72 ? 250 SER   F N     1 
ATOM   13024 C  CA    . SER   E 4  250 ? 2.850   32.476  101.263 1.00 102.82 ? 250 SER   F CA    1 
ATOM   13025 C  C     . SER   E 4  250 ? 2.470   31.163  101.948 1.00 96.35  ? 250 SER   F C     1 
ATOM   13026 O  O     . SER   E 4  250 ? 1.693   31.158  102.905 1.00 89.22  ? 250 SER   F O     1 
ATOM   13027 C  CB    . SER   E 4  250 ? 1.855   32.767  100.119 1.00 97.12  ? 250 SER   F CB    1 
ATOM   13028 O  OG    . SER   E 4  250 ? 0.505   32.858  100.580 1.00 72.34  ? 250 SER   F OG    1 
ATOM   13029 N  N     . ARG   E 4  255 ? -3.710  33.047  100.433 1.00 60.18  ? 255 ARG   F N     1 
ATOM   13030 C  CA    . ARG   E 4  255 ? -4.489  32.541  101.568 1.00 74.96  ? 255 ARG   F CA    1 
ATOM   13031 C  C     . ARG   E 4  255 ? -5.846  33.223  101.732 1.00 91.89  ? 255 ARG   F C     1 
ATOM   13032 O  O     . ARG   E 4  255 ? -6.884  32.555  101.833 1.00 84.35  ? 255 ARG   F O     1 
ATOM   13033 C  CB    . ARG   E 4  255 ? -3.715  32.694  102.874 1.00 80.10  ? 255 ARG   F CB    1 
ATOM   13034 C  CG    . ARG   E 4  255 ? -4.620  32.605  104.103 1.00 84.51  ? 255 ARG   F CG    1 
ATOM   13035 C  CD    . ARG   E 4  255 ? -3.900  32.035  105.327 1.00 93.95  ? 255 ARG   F CD    1 
ATOM   13036 N  NE    . ARG   E 4  255 ? -4.845  31.553  106.331 1.00 104.26 ? 255 ARG   F NE    1 
ATOM   13037 C  CZ    . ARG   E 4  255 ? -4.503  30.998  107.488 1.00 106.33 ? 255 ARG   F CZ    1 
ATOM   13038 N  NH1   . ARG   E 4  255 ? -3.233  30.851  107.837 1.00 81.97  ? 255 ARG   F NH1   1 
ATOM   13039 N  NH2   . ARG   E 4  255 ? -5.460  30.581  108.316 1.00 100.90 ? 255 ARG   F NH2   1 
ATOM   13040 N  N     . TYR   E 4  256 ? -5.827  34.558  101.796 1.00 94.40  ? 256 TYR   F N     1 
ATOM   13041 C  CA    . TYR   E 4  256 ? -7.042  35.359  101.883 1.00 86.08  ? 256 TYR   F CA    1 
ATOM   13042 C  C     . TYR   E 4  256 ? -7.345  36.137  100.611 1.00 86.96  ? 256 TYR   F C     1 
ATOM   13043 O  O     . TYR   E 4  256 ? -8.515  36.428  100.341 1.00 87.05  ? 256 TYR   F O     1 
ATOM   13044 C  CB    . TYR   E 4  256 ? -6.955  36.351  103.048 1.00 72.37  ? 256 TYR   F CB    1 
ATOM   13045 C  CG    . TYR   E 4  256 ? -5.988  35.978  104.154 1.00 77.01  ? 256 TYR   F CG    1 
ATOM   13046 C  CD1   . TYR   E 4  256 ? -4.630  36.247  104.040 1.00 76.95  ? 256 TYR   F CD1   1 
ATOM   13047 C  CD2   . TYR   E 4  256 ? -6.441  35.400  105.333 1.00 85.56  ? 256 TYR   F CD2   1 
ATOM   13048 C  CE1   . TYR   E 4  256 ? -3.748  35.932  105.059 1.00 76.17  ? 256 TYR   F CE1   1 
ATOM   13049 C  CE2   . TYR   E 4  256 ? -5.565  35.083  106.357 1.00 83.22  ? 256 TYR   F CE2   1 
ATOM   13050 C  CZ    . TYR   E 4  256 ? -4.221  35.349  106.213 1.00 78.49  ? 256 TYR   F CZ    1 
ATOM   13051 O  OH    . TYR   E 4  256 ? -3.353  35.035  107.233 1.00 76.59  ? 256 TYR   F OH    1 
ATOM   13052 N  N     . GLU   E 4  257 ? -6.321  36.490  99.835  1.00 78.14  ? 257 GLU   F N     1 
ATOM   13053 C  CA    . GLU   E 4  257 ? -6.494  37.162  98.556  1.00 81.27  ? 257 GLU   F CA    1 
ATOM   13054 C  C     . GLU   E 4  257 ? -5.784  36.366  97.474  1.00 77.97  ? 257 GLU   F C     1 
ATOM   13055 O  O     . GLU   E 4  257 ? -4.666  35.890  97.684  1.00 71.87  ? 257 GLU   F O     1 
ATOM   13056 C  CB    . GLU   E 4  257 ? -5.932  38.595  98.579  1.00 76.02  ? 257 GLU   F CB    1 
ATOM   13057 C  CG    . GLU   E 4  257 ? -6.543  39.512  99.603  1.00 66.46  ? 257 GLU   F CG    1 
ATOM   13058 C  CD    . GLU   E 4  257 ? -5.817  39.457  100.925 1.00 78.84  ? 257 GLU   F CD    1 
ATOM   13059 O  OE1   . GLU   E 4  257 ? -4.572  39.590  100.929 1.00 75.54  ? 257 GLU   F OE1   1 
ATOM   13060 O  OE2   . GLU   E 4  257 ? -6.494  39.272  101.962 1.00 85.96  ? 257 GLU   F OE2   1 
ATOM   13061 N  N     . GLU   E 4  258 ? -6.425  36.236  96.313  1.00 75.12  ? 258 GLU   F N     1 
ATOM   13062 C  CA    . GLU   E 4  258 ? -5.762  35.637  95.160  1.00 76.19  ? 258 GLU   F CA    1 
ATOM   13063 C  C     . GLU   E 4  258 ? -4.551  36.472  94.757  1.00 82.34  ? 258 GLU   F C     1 
ATOM   13064 O  O     . GLU   E 4  258 ? -4.682  37.667  94.470  1.00 84.31  ? 258 GLU   F O     1 
ATOM   13065 C  CB    . GLU   E 4  258 ? -6.740  35.514  93.992  1.00 77.18  ? 258 GLU   F CB    1 
ATOM   13066 C  CG    . GLU   E 4  258 ? -6.162  34.803  92.763  1.00 85.56  ? 258 GLU   F CG    1 
ATOM   13067 C  CD    . GLU   E 4  258 ? -7.166  34.673  91.625  1.00 91.47  ? 258 GLU   F CD    1 
ATOM   13068 O  OE1   . GLU   E 4  258 ? -8.381  34.827  91.874  1.00 98.56  ? 258 GLU   F OE1   1 
ATOM   13069 O  OE2   . GLU   E 4  258 ? -6.743  34.417  90.478  1.00 85.18  ? 258 GLU   F OE2   1 
ATOM   13070 N  N     . GLY   E 4  259 ? -3.373  35.840  94.718  1.00 89.27  ? 259 GLY   F N     1 
ATOM   13071 C  CA    . GLY   E 4  259 ? -2.143  36.518  94.349  1.00 78.40  ? 259 GLY   F CA    1 
ATOM   13072 C  C     . GLY   E 4  259 ? -1.656  37.524  95.358  1.00 78.00  ? 259 GLY   F C     1 
ATOM   13073 O  O     . GLY   E 4  259 ? -0.609  38.151  95.129  1.00 77.75  ? 259 GLY   F O     1 
ATOM   13074 N  N     . ASN   E 4  260 ? -2.368  37.693  96.464  1.00 69.51  ? 260 ASN   F N     1 
ATOM   13075 C  CA    . ASN   E 4  260 ? -2.080  38.670  97.494  1.00 74.75  ? 260 ASN   F CA    1 
ATOM   13076 C  C     . ASN   E 4  260 ? -2.555  40.064  97.100  1.00 76.55  ? 260 ASN   F C     1 
ATOM   13077 O  O     . ASN   E 4  260 ? -2.054  41.073  97.616  1.00 68.32  ? 260 ASN   F O     1 
ATOM   13078 C  CB    . ASN   E 4  260 ? -0.589  38.681  97.849  1.00 74.07  ? 260 ASN   F CB    1 
ATOM   13079 C  CG    . ASN   E 4  260 ? -0.321  38.165  99.252  1.00 75.59  ? 260 ASN   F CG    1 
ATOM   13080 O  OD1   . ASN   E 4  260 ? -1.247  37.788  99.964  1.00 87.92  ? 260 ASN   F OD1   1 
ATOM   13081 N  ND2   . ASN   E 4  260 ? 0.948   38.140  99.652  1.00 73.60  ? 260 ASN   F ND2   1 
ATOM   13082 N  N     . GLU   E 4  261 ? -3.532  40.147  96.204  1.00 80.63  ? 261 GLU   F N     1 
ATOM   13083 C  CA    . GLU   E 4  261 ? -4.064  41.415  95.720  1.00 77.88  ? 261 GLU   F CA    1 
ATOM   13084 C  C     . GLU   E 4  261 ? -5.439  41.642  96.338  1.00 69.67  ? 261 GLU   F C     1 
ATOM   13085 O  O     . GLU   E 4  261 ? -6.380  40.888  96.062  1.00 69.71  ? 261 GLU   F O     1 
ATOM   13086 C  CB    . GLU   E 4  261 ? -4.139  41.418  94.194  1.00 69.48  ? 261 GLU   F CB    1 
ATOM   13087 C  CG    . GLU   E 4  261 ? -2.849  40.995  93.527  1.00 64.34  ? 261 GLU   F CG    1 
ATOM   13088 C  CD    . GLU   E 4  261 ? -2.905  41.114  92.020  1.00 72.36  ? 261 GLU   F CD    1 
ATOM   13089 O  OE1   . GLU   E 4  261 ? -4.025  41.140  91.456  1.00 72.14  ? 261 GLU   F OE1   1 
ATOM   13090 O  OE2   . GLU   E 4  261 ? -1.824  41.192  91.400  1.00 71.38  ? 261 GLU   F OE2   1 
ATOM   13091 N  N     . MET   E 4  262 ? -5.553  42.677  97.172  1.00 69.80  ? 262 MET   F N     1 
ATOM   13092 C  CA    . MET   E 4  262 ? -6.846  43.160  97.641  1.00 76.11  ? 262 MET   F CA    1 
ATOM   13093 C  C     . MET   E 4  262 ? -7.212  44.439  96.889  1.00 74.12  ? 262 MET   F C     1 
ATOM   13094 O  O     . MET   E 4  262 ? -6.489  45.442  96.964  1.00 63.43  ? 262 MET   F O     1 
ATOM   13095 C  CB    . MET   E 4  262 ? -6.846  43.410  99.148  1.00 69.27  ? 262 MET   F CB    1 
ATOM   13096 C  CG    . MET   E 4  262 ? -8.190  43.072  99.768  1.00 66.38  ? 262 MET   F CG    1 
ATOM   13097 S  SD    . MET   E 4  262 ? -8.693  44.139  101.125 1.00 64.51  ? 262 MET   F SD    1 
ATOM   13098 C  CE    . MET   E 4  262 ? -7.280  44.025  102.215 1.00 60.42  ? 262 MET   F CE    1 
ATOM   13099 N  N     . PHE   E 4  263 ? -8.328  44.389  96.161  1.00 70.29  ? 263 PHE   F N     1 
ATOM   13100 C  CA    . PHE   E 4  263 ? -8.863  45.528  95.436  1.00 65.36  ? 263 PHE   F CA    1 
ATOM   13101 C  C     . PHE   E 4  263 ? -9.709  46.393  96.370  1.00 69.55  ? 263 PHE   F C     1 
ATOM   13102 O  O     . PHE   E 4  263 ? -9.806  46.142  97.577  1.00 66.11  ? 263 PHE   F O     1 
ATOM   13103 C  CB    . PHE   E 4  263 ? -9.658  45.055  94.219  1.00 63.16  ? 263 PHE   F CB    1 
ATOM   13104 C  CG    . PHE   E 4  263 ? -8.846  44.234  93.262  1.00 71.12  ? 263 PHE   F CG    1 
ATOM   13105 C  CD1   . PHE   E 4  263 ? -7.757  44.792  92.602  1.00 71.28  ? 263 PHE   F CD1   1 
ATOM   13106 C  CD2   . PHE   E 4  263 ? -9.151  42.903  93.033  1.00 69.31  ? 263 PHE   F CD2   1 
ATOM   13107 C  CE1   . PHE   E 4  263 ? -6.984  44.035  91.723  1.00 70.19  ? 263 PHE   F CE1   1 
ATOM   13108 C  CE2   . PHE   E 4  263 ? -8.390  42.145  92.155  1.00 77.12  ? 263 PHE   F CE2   1 
ATOM   13109 C  CZ    . PHE   E 4  263 ? -7.303  42.714  91.497  1.00 74.36  ? 263 PHE   F CZ    1 
ATOM   13110 N  N     . PHE   E 4  264 ? -10.339 47.428  95.803  1.00 72.73  ? 264 PHE   F N     1 
ATOM   13111 C  CA    . PHE   E 4  264 ? -10.858 48.503  96.643  1.00 63.87  ? 264 PHE   F CA    1 
ATOM   13112 C  C     . PHE   E 4  264 ? -12.225 48.183  97.220  1.00 60.57  ? 264 PHE   F C     1 
ATOM   13113 O  O     . PHE   E 4  264 ? -12.466 48.444  98.401  1.00 63.77  ? 264 PHE   F O     1 
ATOM   13114 C  CB    . PHE   E 4  264 ? -10.890 49.817  95.868  1.00 57.45  ? 264 PHE   F CB    1 
ATOM   13115 C  CG    . PHE   E 4  264 ? -9.599  50.579  95.947  1.00 59.45  ? 264 PHE   F CG    1 
ATOM   13116 C  CD1   . PHE   E 4  264 ? -8.458  49.972  96.468  1.00 54.40  ? 264 PHE   F CD1   1 
ATOM   13117 C  CD2   . PHE   E 4  264 ? -9.520  51.893  95.526  1.00 46.41  ? 264 PHE   F CD2   1 
ATOM   13118 C  CE1   . PHE   E 4  264 ? -7.267  50.656  96.557  1.00 46.74  ? 264 PHE   F CE1   1 
ATOM   13119 C  CE2   . PHE   E 4  264 ? -8.332  52.586  95.608  1.00 49.58  ? 264 PHE   F CE2   1 
ATOM   13120 C  CZ    . PHE   E 4  264 ? -7.202  51.966  96.121  1.00 56.12  ? 264 PHE   F CZ    1 
ATOM   13121 N  N     . GLU   E 4  265 ? -13.128 47.618  96.416  1.00 65.55  ? 265 GLU   F N     1 
ATOM   13122 C  CA    . GLU   E 4  265 ? -14.450 47.268  96.928  1.00 63.83  ? 265 GLU   F CA    1 
ATOM   13123 C  C     . GLU   E 4  265 ? -14.349 46.445  98.207  1.00 71.50  ? 265 GLU   F C     1 
ATOM   13124 O  O     . GLU   E 4  265 ? -15.173 46.593  99.118  1.00 69.25  ? 265 GLU   F O     1 
ATOM   13125 C  CB    . GLU   E 4  265 ? -15.247 46.511  95.871  1.00 73.30  ? 265 GLU   F CB    1 
ATOM   13126 C  CG    . GLU   E 4  265 ? -16.600 46.011  96.349  1.00 70.68  ? 265 GLU   F CG    1 
ATOM   13127 C  CD    . GLU   E 4  265 ? -17.487 45.595  95.196  1.00 74.83  ? 265 GLU   F CD    1 
ATOM   13128 O  OE1   . GLU   E 4  265 ? -17.163 45.950  94.043  1.00 82.53  ? 265 GLU   F OE1   1 
ATOM   13129 O  OE2   . GLU   E 4  265 ? -18.508 44.922  95.435  1.00 73.60  ? 265 GLU   F OE2   1 
ATOM   13130 N  N     . GLU   E 4  266 ? -13.334 45.577  98.297  1.00 72.80  ? 266 GLU   F N     1 
ATOM   13131 C  CA    . GLU   E 4  266 ? -13.168 44.746  99.485  1.00 67.69  ? 266 GLU   F CA    1 
ATOM   13132 C  C     . GLU   E 4  266 ? -12.463 45.502  100.602 1.00 68.74  ? 266 GLU   F C     1 
ATOM   13133 O  O     . GLU   E 4  266 ? -12.830 45.368  101.774 1.00 68.89  ? 266 GLU   F O     1 
ATOM   13134 C  CB    . GLU   E 4  266 ? -12.398 43.472  99.137  1.00 66.01  ? 266 GLU   F CB    1 
ATOM   13135 C  CG    . GLU   E 4  266 ? -12.832 42.259  99.951  1.00 77.14  ? 266 GLU   F CG    1 
ATOM   13136 C  CD    . GLU   E 4  266 ? -11.680 41.583  100.667 1.00 82.77  ? 266 GLU   F CD    1 
ATOM   13137 O  OE1   . GLU   E 4  266 ? -10.896 40.881  99.986  1.00 65.98  ? 266 GLU   F OE1   1 
ATOM   13138 O  OE2   . GLU   E 4  266 ? -11.562 41.763  101.907 1.00 79.73  ? 266 GLU   F OE2   1 
ATOM   13139 N  N     . PHE   E 4  267 ? -11.444 46.295  100.263 1.00 68.03  ? 267 PHE   F N     1 
ATOM   13140 C  CA    . PHE   E 4  267 ? -10.766 47.066  101.295 1.00 58.91  ? 267 PHE   F CA    1 
ATOM   13141 C  C     . PHE   E 4  267 ? -11.666 48.156  101.847 1.00 60.77  ? 267 PHE   F C     1 
ATOM   13142 O  O     . PHE   E 4  267 ? -11.523 48.546  103.011 1.00 64.90  ? 267 PHE   F O     1 
ATOM   13143 C  CB    . PHE   E 4  267 ? -9.482  47.676  100.754 1.00 56.47  ? 267 PHE   F CB    1 
ATOM   13144 C  CG    . PHE   E 4  267 ? -8.713  48.442  101.782 1.00 55.55  ? 267 PHE   F CG    1 
ATOM   13145 C  CD1   . PHE   E 4  267 ? -8.532  47.922  103.046 1.00 52.24  ? 267 PHE   F CD1   1 
ATOM   13146 C  CD2   . PHE   E 4  267 ? -8.171  49.678  101.487 1.00 64.77  ? 267 PHE   F CD2   1 
ATOM   13147 C  CE1   . PHE   E 4  267 ? -7.821  48.610  104.001 1.00 61.31  ? 267 PHE   F CE1   1 
ATOM   13148 C  CE2   . PHE   E 4  267 ? -7.462  50.384  102.436 1.00 60.67  ? 267 PHE   F CE2   1 
ATOM   13149 C  CZ    . PHE   E 4  267 ? -7.285  49.845  103.700 1.00 71.84  ? 267 PHE   F CZ    1 
ATOM   13150 N  N     . ASN   E 4  268 ? -12.586 48.663  101.022 1.00 63.88  ? 268 ASN   F N     1 
ATOM   13151 C  CA    . ASN   E 4  268 ? -13.560 49.649  101.478 1.00 63.94  ? 268 ASN   F CA    1 
ATOM   13152 C  C     . ASN   E 4  268 ? -14.606 48.990  102.362 1.00 68.18  ? 268 ASN   F C     1 
ATOM   13153 O  O     . ASN   E 4  268 ? -14.906 49.473  103.462 1.00 63.13  ? 268 ASN   F O     1 
ATOM   13154 C  CB    . ASN   E 4  268 ? -14.208 50.326  100.263 1.00 63.50  ? 268 ASN   F CB    1 
ATOM   13155 C  CG    . ASN   E 4  268 ? -15.256 51.367  100.638 1.00 57.49  ? 268 ASN   F CG    1 
ATOM   13156 O  OD1   . ASN   E 4  268 ? -14.970 52.354  101.323 1.00 52.29  ? 268 ASN   F OD1   1 
ATOM   13157 N  ND2   . ASN   E 4  268 ? -16.470 51.166  100.150 1.00 50.68  ? 268 ASN   F ND2   1 
ATOM   13158 N  N     . GLN   E 4  269 ? -15.161 47.870  101.893 1.00 72.93  ? 269 GLN   F N     1 
ATOM   13159 C  CA    . GLN   E 4  269 ? -16.094 47.089  102.695 1.00 70.03  ? 269 GLN   F CA    1 
ATOM   13160 C  C     . GLN   E 4  269 ? -15.468 46.640  104.017 1.00 65.81  ? 269 GLN   F C     1 
ATOM   13161 O  O     . GLN   E 4  269 ? -16.162 46.555  105.036 1.00 64.02  ? 269 GLN   F O     1 
ATOM   13162 C  CB    . GLN   E 4  269 ? -16.578 45.895  101.872 1.00 63.66  ? 269 GLN   F CB    1 
ATOM   13163 C  CG    . GLN   E 4  269 ? -17.721 45.154  102.473 1.00 56.51  ? 269 GLN   F CG    1 
ATOM   13164 C  CD    . GLN   E 4  269 ? -18.796 46.079  102.951 1.00 70.68  ? 269 GLN   F CD    1 
ATOM   13165 O  OE1   . GLN   E 4  269 ? -19.392 46.816  102.165 1.00 80.96  ? 269 GLN   F OE1   1 
ATOM   13166 N  NE2   . GLN   E 4  269 ? -19.046 46.064  104.256 1.00 66.52  ? 269 GLN   F NE2   1 
ATOM   13167 N  N     . TYR   E 4  270 ? -14.162 46.363  104.028 1.00 65.18  ? 270 TYR   F N     1 
ATOM   13168 C  CA    . TYR   E 4  270 ? -13.488 46.059  105.285 1.00 58.50  ? 270 TYR   F CA    1 
ATOM   13169 C  C     . TYR   E 4  270 ? -13.394 47.295  106.170 1.00 67.57  ? 270 TYR   F C     1 
ATOM   13170 O  O     . TYR   E 4  270 ? -13.653 47.228  107.378 1.00 66.98  ? 270 TYR   F O     1 
ATOM   13171 C  CB    . TYR   E 4  270 ? -12.092 45.506  105.025 1.00 53.01  ? 270 TYR   F CB    1 
ATOM   13172 C  CG    . TYR   E 4  270 ? -11.215 45.525  106.261 1.00 55.43  ? 270 TYR   F CG    1 
ATOM   13173 C  CD1   . TYR   E 4  270 ? -11.260 44.490  107.182 1.00 59.75  ? 270 TYR   F CD1   1 
ATOM   13174 C  CD2   . TYR   E 4  270 ? -10.338 46.571  106.505 1.00 57.05  ? 270 TYR   F CD2   1 
ATOM   13175 C  CE1   . TYR   E 4  270 ? -10.456 44.496  108.316 1.00 56.36  ? 270 TYR   F CE1   1 
ATOM   13176 C  CE2   . TYR   E 4  270 ? -9.532  46.588  107.639 1.00 47.39  ? 270 TYR   F CE2   1 
ATOM   13177 C  CZ    . TYR   E 4  270 ? -9.598  45.545  108.539 1.00 57.47  ? 270 TYR   F CZ    1 
ATOM   13178 O  OH    . TYR   E 4  270 ? -8.805  45.536  109.665 1.00 54.54  ? 270 TYR   F OH    1 
ATOM   13179 N  N     . LEU   E 4  271 ? -12.981 48.430  105.595 1.00 69.40  ? 271 LEU   F N     1 
ATOM   13180 C  CA    . LEU   E 4  271 ? -12.828 49.631  106.408 1.00 64.65  ? 271 LEU   F CA    1 
ATOM   13181 C  C     . LEU   E 4  271 ? -14.153 50.014  107.055 1.00 65.08  ? 271 LEU   F C     1 
ATOM   13182 O  O     . LEU   E 4  271 ? -14.188 50.430  108.222 1.00 62.21  ? 271 LEU   F O     1 
ATOM   13183 C  CB    . LEU   E 4  271 ? -12.267 50.777  105.561 1.00 56.83  ? 271 LEU   F CB    1 
ATOM   13184 C  CG    . LEU   E 4  271 ? -10.749 50.789  105.299 1.00 63.26  ? 271 LEU   F CG    1 
ATOM   13185 C  CD1   . LEU   E 4  271 ? -10.423 51.656  104.083 1.00 54.71  ? 271 LEU   F CD1   1 
ATOM   13186 C  CD2   . LEU   E 4  271 ? -9.909  51.236  106.528 1.00 50.90  ? 271 LEU   F CD2   1 
ATOM   13187 N  N     . MET   E 4  272 ? -15.259 49.844  106.324 1.00 54.73  ? 272 MET   F N     1 
ATOM   13188 C  CA    . MET   E 4  272 ? -16.564 50.157  106.887 1.00 55.08  ? 272 MET   F CA    1 
ATOM   13189 C  C     . MET   E 4  272 ? -16.832 49.319  108.125 1.00 68.76  ? 272 MET   F C     1 
ATOM   13190 O  O     . MET   E 4  272 ? -17.242 49.845  109.166 1.00 68.08  ? 272 MET   F O     1 
ATOM   13191 C  CB    . MET   E 4  272 ? -17.651 49.936  105.842 1.00 56.53  ? 272 MET   F CB    1 
ATOM   13192 C  CG    . MET   E 4  272 ? -17.947 51.156  104.998 1.00 64.33  ? 272 MET   F CG    1 
ATOM   13193 S  SD    . MET   E 4  272 ? -18.657 50.701  103.405 1.00 83.09  ? 272 MET   F SD    1 
ATOM   13194 C  CE    . MET   E 4  272 ? -20.377 50.393  103.824 1.00 85.88  ? 272 MET   F CE    1 
ATOM   13195 N  N     . ASP   E 4  273 ? -16.566 48.010  108.042 1.00 66.14  ? 273 ASP   F N     1 
ATOM   13196 C  CA    . ASP   E 4  273 ? -16.979 47.086  109.094 1.00 54.70  ? 273 ASP   F CA    1 
ATOM   13197 C  C     . ASP   E 4  273 ? -16.048 47.109  110.301 1.00 61.24  ? 273 ASP   F C     1 
ATOM   13198 O  O     . ASP   E 4  273 ? -16.516 46.956  111.437 1.00 55.00  ? 273 ASP   F O     1 
ATOM   13199 C  CB    . ASP   E 4  273 ? -17.080 45.672  108.527 1.00 52.46  ? 273 ASP   F CB    1 
ATOM   13200 C  CG    . ASP   E 4  273 ? -18.175 45.541  107.467 1.00 70.01  ? 273 ASP   F CG    1 
ATOM   13201 O  OD1   . ASP   E 4  273 ? -19.141 46.345  107.505 1.00 61.16  ? 273 ASP   F OD1   1 
ATOM   13202 O  OD2   . ASP   E 4  273 ? -18.066 44.633  106.600 1.00 60.63  ? 273 ASP   F OD2   1 
ATOM   13203 N  N     . ALA   E 4  274 ? -14.746 47.309  110.090 1.00 55.14  ? 274 ALA   F N     1 
ATOM   13204 C  CA    . ALA   E 4  274 ? -13.782 47.308  111.183 1.00 48.68  ? 274 ALA   F CA    1 
ATOM   13205 C  C     . ALA   E 4  274 ? -13.462 48.690  111.716 1.00 60.23  ? 274 ALA   F C     1 
ATOM   13206 O  O     . ALA   E 4  274 ? -13.190 48.827  112.912 1.00 64.08  ? 274 ALA   F O     1 
ATOM   13207 C  CB    . ALA   E 4  274 ? -12.470 46.656  110.743 1.00 61.50  ? 274 ALA   F CB    1 
ATOM   13208 N  N     . LEU   E 4  275 ? -13.456 49.712  110.856 1.00 66.12  ? 275 LEU   F N     1 
ATOM   13209 C  CA    A LEU   E 4  275 ? -13.140 51.066  111.281 1.00 60.54  ? 275 LEU   F CA    1 
ATOM   13210 C  CA    B LEU   E 4  275 ? -13.130 51.073  111.258 0.00 60.63  ? 275 LEU   F CA    1 
ATOM   13211 C  C     . LEU   E 4  275 ? -14.294 52.046  111.132 1.00 55.71  ? 275 LEU   F C     1 
ATOM   13212 O  O     . LEU   E 4  275 ? -14.180 53.183  111.607 1.00 49.52  ? 275 LEU   F O     1 
ATOM   13213 C  CB    A LEU   E 4  275 ? -11.929 51.608  110.508 1.00 64.07  ? 275 LEU   F CB    1 
ATOM   13214 C  CB    B LEU   E 4  275 ? -11.943 51.599  110.438 0.00 63.64  ? 275 LEU   F CB    1 
ATOM   13215 C  CG    A LEU   E 4  275 ? -10.536 51.058  110.817 1.00 61.82  ? 275 LEU   F CG    1 
ATOM   13216 C  CG    B LEU   E 4  275 ? -10.596 50.910  110.668 0.00 61.57  ? 275 LEU   F CG    1 
ATOM   13217 C  CD1   A LEU   E 4  275 ? -10.459 50.531  112.254 1.00 57.57  ? 275 LEU   F CD1   1 
ATOM   13218 C  CD1   B LEU   E 4  275 ? -9.519  51.535  109.796 0.00 61.25  ? 275 LEU   F CD1   1 
ATOM   13219 C  CD2   A LEU   E 4  275 ? -10.164 50.007  109.774 1.00 60.27  ? 275 LEU   F CD2   1 
ATOM   13220 C  CD2   B LEU   E 4  275 ? -10.205 50.974  112.137 0.00 60.19  ? 275 LEU   F CD2   1 
ATOM   13221 N  N     . ASN   E 4  276 ? -15.398 51.650  110.492 1.00 57.15  ? 276 ASN   F N     1 
ATOM   13222 C  CA    . ASN   E 4  276 ? -16.601 52.479  110.454 1.00 64.54  ? 276 ASN   F CA    1 
ATOM   13223 C  C     . ASN   E 4  276 ? -16.416 53.714  109.564 1.00 69.75  ? 276 ASN   F C     1 
ATOM   13224 O  O     . ASN   E 4  276 ? -16.957 54.797  109.829 1.00 60.84  ? 276 ASN   F O     1 
ATOM   13225 C  CB    . ASN   E 4  276 ? -17.006 52.870  111.882 1.00 57.93  ? 276 ASN   F CB    1 
ATOM   13226 C  CG    . ASN   E 4  276 ? -18.305 53.616  111.940 1.00 60.48  ? 276 ASN   F CG    1 
ATOM   13227 O  OD1   . ASN   E 4  276 ? -19.230 53.370  111.152 1.00 48.60  ? 276 ASN   F OD1   1 
ATOM   13228 N  ND2   . ASN   E 4  276 ? -18.384 54.554  112.876 1.00 56.19  ? 276 ASN   F ND2   1 
ATOM   13229 N  N     . THR   E 4  277 ? -15.658 53.556  108.489 1.00 62.66  ? 277 THR   F N     1 
ATOM   13230 C  CA    A THR   E 4  277 ? -15.327 54.657  107.604 1.00 57.08  ? 277 THR   F CA    1 
ATOM   13231 C  CA    B THR   E 4  277 ? -15.354 54.668  107.599 0.00 57.13  ? 277 THR   F CA    1 
ATOM   13232 C  C     . THR   E 4  277 ? -15.432 54.150  106.170 1.00 61.88  ? 277 THR   F C     1 
ATOM   13233 O  O     . THR   E 4  277 ? -16.020 53.095  105.901 1.00 56.50  ? 277 THR   F O     1 
ATOM   13234 C  CB    A THR   E 4  277 ? -13.938 55.203  107.948 1.00 54.10  ? 277 THR   F CB    1 
ATOM   13235 C  CB    B THR   E 4  277 ? -13.987 55.282  107.939 0.00 54.23  ? 277 THR   F CB    1 
ATOM   13236 O  OG1   A THR   E 4  277 ? -13.571 56.213  107.006 1.00 53.49  ? 277 THR   F OG1   1 
ATOM   13237 O  OG1   B THR   E 4  277 ? -13.720 56.379  107.057 0.00 53.97  ? 277 THR   F OG1   1 
ATOM   13238 C  CG2   A THR   E 4  277 ? -12.928 54.089  107.885 1.00 59.37  ? 277 THR   F CG2   1 
ATOM   13239 C  CG2   B THR   E 4  277 ? -12.885 54.243  107.794 0.00 58.97  ? 277 THR   F CG2   1 
ATOM   13240 N  N     . THR   E 4  278 ? -14.862 54.914  105.238 1.00 60.48  ? 278 THR   F N     1 
ATOM   13241 C  CA    . THR   E 4  278 ? -14.754 54.529  103.842 1.00 59.33  ? 278 THR   F CA    1 
ATOM   13242 C  C     . THR   E 4  278 ? -13.309 54.708  103.418 1.00 51.57  ? 278 THR   F C     1 
ATOM   13243 O  O     . THR   E 4  278 ? -12.546 55.448  104.048 1.00 42.62  ? 278 THR   F O     1 
ATOM   13244 C  CB    . THR   E 4  278 ? -15.664 55.353  102.907 1.00 60.58  ? 278 THR   F CB    1 
ATOM   13245 O  OG1   . THR   E 4  278 ? -15.797 56.690  103.404 1.00 55.33  ? 278 THR   F OG1   1 
ATOM   13246 C  CG2   . THR   E 4  278 ? -17.036 54.703  102.745 1.00 50.88  ? 278 THR   F CG2   1 
ATOM   13247 N  N     . LEU   E 4  279 ? -12.941 53.992  102.349 1.00 53.18  ? 279 LEU   F N     1 
ATOM   13248 C  CA    . LEU   E 4  279 ? -11.632 54.188  101.738 1.00 49.86  ? 279 LEU   F CA    1 
ATOM   13249 C  C     . LEU   E 4  279 ? -11.451 55.647  101.332 1.00 58.18  ? 279 LEU   F C     1 
ATOM   13250 O  O     . LEU   E 4  279 ? -10.442 56.283  101.669 1.00 57.08  ? 279 LEU   F O     1 
ATOM   13251 C  CB    . LEU   E 4  279 ? -11.479 53.247  100.541 1.00 48.64  ? 279 LEU   F CB    1 
ATOM   13252 C  CG    . LEU   E 4  279 ? -10.194 53.299  99.709  1.00 48.40  ? 279 LEU   F CG    1 
ATOM   13253 C  CD1   . LEU   E 4  279 ? -8.954  53.127  100.574 1.00 46.05  ? 279 LEU   F CD1   1 
ATOM   13254 C  CD2   . LEU   E 4  279 ? -10.246 52.241  98.640  1.00 50.95  ? 279 LEU   F CD2   1 
ATOM   13255 N  N     . GLU   E 4  280 ? -12.448 56.202  100.637 1.00 52.12  ? 280 GLU   F N     1 
ATOM   13256 C  CA    . GLU   E 4  280 ? -12.528 57.623  100.315 1.00 53.87  ? 280 GLU   F CA    1 
ATOM   13257 C  C     . GLU   E 4  280 ? -12.076 58.538  101.449 1.00 57.40  ? 280 GLU   F C     1 
ATOM   13258 O  O     . GLU   E 4  280 ? -10.998 59.134  101.387 1.00 57.42  ? 280 GLU   F O     1 
ATOM   13259 C  CB    . GLU   E 4  280 ? -13.962 57.991  99.943  1.00 58.44  ? 280 GLU   F CB    1 
ATOM   13260 C  CG    . GLU   E 4  280 ? -14.047 59.375  99.381  1.00 61.49  ? 280 GLU   F CG    1 
ATOM   13261 C  CD    . GLU   E 4  280 ? -13.028 59.562  98.286  1.00 66.14  ? 280 GLU   F CD    1 
ATOM   13262 O  OE1   . GLU   E 4  280 ? -13.021 58.721  97.345  1.00 67.18  ? 280 GLU   F OE1   1 
ATOM   13263 O  OE2   . GLU   E 4  280 ? -12.227 60.523  98.389  1.00 52.01  ? 280 GLU   F OE2   1 
ATOM   13264 N  N     . ASN   E 4  281 ? -12.912 58.685  102.476 1.00 55.88  ? 281 ASN   F N     1 
ATOM   13265 C  CA    . ASN   E 4  281 ? -12.589 59.606  103.558 1.00 51.79  ? 281 ASN   F CA    1 
ATOM   13266 C  C     . ASN   E 4  281 ? -11.232 59.284  104.174 1.00 49.78  ? 281 ASN   F C     1 
ATOM   13267 O  O     . ASN   E 4  281 ? -10.396 60.174  104.371 1.00 49.18  ? 281 ASN   F O     1 
ATOM   13268 C  CB    . ASN   E 4  281 ? -13.674 59.552  104.632 1.00 52.04  ? 281 ASN   F CB    1 
ATOM   13269 C  CG    . ASN   E 4  281 ? -15.024 60.000  104.135 1.00 51.44  ? 281 ASN   F CG    1 
ATOM   13270 O  OD1   . ASN   E 4  281 ? -15.322 59.975  102.932 1.00 43.22  ? 281 ASN   F OD1   1 
ATOM   13271 N  ND2   . ASN   E 4  281 ? -15.867 60.407  105.077 1.00 43.56  ? 281 ASN   F ND2   1 
ATOM   13272 N  N     . SER   E 4  282 ? -10.999 58.013  104.500 1.00 54.88  ? 282 SER   F N     1 
ATOM   13273 C  CA    . SER   E 4  282 ? -9.854  57.682  105.343 1.00 54.07  ? 282 SER   F CA    1 
ATOM   13274 C  C     . SER   E 4  282 ? -8.530  57.759  104.583 1.00 51.49  ? 282 SER   F C     1 
ATOM   13275 O  O     . SER   E 4  282 ? -7.551  58.293  105.117 1.00 47.48  ? 282 SER   F O     1 
ATOM   13276 C  CB    . SER   E 4  282 ? -10.047 56.297  105.978 1.00 55.45  ? 282 SER   F CB    1 
ATOM   13277 O  OG    . SER   E 4  282 ? -10.606 55.358  105.067 1.00 51.34  ? 282 SER   F OG    1 
ATOM   13278 N  N     . ILE   E 4  283 ? -8.475  57.257  103.337 1.00 39.96  ? 283 ILE   F N     1 
ATOM   13279 C  CA    . ILE   E 4  283 ? -7.219  57.080  102.614 1.00 52.30  ? 283 ILE   F CA    1 
ATOM   13280 C  C     . ILE   E 4  283 ? -7.171  57.902  101.323 1.00 54.94  ? 283 ILE   F C     1 
ATOM   13281 O  O     . ILE   E 4  283 ? -6.213  58.650  101.089 1.00 41.43  ? 283 ILE   F O     1 
ATOM   13282 C  CB    . ILE   E 4  283 ? -6.949  55.589  102.311 1.00 54.17  ? 283 ILE   F CB    1 
ATOM   13283 C  CG1   . ILE   E 4  283 ? -7.340  54.702  103.504 1.00 57.71  ? 283 ILE   F CG1   1 
ATOM   13284 C  CG2   . ILE   E 4  283 ? -5.495  55.401  101.899 1.00 44.00  ? 283 ILE   F CG2   1 
ATOM   13285 C  CD1   . ILE   E 4  283 ? -6.176  54.230  104.370 1.00 47.61  ? 283 ILE   F CD1   1 
ATOM   13286 N  N     . LEU   E 4  284 ? -8.192  57.764  100.459 1.00 47.80  ? 284 LEU   F N     1 
ATOM   13287 C  CA    A LEU   E 4  284 ? -8.084  58.274  99.093  0.21 49.46  ? 284 LEU   F CA    1 
ATOM   13288 C  CA    B LEU   E 4  284 ? -8.074  58.272  99.093  0.79 49.40  ? 284 LEU   F CA    1 
ATOM   13289 C  C     . LEU   E 4  284 ? -7.837  59.779  99.066  1.00 53.81  ? 284 LEU   F C     1 
ATOM   13290 O  O     . LEU   E 4  284 ? -7.071  60.277  98.232  1.00 53.59  ? 284 LEU   F O     1 
ATOM   13291 C  CB    A LEU   E 4  284 ? -9.344  57.925  98.302  0.21 49.39  ? 284 LEU   F CB    1 
ATOM   13292 C  CB    B LEU   E 4  284 ? -9.311  57.900  98.274  0.79 49.34  ? 284 LEU   F CB    1 
ATOM   13293 C  CG    A LEU   E 4  284 ? -9.128  57.514  96.841  0.21 48.38  ? 284 LEU   F CG    1 
ATOM   13294 C  CG    B LEU   E 4  284 ? -9.360  56.517  97.596  0.79 47.58  ? 284 LEU   F CG    1 
ATOM   13295 C  CD1   A LEU   E 4  284 ? -8.454  56.154  96.762  0.21 43.90  ? 284 LEU   F CD1   1 
ATOM   13296 C  CD1   B LEU   E 4  284 ? -10.681 56.295  96.860  0.79 46.91  ? 284 LEU   F CD1   1 
ATOM   13297 C  CD2   A LEU   E 4  284 ? -10.441 57.508  96.074  0.21 48.90  ? 284 LEU   F CD2   1 
ATOM   13298 C  CD2   B LEU   E 4  284 ? -8.214  56.334  96.636  0.79 42.75  ? 284 LEU   F CD2   1 
ATOM   13299 N  N     . LEU   E 4  285 ? -8.473  60.527  99.970  1.00 62.04  ? 285 LEU   F N     1 
ATOM   13300 C  CA    . LEU   E 4  285 ? -8.278  61.974  99.975  1.00 52.64  ? 285 LEU   F CA    1 
ATOM   13301 C  C     . LEU   E 4  285 ? -6.815  62.341  100.185 1.00 54.07  ? 285 LEU   F C     1 
ATOM   13302 O  O     . LEU   E 4  285 ? -6.302  63.260  99.540  1.00 62.52  ? 285 LEU   F O     1 
ATOM   13303 C  CB    . LEU   E 4  285 ? -9.157  62.624  101.036 1.00 51.07  ? 285 LEU   F CB    1 
ATOM   13304 C  CG    . LEU   E 4  285 ? -10.420 63.249  100.444 1.00 53.14  ? 285 LEU   F CG    1 
ATOM   13305 C  CD1   . LEU   E 4  285 ? -11.436 63.556  101.529 1.00 53.34  ? 285 LEU   F CD1   1 
ATOM   13306 C  CD2   . LEU   E 4  285 ? -10.046 64.512  99.677  1.00 54.37  ? 285 LEU   F CD2   1 
ATOM   13307 N  N     . GLN   E 4  286 ? -6.120  61.635  101.071 1.00 55.55  ? 286 GLN   F N     1 
ATOM   13308 C  CA    . GLN   E 4  286 ? -4.695  61.909  101.240 1.00 58.02  ? 286 GLN   F CA    1 
ATOM   13309 C  C     . GLN   E 4  286 ? -3.886  61.471  100.019 1.00 50.15  ? 286 GLN   F C     1 
ATOM   13310 O  O     . GLN   E 4  286 ? -2.883  62.109  99.684  1.00 50.48  ? 286 GLN   F O     1 
ATOM   13311 C  CB    . GLN   E 4  286 ? -4.170  61.222  102.508 1.00 47.37  ? 286 GLN   F CB    1 
ATOM   13312 C  CG    . GLN   E 4  286 ? -4.889  61.629  103.780 1.00 39.90  ? 286 GLN   F CG    1 
ATOM   13313 C  CD    . GLN   E 4  286 ? -4.500  60.777  104.968 1.00 55.27  ? 286 GLN   F CD    1 
ATOM   13314 O  OE1   . GLN   E 4  286 ? -3.446  60.980  105.586 1.00 53.34  ? 286 GLN   F OE1   1 
ATOM   13315 N  NE2   . GLN   E 4  286 ? -5.351  59.812  105.299 1.00 56.36  ? 286 GLN   F NE2   1 
ATOM   13316 N  N     . ILE   E 4  287 ? -4.292  60.386  99.353  1.00 48.13  ? 287 ILE   F N     1 
ATOM   13317 C  CA    . ILE   E 4  287 ? -3.566  59.919  98.175  1.00 47.46  ? 287 ILE   F CA    1 
ATOM   13318 C  C     . ILE   E 4  287 ? -3.624  60.971  97.074  1.00 50.53  ? 287 ILE   F C     1 
ATOM   13319 O  O     . ILE   E 4  287 ? -2.590  61.410  96.546  1.00 40.62  ? 287 ILE   F O     1 
ATOM   13320 C  CB    . ILE   E 4  287 ? -4.131  58.569  97.691  1.00 48.95  ? 287 ILE   F CB    1 
ATOM   13321 C  CG1   . ILE   E 4  287 ? -3.623  57.409  98.545  1.00 53.95  ? 287 ILE   F CG1   1 
ATOM   13322 C  CG2   . ILE   E 4  287 ? -3.776  58.324  96.226  1.00 52.52  ? 287 ILE   F CG2   1 
ATOM   13323 C  CD1   . ILE   E 4  287 ? -4.206  56.063  98.113  1.00 46.85  ? 287 ILE   F CD1   1 
ATOM   13324 N  N     . LYS   E 4  288 ? -4.840  61.397  96.718  1.00 49.83  ? 288 LYS   F N     1 
ATOM   13325 C  CA    . LYS   E 4  288 ? -5.007  62.424  95.695  1.00 47.30  ? 288 LYS   F CA    1 
ATOM   13326 C  C     . LYS   E 4  288 ? -4.173  63.660  96.017  1.00 44.32  ? 288 LYS   F C     1 
ATOM   13327 O  O     . LYS   E 4  288 ? -3.435  64.164  95.167  1.00 54.40  ? 288 LYS   F O     1 
ATOM   13328 C  CB    . LYS   E 4  288 ? -6.490  62.766  95.546  1.00 40.02  ? 288 LYS   F CB    1 
ATOM   13329 C  CG    . LYS   E 4  288 ? -7.338  61.508  95.432  1.00 47.45  ? 288 LYS   F CG    1 
ATOM   13330 C  CD    . LYS   E 4  288 ? -8.687  61.703  94.774  1.00 30.63  ? 288 LYS   F CD    1 
ATOM   13331 C  CE    . LYS   E 4  288 ? -9.815  61.659  95.785  1.00 45.36  ? 288 LYS   F CE    1 
ATOM   13332 N  NZ    . LYS   E 4  288 ? -11.095 61.187  95.168  1.00 51.31  ? 288 LYS   F NZ    1 
ATOM   13333 N  N     . HIS   E 4  289 ? -4.242  64.141  97.252  1.00 39.36  ? 289 HIS   F N     1 
ATOM   13334 C  CA    . HIS   E 4  289 ? -3.439  65.300  97.610  1.00 45.57  ? 289 HIS   F CA    1 
ATOM   13335 C  C     . HIS   E 4  289 ? -1.950  65.019  97.498  1.00 50.22  ? 289 HIS   F C     1 
ATOM   13336 O  O     . HIS   E 4  289 ? -1.161  65.963  97.352  1.00 47.87  ? 289 HIS   F O     1 
ATOM   13337 C  CB    . HIS   E 4  289 ? -3.760  65.780  99.030  1.00 49.16  ? 289 HIS   F CB    1 
ATOM   13338 C  CG    . HIS   E 4  289 ? -2.791  66.797  99.547  1.00 50.67  ? 289 HIS   F CG    1 
ATOM   13339 N  ND1   . HIS   E 4  289 ? -2.848  68.129  99.190  1.00 44.61  ? 289 HIS   F ND1   1 
ATOM   13340 C  CD2   . HIS   E 4  289 ? -1.716  66.670  100.363 1.00 43.98  ? 289 HIS   F CD2   1 
ATOM   13341 C  CE1   . HIS   E 4  289 ? -1.862  68.780  99.782  1.00 46.17  ? 289 HIS   F CE1   1 
ATOM   13342 N  NE2   . HIS   E 4  289 ? -1.162  67.919  100.501 1.00 44.30  ? 289 HIS   F NE2   1 
ATOM   13343 N  N     . ILE   E 4  290 ? -1.539  63.752  97.568  1.00 51.06  ? 290 ILE   F N     1 
ATOM   13344 C  CA    . ILE   E 4  290 ? -0.113  63.464  97.445  1.00 51.49  ? 290 ILE   F CA    1 
ATOM   13345 C  C     . ILE   E 4  290 ? 0.292   63.385  95.980  1.00 44.81  ? 290 ILE   F C     1 
ATOM   13346 O  O     . ILE   E 4  290 ? 1.331   63.928  95.591  1.00 34.88  ? 290 ILE   F O     1 
ATOM   13347 C  CB    . ILE   E 4  290 ? 0.260   62.189  98.220  1.00 44.80  ? 290 ILE   F CB    1 
ATOM   13348 C  CG1   . ILE   E 4  290 ? 0.016   62.416  99.718  1.00 49.54  ? 290 ILE   F CG1   1 
ATOM   13349 C  CG2   . ILE   E 4  290 ? 1.717   61.836  97.967  1.00 46.61  ? 290 ILE   F CG2   1 
ATOM   13350 C  CD1   . ILE   E 4  290 ? 0.442   61.280  100.629 1.00 49.93  ? 290 ILE   F CD1   1 
ATOM   13351 N  N     . ILE   E 4  291 ? -0.532  62.731  95.153  1.00 34.81  ? 291 ILE   F N     1 
ATOM   13352 C  CA    . ILE   E 4  291 ? -0.296  62.699  93.714  1.00 36.16  ? 291 ILE   F CA    1 
ATOM   13353 C  C     . ILE   E 4  291 ? -0.299  64.115  93.144  1.00 48.57  ? 291 ILE   F C     1 
ATOM   13354 O  O     . ILE   E 4  291 ? 0.627   64.522  92.429  1.00 41.92  ? 291 ILE   F O     1 
ATOM   13355 C  CB    . ILE   E 4  291 ? -1.354  61.826  93.015  1.00 48.21  ? 291 ILE   F CB    1 
ATOM   13356 C  CG1   . ILE   E 4  291 ? -1.472  60.451  93.678  1.00 43.10  ? 291 ILE   F CG1   1 
ATOM   13357 C  CG2   . ILE   E 4  291 ? -1.042  61.688  91.518  1.00 42.62  ? 291 ILE   F CG2   1 
ATOM   13358 C  CD1   . ILE   E 4  291 ? -2.563  59.586  93.079  1.00 31.82  ? 291 ILE   F CD1   1 
ATOM   13359 N  N     . ARG   E 4  292 ? -1.350  64.885  93.443  1.00 49.05  ? 292 ARG   F N     1 
ATOM   13360 C  CA    . ARG   E 4  292 ? -1.465  66.214  92.857  1.00 45.22  ? 292 ARG   F CA    1 
ATOM   13361 C  C     . ARG   E 4  292 ? -0.280  67.082  93.261  1.00 47.45  ? 292 ARG   F C     1 
ATOM   13362 O  O     . ARG   E 4  292 ? 0.305   67.773  92.424  1.00 42.20  ? 292 ARG   F O     1 
ATOM   13363 C  CB    . ARG   E 4  292 ? -2.789  66.861  93.268  1.00 45.45  ? 292 ARG   F CB    1 
ATOM   13364 C  CG    . ARG   E 4  292 ? -3.539  67.575  92.143  1.00 51.68  ? 292 ARG   F CG    1 
ATOM   13365 C  CD    . ARG   E 4  292 ? -4.582  68.595  92.665  1.00 54.10  ? 292 ARG   F CD    1 
ATOM   13366 N  NE    . ARG   E 4  292 ? -4.985  68.341  94.046  1.00 65.55  ? 292 ARG   F NE    1 
ATOM   13367 C  CZ    . ARG   E 4  292 ? -5.900  67.447  94.418  1.00 68.70  ? 292 ARG   F CZ    1 
ATOM   13368 N  NH1   . ARG   E 4  292 ? -6.554  66.715  93.531  1.00 69.20  ? 292 ARG   F NH1   1 
ATOM   13369 N  NH2   . ARG   E 4  292 ? -6.161  67.275  95.715  1.00 54.21  ? 292 ARG   F NH2   1 
ATOM   13370 N  N     . SER   E 4  293 ? 0.111   67.037  94.535  1.00 42.96  ? 293 SER   F N     1 
ATOM   13371 C  CA    . SER   E 4  293 ? 1.237   67.859  94.970  1.00 48.24  ? 293 SER   F CA    1 
ATOM   13372 C  C     . SER   E 4  293 ? 2.527   67.465  94.267  1.00 45.82  ? 293 SER   F C     1 
ATOM   13373 O  O     . SER   E 4  293 ? 3.315   68.331  93.874  1.00 53.88  ? 293 SER   F O     1 
ATOM   13374 C  CB    . SER   E 4  293 ? 1.419   67.769  96.486  1.00 37.53  ? 293 SER   F CB    1 
ATOM   13375 O  OG    . SER   E 4  293 ? 0.287   68.298  97.132  1.00 41.32  ? 293 SER   F OG    1 
ATOM   13376 N  N     . CYS   E 4  294 ? 2.783   66.164  94.131  1.00 47.67  ? 294 CYS   F N     1 
ATOM   13377 C  CA    . CYS   E 4  294 ? 4.047   65.730  93.551  1.00 46.15  ? 294 CYS   F CA    1 
ATOM   13378 C  C     . CYS   E 4  294 ? 4.180   66.207  92.114  1.00 45.36  ? 294 CYS   F C     1 
ATOM   13379 O  O     . CYS   E 4  294 ? 5.192   66.809  91.740  1.00 42.45  ? 294 CYS   F O     1 
ATOM   13380 C  CB    . CYS   E 4  294 ? 4.172   64.210  93.621  1.00 38.68  ? 294 CYS   F CB    1 
ATOM   13381 S  SG    . CYS   E 4  294 ? 4.540   63.592  95.238  1.00 50.50  ? 294 CYS   F SG    1 
ATOM   13382 N  N     . LEU   E 4  295 ? 3.158   65.949  91.296  1.00 39.99  ? 295 LEU   F N     1 
ATOM   13383 C  CA    . LEU   E 4  295 ? 3.261   66.186  89.865  1.00 43.49  ? 295 LEU   F CA    1 
ATOM   13384 C  C     . LEU   E 4  295 ? 3.164   67.665  89.507  1.00 43.70  ? 295 LEU   F C     1 
ATOM   13385 O  O     . LEU   E 4  295 ? 3.760   68.097  88.514  1.00 46.70  ? 295 LEU   F O     1 
ATOM   13386 C  CB    . LEU   E 4  295 ? 2.187   65.377  89.129  1.00 36.27  ? 295 LEU   F CB    1 
ATOM   13387 C  CG    . LEU   E 4  295 ? 2.456   63.867  89.177  1.00 40.73  ? 295 LEU   F CG    1 
ATOM   13388 C  CD1   . LEU   E 4  295 ? 1.191   63.052  88.897  1.00 33.45  ? 295 LEU   F CD1   1 
ATOM   13389 C  CD2   . LEU   E 4  295 ? 3.557   63.508  88.203  1.00 35.87  ? 295 LEU   F CD2   1 
ATOM   13390 N  N     . MET   E 4  296 ? 2.435   68.460  90.286  1.00 39.21  ? 296 MET   F N     1 
ATOM   13391 C  CA    . MET   E 4  296 ? 2.431   69.893  90.031  1.00 42.71  ? 296 MET   F CA    1 
ATOM   13392 C  C     . MET   E 4  296 ? 3.770   70.533  90.383  1.00 34.63  ? 296 MET   F C     1 
ATOM   13393 O  O     . MET   E 4  296 ? 4.172   71.518  89.757  1.00 30.28  ? 296 MET   F O     1 
ATOM   13394 C  CB    . MET   E 4  296 ? 1.301   70.553  90.806  1.00 46.01  ? 296 MET   F CB    1 
ATOM   13395 C  CG    . MET   E 4  296 ? -0.053  70.379  90.161  1.00 51.83  ? 296 MET   F CG    1 
ATOM   13396 S  SD    . MET   E 4  296 ? -1.323  70.758  91.390  1.00 88.51  ? 296 MET   F SD    1 
ATOM   13397 C  CE    . MET   E 4  296 ? -0.588  72.190  92.208  1.00 69.88  ? 296 MET   F CE    1 
ATOM   13398 N  N     . CYS   E 4  297 ? 4.472   69.986  91.367  1.00 31.57  ? 297 CYS   F N     1 
ATOM   13399 C  CA    . CYS   E 4  297 ? 5.791   70.491  91.722  1.00 30.48  ? 297 CYS   F CA    1 
ATOM   13400 C  C     . CYS   E 4  297 ? 6.745   70.497  90.526  1.00 42.64  ? 297 CYS   F C     1 
ATOM   13401 O  O     . CYS   E 4  297 ? 7.478   71.470  90.307  1.00 44.69  ? 297 CYS   F O     1 
ATOM   13402 C  CB    . CYS   E 4  297 ? 6.349   69.637  92.846  1.00 34.43  ? 297 CYS   F CB    1 
ATOM   13403 S  SG    . CYS   E 4  297 ? 8.000   70.027  93.286  1.00 47.73  ? 297 CYS   F SG    1 
ATOM   13404 N  N     . ILE   E 4  298 ? 6.759   69.412  89.744  1.00 37.16  ? 298 ILE   F N     1 
ATOM   13405 C  CA    . ILE   E 4  298 ? 7.677   69.281  88.619  1.00 36.70  ? 298 ILE   F CA    1 
ATOM   13406 C  C     . ILE   E 4  298 ? 7.054   69.722  87.300  1.00 42.13  ? 298 ILE   F C     1 
ATOM   13407 O  O     . ILE   E 4  298 ? 7.742   69.724  86.263  1.00 43.45  ? 298 ILE   F O     1 
ATOM   13408 C  CB    . ILE   E 4  298 ? 8.176   67.822  88.509  1.00 32.16  ? 298 ILE   F CB    1 
ATOM   13409 C  CG1   . ILE   E 4  298 ? 7.029   66.913  88.054  1.00 34.64  ? 298 ILE   F CG1   1 
ATOM   13410 C  CG2   . ILE   E 4  298 ? 8.738   67.365  89.844  1.00 39.90  ? 298 ILE   F CG2   1 
ATOM   13411 C  CD1   . ILE   E 4  298 ? 7.216   65.469  88.362  1.00 36.11  ? 298 ILE   F CD1   1 
ATOM   13412 N  N     . GLU   E 4  299 ? 5.779   70.102  87.301  1.00 31.85  ? 299 GLU   F N     1 
ATOM   13413 C  CA    . GLU   E 4  299 ? 5.130   70.470  86.047  1.00 39.06  ? 299 GLU   F CA    1 
ATOM   13414 C  C     . GLU   E 4  299 ? 5.897   71.522  85.246  1.00 40.29  ? 299 GLU   F C     1 
ATOM   13415 O  O     . GLU   E 4  299 ? 5.922   71.415  84.008  1.00 46.23  ? 299 GLU   F O     1 
ATOM   13416 C  CB    . GLU   E 4  299 ? 3.688   70.929  86.315  1.00 28.81  ? 299 GLU   F CB    1 
ATOM   13417 C  CG    . GLU   E 4  299 ? 3.172   71.868  85.248  1.00 34.45  ? 299 GLU   F CG    1 
ATOM   13418 C  CD    . GLU   E 4  299 ? 1.660   71.957  85.184  1.00 51.03  ? 299 GLU   F CD    1 
ATOM   13419 O  OE1   . GLU   E 4  299 ? 0.987   71.917  86.242  1.00 56.87  ? 299 GLU   F OE1   1 
ATOM   13420 O  OE2   . GLU   E 4  299 ? 1.136   72.075  84.054  1.00 59.56  ? 299 GLU   F OE2   1 
ATOM   13421 N  N     . PRO   E 4  300 ? 6.518   72.539  85.844  1.00 34.81  ? 300 PRO   F N     1 
ATOM   13422 C  CA    . PRO   E 4  300 ? 7.299   73.489  85.033  1.00 43.28  ? 300 PRO   F CA    1 
ATOM   13423 C  C     . PRO   E 4  300 ? 8.517   72.879  84.375  1.00 39.57  ? 300 PRO   F C     1 
ATOM   13424 O  O     . PRO   E 4  300 ? 8.972   73.405  83.352  1.00 47.17  ? 300 PRO   F O     1 
ATOM   13425 C  CB    . PRO   E 4  300 ? 7.703   74.580  86.041  1.00 36.05  ? 300 PRO   F CB    1 
ATOM   13426 C  CG    . PRO   E 4  300 ? 7.553   73.951  87.364  1.00 46.04  ? 300 PRO   F CG    1 
ATOM   13427 C  CD    . PRO   E 4  300 ? 6.388   72.999  87.231  1.00 41.24  ? 300 PRO   F CD    1 
ATOM   13428 N  N     . ALA   E 4  301 ? 9.060   71.792  84.902  1.00 40.19  ? 301 ALA   F N     1 
ATOM   13429 C  CA    . ALA   E 4  301 ? 10.275  71.240  84.323  1.00 39.09  ? 301 ALA   F CA    1 
ATOM   13430 C  C     . ALA   E 4  301 ? 10.019  70.146  83.294  1.00 39.96  ? 301 ALA   F C     1 
ATOM   13431 O  O     . ALA   E 4  301 ? 10.955  69.768  82.586  1.00 37.61  ? 301 ALA   F O     1 
ATOM   13432 C  CB    . ALA   E 4  301 ? 11.185  70.690  85.431  1.00 31.81  ? 301 ALA   F CB    1 
ATOM   13433 N  N     . ILE   E 4  302 ? 8.798   69.613  83.197  1.00 39.08  ? 302 ILE   F N     1 
ATOM   13434 C  CA    . ILE   E 4  302 ? 8.569   68.470  82.318  1.00 36.49  ? 302 ILE   F CA    1 
ATOM   13435 C  C     . ILE   E 4  302 ? 7.330   68.654  81.450  1.00 39.39  ? 302 ILE   F C     1 
ATOM   13436 O  O     . ILE   E 4  302 ? 7.081   67.857  80.541  1.00 40.09  ? 302 ILE   F O     1 
ATOM   13437 C  CB    . ILE   E 4  302 ? 8.483   67.156  83.124  1.00 36.08  ? 302 ILE   F CB    1 
ATOM   13438 C  CG1   . ILE   E 4  302 ? 7.218   67.096  83.986  1.00 32.38  ? 302 ILE   F CG1   1 
ATOM   13439 C  CG2   . ILE   E 4  302 ? 9.715   66.992  83.991  1.00 34.44  ? 302 ILE   F CG2   1 
ATOM   13440 C  CD1   . ILE   E 4  302 ? 7.094   65.784  84.748  1.00 25.92  ? 302 ILE   F CD1   1 
ATOM   13441 N  N     . SER   E 4  303 ? 6.545   69.701  81.706  1.00 47.02  ? 303 SER   F N     1 
ATOM   13442 C  CA    . SER   E 4  303 ? 5.409   69.988  80.835  1.00 43.50  ? 303 SER   F CA    1 
ATOM   13443 C  C     . SER   E 4  303 ? 5.876   70.066  79.383  1.00 45.05  ? 303 SER   F C     1 
ATOM   13444 O  O     . SER   E 4  303 ? 7.021   70.423  79.091  1.00 43.25  ? 303 SER   F O     1 
ATOM   13445 C  CB    . SER   E 4  303 ? 4.732   71.300  81.247  1.00 35.29  ? 303 SER   F CB    1 
ATOM   13446 O  OG    . SER   E 4  303 ? 3.425   71.422  80.694  1.00 42.74  ? 303 SER   F OG    1 
ATOM   13447 N  N     . THR   E 4  304 ? 4.989   69.714  78.463  1.00 39.37  ? 304 THR   F N     1 
ATOM   13448 C  CA    . THR   E 4  304 ? 5.284   69.862  77.045  1.00 41.03  ? 304 THR   F CA    1 
ATOM   13449 C  C     . THR   E 4  304 ? 4.246   70.734  76.349  1.00 45.62  ? 304 THR   F C     1 
ATOM   13450 O  O     . THR   E 4  304 ? 4.025   70.608  75.147  1.00 45.94  ? 304 THR   F O     1 
ATOM   13451 C  CB    . THR   E 4  304 ? 5.394   68.496  76.379  1.00 43.60  ? 304 THR   F CB    1 
ATOM   13452 O  OG1   . THR   E 4  304 ? 4.080   67.934  76.213  1.00 41.24  ? 304 THR   F OG1   1 
ATOM   13453 C  CG2   . THR   E 4  304 ? 6.268   67.589  77.251  1.00 34.90  ? 304 THR   F CG2   1 
ATOM   13454 N  N     . LYS   E 4  305 ? 3.613   71.633  77.107  1.00 50.92  ? 305 LYS   F N     1 
ATOM   13455 C  CA    . LYS   E 4  305 ? 2.670   72.605  76.567  1.00 55.11  ? 305 LYS   F CA    1 
ATOM   13456 C  C     . LYS   E 4  305 ? 3.114   73.175  75.215  1.00 49.85  ? 305 LYS   F C     1 
ATOM   13457 O  O     . LYS   E 4  305 ? 2.432   72.998  74.198  1.00 54.42  ? 305 LYS   F O     1 
ATOM   13458 C  CB    . LYS   E 4  305 ? 2.467   73.734  77.590  1.00 51.12  ? 305 LYS   F CB    1 
ATOM   13459 C  CG    . LYS   E 4  305 ? 1.012   74.142  77.770  1.00 60.52  ? 305 LYS   F CG    1 
ATOM   13460 C  CD    . LYS   E 4  305 ? 0.846   75.506  78.450  1.00 69.30  ? 305 LYS   F CD    1 
ATOM   13461 C  CE    . LYS   E 4  305 ? -0.648  75.830  78.635  1.00 81.32  ? 305 LYS   F CE    1 
ATOM   13462 N  NZ    . LYS   E 4  305 ? -0.944  77.238  79.046  1.00 63.73  ? 305 LYS   F NZ    1 
ATOM   13463 N  N     . HIS   E 4  306 ? 4.243   73.875  75.184  1.00 40.69  ? 306 HIS   F N     1 
ATOM   13464 C  CA    . HIS   E 4  306 ? 4.725   74.507  73.959  1.00 48.96  ? 306 HIS   F CA    1 
ATOM   13465 C  C     . HIS   E 4  306 ? 5.971   73.807  73.433  1.00 50.21  ? 306 HIS   F C     1 
ATOM   13466 O  O     . HIS   E 4  306 ? 6.917   74.450  72.980  1.00 49.35  ? 306 HIS   F O     1 
ATOM   13467 C  CB    . HIS   E 4  306 ? 5.040   75.989  74.165  1.00 56.63  ? 306 HIS   F CB    1 
ATOM   13468 C  CG    . HIS   E 4  306 ? 4.114   76.702  75.099  1.00 61.60  ? 306 HIS   F CG    1 
ATOM   13469 N  ND1   . HIS   E 4  306 ? 2.805   76.996  74.775  1.00 60.43  ? 306 HIS   F ND1   1 
ATOM   13470 C  CD2   . HIS   E 4  306 ? 4.320   77.210  76.338  1.00 60.28  ? 306 HIS   F CD2   1 
ATOM   13471 C  CE1   . HIS   E 4  306 ? 2.237   77.633  75.785  1.00 64.29  ? 306 HIS   F CE1   1 
ATOM   13472 N  NE2   . HIS   E 4  306 ? 3.134   77.773  76.746  1.00 70.21  ? 306 HIS   F NE2   1 
ATOM   13473 N  N     . LEU   E 4  307 ? 6.013   72.491  73.521  1.00 45.30  ? 307 LEU   F N     1 
ATOM   13474 C  CA    . LEU   E 4  307 ? 7.170   71.757  73.048  1.00 37.28  ? 307 LEU   F CA    1 
ATOM   13475 C  C     . LEU   E 4  307 ? 6.857   71.185  71.669  1.00 42.75  ? 307 LEU   F C     1 
ATOM   13476 O  O     . LEU   E 4  307 ? 5.689   71.010  71.301  1.00 40.24  ? 307 LEU   F O     1 
ATOM   13477 C  CB    . LEU   E 4  307 ? 7.545   70.651  74.038  1.00 37.99  ? 307 LEU   F CB    1 
ATOM   13478 C  CG    . LEU   E 4  307 ? 9.010   70.225  74.013  1.00 44.19  ? 307 LEU   F CG    1 
ATOM   13479 C  CD1   . LEU   E 4  307 ? 9.909   71.416  74.320  1.00 30.92  ? 307 LEU   F CD1   1 
ATOM   13480 C  CD2   . LEU   E 4  307 ? 9.279   69.050  74.970  1.00 38.39  ? 307 LEU   F CD2   1 
ATOM   13481 N  N     . HIS   E 4  308 ? 7.920   70.908  70.898  1.00 30.08  ? 308 HIS   F N     1 
ATOM   13482 C  CA    . HIS   E 4  308 ? 7.764   70.400  69.534  1.00 25.52  ? 308 HIS   F CA    1 
ATOM   13483 C  C     . HIS   E 4  308 ? 7.349   68.930  69.473  1.00 31.53  ? 308 HIS   F C     1 
ATOM   13484 O  O     . HIS   E 4  308 ? 7.004   68.455  68.383  1.00 36.65  ? 308 HIS   F O     1 
ATOM   13485 C  CB    . HIS   E 4  308 ? 9.049   70.602  68.740  1.00 27.13  ? 308 HIS   F CB    1 
ATOM   13486 C  CG    . HIS   E 4  308 ? 10.282  70.395  69.549  1.00 31.81  ? 308 HIS   F CG    1 
ATOM   13487 N  ND1   . HIS   E 4  308 ? 10.722  71.314  70.481  1.00 40.14  ? 308 HIS   F ND1   1 
ATOM   13488 C  CD2   . HIS   E 4  308 ? 11.161  69.371  69.584  1.00 27.31  ? 308 HIS   F CD2   1 
ATOM   13489 C  CE1   . HIS   E 4  308 ? 11.820  70.864  71.056  1.00 30.97  ? 308 HIS   F CE1   1 
ATOM   13490 N  NE2   . HIS   E 4  308 ? 12.101  69.682  70.537  1.00 44.97  ? 308 HIS   F NE2   1 
ATOM   13491 N  N     . TYR   E 4  309 ? 7.379   68.210  70.594  1.00 33.47  ? 309 TYR   F N     1 
ATOM   13492 C  CA    . TYR   E 4  309 ? 6.714   66.923  70.751  1.00 33.44  ? 309 TYR   F CA    1 
ATOM   13493 C  C     . TYR   E 4  309 ? 5.947   66.962  72.064  1.00 35.58  ? 309 TYR   F C     1 
ATOM   13494 O  O     . TYR   E 4  309 ? 6.211   67.803  72.926  1.00 34.49  ? 309 TYR   F O     1 
ATOM   13495 C  CB    . TYR   E 4  309 ? 7.699   65.743  70.752  1.00 28.69  ? 309 TYR   F CB    1 
ATOM   13496 C  CG    . TYR   E 4  309 ? 8.581   65.734  71.989  1.00 34.93  ? 309 TYR   F CG    1 
ATOM   13497 C  CD1   . TYR   E 4  309 ? 8.174   65.109  73.152  1.00 27.82  ? 309 TYR   F CD1   1 
ATOM   13498 C  CD2   . TYR   E 4  309 ? 9.800   66.375  71.996  1.00 28.36  ? 309 TYR   F CD2   1 
ATOM   13499 C  CE1   . TYR   E 4  309 ? 8.948   65.117  74.262  1.00 24.58  ? 309 TYR   F CE1   1 
ATOM   13500 C  CE2   . TYR   E 4  309 ? 10.577  66.386  73.110  1.00 31.68  ? 309 TYR   F CE2   1 
ATOM   13501 C  CZ    . TYR   E 4  309 ? 10.147  65.761  74.241  1.00 29.26  ? 309 TYR   F CZ    1 
ATOM   13502 O  OH    . TYR   E 4  309 ? 10.940  65.767  75.359  1.00 36.95  ? 309 TYR   F OH    1 
ATOM   13503 N  N     . GLN   E 4  310 ? 4.992   66.048  72.205  1.00 35.54  ? 310 GLN   F N     1 
ATOM   13504 C  CA    . GLN   E 4  310 ? 4.173   65.908  73.400  1.00 30.53  ? 310 GLN   F CA    1 
ATOM   13505 C  C     . GLN   E 4  310 ? 4.521   64.617  74.132  1.00 34.27  ? 310 GLN   F C     1 
ATOM   13506 O  O     . GLN   E 4  310 ? 4.986   63.645  73.528  1.00 36.62  ? 310 GLN   F O     1 
ATOM   13507 C  CB    . GLN   E 4  310 ? 2.676   65.886  73.056  1.00 34.65  ? 310 GLN   F CB    1 
ATOM   13508 C  CG    . GLN   E 4  310 ? 2.145   67.091  72.328  1.00 28.45  ? 310 GLN   F CG    1 
ATOM   13509 C  CD    . GLN   E 4  310 ? 2.255   68.348  73.141  1.00 39.78  ? 310 GLN   F CD    1 
ATOM   13510 O  OE1   . GLN   E 4  310 ? 1.678   68.462  74.230  1.00 50.20  ? 310 GLN   F OE1   1 
ATOM   13511 N  NE2   . GLN   E 4  310 ? 3.014   69.309  72.629  1.00 52.56  ? 310 GLN   F NE2   1 
ATOM   13512 N  N     . SER   E 4  311 ? 4.253   64.612  75.444  1.00 33.11  ? 311 SER   F N     1 
ATOM   13513 C  CA    . SER   E 4  311 ? 4.426   63.452  76.310  1.00 31.19  ? 311 SER   F CA    1 
ATOM   13514 C  C     . SER   E 4  311 ? 3.142   63.140  77.066  1.00 37.05  ? 311 SER   F C     1 
ATOM   13515 O  O     . SER   E 4  311 ? 2.381   64.035  77.446  1.00 35.09  ? 311 SER   F O     1 
ATOM   13516 C  CB    . SER   E 4  311 ? 5.542   63.652  77.374  1.00 31.80  ? 311 SER   F CB    1 
ATOM   13517 O  OG    . SER   E 4  311 ? 6.837   63.776  76.818  1.00 29.21  ? 311 SER   F OG    1 
ATOM   13518 N  N     . PHE   E 4  312 ? 2.926   61.850  77.305  1.00 46.30  ? 312 PHE   F N     1 
ATOM   13519 C  CA    . PHE   E 4  312 ? 2.103   61.359  78.405  1.00 42.75  ? 312 PHE   F CA    1 
ATOM   13520 C  C     . PHE   E 4  312 ? 2.939   60.328  79.163  1.00 39.70  ? 312 PHE   F C     1 
ATOM   13521 O  O     . PHE   E 4  312 ? 4.077   60.034  78.783  1.00 37.83  ? 312 PHE   F O     1 
ATOM   13522 C  CB    . PHE   E 4  312 ? 0.760   60.792  77.907  1.00 40.38  ? 312 PHE   F CB    1 
ATOM   13523 C  CG    . PHE   E 4  312 ? 0.889   59.557  77.054  1.00 44.24  ? 312 PHE   F CG    1 
ATOM   13524 C  CD1   . PHE   E 4  312 ? 1.030   59.657  75.684  1.00 43.94  ? 312 PHE   F CD1   1 
ATOM   13525 C  CD2   . PHE   E 4  312 ? 0.861   58.290  77.629  1.00 42.87  ? 312 PHE   F CD2   1 
ATOM   13526 C  CE1   . PHE   E 4  312 ? 1.148   58.510  74.903  1.00 52.06  ? 312 PHE   F CE1   1 
ATOM   13527 C  CE2   . PHE   E 4  312 ? 0.974   57.143  76.850  1.00 41.00  ? 312 PHE   F CE2   1 
ATOM   13528 C  CZ    . PHE   E 4  312 ? 1.119   57.248  75.493  1.00 40.81  ? 312 PHE   F CZ    1 
ATOM   13529 N  N     . GLN   E 4  313 ? 2.405   59.800  80.263  1.00 47.24  ? 313 GLN   F N     1 
ATOM   13530 C  CA    . GLN   E 4  313 ? 3.144   58.785  81.010  1.00 40.30  ? 313 GLN   F CA    1 
ATOM   13531 C  C     . GLN   E 4  313 ? 2.258   58.198  82.095  1.00 41.56  ? 313 GLN   F C     1 
ATOM   13532 O  O     . GLN   E 4  313 ? 1.409   58.888  82.666  1.00 37.38  ? 313 GLN   F O     1 
ATOM   13533 C  CB    . GLN   E 4  313 ? 4.425   59.353  81.634  1.00 38.14  ? 313 GLN   F CB    1 
ATOM   13534 C  CG    . GLN   E 4  313 ? 5.325   58.301  82.279  1.00 35.67  ? 313 GLN   F CG    1 
ATOM   13535 C  CD    . GLN   E 4  313 ? 6.631   58.888  82.787  1.00 37.10  ? 313 GLN   F CD    1 
ATOM   13536 O  OE1   . GLN   E 4  313 ? 7.058   59.951  82.319  1.00 32.46  ? 313 GLN   F OE1   1 
ATOM   13537 N  NE2   . GLN   E 4  313 ? 7.265   58.214  83.763  1.00 31.94  ? 313 GLN   F NE2   1 
ATOM   13538 N  N     . LEU   E 4  314 ? 2.468   56.910  82.359  1.00 44.08  ? 314 LEU   F N     1 
ATOM   13539 C  CA    . LEU   E 4  314 ? 1.785   56.182  83.418  1.00 41.71  ? 314 LEU   F CA    1 
ATOM   13540 C  C     . LEU   E 4  314 ? 2.729   56.040  84.606  1.00 39.31  ? 314 LEU   F C     1 
ATOM   13541 O  O     . LEU   E 4  314 ? 3.878   55.612  84.447  1.00 35.39  ? 314 LEU   F O     1 
ATOM   13542 C  CB    . LEU   E 4  314 ? 1.325   54.807  82.927  1.00 35.99  ? 314 LEU   F CB    1 
ATOM   13543 C  CG    . LEU   E 4  314 ? 0.345   54.020  83.804  1.00 40.91  ? 314 LEU   F CG    1 
ATOM   13544 C  CD1   . LEU   E 4  314 ? -0.980  54.755  83.986  1.00 35.22  ? 314 LEU   F CD1   1 
ATOM   13545 C  CD2   . LEU   E 4  314 ? 0.086   52.665  83.196  1.00 41.11  ? 314 LEU   F CD2   1 
ATOM   13546 N  N     . PHE   E 4  315 ? 2.250   56.422  85.783  1.00 36.97  ? 315 PHE   F N     1 
ATOM   13547 C  CA    . PHE   E 4  315 ? 3.015   56.355  87.013  1.00 32.22  ? 315 PHE   F CA    1 
ATOM   13548 C  C     . PHE   E 4  315 ? 2.388   55.334  87.946  1.00 42.97  ? 315 PHE   F C     1 
ATOM   13549 O  O     . PHE   E 4  315 ? 1.160   55.215  88.020  1.00 40.68  ? 315 PHE   F O     1 
ATOM   13550 C  CB    . PHE   E 4  315 ? 3.068   57.716  87.713  1.00 39.00  ? 315 PHE   F CB    1 
ATOM   13551 C  CG    . PHE   E 4  315 ? 3.785   58.778  86.934  1.00 41.22  ? 315 PHE   F CG    1 
ATOM   13552 C  CD1   . PHE   E 4  315 ? 3.091   59.597  86.051  1.00 40.86  ? 315 PHE   F CD1   1 
ATOM   13553 C  CD2   . PHE   E 4  315 ? 5.155   58.966  87.084  1.00 39.24  ? 315 PHE   F CD2   1 
ATOM   13554 C  CE1   . PHE   E 4  315 ? 3.748   60.583  85.328  1.00 31.04  ? 315 PHE   F CE1   1 
ATOM   13555 C  CE2   . PHE   E 4  315 ? 5.813   59.948  86.357  1.00 40.58  ? 315 PHE   F CE2   1 
ATOM   13556 C  CZ    . PHE   E 4  315 ? 5.098   60.758  85.481  1.00 26.45  ? 315 PHE   F CZ    1 
ATOM   13557 N  N     . GLY   E 4  316 ? 3.231   54.601  88.658  1.00 46.10  ? 316 GLY   F N     1 
ATOM   13558 C  CA    . GLY   E 4  316 ? 2.729   53.814  89.757  1.00 41.80  ? 316 GLY   F CA    1 
ATOM   13559 C  C     . GLY   E 4  316 ? 3.137   54.475  91.052  1.00 43.14  ? 316 GLY   F C     1 
ATOM   13560 O  O     . GLY   E 4  316 ? 4.332   54.595  91.308  1.00 63.32  ? 316 GLY   F O     1 
ATOM   13561 N  N     . PHE   E 4  317 ? 2.183   54.932  91.860  1.00 40.18  ? 317 PHE   F N     1 
ATOM   13562 C  CA    . PHE   E 4  317 ? 2.476   55.520  93.163  1.00 50.20  ? 317 PHE   F CA    1 
ATOM   13563 C  C     . PHE   E 4  317 ? 2.234   54.482  94.256  1.00 55.39  ? 317 PHE   F C     1 
ATOM   13564 O  O     . PHE   E 4  317 ? 1.232   53.756  94.225  1.00 47.42  ? 317 PHE   F O     1 
ATOM   13565 C  CB    . PHE   E 4  317 ? 1.609   56.759  93.423  1.00 45.62  ? 317 PHE   F CB    1 
ATOM   13566 C  CG    . PHE   E 4  317 ? 2.089   58.017  92.736  1.00 48.90  ? 317 PHE   F CG    1 
ATOM   13567 C  CD1   . PHE   E 4  317 ? 1.788   58.262  91.397  1.00 52.82  ? 317 PHE   F CD1   1 
ATOM   13568 C  CD2   . PHE   E 4  317 ? 2.793   58.978  93.437  1.00 46.14  ? 317 PHE   F CD2   1 
ATOM   13569 C  CE1   . PHE   E 4  317 ? 2.210   59.423  90.771  1.00 39.78  ? 317 PHE   F CE1   1 
ATOM   13570 C  CE2   . PHE   E 4  317 ? 3.212   60.147  92.813  1.00 43.54  ? 317 PHE   F CE2   1 
ATOM   13571 C  CZ    . PHE   E 4  317 ? 2.922   60.368  91.482  1.00 37.63  ? 317 PHE   F CZ    1 
ATOM   13572 N  N     . ASP   E 4  318 ? 3.150   54.415  95.227  1.00 51.10  ? 318 ASP   F N     1 
ATOM   13573 C  CA    . ASP   E 4  318 ? 3.072   53.432  96.303  1.00 48.77  ? 318 ASP   F CA    1 
ATOM   13574 C  C     . ASP   E 4  318 ? 2.951   54.128  97.653  1.00 52.15  ? 318 ASP   F C     1 
ATOM   13575 O  O     . ASP   E 4  318 ? 3.783   54.973  97.993  1.00 52.44  ? 318 ASP   F O     1 
ATOM   13576 C  CB    . ASP   E 4  318 ? 4.290   52.508  96.281  1.00 48.92  ? 318 ASP   F CB    1 
ATOM   13577 C  CG    . ASP   E 4  318 ? 4.329   51.624  95.034  1.00 58.18  ? 318 ASP   F CG    1 
ATOM   13578 O  OD1   . ASP   E 4  318 ? 3.252   51.383  94.432  1.00 48.83  ? 318 ASP   F OD1   1 
ATOM   13579 O  OD2   . ASP   E 4  318 ? 5.435   51.165  94.661  1.00 58.53  ? 318 ASP   F OD2   1 
ATOM   13580 N  N     . PHE   E 4  319 ? 1.928   53.750  98.428  1.00 53.07  ? 319 PHE   F N     1 
ATOM   13581 C  CA    . PHE   E 4  319 ? 1.600   54.386  99.697  1.00 52.29  ? 319 PHE   F CA    1 
ATOM   13582 C  C     . PHE   E 4  319 ? 1.560   53.379  100.838 1.00 48.26  ? 319 PHE   F C     1 
ATOM   13583 O  O     . PHE   E 4  319 ? 1.399   52.174  100.633 1.00 40.71  ? 319 PHE   F O     1 
ATOM   13584 C  CB    . PHE   E 4  319 ? 0.241   55.098  99.637  1.00 53.18  ? 319 PHE   F CB    1 
ATOM   13585 C  CG    . PHE   E 4  319 ? 0.154   56.146  98.579  1.00 50.68  ? 319 PHE   F CG    1 
ATOM   13586 C  CD1   . PHE   E 4  319 ? 0.592   57.434  98.831  1.00 51.51  ? 319 PHE   F CD1   1 
ATOM   13587 C  CD2   . PHE   E 4  319 ? -0.354  55.837  97.328  1.00 51.39  ? 319 PHE   F CD2   1 
ATOM   13588 C  CE1   . PHE   E 4  319 ? 0.521   58.398  97.854  1.00 56.67  ? 319 PHE   F CE1   1 
ATOM   13589 C  CE2   . PHE   E 4  319 ? -0.429  56.791  96.347  1.00 53.75  ? 319 PHE   F CE2   1 
ATOM   13590 C  CZ    . PHE   E 4  319 ? 0.001   58.079  96.609  1.00 55.17  ? 319 PHE   F CZ    1 
ATOM   13591 N  N     . MET   E 4  320 ? 1.654   53.917  102.055 1.00 52.42  ? 320 MET   F N     1 
ATOM   13592 C  CA    . MET   E 4  320 ? 1.622   53.149  103.296 1.00 58.98  ? 320 MET   F CA    1 
ATOM   13593 C  C     . MET   E 4  320 ? 0.660   53.803  104.278 1.00 61.25  ? 320 MET   F C     1 
ATOM   13594 O  O     . MET   E 4  320 ? 0.913   54.926  104.727 1.00 67.97  ? 320 MET   F O     1 
ATOM   13595 C  CB    . MET   E 4  320 ? 3.023   53.068  103.904 1.00 51.18  ? 320 MET   F CB    1 
ATOM   13596 C  CG    . MET   E 4  320 ? 3.801   51.873  103.426 1.00 57.51  ? 320 MET   F CG    1 
ATOM   13597 S  SD    . MET   E 4  320 ? 3.146   50.389  104.207 1.00 90.98  ? 320 MET   F SD    1 
ATOM   13598 C  CE    . MET   E 4  320 ? 3.511   50.765  105.930 1.00 78.68  ? 320 MET   F CE    1 
ATOM   13599 N  N     . VAL   E 4  321 ? -0.426  53.107  104.630 1.00 57.79  ? 321 VAL   F N     1 
ATOM   13600 C  CA    . VAL   E 4  321 ? -1.392  53.608  105.611 1.00 54.46  ? 321 VAL   F CA    1 
ATOM   13601 C  C     . VAL   E 4  321 ? -0.978  53.142  107.000 1.00 61.41  ? 321 VAL   F C     1 
ATOM   13602 O  O     . VAL   E 4  321 ? -0.935  51.936  107.257 1.00 68.50  ? 321 VAL   F O     1 
ATOM   13603 C  CB    . VAL   E 4  321 ? -2.813  53.122  105.299 1.00 54.70  ? 321 VAL   F CB    1 
ATOM   13604 C  CG1   . VAL   E 4  321 ? -3.792  53.767  106.269 1.00 59.70  ? 321 VAL   F CG1   1 
ATOM   13605 C  CG2   . VAL   E 4  321 ? -3.184  53.405  103.853 1.00 49.80  ? 321 VAL   F CG2   1 
ATOM   13606 N  N     . ASP   E 4  322 ? -0.715  54.078  107.914 1.00 60.82  ? 322 ASP   F N     1 
ATOM   13607 C  CA    . ASP   E 4  322 ? -0.219  53.676  109.227 1.00 65.13  ? 322 ASP   F CA    1 
ATOM   13608 C  C     . ASP   E 4  322 ? -1.372  53.441  110.214 1.00 66.32  ? 322 ASP   F C     1 
ATOM   13609 O  O     . ASP   E 4  322 ? -2.550  53.388  109.846 1.00 67.96  ? 322 ASP   F O     1 
ATOM   13610 C  CB    . ASP   E 4  322 ? 0.812   54.681  109.755 1.00 62.32  ? 322 ASP   F CB    1 
ATOM   13611 C  CG    . ASP   E 4  322 ? 0.193   55.925  110.374 1.00 65.27  ? 322 ASP   F CG    1 
ATOM   13612 O  OD1   . ASP   E 4  322 ? -1.050  56.090  110.324 1.00 55.86  ? 322 ASP   F OD1   1 
ATOM   13613 O  OD2   . ASP   E 4  322 ? 0.980   56.747  110.915 1.00 57.85  ? 322 ASP   F OD2   1 
ATOM   13614 N  N     . GLU   E 4  323 ? -1.015  53.273  111.491 1.00 72.90  ? 323 GLU   F N     1 
ATOM   13615 C  CA    . GLU   E 4  323 ? -1.978  52.903  112.529 1.00 71.08  ? 323 GLU   F CA    1 
ATOM   13616 C  C     . GLU   E 4  323 ? -3.110  53.917  112.628 1.00 63.26  ? 323 GLU   F C     1 
ATOM   13617 O  O     . GLU   E 4  323 ? -4.289  53.547  112.690 1.00 56.81  ? 323 GLU   F O     1 
ATOM   13618 C  CB    . GLU   E 4  323 ? -1.250  52.791  113.871 1.00 74.07  ? 323 GLU   F CB    1 
ATOM   13619 C  CG    . GLU   E 4  323 ? -1.730  51.703  114.815 1.00 72.50  ? 323 GLU   F CG    1 
ATOM   13620 C  CD    . GLU   E 4  323 ? -0.753  51.495  115.962 1.00 82.28  ? 323 GLU   F CD    1 
ATOM   13621 O  OE1   . GLU   E 4  323 ? -0.274  52.499  116.540 1.00 85.26  ? 323 GLU   F OE1   1 
ATOM   13622 O  OE2   . GLU   E 4  323 ? -0.442  50.328  116.269 1.00 79.66  ? 323 GLU   F OE2   1 
ATOM   13623 N  N     . GLU   E 4  324 ? -2.762  55.204  112.658 1.00 61.38  ? 324 GLU   F N     1 
ATOM   13624 C  CA    . GLU   E 4  324 ? -3.710  56.297  112.824 1.00 63.50  ? 324 GLU   F CA    1 
ATOM   13625 C  C     . GLU   E 4  324 ? -4.426  56.686  111.532 1.00 57.97  ? 324 GLU   F C     1 
ATOM   13626 O  O     . GLU   E 4  324 ? -5.099  57.718  111.507 1.00 62.84  ? 324 GLU   F O     1 
ATOM   13627 C  CB    . GLU   E 4  324 ? -2.994  57.515  113.406 1.00 55.20  ? 324 GLU   F CB    1 
ATOM   13628 C  CG    . GLU   E 4  324 ? -2.750  57.407  114.896 1.00 65.44  ? 324 GLU   F CG    1 
ATOM   13629 C  CD    . GLU   E 4  324 ? -4.033  57.123  115.661 1.00 83.39  ? 324 GLU   F CD    1 
ATOM   13630 O  OE1   . GLU   E 4  324 ? -5.100  57.660  115.268 1.00 78.89  ? 324 GLU   F OE1   1 
ATOM   13631 O  OE2   . GLU   E 4  324 ? -3.978  56.347  116.645 1.00 89.12  ? 324 GLU   F OE2   1 
ATOM   13632 N  N     . LEU   E 4  325 ? -4.318  55.892  110.471 1.00 51.17  ? 325 LEU   F N     1 
ATOM   13633 C  CA    . LEU   E 4  325 ? -4.960  56.222  109.207 1.00 55.24  ? 325 LEU   F CA    1 
ATOM   13634 C  C     . LEU   E 4  325 ? -4.357  57.495  108.603 1.00 64.19  ? 325 LEU   F C     1 
ATOM   13635 O  O     . LEU   E 4  325 ? -5.073  58.367  108.099 1.00 61.53  ? 325 LEU   F O     1 
ATOM   13636 C  CB    . LEU   E 4  325 ? -6.472  56.344  109.383 1.00 52.71  ? 325 LEU   F CB    1 
ATOM   13637 C  CG    . LEU   E 4  325 ? -7.107  55.005  109.768 1.00 53.23  ? 325 LEU   F CG    1 
ATOM   13638 C  CD1   . LEU   E 4  325 ? -8.613  55.106  109.891 1.00 54.00  ? 325 LEU   F CD1   1 
ATOM   13639 C  CD2   . LEU   E 4  325 ? -6.745  53.960  108.728 1.00 61.60  ? 325 LEU   F CD2   1 
ATOM   13640 N  N     . LYS   E 4  326 ? -3.029  57.595  108.670 1.00 51.18  ? 326 LYS   F N     1 
ATOM   13641 C  CA    . LYS   E 4  326 ? -2.257  58.641  108.018 1.00 49.36  ? 326 LYS   F CA    1 
ATOM   13642 C  C     . LYS   E 4  326 ? -1.454  58.018  106.885 1.00 59.70  ? 326 LYS   F C     1 
ATOM   13643 O  O     . LYS   E 4  326 ? -0.668  57.094  107.117 1.00 65.65  ? 326 LYS   F O     1 
ATOM   13644 C  CB    . LYS   E 4  326 ? -1.325  59.334  109.005 1.00 53.58  ? 326 LYS   F CB    1 
ATOM   13645 C  CG    . LYS   E 4  326 ? -0.196  60.080  108.330 1.00 50.78  ? 326 LYS   F CG    1 
ATOM   13646 C  CD    . LYS   E 4  326 ? 0.503   60.999  109.306 1.00 60.26  ? 326 LYS   F CD    1 
ATOM   13647 C  CE    . LYS   E 4  326 ? 1.561   61.850  108.622 1.00 46.86  ? 326 LYS   F CE    1 
ATOM   13648 N  NZ    . LYS   E 4  326 ? 2.023   62.960  109.511 1.00 58.15  ? 326 LYS   F NZ    1 
ATOM   13649 N  N     . VAL   E 4  327 ? -1.646  58.529  105.665 1.00 56.52  ? 327 VAL   F N     1 
ATOM   13650 C  CA    . VAL   E 4  327 ? -1.005  57.979  104.476 1.00 44.56  ? 327 VAL   F CA    1 
ATOM   13651 C  C     . VAL   E 4  327 ? 0.435   58.474  104.376 1.00 49.67  ? 327 VAL   F C     1 
ATOM   13652 O  O     . VAL   E 4  327 ? 0.740   59.635  104.669 1.00 51.89  ? 327 VAL   F O     1 
ATOM   13653 C  CB    . VAL   E 4  327 ? -1.812  58.346  103.219 1.00 44.51  ? 327 VAL   F CB    1 
ATOM   13654 C  CG1   . VAL   E 4  327 ? -1.028  58.001  101.970 1.00 56.02  ? 327 VAL   F CG1   1 
ATOM   13655 C  CG2   . VAL   E 4  327 ? -3.144  57.633  103.210 1.00 49.20  ? 327 VAL   F CG2   1 
ATOM   13656 N  N     . TRP   E 4  328 ? 1.333   57.586  103.951 1.00 54.85  ? 328 TRP   F N     1 
ATOM   13657 C  CA    . TRP   E 4  328 ? 2.734   57.911  103.726 1.00 52.33  ? 328 TRP   F CA    1 
ATOM   13658 C  C     . TRP   E 4  328 ? 3.136   57.465  102.329 1.00 58.63  ? 328 TRP   F C     1 
ATOM   13659 O  O     . TRP   E 4  328 ? 2.754   56.378  101.881 1.00 52.81  ? 328 TRP   F O     1 
ATOM   13660 C  CB    . TRP   E 4  328 ? 3.642   57.239  104.768 1.00 56.18  ? 328 TRP   F CB    1 
ATOM   13661 C  CG    . TRP   E 4  328 ? 3.397   57.723  106.156 1.00 54.45  ? 328 TRP   F CG    1 
ATOM   13662 C  CD1   . TRP   E 4  328 ? 2.482   57.238  107.048 1.00 51.18  ? 328 TRP   F CD1   1 
ATOM   13663 C  CD2   . TRP   E 4  328 ? 4.075   58.796  106.815 1.00 47.83  ? 328 TRP   F CD2   1 
ATOM   13664 N  NE1   . TRP   E 4  328 ? 2.550   57.947  108.226 1.00 47.22  ? 328 TRP   F NE1   1 
ATOM   13665 C  CE2   . TRP   E 4  328 ? 3.518   58.910  108.109 1.00 47.37  ? 328 TRP   F CE2   1 
ATOM   13666 C  CE3   . TRP   E 4  328 ? 5.098   59.673  106.436 1.00 47.37  ? 328 TRP   F CE3   1 
ATOM   13667 C  CZ2   . TRP   E 4  328 ? 3.946   59.874  109.026 1.00 42.51  ? 328 TRP   F CZ2   1 
ATOM   13668 C  CZ3   . TRP   E 4  328 ? 5.526   60.626  107.345 1.00 54.19  ? 328 TRP   F CZ3   1 
ATOM   13669 C  CH2   . TRP   E 4  328 ? 4.949   60.717  108.630 1.00 55.63  ? 328 TRP   F CH2   1 
ATOM   13670 N  N     . LEU   E 4  329 ? 3.908   58.310  101.643 1.00 61.13  ? 329 LEU   F N     1 
ATOM   13671 C  CA    . LEU   E 4  329 ? 4.406   57.999  100.307 1.00 59.92  ? 329 LEU   F CA    1 
ATOM   13672 C  C     . LEU   E 4  329 ? 5.710   57.206  100.407 1.00 58.58  ? 329 LEU   F C     1 
ATOM   13673 O  O     . LEU   E 4  329 ? 6.630   57.594  101.140 1.00 53.51  ? 329 LEU   F O     1 
ATOM   13674 C  CB    . LEU   E 4  329 ? 4.608   59.288  99.497  1.00 55.46  ? 329 LEU   F CB    1 
ATOM   13675 C  CG    . LEU   E 4  329 ? 5.197   59.204  98.075  1.00 51.80  ? 329 LEU   F CG    1 
ATOM   13676 C  CD1   . LEU   E 4  329 ? 4.314   58.424  97.099  1.00 41.32  ? 329 LEU   F CD1   1 
ATOM   13677 C  CD2   . LEU   E 4  329 ? 5.504   60.593  97.526  1.00 50.19  ? 329 LEU   F CD2   1 
ATOM   13678 N  N     . ILE   E 4  330 ? 5.784   56.099  99.660  1.00 57.17  ? 330 ILE   F N     1 
ATOM   13679 C  CA    . ILE   E 4  330 ? 6.957   55.224  99.634  1.00 62.62  ? 330 ILE   F CA    1 
ATOM   13680 C  C     . ILE   E 4  330 ? 7.795   55.501  98.391  1.00 58.99  ? 330 ILE   F C     1 
ATOM   13681 O  O     . ILE   E 4  330 ? 8.877   56.092  98.477  1.00 53.75  ? 330 ILE   F O     1 
ATOM   13682 C  CB    . ILE   E 4  330 ? 6.552   53.736  99.684  1.00 65.15  ? 330 ILE   F CB    1 
ATOM   13683 C  CG1   . ILE   E 4  330 ? 5.829   53.413  100.989 1.00 59.00  ? 330 ILE   F CG1   1 
ATOM   13684 C  CG2   . ILE   E 4  330 ? 7.774   52.849  99.539  1.00 57.96  ? 330 ILE   F CG2   1 
ATOM   13685 C  CD1   . ILE   E 4  330 ? 6.665   53.684  102.214 1.00 49.96  ? 330 ILE   F CD1   1 
ATOM   13686 N  N     . GLU   E 4  331 ? 7.312   55.056  97.229  1.00 61.99  ? 331 GLU   F N     1 
ATOM   13687 C  CA    . GLU   E 4  331 ? 8.031   55.247  95.977  1.00 65.00  ? 331 GLU   F CA    1 
ATOM   13688 C  C     . GLU   E 4  331 ? 7.054   55.665  94.882  1.00 65.38  ? 331 GLU   F C     1 
ATOM   13689 O  O     . GLU   E 4  331 ? 5.834   55.474  94.986  1.00 55.44  ? 331 GLU   F O     1 
ATOM   13690 C  CB    . GLU   E 4  331 ? 8.821   53.979  95.548  1.00 57.09  ? 331 GLU   F CB    1 
ATOM   13691 C  CG    . GLU   E 4  331 ? 7.993   52.823  94.940  1.00 65.21  ? 331 GLU   F CG    1 
ATOM   13692 C  CD    . GLU   E 4  331 ? 8.858   51.661  94.400  1.00 87.44  ? 331 GLU   F CD    1 
ATOM   13693 O  OE1   . GLU   E 4  331 ? 10.055  51.894  94.110  1.00 81.91  ? 331 GLU   F OE1   1 
ATOM   13694 O  OE2   . GLU   E 4  331 ? 8.342   50.515  94.264  1.00 87.55  ? 331 GLU   F OE2   1 
ATOM   13695 N  N     . VAL   E 4  332 ? 7.618   56.268  93.833  1.00 61.32  ? 332 VAL   F N     1 
ATOM   13696 C  CA    . VAL   E 4  332 ? 6.916   56.514  92.580  1.00 51.15  ? 332 VAL   F CA    1 
ATOM   13697 C  C     . VAL   E 4  332 ? 7.637   55.732  91.492  1.00 47.69  ? 332 VAL   F C     1 
ATOM   13698 O  O     . VAL   E 4  332 ? 8.863   55.822  91.363  1.00 55.29  ? 332 VAL   F O     1 
ATOM   13699 C  CB    . VAL   E 4  332 ? 6.850   58.014  92.236  1.00 47.28  ? 332 VAL   F CB    1 
ATOM   13700 C  CG1   . VAL   E 4  332 ? 5.730   58.270  91.270  1.00 44.39  ? 332 VAL   F CG1   1 
ATOM   13701 C  CG2   . VAL   E 4  332 ? 6.666   58.831  93.493  1.00 51.19  ? 332 VAL   F CG2   1 
ATOM   13702 N  N     . ASN   E 4  333 ? 6.877   54.955  90.731  1.00 50.19  ? 333 ASN   F N     1 
ATOM   13703 C  CA    . ASN   E 4  333 ? 7.388   54.060  89.703  1.00 46.92  ? 333 ASN   F CA    1 
ATOM   13704 C  C     . ASN   E 4  333 ? 7.103   54.672  88.338  1.00 50.26  ? 333 ASN   F C     1 
ATOM   13705 O  O     . ASN   E 4  333 ? 5.938   54.932  88.002  1.00 42.39  ? 333 ASN   F O     1 
ATOM   13706 C  CB    . ASN   E 4  333 ? 6.734   52.681  89.822  1.00 57.46  ? 333 ASN   F CB    1 
ATOM   13707 C  CG    . ASN   E 4  333 ? 7.673   51.630  90.389  1.00 71.58  ? 333 ASN   F CG    1 
ATOM   13708 O  OD1   . ASN   E 4  333 ? 7.796   51.480  91.610  1.00 67.57  ? 333 ASN   F OD1   1 
ATOM   13709 N  ND2   . ASN   E 4  333 ? 8.336   50.885  89.499  1.00 72.90  ? 333 ASN   F ND2   1 
ATOM   13710 N  N     . GLY   E 4  334 ? 8.165   54.883  87.551  1.00 46.14  ? 334 GLY   F N     1 
ATOM   13711 C  CA    . GLY   E 4  334 ? 8.042   55.511  86.242  1.00 47.68  ? 334 GLY   F CA    1 
ATOM   13712 C  C     . GLY   E 4  334 ? 7.559   54.594  85.138  1.00 46.54  ? 334 GLY   F C     1 
ATOM   13713 O  O     . GLY   E 4  334 ? 7.007   55.078  84.142  1.00 39.47  ? 334 GLY   F O     1 
ATOM   13714 N  N     . ALA   E 4  335 ? 7.748   53.282  85.302  1.00 47.83  ? 335 ALA   F N     1 
ATOM   13715 C  CA    . ALA   E 4  335 ? 7.212   52.263  84.401  1.00 45.34  ? 335 ALA   F CA    1 
ATOM   13716 C  C     . ALA   E 4  335 ? 6.444   51.242  85.230  1.00 43.96  ? 335 ALA   F C     1 
ATOM   13717 O  O     . ALA   E 4  335 ? 6.938   50.139  85.480  1.00 47.11  ? 335 ALA   F O     1 
ATOM   13718 C  CB    . ALA   E 4  335 ? 8.326   51.588  83.598  1.00 39.66  ? 335 ALA   F CB    1 
ATOM   13719 N  N     . PRO   E 4  336 ? 5.238   51.579  85.683  1.00 46.64  ? 336 PRO   F N     1 
ATOM   13720 C  CA    . PRO   E 4  336 ? 4.429   50.596  86.420  1.00 52.76  ? 336 PRO   F CA    1 
ATOM   13721 C  C     . PRO   E 4  336 ? 4.002   49.432  85.547  1.00 48.54  ? 336 PRO   F C     1 
ATOM   13722 O  O     . PRO   E 4  336 ? 3.785   49.577  84.343  1.00 51.91  ? 336 PRO   F O     1 
ATOM   13723 C  CB    . PRO   E 4  336 ? 3.203   51.401  86.865  1.00 46.87  ? 336 PRO   F CB    1 
ATOM   13724 C  CG    . PRO   E 4  336 ? 3.133   52.545  85.892  1.00 48.80  ? 336 PRO   F CG    1 
ATOM   13725 C  CD    . PRO   E 4  336 ? 4.584   52.894  85.633  1.00 42.93  ? 336 PRO   F CD    1 
ATOM   13726 N  N     . ALA   E 4  337 ? 3.882   48.267  86.174  1.00 47.32  ? 337 ALA   F N     1 
ATOM   13727 C  CA    . ALA   E 4  337 ? 3.083   47.179  85.632  1.00 54.49  ? 337 ALA   F CA    1 
ATOM   13728 C  C     . ALA   E 4  337 ? 1.703   47.238  86.275  1.00 58.13  ? 337 ALA   F C     1 
ATOM   13729 O  O     . ALA   E 4  337 ? 1.500   47.918  87.287  1.00 57.79  ? 337 ALA   F O     1 
ATOM   13730 C  CB    . ALA   E 4  337 ? 3.740   45.820  85.881  1.00 42.67  ? 337 ALA   F CB    1 
ATOM   13731 N  N     . CYS   E 4  338 ? 0.742   46.539  85.677  1.00 52.92  ? 338 CYS   F N     1 
ATOM   13732 C  CA    . CYS   E 4  338 ? -0.607  46.597  86.221  1.00 54.85  ? 338 CYS   F CA    1 
ATOM   13733 C  C     . CYS   E 4  338 ? -0.826  45.430  87.185  1.00 62.06  ? 338 CYS   F C     1 
ATOM   13734 O  O     . CYS   E 4  338 ? 0.128   44.809  87.659  1.00 69.96  ? 338 CYS   F O     1 
ATOM   13735 C  CB    . CYS   E 4  338 ? -1.635  46.614  85.094  1.00 49.64  ? 338 CYS   F CB    1 
ATOM   13736 S  SG    . CYS   E 4  338 ? -3.216  47.271  85.656  1.00 64.49  ? 338 CYS   F SG    1 
ATOM   13737 N  N     . ALA   E 4  339 ? -2.080  45.153  87.519  1.00 63.91  ? 339 ALA   F N     1 
ATOM   13738 C  CA    . ALA   E 4  339 ? -2.482  43.902  88.142  1.00 57.62  ? 339 ALA   F CA    1 
ATOM   13739 C  C     . ALA   E 4  339 ? -3.325  43.131  87.138  1.00 68.20  ? 339 ALA   F C     1 
ATOM   13740 O  O     . ALA   E 4  339 ? -4.133  43.723  86.415  1.00 68.09  ? 339 ALA   F O     1 
ATOM   13741 C  CB    . ALA   E 4  339 ? -3.265  44.145  89.428  1.00 57.74  ? 339 ALA   F CB    1 
ATOM   13742 N  N     . GLN   E 4  340 ? -3.127  41.813  87.079  1.00 64.33  ? 340 GLN   F N     1 
ATOM   13743 C  CA    . GLN   E 4  340 ? -3.707  41.051  85.983  1.00 58.29  ? 340 GLN   F CA    1 
ATOM   13744 C  C     . GLN   E 4  340 ? -5.193  41.348  85.816  1.00 61.39  ? 340 GLN   F C     1 
ATOM   13745 O  O     . GLN   E 4  340 ? -5.675  41.517  84.692  1.00 59.51  ? 340 GLN   F O     1 
ATOM   13746 C  CB    . GLN   E 4  340 ? -3.469  39.557  86.197  1.00 67.88  ? 340 GLN   F CB    1 
ATOM   13747 C  CG    . GLN   E 4  340 ? -3.209  38.776  84.907  1.00 63.68  ? 340 GLN   F CG    1 
ATOM   13748 C  CD    . GLN   E 4  340 ? -4.419  38.741  83.979  1.00 85.06  ? 340 GLN   F CD    1 
ATOM   13749 O  OE1   . GLN   E 4  340 ? -5.530  38.406  84.399  1.00 88.65  ? 340 GLN   F OE1   1 
ATOM   13750 N  NE2   . GLN   E 4  340 ? -4.206  39.089  82.711  1.00 76.93  ? 340 GLN   F NE2   1 
ATOM   13751 N  N     . LYS   E 4  341 ? -5.934  41.442  86.922  1.00 71.00  ? 341 LYS   F N     1 
ATOM   13752 C  CA    . LYS   E 4  341 ? -7.375  41.663  86.812  1.00 66.16  ? 341 LYS   F CA    1 
ATOM   13753 C  C     . LYS   E 4  341 ? -7.705  42.933  86.030  1.00 62.40  ? 341 LYS   F C     1 
ATOM   13754 O  O     . LYS   E 4  341 ? -8.729  42.980  85.337  1.00 67.67  ? 341 LYS   F O     1 
ATOM   13755 C  CB    . LYS   E 4  341 ? -8.014  41.725  88.204  1.00 70.52  ? 341 LYS   F CB    1 
ATOM   13756 C  CG    . LYS   E 4  341 ? -9.557  41.770  88.181  1.00 78.05  ? 341 LYS   F CG    1 
ATOM   13757 C  CD    . LYS   E 4  341 ? -10.163 42.306  89.497  1.00 74.64  ? 341 LYS   F CD    1 
ATOM   13758 C  CE    . LYS   E 4  341 ? -11.701 42.350  89.445  1.00 71.59  ? 341 LYS   F CE    1 
ATOM   13759 N  NZ    . LYS   E 4  341 ? -12.273 43.577  90.088  1.00 60.79  ? 341 LYS   F NZ    1 
ATOM   13760 N  N     . LEU   E 4  342 ? -6.841  43.960  86.107  1.00 70.74  ? 342 LEU   F N     1 
ATOM   13761 C  CA    . LEU   E 4  342 ? -7.172  45.320  85.680  1.00 66.54  ? 342 LEU   F CA    1 
ATOM   13762 C  C     . LEU   E 4  342 ? -6.513  45.767  84.378  1.00 65.81  ? 342 LEU   F C     1 
ATOM   13763 O  O     . LEU   E 4  342 ? -6.824  46.870  83.906  1.00 58.85  ? 342 LEU   F O     1 
ATOM   13764 C  CB    . LEU   E 4  342 ? -6.802  46.323  86.786  1.00 54.69  ? 342 LEU   F CB    1 
ATOM   13765 C  CG    . LEU   E 4  342 ? -7.534  46.171  88.126  1.00 54.31  ? 342 LEU   F CG    1 
ATOM   13766 C  CD1   . LEU   E 4  342 ? -6.838  46.928  89.230  1.00 43.77  ? 342 LEU   F CD1   1 
ATOM   13767 C  CD2   . LEU   E 4  342 ? -8.969  46.640  88.004  1.00 58.79  ? 342 LEU   F CD2   1 
ATOM   13768 N  N     . TYR   E 4  343 ? -5.617  44.958  83.791  1.00 67.81  ? 343 TYR   F N     1 
ATOM   13769 C  CA    . TYR   E 4  343 ? -4.967  45.319  82.528  1.00 57.39  ? 343 TYR   F CA    1 
ATOM   13770 C  C     . TYR   E 4  343 ? -5.976  45.784  81.490  1.00 59.20  ? 343 TYR   F C     1 
ATOM   13771 O  O     . TYR   E 4  343 ? -5.802  46.836  80.866  1.00 62.43  ? 343 TYR   F O     1 
ATOM   13772 C  CB    . TYR   E 4  343 ? -4.178  44.136  81.970  1.00 48.25  ? 343 TYR   F CB    1 
ATOM   13773 C  CG    . TYR   E 4  343 ? -2.734  44.120  82.377  1.00 59.27  ? 343 TYR   F CG    1 
ATOM   13774 C  CD1   . TYR   E 4  343 ? -1.782  44.820  81.653  1.00 64.33  ? 343 TYR   F CD1   1 
ATOM   13775 C  CD2   . TYR   E 4  343 ? -2.316  43.403  83.487  1.00 62.88  ? 343 TYR   F CD2   1 
ATOM   13776 C  CE1   . TYR   E 4  343 ? -0.443  44.807  82.030  1.00 58.30  ? 343 TYR   F CE1   1 
ATOM   13777 C  CE2   . TYR   E 4  343 ? -0.989  43.378  83.866  1.00 61.76  ? 343 TYR   F CE2   1 
ATOM   13778 C  CZ    . TYR   E 4  343 ? -0.056  44.080  83.136  1.00 58.59  ? 343 TYR   F CZ    1 
ATOM   13779 O  OH    . TYR   E 4  343 ? 1.264   44.056  83.526  1.00 66.49  ? 343 TYR   F OH    1 
ATOM   13780 N  N     . ALA   E 4  344 ? -7.028  44.994  81.273  1.00 60.47  ? 344 ALA   F N     1 
ATOM   13781 C  CA    . ALA   E 4  344 ? -8.020  45.335  80.260  1.00 57.48  ? 344 ALA   F CA    1 
ATOM   13782 C  C     . ALA   E 4  344 ? -8.434  46.797  80.367  1.00 62.67  ? 344 ALA   F C     1 
ATOM   13783 O  O     . ALA   E 4  344 ? -8.382  47.548  79.384  1.00 55.27  ? 344 ALA   F O     1 
ATOM   13784 C  CB    . ALA   E 4  344 ? -9.245  44.423  80.395  1.00 47.39  ? 344 ALA   F CB    1 
ATOM   13785 N  N     . GLU   E 4  345 ? -8.817  47.222  81.574  1.00 65.43  ? 345 GLU   F N     1 
ATOM   13786 C  CA    . GLU   E 4  345 ? -9.496  48.501  81.750  1.00 61.59  ? 345 GLU   F CA    1 
ATOM   13787 C  C     . GLU   E 4  345 ? -8.520  49.670  81.743  1.00 63.14  ? 345 GLU   F C     1 
ATOM   13788 O  O     . GLU   E 4  345 ? -8.778  50.694  81.101  1.00 57.05  ? 345 GLU   F O     1 
ATOM   13789 C  CB    . GLU   E 4  345 ? -10.299 48.494  83.051  1.00 60.59  ? 345 GLU   F CB    1 
ATOM   13790 C  CG    . GLU   E 4  345 ? -11.711 48.998  82.891  1.00 63.68  ? 345 GLU   F CG    1 
ATOM   13791 C  CD    . GLU   E 4  345 ? -12.238 49.618  84.156  1.00 63.25  ? 345 GLU   F CD    1 
ATOM   13792 O  OE1   . GLU   E 4  345 ? -11.467 49.723  85.134  1.00 64.30  ? 345 GLU   F OE1   1 
ATOM   13793 O  OE2   . GLU   E 4  345 ? -13.422 50.007  84.168  1.00 61.41  ? 345 GLU   F OE2   1 
ATOM   13794 N  N     . LEU   E 4  346 ? -7.408  49.552  82.474  1.00 65.64  ? 346 LEU   F N     1 
ATOM   13795 C  CA    . LEU   E 4  346 ? -6.430  50.634  82.466  1.00 62.53  ? 346 LEU   F CA    1 
ATOM   13796 C  C     . LEU   E 4  346 ? -5.848  50.834  81.070  1.00 60.30  ? 346 LEU   F C     1 
ATOM   13797 O  O     . LEU   E 4  346 ? -5.595  51.969  80.651  1.00 57.79  ? 346 LEU   F O     1 
ATOM   13798 C  CB    . LEU   E 4  346 ? -5.320  50.360  83.480  1.00 55.04  ? 346 LEU   F CB    1 
ATOM   13799 C  CG    . LEU   E 4  346 ? -4.317  51.505  83.563  1.00 46.57  ? 346 LEU   F CG    1 
ATOM   13800 C  CD1   . LEU   E 4  346 ? -5.053  52.803  83.802  1.00 49.66  ? 346 LEU   F CD1   1 
ATOM   13801 C  CD2   . LEU   E 4  346 ? -3.285  51.278  84.650  1.00 49.44  ? 346 LEU   F CD2   1 
ATOM   13802 N  N     . CYS   E 4  347 ? -5.657  49.745  80.323  1.00 54.44  ? 347 CYS   F N     1 
ATOM   13803 C  CA    . CYS   E 4  347 ? -5.025  49.852  79.019  1.00 50.14  ? 347 CYS   F CA    1 
ATOM   13804 C  C     . CYS   E 4  347 ? -5.963  50.398  77.950  1.00 56.76  ? 347 CYS   F C     1 
ATOM   13805 O  O     . CYS   E 4  347 ? -5.486  50.956  76.957  1.00 66.72  ? 347 CYS   F O     1 
ATOM   13806 C  CB    . CYS   E 4  347 ? -4.455  48.498  78.604  1.00 53.36  ? 347 CYS   F CB    1 
ATOM   13807 S  SG    . CYS   E 4  347 ? -2.861  48.101  79.416  1.00 50.37  ? 347 CYS   F SG    1 
ATOM   13808 N  N     . GLN   E 4  348 ? -7.277  50.272  78.118  1.00 54.26  ? 348 GLN   F N     1 
ATOM   13809 C  CA    . GLN   E 4  348 ? -8.163  50.977  77.200  1.00 53.38  ? 348 GLN   F CA    1 
ATOM   13810 C  C     . GLN   E 4  348 ? -8.311  52.437  77.585  1.00 56.22  ? 348 GLN   F C     1 
ATOM   13811 O  O     . GLN   E 4  348 ? -8.556  53.282  76.716  1.00 57.25  ? 348 GLN   F O     1 
ATOM   13812 C  CB    . GLN   E 4  348 ? -9.547  50.335  77.155  1.00 51.86  ? 348 GLN   F CB    1 
ATOM   13813 C  CG    . GLN   E 4  348 ? -10.473 51.024  76.163  1.00 50.82  ? 348 GLN   F CG    1 
ATOM   13814 C  CD    . GLN   E 4  348 ? -10.099 50.714  74.721  1.00 60.07  ? 348 GLN   F CD    1 
ATOM   13815 O  OE1   . GLN   E 4  348 ? -9.438  49.708  74.444  1.00 49.76  ? 348 GLN   F OE1   1 
ATOM   13816 N  NE2   . GLN   E 4  348 ? -10.518 51.578  73.794  1.00 57.12  ? 348 GLN   F NE2   1 
ATOM   13817 N  N     . GLY   E 4  349 ? -8.185  52.742  78.877  1.00 53.28  ? 349 GLY   F N     1 
ATOM   13818 C  CA    . GLY   E 4  349 ? -8.221  54.126  79.309  1.00 53.77  ? 349 GLY   F CA    1 
ATOM   13819 C  C     . GLY   E 4  349 ? -7.020  54.904  78.815  1.00 63.41  ? 349 GLY   F C     1 
ATOM   13820 O  O     . GLY   E 4  349 ? -7.161  56.029  78.323  1.00 65.85  ? 349 GLY   F O     1 
ATOM   13821 N  N     . ILE   E 4  350 ? -5.822  54.314  78.926  1.00 60.48  ? 350 ILE   F N     1 
ATOM   13822 C  CA    . ILE   E 4  350 ? -4.625  54.940  78.363  1.00 57.33  ? 350 ILE   F CA    1 
ATOM   13823 C  C     . ILE   E 4  350 ? -4.864  55.297  76.902  1.00 46.92  ? 350 ILE   F C     1 
ATOM   13824 O  O     . ILE   E 4  350 ? -4.585  56.418  76.465  1.00 45.03  ? 350 ILE   F O     1 
ATOM   13825 C  CB    . ILE   E 4  350 ? -3.398  54.019  78.536  1.00 54.36  ? 350 ILE   F CB    1 
ATOM   13826 C  CG1   . ILE   E 4  350 ? -3.176  53.700  80.019  1.00 48.93  ? 350 ILE   F CG1   1 
ATOM   13827 C  CG2   . ILE   E 4  350 ? -2.154  54.659  77.942  1.00 49.81  ? 350 ILE   F CG2   1 
ATOM   13828 C  CD1   . ILE   E 4  350 ? -2.009  52.773  80.321  1.00 37.70  ? 350 ILE   F CD1   1 
ATOM   13829 N  N     . VAL   E 4  351 ? -5.422  54.355  76.135  1.00 53.97  ? 351 VAL   F N     1 
ATOM   13830 C  CA    . VAL   E 4  351 ? -5.646  54.575  74.707  1.00 50.10  ? 351 VAL   F CA    1 
ATOM   13831 C  C     . VAL   E 4  351 ? -6.617  55.723  74.479  1.00 59.13  ? 351 VAL   F C     1 
ATOM   13832 O  O     . VAL   E 4  351 ? -6.486  56.484  73.513  1.00 53.58  ? 351 VAL   F O     1 
ATOM   13833 C  CB    . VAL   E 4  351 ? -6.160  53.293  74.040  1.00 53.68  ? 351 VAL   F CB    1 
ATOM   13834 C  CG1   . VAL   E 4  351 ? -6.670  53.634  72.646  1.00 48.25  ? 351 VAL   F CG1   1 
ATOM   13835 C  CG2   . VAL   E 4  351 ? -5.061  52.238  73.991  1.00 59.21  ? 351 VAL   F CG2   1 
ATOM   13836 N  N     . ASP   E 4  352 ? -7.622  55.851  75.347  1.00 60.23  ? 352 ASP   F N     1 
ATOM   13837 C  CA    . ASP   E 4  352 ? -8.665  56.850  75.162  1.00 53.93  ? 352 ASP   F CA    1 
ATOM   13838 C  C     . ASP   E 4  352 ? -8.274  58.206  75.726  1.00 52.04  ? 352 ASP   F C     1 
ATOM   13839 O  O     . ASP   E 4  352 ? -8.444  59.233  75.065  1.00 64.70  ? 352 ASP   F O     1 
ATOM   13840 C  CB    . ASP   E 4  352 ? -9.967  56.365  75.798  1.00 59.72  ? 352 ASP   F CB    1 
ATOM   13841 C  CG    . ASP   E 4  352 ? -10.608 55.243  75.005  1.00 69.97  ? 352 ASP   F CG    1 
ATOM   13842 O  OD1   . ASP   E 4  352 ? -10.593 55.335  73.751  1.00 72.48  ? 352 ASP   F OD1   1 
ATOM   13843 O  OD2   . ASP   E 4  352 ? -11.103 54.271  75.626  1.00 61.35  ? 352 ASP   F OD2   1 
ATOM   13844 N  N     . VAL   E 4  353 ? -7.737  58.227  76.937  1.00 49.50  ? 353 VAL   F N     1 
ATOM   13845 C  CA    A VAL   E 4  353 ? -7.347  59.491  77.548  0.80 52.07  ? 353 VAL   F CA    1 
ATOM   13846 C  CA    B VAL   E 4  353 ? -7.346  59.492  77.549  0.20 52.09  ? 353 VAL   F CA    1 
ATOM   13847 C  C     . VAL   E 4  353 ? -6.094  60.055  76.881  1.00 54.71  ? 353 VAL   F C     1 
ATOM   13848 O  O     . VAL   E 4  353 ? -6.031  61.247  76.554  1.00 47.65  ? 353 VAL   F O     1 
ATOM   13849 C  CB    A VAL   E 4  353 ? -7.142  59.302  79.058  0.80 51.61  ? 353 VAL   F CB    1 
ATOM   13850 C  CB    B VAL   E 4  353 ? -7.141  59.307  79.062  0.20 51.64  ? 353 VAL   F CB    1 
ATOM   13851 C  CG1   A VAL   E 4  353 ? -6.792  60.622  79.705  0.80 53.26  ? 353 VAL   F CG1   1 
ATOM   13852 C  CG1   B VAL   E 4  353 ? -6.653  60.598  79.685  0.20 53.21  ? 353 VAL   F CG1   1 
ATOM   13853 C  CG2   A VAL   E 4  353 ? -8.382  58.703  79.670  0.80 55.14  ? 353 VAL   F CG2   1 
ATOM   13854 C  CG2   B VAL   E 4  353 ? -8.432  58.847  79.713  0.20 55.01  ? 353 VAL   F CG2   1 
ATOM   13855 N  N     . ALA   E 4  354 ? -5.077  59.205  76.662  1.00 42.73  ? 354 ALA   F N     1 
ATOM   13856 C  CA    . ALA   E 4  354 ? -3.734  59.670  76.315  1.00 45.83  ? 354 ALA   F CA    1 
ATOM   13857 C  C     . ALA   E 4  354 ? -3.362  59.596  74.833  1.00 49.42  ? 354 ALA   F C     1 
ATOM   13858 O  O     . ALA   E 4  354 ? -2.497  60.360  74.394  1.00 45.38  ? 354 ALA   F O     1 
ATOM   13859 C  CB    . ALA   E 4  354 ? -2.688  58.882  77.112  1.00 48.72  ? 354 ALA   F CB    1 
ATOM   13860 N  N     . ILE   E 4  355 ? -3.947  58.702  74.045  1.00 46.32  ? 355 ILE   F N     1 
ATOM   13861 C  CA    . ILE   E 4  355 ? -3.533  58.491  72.664  1.00 47.56  ? 355 ILE   F CA    1 
ATOM   13862 C  C     . ILE   E 4  355 ? -4.611  58.938  71.676  1.00 52.54  ? 355 ILE   F C     1 
ATOM   13863 O  O     . ILE   E 4  355 ? -4.327  59.665  70.720  1.00 50.45  ? 355 ILE   F O     1 
ATOM   13864 C  CB    . ILE   E 4  355 ? -3.126  57.017  72.433  1.00 44.64  ? 355 ILE   F CB    1 
ATOM   13865 C  CG1   . ILE   E 4  355 ? -1.857  56.712  73.225  1.00 40.04  ? 355 ILE   F CG1   1 
ATOM   13866 C  CG2   . ILE   E 4  355 ? -2.899  56.736  70.961  1.00 46.62  ? 355 ILE   F CG2   1 
ATOM   13867 C  CD1   . ILE   E 4  355 ? -1.586  55.255  73.428  1.00 44.85  ? 355 ILE   F CD1   1 
ATOM   13868 N  N     . SER   E 4  356 ? -5.863  58.527  71.900  1.00 60.06  ? 356 SER   F N     1 
ATOM   13869 C  CA    . SER   E 4  356 ? -6.950  58.950  71.018  1.00 59.72  ? 356 SER   F CA    1 
ATOM   13870 C  C     . SER   E 4  356 ? -7.315  60.416  71.209  1.00 52.95  ? 356 SER   F C     1 
ATOM   13871 O  O     . SER   E 4  356 ? -7.924  61.017  70.319  1.00 49.59  ? 356 SER   F O     1 
ATOM   13872 C  CB    . SER   E 4  356 ? -8.179  58.065  71.233  1.00 52.01  ? 356 SER   F CB    1 
ATOM   13873 O  OG    . SER   E 4  356 ? -8.129  56.940  70.372  1.00 58.14  ? 356 SER   F OG    1 
ATOM   13874 N  N     . SER   E 4  357 ? -6.949  61.004  72.344  1.00 55.41  ? 357 SER   F N     1 
ATOM   13875 C  CA    . SER   E 4  357 ? -7.177  62.423  72.560  1.00 45.98  ? 357 SER   F CA    1 
ATOM   13876 C  C     . SER   E 4  357 ? -6.305  63.293  71.675  1.00 49.11  ? 357 SER   F C     1 
ATOM   13877 O  O     . SER   E 4  357 ? -6.617  64.470  71.487  1.00 53.75  ? 357 SER   F O     1 
ATOM   13878 C  CB    . SER   E 4  357 ? -6.891  62.768  74.012  1.00 54.07  ? 357 SER   F CB    1 
ATOM   13879 O  OG    . SER   E 4  357 ? -5.535  62.481  74.310  1.00 56.72  ? 357 SER   F OG    1 
ATOM   13880 N  N     . VAL   E 4  358 ? -5.183  62.762  71.207  1.00 48.88  ? 358 VAL   F N     1 
ATOM   13881 C  CA    . VAL   E 4  358 ? -4.253  63.502  70.382  1.00 50.48  ? 358 VAL   F CA    1 
ATOM   13882 C  C     . VAL   E 4  358 ? -4.315  63.066  68.940  1.00 50.20  ? 358 VAL   F C     1 
ATOM   13883 O  O     . VAL   E 4  358 ? -4.128  63.898  68.045  1.00 48.64  ? 358 VAL   F O     1 
ATOM   13884 C  CB    . VAL   E 4  358 ? -2.806  63.357  70.923  1.00 38.78  ? 358 VAL   F CB    1 
ATOM   13885 C  CG1   . VAL   E 4  358 ? -1.805  63.526  69.810  1.00 26.88  ? 358 VAL   F CG1   1 
ATOM   13886 C  CG2   . VAL   E 4  358 ? -2.514  64.370  71.993  1.00 43.41  ? 358 VAL   F CG2   1 
ATOM   13887 N  N     . PHE   E 4  359 ? -4.622  61.805  68.702  1.00 56.69  ? 359 PHE   F N     1 
ATOM   13888 C  CA    . PHE   E 4  359 ? -4.903  61.278  67.380  1.00 56.90  ? 359 PHE   F CA    1 
ATOM   13889 C  C     . PHE   E 4  359 ? -6.277  60.631  67.463  1.00 58.26  ? 359 PHE   F C     1 
ATOM   13890 O  O     . PHE   E 4  359 ? -6.401  59.446  67.823  1.00 61.44  ? 359 PHE   F O     1 
ATOM   13891 C  CB    . PHE   E 4  359 ? -3.822  60.301  66.948  1.00 45.17  ? 359 PHE   F CB    1 
ATOM   13892 C  CG    . PHE   E 4  359 ? -2.447  60.727  67.329  1.00 40.75  ? 359 PHE   F CG    1 
ATOM   13893 C  CD1   . PHE   E 4  359 ? -1.735  61.601  66.533  1.00 38.75  ? 359 PHE   F CD1   1 
ATOM   13894 C  CD2   . PHE   E 4  359 ? -1.860  60.249  68.490  1.00 41.16  ? 359 PHE   F CD2   1 
ATOM   13895 C  CE1   . PHE   E 4  359 ? -0.453  61.983  66.881  1.00 35.85  ? 359 PHE   F CE1   1 
ATOM   13896 C  CE2   . PHE   E 4  359 ? -0.569  60.617  68.846  1.00 34.50  ? 359 PHE   F CE2   1 
ATOM   13897 C  CZ    . PHE   E 4  359 ? 0.133   61.488  68.045  1.00 40.83  ? 359 PHE   F CZ    1 
ATOM   13898 N  N     . PRO   E 4  360 ? -7.335  61.381  67.149  1.00 52.36  ? 360 PRO   F N     1 
ATOM   13899 C  CA    . PRO   E 4  360 ? -8.691  60.843  67.266  1.00 48.27  ? 360 PRO   F CA    1 
ATOM   13900 C  C     . PRO   E 4  360 ? -9.036  59.867  66.154  1.00 57.73  ? 360 PRO   F C     1 
ATOM   13901 O  O     . PRO   E 4  360 ? -8.482  59.908  65.050  1.00 61.95  ? 360 PRO   F O     1 
ATOM   13902 C  CB    . PRO   E 4  360 ? -9.571  62.095  67.210  1.00 45.70  ? 360 PRO   F CB    1 
ATOM   13903 C  CG    . PRO   E 4  360 ? -8.776  63.071  66.494  1.00 57.50  ? 360 PRO   F CG    1 
ATOM   13904 C  CD    . PRO   E 4  360 ? -7.339  62.811  66.819  1.00 57.12  ? 360 PRO   F CD    1 
ATOM   13905 N  N     . LEU   E 4  361 ? -9.973  58.980  66.471  1.00 65.93  ? 361 LEU   F N     1 
ATOM   13906 C  CA    . LEU   E 4  361 ? -10.404 57.899  65.604  1.00 68.47  ? 361 LEU   F CA    1 
ATOM   13907 C  C     . LEU   E 4  361 ? -11.558 58.334  64.701  1.00 78.44  ? 361 LEU   F C     1 
ATOM   13908 O  O     . LEU   E 4  361 ? -12.119 59.427  64.832  1.00 60.64  ? 361 LEU   F O     1 
ATOM   13909 C  CB    . LEU   E 4  361 ? -10.805 56.698  66.452  1.00 55.34  ? 361 LEU   F CB    1 
ATOM   13910 C  CG    . LEU   E 4  361 ? -9.594  56.171  67.206  1.00 64.31  ? 361 LEU   F CG    1 
ATOM   13911 C  CD1   . LEU   E 4  361 ? -9.960  54.995  68.078  1.00 48.04  ? 361 LEU   F CD1   1 
ATOM   13912 C  CD2   . LEU   E 4  361 ? -8.508  55.795  66.196  1.00 72.18  ? 361 LEU   F CD2   1 
ATOM   13913 N  N     . ALA   E 4  362 ? -11.909 57.450  63.769  1.00 87.98  ? 362 ALA   F N     1 
ATOM   13914 C  CA    . ALA   E 4  362 ? -12.997 57.698  62.830  1.00 83.75  ? 362 ALA   F CA    1 
ATOM   13915 C  C     . ALA   E 4  362 ? -14.348 57.317  63.445  1.00 86.52  ? 362 ALA   F C     1 
ATOM   13916 O  O     . ALA   E 4  362 ? -15.360 58.004  63.247  1.00 99.58  ? 362 ALA   F O     1 
ATOM   13917 C  CB    . ALA   E 4  362 ? -12.758 56.932  61.536  1.00 64.73  ? 362 ALA   F CB    1 
ATOM   13918 N  N     . THR   E 4  372 ? -18.887 57.012  82.701  1.00 84.61  ? 372 THR   F N     1 
ATOM   13919 C  CA    . THR   E 4  372 ? -18.349 56.656  81.393  1.00 93.60  ? 372 THR   F CA    1 
ATOM   13920 C  C     . THR   E 4  372 ? -16.837 56.929  81.317  1.00 109.25 ? 372 THR   F C     1 
ATOM   13921 O  O     . THR   E 4  372 ? -16.263 56.988  80.224  1.00 100.51 ? 372 THR   F O     1 
ATOM   13922 C  CB    . THR   E 4  372 ? -19.065 57.425  80.255  1.00 100.68 ? 372 THR   F CB    1 
ATOM   13923 O  OG1   . THR   E 4  372 ? -20.387 57.781  80.674  1.00 112.93 ? 372 THR   F OG1   1 
ATOM   13924 C  CG2   . THR   E 4  372 ? -19.163 56.566  78.995  1.00 91.23  ? 372 THR   F CG2   1 
ATOM   13925 N  N     . SER   E 4  373 ? -16.196 57.099  82.478  1.00 108.56 ? 373 SER   F N     1 
ATOM   13926 C  CA    . SER   E 4  373 ? -14.745 57.258  82.557  1.00 88.99  ? 373 SER   F CA    1 
ATOM   13927 C  C     . SER   E 4  373 ? -14.206 56.493  83.755  1.00 82.68  ? 373 SER   F C     1 
ATOM   13928 O  O     . SER   E 4  373 ? -14.751 56.591  84.859  1.00 78.15  ? 373 SER   F O     1 
ATOM   13929 C  CB    . SER   E 4  373 ? -14.334 58.731  82.657  1.00 85.92  ? 373 SER   F CB    1 
ATOM   13930 O  OG    . SER   E 4  373 ? -14.183 59.297  81.367  1.00 100.37 ? 373 SER   F OG    1 
ATOM   13931 N  N     . ILE   E 4  374 ? -13.124 55.740  83.524  1.00 71.41  ? 374 ILE   F N     1 
ATOM   13932 C  CA    . ILE   E 4  374 ? -12.492 54.932  84.565  1.00 63.41  ? 374 ILE   F CA    1 
ATOM   13933 C  C     . ILE   E 4  374 ? -11.571 55.733  85.468  1.00 60.40  ? 374 ILE   F C     1 
ATOM   13934 O  O     . ILE   E 4  374 ? -10.996 55.163  86.403  1.00 59.57  ? 374 ILE   F O     1 
ATOM   13935 C  CB    . ILE   E 4  374 ? -11.656 53.802  83.936  1.00 64.00  ? 374 ILE   F CB    1 
ATOM   13936 C  CG1   . ILE   E 4  374 ? -10.518 54.411  83.113  1.00 59.05  ? 374 ILE   F CG1   1 
ATOM   13937 C  CG2   . ILE   E 4  374 ? -12.522 52.910  83.059  1.00 66.28  ? 374 ILE   F CG2   1 
ATOM   13938 C  CD1   . ILE   E 4  374 ? -9.477  53.419  82.647  1.00 53.15  ? 374 ILE   F CD1   1 
ATOM   13939 N  N     . PHE   E 4  375 ? -11.392 57.024  85.203  1.00 59.85  ? 375 PHE   F N     1 
ATOM   13940 C  CA    . PHE   E 4  375 ? -10.384 57.848  85.853  1.00 60.98  ? 375 PHE   F CA    1 
ATOM   13941 C  C     . PHE   E 4  375 ? -11.035 58.908  86.728  1.00 62.13  ? 375 PHE   F C     1 
ATOM   13942 O  O     . PHE   E 4  375 ? -12.206 59.259  86.556  1.00 68.07  ? 375 PHE   F O     1 
ATOM   13943 C  CB    . PHE   E 4  375 ? -9.478  58.548  84.822  1.00 58.27  ? 375 PHE   F CB    1 
ATOM   13944 C  CG    . PHE   E 4  375 ? -8.487  57.640  84.156  1.00 45.26  ? 375 PHE   F CG    1 
ATOM   13945 C  CD1   . PHE   E 4  375 ? -7.513  57.002  84.892  1.00 49.78  ? 375 PHE   F CD1   1 
ATOM   13946 C  CD2   . PHE   E 4  375 ? -8.520  57.446  82.796  1.00 45.39  ? 375 PHE   F CD2   1 
ATOM   13947 C  CE1   . PHE   E 4  375 ? -6.609  56.169  84.283  1.00 48.28  ? 375 PHE   F CE1   1 
ATOM   13948 C  CE2   . PHE   E 4  375 ? -7.614  56.612  82.181  1.00 53.70  ? 375 PHE   F CE2   1 
ATOM   13949 C  CZ    . PHE   E 4  375 ? -6.657  55.974  82.930  1.00 52.64  ? 375 PHE   F CZ    1 
ATOM   13950 N  N     . ILE   E 4  376 ? -10.239 59.434  87.658  1.00 56.00  ? 376 ILE   F N     1 
ATOM   13951 C  CA    . ILE   E 4  376 ? -10.611 60.585  88.473  1.00 51.02  ? 376 ILE   F CA    1 
ATOM   13952 C  C     . ILE   E 4  376 ? -9.585  61.677  88.180  1.00 54.41  ? 376 ILE   F C     1 
ATOM   13953 O  O     . ILE   E 4  376 ? -8.440  61.616  88.648  1.00 51.04  ? 376 ILE   F O     1 
ATOM   13954 C  CB    . ILE   E 4  376 ? -10.658 60.248  89.964  1.00 46.89  ? 376 ILE   F CB    1 
ATOM   13955 C  CG1   . ILE   E 4  376 ? -11.613 59.079  90.213  1.00 61.00  ? 376 ILE   F CG1   1 
ATOM   13956 C  CG2   . ILE   E 4  376 ? -11.030 61.484  90.784  1.00 38.27  ? 376 ILE   F CG2   1 
ATOM   13957 C  CD1   . ILE   E 4  376 ? -13.066 59.363  89.830  1.00 72.61  ? 376 ILE   F CD1   1 
ATOM   13958 N  N     . LYS   E 4  377 ? -9.986  62.686  87.407  1.00 50.71  ? 377 LYS   F N     1 
ATOM   13959 C  CA    . LYS   E 4  377 ? -9.106  63.816  87.126  1.00 53.89  ? 377 LYS   F CA    1 
ATOM   13960 C  C     . LYS   E 4  377 ? -8.843  64.594  88.418  1.00 42.45  ? 377 LYS   F C     1 
ATOM   13961 O  O     . LYS   E 4  377 ? -9.771  65.128  89.032  1.00 42.10  ? 377 LYS   F O     1 
ATOM   13962 C  CB    . LYS   E 4  377 ? -9.732  64.709  86.049  1.00 43.97  ? 377 LYS   F CB    1 
ATOM   13963 C  CG    . LYS   E 4  377 ? -9.043  66.061  85.851  1.00 53.83  ? 377 LYS   F CG    1 
ATOM   13964 C  CD    . LYS   E 4  377 ? -9.777  66.982  84.855  1.00 62.98  ? 377 LYS   F CD    1 
ATOM   13965 C  CE    . LYS   E 4  377 ? -9.352  66.748  83.395  1.00 63.48  ? 377 LYS   F CE    1 
ATOM   13966 N  NZ    . LYS   E 4  377 ? -9.977  67.707  82.418  1.00 66.66  ? 377 LYS   F NZ    1 
ATOM   13967 N  N     . LEU   E 4  378 ? -7.587  64.656  88.839  1.00 32.35  ? 378 LEU   F N     1 
ATOM   13968 C  CA    . LEU   E 4  378 ? -7.232  65.402  90.048  1.00 45.81  ? 378 LEU   F CA    1 
ATOM   13969 C  C     . LEU   E 4  378 ? -7.122  66.896  89.719  1.00 54.73  ? 378 LEU   F C     1 
ATOM   13970 O  O     . LEU   E 4  378 ? -6.077  67.371  89.268  1.00 55.78  ? 378 LEU   F O     1 
ATOM   13971 C  CB    . LEU   E 4  378 ? -5.943  64.846  90.642  1.00 41.25  ? 378 LEU   F CB    1 
ATOM   13972 C  CG    . LEU   E 4  378 ? -5.951  63.378  91.095  1.00 41.80  ? 378 LEU   F CG    1 
ATOM   13973 C  CD1   . LEU   E 4  378 ? -4.792  63.060  92.058  1.00 42.72  ? 378 LEU   F CD1   1 
ATOM   13974 C  CD2   . LEU   E 4  378 ? -7.272  62.995  91.724  1.00 36.62  ? 378 LEU   F CD2   1 
ATOM   13975 N  N     . HIS   E 4  379 ? -8.200  67.652  89.977  1.00 65.49  ? 379 HIS   F N     1 
ATOM   13976 C  CA    . HIS   E 4  379 ? -8.364  69.020  89.469  1.00 60.39  ? 379 HIS   F CA    1 
ATOM   13977 C  C     . HIS   E 4  379 ? -7.449  69.994  90.199  1.00 80.44  ? 379 HIS   F C     1 
ATOM   13978 O  O     . HIS   E 4  379 ? -7.703  70.349  91.358  1.00 73.87  ? 379 HIS   F O     1 
ATOM   13979 C  CB    . HIS   E 4  379 ? -9.812  69.484  89.599  1.00 52.57  ? 379 HIS   F CB    1 
ATOM   13980 C  CG    . HIS   E 4  379 ? -10.708 68.986  88.511  1.00 61.98  ? 379 HIS   F CG    1 
ATOM   13981 N  ND1   . HIS   E 4  379 ? -11.918 68.373  88.764  1.00 70.59  ? 379 HIS   F ND1   1 
ATOM   13982 C  CD2   . HIS   E 4  379 ? -10.574 69.008  87.164  1.00 77.87  ? 379 HIS   F CD2   1 
ATOM   13983 C  CE1   . HIS   E 4  379 ? -12.487 68.034  87.621  1.00 74.19  ? 379 HIS   F CE1   1 
ATOM   13984 N  NE2   . HIS   E 4  379 ? -11.695 68.413  86.634  1.00 85.95  ? 379 HIS   F NE2   1 
ATOM   13985 N  N     . HIS   E 4  380 ? -6.418  70.461  89.489  1.00 91.66  ? 380 HIS   F N     1 
ATOM   13986 C  CA    . HIS   E 4  380 ? -5.524  71.532  89.931  1.00 80.03  ? 380 HIS   F CA    1 
ATOM   13987 C  C     . HIS   E 4  380 ? -5.678  72.772  89.033  1.00 90.94  ? 380 HIS   F C     1 
ATOM   13988 O  O     . HIS   E 4  380 ? -5.609  73.922  89.489  1.00 82.66  ? 380 HIS   F O     1 
ATOM   13989 C  CB    . HIS   E 4  380 ? -4.070  71.049  89.928  1.00 67.89  ? 380 HIS   F CB    1 
ATOM   13990 C  CG    . HIS   E 4  380 ? -3.538  70.691  88.568  1.00 84.53  ? 380 HIS   F CG    1 
ATOM   13991 N  ND1   . HIS   E 4  380 ? -2.211  70.851  88.222  1.00 86.17  ? 380 HIS   F ND1   1 
ATOM   13992 C  CD2   . HIS   E 4  380 ? -4.148  70.169  87.475  1.00 81.79  ? 380 HIS   F CD2   1 
ATOM   13993 C  CE1   . HIS   E 4  380 ? -2.027  70.452  86.976  1.00 63.49  ? 380 HIS   F CE1   1 
ATOM   13994 N  NE2   . HIS   E 4  380 ? -3.187  70.034  86.500  1.00 74.80  ? 380 HIS   F NE2   1 
ATOM   13995 N  N     . MET   F 2  1   ? 28.471  77.901  31.732  1.00 72.70  ? 1   MET   B N     1 
ATOM   13996 C  CA    . MET   F 2  1   ? 27.132  77.673  31.194  1.00 77.84  ? 1   MET   B CA    1 
ATOM   13997 C  C     . MET   F 2  1   ? 26.629  76.239  31.418  1.00 65.04  ? 1   MET   B C     1 
ATOM   13998 O  O     . MET   F 2  1   ? 25.507  75.915  31.028  1.00 61.30  ? 1   MET   B O     1 
ATOM   13999 C  CB    . MET   F 2  1   ? 27.093  77.994  29.691  1.00 77.77  ? 1   MET   B CB    1 
ATOM   14000 C  CG    . MET   F 2  1   ? 27.466  79.427  29.331  1.00 86.39  ? 1   MET   B CG    1 
ATOM   14001 S  SD    . MET   F 2  1   ? 26.343  80.649  30.037  1.00 112.76 ? 1   MET   B SD    1 
ATOM   14002 C  CE    . MET   F 2  1   ? 26.927  80.734  31.729  1.00 97.48  ? 1   MET   B CE    1 
ATOM   14003 N  N     . ARG   F 2  2   ? 27.454  75.391  32.037  1.00 52.92  ? 2   ARG   B N     1 
ATOM   14004 C  CA    . ARG   F 2  2   ? 27.104  73.989  32.242  1.00 50.04  ? 2   ARG   B CA    1 
ATOM   14005 C  C     . ARG   F 2  2   ? 26.266  73.457  31.070  1.00 49.33  ? 2   ARG   B C     1 
ATOM   14006 O  O     . ARG   F 2  2   ? 25.029  73.451  31.103  1.00 45.15  ? 2   ARG   B O     1 
ATOM   14007 C  CB    . ARG   F 2  2   ? 26.417  73.824  33.602  1.00 33.80  ? 2   ARG   B CB    1 
ATOM   14008 C  CG    . ARG   F 2  2   ? 27.433  73.649  34.740  1.00 46.95  ? 2   ARG   B CG    1 
ATOM   14009 C  CD    . ARG   F 2  2   ? 27.289  72.263  35.404  1.00 53.54  ? 2   ARG   B CD    1 
ATOM   14010 N  NE    . ARG   F 2  2   ? 28.553  71.634  35.778  1.00 43.33  ? 2   ARG   B NE    1 
ATOM   14011 C  CZ    . ARG   F 2  2   ? 28.763  70.319  35.789  1.00 55.05  ? 2   ARG   B CZ    1 
ATOM   14012 N  NH1   . ARG   F 2  2   ? 27.810  69.461  35.454  1.00 46.96  ? 2   ARG   B NH1   1 
ATOM   14013 N  NH2   . ARG   F 2  2   ? 29.964  69.851  36.129  1.00 57.25  ? 2   ARG   B NH2   1 
ATOM   14014 N  N     . GLU   F 2  3   ? 26.953  73.050  30.005  1.00 44.39  ? 3   GLU   B N     1 
ATOM   14015 C  CA    . GLU   F 2  3   ? 26.347  72.524  28.797  1.00 35.78  ? 3   GLU   B CA    1 
ATOM   14016 C  C     . GLU   F 2  3   ? 26.153  71.016  28.893  1.00 34.91  ? 3   GLU   B C     1 
ATOM   14017 O  O     . GLU   F 2  3   ? 26.811  70.314  29.662  1.00 37.07  ? 3   GLU   B O     1 
ATOM   14018 C  CB    . GLU   F 2  3   ? 27.202  72.836  27.564  1.00 41.24  ? 3   GLU   B CB    1 
ATOM   14019 C  CG    . GLU   F 2  3   ? 27.434  74.303  27.283  1.00 37.39  ? 3   GLU   B CG    1 
ATOM   14020 C  CD    . GLU   F 2  3   ? 28.662  74.833  27.981  1.00 46.51  ? 3   GLU   B CD    1 
ATOM   14021 O  OE1   . GLU   F 2  3   ? 29.195  74.146  28.889  1.00 42.31  ? 3   GLU   B OE1   1 
ATOM   14022 O  OE2   . GLU   F 2  3   ? 29.107  75.935  27.612  1.00 45.11  ? 3   GLU   B OE2   1 
ATOM   14023 N  N     . ILE   F 2  4   ? 25.238  70.525  28.072  1.00 39.28  ? 4   ILE   B N     1 
ATOM   14024 C  CA    . ILE   F 2  4   ? 24.990  69.104  27.912  1.00 41.66  ? 4   ILE   B CA    1 
ATOM   14025 C  C     . ILE   F 2  4   ? 25.074  68.781  26.420  1.00 37.40  ? 4   ILE   B C     1 
ATOM   14026 O  O     . ILE   F 2  4   ? 24.437  69.453  25.601  1.00 29.08  ? 4   ILE   B O     1 
ATOM   14027 C  CB    . ILE   F 2  4   ? 23.621  68.717  28.508  1.00 26.08  ? 4   ILE   B CB    1 
ATOM   14028 C  CG1   . ILE   F 2  4   ? 23.618  69.032  30.004  1.00 29.16  ? 4   ILE   B CG1   1 
ATOM   14029 C  CG2   . ILE   F 2  4   ? 23.302  67.246  28.239  1.00 25.86  ? 4   ILE   B CG2   1 
ATOM   14030 C  CD1   . ILE   F 2  4   ? 22.334  68.704  30.734  1.00 24.85  ? 4   ILE   B CD1   1 
ATOM   14031 N  N     . VAL   F 2  5   ? 25.876  67.779  26.066  1.00 31.88  ? 5   VAL   B N     1 
ATOM   14032 C  CA    . VAL   F 2  5   ? 25.956  67.289  24.687  1.00 44.22  ? 5   VAL   B CA    1 
ATOM   14033 C  C     . VAL   F 2  5   ? 24.991  66.109  24.511  1.00 38.41  ? 5   VAL   B C     1 
ATOM   14034 O  O     . VAL   F 2  5   ? 25.150  65.056  25.147  1.00 32.15  ? 5   VAL   B O     1 
ATOM   14035 C  CB    . VAL   F 2  5   ? 27.397  66.893  24.307  1.00 39.75  ? 5   VAL   B CB    1 
ATOM   14036 C  CG1   . VAL   F 2  5   ? 27.484  66.591  22.819  1.00 37.22  ? 5   VAL   B CG1   1 
ATOM   14037 C  CG2   . VAL   F 2  5   ? 28.384  67.996  24.670  1.00 36.84  ? 5   VAL   B CG2   1 
ATOM   14038 N  N     . HIS   F 2  6   ? 23.993  66.292  23.641  1.00 30.21  ? 6   HIS   B N     1 
ATOM   14039 C  CA    . HIS   F 2  6   ? 22.976  65.288  23.367  1.00 36.10  ? 6   HIS   B CA    1 
ATOM   14040 C  C     . HIS   F 2  6   ? 23.399  64.459  22.158  1.00 36.50  ? 6   HIS   B C     1 
ATOM   14041 O  O     . HIS   F 2  6   ? 23.744  65.008  21.111  1.00 46.10  ? 6   HIS   B O     1 
ATOM   14042 C  CB    . HIS   F 2  6   ? 21.612  65.962  23.132  1.00 32.32  ? 6   HIS   B CB    1 
ATOM   14043 C  CG    . HIS   F 2  6   ? 20.560  65.063  22.538  1.00 41.62  ? 6   HIS   B CG    1 
ATOM   14044 N  ND1   . HIS   F 2  6   ? 19.681  64.325  23.308  1.00 38.85  ? 6   HIS   B ND1   1 
ATOM   14045 C  CD2   . HIS   F 2  6   ? 20.233  64.803  21.244  1.00 37.49  ? 6   HIS   B CD2   1 
ATOM   14046 C  CE1   . HIS   F 2  6   ? 18.877  63.634  22.517  1.00 37.86  ? 6   HIS   B CE1   1 
ATOM   14047 N  NE2   . HIS   F 2  6   ? 19.185  63.912  21.260  1.00 41.17  ? 6   HIS   B NE2   1 
ATOM   14048 N  N     . ILE   F 2  7   ? 23.383  63.141  22.312  1.00 30.10  ? 7   ILE   B N     1 
ATOM   14049 C  CA    . ILE   F 2  7   ? 23.679  62.196  21.243  1.00 34.38  ? 7   ILE   B CA    1 
ATOM   14050 C  C     . ILE   F 2  7   ? 22.452  61.306  21.080  1.00 37.10  ? 7   ILE   B C     1 
ATOM   14051 O  O     . ILE   F 2  7   ? 21.950  60.763  22.070  1.00 30.53  ? 7   ILE   B O     1 
ATOM   14052 C  CB    . ILE   F 2  7   ? 24.921  61.341  21.570  1.00 23.31  ? 7   ILE   B CB    1 
ATOM   14053 C  CG1   . ILE   F 2  7   ? 26.056  62.186  22.092  1.00 28.29  ? 7   ILE   B CG1   1 
ATOM   14054 C  CG2   . ILE   F 2  7   ? 25.418  60.612  20.370  1.00 25.07  ? 7   ILE   B CG2   1 
ATOM   14055 C  CD1   . ILE   F 2  7   ? 27.298  61.383  22.307  1.00 26.83  ? 7   ILE   B CD1   1 
ATOM   14056 N  N     . GLN   F 2  8   ? 21.969  61.147  19.846  1.00 33.73  ? 8   GLN   B N     1 
ATOM   14057 C  CA    . GLN   F 2  8   ? 20.872  60.218  19.578  1.00 30.47  ? 8   GLN   B CA    1 
ATOM   14058 C  C     . GLN   F 2  8   ? 21.279  59.261  18.475  1.00 29.07  ? 8   GLN   B C     1 
ATOM   14059 O  O     . GLN   F 2  8   ? 21.699  59.697  17.401  1.00 37.92  ? 8   GLN   B O     1 
ATOM   14060 C  CB    . GLN   F 2  8   ? 19.596  60.949  19.189  1.00 29.81  ? 8   GLN   B CB    1 
ATOM   14061 C  CG    . GLN   F 2  8   ? 19.710  61.809  17.961  1.00 31.78  ? 8   GLN   B CG    1 
ATOM   14062 C  CD    . GLN   F 2  8   ? 18.522  62.738  17.823  1.00 33.17  ? 8   GLN   B CD    1 
ATOM   14063 O  OE1   . GLN   F 2  8   ? 18.197  63.493  18.757  1.00 34.76  ? 8   GLN   B OE1   1 
ATOM   14064 N  NE2   . GLN   F 2  8   ? 17.837  62.665  16.680  1.00 29.09  ? 8   GLN   B NE2   1 
ATOM   14065 N  N     . ALA   F 2  9   ? 21.157  57.964  18.739  1.00 26.58  ? 9   ALA   B N     1 
ATOM   14066 C  CA    . ALA   F 2  9   ? 21.673  56.936  17.847  1.00 25.05  ? 9   ALA   B CA    1 
ATOM   14067 C  C     . ALA   F 2  9   ? 20.604  55.892  17.564  1.00 31.79  ? 9   ALA   B C     1 
ATOM   14068 O  O     . ALA   F 2  9   ? 19.830  55.534  18.452  1.00 30.86  ? 9   ALA   B O     1 
ATOM   14069 C  CB    . ALA   F 2  9   ? 22.909  56.273  18.437  1.00 23.39  ? 9   ALA   B CB    1 
ATOM   14070 N  N     . GLY   F 2  10  ? 20.566  55.402  16.314  1.00 36.26  ? 10  GLY   B N     1 
ATOM   14071 C  CA    . GLY   F 2  10  ? 19.610  54.386  15.915  1.00 28.35  ? 10  GLY   B CA    1 
ATOM   14072 C  C     . GLY   F 2  10  ? 18.248  54.970  15.556  1.00 30.73  ? 10  GLY   B C     1 
ATOM   14073 O  O     . GLY   F 2  10  ? 18.000  56.176  15.655  1.00 30.38  ? 10  GLY   B O     1 
ATOM   14074 N  N     . GLN   F 2  11  ? 17.345  54.077  15.128  1.00 21.57  ? 11  GLN   B N     1 
ATOM   14075 C  CA    . GLN   F 2  11  ? 15.969  54.455  14.803  1.00 33.54  ? 11  GLN   B CA    1 
ATOM   14076 C  C     . GLN   F 2  11  ? 15.242  54.977  16.034  1.00 27.01  ? 11  GLN   B C     1 
ATOM   14077 O  O     . GLN   F 2  11  ? 14.920  56.167  16.106  1.00 27.90  ? 11  GLN   B O     1 
ATOM   14078 C  CB    . GLN   F 2  11  ? 15.185  53.283  14.201  1.00 30.99  ? 11  GLN   B CB    1 
ATOM   14079 C  CG    . GLN   F 2  11  ? 14.069  53.701  13.231  1.00 43.80  ? 11  GLN   B CG    1 
ATOM   14080 C  CD    . GLN   F 2  11  ? 12.836  52.788  13.289  1.00 53.51  ? 11  GLN   B CD    1 
ATOM   14081 O  OE1   . GLN   F 2  11  ? 12.809  51.691  12.696  1.00 44.53  ? 11  GLN   B OE1   1 
ATOM   14082 N  NE2   . GLN   F 2  11  ? 11.803  53.246  14.007  1.00 48.18  ? 11  GLN   B NE2   1 
ATOM   14083 N  N     . CYS   F 2  12  ? 14.999  54.101  17.011  1.00 23.83  ? 12  CYS   B N     1 
ATOM   14084 C  CA    . CYS   F 2  12  ? 14.366  54.532  18.251  1.00 20.14  ? 12  CYS   B CA    1 
ATOM   14085 C  C     . CYS   F 2  12  ? 15.051  55.775  18.824  1.00 24.77  ? 12  CYS   B C     1 
ATOM   14086 O  O     . CYS   F 2  12  ? 14.408  56.800  19.076  1.00 28.85  ? 12  CYS   B O     1 
ATOM   14087 C  CB    . CYS   F 2  12  ? 14.379  53.385  19.257  1.00 16.88  ? 12  CYS   B CB    1 
ATOM   14088 S  SG    . CYS   F 2  12  ? 13.644  53.790  20.838  1.00 28.84  ? 12  CYS   B SG    1 
ATOM   14089 N  N     . GLY   F 2  13  ? 16.366  55.702  19.020  1.00 24.98  ? 13  GLY   B N     1 
ATOM   14090 C  CA    . GLY   F 2  13  ? 17.072  56.809  19.632  1.00 26.21  ? 13  GLY   B CA    1 
ATOM   14091 C  C     . GLY   F 2  13  ? 16.859  58.114  18.899  1.00 27.88  ? 13  GLY   B C     1 
ATOM   14092 O  O     . GLY   F 2  13  ? 16.677  59.157  19.525  1.00 30.99  ? 13  GLY   B O     1 
ATOM   14093 N  N     . ASN   F 2  14  ? 16.877  58.070  17.559  1.00 33.26  ? 14  ASN   B N     1 
ATOM   14094 C  CA    . ASN   F 2  14  ? 16.720  59.274  16.741  1.00 29.70  ? 14  ASN   B CA    1 
ATOM   14095 C  C     . ASN   F 2  14  ? 15.283  59.762  16.709  1.00 32.42  ? 14  ASN   B C     1 
ATOM   14096 O  O     . ASN   F 2  14  ? 15.044  60.952  16.475  1.00 33.27  ? 14  ASN   B O     1 
ATOM   14097 C  CB    . ASN   F 2  14  ? 17.192  59.017  15.311  1.00 27.86  ? 14  ASN   B CB    1 
ATOM   14098 C  CG    . ASN   F 2  14  ? 18.631  59.362  15.125  1.00 35.11  ? 14  ASN   B CG    1 
ATOM   14099 O  OD1   . ASN   F 2  14  ? 18.969  60.522  14.906  1.00 26.60  ? 14  ASN   B OD1   1 
ATOM   14100 N  ND2   . ASN   F 2  14  ? 19.506  58.359  15.243  1.00 34.58  ? 14  ASN   B ND2   1 
ATOM   14101 N  N     . GLN   F 2  15  ? 14.322  58.860  16.920  1.00 28.50  ? 15  GLN   B N     1 
ATOM   14102 C  CA    . GLN   F 2  15  ? 12.915  59.235  16.872  1.00 34.44  ? 15  GLN   B CA    1 
ATOM   14103 C  C     . GLN   F 2  15  ? 12.422  59.787  18.213  1.00 36.28  ? 15  GLN   B C     1 
ATOM   14104 O  O     . GLN   F 2  15  ? 11.620  60.729  18.231  1.00 27.32  ? 15  GLN   B O     1 
ATOM   14105 C  CB    . GLN   F 2  15  ? 12.078  58.040  16.420  1.00 33.15  ? 15  GLN   B CB    1 
ATOM   14106 C  CG    . GLN   F 2  15  ? 11.358  58.282  15.104  1.00 36.81  ? 15  GLN   B CG    1 
ATOM   14107 C  CD    . GLN   F 2  15  ? 11.103  56.996  14.317  1.00 56.70  ? 15  GLN   B CD    1 
ATOM   14108 O  OE1   . GLN   F 2  15  ? 11.231  55.869  14.850  1.00 38.68  ? 15  GLN   B OE1   1 
ATOM   14109 N  NE2   . GLN   F 2  15  ? 10.734  57.156  13.033  1.00 48.22  ? 15  GLN   B NE2   1 
ATOM   14110 N  N     . ILE   F 2  16  ? 12.869  59.229  19.347  1.00 36.36  ? 16  ILE   B N     1 
ATOM   14111 C  CA    . ILE   F 2  16  ? 12.514  59.876  20.616  1.00 31.88  ? 16  ILE   B CA    1 
ATOM   14112 C  C     . ILE   F 2  16  ? 13.400  61.094  20.862  1.00 32.38  ? 16  ILE   B C     1 
ATOM   14113 O  O     . ILE   F 2  16  ? 12.982  62.036  21.556  1.00 32.52  ? 16  ILE   B O     1 
ATOM   14114 C  CB    . ILE   F 2  16  ? 12.568  58.922  21.829  1.00 21.33  ? 16  ILE   B CB    1 
ATOM   14115 C  CG1   . ILE   F 2  16  ? 14.003  58.580  22.205  1.00 27.61  ? 16  ILE   B CG1   1 
ATOM   14116 C  CG2   . ILE   F 2  16  ? 11.753  57.654  21.578  1.00 21.64  ? 16  ILE   B CG2   1 
ATOM   14117 C  CD1   . ILE   F 2  16  ? 14.114  57.862  23.522  1.00 19.86  ? 16  ILE   B CD1   1 
ATOM   14118 N  N     . GLY   F 2  17  ? 14.591  61.122  20.263  1.00 30.16  ? 17  GLY   B N     1 
ATOM   14119 C  CA    . GLY   F 2  17  ? 15.429  62.307  20.354  1.00 32.03  ? 17  GLY   B CA    1 
ATOM   14120 C  C     . GLY   F 2  17  ? 14.857  63.488  19.594  1.00 30.82  ? 17  GLY   B C     1 
ATOM   14121 O  O     . GLY   F 2  17  ? 14.834  64.610  20.097  1.00 36.47  ? 17  GLY   B O     1 
ATOM   14122 N  N     . ALA   F 2  18  ? 14.395  63.256  18.367  1.00 35.90  ? 18  ALA   B N     1 
ATOM   14123 C  CA    . ALA   F 2  18  ? 13.798  64.347  17.604  1.00 31.97  ? 18  ALA   B CA    1 
ATOM   14124 C  C     . ALA   F 2  18  ? 12.541  64.864  18.276  1.00 31.17  ? 18  ALA   B C     1 
ATOM   14125 O  O     . ALA   F 2  18  ? 12.185  66.034  18.125  1.00 38.35  ? 18  ALA   B O     1 
ATOM   14126 C  CB    . ALA   F 2  18  ? 13.484  63.888  16.186  1.00 29.64  ? 18  ALA   B CB    1 
ATOM   14127 N  N     . LYS   F 2  19  ? 11.860  64.006  19.020  1.00 36.06  ? 19  LYS   B N     1 
ATOM   14128 C  CA    . LYS   F 2  19  ? 10.620  64.394  19.668  1.00 30.96  ? 19  LYS   B CA    1 
ATOM   14129 C  C     . LYS   F 2  19  ? 10.917  65.099  20.992  1.00 39.15  ? 19  LYS   B C     1 
ATOM   14130 O  O     . LYS   F 2  19  ? 10.230  66.057  21.361  1.00 43.92  ? 19  LYS   B O     1 
ATOM   14131 C  CB    . LYS   F 2  19  ? 9.747   63.145  19.839  1.00 27.85  ? 19  LYS   B CB    1 
ATOM   14132 C  CG    . LYS   F 2  19  ? 8.279   63.278  19.478  1.00 35.79  ? 19  LYS   B CG    1 
ATOM   14133 C  CD    . LYS   F 2  19  ? 7.484   63.979  20.604  1.00 38.83  ? 19  LYS   B CD    1 
ATOM   14134 C  CE    . LYS   F 2  19  ? 6.051   63.431  20.723  1.00 44.12  ? 19  LYS   B CE    1 
ATOM   14135 N  NZ    . LYS   F 2  19  ? 5.041   64.447  21.196  1.00 51.21  ? 19  LYS   B NZ    1 
ATOM   14136 N  N     . PHE   F 2  20  ? 11.962  64.675  21.701  1.00 30.32  ? 20  PHE   B N     1 
ATOM   14137 C  CA    . PHE   F 2  20  ? 12.439  65.483  22.816  1.00 33.36  ? 20  PHE   B CA    1 
ATOM   14138 C  C     . PHE   F 2  20  ? 12.770  66.901  22.356  1.00 36.92  ? 20  PHE   B C     1 
ATOM   14139 O  O     . PHE   F 2  20  ? 12.423  67.883  23.025  1.00 34.29  ? 20  PHE   B O     1 
ATOM   14140 C  CB    . PHE   F 2  20  ? 13.651  64.807  23.465  1.00 28.44  ? 20  PHE   B CB    1 
ATOM   14141 C  CG    . PHE   F 2  20  ? 14.465  65.708  24.368  1.00 31.16  ? 20  PHE   B CG    1 
ATOM   14142 C  CD1   . PHE   F 2  20  ? 14.083  65.937  25.673  1.00 37.25  ? 20  PHE   B CD1   1 
ATOM   14143 C  CD2   . PHE   F 2  20  ? 15.632  66.299  23.910  1.00 35.03  ? 20  PHE   B CD2   1 
ATOM   14144 C  CE1   . PHE   F 2  20  ? 14.850  66.752  26.506  1.00 39.20  ? 20  PHE   B CE1   1 
ATOM   14145 C  CE2   . PHE   F 2  20  ? 16.407  67.107  24.730  1.00 35.20  ? 20  PHE   B CE2   1 
ATOM   14146 C  CZ    . PHE   F 2  20  ? 16.019  67.334  26.031  1.00 38.41  ? 20  PHE   B CZ    1 
ATOM   14147 N  N     . TRP   F 2  21  ? 13.412  67.027  21.194  1.00 44.08  ? 21  TRP   B N     1 
ATOM   14148 C  CA    . TRP   F 2  21  ? 13.895  68.332  20.757  1.00 41.21  ? 21  TRP   B CA    1 
ATOM   14149 C  C     . TRP   F 2  21  ? 12.754  69.252  20.371  1.00 35.62  ? 21  TRP   B C     1 
ATOM   14150 O  O     . TRP   F 2  21  ? 12.786  70.446  20.679  1.00 39.69  ? 21  TRP   B O     1 
ATOM   14151 C  CB    . TRP   F 2  21  ? 14.885  68.172  19.604  1.00 34.21  ? 21  TRP   B CB    1 
ATOM   14152 C  CG    . TRP   F 2  21  ? 16.261  67.985  20.144  1.00 38.84  ? 21  TRP   B CG    1 
ATOM   14153 C  CD1   . TRP   F 2  21  ? 17.008  66.854  20.110  1.00 36.00  ? 21  TRP   B CD1   1 
ATOM   14154 C  CD2   . TRP   F 2  21  ? 17.028  68.953  20.867  1.00 32.94  ? 21  TRP   B CD2   1 
ATOM   14155 N  NE1   . TRP   F 2  21  ? 18.205  67.059  20.743  1.00 36.03  ? 21  TRP   B NE1   1 
ATOM   14156 C  CE2   . TRP   F 2  21  ? 18.242  68.341  21.220  1.00 31.54  ? 21  TRP   B CE2   1 
ATOM   14157 C  CE3   . TRP   F 2  21  ? 16.808  70.283  21.237  1.00 34.00  ? 21  TRP   B CE3   1 
ATOM   14158 C  CZ2   . TRP   F 2  21  ? 19.242  69.011  21.927  1.00 35.20  ? 21  TRP   B CZ2   1 
ATOM   14159 C  CZ3   . TRP   F 2  21  ? 17.803  70.953  21.942  1.00 38.47  ? 21  TRP   B CZ3   1 
ATOM   14160 C  CH2   . TRP   F 2  21  ? 19.004  70.315  22.280  1.00 38.64  ? 21  TRP   B CH2   1 
ATOM   14161 N  N     . GLU   F 2  22  ? 11.732  68.729  19.707  1.00 32.62  ? 22  GLU   B N     1 
ATOM   14162 C  CA    . GLU   F 2  22  ? 10.657  69.628  19.338  1.00 40.05  ? 22  GLU   B CA    1 
ATOM   14163 C  C     . GLU   F 2  22  ? 9.849   70.042  20.554  1.00 45.70  ? 22  GLU   B C     1 
ATOM   14164 O  O     . GLU   F 2  22  ? 9.298   71.146  20.568  1.00 44.01  ? 22  GLU   B O     1 
ATOM   14165 C  CB    . GLU   F 2  22  ? 9.762   69.008  18.270  1.00 39.93  ? 22  GLU   B CB    1 
ATOM   14166 C  CG    . GLU   F 2  22  ? 9.310   67.604  18.512  1.00 45.01  ? 22  GLU   B CG    1 
ATOM   14167 C  CD    . GLU   F 2  22  ? 8.298   67.162  17.463  1.00 57.39  ? 22  GLU   B CD    1 
ATOM   14168 O  OE1   . GLU   F 2  22  ? 7.155   67.683  17.495  1.00 56.07  ? 22  GLU   B OE1   1 
ATOM   14169 O  OE2   . GLU   F 2  22  ? 8.657   66.323  16.596  1.00 51.72  ? 22  GLU   B OE2   1 
ATOM   14170 N  N     . VAL   F 2  23  ? 9.792   69.195  21.589  1.00 46.54  ? 23  VAL   B N     1 
ATOM   14171 C  CA    . VAL   F 2  23  ? 9.003   69.531  22.772  1.00 41.73  ? 23  VAL   B CA    1 
ATOM   14172 C  C     . VAL   F 2  23  ? 9.707   70.594  23.613  1.00 46.36  ? 23  VAL   B C     1 
ATOM   14173 O  O     . VAL   F 2  23  ? 9.097   71.607  23.983  1.00 39.51  ? 23  VAL   B O     1 
ATOM   14174 C  CB    . VAL   F 2  23  ? 8.698   68.283  23.609  1.00 39.22  ? 23  VAL   B CB    1 
ATOM   14175 C  CG1   . VAL   F 2  23  ? 7.952   68.710  24.861  1.00 46.16  ? 23  VAL   B CG1   1 
ATOM   14176 C  CG2   . VAL   F 2  23  ? 7.887   67.299  22.823  1.00 37.79  ? 23  VAL   B CG2   1 
ATOM   14177 N  N     . ILE   F 2  24  ? 10.987  70.377  23.955  1.00 36.48  ? 24  ILE   B N     1 
ATOM   14178 C  CA    . ILE   F 2  24  ? 11.661  71.406  24.746  1.00 39.52  ? 24  ILE   B CA    1 
ATOM   14179 C  C     . ILE   F 2  24  ? 11.836  72.671  23.922  1.00 44.34  ? 24  ILE   B C     1 
ATOM   14180 O  O     . ILE   F 2  24  ? 11.829  73.779  24.474  1.00 42.57  ? 24  ILE   B O     1 
ATOM   14181 C  CB    . ILE   F 2  24  ? 13.025  70.965  25.331  1.00 30.13  ? 24  ILE   B CB    1 
ATOM   14182 C  CG1   . ILE   F 2  24  ? 14.065  70.797  24.234  1.00 34.52  ? 24  ILE   B CG1   1 
ATOM   14183 C  CG2   . ILE   F 2  24  ? 12.909  69.748  26.240  1.00 28.90  ? 24  ILE   B CG2   1 
ATOM   14184 C  CD1   . ILE   F 2  24  ? 15.479  70.772  24.762  1.00 34.05  ? 24  ILE   B CD1   1 
ATOM   14185 N  N     . SER   F 2  25  ? 12.006  72.550  22.605  1.00 43.78  ? 25  SER   B N     1 
ATOM   14186 C  CA    . SER   F 2  25  ? 12.108  73.760  21.797  1.00 44.67  ? 25  SER   B CA    1 
ATOM   14187 C  C     . SER   F 2  25  ? 10.878  74.631  21.994  1.00 43.20  ? 25  SER   B C     1 
ATOM   14188 O  O     . SER   F 2  25  ? 10.988  75.823  22.291  1.00 48.58  ? 25  SER   B O     1 
ATOM   14189 C  CB    . SER   F 2  25  ? 12.305  73.412  20.325  1.00 40.96  ? 25  SER   B CB    1 
ATOM   14190 O  OG    . SER   F 2  25  ? 13.643  73.011  20.127  1.00 43.00  ? 25  SER   B OG    1 
ATOM   14191 N  N     . ASP   F 2  26  ? 9.693   74.041  21.870  1.00 46.17  ? 26  ASP   B N     1 
ATOM   14192 C  CA    . ASP   F 2  26  ? 8.470   74.733  22.251  1.00 42.76  ? 26  ASP   B CA    1 
ATOM   14193 C  C     . ASP   F 2  26  ? 8.614   75.371  23.637  1.00 57.17  ? 26  ASP   B C     1 
ATOM   14194 O  O     . ASP   F 2  26  ? 8.583   76.600  23.777  1.00 48.67  ? 26  ASP   B O     1 
ATOM   14195 C  CB    . ASP   F 2  26  ? 7.305   73.751  22.207  1.00 42.38  ? 26  ASP   B CB    1 
ATOM   14196 C  CG    . ASP   F 2  26  ? 5.974   74.437  22.116  1.00 56.51  ? 26  ASP   B CG    1 
ATOM   14197 O  OD1   . ASP   F 2  26  ? 5.725   75.132  21.109  1.00 74.90  ? 26  ASP   B OD1   1 
ATOM   14198 O  OD2   . ASP   F 2  26  ? 5.166   74.272  23.048  1.00 65.82  ? 26  ASP   B OD2   1 
ATOM   14199 N  N     . GLU   F 2  27  ? 8.799   74.548  24.677  1.00 52.00  ? 27  GLU   B N     1 
ATOM   14200 C  CA    . GLU   F 2  27  ? 8.919   75.050  26.045  1.00 41.37  ? 27  GLU   B CA    1 
ATOM   14201 C  C     . GLU   F 2  27  ? 9.804   76.295  26.140  1.00 49.65  ? 27  GLU   B C     1 
ATOM   14202 O  O     . GLU   F 2  27  ? 9.528   77.199  26.934  1.00 49.14  ? 27  GLU   B O     1 
ATOM   14203 C  CB    . GLU   F 2  27  ? 9.461   73.951  26.960  1.00 32.79  ? 27  GLU   B CB    1 
ATOM   14204 C  CG    . GLU   F 2  27  ? 8.508   72.792  27.127  1.00 31.51  ? 27  GLU   B CG    1 
ATOM   14205 C  CD    . GLU   F 2  27  ? 8.817   71.903  28.329  1.00 34.86  ? 27  GLU   B CD    1 
ATOM   14206 O  OE1   . GLU   F 2  27  ? 9.838   72.122  29.030  1.00 31.39  ? 27  GLU   B OE1   1 
ATOM   14207 O  OE2   . GLU   F 2  27  ? 8.008   70.982  28.579  1.00 35.17  ? 27  GLU   B OE2   1 
ATOM   14208 N  N     . HIS   F 2  28  ? 10.864  76.357  25.333  1.00 47.13  ? 28  HIS   B N     1 
ATOM   14209 C  CA    . HIS   F 2  28  ? 11.792  77.474  25.339  1.00 38.14  ? 28  HIS   B CA    1 
ATOM   14210 C  C     . HIS   F 2  28  ? 11.483  78.522  24.279  1.00 44.92  ? 28  HIS   B C     1 
ATOM   14211 O  O     . HIS   F 2  28  ? 12.141  79.564  24.259  1.00 42.85  ? 28  HIS   B O     1 
ATOM   14212 C  CB    . HIS   F 2  28  ? 13.221  76.969  25.135  1.00 35.19  ? 28  HIS   B CB    1 
ATOM   14213 C  CG    . HIS   F 2  28  ? 13.760  76.212  26.301  1.00 39.26  ? 28  HIS   B CG    1 
ATOM   14214 N  ND1   . HIS   F 2  28  ? 14.535  76.803  27.278  1.00 47.73  ? 28  HIS   B ND1   1 
ATOM   14215 C  CD2   . HIS   F 2  28  ? 13.627  74.915  26.661  1.00 39.33  ? 28  HIS   B CD2   1 
ATOM   14216 C  CE1   . HIS   F 2  28  ? 14.857  75.901  28.187  1.00 42.60  ? 28  HIS   B CE1   1 
ATOM   14217 N  NE2   . HIS   F 2  28  ? 14.324  74.744  27.834  1.00 38.13  ? 28  HIS   B NE2   1 
ATOM   14218 N  N     . GLY   F 2  29  ? 10.527  78.266  23.391  1.00 48.29  ? 29  GLY   B N     1 
ATOM   14219 C  CA    . GLY   F 2  29  ? 10.119  79.246  22.397  1.00 41.05  ? 29  GLY   B CA    1 
ATOM   14220 C  C     . GLY   F 2  29  ? 11.011  79.380  21.179  1.00 50.25  ? 29  GLY   B C     1 
ATOM   14221 O  O     . GLY   F 2  29  ? 11.199  80.496  20.672  1.00 56.38  ? 29  GLY   B O     1 
ATOM   14222 N  N     . ILE   F 2  30  ? 11.566  78.279  20.683  1.00 40.71  ? 30  ILE   B N     1 
ATOM   14223 C  CA    . ILE   F 2  30  ? 12.347  78.277  19.454  1.00 46.33  ? 30  ILE   B CA    1 
ATOM   14224 C  C     . ILE   F 2  30  ? 11.505  77.651  18.353  1.00 50.74  ? 30  ILE   B C     1 
ATOM   14225 O  O     . ILE   F 2  30  ? 10.893  76.596  18.559  1.00 43.99  ? 30  ILE   B O     1 
ATOM   14226 C  CB    . ILE   F 2  30  ? 13.671  77.521  19.625  1.00 48.66  ? 30  ILE   B CB    1 
ATOM   14227 C  CG1   . ILE   F 2  30  ? 14.565  78.256  20.619  1.00 53.06  ? 30  ILE   B CG1   1 
ATOM   14228 C  CG2   . ILE   F 2  30  ? 14.354  77.361  18.278  1.00 51.63  ? 30  ILE   B CG2   1 
ATOM   14229 C  CD1   . ILE   F 2  30  ? 14.048  78.215  22.034  1.00 56.46  ? 30  ILE   B CD1   1 
ATOM   14230 N  N     . ASP   F 2  31  ? 11.452  78.307  17.199  1.00 56.65  ? 31  ASP   B N     1 
ATOM   14231 C  CA    . ASP   F 2  31  ? 10.734  77.772  16.048  1.00 62.21  ? 31  ASP   B CA    1 
ATOM   14232 C  C     . ASP   F 2  31  ? 11.661  76.904  15.214  1.00 60.74  ? 31  ASP   B C     1 
ATOM   14233 O  O     . ASP   F 2  31  ? 12.884  76.920  15.383  1.00 53.80  ? 31  ASP   B O     1 
ATOM   14234 C  CB    . ASP   F 2  31  ? 10.131  78.911  15.217  1.00 54.63  ? 31  ASP   B CB    1 
ATOM   14235 C  CG    . ASP   F 2  31  ? 11.166  79.937  14.749  1.00 63.22  ? 31  ASP   B CG    1 
ATOM   14236 O  OD1   . ASP   F 2  31  ? 12.379  79.631  14.720  1.00 60.61  ? 31  ASP   B OD1   1 
ATOM   14237 O  OD2   . ASP   F 2  31  ? 10.752  81.066  14.405  1.00 55.39  ? 31  ASP   B OD2   1 
ATOM   14238 N  N     . PRO   F 2  32  ? 11.104  76.116  14.298  1.00 54.30  ? 32  PRO   B N     1 
ATOM   14239 C  CA    . PRO   F 2  32  ? 11.933  75.190  13.516  1.00 58.96  ? 32  PRO   B CA    1 
ATOM   14240 C  C     . PRO   F 2  32  ? 13.127  75.842  12.840  1.00 62.17  ? 32  PRO   B C     1 
ATOM   14241 O  O     . PRO   F 2  32  ? 13.974  75.138  12.283  1.00 69.52  ? 32  PRO   B O     1 
ATOM   14242 C  CB    . PRO   F 2  32  ? 10.946  74.632  12.487  1.00 55.59  ? 32  PRO   B CB    1 
ATOM   14243 C  CG    . PRO   F 2  32  ? 9.637   74.667  13.210  1.00 52.66  ? 32  PRO   B CG    1 
ATOM   14244 C  CD    . PRO   F 2  32  ? 9.668   75.899  14.070  1.00 43.19  ? 32  PRO   B CD    1 
ATOM   14245 N  N     . THR   F 2  33  ? 13.214  77.170  12.879  1.00 67.57  ? 33  THR   B N     1 
ATOM   14246 C  CA    . THR   F 2  33  ? 14.330  77.904  12.293  1.00 64.23  ? 33  THR   B CA    1 
ATOM   14247 C  C     . THR   F 2  33  ? 15.329  78.394  13.336  1.00 66.51  ? 33  THR   B C     1 
ATOM   14248 O  O     . THR   F 2  33  ? 16.311  79.052  12.974  1.00 65.77  ? 33  THR   B O     1 
ATOM   14249 C  CB    . THR   F 2  33  ? 13.805  79.090  11.481  1.00 65.94  ? 33  THR   B CB    1 
ATOM   14250 O  OG1   . THR   F 2  33  ? 13.265  80.082  12.369  1.00 67.30  ? 33  THR   B OG1   1 
ATOM   14251 C  CG2   . THR   F 2  33  ? 12.710  78.624  10.529  1.00 61.32  ? 33  THR   B CG2   1 
ATOM   14252 N  N     . GLY   F 2  34  ? 15.099  78.101  14.615  1.00 61.04  ? 34  GLY   B N     1 
ATOM   14253 C  CA    . GLY   F 2  34  ? 16.057  78.424  15.656  1.00 65.12  ? 34  GLY   B CA    1 
ATOM   14254 C  C     . GLY   F 2  34  ? 15.962  79.814  16.238  1.00 63.78  ? 34  GLY   B C     1 
ATOM   14255 O  O     . GLY   F 2  34  ? 16.926  80.277  16.857  1.00 64.66  ? 34  GLY   B O     1 
ATOM   14256 N  N     . SER   F 2  35  ? 14.831  80.491  16.077  1.00 64.93  ? 35  SER   B N     1 
ATOM   14257 C  CA    . SER   F 2  35  ? 14.675  81.881  16.479  1.00 62.04  ? 35  SER   B CA    1 
ATOM   14258 C  C     . SER   F 2  35  ? 13.841  81.937  17.743  1.00 59.11  ? 35  SER   B C     1 
ATOM   14259 O  O     . SER   F 2  35  ? 12.809  81.263  17.834  1.00 58.17  ? 35  SER   B O     1 
ATOM   14260 C  CB    . SER   F 2  35  ? 14.008  82.701  15.374  1.00 68.35  ? 35  SER   B CB    1 
ATOM   14261 O  OG    . SER   F 2  35  ? 14.632  82.476  14.121  1.00 79.44  ? 35  SER   B OG    1 
ATOM   14262 N  N     . TYR   F 2  36  ? 14.277  82.741  18.706  1.00 58.65  ? 36  TYR   B N     1 
ATOM   14263 C  CA    . TYR   F 2  36  ? 13.512  82.862  19.935  1.00 58.01  ? 36  TYR   B CA    1 
ATOM   14264 C  C     . TYR   F 2  36  ? 12.264  83.681  19.682  1.00 50.71  ? 36  TYR   B C     1 
ATOM   14265 O  O     . TYR   F 2  36  ? 12.333  84.768  19.112  1.00 56.64  ? 36  TYR   B O     1 
ATOM   14266 C  CB    . TYR   F 2  36  ? 14.330  83.511  21.054  1.00 60.92  ? 36  TYR   B CB    1 
ATOM   14267 C  CG    . TYR   F 2  36  ? 13.502  83.662  22.317  1.00 59.61  ? 36  TYR   B CG    1 
ATOM   14268 C  CD1   . TYR   F 2  36  ? 12.931  82.548  22.926  1.00 57.74  ? 36  TYR   B CD1   1 
ATOM   14269 C  CD2   . TYR   F 2  36  ? 13.259  84.907  22.878  1.00 51.57  ? 36  TYR   B CD2   1 
ATOM   14270 C  CE1   . TYR   F 2  36  ? 12.162  82.668  24.062  1.00 51.69  ? 36  TYR   B CE1   1 
ATOM   14271 C  CE2   . TYR   F 2  36  ? 12.486  85.034  24.013  1.00 56.45  ? 36  TYR   B CE2   1 
ATOM   14272 C  CZ    . TYR   F 2  36  ? 11.942  83.907  24.599  1.00 58.77  ? 36  TYR   B CZ    1 
ATOM   14273 O  OH    . TYR   F 2  36  ? 11.166  84.013  25.728  1.00 70.80  ? 36  TYR   B OH    1 
ATOM   14274 N  N     . HIS   F 2  37  ? 11.123  83.174  20.125  1.00 54.70  ? 37  HIS   B N     1 
ATOM   14275 C  CA    . HIS   F 2  37  ? 9.890   83.946  20.076  1.00 58.32  ? 37  HIS   B CA    1 
ATOM   14276 C  C     . HIS   F 2  37  ? 9.055   83.679  21.319  1.00 60.68  ? 37  HIS   B C     1 
ATOM   14277 O  O     . HIS   F 2  37  ? 7.842   83.479  21.254  1.00 69.26  ? 37  HIS   B O     1 
ATOM   14278 C  CB    . HIS   F 2  37  ? 9.143   83.655  18.782  1.00 55.15  ? 37  HIS   B CB    1 
ATOM   14279 C  CG    . HIS   F 2  37  ? 9.791   84.286  17.596  1.00 67.35  ? 37  HIS   B CG    1 
ATOM   14280 N  ND1   . HIS   F 2  37  ? 9.716   85.641  17.348  1.00 69.39  ? 37  HIS   B ND1   1 
ATOM   14281 C  CD2   . HIS   F 2  37  ? 10.584  83.768  16.629  1.00 69.96  ? 37  HIS   B CD2   1 
ATOM   14282 C  CE1   . HIS   F 2  37  ? 10.409  85.925  16.259  1.00 71.28  ? 37  HIS   B CE1   1 
ATOM   14283 N  NE2   . HIS   F 2  37  ? 10.947  84.807  15.803  1.00 74.03  ? 37  HIS   B NE2   1 
ATOM   14284 N  N     . GLY   F 2  38  ? 9.717   83.707  22.484  1.00 53.64  ? 38  GLY   B N     1 
ATOM   14285 C  CA    . GLY   F 2  38  ? 9.042   83.443  23.737  1.00 61.00  ? 38  GLY   B CA    1 
ATOM   14286 C  C     . GLY   F 2  38  ? 8.576   84.697  24.442  1.00 62.43  ? 38  GLY   B C     1 
ATOM   14287 O  O     . GLY   F 2  38  ? 8.965   85.815  24.106  1.00 59.70  ? 38  GLY   B O     1 
ATOM   14288 N  N     . ASP   F 2  39  ? 7.721   84.489  25.442  1.00 71.06  ? 39  ASP   B N     1 
ATOM   14289 C  CA    . ASP   F 2  39  ? 7.132   85.580  26.212  1.00 72.50  ? 39  ASP   B CA    1 
ATOM   14290 C  C     . ASP   F 2  39  ? 7.551   85.496  27.671  1.00 69.08  ? 39  ASP   B C     1 
ATOM   14291 O  O     . ASP   F 2  39  ? 6.710   85.623  28.568  1.00 72.84  ? 39  ASP   B O     1 
ATOM   14292 C  CB    . ASP   F 2  39  ? 5.607   85.546  26.114  1.00 72.82  ? 39  ASP   B CB    1 
ATOM   14293 C  CG    . ASP   F 2  39  ? 5.011   84.326  26.790  1.00 81.18  ? 39  ASP   B CG    1 
ATOM   14294 O  OD1   . ASP   F 2  39  ? 5.667   83.259  26.786  1.00 78.49  ? 39  ASP   B OD1   1 
ATOM   14295 O  OD2   . ASP   F 2  39  ? 3.892   84.432  27.336  1.00 91.12  ? 39  ASP   B OD2   1 
ATOM   14296 N  N     . SER   F 2  40  ? 8.841   85.271  27.918  1.00 63.56  ? 40  SER   B N     1 
ATOM   14297 C  CA    . SER   F 2  40  ? 9.334   85.154  29.284  1.00 66.05  ? 40  SER   B CA    1 
ATOM   14298 C  C     . SER   F 2  40  ? 10.853  85.069  29.314  1.00 71.26  ? 40  SER   B C     1 
ATOM   14299 O  O     . SER   F 2  40  ? 11.459  84.320  28.541  1.00 65.37  ? 40  SER   B O     1 
ATOM   14300 C  CB    . SER   F 2  40  ? 8.726   83.930  29.969  1.00 66.50  ? 40  SER   B CB    1 
ATOM   14301 O  OG    . SER   F 2  40  ? 9.543   83.469  31.031  1.00 67.54  ? 40  SER   B OG    1 
ATOM   14302 N  N     . ASP   F 2  41  ? 11.476  85.848  30.199  1.00 68.17  ? 41  ASP   B N     1 
ATOM   14303 C  CA    . ASP   F 2  41  ? 12.915  85.753  30.384  1.00 66.87  ? 41  ASP   B CA    1 
ATOM   14304 C  C     . ASP   F 2  41  ? 13.312  84.411  30.991  1.00 74.32  ? 41  ASP   B C     1 
ATOM   14305 O  O     . ASP   F 2  41  ? 14.489  84.027  30.923  1.00 64.87  ? 41  ASP   B O     1 
ATOM   14306 C  CB    . ASP   F 2  41  ? 13.394  86.915  31.261  1.00 82.71  ? 41  ASP   B CB    1 
ATOM   14307 C  CG    . ASP   F 2  41  ? 12.820  88.263  30.820  1.00 93.18  ? 41  ASP   B CG    1 
ATOM   14308 O  OD1   . ASP   F 2  41  ? 12.635  88.475  29.598  1.00 96.78  ? 41  ASP   B OD1   1 
ATOM   14309 O  OD2   . ASP   F 2  41  ? 12.553  89.114  31.700  1.00 92.46  ? 41  ASP   B OD2   1 
ATOM   14310 N  N     . LEU   F 2  42  ? 12.344  83.691  31.572  1.00 68.80  ? 42  LEU   B N     1 
ATOM   14311 C  CA    . LEU   F 2  42  ? 12.610  82.382  32.155  1.00 60.61  ? 42  LEU   B CA    1 
ATOM   14312 C  C     . LEU   F 2  42  ? 12.949  81.350  31.085  1.00 60.40  ? 42  LEU   B C     1 
ATOM   14313 O  O     . LEU   F 2  42  ? 13.669  80.380  31.361  1.00 54.87  ? 42  LEU   B O     1 
ATOM   14314 C  CB    . LEU   F 2  42  ? 11.399  81.935  32.978  1.00 58.43  ? 42  LEU   B CB    1 
ATOM   14315 C  CG    . LEU   F 2  42  ? 11.674  81.418  34.400  1.00 73.02  ? 42  LEU   B CG    1 
ATOM   14316 C  CD1   . LEU   F 2  42  ? 12.555  82.390  35.228  1.00 50.15  ? 42  LEU   B CD1   1 
ATOM   14317 C  CD2   . LEU   F 2  42  ? 10.365  81.086  35.129  1.00 52.36  ? 42  LEU   B CD2   1 
ATOM   14318 N  N     . GLN   F 2  43  ? 12.450  81.547  29.862  1.00 56.79  ? 45  GLN   B N     1 
ATOM   14319 C  CA    . GLN   F 2  43  ? 12.699  80.609  28.779  1.00 48.70  ? 45  GLN   B CA    1 
ATOM   14320 C  C     . GLN   F 2  43  ? 14.136  80.660  28.272  1.00 53.12  ? 45  GLN   B C     1 
ATOM   14321 O  O     . GLN   F 2  43  ? 14.611  79.673  27.696  1.00 54.30  ? 45  GLN   B O     1 
ATOM   14322 C  CB    . GLN   F 2  43  ? 11.730  80.877  27.627  1.00 48.94  ? 45  GLN   B CB    1 
ATOM   14323 C  CG    . GLN   F 2  43  ? 10.352  80.255  27.816  1.00 52.39  ? 45  GLN   B CG    1 
ATOM   14324 C  CD    . GLN   F 2  43  ? 9.252   81.015  27.102  1.00 53.28  ? 45  GLN   B CD    1 
ATOM   14325 O  OE1   . GLN   F 2  43  ? 9.498   81.695  26.110  1.00 52.37  ? 45  GLN   B OE1   1 
ATOM   14326 N  NE2   . GLN   F 2  43  ? 8.029   80.930  27.629  1.00 64.13  ? 45  GLN   B NE2   1 
ATOM   14327 N  N     . LEU   F 2  44  ? 14.842  81.773  28.464  1.00 52.96  ? 46  LEU   B N     1 
ATOM   14328 C  CA    . LEU   F 2  44  ? 16.182  81.919  27.911  1.00 45.94  ? 46  LEU   B CA    1 
ATOM   14329 C  C     . LEU   F 2  44  ? 17.282  81.860  28.950  1.00 37.64  ? 46  LEU   B C     1 
ATOM   14330 O  O     . LEU   F 2  44  ? 18.454  81.815  28.573  1.00 40.31  ? 46  LEU   B O     1 
ATOM   14331 C  CB    . LEU   F 2  44  ? 16.303  83.239  27.135  1.00 42.41  ? 46  LEU   B CB    1 
ATOM   14332 C  CG    . LEU   F 2  44  ? 15.558  83.238  25.797  1.00 52.14  ? 46  LEU   B CG    1 
ATOM   14333 C  CD1   . LEU   F 2  44  ? 15.636  84.599  25.136  1.00 57.01  ? 46  LEU   B CD1   1 
ATOM   14334 C  CD2   . LEU   F 2  44  ? 16.101  82.154  24.870  1.00 50.37  ? 46  LEU   B CD2   1 
ATOM   14335 N  N     . GLU   F 2  45  ? 16.944  81.859  30.237  1.00 42.78  ? 47  GLU   B N     1 
ATOM   14336 C  CA    . GLU   F 2  45  ? 17.970  81.960  31.268  1.00 51.19  ? 47  GLU   B CA    1 
ATOM   14337 C  C     . GLU   F 2  45  ? 18.956  80.798  31.175  1.00 47.47  ? 47  GLU   B C     1 
ATOM   14338 O  O     . GLU   F 2  45  ? 20.169  80.994  31.051  1.00 41.54  ? 47  GLU   B O     1 
ATOM   14339 C  CB    . GLU   F 2  45  ? 17.313  82.026  32.651  1.00 53.94  ? 47  GLU   B CB    1 
ATOM   14340 C  CG    . GLU   F 2  45  ? 18.183  82.648  33.732  1.00 58.76  ? 47  GLU   B CG    1 
ATOM   14341 C  CD    . GLU   F 2  45  ? 17.364  83.380  34.784  1.00 82.89  ? 47  GLU   B CD    1 
ATOM   14342 O  OE1   . GLU   F 2  45  ? 16.120  83.222  34.796  1.00 82.25  ? 47  GLU   B OE1   1 
ATOM   14343 O  OE2   . GLU   F 2  45  ? 17.963  84.123  35.595  1.00 100.33 ? 47  GLU   B OE2   1 
ATOM   14344 N  N     . ARG   F 2  46  ? 18.457  79.571  31.227  1.00 43.98  ? 48  ARG   B N     1 
ATOM   14345 C  CA    . ARG   F 2  46  ? 19.337  78.419  31.150  1.00 40.95  ? 48  ARG   B CA    1 
ATOM   14346 C  C     . ARG   F 2  46  ? 19.340  77.790  29.764  1.00 48.17  ? 48  ARG   B C     1 
ATOM   14347 O  O     . ARG   F 2  46  ? 19.607  76.592  29.638  1.00 50.36  ? 48  ARG   B O     1 
ATOM   14348 C  CB    . ARG   F 2  46  ? 18.946  77.392  32.208  1.00 48.05  ? 48  ARG   B CB    1 
ATOM   14349 C  CG    . ARG   F 2  46  ? 19.066  77.894  33.623  1.00 33.77  ? 48  ARG   B CG    1 
ATOM   14350 C  CD    . ARG   F 2  46  ? 19.984  76.976  34.399  1.00 43.10  ? 48  ARG   B CD    1 
ATOM   14351 N  NE    . ARG   F 2  46  ? 19.260  75.927  35.109  1.00 43.00  ? 48  ARG   B NE    1 
ATOM   14352 C  CZ    . ARG   F 2  46  ? 19.817  74.804  35.552  1.00 52.45  ? 48  ARG   B CZ    1 
ATOM   14353 N  NH1   . ARG   F 2  46  ? 21.084  74.506  35.284  1.00 54.83  ? 48  ARG   B NH1   1 
ATOM   14354 N  NH2   . ARG   F 2  46  ? 19.088  73.959  36.284  1.00 45.02  ? 48  ARG   B NH2   1 
ATOM   14355 N  N     . ILE   F 2  47  ? 19.064  78.583  28.718  1.00 54.35  ? 49  ILE   B N     1 
ATOM   14356 C  CA    . ILE   F 2  47  ? 18.897  78.029  27.376  1.00 50.62  ? 49  ILE   B CA    1 
ATOM   14357 C  C     . ILE   F 2  47  ? 20.162  77.321  26.929  1.00 52.59  ? 49  ILE   B C     1 
ATOM   14358 O  O     . ILE   F 2  47  ? 20.100  76.341  26.175  1.00 52.63  ? 49  ILE   B O     1 
ATOM   14359 C  CB    . ILE   F 2  47  ? 18.488  79.124  26.365  1.00 58.68  ? 49  ILE   B CB    1 
ATOM   14360 C  CG1   . ILE   F 2  47  ? 17.854  78.499  25.115  1.00 52.93  ? 49  ILE   B CG1   1 
ATOM   14361 C  CG2   . ILE   F 2  47  ? 19.695  79.930  25.922  1.00 50.77  ? 49  ILE   B CG2   1 
ATOM   14362 C  CD1   . ILE   F 2  47  ? 16.669  77.614  25.416  1.00 44.54  ? 49  ILE   B CD1   1 
ATOM   14363 N  N     . ASN   F 2  48  ? 21.322  77.778  27.397  1.00 46.23  ? 50  ASN   B N     1 
ATOM   14364 C  CA    . ASN   F 2  48  ? 22.590  77.269  26.894  1.00 45.33  ? 50  ASN   B CA    1 
ATOM   14365 C  C     . ASN   F 2  48  ? 22.960  75.903  27.457  1.00 48.07  ? 50  ASN   B C     1 
ATOM   14366 O  O     . ASN   F 2  48  ? 24.051  75.404  27.160  1.00 47.40  ? 50  ASN   B O     1 
ATOM   14367 C  CB    . ASN   F 2  48  ? 23.687  78.297  27.164  1.00 54.05  ? 50  ASN   B CB    1 
ATOM   14368 C  CG    . ASN   F 2  48  ? 23.656  79.450  26.144  1.00 77.98  ? 50  ASN   B CG    1 
ATOM   14369 O  OD1   . ASN   F 2  48  ? 23.112  80.531  26.409  1.00 69.66  ? 50  ASN   B OD1   1 
ATOM   14370 N  ND2   . ASN   F 2  48  ? 24.213  79.201  24.954  1.00 72.51  ? 50  ASN   B ND2   1 
ATOM   14371 N  N     . VAL   F 2  49  ? 22.078  75.285  28.245  1.00 45.89  ? 51  VAL   B N     1 
ATOM   14372 C  CA    . VAL   F 2  49  ? 22.277  73.903  28.669  1.00 42.21  ? 51  VAL   B CA    1 
ATOM   14373 C  C     . VAL   F 2  49  ? 22.088  72.955  27.488  1.00 48.09  ? 51  VAL   B C     1 
ATOM   14374 O  O     . VAL   F 2  49  ? 22.808  71.953  27.349  1.00 38.95  ? 51  VAL   B O     1 
ATOM   14375 C  CB    . VAL   F 2  49  ? 21.309  73.575  29.821  1.00 44.61  ? 51  VAL   B CB    1 
ATOM   14376 C  CG1   . VAL   F 2  49  ? 21.276  72.078  30.112  1.00 32.11  ? 51  VAL   B CG1   1 
ATOM   14377 C  CG2   . VAL   F 2  49  ? 21.654  74.393  31.060  1.00 40.38  ? 51  VAL   B CG2   1 
ATOM   14378 N  N     . TYR   F 2  50  ? 21.124  73.262  26.610  1.00 39.47  ? 52  TYR   B N     1 
ATOM   14379 C  CA    . TYR   F 2  50  ? 20.842  72.426  25.459  1.00 41.49  ? 52  TYR   B CA    1 
ATOM   14380 C  C     . TYR   F 2  50  ? 21.111  73.083  24.099  1.00 45.35  ? 52  TYR   B C     1 
ATOM   14381 O  O     . TYR   F 2  50  ? 21.156  72.360  23.094  1.00 43.09  ? 52  TYR   B O     1 
ATOM   14382 C  CB    . TYR   F 2  50  ? 19.386  71.916  25.527  1.00 33.46  ? 52  TYR   B CB    1 
ATOM   14383 C  CG    . TYR   F 2  50  ? 19.237  70.733  26.475  1.00 44.83  ? 52  TYR   B CG    1 
ATOM   14384 C  CD1   . TYR   F 2  50  ? 19.504  69.428  26.052  1.00 36.74  ? 52  TYR   B CD1   1 
ATOM   14385 C  CD2   . TYR   F 2  50  ? 18.867  70.924  27.805  1.00 50.73  ? 52  TYR   B CD2   1 
ATOM   14386 C  CE1   . TYR   F 2  50  ? 19.395  68.350  26.923  1.00 36.06  ? 52  TYR   B CE1   1 
ATOM   14387 C  CE2   . TYR   F 2  50  ? 18.760  69.855  28.686  1.00 39.87  ? 52  TYR   B CE2   1 
ATOM   14388 C  CZ    . TYR   F 2  50  ? 19.026  68.571  28.243  1.00 40.69  ? 52  TYR   B CZ    1 
ATOM   14389 O  OH    . TYR   F 2  50  ? 18.901  67.523  29.127  1.00 28.61  ? 52  TYR   B OH    1 
ATOM   14390 N  N     . TYR   F 2  51  ? 21.342  74.401  24.028  1.00 42.35  ? 53  TYR   B N     1 
ATOM   14391 C  CA    . TYR   F 2  51  ? 21.482  75.105  22.751  1.00 42.43  ? 53  TYR   B CA    1 
ATOM   14392 C  C     . TYR   F 2  51  ? 22.815  75.849  22.642  1.00 43.16  ? 53  TYR   B C     1 
ATOM   14393 O  O     . TYR   F 2  51  ? 23.413  76.239  23.648  1.00 56.88  ? 53  TYR   B O     1 
ATOM   14394 C  CB    . TYR   F 2  51  ? 20.322  76.092  22.554  1.00 34.90  ? 53  TYR   B CB    1 
ATOM   14395 C  CG    . TYR   F 2  51  ? 18.967  75.419  22.390  1.00 44.09  ? 53  TYR   B CG    1 
ATOM   14396 C  CD1   . TYR   F 2  51  ? 18.221  75.008  23.500  1.00 40.69  ? 53  TYR   B CD1   1 
ATOM   14397 C  CD2   . TYR   F 2  51  ? 18.436  75.179  21.122  1.00 40.43  ? 53  TYR   B CD2   1 
ATOM   14398 C  CE1   . TYR   F 2  51  ? 16.977  74.379  23.345  1.00 32.65  ? 53  TYR   B CE1   1 
ATOM   14399 C  CE2   . TYR   F 2  51  ? 17.195  74.560  20.953  1.00 38.94  ? 53  TYR   B CE2   1 
ATOM   14400 C  CZ    . TYR   F 2  51  ? 16.471  74.161  22.065  1.00 44.34  ? 53  TYR   B CZ    1 
ATOM   14401 O  OH    . TYR   F 2  51  ? 15.239  73.557  21.882  1.00 47.34  ? 53  TYR   B OH    1 
ATOM   14402 N  N     . ASN   F 2  52  ? 23.296  76.022  21.413  1.00 44.71  ? 54  ASN   B N     1 
ATOM   14403 C  CA    . ASN   F 2  52  ? 24.315  77.018  21.096  1.00 52.45  ? 54  ASN   B CA    1 
ATOM   14404 C  C     . ASN   F 2  52  ? 23.657  78.208  20.418  1.00 55.20  ? 54  ASN   B C     1 
ATOM   14405 O  O     . ASN   F 2  52  ? 22.577  78.092  19.830  1.00 50.97  ? 54  ASN   B O     1 
ATOM   14406 C  CB    . ASN   F 2  52  ? 25.401  76.481  20.159  1.00 44.11  ? 54  ASN   B CB    1 
ATOM   14407 C  CG    . ASN   F 2  52  ? 26.072  75.244  20.682  1.00 45.24  ? 54  ASN   B CG    1 
ATOM   14408 O  OD1   . ASN   F 2  52  ? 26.593  75.227  21.796  1.00 51.92  ? 54  ASN   B OD1   1 
ATOM   14409 N  ND2   . ASN   F 2  52  ? 26.070  74.188  19.873  1.00 47.36  ? 54  ASN   B ND2   1 
ATOM   14410 N  N     . GLU   F 2  53  ? 24.334  79.353  20.478  1.00 70.55  ? 55  GLU   B N     1 
ATOM   14411 C  CA    . GLU   F 2  53  ? 23.876  80.551  19.789  1.00 75.99  ? 55  GLU   B CA    1 
ATOM   14412 C  C     . GLU   F 2  53  ? 24.810  80.882  18.632  1.00 73.89  ? 55  GLU   B C     1 
ATOM   14413 O  O     . GLU   F 2  53  ? 25.986  80.509  18.637  1.00 69.01  ? 55  GLU   B O     1 
ATOM   14414 C  CB    . GLU   F 2  53  ? 23.769  81.748  20.749  1.00 86.94  ? 55  GLU   B CB    1 
ATOM   14415 C  CG    . GLU   F 2  53  ? 22.669  82.761  20.343  1.00 93.43  ? 55  GLU   B CG    1 
ATOM   14416 C  CD    . GLU   F 2  53  ? 22.401  83.843  21.391  1.00 92.85  ? 55  GLU   B CD    1 
ATOM   14417 O  OE1   . GLU   F 2  53  ? 23.209  83.982  22.339  1.00 94.20  ? 55  GLU   B OE1   1 
ATOM   14418 O  OE2   . GLU   F 2  53  ? 21.372  84.551  21.258  1.00 85.77  ? 55  GLU   B OE2   1 
ATOM   14419 N  N     . ALA   F 2  54  ? 24.261  81.574  17.629  1.00 84.34  ? 56  ALA   B N     1 
ATOM   14420 C  CA    . ALA   F 2  54  ? 25.020  82.078  16.491  1.00 86.92  ? 56  ALA   B CA    1 
ATOM   14421 C  C     . ALA   F 2  54  ? 24.475  83.447  16.105  1.00 95.04  ? 56  ALA   B C     1 
ATOM   14422 O  O     . ALA   F 2  54  ? 23.469  83.910  16.651  1.00 96.22  ? 56  ALA   B O     1 
ATOM   14423 C  CB    . ALA   F 2  54  ? 24.962  81.110  15.302  1.00 92.99  ? 56  ALA   B CB    1 
ATOM   14424 N  N     . THR   F 2  55  ? 25.147  84.100  15.152  1.00 102.25 ? 57  THR   B N     1 
ATOM   14425 C  CA    . THR   F 2  55  ? 24.704  85.412  14.690  1.00 102.03 ? 57  THR   B CA    1 
ATOM   14426 C  C     . THR   F 2  55  ? 23.350  85.306  13.998  1.00 103.19 ? 57  THR   B C     1 
ATOM   14427 O  O     . THR   F 2  55  ? 23.051  84.332  13.301  1.00 99.90  ? 57  THR   B O     1 
ATOM   14428 C  CB    . THR   F 2  55  ? 25.729  86.049  13.743  1.00 110.12 ? 57  THR   B CB    1 
ATOM   14429 O  OG1   . THR   F 2  55  ? 26.751  86.712  14.504  1.00 106.90 ? 57  THR   B OG1   1 
ATOM   14430 C  CG2   . THR   F 2  55  ? 25.057  87.073  12.826  1.00 108.60 ? 57  THR   B CG2   1 
ATOM   14431 N  N     . GLY   F 2  56  ? 22.540  86.346  14.175  1.00 102.72 ? 58  GLY   B N     1 
ATOM   14432 C  CA    . GLY   F 2  56  ? 21.116  86.259  13.962  1.00 95.39  ? 58  GLY   B CA    1 
ATOM   14433 C  C     . GLY   F 2  56  ? 20.352  85.964  15.229  1.00 93.85  ? 58  GLY   B C     1 
ATOM   14434 O  O     . GLY   F 2  56  ? 19.113  85.948  15.203  1.00 86.89  ? 58  GLY   B O     1 
ATOM   14435 N  N     . ASN   F 2  57  ? 21.059  85.756  16.342  1.00 99.32  ? 59  ASN   B N     1 
ATOM   14436 C  CA    . ASN   F 2  57  ? 20.461  85.341  17.607  1.00 95.00  ? 59  ASN   B CA    1 
ATOM   14437 C  C     . ASN   F 2  57  ? 19.613  84.086  17.404  1.00 85.06  ? 59  ASN   B C     1 
ATOM   14438 O  O     . ASN   F 2  57  ? 18.468  83.989  17.851  1.00 84.80  ? 59  ASN   B O     1 
ATOM   14439 C  CB    . ASN   F 2  57  ? 19.655  86.483  18.232  1.00 95.13  ? 59  ASN   B CB    1 
ATOM   14440 C  CG    . ASN   F 2  57  ? 20.488  87.744  18.431  1.00 98.47  ? 59  ASN   B CG    1 
ATOM   14441 O  OD1   . ASN   F 2  57  ? 21.688  87.757  18.139  1.00 99.18  ? 59  ASN   B OD1   1 
ATOM   14442 N  ND2   . ASN   F 2  57  ? 19.853  88.815  18.914  1.00 82.70  ? 59  ASN   B ND2   1 
ATOM   14443 N  N     . LYS   F 2  58  ? 20.192  83.117  16.700  1.00 82.51  ? 60  LYS   B N     1 
ATOM   14444 C  CA    . LYS   F 2  58  ? 19.563  81.828  16.465  1.00 71.70  ? 60  LYS   B CA    1 
ATOM   14445 C  C     . LYS   F 2  58  ? 20.140  80.791  17.423  1.00 67.94  ? 60  LYS   B C     1 
ATOM   14446 O  O     . LYS   F 2  58  ? 21.283  80.908  17.881  1.00 65.89  ? 60  LYS   B O     1 
ATOM   14447 C  CB    . LYS   F 2  58  ? 19.746  81.384  15.009  1.00 69.53  ? 60  LYS   B CB    1 
ATOM   14448 C  CG    . LYS   F 2  58  ? 18.910  82.204  14.004  1.00 84.14  ? 60  LYS   B CG    1 
ATOM   14449 C  CD    . LYS   F 2  58  ? 18.230  81.316  12.953  1.00 79.43  ? 60  LYS   B CD    1 
ATOM   14450 C  CE    . LYS   F 2  58  ? 17.058  82.020  12.255  1.00 74.14  ? 60  LYS   B CE    1 
ATOM   14451 N  NZ    . LYS   F 2  58  ? 17.464  82.915  11.123  1.00 84.55  ? 60  LYS   B NZ    1 
ATOM   14452 N  N     . TYR   F 2  59  ? 19.325  79.789  17.748  1.00 53.03  ? 61  TYR   B N     1 
ATOM   14453 C  CA    . TYR   F 2  59  ? 19.717  78.722  18.656  1.00 42.79  ? 61  TYR   B CA    1 
ATOM   14454 C  C     . TYR   F 2  59  ? 19.752  77.395  17.916  1.00 49.02  ? 61  TYR   B C     1 
ATOM   14455 O  O     . TYR   F 2  59  ? 18.873  77.085  17.101  1.00 46.10  ? 61  TYR   B O     1 
ATOM   14456 C  CB    . TYR   F 2  59  ? 18.781  78.674  19.861  1.00 45.49  ? 61  TYR   B CB    1 
ATOM   14457 C  CG    . TYR   F 2  59  ? 18.736  80.016  20.571  1.00 51.47  ? 61  TYR   B CG    1 
ATOM   14458 C  CD1   . TYR   F 2  59  ? 19.663  80.344  21.555  1.00 50.05  ? 61  TYR   B CD1   1 
ATOM   14459 C  CD2   . TYR   F 2  59  ? 17.806  80.979  20.212  1.00 60.54  ? 61  TYR   B CD2   1 
ATOM   14460 C  CE1   . TYR   F 2  59  ? 19.641  81.586  22.181  1.00 62.04  ? 61  TYR   B CE1   1 
ATOM   14461 C  CE2   . TYR   F 2  59  ? 17.779  82.221  20.832  1.00 65.07  ? 61  TYR   B CE2   1 
ATOM   14462 C  CZ    . TYR   F 2  59  ? 18.695  82.517  21.811  1.00 62.83  ? 61  TYR   B CZ    1 
ATOM   14463 O  OH    . TYR   F 2  59  ? 18.651  83.750  22.413  1.00 67.60  ? 61  TYR   B OH    1 
ATOM   14464 N  N     . VAL   F 2  60  ? 20.805  76.633  18.159  1.00 46.38  ? 62  VAL   B N     1 
ATOM   14465 C  CA    . VAL   F 2  60  ? 21.034  75.382  17.452  1.00 49.93  ? 62  VAL   B CA    1 
ATOM   14466 C  C     . VAL   F 2  60  ? 21.159  74.282  18.501  1.00 53.95  ? 62  VAL   B C     1 
ATOM   14467 O  O     . VAL   F 2  60  ? 22.041  74.358  19.367  1.00 48.17  ? 62  VAL   B O     1 
ATOM   14468 C  CB    . VAL   F 2  60  ? 22.294  75.443  16.569  1.00 42.27  ? 62  VAL   B CB    1 
ATOM   14469 C  CG1   . VAL   F 2  60  ? 22.406  74.199  15.695  1.00 29.77  ? 62  VAL   B CG1   1 
ATOM   14470 C  CG2   . VAL   F 2  60  ? 22.312  76.719  15.739  1.00 32.09  ? 62  VAL   B CG2   1 
ATOM   14471 N  N     . PRO   F 2  61  ? 20.303  73.257  18.483  1.00 45.48  ? 63  PRO   B N     1 
ATOM   14472 C  CA    . PRO   F 2  61  ? 20.446  72.165  19.454  1.00 36.66  ? 63  PRO   B CA    1 
ATOM   14473 C  C     . PRO   F 2  61  ? 21.876  71.663  19.484  1.00 36.98  ? 63  PRO   B C     1 
ATOM   14474 O  O     . PRO   F 2  61  ? 22.474  71.399  18.445  1.00 40.49  ? 63  PRO   B O     1 
ATOM   14475 C  CB    . PRO   F 2  61  ? 19.480  71.097  18.938  1.00 28.85  ? 63  PRO   B CB    1 
ATOM   14476 C  CG    . PRO   F 2  61  ? 18.431  71.882  18.212  1.00 43.20  ? 63  PRO   B CG    1 
ATOM   14477 C  CD    . PRO   F 2  61  ? 19.148  73.066  17.590  1.00 41.66  ? 63  PRO   B CD    1 
ATOM   14478 N  N     . ARG   F 2  62  ? 22.441  71.582  20.694  1.00 45.79  ? 64  ARG   B N     1 
ATOM   14479 C  CA    . ARG   F 2  62  ? 23.748  70.975  20.899  1.00 37.78  ? 64  ARG   B CA    1 
ATOM   14480 C  C     . ARG   F 2  62  ? 23.608  69.464  20.792  1.00 38.73  ? 64  ARG   B C     1 
ATOM   14481 O  O     . ARG   F 2  62  ? 23.857  68.739  21.759  1.00 37.92  ? 64  ARG   B O     1 
ATOM   14482 C  CB    . ARG   F 2  62  ? 24.340  71.380  22.251  1.00 30.79  ? 64  ARG   B CB    1 
ATOM   14483 C  CG    . ARG   F 2  62  ? 25.857  71.088  22.345  1.00 34.80  ? 64  ARG   B CG    1 
ATOM   14484 C  CD    . ARG   F 2  62  ? 26.482  71.541  23.649  1.00 42.12  ? 64  ARG   B CD    1 
ATOM   14485 N  NE    . ARG   F 2  62  ? 26.412  72.985  23.839  1.00 43.26  ? 64  ARG   B NE    1 
ATOM   14486 C  CZ    . ARG   F 2  62  ? 25.404  73.612  24.431  1.00 47.51  ? 64  ARG   B CZ    1 
ATOM   14487 N  NH1   . ARG   F 2  62  ? 24.368  72.951  24.922  1.00 45.78  ? 64  ARG   B NH1   1 
ATOM   14488 N  NH2   . ARG   F 2  62  ? 25.433  74.937  24.532  1.00 47.56  ? 64  ARG   B NH2   1 
ATOM   14489 N  N     . ALA   F 2  63  ? 23.220  68.987  19.609  1.00 37.17  ? 65  ALA   B N     1 
ATOM   14490 C  CA    . ALA   F 2  63  ? 22.789  67.612  19.404  1.00 34.55  ? 65  ALA   B CA    1 
ATOM   14491 C  C     . ALA   F 2  63  ? 23.501  66.984  18.211  1.00 39.12  ? 65  ALA   B C     1 
ATOM   14492 O  O     . ALA   F 2  63  ? 23.771  67.647  17.202  1.00 40.80  ? 65  ALA   B O     1 
ATOM   14493 C  CB    . ALA   F 2  63  ? 21.273  67.550  19.188  1.00 41.87  ? 65  ALA   B CB    1 
ATOM   14494 N  N     . ILE   F 2  64  ? 23.769  65.684  18.330  1.00 31.78  ? 66  ILE   B N     1 
ATOM   14495 C  CA    . ILE   F 2  64  ? 24.511  64.909  17.344  1.00 29.56  ? 66  ILE   B CA    1 
ATOM   14496 C  C     . ILE   F 2  64  ? 23.658  63.711  16.969  1.00 28.67  ? 66  ILE   B C     1 
ATOM   14497 O  O     . ILE   F 2  64  ? 23.201  62.976  17.849  1.00 43.48  ? 66  ILE   B O     1 
ATOM   14498 C  CB    . ILE   F 2  64  ? 25.876  64.457  17.906  1.00 30.18  ? 66  ILE   B CB    1 
ATOM   14499 C  CG1   . ILE   F 2  64  ? 26.599  65.648  18.546  1.00 29.65  ? 66  ILE   B CG1   1 
ATOM   14500 C  CG2   . ILE   F 2  64  ? 26.735  63.782  16.834  1.00 23.84  ? 66  ILE   B CG2   1 
ATOM   14501 C  CD1   . ILE   F 2  64  ? 27.985  65.313  19.128  1.00 34.63  ? 66  ILE   B CD1   1 
ATOM   14502 N  N     . LEU   F 2  65  ? 23.444  63.507  15.679  1.00 37.28  ? 67  LEU   B N     1 
ATOM   14503 C  CA    . LEU   F 2  65  ? 22.519  62.492  15.183  1.00 37.77  ? 67  LEU   B CA    1 
ATOM   14504 C  C     . LEU   F 2  65  ? 23.294  61.373  14.498  1.00 36.67  ? 67  LEU   B C     1 
ATOM   14505 O  O     . LEU   F 2  65  ? 23.939  61.608  13.472  1.00 37.38  ? 67  LEU   B O     1 
ATOM   14506 C  CB    . LEU   F 2  65  ? 21.513  63.123  14.221  1.00 29.97  ? 67  LEU   B CB    1 
ATOM   14507 C  CG    . LEU   F 2  65  ? 20.748  64.310  14.819  1.00 35.63  ? 67  LEU   B CG    1 
ATOM   14508 C  CD1   . LEU   F 2  65  ? 21.598  65.587  14.704  1.00 42.70  ? 67  LEU   B CD1   1 
ATOM   14509 C  CD2   . LEU   F 2  65  ? 19.365  64.506  14.184  1.00 22.93  ? 67  LEU   B CD2   1 
ATOM   14510 N  N     . VAL   F 2  66  ? 23.205  60.154  15.040  1.00 34.72  ? 68  VAL   B N     1 
ATOM   14511 C  CA    . VAL   F 2  66  ? 23.988  59.015  14.555  1.00 33.52  ? 68  VAL   B CA    1 
ATOM   14512 C  C     . VAL   F 2  66  ? 23.088  57.834  14.186  1.00 30.15  ? 68  VAL   B C     1 
ATOM   14513 O  O     . VAL   F 2  66  ? 22.250  57.416  14.988  1.00 36.19  ? 68  VAL   B O     1 
ATOM   14514 C  CB    . VAL   F 2  66  ? 25.021  58.584  15.603  1.00 29.35  ? 68  VAL   B CB    1 
ATOM   14515 C  CG1   . VAL   F 2  66  ? 25.675  57.278  15.182  1.00 34.93  ? 68  VAL   B CG1   1 
ATOM   14516 C  CG2   . VAL   F 2  66  ? 26.051  59.669  15.768  1.00 39.69  ? 68  VAL   B CG2   1 
ATOM   14517 N  N     . ASP   F 2  67  ? 23.285  57.277  12.985  1.00 34.32  ? 69  ASP   B N     1 
ATOM   14518 C  CA    . ASP   F 2  67  ? 22.727  55.972  12.633  1.00 28.22  ? 69  ASP   B CA    1 
ATOM   14519 C  C     . ASP   F 2  67  ? 23.657  55.242  11.676  1.00 34.29  ? 69  ASP   B C     1 
ATOM   14520 O  O     . ASP   F 2  67  ? 24.399  55.857  10.908  1.00 29.03  ? 69  ASP   B O     1 
ATOM   14521 C  CB    . ASP   F 2  67  ? 21.350  56.081  11.984  1.00 27.66  ? 69  ASP   B CB    1 
ATOM   14522 C  CG    . ASP   F 2  67  ? 20.417  54.968  12.397  1.00 33.88  ? 69  ASP   B CG    1 
ATOM   14523 O  OD1   . ASP   F 2  67  ? 20.894  53.880  12.808  1.00 35.82  ? 69  ASP   B OD1   1 
ATOM   14524 O  OD2   . ASP   F 2  67  ? 19.186  55.187  12.299  1.00 40.58  ? 69  ASP   B OD2   1 
ATOM   14525 N  N     . LEU   F 2  68  ? 23.594  53.914  11.709  1.00 40.27  ? 70  LEU   B N     1 
ATOM   14526 C  CA    . LEU   F 2  68  ? 24.381  53.136  10.765  1.00 37.19  ? 70  LEU   B CA    1 
ATOM   14527 C  C     . LEU   F 2  68  ? 23.736  53.048  9.390   1.00 36.73  ? 70  LEU   B C     1 
ATOM   14528 O  O     . LEU   F 2  68  ? 24.356  52.497  8.476   1.00 38.74  ? 70  LEU   B O     1 
ATOM   14529 C  CB    . LEU   F 2  68  ? 24.638  51.728  11.314  1.00 30.22  ? 70  LEU   B CB    1 
ATOM   14530 C  CG    . LEU   F 2  68  ? 25.889  51.623  12.203  1.00 30.50  ? 70  LEU   B CG    1 
ATOM   14531 C  CD1   . LEU   F 2  68  ? 26.212  50.182  12.608  1.00 29.39  ? 70  LEU   B CD1   1 
ATOM   14532 C  CD2   . LEU   F 2  68  ? 27.088  52.252  11.554  1.00 24.28  ? 70  LEU   B CD2   1 
ATOM   14533 N  N     . GLU   F 2  69  ? 22.525  53.574  9.224   1.00 48.22  ? 71  GLU   B N     1 
ATOM   14534 C  CA    . GLU   F 2  69  ? 21.837  53.607  7.941   1.00 45.89  ? 71  GLU   B CA    1 
ATOM   14535 C  C     . GLU   F 2  69  ? 21.163  54.953  7.724   1.00 41.94  ? 71  GLU   B C     1 
ATOM   14536 O  O     . GLU   F 2  69  ? 20.970  55.726  8.671   1.00 47.21  ? 71  GLU   B O     1 
ATOM   14537 C  CB    . GLU   F 2  69  ? 20.806  52.484  7.844   1.00 49.05  ? 71  GLU   B CB    1 
ATOM   14538 C  CG    . GLU   F 2  69  ? 19.761  52.528  8.909   1.00 41.10  ? 71  GLU   B CG    1 
ATOM   14539 C  CD    . GLU   F 2  69  ? 18.561  51.723  8.491   1.00 55.68  ? 71  GLU   B CD    1 
ATOM   14540 O  OE1   . GLU   F 2  69  ? 18.400  51.490  7.264   1.00 50.90  ? 71  GLU   B OE1   1 
ATOM   14541 O  OE2   . GLU   F 2  69  ? 17.789  51.324  9.380   1.00 53.77  ? 71  GLU   B OE2   1 
ATOM   14542 N  N     . PRO   F 2  70  ? 20.766  55.250  6.498   1.00 47.29  ? 72  PRO   B N     1 
ATOM   14543 C  CA    . PRO   F 2  70  ? 20.526  56.647  6.119   1.00 47.05  ? 72  PRO   B CA    1 
ATOM   14544 C  C     . PRO   F 2  70  ? 19.094  57.128  6.304   1.00 56.78  ? 72  PRO   B C     1 
ATOM   14545 O  O     . PRO   F 2  70  ? 18.863  58.338  6.378   1.00 59.17  ? 72  PRO   B O     1 
ATOM   14546 C  CB    . PRO   F 2  70  ? 20.928  56.659  4.645   1.00 49.08  ? 72  PRO   B CB    1 
ATOM   14547 C  CG    . PRO   F 2  70  ? 20.472  55.320  4.182   1.00 63.44  ? 72  PRO   B CG    1 
ATOM   14548 C  CD    . PRO   F 2  70  ? 20.636  54.352  5.343   1.00 56.44  ? 72  PRO   B CD    1 
ATOM   14549 N  N     . GLY   F 2  71  ? 18.116  56.230  6.385   1.00 58.26  ? 73  GLY   B N     1 
ATOM   14550 C  CA    . GLY   F 2  71  ? 16.783  56.697  6.718   1.00 39.58  ? 73  GLY   B CA    1 
ATOM   14551 C  C     . GLY   F 2  71  ? 16.824  57.439  8.035   1.00 62.44  ? 73  GLY   B C     1 
ATOM   14552 O  O     . GLY   F 2  71  ? 17.890  57.906  8.451   1.00 66.04  ? 73  GLY   B O     1 
ATOM   14553 N  N     . THR   F 2  72  ? 15.694  57.531  8.734   1.00 65.30  ? 74  THR   B N     1 
ATOM   14554 C  CA    . THR   F 2  72  ? 15.667  58.220  10.025  1.00 59.64  ? 74  THR   B CA    1 
ATOM   14555 C  C     . THR   F 2  72  ? 16.344  59.592  9.953   1.00 57.96  ? 74  THR   B C     1 
ATOM   14556 O  O     . THR   F 2  72  ? 15.687  60.608  10.196  1.00 68.91  ? 74  THR   B O     1 
ATOM   14557 C  CB    . THR   F 2  72  ? 16.300  57.358  11.126  1.00 54.91  ? 74  THR   B CB    1 
ATOM   14558 O  OG1   . THR   F 2  72  ? 17.553  56.784  10.679  1.00 48.96  ? 74  THR   B OG1   1 
ATOM   14559 C  CG2   . THR   F 2  72  ? 15.305  56.275  11.586  1.00 34.17  ? 74  THR   B CG2   1 
ATOM   14560 N  N     . MET   F 2  73  ? 17.642  59.651  9.634   1.00 54.28  ? 75  MET   B N     1 
ATOM   14561 C  CA    . MET   F 2  73  ? 18.257  60.937  9.305   1.00 62.60  ? 75  MET   B CA    1 
ATOM   14562 C  C     . MET   F 2  73  ? 17.382  61.713  8.322   1.00 60.92  ? 75  MET   B C     1 
ATOM   14563 O  O     . MET   F 2  73  ? 16.959  62.843  8.602   1.00 57.10  ? 75  MET   B O     1 
ATOM   14564 C  CB    . MET   F 2  73  ? 19.671  60.735  8.734   1.00 63.44  ? 75  MET   B CB    1 
ATOM   14565 C  CG    . MET   F 2  73  ? 20.532  59.688  9.498   1.00 79.63  ? 75  MET   B CG    1 
ATOM   14566 S  SD    . MET   F 2  73  ? 21.133  60.116  11.167  1.00 61.33  ? 75  MET   B SD    1 
ATOM   14567 C  CE    . MET   F 2  73  ? 22.401  61.310  10.740  1.00 50.71  ? 75  MET   B CE    1 
ATOM   14568 N  N     . ASP   F 2  74  ? 17.087  61.108  7.165   1.00 53.46  ? 76  ASP   B N     1 
ATOM   14569 C  CA    . ASP   F 2  74  ? 16.126  61.698  6.238   1.00 53.08  ? 76  ASP   B CA    1 
ATOM   14570 C  C     . ASP   F 2  74  ? 14.802  61.974  6.924   1.00 53.98  ? 76  ASP   B C     1 
ATOM   14571 O  O     . ASP   F 2  74  ? 14.247  63.071  6.827   1.00 57.62  ? 76  ASP   B O     1 
ATOM   14572 C  CB    . ASP   F 2  74  ? 15.911  60.770  5.051   1.00 52.16  ? 76  ASP   B CB    1 
ATOM   14573 C  CG    . ASP   F 2  74  ? 17.192  60.414  4.381   1.00 60.16  ? 76  ASP   B CG    1 
ATOM   14574 O  OD1   . ASP   F 2  74  ? 18.221  61.014  4.770   1.00 55.55  ? 76  ASP   B OD1   1 
ATOM   14575 O  OD2   . ASP   F 2  74  ? 17.173  59.541  3.482   1.00 65.99  ? 76  ASP   B OD2   1 
ATOM   14576 N  N     . SER   F 2  75  ? 14.270  60.973  7.615   1.00 54.63  ? 77  SER   B N     1 
ATOM   14577 C  CA    . SER   F 2  75  ? 13.023  61.166  8.337   1.00 53.44  ? 77  SER   B CA    1 
ATOM   14578 C  C     . SER   F 2  75  ? 13.098  62.384  9.250   1.00 53.14  ? 77  SER   B C     1 
ATOM   14579 O  O     . SER   F 2  75  ? 12.177  63.205  9.283   1.00 61.90  ? 77  SER   B O     1 
ATOM   14580 C  CB    . SER   F 2  75  ? 12.697  59.905  9.132   1.00 56.60  ? 77  SER   B CB    1 
ATOM   14581 O  OG    . SER   F 2  75  ? 11.312  59.819  9.384   1.00 73.74  ? 77  SER   B OG    1 
ATOM   14582 N  N     . VAL   F 2  76  ? 14.202  62.528  9.985   1.00 52.35  ? 78  VAL   B N     1 
ATOM   14583 C  CA    . VAL   F 2  76  ? 14.333  63.627  10.937  1.00 52.86  ? 78  VAL   B CA    1 
ATOM   14584 C  C     . VAL   F 2  76  ? 14.578  64.947  10.220  1.00 55.93  ? 78  VAL   B C     1 
ATOM   14585 O  O     . VAL   F 2  76  ? 14.022  65.982  10.606  1.00 56.25  ? 78  VAL   B O     1 
ATOM   14586 C  CB    . VAL   F 2  76  ? 15.451  63.338  11.952  1.00 60.34  ? 78  VAL   B CB    1 
ATOM   14587 C  CG1   . VAL   F 2  76  ? 15.577  64.500  12.936  1.00 51.59  ? 78  VAL   B CG1   1 
ATOM   14588 C  CG2   . VAL   F 2  76  ? 15.181  62.036  12.682  1.00 51.90  ? 78  VAL   B CG2   1 
ATOM   14589 N  N     . ARG   F 2  77  ? 15.430  64.946  9.183   1.00 61.75  ? 79  ARG   B N     1 
ATOM   14590 C  CA    . ARG   F 2  77  ? 15.680  66.182  8.438   1.00 54.92  ? 79  ARG   B CA    1 
ATOM   14591 C  C     . ARG   F 2  77  ? 14.388  66.743  7.870   1.00 56.55  ? 79  ARG   B C     1 
ATOM   14592 O  O     . ARG   F 2  77  ? 14.200  67.965  7.824   1.00 60.11  ? 79  ARG   B O     1 
ATOM   14593 C  CB    . ARG   F 2  77  ? 16.686  65.947  7.316   1.00 41.97  ? 79  ARG   B CB    1 
ATOM   14594 C  CG    . ARG   F 2  77  ? 17.502  67.187  6.949   1.00 50.51  ? 79  ARG   B CG    1 
ATOM   14595 C  CD    . ARG   F 2  77  ? 18.455  66.913  5.788   1.00 48.09  ? 79  ARG   B CD    1 
ATOM   14596 N  NE    . ARG   F 2  77  ? 19.022  65.574  5.896   1.00 64.47  ? 79  ARG   B NE    1 
ATOM   14597 C  CZ    . ARG   F 2  77  ? 20.185  65.289  6.466   1.00 63.18  ? 79  ARG   B CZ    1 
ATOM   14598 N  NH1   . ARG   F 2  77  ? 20.986  66.246  6.927   1.00 52.67  ? 79  ARG   B NH1   1 
ATOM   14599 N  NH2   . ARG   F 2  77  ? 20.560  64.013  6.568   1.00 56.31  ? 79  ARG   B NH2   1 
ATOM   14600 N  N     . SER   F 2  78  ? 13.482  65.861  7.443   1.00 46.43  ? 80  SER   B N     1 
ATOM   14601 C  CA    . SER   F 2  78  ? 12.183  66.233  6.904   1.00 55.82  ? 80  SER   B CA    1 
ATOM   14602 C  C     . SER   F 2  78  ? 11.069  66.101  7.937   1.00 66.50  ? 80  SER   B C     1 
ATOM   14603 O  O     . SER   F 2  78  ? 9.912   65.861  7.580   1.00 60.84  ? 80  SER   B O     1 
ATOM   14604 C  CB    . SER   F 2  78  ? 11.876  65.390  5.673   1.00 66.16  ? 80  SER   B CB    1 
ATOM   14605 O  OG    . SER   F 2  78  ? 12.509  64.127  5.783   1.00 72.80  ? 80  SER   B OG    1 
ATOM   14606 N  N     . GLY   F 2  79  ? 11.402  66.243  9.219   1.00 72.86  ? 81  GLY   B N     1 
ATOM   14607 C  CA    . GLY   F 2  79  ? 10.415  66.320  10.269  1.00 63.20  ? 81  GLY   B CA    1 
ATOM   14608 C  C     . GLY   F 2  79  ? 10.141  67.765  10.630  1.00 66.07  ? 81  GLY   B C     1 
ATOM   14609 O  O     . GLY   F 2  79  ? 10.715  68.691  10.043  1.00 63.38  ? 81  GLY   B O     1 
ATOM   14610 N  N     . PRO   F 2  80  ? 9.261   67.989  11.614  1.00 68.86  ? 82  PRO   B N     1 
ATOM   14611 C  CA    . PRO   F 2  80  ? 8.868   69.366  11.953  1.00 65.91  ? 82  PRO   B CA    1 
ATOM   14612 C  C     . PRO   F 2  80  ? 10.066  70.269  12.197  1.00 68.91  ? 82  PRO   B C     1 
ATOM   14613 O  O     . PRO   F 2  80  ? 10.311  71.209  11.428  1.00 69.31  ? 82  PRO   B O     1 
ATOM   14614 C  CB    . PRO   F 2  80  ? 8.019   69.193  13.224  1.00 65.40  ? 82  PRO   B CB    1 
ATOM   14615 C  CG    . PRO   F 2  80  ? 8.341   67.822  13.748  1.00 62.58  ? 82  PRO   B CG    1 
ATOM   14616 C  CD    . PRO   F 2  80  ? 8.665   67.000  12.529  1.00 69.59  ? 82  PRO   B CD    1 
ATOM   14617 N  N     . PHE   F 2  81  ? 10.825  69.994  13.260  1.00 56.97  ? 83  PHE   B N     1 
ATOM   14618 C  CA    . PHE   F 2  81  ? 11.990  70.803  13.592  1.00 56.06  ? 83  PHE   B CA    1 
ATOM   14619 C  C     . PHE   F 2  81  ? 13.241  70.317  12.882  1.00 55.23  ? 83  PHE   B C     1 
ATOM   14620 O  O     . PHE   F 2  81  ? 14.355  70.581  13.352  1.00 54.92  ? 83  PHE   B O     1 
ATOM   14621 C  CB    . PHE   F 2  81  ? 12.215  70.828  15.112  1.00 54.06  ? 83  PHE   B CB    1 
ATOM   14622 C  CG    . PHE   F 2  81  ? 11.266  71.733  15.867  1.00 47.33  ? 83  PHE   B CG    1 
ATOM   14623 C  CD1   . PHE   F 2  81  ? 9.892   71.606  15.726  1.00 48.52  ? 83  PHE   B CD1   1 
ATOM   14624 C  CD2   . PHE   F 2  81  ? 11.748  72.699  16.729  1.00 54.68  ? 83  PHE   B CD2   1 
ATOM   14625 C  CE1   . PHE   F 2  81  ? 9.023   72.437  16.421  1.00 48.86  ? 83  PHE   B CE1   1 
ATOM   14626 C  CE2   . PHE   F 2  81  ? 10.876  73.529  17.433  1.00 49.96  ? 83  PHE   B CE2   1 
ATOM   14627 C  CZ    . PHE   F 2  81  ? 9.517   73.395  17.272  1.00 41.73  ? 83  PHE   B CZ    1 
ATOM   14628 N  N     . GLY   F 2  82  ? 13.082  69.620  11.756  1.00 50.03  ? 84  GLY   B N     1 
ATOM   14629 C  CA    . GLY   F 2  82  ? 14.225  69.006  11.115  1.00 46.38  ? 84  GLY   B CA    1 
ATOM   14630 C  C     . GLY   F 2  82  ? 15.329  69.990  10.802  1.00 47.55  ? 84  GLY   B C     1 
ATOM   14631 O  O     . GLY   F 2  82  ? 16.512  69.640  10.851  1.00 49.03  ? 84  GLY   B O     1 
ATOM   14632 N  N     . GLN   F 2  83  ? 14.968  71.232  10.498  1.00 51.69  ? 85  GLN   B N     1 
ATOM   14633 C  CA    . GLN   F 2  83  ? 15.950  72.161  9.967   1.00 50.73  ? 85  GLN   B CA    1 
ATOM   14634 C  C     . GLN   F 2  83  ? 16.809  72.832  11.036  1.00 57.54  ? 85  GLN   B C     1 
ATOM   14635 O  O     . GLN   F 2  83  ? 17.773  73.515  10.669  1.00 55.80  ? 85  GLN   B O     1 
ATOM   14636 C  CB    . GLN   F 2  83  ? 15.251  73.217  9.105   1.00 58.56  ? 85  GLN   B CB    1 
ATOM   14637 C  CG    . GLN   F 2  83  ? 13.909  73.716  9.635   1.00 71.48  ? 85  GLN   B CG    1 
ATOM   14638 C  CD    . GLN   F 2  83  ? 13.394  74.960  8.882   1.00 80.14  ? 85  GLN   B CD    1 
ATOM   14639 O  OE1   . GLN   F 2  83  ? 14.178  75.825  8.482   1.00 59.88  ? 85  GLN   B OE1   1 
ATOM   14640 N  NE2   . GLN   F 2  83  ? 12.071  75.047  8.700   1.00 79.27  ? 85  GLN   B NE2   1 
ATOM   14641 N  N     . ILE   F 2  84  ? 16.520  72.649  12.333  1.00 50.96  ? 86  ILE   B N     1 
ATOM   14642 C  CA    . ILE   F 2  84  ? 17.311  73.374  13.330  1.00 59.43  ? 86  ILE   B CA    1 
ATOM   14643 C  C     . ILE   F 2  84  ? 18.663  72.723  13.563  1.00 58.43  ? 86  ILE   B C     1 
ATOM   14644 O  O     . ILE   F 2  84  ? 19.625  73.414  13.920  1.00 53.63  ? 86  ILE   B O     1 
ATOM   14645 C  CB    . ILE   F 2  84  ? 16.596  73.544  14.685  1.00 59.00  ? 86  ILE   B CB    1 
ATOM   14646 C  CG1   . ILE   F 2  84  ? 15.823  72.299  15.098  1.00 53.14  ? 86  ILE   B CG1   1 
ATOM   14647 C  CG2   . ILE   F 2  84  ? 15.737  74.792  14.697  1.00 66.06  ? 86  ILE   B CG2   1 
ATOM   14648 C  CD1   . ILE   F 2  84  ? 14.986  72.562  16.314  1.00 51.77  ? 86  ILE   B CD1   1 
ATOM   14649 N  N     . PHE   F 2  85  ? 18.776  71.410  13.397  1.00 49.07  ? 87  PHE   B N     1 
ATOM   14650 C  CA    . PHE   F 2  85  ? 20.033  70.756  13.726  1.00 47.97  ? 87  PHE   B CA    1 
ATOM   14651 C  C     . PHE   F 2  85  ? 21.139  71.204  12.770  1.00 43.40  ? 87  PHE   B C     1 
ATOM   14652 O  O     . PHE   F 2  85  ? 20.952  71.235  11.551  1.00 54.67  ? 87  PHE   B O     1 
ATOM   14653 C  CB    . PHE   F 2  85  ? 19.861  69.237  13.698  1.00 43.56  ? 87  PHE   B CB    1 
ATOM   14654 C  CG    . PHE   F 2  85  ? 18.835  68.724  14.677  1.00 39.63  ? 87  PHE   B CG    1 
ATOM   14655 C  CD1   . PHE   F 2  85  ? 19.140  68.604  16.027  1.00 38.20  ? 87  PHE   B CD1   1 
ATOM   14656 C  CD2   . PHE   F 2  85  ? 17.566  68.345  14.245  1.00 46.07  ? 87  PHE   B CD2   1 
ATOM   14657 C  CE1   . PHE   F 2  85  ? 18.197  68.133  16.934  1.00 37.49  ? 87  PHE   B CE1   1 
ATOM   14658 C  CE2   . PHE   F 2  85  ? 16.615  67.871  15.148  1.00 38.27  ? 87  PHE   B CE2   1 
ATOM   14659 C  CZ    . PHE   F 2  85  ? 16.935  67.764  16.493  1.00 36.16  ? 87  PHE   B CZ    1 
ATOM   14660 N  N     . ARG   F 2  86  ? 22.277  71.591  13.332  1.00 34.72  ? 88  ARG   B N     1 
ATOM   14661 C  CA    . ARG   F 2  86  ? 23.516  71.760  12.589  1.00 38.35  ? 88  ARG   B CA    1 
ATOM   14662 C  C     . ARG   F 2  86  ? 23.683  70.617  11.584  1.00 52.59  ? 88  ARG   B C     1 
ATOM   14663 O  O     . ARG   F 2  86  ? 23.755  69.449  11.991  1.00 54.43  ? 88  ARG   B O     1 
ATOM   14664 C  CB    . ARG   F 2  86  ? 24.689  71.805  13.571  1.00 39.56  ? 88  ARG   B CB    1 
ATOM   14665 C  CG    . ARG   F 2  86  ? 26.037  72.062  12.931  1.00 52.22  ? 88  ARG   B CG    1 
ATOM   14666 C  CD    . ARG   F 2  86  ? 27.170  72.275  13.954  1.00 55.29  ? 88  ARG   B CD    1 
ATOM   14667 N  NE    . ARG   F 2  86  ? 28.434  72.496  13.252  1.00 84.11  ? 88  ARG   B NE    1 
ATOM   14668 C  CZ    . ARG   F 2  86  ? 29.353  71.562  13.015  1.00 87.22  ? 88  ARG   B CZ    1 
ATOM   14669 N  NH1   . ARG   F 2  86  ? 29.270  70.348  13.553  1.00 71.19  ? 88  ARG   B NH1   1 
ATOM   14670 N  NH2   . ARG   F 2  86  ? 30.380  71.850  12.212  1.00 72.61  ? 88  ARG   B NH2   1 
ATOM   14671 N  N     . PRO   F 2  87  ? 23.749  70.903  10.273  1.00 52.33  ? 89  PRO   B N     1 
ATOM   14672 C  CA    . PRO   F 2  87  ? 23.852  69.809  9.285   1.00 52.33  ? 89  PRO   B CA    1 
ATOM   14673 C  C     . PRO   F 2  87  ? 25.085  68.936  9.438   1.00 51.16  ? 89  PRO   B C     1 
ATOM   14674 O  O     . PRO   F 2  87  ? 24.986  67.718  9.278   1.00 54.34  ? 89  PRO   B O     1 
ATOM   14675 C  CB    . PRO   F 2  87  ? 23.864  70.557  7.948   1.00 50.47  ? 89  PRO   B CB    1 
ATOM   14676 C  CG    . PRO   F 2  87  ? 23.150  71.823  8.225   1.00 48.40  ? 89  PRO   B CG    1 
ATOM   14677 C  CD    . PRO   F 2  87  ? 23.593  72.207  9.610   1.00 55.69  ? 89  PRO   B CD    1 
ATOM   14678 N  N     . ASP   F 2  88  ? 26.247  69.513  9.743   1.00 57.69  ? 90  ASP   B N     1 
ATOM   14679 C  CA    . ASP   F 2  88  ? 27.446  68.708  9.958   1.00 52.77  ? 90  ASP   B CA    1 
ATOM   14680 C  C     . ASP   F 2  88  ? 27.324  67.747  11.131  1.00 60.14  ? 90  ASP   B C     1 
ATOM   14681 O  O     . ASP   F 2  88  ? 28.231  66.930  11.339  1.00 59.47  ? 90  ASP   B O     1 
ATOM   14682 C  CB    . ASP   F 2  88  ? 28.644  69.614  10.190  1.00 62.17  ? 90  ASP   B CB    1 
ATOM   14683 C  CG    . ASP   F 2  88  ? 29.115  70.268  8.925   1.00 71.93  ? 90  ASP   B CG    1 
ATOM   14684 O  OD1   . ASP   F 2  88  ? 28.888  69.683  7.835   1.00 56.54  ? 90  ASP   B OD1   1 
ATOM   14685 O  OD2   . ASP   F 2  88  ? 29.717  71.359  9.032   1.00 74.25  ? 90  ASP   B OD2   1 
ATOM   14686 N  N     . ASN   F 2  89  ? 26.251  67.844  11.914  1.00 59.34  ? 91  ASN   B N     1 
ATOM   14687 C  CA    . ASN   F 2  89  ? 26.044  67.002  13.082  1.00 47.60  ? 91  ASN   B CA    1 
ATOM   14688 C  C     . ASN   F 2  89  ? 25.249  65.740  12.759  1.00 53.54  ? 91  ASN   B C     1 
ATOM   14689 O  O     . ASN   F 2  89  ? 25.040  64.906  13.649  1.00 40.05  ? 91  ASN   B O     1 
ATOM   14690 C  CB    . ASN   F 2  89  ? 25.342  67.810  14.173  1.00 42.56  ? 91  ASN   B CB    1 
ATOM   14691 C  CG    . ASN   F 2  89  ? 26.288  68.701  14.937  1.00 44.48  ? 91  ASN   B CG    1 
ATOM   14692 O  OD1   . ASN   F 2  89  ? 27.373  69.033  14.468  1.00 48.85  ? 91  ASN   B OD1   1 
ATOM   14693 N  ND2   . ASN   F 2  89  ? 25.888  69.079  16.137  1.00 38.74  ? 91  ASN   B ND2   1 
ATOM   14694 N  N     . PHE   F 2  90  ? 24.779  65.592  11.518  1.00 49.13  ? 92  PHE   B N     1 
ATOM   14695 C  CA    . PHE   F 2  90  ? 24.252  64.315  11.056  1.00 42.11  ? 92  PHE   B CA    1 
ATOM   14696 C  C     . PHE   F 2  90  ? 25.431  63.445  10.660  1.00 38.89  ? 92  PHE   B C     1 
ATOM   14697 O  O     . PHE   F 2  90  ? 26.138  63.757  9.700   1.00 51.67  ? 92  PHE   B O     1 
ATOM   14698 C  CB    . PHE   F 2  90  ? 23.320  64.494  9.869   1.00 34.19  ? 92  PHE   B CB    1 
ATOM   14699 C  CG    . PHE   F 2  90  ? 21.999  65.106  10.199  1.00 36.32  ? 92  PHE   B CG    1 
ATOM   14700 C  CD1   . PHE   F 2  90  ? 21.901  66.438  10.544  1.00 38.37  ? 92  PHE   B CD1   1 
ATOM   14701 C  CD2   . PHE   F 2  90  ? 20.832  64.362  10.086  1.00 42.56  ? 92  PHE   B CD2   1 
ATOM   14702 C  CE1   . PHE   F 2  90  ? 20.662  67.008  10.807  1.00 35.36  ? 92  PHE   B CE1   1 
ATOM   14703 C  CE2   . PHE   F 2  90  ? 19.597  64.929  10.337  1.00 37.41  ? 92  PHE   B CE2   1 
ATOM   14704 C  CZ    . PHE   F 2  90  ? 19.518  66.255  10.701  1.00 37.46  ? 92  PHE   B CZ    1 
ATOM   14705 N  N     . VAL   F 2  91  ? 25.654  62.367  11.399  1.00 43.35  ? 93  VAL   B N     1 
ATOM   14706 C  CA    . VAL   F 2  91  ? 26.687  61.384  11.089  1.00 44.80  ? 93  VAL   B CA    1 
ATOM   14707 C  C     . VAL   F 2  91  ? 25.996  60.045  10.848  1.00 50.96  ? 93  VAL   B C     1 
ATOM   14708 O  O     . VAL   F 2  91  ? 25.403  59.467  11.770  1.00 44.82  ? 93  VAL   B O     1 
ATOM   14709 C  CB    . VAL   F 2  91  ? 27.718  61.275  12.212  1.00 40.63  ? 93  VAL   B CB    1 
ATOM   14710 C  CG1   . VAL   F 2  91  ? 28.704  60.202  11.902  1.00 33.61  ? 93  VAL   B CG1   1 
ATOM   14711 C  CG2   . VAL   F 2  91  ? 28.403  62.610  12.408  1.00 46.57  ? 93  VAL   B CG2   1 
ATOM   14712 N  N     . PHE   F 2  92  ? 26.056  59.550  9.613   1.00 51.28  ? 94  PHE   B N     1 
ATOM   14713 C  CA    . PHE   F 2  92  ? 25.371  58.308  9.291   1.00 55.08  ? 94  PHE   B CA    1 
ATOM   14714 C  C     . PHE   F 2  92  ? 26.163  57.491  8.273   1.00 42.01  ? 94  PHE   B C     1 
ATOM   14715 O  O     . PHE   F 2  92  ? 26.911  58.033  7.456   1.00 52.59  ? 94  PHE   B O     1 
ATOM   14716 C  CB    . PHE   F 2  92  ? 23.939  58.590  8.787   1.00 55.67  ? 94  PHE   B CB    1 
ATOM   14717 C  CG    . PHE   F 2  92  ? 23.866  59.558  7.636   1.00 62.30  ? 94  PHE   B CG    1 
ATOM   14718 C  CD1   . PHE   F 2  92  ? 24.149  59.143  6.337   1.00 57.15  ? 94  PHE   B CD1   1 
ATOM   14719 C  CD2   . PHE   F 2  92  ? 23.476  60.878  7.845   1.00 70.97  ? 94  PHE   B CD2   1 
ATOM   14720 C  CE1   . PHE   F 2  92  ? 24.065  60.031  5.276   1.00 63.23  ? 94  PHE   B CE1   1 
ATOM   14721 C  CE2   . PHE   F 2  92  ? 23.383  61.778  6.783   1.00 61.12  ? 94  PHE   B CE2   1 
ATOM   14722 C  CZ    . PHE   F 2  92  ? 23.680  61.350  5.497   1.00 71.50  ? 94  PHE   B CZ    1 
ATOM   14723 N  N     . GLY   F 2  93  ? 25.998  56.174  8.353   1.00 36.64  ? 95  GLY   B N     1 
ATOM   14724 C  CA    . GLY   F 2  93  ? 26.507  55.233  7.374   1.00 41.78  ? 95  GLY   B CA    1 
ATOM   14725 C  C     . GLY   F 2  93  ? 25.421  54.725  6.438   1.00 42.20  ? 95  GLY   B C     1 
ATOM   14726 O  O     . GLY   F 2  93  ? 24.389  55.374  6.228   1.00 43.66  ? 95  GLY   B O     1 
ATOM   14727 N  N     . GLN   F 2  94  ? 25.655  53.522  5.872   1.00 42.28  ? 96  GLN   B N     1 
ATOM   14728 C  CA    . GLN   F 2  94  ? 24.822  52.957  4.805   1.00 41.93  ? 96  GLN   B CA    1 
ATOM   14729 C  C     . GLN   F 2  94  ? 24.434  51.514  5.050   1.00 35.07  ? 96  GLN   B C     1 
ATOM   14730 O  O     . GLN   F 2  94  ? 23.331  51.104  4.695   1.00 49.78  ? 96  GLN   B O     1 
ATOM   14731 C  CB    . GLN   F 2  94  ? 25.558  53.050  3.450   1.00 47.04  ? 96  GLN   B CB    1 
ATOM   14732 C  CG    . GLN   F 2  94  ? 25.526  54.422  2.784   1.00 48.21  ? 96  GLN   B CG    1 
ATOM   14733 C  CD    . GLN   F 2  94  ? 24.119  54.852  2.410   1.00 56.34  ? 96  GLN   B CD    1 
ATOM   14734 O  OE1   . GLN   F 2  94  ? 23.296  54.031  2.001   1.00 47.34  ? 96  GLN   B OE1   1 
ATOM   14735 N  NE2   . GLN   F 2  94  ? 23.832  56.146  2.559   1.00 62.58  ? 96  GLN   B NE2   1 
ATOM   14736 N  N     . SER   F 2  95  ? 25.326  50.733  5.640   1.00 46.68  ? 97  SER   B N     1 
ATOM   14737 C  CA    . SER   F 2  95  ? 25.094  49.309  5.840   1.00 48.01  ? 97  SER   B CA    1 
ATOM   14738 C  C     . SER   F 2  95  ? 23.835  49.039  6.665   1.00 47.28  ? 97  SER   B C     1 
ATOM   14739 O  O     . SER   F 2  95  ? 23.034  48.163  6.321   1.00 57.17  ? 97  SER   B O     1 
ATOM   14740 C  CB    . SER   F 2  95  ? 26.314  48.714  6.538   1.00 53.00  ? 97  SER   B CB    1 
ATOM   14741 O  OG    . SER   F 2  95  ? 26.639  49.515  7.683   1.00 43.37  ? 97  SER   B OG    1 
ATOM   14742 N  N     . GLY   F 2  96  ? 23.669  49.737  7.786   1.00 34.63  ? 98  GLY   B N     1 
ATOM   14743 C  CA    . GLY   F 2  96  ? 22.757  49.294  8.818   1.00 37.77  ? 98  GLY   B CA    1 
ATOM   14744 C  C     . GLY   F 2  96  ? 23.403  48.306  9.786   1.00 33.20  ? 98  GLY   B C     1 
ATOM   14745 O  O     . GLY   F 2  96  ? 24.548  47.879  9.636   1.00 31.28  ? 98  GLY   B O     1 
ATOM   14746 N  N     . ALA   F 2  97  ? 22.654  47.945  10.820  1.00 29.55  ? 99  ALA   B N     1 
ATOM   14747 C  CA    . ALA   F 2  97  ? 23.155  46.971  11.782  1.00 23.26  ? 99  ALA   B CA    1 
ATOM   14748 C  C     . ALA   F 2  97  ? 22.231  45.769  11.946  1.00 25.84  ? 99  ALA   B C     1 
ATOM   14749 O  O     . ALA   F 2  97  ? 22.507  44.905  12.796  1.00 27.53  ? 99  ALA   B O     1 
ATOM   14750 C  CB    . ALA   F 2  97  ? 23.415  47.631  13.137  1.00 25.95  ? 99  ALA   B CB    1 
ATOM   14751 N  N     . GLY   F 2  98  ? 21.161  45.682  11.154  1.00 22.33  ? 100 GLY   B N     1 
ATOM   14752 C  CA    . GLY   F 2  98  ? 20.337  44.477  11.145  1.00 13.54  ? 100 GLY   B CA    1 
ATOM   14753 C  C     . GLY   F 2  98  ? 19.934  43.976  12.520  1.00 31.98  ? 100 GLY   B C     1 
ATOM   14754 O  O     . GLY   F 2  98  ? 19.891  42.759  12.742  1.00 25.61  ? 100 GLY   B O     1 
ATOM   14755 N  N     . ASN   F 2  99  ? 19.623  44.888  13.459  1.00 20.29  ? 101 ASN   B N     1 
ATOM   14756 C  CA    . ASN   F 2  99  ? 19.218  44.491  14.806  1.00 24.61  ? 101 ASN   B CA    1 
ATOM   14757 C  C     . ASN   F 2  99  ? 20.249  43.594  15.464  1.00 23.63  ? 101 ASN   B C     1 
ATOM   14758 O  O     . ASN   F 2  99  ? 19.895  42.663  16.185  1.00 24.73  ? 101 ASN   B O     1 
ATOM   14759 C  CB    . ASN   F 2  99  ? 17.879  43.770  14.801  1.00 23.73  ? 101 ASN   B CB    1 
ATOM   14760 C  CG    . ASN   F 2  99  ? 16.729  44.705  14.701  1.00 34.33  ? 101 ASN   B CG    1 
ATOM   14761 O  OD1   . ASN   F 2  99  ? 16.715  45.771  15.329  1.00 27.00  ? 101 ASN   B OD1   1 
ATOM   14762 N  ND2   . ASN   F 2  99  ? 15.739  44.324  13.900  1.00 45.60  ? 101 ASN   B ND2   1 
ATOM   14763 N  N     . ASN   F 2  100 ? 21.520  43.845  15.188  1.00 20.10  ? 102 ASN   B N     1 
ATOM   14764 C  CA    . ASN   F 2  100 ? 22.598  42.974  15.638  1.00 28.51  ? 102 ASN   B CA    1 
ATOM   14765 C  C     . ASN   F 2  100 ? 23.538  43.797  16.508  1.00 25.95  ? 102 ASN   B C     1 
ATOM   14766 O  O     . ASN   F 2  100 ? 24.208  44.713  16.019  1.00 23.78  ? 102 ASN   B O     1 
ATOM   14767 C  CB    . ASN   F 2  100 ? 23.345  42.348  14.450  1.00 25.78  ? 102 ASN   B CB    1 
ATOM   14768 C  CG    . ASN   F 2  100 ? 24.324  41.245  14.887  1.00 27.79  ? 102 ASN   B CG    1 
ATOM   14769 O  OD1   . ASN   F 2  100 ? 25.112  41.420  15.810  1.00 29.94  ? 102 ASN   B OD1   1 
ATOM   14770 N  ND2   . ASN   F 2  100 ? 24.261  40.113  14.227  1.00 32.62  ? 102 ASN   B ND2   1 
ATOM   14771 N  N     . TRP   F 2  101 ? 23.583  43.480  17.796  1.00 26.67  ? 103 TRP   B N     1 
ATOM   14772 C  CA    . TRP   F 2  101 ? 24.401  44.283  18.701  1.00 32.70  ? 103 TRP   B CA    1 
ATOM   14773 C  C     . TRP   F 2  101 ? 25.865  44.266  18.279  1.00 27.48  ? 103 TRP   B C     1 
ATOM   14774 O  O     . TRP   F 2  101 ? 26.517  45.318  18.237  1.00 28.70  ? 103 TRP   B O     1 
ATOM   14775 C  CB    . TRP   F 2  101 ? 24.229  43.780  20.133  1.00 31.69  ? 103 TRP   B CB    1 
ATOM   14776 C  CG    . TRP   F 2  101 ? 24.862  44.620  21.207  1.00 32.73  ? 103 TRP   B CG    1 
ATOM   14777 C  CD1   . TRP   F 2  101 ? 24.268  45.622  21.930  1.00 26.30  ? 103 TRP   B CD1   1 
ATOM   14778 C  CD2   . TRP   F 2  101 ? 26.190  44.486  21.725  1.00 34.29  ? 103 TRP   B CD2   1 
ATOM   14779 N  NE1   . TRP   F 2  101 ? 25.152  46.131  22.844  1.00 29.30  ? 103 TRP   B NE1   1 
ATOM   14780 C  CE2   . TRP   F 2  101 ? 26.339  45.454  22.745  1.00 28.98  ? 103 TRP   B CE2   1 
ATOM   14781 C  CE3   . TRP   F 2  101 ? 27.275  43.650  21.418  1.00 33.80  ? 103 TRP   B CE3   1 
ATOM   14782 C  CZ2   . TRP   F 2  101 ? 27.526  45.612  23.460  1.00 23.46  ? 103 TRP   B CZ2   1 
ATOM   14783 C  CZ3   . TRP   F 2  101 ? 28.464  43.807  22.137  1.00 29.08  ? 103 TRP   B CZ3   1 
ATOM   14784 C  CH2   . TRP   F 2  101 ? 28.572  44.778  23.149  1.00 25.88  ? 103 TRP   B CH2   1 
ATOM   14785 N  N     . ALA   F 2  102 ? 26.389  43.088  17.933  1.00 21.97  ? 104 ALA   B N     1 
ATOM   14786 C  CA    . ALA   F 2  102 ? 27.791  42.990  17.523  1.00 26.04  ? 104 ALA   B CA    1 
ATOM   14787 C  C     . ALA   F 2  102 ? 28.098  43.863  16.298  1.00 25.44  ? 104 ALA   B C     1 
ATOM   14788 O  O     . ALA   F 2  102 ? 29.168  44.471  16.220  1.00 27.17  ? 104 ALA   B O     1 
ATOM   14789 C  CB    . ALA   F 2  102 ? 28.155  41.529  17.271  1.00 24.37  ? 104 ALA   B CB    1 
ATOM   14790 N  N     . LYS   F 2  103 ? 27.166  43.967  15.346  1.00 24.73  ? 105 LYS   B N     1 
ATOM   14791 C  CA    . LYS   F 2  103 ? 27.367  44.878  14.219  1.00 25.53  ? 105 LYS   B CA    1 
ATOM   14792 C  C     . LYS   F 2  103 ? 27.489  46.328  14.666  1.00 26.49  ? 105 LYS   B C     1 
ATOM   14793 O  O     . LYS   F 2  103 ? 28.316  47.080  14.129  1.00 31.02  ? 105 LYS   B O     1 
ATOM   14794 C  CB    . LYS   F 2  103 ? 26.244  44.731  13.196  1.00 19.53  ? 105 LYS   B CB    1 
ATOM   14795 C  CG    . LYS   F 2  103 ? 26.295  43.390  12.595  1.00 27.14  ? 105 LYS   B CG    1 
ATOM   14796 C  CD    . LYS   F 2  103 ? 25.353  43.229  11.465  1.00 32.02  ? 105 LYS   B CD    1 
ATOM   14797 C  CE    . LYS   F 2  103 ? 25.397  41.775  11.015  1.00 20.74  ? 105 LYS   B CE    1 
ATOM   14798 N  NZ    . LYS   F 2  103 ? 24.752  41.701  9.704   1.00 26.62  ? 105 LYS   B NZ    1 
ATOM   14799 N  N     . GLY   F 2  104 ? 26.680  46.745  15.642  1.00 23.74  ? 106 GLY   B N     1 
ATOM   14800 C  CA    . GLY   F 2  104 ? 26.798  48.103  16.145  1.00 20.35  ? 106 GLY   B CA    1 
ATOM   14801 C  C     . GLY   F 2  104 ? 28.072  48.333  16.942  1.00 28.38  ? 106 GLY   B C     1 
ATOM   14802 O  O     . GLY   F 2  104 ? 28.716  49.376  16.801  1.00 26.44  ? 106 GLY   B O     1 
ATOM   14803 N  N     . HIS   F 2  105 ? 28.461  47.360  17.780  1.00 22.74  ? 107 HIS   B N     1 
ATOM   14804 C  CA    . HIS   F 2  105 ? 29.542  47.578  18.743  1.00 30.40  ? 107 HIS   B CA    1 
ATOM   14805 C  C     . HIS   F 2  105 ? 30.918  47.399  18.125  1.00 37.81  ? 107 HIS   B C     1 
ATOM   14806 O  O     . HIS   F 2  105 ? 31.840  48.171  18.427  1.00 30.62  ? 107 HIS   B O     1 
ATOM   14807 C  CB    . HIS   F 2  105 ? 29.416  46.607  19.915  1.00 28.18  ? 107 HIS   B CB    1 
ATOM   14808 C  CG    . HIS   F 2  105 ? 30.079  47.071  21.176  1.00 31.11  ? 107 HIS   B CG    1 
ATOM   14809 N  ND1   . HIS   F 2  105 ? 29.584  48.108  21.942  1.00 37.00  ? 107 HIS   B ND1   1 
ATOM   14810 C  CD2   . HIS   F 2  105 ? 31.158  46.598  21.843  1.00 35.10  ? 107 HIS   B CD2   1 
ATOM   14811 C  CE1   . HIS   F 2  105 ? 30.335  48.260  23.020  1.00 28.54  ? 107 HIS   B CE1   1 
ATOM   14812 N  NE2   . HIS   F 2  105 ? 31.296  47.356  22.984  1.00 31.44  ? 107 HIS   B NE2   1 
ATOM   14813 N  N     . TYR   F 2  106 ? 31.063  46.376  17.273  1.00 29.47  ? 108 TYR   B N     1 
ATOM   14814 C  CA    . TYR   F 2  106 ? 32.344  45.810  16.890  1.00 25.21  ? 108 TYR   B CA    1 
ATOM   14815 C  C     . TYR   F 2  106 ? 32.712  46.006  15.431  1.00 33.10  ? 108 TYR   B C     1 
ATOM   14816 O  O     . TYR   F 2  106 ? 33.864  46.338  15.144  1.00 41.66  ? 108 TYR   B O     1 
ATOM   14817 C  CB    . TYR   F 2  106 ? 32.350  44.318  17.183  1.00 22.77  ? 108 TYR   B CB    1 
ATOM   14818 C  CG    . TYR   F 2  106 ? 32.514  44.016  18.611  1.00 30.37  ? 108 TYR   B CG    1 
ATOM   14819 C  CD1   . TYR   F 2  106 ? 33.544  44.612  19.354  1.00 29.83  ? 108 TYR   B CD1   1 
ATOM   14820 C  CD2   . TYR   F 2  106 ? 31.644  43.141  19.240  1.00 25.60  ? 108 TYR   B CD2   1 
ATOM   14821 C  CE1   . TYR   F 2  106 ? 33.697  44.331  20.691  1.00 32.13  ? 108 TYR   B CE1   1 
ATOM   14822 C  CE2   . TYR   F 2  106 ? 31.789  42.839  20.568  1.00 33.00  ? 108 TYR   B CE2   1 
ATOM   14823 C  CZ    . TYR   F 2  106 ? 32.807  43.438  21.302  1.00 37.49  ? 108 TYR   B CZ    1 
ATOM   14824 O  OH    . TYR   F 2  106 ? 32.912  43.132  22.642  1.00 27.91  ? 108 TYR   B OH    1 
ATOM   14825 N  N     . THR   F 2  107 ? 31.788  45.750  14.497  1.00 31.68  ? 109 THR   B N     1 
ATOM   14826 C  CA    . THR   F 2  107 ? 32.144  45.721  13.082  1.00 30.04  ? 109 THR   B CA    1 
ATOM   14827 C  C     . THR   F 2  107 ? 31.661  46.975  12.350  1.00 33.93  ? 109 THR   B C     1 
ATOM   14828 O  O     . THR   F 2  107 ? 32.428  47.931  12.178  1.00 33.72  ? 109 THR   B O     1 
ATOM   14829 C  CB    . THR   F 2  107 ? 31.617  44.432  12.442  1.00 32.04  ? 109 THR   B CB    1 
ATOM   14830 O  OG1   . THR   F 2  107 ? 30.202  44.314  12.638  1.00 31.13  ? 109 THR   B OG1   1 
ATOM   14831 C  CG2   . THR   F 2  107 ? 32.299  43.234  13.078  1.00 24.05  ? 109 THR   B CG2   1 
ATOM   14832 N  N     . GLU   F 2  108 ? 30.389  47.004  11.950  1.00 36.20  ? 110 GLU   B N     1 
ATOM   14833 C  CA    . GLU   F 2  108 ? 29.863  48.151  11.211  1.00 25.39  ? 110 GLU   B CA    1 
ATOM   14834 C  C     . GLU   F 2  108 ? 30.113  49.456  11.949  1.00 29.64  ? 110 GLU   B C     1 
ATOM   14835 O  O     . GLU   F 2  108 ? 30.678  50.401  11.392  1.00 36.23  ? 110 GLU   B O     1 
ATOM   14836 C  CB    . GLU   F 2  108 ? 28.368  47.959  10.964  1.00 32.03  ? 110 GLU   B CB    1 
ATOM   14837 C  CG    . GLU   F 2  108 ? 28.026  46.613  10.389  1.00 27.03  ? 110 GLU   B CG    1 
ATOM   14838 C  CD    . GLU   F 2  108 ? 28.707  46.427  9.088   1.00 37.40  ? 110 GLU   B CD    1 
ATOM   14839 O  OE1   . GLU   F 2  108 ? 28.500  47.308  8.243   1.00 25.74  ? 110 GLU   B OE1   1 
ATOM   14840 O  OE2   . GLU   F 2  108 ? 29.476  45.443  8.927   1.00 46.50  ? 110 GLU   B OE2   1 
ATOM   14841 N  N     . GLY   F 2  109 ? 29.686  49.527  13.212  1.00 34.39  ? 111 GLY   B N     1 
ATOM   14842 C  CA    . GLY   F 2  109 ? 29.749  50.778  13.942  1.00 34.24  ? 111 GLY   B CA    1 
ATOM   14843 C  C     . GLY   F 2  109 ? 31.163  51.197  14.276  1.00 42.93  ? 111 GLY   B C     1 
ATOM   14844 O  O     . GLY   F 2  109 ? 31.441  52.398  14.405  1.00 39.48  ? 111 GLY   B O     1 
ATOM   14845 N  N     . ALA   F 2  110 ? 32.066  50.218  14.443  1.00 39.73  ? 112 ALA   B N     1 
ATOM   14846 C  CA    . ALA   F 2  110 ? 33.497  50.505  14.563  1.00 42.58  ? 112 ALA   B CA    1 
ATOM   14847 C  C     . ALA   F 2  110 ? 33.979  51.408  13.428  1.00 36.29  ? 112 ALA   B C     1 
ATOM   14848 O  O     . ALA   F 2  110 ? 34.600  52.449  13.656  1.00 38.40  ? 112 ALA   B O     1 
ATOM   14849 C  CB    . ALA   F 2  110 ? 34.283  49.192  14.576  1.00 37.27  ? 112 ALA   B CB    1 
ATOM   14850 N  N     . GLU   F 2  111 ? 33.685  51.029  12.189  1.00 32.66  ? 113 GLU   B N     1 
ATOM   14851 C  CA    . GLU   F 2  111 ? 34.031  51.889  11.070  1.00 42.13  ? 113 GLU   B CA    1 
ATOM   14852 C  C     . GLU   F 2  111 ? 33.535  53.333  11.252  1.00 44.41  ? 113 GLU   B C     1 
ATOM   14853 O  O     . GLU   F 2  111 ? 34.242  54.282  10.898  1.00 48.47  ? 113 GLU   B O     1 
ATOM   14854 C  CB    . GLU   F 2  111 ? 33.482  51.279  9.783   1.00 44.67  ? 113 GLU   B CB    1 
ATOM   14855 C  CG    . GLU   F 2  111 ? 33.887  52.049  8.549   1.00 45.30  ? 113 GLU   B CG    1 
ATOM   14856 C  CD    . GLU   F 2  111 ? 33.802  51.211  7.294   1.00 56.08  ? 113 GLU   B CD    1 
ATOM   14857 O  OE1   . GLU   F 2  111 ? 33.306  50.055  7.372   1.00 59.50  ? 113 GLU   B OE1   1 
ATOM   14858 O  OE2   . GLU   F 2  111 ? 34.238  51.721  6.235   1.00 63.14  ? 113 GLU   B OE2   1 
ATOM   14859 N  N     . LEU   F 2  112 ? 32.331  53.530  11.803  1.00 40.09  ? 114 LEU   B N     1 
ATOM   14860 C  CA    . LEU   F 2  112 ? 31.728  54.865  11.784  1.00 37.36  ? 114 LEU   B CA    1 
ATOM   14861 C  C     . LEU   F 2  112 ? 32.011  55.692  13.028  1.00 34.30  ? 114 LEU   B C     1 
ATOM   14862 O  O     . LEU   F 2  112 ? 31.815  56.910  12.985  1.00 30.10  ? 114 LEU   B O     1 
ATOM   14863 C  CB    . LEU   F 2  112 ? 30.201  54.779  11.592  1.00 33.48  ? 114 LEU   B CB    1 
ATOM   14864 C  CG    . LEU   F 2  112 ? 29.369  56.073  11.641  1.00 31.57  ? 114 LEU   B CG    1 
ATOM   14865 C  CD1   . LEU   F 2  112 ? 29.780  57.101  10.573  1.00 28.73  ? 114 LEU   B CD1   1 
ATOM   14866 C  CD2   . LEU   F 2  112 ? 27.878  55.795  11.547  1.00 33.70  ? 114 LEU   B CD2   1 
ATOM   14867 N  N     . VAL   F 2  113 ? 32.486  55.072  14.112  1.00 34.47  ? 115 VAL   B N     1 
ATOM   14868 C  CA    . VAL   F 2  113 ? 32.452  55.709  15.429  1.00 30.18  ? 115 VAL   B CA    1 
ATOM   14869 C  C     . VAL   F 2  113 ? 33.294  56.989  15.451  1.00 41.79  ? 115 VAL   B C     1 
ATOM   14870 O  O     . VAL   F 2  113 ? 32.837  58.042  15.920  1.00 43.00  ? 115 VAL   B O     1 
ATOM   14871 C  CB    . VAL   F 2  113 ? 32.897  54.707  16.513  1.00 37.26  ? 115 VAL   B CB    1 
ATOM   14872 C  CG1   . VAL   F 2  113 ? 34.330  54.247  16.290  1.00 32.49  ? 115 VAL   B CG1   1 
ATOM   14873 C  CG2   . VAL   F 2  113 ? 32.731  55.287  17.908  1.00 38.64  ? 115 VAL   B CG2   1 
ATOM   14874 N  N     . ASP   F 2  114 ? 34.538  56.927  14.955  1.00 43.05  ? 116 ASP   B N     1 
ATOM   14875 C  CA    . ASP   F 2  114 ? 35.397  58.111  15.025  1.00 39.66  ? 116 ASP   B CA    1 
ATOM   14876 C  C     . ASP   F 2  114 ? 34.751  59.328  14.373  1.00 34.64  ? 116 ASP   B C     1 
ATOM   14877 O  O     . ASP   F 2  114 ? 34.968  60.457  14.821  1.00 40.04  ? 116 ASP   B O     1 
ATOM   14878 C  CB    . ASP   F 2  114 ? 36.765  57.843  14.386  1.00 25.61  ? 116 ASP   B CB    1 
ATOM   14879 C  CG    . ASP   F 2  114 ? 37.561  56.807  15.136  1.00 39.07  ? 116 ASP   B CG    1 
ATOM   14880 O  OD1   . ASP   F 2  114 ? 37.008  56.172  16.055  1.00 48.01  ? 116 ASP   B OD1   1 
ATOM   14881 O  OD2   . ASP   F 2  114 ? 38.748  56.623  14.816  1.00 59.73  ? 116 ASP   B OD2   1 
ATOM   14882 N  N     . SER   F 2  115 ? 33.974  59.141  13.310  1.00 35.02  ? 117 SER   B N     1 
ATOM   14883 C  CA    . SER   F 2  115 ? 33.326  60.308  12.719  1.00 36.30  ? 117 SER   B CA    1 
ATOM   14884 C  C     . SER   F 2  115 ? 32.294  60.884  13.666  1.00 38.01  ? 117 SER   B C     1 
ATOM   14885 O  O     . SER   F 2  115 ? 32.093  62.101  13.694  1.00 50.56  ? 117 SER   B O     1 
ATOM   14886 C  CB    . SER   F 2  115 ? 32.675  59.962  11.379  1.00 35.16  ? 117 SER   B CB    1 
ATOM   14887 O  OG    . SER   F 2  115 ? 33.301  58.838  10.788  1.00 52.71  ? 117 SER   B OG    1 
ATOM   14888 N  N     . VAL   F 2  116 ? 31.631  60.031  14.447  1.00 35.54  ? 118 VAL   B N     1 
ATOM   14889 C  CA    . VAL   F 2  116 ? 30.776  60.536  15.514  1.00 39.00  ? 118 VAL   B CA    1 
ATOM   14890 C  C     . VAL   F 2  116 ? 31.611  61.270  16.554  1.00 36.15  ? 118 VAL   B C     1 
ATOM   14891 O  O     . VAL   F 2  116 ? 31.252  62.368  16.989  1.00 40.83  ? 118 VAL   B O     1 
ATOM   14892 C  CB    . VAL   F 2  116 ? 29.956  59.398  16.148  1.00 42.99  ? 118 VAL   B CB    1 
ATOM   14893 C  CG1   . VAL   F 2  116 ? 29.104  59.935  17.300  1.00 24.68  ? 118 VAL   B CG1   1 
ATOM   14894 C  CG2   . VAL   F 2  116 ? 29.089  58.716  15.097  1.00 37.18  ? 118 VAL   B CG2   1 
ATOM   14895 N  N     . LEU   F 2  117 ? 32.741  60.684  16.968  1.00 26.52  ? 119 LEU   B N     1 
ATOM   14896 C  CA    . LEU   F 2  117 ? 33.509  61.310  18.039  1.00 28.61  ? 119 LEU   B CA    1 
ATOM   14897 C  C     . LEU   F 2  117 ? 34.091  62.675  17.652  1.00 44.46  ? 119 LEU   B C     1 
ATOM   14898 O  O     . LEU   F 2  117 ? 34.245  63.531  18.530  1.00 46.79  ? 119 LEU   B O     1 
ATOM   14899 C  CB    . LEU   F 2  117 ? 34.614  60.384  18.513  1.00 27.71  ? 119 LEU   B CB    1 
ATOM   14900 C  CG    . LEU   F 2  117 ? 34.032  59.209  19.274  1.00 43.76  ? 119 LEU   B CG    1 
ATOM   14901 C  CD1   . LEU   F 2  117 ? 34.922  57.998  19.080  1.00 46.91  ? 119 LEU   B CD1   1 
ATOM   14902 C  CD2   . LEU   F 2  117 ? 33.824  59.536  20.762  1.00 32.52  ? 119 LEU   B CD2   1 
ATOM   14903 N  N     . ASP   F 2  118 ? 34.422  62.917  16.371  1.00 43.07  ? 120 ASP   B N     1 
ATOM   14904 C  CA    . ASP   F 2  118 ? 34.957  64.231  16.001  1.00 35.45  ? 120 ASP   B CA    1 
ATOM   14905 C  C     . ASP   F 2  118 ? 33.899  65.322  16.115  1.00 42.96  ? 120 ASP   B C     1 
ATOM   14906 O  O     . ASP   F 2  118 ? 34.228  66.462  16.459  1.00 45.87  ? 120 ASP   B O     1 
ATOM   14907 C  CB    . ASP   F 2  118 ? 35.526  64.243  14.578  1.00 34.02  ? 120 ASP   B CB    1 
ATOM   14908 C  CG    . ASP   F 2  118 ? 36.636  63.245  14.369  1.00 40.26  ? 120 ASP   B CG    1 
ATOM   14909 O  OD1   . ASP   F 2  118 ? 37.379  62.945  15.331  1.00 47.89  ? 120 ASP   B OD1   1 
ATOM   14910 O  OD2   . ASP   F 2  118 ? 36.767  62.760  13.224  1.00 39.57  ? 120 ASP   B OD2   1 
ATOM   14911 N  N     . VAL   F 2  119 ? 32.635  65.006  15.817  1.00 42.27  ? 121 VAL   B N     1 
ATOM   14912 C  CA    . VAL   F 2  119 ? 31.558  65.960  16.074  1.00 36.39  ? 121 VAL   B CA    1 
ATOM   14913 C  C     . VAL   F 2  119 ? 31.321  66.114  17.569  1.00 45.66  ? 121 VAL   B C     1 
ATOM   14914 O  O     . VAL   F 2  119 ? 30.992  67.206  18.047  1.00 47.80  ? 121 VAL   B O     1 
ATOM   14915 C  CB    . VAL   F 2  119 ? 30.267  65.536  15.359  1.00 32.36  ? 121 VAL   B CB    1 
ATOM   14916 C  CG1   . VAL   F 2  119 ? 29.141  66.468  15.729  1.00 30.35  ? 121 VAL   B CG1   1 
ATOM   14917 C  CG2   . VAL   F 2  119 ? 30.473  65.514  13.867  1.00 46.04  ? 121 VAL   B CG2   1 
ATOM   14918 N  N     . VAL   F 2  120 ? 31.449  65.026  18.333  1.00 39.16  ? 122 VAL   B N     1 
ATOM   14919 C  CA    . VAL   F 2  120 ? 31.311  65.143  19.782  1.00 38.37  ? 122 VAL   B CA    1 
ATOM   14920 C  C     . VAL   F 2  120 ? 32.413  66.032  20.325  1.00 42.97  ? 122 VAL   B C     1 
ATOM   14921 O  O     . VAL   F 2  120 ? 32.162  67.021  21.020  1.00 47.10  ? 122 VAL   B O     1 
ATOM   14922 C  CB    . VAL   F 2  120 ? 31.334  63.756  20.458  1.00 35.93  ? 122 VAL   B CB    1 
ATOM   14923 C  CG1   . VAL   F 2  120 ? 31.275  63.911  21.963  1.00 30.89  ? 122 VAL   B CG1   1 
ATOM   14924 C  CG2   . VAL   F 2  120 ? 30.197  62.866  19.962  1.00 33.75  ? 122 VAL   B CG2   1 
ATOM   14925 N  N     . ARG   F 2  121 ? 33.659  65.687  20.009  1.00 48.00  ? 123 ARG   B N     1 
ATOM   14926 C  CA    . ARG   F 2  121 ? 34.790  66.455  20.509  1.00 54.63  ? 123 ARG   B CA    1 
ATOM   14927 C  C     . ARG   F 2  121 ? 34.768  67.882  19.976  1.00 55.92  ? 123 ARG   B C     1 
ATOM   14928 O  O     . ARG   F 2  121 ? 35.174  68.811  20.685  1.00 58.57  ? 123 ARG   B O     1 
ATOM   14929 C  CB    . ARG   F 2  121 ? 36.084  65.731  20.146  1.00 56.20  ? 123 ARG   B CB    1 
ATOM   14930 C  CG    . ARG   F 2  121 ? 37.362  66.529  20.212  1.00 49.90  ? 123 ARG   B CG    1 
ATOM   14931 C  CD    . ARG   F 2  121 ? 38.517  65.555  19.996  1.00 57.29  ? 123 ARG   B CD    1 
ATOM   14932 N  NE    . ARG   F 2  121 ? 38.269  64.705  18.831  1.00 59.06  ? 123 ARG   B NE    1 
ATOM   14933 C  CZ    . ARG   F 2  121 ? 38.074  63.392  18.875  1.00 56.82  ? 123 ARG   B CZ    1 
ATOM   14934 N  NH1   . ARG   F 2  121 ? 38.175  62.717  20.008  1.00 47.45  ? 123 ARG   B NH1   1 
ATOM   14935 N  NH2   . ARG   F 2  121 ? 37.773  62.740  17.750  1.00 45.45  ? 123 ARG   B NH2   1 
ATOM   14936 N  N     . LYS   F 2  122 ? 34.275  68.080  18.750  1.00 44.79  ? 124 LYS   B N     1 
ATOM   14937 C  CA    . LYS   F 2  122 ? 34.056  69.432  18.245  1.00 41.13  ? 124 LYS   B CA    1 
ATOM   14938 C  C     . LYS   F 2  122 ? 33.106  70.200  19.156  1.00 47.09  ? 124 LYS   B C     1 
ATOM   14939 O  O     . LYS   F 2  122 ? 33.446  71.262  19.690  1.00 54.61  ? 124 LYS   B O     1 
ATOM   14940 C  CB    . LYS   F 2  122 ? 33.511  69.366  16.823  1.00 45.90  ? 124 LYS   B CB    1 
ATOM   14941 C  CG    . LYS   F 2  122 ? 33.462  70.675  16.053  1.00 41.34  ? 124 LYS   B CG    1 
ATOM   14942 C  CD    . LYS   F 2  122 ? 32.866  70.420  14.667  1.00 61.33  ? 124 LYS   B CD    1 
ATOM   14943 C  CE    . LYS   F 2  122 ? 33.609  69.286  13.887  1.00 68.48  ? 124 LYS   B CE    1 
ATOM   14944 N  NZ    . LYS   F 2  122 ? 32.773  68.519  12.856  1.00 38.51  ? 124 LYS   B NZ    1 
ATOM   14945 N  N     . GLU   F 2  123 ? 31.908  69.652  19.363  1.00 52.00  ? 125 GLU   B N     1 
ATOM   14946 C  CA    . GLU   F 2  123 ? 30.899  70.310  20.186  1.00 45.56  ? 125 GLU   B CA    1 
ATOM   14947 C  C     . GLU   F 2  123 ? 31.372  70.518  21.621  1.00 42.44  ? 125 GLU   B C     1 
ATOM   14948 O  O     . GLU   F 2  123 ? 31.003  71.514  22.250  1.00 41.44  ? 125 GLU   B O     1 
ATOM   14949 C  CB    . GLU   F 2  123 ? 29.613  69.490  20.149  1.00 37.72  ? 125 GLU   B CB    1 
ATOM   14950 C  CG    . GLU   F 2  123 ? 28.804  69.706  18.901  1.00 24.37  ? 125 GLU   B CG    1 
ATOM   14951 C  CD    . GLU   F 2  123 ? 27.906  70.899  19.028  1.00 39.08  ? 125 GLU   B CD    1 
ATOM   14952 O  OE1   . GLU   F 2  123 ? 28.114  71.666  20.003  1.00 44.48  ? 125 GLU   B OE1   1 
ATOM   14953 O  OE2   . GLU   F 2  123 ? 26.986  71.062  18.184  1.00 38.51  ? 125 GLU   B OE2   1 
ATOM   14954 N  N     . SER   F 2  124 ? 32.199  69.605  22.140  1.00 41.01  ? 126 SER   B N     1 
ATOM   14955 C  CA    . SER   F 2  124 ? 32.692  69.723  23.510  1.00 39.02  ? 126 SER   B CA    1 
ATOM   14956 C  C     . SER   F 2  124 ? 33.762  70.803  23.637  1.00 50.16  ? 126 SER   B C     1 
ATOM   14957 O  O     . SER   F 2  124 ? 33.741  71.587  24.591  1.00 53.91  ? 126 SER   B O     1 
ATOM   14958 C  CB    . SER   F 2  124 ? 33.235  68.378  23.990  1.00 47.63  ? 126 SER   B CB    1 
ATOM   14959 O  OG    . SER   F 2  124 ? 32.188  67.453  24.269  1.00 51.03  ? 126 SER   B OG    1 
ATOM   14960 N  N     . GLU   F 2  125 ? 34.716  70.862  22.703  1.00 56.13  ? 127 GLU   B N     1 
ATOM   14961 C  CA    . GLU   F 2  125 ? 35.784  71.861  22.774  1.00 54.08  ? 127 GLU   B CA    1 
ATOM   14962 C  C     . GLU   F 2  125 ? 35.227  73.278  22.680  1.00 61.77  ? 127 GLU   B C     1 
ATOM   14963 O  O     . GLU   F 2  125 ? 35.986  74.253  22.664  1.00 62.24  ? 127 GLU   B O     1 
ATOM   14964 C  CB    . GLU   F 2  125 ? 36.818  71.658  21.658  1.00 61.72  ? 127 GLU   B CB    1 
ATOM   14965 C  CG    . GLU   F 2  125 ? 37.417  70.257  21.553  1.00 76.19  ? 127 GLU   B CG    1 
ATOM   14966 C  CD    . GLU   F 2  125 ? 37.901  69.700  22.888  1.00 73.53  ? 127 GLU   B CD    1 
ATOM   14967 O  OE1   . GLU   F 2  125 ? 37.112  69.683  23.853  1.00 72.27  ? 127 GLU   B OE1   1 
ATOM   14968 O  OE2   . GLU   F 2  125 ? 39.073  69.271  22.968  1.00 76.76  ? 127 GLU   B OE2   1 
ATOM   14969 N  N     . SER   F 2  126 ? 33.901  73.393  22.597  1.00 58.56  ? 128 SER   B N     1 
ATOM   14970 C  CA    . SER   F 2  126 ? 33.204  74.660  22.413  1.00 47.58  ? 128 SER   B CA    1 
ATOM   14971 C  C     . SER   F 2  126 ? 32.327  74.998  23.619  1.00 52.98  ? 128 SER   B C     1 
ATOM   14972 O  O     . SER   F 2  126 ? 31.376  75.777  23.495  1.00 61.50  ? 128 SER   B O     1 
ATOM   14973 C  CB    . SER   F 2  126 ? 32.379  74.593  21.121  1.00 47.40  ? 128 SER   B CB    1 
ATOM   14974 O  OG    . SER   F 2  126 ? 31.510  75.697  20.946  1.00 55.08  ? 128 SER   B OG    1 
ATOM   14975 N  N     . CYS   F 2  127 ? 32.628  74.429  24.788  1.00 43.66  ? 129 CYS   B N     1 
ATOM   14976 C  CA    . CYS   F 2  127 ? 31.778  74.536  25.972  1.00 51.58  ? 129 CYS   B CA    1 
ATOM   14977 C  C     . CYS   F 2  127 ? 32.526  75.238  27.101  1.00 50.65  ? 129 CYS   B C     1 
ATOM   14978 O  O     . CYS   F 2  127 ? 33.654  74.851  27.437  1.00 45.97  ? 129 CYS   B O     1 
ATOM   14979 C  CB    . CYS   F 2  127 ? 31.311  73.146  26.464  1.00 48.12  ? 129 CYS   B CB    1 
ATOM   14980 S  SG    . CYS   F 2  127 ? 30.081  72.268  25.437  1.00 51.13  ? 129 CYS   B SG    1 
ATOM   14981 N  N     . ASP   F 2  128 ? 31.879  76.244  27.706  1.00 41.26  ? 130 ASP   B N     1 
ATOM   14982 C  CA    . ASP   F 2  128 ? 32.415  76.857  28.921  1.00 41.29  ? 130 ASP   B CA    1 
ATOM   14983 C  C     . ASP   F 2  128 ? 32.650  75.811  30.005  1.00 39.36  ? 130 ASP   B C     1 
ATOM   14984 O  O     . ASP   F 2  128 ? 33.708  75.774  30.638  1.00 38.68  ? 130 ASP   B O     1 
ATOM   14985 C  CB    . ASP   F 2  128 ? 31.453  77.926  29.463  1.00 59.06  ? 130 ASP   B CB    1 
ATOM   14986 C  CG    . ASP   F 2  128 ? 31.317  79.148  28.562  1.00 73.13  ? 130 ASP   B CG    1 
ATOM   14987 O  OD1   . ASP   F 2  128 ? 32.044  79.278  27.543  1.00 73.50  ? 130 ASP   B OD1   1 
ATOM   14988 O  OD2   . ASP   F 2  128 ? 30.453  79.993  28.897  1.00 72.12  ? 130 ASP   B OD2   1 
ATOM   14989 N  N     . CYS   F 2  129 ? 31.651  74.970  30.255  1.00 43.04  ? 131 CYS   B N     1 
ATOM   14990 C  CA    . CYS   F 2  129 ? 31.610  74.170  31.475  1.00 45.63  ? 131 CYS   B CA    1 
ATOM   14991 C  C     . CYS   F 2  129 ? 30.713  72.972  31.146  1.00 46.46  ? 131 CYS   B C     1 
ATOM   14992 O  O     . CYS   F 2  129 ? 29.503  73.029  31.346  1.00 53.76  ? 131 CYS   B O     1 
ATOM   14993 C  CB    . CYS   F 2  129 ? 31.078  75.000  32.637  1.00 57.89  ? 131 CYS   B CB    1 
ATOM   14994 S  SG    . CYS   F 2  129 ? 30.776  74.206  34.238  1.00 54.40  ? 131 CYS   B SG    1 
ATOM   14995 N  N     . LEU   F 2  130 ? 31.320  71.916  30.604  1.00 49.91  ? 132 LEU   B N     1 
ATOM   14996 C  CA    . LEU   F 2  130 ? 30.577  70.758  30.120  1.00 40.74  ? 132 LEU   B CA    1 
ATOM   14997 C  C     . LEU   F 2  130 ? 30.126  69.913  31.305  1.00 45.44  ? 132 LEU   B C     1 
ATOM   14998 O  O     . LEU   F 2  130 ? 30.960  69.453  32.094  1.00 44.43  ? 132 LEU   B O     1 
ATOM   14999 C  CB    . LEU   F 2  130 ? 31.452  69.943  29.168  1.00 43.07  ? 132 LEU   B CB    1 
ATOM   15000 C  CG    . LEU   F 2  130 ? 30.960  68.670  28.472  1.00 32.81  ? 132 LEU   B CG    1 
ATOM   15001 C  CD1   . LEU   F 2  130 ? 30.085  68.997  27.296  1.00 38.40  ? 132 LEU   B CD1   1 
ATOM   15002 C  CD2   . LEU   F 2  130 ? 32.157  67.894  28.005  1.00 35.36  ? 132 LEU   B CD2   1 
ATOM   15003 N  N     . GLN   F 2  131 ? 28.809  69.715  31.441  1.00 42.50  ? 133 GLN   B N     1 
ATOM   15004 C  CA    . GLN   F 2  131 ? 28.316  68.830  32.492  1.00 40.15  ? 133 GLN   B CA    1 
ATOM   15005 C  C     . GLN   F 2  131 ? 28.589  67.378  32.151  1.00 32.55  ? 133 GLN   B C     1 
ATOM   15006 O  O     . GLN   F 2  131 ? 28.915  66.572  33.029  1.00 38.11  ? 133 GLN   B O     1 
ATOM   15007 C  CB    . GLN   F 2  131 ? 26.816  68.999  32.700  1.00 34.97  ? 133 GLN   B CB    1 
ATOM   15008 C  CG    . GLN   F 2  131 ? 26.303  70.386  32.795  1.00 38.35  ? 133 GLN   B CG    1 
ATOM   15009 C  CD    . GLN   F 2  131 ? 24.846  70.372  33.150  1.00 38.69  ? 133 GLN   B CD    1 
ATOM   15010 O  OE1   . GLN   F 2  131 ? 24.421  69.586  34.000  1.00 37.78  ? 133 GLN   B OE1   1 
ATOM   15011 N  NE2   . GLN   F 2  131 ? 24.058  71.215  32.486  1.00 35.32  ? 133 GLN   B NE2   1 
ATOM   15012 N  N     . GLY   F 2  132 ? 28.432  67.029  30.894  1.00 32.16  ? 134 GLY   B N     1 
ATOM   15013 C  CA    . GLY   F 2  132 ? 28.476  65.650  30.467  1.00 36.97  ? 134 GLY   B CA    1 
ATOM   15014 C  C     . GLY   F 2  132 ? 27.593  65.469  29.252  1.00 33.99  ? 134 GLY   B C     1 
ATOM   15015 O  O     . GLY   F 2  132 ? 27.290  66.428  28.546  1.00 36.45  ? 134 GLY   B O     1 
ATOM   15016 N  N     . PHE   F 2  133 ? 27.163  64.229  29.052  1.00 33.77  ? 135 PHE   B N     1 
ATOM   15017 C  CA    . PHE   F 2  133 ? 26.492  63.815  27.828  1.00 32.79  ? 135 PHE   B CA    1 
ATOM   15018 C  C     . PHE   F 2  133 ? 25.151  63.159  28.145  1.00 35.22  ? 135 PHE   B C     1 
ATOM   15019 O  O     . PHE   F 2  133 ? 24.983  62.485  29.172  1.00 30.62  ? 135 PHE   B O     1 
ATOM   15020 C  CB    . PHE   F 2  133 ? 27.408  62.861  27.050  1.00 30.26  ? 135 PHE   B CB    1 
ATOM   15021 C  CG    . PHE   F 2  133 ? 28.815  63.350  26.953  1.00 29.38  ? 135 PHE   B CG    1 
ATOM   15022 C  CD1   . PHE   F 2  133 ? 29.710  63.146  27.995  1.00 33.22  ? 135 PHE   B CD1   1 
ATOM   15023 C  CD2   . PHE   F 2  133 ? 29.241  64.054  25.842  1.00 39.56  ? 135 PHE   B CD2   1 
ATOM   15024 C  CE1   . PHE   F 2  133 ? 31.023  63.615  27.920  1.00 31.38  ? 135 PHE   B CE1   1 
ATOM   15025 C  CE2   . PHE   F 2  133 ? 30.558  64.533  25.758  1.00 41.77  ? 135 PHE   B CE2   1 
ATOM   15026 C  CZ    . PHE   F 2  133 ? 31.442  64.312  26.801  1.00 35.24  ? 135 PHE   B CZ    1 
ATOM   15027 N  N     . GLN   F 2  134 ? 24.180  63.367  27.266  1.00 27.26  ? 136 GLN   B N     1 
ATOM   15028 C  CA    . GLN   F 2  134 ? 22.927  62.636  27.379  1.00 33.27  ? 136 GLN   B CA    1 
ATOM   15029 C  C     . GLN   F 2  134 ? 22.662  61.959  26.049  1.00 30.23  ? 136 GLN   B C     1 
ATOM   15030 O  O     . GLN   F 2  134 ? 22.601  62.633  25.021  1.00 29.51  ? 136 GLN   B O     1 
ATOM   15031 C  CB    . GLN   F 2  134 ? 21.757  63.545  27.785  1.00 29.91  ? 136 GLN   B CB    1 
ATOM   15032 C  CG    . GLN   F 2  134 ? 21.127  64.361  26.674  1.00 34.51  ? 136 GLN   B CG    1 
ATOM   15033 C  CD    . GLN   F 2  134 ? 19.654  64.765  26.965  1.00 38.13  ? 136 GLN   B CD    1 
ATOM   15034 O  OE1   . GLN   F 2  134 ? 19.199  64.774  28.112  1.00 27.93  ? 136 GLN   B OE1   1 
ATOM   15035 N  NE2   . GLN   F 2  134 ? 18.915  65.097  25.901  1.00 38.03  ? 136 GLN   B NE2   1 
ATOM   15036 N  N     . LEU   F 2  135 ? 22.522  60.630  26.075  1.00 34.81  ? 137 LEU   B N     1 
ATOM   15037 C  CA    . LEU   F 2  135 ? 22.268  59.818  24.891  1.00 30.68  ? 137 LEU   B CA    1 
ATOM   15038 C  C     . LEU   F 2  135 ? 20.872  59.211  24.932  1.00 35.84  ? 137 LEU   B C     1 
ATOM   15039 O  O     . LEU   F 2  135 ? 20.439  58.701  25.975  1.00 31.23  ? 137 LEU   B O     1 
ATOM   15040 C  CB    . LEU   F 2  135 ? 23.295  58.699  24.774  1.00 34.69  ? 137 LEU   B CB    1 
ATOM   15041 C  CG    . LEU   F 2  135 ? 22.991  57.541  23.818  1.00 35.27  ? 137 LEU   B CG    1 
ATOM   15042 C  CD1   . LEU   F 2  135 ? 23.536  57.859  22.463  1.00 35.95  ? 137 LEU   B CD1   1 
ATOM   15043 C  CD2   . LEU   F 2  135 ? 23.545  56.190  24.331  1.00 30.49  ? 137 LEU   B CD2   1 
ATOM   15044 N  N     . THR   F 2  136 ? 20.175  59.263  23.789  1.00 26.64  ? 138 THR   B N     1 
ATOM   15045 C  CA    . THR   F 2  136 ? 18.917  58.555  23.591  1.00 27.49  ? 138 THR   B CA    1 
ATOM   15046 C  C     . THR   F 2  136 ? 19.118  57.394  22.618  1.00 33.61  ? 138 THR   B C     1 
ATOM   15047 O  O     . THR   F 2  136 ? 19.756  57.543  21.568  1.00 31.47  ? 138 THR   B O     1 
ATOM   15048 C  CB    . THR   F 2  136 ? 17.794  59.482  23.084  1.00 25.03  ? 138 THR   B CB    1 
ATOM   15049 O  OG1   . THR   F 2  136 ? 18.185  60.145  21.871  1.00 31.50  ? 138 THR   B OG1   1 
ATOM   15050 C  CG2   . THR   F 2  136 ? 17.406  60.512  24.143  1.00 24.88  ? 138 THR   B CG2   1 
ATOM   15051 N  N     . HIS   F 2  137 ? 18.547  56.242  22.961  1.00 23.45  ? 139 HIS   B N     1 
ATOM   15052 C  CA    . HIS   F 2  137 ? 18.745  55.033  22.179  1.00 27.43  ? 139 HIS   B CA    1 
ATOM   15053 C  C     . HIS   F 2  137 ? 17.849  53.935  22.743  1.00 33.44  ? 139 HIS   B C     1 
ATOM   15054 O  O     . HIS   F 2  137 ? 17.321  54.034  23.857  1.00 25.95  ? 139 HIS   B O     1 
ATOM   15055 C  CB    . HIS   F 2  137 ? 20.214  54.585  22.204  1.00 29.01  ? 139 HIS   B CB    1 
ATOM   15056 C  CG    . HIS   F 2  137 ? 20.650  54.055  23.539  1.00 34.11  ? 139 HIS   B CG    1 
ATOM   15057 N  ND1   . HIS   F 2  137 ? 21.550  53.020  23.677  1.00 26.55  ? 139 HIS   B ND1   1 
ATOM   15058 C  CD2   . HIS   F 2  137 ? 20.286  54.407  24.797  1.00 31.02  ? 139 HIS   B CD2   1 
ATOM   15059 C  CE1   . HIS   F 2  137 ? 21.720  52.758  24.961  1.00 30.66  ? 139 HIS   B CE1   1 
ATOM   15060 N  NE2   . HIS   F 2  137 ? 20.964  53.586  25.661  1.00 30.69  ? 139 HIS   B NE2   1 
ATOM   15061 N  N     . SER   F 2  138 ? 17.713  52.874  21.963  1.00 28.18  ? 140 SER   B N     1 
ATOM   15062 C  CA    . SER   F 2  138 ? 17.056  51.647  22.374  1.00 31.01  ? 140 SER   B CA    1 
ATOM   15063 C  C     . SER   F 2  138 ? 18.099  50.572  22.675  1.00 28.59  ? 140 SER   B C     1 
ATOM   15064 O  O     . SER   F 2  138 ? 19.238  50.634  22.207  1.00 24.42  ? 140 SER   B O     1 
ATOM   15065 C  CB    . SER   F 2  138 ? 16.124  51.171  21.272  1.00 21.64  ? 140 SER   B CB    1 
ATOM   15066 O  OG    . SER   F 2  138 ? 16.893  51.156  20.091  1.00 30.39  ? 140 SER   B OG    1 
ATOM   15067 N  N     . LEU   F 2  139 ? 17.692  49.578  23.470  1.00 20.34  ? 141 LEU   B N     1 
ATOM   15068 C  CA    . LEU   F 2  139 ? 18.580  48.477  23.813  1.00 18.22  ? 141 LEU   B CA    1 
ATOM   15069 C  C     . LEU   F 2  139 ? 18.307  47.224  23.005  1.00 24.36  ? 141 LEU   B C     1 
ATOM   15070 O  O     . LEU   F 2  139 ? 19.146  46.315  23.007  1.00 21.75  ? 141 LEU   B O     1 
ATOM   15071 C  CB    . LEU   F 2  139 ? 18.481  48.134  25.302  1.00 21.04  ? 141 LEU   B CB    1 
ATOM   15072 C  CG    . LEU   F 2  139 ? 18.657  49.343  26.224  1.00 25.90  ? 141 LEU   B CG    1 
ATOM   15073 C  CD1   . LEU   F 2  139 ? 18.856  48.913  27.712  1.00 19.20  ? 141 LEU   B CD1   1 
ATOM   15074 C  CD2   . LEU   F 2  139 ? 19.787  50.216  25.702  1.00 13.64  ? 141 LEU   B CD2   1 
ATOM   15075 N  N     . GLY   F 2  140 ? 17.173  47.173  22.295  1.00 24.89  ? 142 GLY   B N     1 
ATOM   15076 C  CA    . GLY   F 2  140 ? 16.738  45.974  21.613  1.00 18.71  ? 142 GLY   B CA    1 
ATOM   15077 C  C     . GLY   F 2  140 ? 17.301  45.786  20.218  1.00 22.15  ? 142 GLY   B C     1 
ATOM   15078 O  O     . GLY   F 2  140 ? 17.293  44.671  19.684  1.00 21.88  ? 142 GLY   B O     1 
ATOM   15079 N  N     . GLY   F 2  141 ? 17.791  46.861  19.622  1.00 21.76  ? 143 GLY   B N     1 
ATOM   15080 C  CA    . GLY   F 2  141 ? 18.308  46.834  18.265  1.00 19.79  ? 143 GLY   B CA    1 
ATOM   15081 C  C     . GLY   F 2  141 ? 19.801  46.602  18.177  1.00 30.01  ? 143 GLY   B C     1 
ATOM   15082 O  O     . GLY   F 2  141 ? 20.428  45.998  19.062  1.00 28.06  ? 143 GLY   B O     1 
ATOM   15083 N  N     . GLY   F 2  142 ? 20.372  47.075  17.071  1.00 22.74  ? 144 GLY   B N     1 
ATOM   15084 C  CA    . GLY   F 2  142 ? 21.783  46.935  16.818  1.00 20.69  ? 144 GLY   B CA    1 
ATOM   15085 C  C     . GLY   F 2  142 ? 22.543  48.239  16.907  1.00 25.73  ? 144 GLY   B C     1 
ATOM   15086 O  O     . GLY   F 2  142 ? 23.594  48.296  17.539  1.00 27.02  ? 144 GLY   B O     1 
ATOM   15087 N  N     . THR   F 2  143 ? 22.035  49.297  16.281  1.00 20.22  ? 145 THR   B N     1 
ATOM   15088 C  CA    . THR   F 2  143 ? 22.794  50.539  16.237  1.00 22.79  ? 145 THR   B CA    1 
ATOM   15089 C  C     . THR   F 2  143 ? 22.750  51.290  17.565  1.00 29.35  ? 145 THR   B C     1 
ATOM   15090 O  O     . THR   F 2  143 ? 23.796  51.572  18.164  1.00 35.15  ? 145 THR   B O     1 
ATOM   15091 C  CB    . THR   F 2  143 ? 22.278  51.417  15.102  1.00 23.23  ? 145 THR   B CB    1 
ATOM   15092 O  OG1   . THR   F 2  143 ? 22.541  50.754  13.868  1.00 28.35  ? 145 THR   B OG1   1 
ATOM   15093 C  CG2   . THR   F 2  143 ? 22.952  52.781  15.127  1.00 25.99  ? 145 THR   B CG2   1 
ATOM   15094 N  N     . GLY   F 2  144 ? 21.553  51.657  18.029  1.00 28.80  ? 146 GLY   B N     1 
ATOM   15095 C  CA    . GLY   F 2  144 ? 21.463  52.346  19.306  1.00 28.97  ? 146 GLY   B CA    1 
ATOM   15096 C  C     . GLY   F 2  144 ? 22.025  51.504  20.428  1.00 24.33  ? 146 GLY   B C     1 
ATOM   15097 O  O     . GLY   F 2  144 ? 22.696  52.010  21.331  1.00 30.40  ? 146 GLY   B O     1 
ATOM   15098 N  N     . SER   F 2  145 ? 21.776  50.201  20.367  1.00 19.93  ? 147 SER   B N     1 
ATOM   15099 C  CA    . SER   F 2  145 ? 22.231  49.273  21.392  1.00 22.45  ? 147 SER   B CA    1 
ATOM   15100 C  C     . SER   F 2  145 ? 23.748  49.073  21.333  1.00 26.45  ? 147 SER   B C     1 
ATOM   15101 O  O     . SER   F 2  145 ? 24.472  49.401  22.279  1.00 26.84  ? 147 SER   B O     1 
ATOM   15102 C  CB    . SER   F 2  145 ? 21.504  47.949  21.214  1.00 21.83  ? 147 SER   B CB    1 
ATOM   15103 O  OG    . SER   F 2  145 ? 21.706  47.117  22.339  1.00 30.11  ? 147 SER   B OG    1 
ATOM   15104 N  N     . GLY   F 2  146 ? 24.248  48.498  20.245  1.00 28.32  ? 148 GLY   B N     1 
ATOM   15105 C  CA    . GLY   F 2  146 ? 25.642  48.118  20.140  1.00 26.04  ? 148 GLY   B CA    1 
ATOM   15106 C  C     . GLY   F 2  146 ? 26.559  49.294  19.888  1.00 30.05  ? 148 GLY   B C     1 
ATOM   15107 O  O     . GLY   F 2  146 ? 27.572  49.453  20.590  1.00 28.60  ? 148 GLY   B O     1 
ATOM   15108 N  N     . MET   F 2  147 ? 26.203  50.136  18.908  1.00 20.44  ? 149 MET   B N     1 
ATOM   15109 C  CA    . MET   F 2  147 ? 26.987  51.344  18.658  1.00 31.94  ? 149 MET   B CA    1 
ATOM   15110 C  C     . MET   F 2  147 ? 26.715  52.453  19.682  1.00 35.97  ? 149 MET   B C     1 
ATOM   15111 O  O     . MET   F 2  147 ? 27.618  53.248  19.987  1.00 34.04  ? 149 MET   B O     1 
ATOM   15112 C  CB    . MET   F 2  147 ? 26.729  51.876  17.245  1.00 26.77  ? 149 MET   B CB    1 
ATOM   15113 C  CG    . MET   F 2  147 ? 27.846  52.791  16.757  1.00 30.35  ? 149 MET   B CG    1 
ATOM   15114 S  SD    . MET   F 2  147 ? 27.444  53.811  15.326  1.00 38.57  ? 149 MET   B SD    1 
ATOM   15115 C  CE    . MET   F 2  147 ? 28.831  54.949  15.321  1.00 38.68  ? 149 MET   B CE    1 
ATOM   15116 N  N     . GLY   F 2  148 ? 25.489  52.539  20.206  1.00 28.53  ? 150 GLY   B N     1 
ATOM   15117 C  CA    . GLY   F 2  148 ? 25.230  53.477  21.286  1.00 25.29  ? 150 GLY   B CA    1 
ATOM   15118 C  C     . GLY   F 2  148 ? 26.172  53.280  22.460  1.00 27.27  ? 150 GLY   B C     1 
ATOM   15119 O  O     . GLY   F 2  148 ? 26.796  54.229  22.931  1.00 23.87  ? 150 GLY   B O     1 
ATOM   15120 N  N     . THR   F 2  149 ? 26.306  52.029  22.937  1.00 26.20  ? 151 THR   B N     1 
ATOM   15121 C  CA    . THR   F 2  149 ? 27.172  51.768  24.085  1.00 22.55  ? 151 THR   B CA    1 
ATOM   15122 C  C     . THR   F 2  149 ? 28.658  51.781  23.719  1.00 23.86  ? 151 THR   B C     1 
ATOM   15123 O  O     . THR   F 2  149 ? 29.491  52.112  24.566  1.00 31.31  ? 151 THR   B O     1 
ATOM   15124 C  CB    . THR   F 2  149 ? 26.815  50.437  24.763  1.00 17.57  ? 151 THR   B CB    1 
ATOM   15125 O  OG1   . THR   F 2  149 ? 26.999  49.368  23.853  1.00 25.56  ? 151 THR   B OG1   1 
ATOM   15126 C  CG2   . THR   F 2  149 ? 25.387  50.422  25.278  1.00 19.33  ? 151 THR   B CG2   1 
ATOM   15127 N  N     . LEU   F 2  150 ? 29.026  51.428  22.489  1.00 30.73  ? 152 LEU   B N     1 
ATOM   15128 C  CA    . LEU   F 2  150 ? 30.396  51.680  22.059  1.00 31.70  ? 152 LEU   B CA    1 
ATOM   15129 C  C     . LEU   F 2  150 ? 30.763  53.147  22.268  1.00 35.12  ? 152 LEU   B C     1 
ATOM   15130 O  O     . LEU   F 2  150 ? 31.816  53.459  22.835  1.00 31.93  ? 152 LEU   B O     1 
ATOM   15131 C  CB    . LEU   F 2  150 ? 30.589  51.288  20.591  1.00 32.30  ? 152 LEU   B CB    1 
ATOM   15132 C  CG    . LEU   F 2  150 ? 32.026  51.485  20.059  1.00 29.94  ? 152 LEU   B CG    1 
ATOM   15133 C  CD1   . LEU   F 2  150 ? 32.980  50.577  20.789  1.00 28.50  ? 152 LEU   B CD1   1 
ATOM   15134 C  CD2   . LEU   F 2  150 ? 32.122  51.241  18.572  1.00 29.27  ? 152 LEU   B CD2   1 
ATOM   15135 N  N     . LEU   F 2  151 ? 29.892  54.062  21.822  1.00 26.59  ? 153 LEU   B N     1 
ATOM   15136 C  CA    . LEU   F 2  151 ? 30.171  55.491  21.933  1.00 27.64  ? 153 LEU   B CA    1 
ATOM   15137 C  C     . LEU   F 2  151 ? 30.298  55.948  23.387  1.00 38.61  ? 153 LEU   B C     1 
ATOM   15138 O  O     . LEU   F 2  151 ? 31.066  56.871  23.694  1.00 40.34  ? 153 LEU   B O     1 
ATOM   15139 C  CB    . LEU   F 2  151 ? 29.066  56.272  21.239  1.00 30.24  ? 153 LEU   B CB    1 
ATOM   15140 C  CG    . LEU   F 2  151 ? 29.137  56.436  19.732  1.00 27.46  ? 153 LEU   B CG    1 
ATOM   15141 C  CD1   . LEU   F 2  151 ? 27.722  56.607  19.206  1.00 30.47  ? 153 LEU   B CD1   1 
ATOM   15142 C  CD2   . LEU   F 2  151 ? 29.965  57.662  19.468  1.00 34.63  ? 153 LEU   B CD2   1 
ATOM   15143 N  N     . ILE   F 2  152 ? 29.517  55.351  24.283  1.00 34.64  ? 154 ILE   B N     1 
ATOM   15144 C  CA    . ILE   F 2  152 ? 29.615  55.656  25.702  1.00 30.00  ? 154 ILE   B CA    1 
ATOM   15145 C  C     . ILE   F 2  152 ? 30.990  55.259  26.234  1.00 28.91  ? 154 ILE   B C     1 
ATOM   15146 O  O     . ILE   F 2  152 ? 31.597  55.980  27.033  1.00 31.95  ? 154 ILE   B O     1 
ATOM   15147 C  CB    . ILE   F 2  152 ? 28.453  54.950  26.433  1.00 28.23  ? 154 ILE   B CB    1 
ATOM   15148 C  CG1   . ILE   F 2  152 ? 27.125  55.643  26.076  1.00 22.68  ? 154 ILE   B CG1   1 
ATOM   15149 C  CG2   . ILE   F 2  152 ? 28.683  54.858  27.920  1.00 15.43  ? 154 ILE   B CG2   1 
ATOM   15150 C  CD1   . ILE   F 2  152 ? 25.923  54.974  26.667  1.00 24.49  ? 154 ILE   B CD1   1 
ATOM   15151 N  N     . SER   F 2  153 ? 31.524  54.129  25.765  1.00 33.37  ? 155 SER   B N     1 
ATOM   15152 C  CA    . SER   F 2  153 ? 32.830  53.678  26.241  1.00 34.65  ? 155 SER   B CA    1 
ATOM   15153 C  C     . SER   F 2  153 ? 33.943  54.558  25.702  1.00 35.46  ? 155 SER   B C     1 
ATOM   15154 O  O     . SER   F 2  153 ? 34.927  54.828  26.399  1.00 41.89  ? 155 SER   B O     1 
ATOM   15155 C  CB    . SER   F 2  153 ? 33.078  52.228  25.845  1.00 27.16  ? 155 SER   B CB    1 
ATOM   15156 O  OG    . SER   F 2  153 ? 34.045  51.650  26.693  1.00 34.26  ? 155 SER   B OG    1 
ATOM   15157 N  N     . LYS   F 2  154 ? 33.812  55.006  24.461  1.00 33.19  ? 156 LYS   B N     1 
ATOM   15158 C  CA    . LYS   F 2  154 ? 34.771  55.950  23.919  1.00 30.76  ? 156 LYS   B CA    1 
ATOM   15159 C  C     . LYS   F 2  154 ? 34.668  57.285  24.638  1.00 37.87  ? 156 LYS   B C     1 
ATOM   15160 O  O     . LYS   F 2  154 ? 35.661  57.795  25.172  1.00 42.38  ? 156 LYS   B O     1 
ATOM   15161 C  CB    . LYS   F 2  154 ? 34.541  56.101  22.417  1.00 34.84  ? 156 LYS   B CB    1 
ATOM   15162 C  CG    . LYS   F 2  154 ? 34.648  54.762  21.693  1.00 31.90  ? 156 LYS   B CG    1 
ATOM   15163 C  CD    . LYS   F 2  154 ? 35.382  54.860  20.378  1.00 35.25  ? 156 LYS   B CD    1 
ATOM   15164 C  CE    . LYS   F 2  154 ? 35.992  53.519  20.024  1.00 46.05  ? 156 LYS   B CE    1 
ATOM   15165 N  NZ    . LYS   F 2  154 ? 36.401  52.821  21.267  1.00 44.99  ? 156 LYS   B NZ    1 
ATOM   15166 N  N     . ILE   F 2  155 ? 33.459  57.844  24.697  1.00 39.59  ? 157 ILE   B N     1 
ATOM   15167 C  CA    . ILE   F 2  155 ? 33.278  59.168  25.283  1.00 38.15  ? 157 ILE   B CA    1 
ATOM   15168 C  C     . ILE   F 2  155 ? 33.757  59.183  26.729  1.00 38.59  ? 157 ILE   B C     1 
ATOM   15169 O  O     . ILE   F 2  155 ? 34.377  60.153  27.183  1.00 44.26  ? 157 ILE   B O     1 
ATOM   15170 C  CB    . ILE   F 2  155 ? 31.809  59.608  25.151  1.00 31.88  ? 157 ILE   B CB    1 
ATOM   15171 C  CG1   . ILE   F 2  155 ? 31.459  59.846  23.678  1.00 29.94  ? 157 ILE   B CG1   1 
ATOM   15172 C  CG2   . ILE   F 2  155 ? 31.544  60.837  25.993  1.00 28.24  ? 157 ILE   B CG2   1 
ATOM   15173 C  CD1   . ILE   F 2  155 ? 29.957  59.980  23.418  1.00 35.44  ? 157 ILE   B CD1   1 
ATOM   15174 N  N     . ARG   F 2  156 ? 33.511  58.105  27.469  1.00 30.18  ? 158 ARG   B N     1 
ATOM   15175 C  CA    . ARG   F 2  156 ? 33.971  58.095  28.848  1.00 31.84  ? 158 ARG   B CA    1 
ATOM   15176 C  C     . ARG   F 2  156 ? 35.491  58.109  28.926  1.00 39.83  ? 158 ARG   B C     1 
ATOM   15177 O  O     . ARG   F 2  156 ? 36.062  58.650  29.883  1.00 40.47  ? 158 ARG   B O     1 
ATOM   15178 C  CB    . ARG   F 2  156 ? 33.414  56.881  29.597  1.00 30.31  ? 158 ARG   B CB    1 
ATOM   15179 C  CG    . ARG   F 2  156 ? 33.834  56.875  31.061  1.00 33.00  ? 158 ARG   B CG    1 
ATOM   15180 C  CD    . ARG   F 2  156 ? 33.215  55.750  31.823  1.00 34.48  ? 158 ARG   B CD    1 
ATOM   15181 N  NE    . ARG   F 2  156 ? 33.536  55.893  33.232  1.00 38.77  ? 158 ARG   B NE    1 
ATOM   15182 C  CZ    . ARG   F 2  156 ? 33.409  54.933  34.141  1.00 44.36  ? 158 ARG   B CZ    1 
ATOM   15183 N  NH1   . ARG   F 2  156 ? 32.928  53.740  33.830  1.00 38.52  ? 158 ARG   B NH1   1 
ATOM   15184 N  NH2   . ARG   F 2  156 ? 33.784  55.173  35.397  1.00 47.05  ? 158 ARG   B NH2   1 
ATOM   15185 N  N     . GLU   F 2  157 ? 36.164  57.508  27.944  1.00 46.44  ? 159 GLU   B N     1 
ATOM   15186 C  CA    . GLU   F 2  157 ? 37.618  57.451  27.985  1.00 42.79  ? 159 GLU   B CA    1 
ATOM   15187 C  C     . GLU   F 2  157 ? 38.230  58.796  27.629  1.00 42.14  ? 159 GLU   B C     1 
ATOM   15188 O  O     . GLU   F 2  157 ? 39.285  59.150  28.168  1.00 45.46  ? 159 GLU   B O     1 
ATOM   15189 C  CB    . GLU   F 2  157 ? 38.112  56.339  27.068  1.00 33.32  ? 159 GLU   B CB    1 
ATOM   15190 C  CG    . GLU   F 2  157 ? 39.494  56.533  26.526  1.00 44.07  ? 159 GLU   B CG    1 
ATOM   15191 C  CD    . GLU   F 2  157 ? 40.033  55.284  25.842  1.00 54.68  ? 159 GLU   B CD    1 
ATOM   15192 O  OE1   . GLU   F 2  157 ? 39.720  55.064  24.642  1.00 40.76  ? 159 GLU   B OE1   1 
ATOM   15193 O  OE2   . GLU   F 2  157 ? 40.765  54.522  26.523  1.00 56.66  ? 159 GLU   B OE2   1 
ATOM   15194 N  N     . GLU   F 2  158 ? 37.562  59.567  26.768  1.00 35.15  ? 160 GLU   B N     1 
ATOM   15195 C  CA    . GLU   F 2  158 ? 37.980  60.932  26.475  1.00 37.01  ? 160 GLU   B CA    1 
ATOM   15196 C  C     . GLU   F 2  158 ? 37.561  61.931  27.558  1.00 44.63  ? 160 GLU   B C     1 
ATOM   15197 O  O     . GLU   F 2  158 ? 38.248  62.936  27.774  1.00 33.16  ? 160 GLU   B O     1 
ATOM   15198 C  CB    . GLU   F 2  158 ? 37.399  61.369  25.134  1.00 35.75  ? 160 GLU   B CB    1 
ATOM   15199 C  CG    . GLU   F 2  158 ? 38.168  60.875  23.931  1.00 52.73  ? 160 GLU   B CG    1 
ATOM   15200 C  CD    . GLU   F 2  158 ? 37.944  61.749  22.715  1.00 62.06  ? 160 GLU   B CD    1 
ATOM   15201 O  OE1   . GLU   F 2  158 ? 37.946  63.005  22.872  1.00 40.16  ? 160 GLU   B OE1   1 
ATOM   15202 O  OE2   . GLU   F 2  158 ? 37.760  61.168  21.609  1.00 57.96  ? 160 GLU   B OE2   1 
ATOM   15203 N  N     . TYR   F 2  159 ? 36.436  61.693  28.221  1.00 38.28  ? 161 TYR   B N     1 
ATOM   15204 C  CA    . TYR   F 2  159 ? 35.884  62.617  29.209  1.00 33.84  ? 161 TYR   B CA    1 
ATOM   15205 C  C     . TYR   F 2  159 ? 35.623  61.856  30.491  1.00 37.27  ? 161 TYR   B C     1 
ATOM   15206 O  O     . TYR   F 2  159 ? 34.491  61.782  30.967  1.00 38.96  ? 161 TYR   B O     1 
ATOM   15207 C  CB    . TYR   F 2  159 ? 34.606  63.259  28.688  1.00 35.21  ? 161 TYR   B CB    1 
ATOM   15208 C  CG    . TYR   F 2  159 ? 34.809  63.954  27.370  1.00 42.85  ? 161 TYR   B CG    1 
ATOM   15209 C  CD1   . TYR   F 2  159 ? 34.712  63.256  26.177  1.00 45.37  ? 161 TYR   B CD1   1 
ATOM   15210 C  CD2   . TYR   F 2  159 ? 35.099  65.307  27.314  1.00 33.18  ? 161 TYR   B CD2   1 
ATOM   15211 C  CE1   . TYR   F 2  159 ? 34.889  63.891  24.965  1.00 42.70  ? 161 TYR   B CE1   1 
ATOM   15212 C  CE2   . TYR   F 2  159 ? 35.282  65.945  26.113  1.00 39.23  ? 161 TYR   B CE2   1 
ATOM   15213 C  CZ    . TYR   F 2  159 ? 35.176  65.236  24.939  1.00 46.45  ? 161 TYR   B CZ    1 
ATOM   15214 O  OH    . TYR   F 2  159 ? 35.352  65.871  23.725  1.00 58.98  ? 161 TYR   B OH    1 
ATOM   15215 N  N     . PRO   F 2  160 ? 36.664  61.261  31.072  1.00 42.74  ? 162 PRO   B N     1 
ATOM   15216 C  CA    . PRO   F 2  160 ? 36.462  60.364  32.218  1.00 30.97  ? 162 PRO   B CA    1 
ATOM   15217 C  C     . PRO   F 2  160 ? 35.799  61.024  33.414  1.00 34.60  ? 162 PRO   B C     1 
ATOM   15218 O  O     . PRO   F 2  160 ? 35.360  60.304  34.322  1.00 38.97  ? 162 PRO   B O     1 
ATOM   15219 C  CB    . PRO   F 2  160 ? 37.892  59.916  32.564  1.00 29.23  ? 162 PRO   B CB    1 
ATOM   15220 C  CG    . PRO   F 2  160 ? 38.744  60.994  32.066  1.00 34.78  ? 162 PRO   B CG    1 
ATOM   15221 C  CD    . PRO   F 2  160 ? 38.090  61.518  30.815  1.00 39.60  ? 162 PRO   B CD    1 
ATOM   15222 N  N     . ASP   F 2  161 ? 35.732  62.354  33.458  1.00 36.26  ? 163 ASP   B N     1 
ATOM   15223 C  CA    . ASP   F 2  161 ? 35.197  63.070  34.608  1.00 28.25  ? 163 ASP   B CA    1 
ATOM   15224 C  C     . ASP   F 2  161 ? 33.958  63.907  34.298  1.00 33.94  ? 163 ASP   B C     1 
ATOM   15225 O  O     . ASP   F 2  161 ? 33.580  64.734  35.127  1.00 36.26  ? 163 ASP   B O     1 
ATOM   15226 C  CB    . ASP   F 2  161 ? 36.274  63.973  35.185  1.00 36.44  ? 163 ASP   B CB    1 
ATOM   15227 C  CG    . ASP   F 2  161 ? 36.518  65.183  34.320  1.00 43.17  ? 163 ASP   B CG    1 
ATOM   15228 O  OD1   . ASP   F 2  161 ? 35.946  65.253  33.219  1.00 36.91  ? 163 ASP   B OD1   1 
ATOM   15229 O  OD2   . ASP   F 2  161 ? 37.274  66.073  34.742  1.00 59.86  ? 163 ASP   B OD2   1 
ATOM   15230 N  N     . ARG   F 2  162 ? 33.348  63.761  33.117  1.00 36.48  ? 164 ARG   B N     1 
ATOM   15231 C  CA    . ARG   F 2  162 ? 32.036  64.338  32.851  1.00 33.13  ? 164 ARG   B CA    1 
ATOM   15232 C  C     . ARG   F 2  162 ? 30.950  63.295  33.137  1.00 31.18  ? 164 ARG   B C     1 
ATOM   15233 O  O     . ARG   F 2  162 ? 31.235  62.126  33.398  1.00 31.85  ? 164 ARG   B O     1 
ATOM   15234 C  CB    . ARG   F 2  162 ? 31.953  64.861  31.419  1.00 34.53  ? 164 ARG   B CB    1 
ATOM   15235 C  CG    . ARG   F 2  162 ? 33.055  65.852  31.036  1.00 36.58  ? 164 ARG   B CG    1 
ATOM   15236 C  CD    . ARG   F 2  162 ? 32.874  67.237  31.657  1.00 41.61  ? 164 ARG   B CD    1 
ATOM   15237 N  NE    . ARG   F 2  162 ? 33.844  67.542  32.710  1.00 62.19  ? 164 ARG   B NE    1 
ATOM   15238 C  CZ    . ARG   F 2  162 ? 33.551  68.210  33.826  1.00 71.89  ? 164 ARG   B CZ    1 
ATOM   15239 N  NH1   . ARG   F 2  162 ? 32.317  68.628  34.079  1.00 64.78  ? 164 ARG   B NH1   1 
ATOM   15240 N  NH2   . ARG   F 2  162 ? 34.514  68.452  34.720  1.00 57.90  ? 164 ARG   B NH2   1 
ATOM   15241 N  N     . ILE   F 2  163 ? 29.696  63.731  33.143  1.00 30.24  ? 165 ILE   B N     1 
ATOM   15242 C  CA    . ILE   F 2  163 ? 28.594  62.849  33.516  1.00 28.50  ? 165 ILE   B CA    1 
ATOM   15243 C  C     . ILE   F 2  163 ? 28.036  62.212  32.258  1.00 28.31  ? 165 ILE   B C     1 
ATOM   15244 O  O     . ILE   F 2  163 ? 27.807  62.896  31.255  1.00 33.65  ? 165 ILE   B O     1 
ATOM   15245 C  CB    . ILE   F 2  163 ? 27.491  63.605  34.291  1.00 33.46  ? 165 ILE   B CB    1 
ATOM   15246 C  CG1   . ILE   F 2  163 ? 27.996  64.103  35.655  1.00 28.47  ? 165 ILE   B CG1   1 
ATOM   15247 C  CG2   . ILE   F 2  163 ? 26.264  62.676  34.524  1.00 27.33  ? 165 ILE   B CG2   1 
ATOM   15248 C  CD1   . ILE   F 2  163 ? 28.205  62.984  36.692  1.00 23.19  ? 165 ILE   B CD1   1 
ATOM   15249 N  N     . MET   F 2  164 ? 27.827  60.898  32.304  1.00 27.12  ? 166 MET   B N     1 
ATOM   15250 C  CA    . MET   F 2  164 ? 27.217  60.161  31.208  1.00 25.36  ? 166 MET   B CA    1 
ATOM   15251 C  C     . MET   F 2  164 ? 25.785  59.781  31.589  1.00 37.25  ? 166 MET   B C     1 
ATOM   15252 O  O     . MET   F 2  164 ? 25.549  59.075  32.585  1.00 26.78  ? 166 MET   B O     1 
ATOM   15253 C  CB    . MET   F 2  164 ? 28.029  58.919  30.848  1.00 21.14  ? 166 MET   B CB    1 
ATOM   15254 C  CG    . MET   F 2  164 ? 27.457  58.186  29.644  1.00 21.71  ? 166 MET   B CG    1 
ATOM   15255 S  SD    . MET   F 2  164 ? 27.598  59.223  28.185  1.00 39.44  ? 166 MET   B SD    1 
ATOM   15256 C  CE    . MET   F 2  164 ? 26.354  58.453  27.184  1.00 38.15  ? 166 MET   B CE    1 
ATOM   15257 N  N     . ASN   F 2  165 ? 24.839  60.231  30.775  1.00 38.47  ? 167 ASN   B N     1 
ATOM   15258 C  CA    . ASN   F 2  165 ? 23.415  60.115  31.046  1.00 40.74  ? 167 ASN   B CA    1 
ATOM   15259 C  C     . ASN   F 2  165 ? 22.748  59.535  29.810  1.00 36.53  ? 167 ASN   B C     1 
ATOM   15260 O  O     . ASN   F 2  165 ? 23.033  59.969  28.687  1.00 33.55  ? 167 ASN   B O     1 
ATOM   15261 C  CB    . ASN   F 2  165 ? 22.837  61.499  31.393  1.00 43.05  ? 167 ASN   B CB    1 
ATOM   15262 C  CG    . ASN   F 2  165 ? 21.366  61.467  31.737  1.00 38.85  ? 167 ASN   B CG    1 
ATOM   15263 O  OD1   . ASN   F 2  165 ? 21.009  61.320  32.899  1.00 44.75  ? 167 ASN   B OD1   1 
ATOM   15264 N  ND2   . ASN   F 2  165 ? 20.505  61.651  30.735  1.00 27.86  ? 167 ASN   B ND2   1 
ATOM   15265 N  N     . THR   F 2  166 ? 21.869  58.562  30.008  1.00 30.77  ? 168 THR   B N     1 
ATOM   15266 C  CA    A THR   F 2  166 ? 21.163  57.966  28.890  1.00 67.92  ? 168 THR   B CA    1 
ATOM   15267 C  CA    B THR   F 2  166 ? 21.172  57.941  28.895  0.00 76.62  ? 168 THR   B CA    1 
ATOM   15268 C  C     . THR   F 2  166 ? 19.696  57.785  29.224  1.00 38.71  ? 168 THR   B C     1 
ATOM   15269 O  O     . THR   F 2  166 ? 19.314  57.578  30.382  1.00 31.58  ? 168 THR   B O     1 
ATOM   15270 C  CB    A THR   F 2  166 ? 21.701  56.599  28.502  1.00 36.20  ? 168 THR   B CB    1 
ATOM   15271 C  CB    B THR   F 2  166 ? 21.769  56.569  28.546  0.00 36.37  ? 168 THR   B CB    1 
ATOM   15272 O  OG1   A THR   F 2  166 ? 21.089  55.622  29.338  1.00 27.49  ? 168 THR   B OG1   1 
ATOM   15273 O  OG1   B THR   F 2  166 ? 21.693  55.707  29.688  0.00 32.64  ? 168 THR   B OG1   1 
ATOM   15274 C  CG2   A THR   F 2  166 ? 23.206  56.537  28.638  1.00 32.31  ? 168 THR   B CG2   1 
ATOM   15275 C  CG2   B THR   F 2  166 ? 23.223  56.714  28.121  0.00 34.83  ? 168 THR   B CG2   1 
ATOM   15276 N  N     . PHE   F 2  167 ? 18.881  57.878  28.182  1.00 38.82  ? 169 PHE   B N     1 
ATOM   15277 C  CA    . PHE   F 2  167 ? 17.486  57.468  28.198  1.00 27.57  ? 169 PHE   B CA    1 
ATOM   15278 C  C     . PHE   F 2  167 ? 17.481  56.181  27.390  1.00 24.95  ? 169 PHE   B C     1 
ATOM   15279 O  O     . PHE   F 2  167 ? 17.604  56.223  26.164  1.00 31.00  ? 169 PHE   B O     1 
ATOM   15280 C  CB    . PHE   F 2  167 ? 16.592  58.529  27.579  1.00 27.86  ? 169 PHE   B CB    1 
ATOM   15281 C  CG    . PHE   F 2  167 ? 16.518  59.795  28.364  1.00 32.07  ? 169 PHE   B CG    1 
ATOM   15282 C  CD1   . PHE   F 2  167 ? 17.609  60.642  28.443  1.00 26.75  ? 169 PHE   B CD1   1 
ATOM   15283 C  CD2   . PHE   F 2  167 ? 15.343  60.152  29.015  1.00 29.31  ? 169 PHE   B CD2   1 
ATOM   15284 C  CE1   . PHE   F 2  167 ? 17.535  61.810  29.158  1.00 31.95  ? 169 PHE   B CE1   1 
ATOM   15285 C  CE2   . PHE   F 2  167 ? 15.261  61.329  29.718  1.00 26.70  ? 169 PHE   B CE2   1 
ATOM   15286 C  CZ    . PHE   F 2  167 ? 16.358  62.154  29.800  1.00 25.28  ? 169 PHE   B CZ    1 
ATOM   15287 N  N     . SER   F 2  168 ? 17.385  55.038  28.065  1.00 23.39  ? 170 SER   B N     1 
ATOM   15288 C  CA    . SER   F 2  168 ? 17.561  53.731  27.419  1.00 30.38  ? 170 SER   B CA    1 
ATOM   15289 C  C     . SER   F 2  168 ? 16.220  53.007  27.267  1.00 19.64  ? 170 SER   B C     1 
ATOM   15290 O  O     . SER   F 2  168 ? 15.683  52.506  28.255  1.00 21.21  ? 170 SER   B O     1 
ATOM   15291 C  CB    . SER   F 2  168 ? 18.549  52.881  28.219  1.00 27.87  ? 170 SER   B CB    1 
ATOM   15292 O  OG    . SER   F 2  168 ? 19.746  53.595  28.477  1.00 28.22  ? 170 SER   B OG    1 
ATOM   15293 N  N     . VAL   F 2  169 ? 15.703  52.919  26.034  1.00 16.15  ? 171 VAL   B N     1 
ATOM   15294 C  CA    . VAL   F 2  169 ? 14.429  52.235  25.770  1.00 22.61  ? 171 VAL   B CA    1 
ATOM   15295 C  C     . VAL   F 2  169 ? 14.621  50.719  25.757  1.00 23.55  ? 171 VAL   B C     1 
ATOM   15296 O  O     . VAL   F 2  169 ? 15.352  50.187  24.911  1.00 19.44  ? 171 VAL   B O     1 
ATOM   15297 C  CB    . VAL   F 2  169 ? 13.791  52.689  24.449  1.00 22.64  ? 171 VAL   B CB    1 
ATOM   15298 C  CG1   . VAL   F 2  169 ? 12.438  52.015  24.323  1.00 20.75  ? 171 VAL   B CG1   1 
ATOM   15299 C  CG2   . VAL   F 2  169 ? 13.624  54.181  24.398  1.00 21.96  ? 171 VAL   B CG2   1 
ATOM   15300 N  N     . MET   F 2  170 ? 13.925  50.016  26.681  1.00 16.40  ? 172 MET   B N     1 
ATOM   15301 C  CA    . MET   F 2  170 ? 14.021  48.567  26.885  1.00 26.72  ? 172 MET   B CA    1 
ATOM   15302 C  C     . MET   F 2  170 ? 12.963  47.826  26.062  1.00 31.06  ? 172 MET   B C     1 
ATOM   15303 O  O     . MET   F 2  170 ? 11.811  48.278  25.959  1.00 23.57  ? 172 MET   B O     1 
ATOM   15304 C  CB    . MET   F 2  170 ? 13.833  48.180  28.354  1.00 22.92  ? 172 MET   B CB    1 
ATOM   15305 C  CG    . MET   F 2  170 ? 14.398  49.150  29.354  1.00 33.44  ? 172 MET   B CG    1 
ATOM   15306 S  SD    . MET   F 2  170 ? 16.180  49.035  29.527  0.56 30.64  ? 172 MET   B SD    1 
ATOM   15307 C  CE    . MET   F 2  170 ? 16.390  47.268  29.711  0.56 27.09  ? 172 MET   B CE    1 
ATOM   15308 N  N     . PRO   F 2  171 ? 13.354  46.669  25.542  1.00 22.67  ? 173 PRO   B N     1 
ATOM   15309 C  CA    . PRO   F 2  171 ? 12.487  45.919  24.634  1.00 28.19  ? 173 PRO   B CA    1 
ATOM   15310 C  C     . PRO   F 2  171 ? 11.448  45.083  25.362  1.00 23.63  ? 173 PRO   B C     1 
ATOM   15311 O  O     . PRO   F 2  171 ? 11.659  44.620  26.484  1.00 22.85  ? 173 PRO   B O     1 
ATOM   15312 C  CB    . PRO   F 2  171 ? 13.479  45.013  23.894  1.00 21.40  ? 173 PRO   B CB    1 
ATOM   15313 C  CG    . PRO   F 2  171 ? 14.489  44.729  24.916  1.00 21.35  ? 173 PRO   B CG    1 
ATOM   15314 C  CD    . PRO   F 2  171 ? 14.675  46.041  25.668  1.00 23.36  ? 173 PRO   B CD    1 
ATOM   15315 N  N     . SER   F 2  172 ? 10.333  44.838  24.666  1.00 21.10  ? 174 SER   B N     1 
ATOM   15316 C  CA    . SER   F 2  172 ? 9.251   44.022  25.196  1.00 19.18  ? 174 SER   B CA    1 
ATOM   15317 C  C     . SER   F 2  172 ? 8.570   43.206  24.100  1.00 19.07  ? 174 SER   B C     1 
ATOM   15318 O  O     . SER   F 2  172 ? 8.258   43.756  23.042  1.00 24.45  ? 174 SER   B O     1 
ATOM   15319 C  CB    . SER   F 2  172 ? 8.242   44.926  25.908  1.00 21.80  ? 174 SER   B CB    1 
ATOM   15320 O  OG    . SER   F 2  172 ? 6.901   44.557  25.674  1.00 24.52  ? 174 SER   B OG    1 
ATOM   15321 N  N     . PRO   F 2  173 ? 8.315   41.913  24.311  1.00 25.56  ? 175 PRO   B N     1 
ATOM   15322 C  CA    . PRO   F 2  173 ? 7.601   41.143  23.280  1.00 24.94  ? 175 PRO   B CA    1 
ATOM   15323 C  C     . PRO   F 2  173 ? 6.168   41.600  23.054  1.00 27.46  ? 175 PRO   B C     1 
ATOM   15324 O  O     . PRO   F 2  173 ? 5.534   41.118  22.109  1.00 33.37  ? 175 PRO   B O     1 
ATOM   15325 C  CB    . PRO   F 2  173 ? 7.661   39.693  23.798  1.00 19.91  ? 175 PRO   B CB    1 
ATOM   15326 C  CG    . PRO   F 2  173 ? 8.031   39.762  25.190  1.00 24.82  ? 175 PRO   B CG    1 
ATOM   15327 C  CD    . PRO   F 2  173 ? 8.726   41.075  25.454  1.00 32.74  ? 175 PRO   B CD    1 
ATOM   15328 N  N     . LYS   F 2  174 ? 5.635   42.510  23.877  1.00 28.23  ? 176 LYS   B N     1 
ATOM   15329 C  CA    . LYS   F 2  174 ? 4.315   43.074  23.599  1.00 30.85  ? 176 LYS   B CA    1 
ATOM   15330 C  C     . LYS   F 2  174 ? 4.352   44.027  22.420  1.00 33.20  ? 176 LYS   B C     1 
ATOM   15331 O  O     . LYS   F 2  174 ? 3.308   44.273  21.802  1.00 31.82  ? 176 LYS   B O     1 
ATOM   15332 C  CB    . LYS   F 2  174 ? 3.751   43.807  24.832  1.00 29.71  ? 176 LYS   B CB    1 
ATOM   15333 C  CG    . LYS   F 2  174 ? 3.586   42.920  26.076  1.00 32.90  ? 176 LYS   B CG    1 
ATOM   15334 C  CD    . LYS   F 2  174 ? 2.960   43.689  27.244  1.00 42.25  ? 176 LYS   B CD    1 
ATOM   15335 C  CE    . LYS   F 2  174 ? 2.567   42.756  28.388  1.00 45.77  ? 176 LYS   B CE    1 
ATOM   15336 N  NZ    . LYS   F 2  174 ? 1.858   43.471  29.502  1.00 53.39  ? 176 LYS   B NZ    1 
ATOM   15337 N  N     . VAL   F 2  175 ? 5.533   44.550  22.080  1.00 32.63  ? 177 VAL   B N     1 
ATOM   15338 C  CA    . VAL   F 2  175 ? 5.639   45.607  21.082  1.00 25.08  ? 177 VAL   B CA    1 
ATOM   15339 C  C     . VAL   F 2  175 ? 6.436   45.149  19.868  1.00 23.76  ? 177 VAL   B C     1 
ATOM   15340 O  O     . VAL   F 2  175 ? 6.263   45.681  18.769  1.00 28.42  ? 177 VAL   B O     1 
ATOM   15341 C  CB    . VAL   F 2  175 ? 6.249   46.871  21.709  1.00 22.04  ? 177 VAL   B CB    1 
ATOM   15342 C  CG1   . VAL   F 2  175 ? 6.702   47.836  20.632  1.00 24.29  ? 177 VAL   B CG1   1 
ATOM   15343 C  CG2   . VAL   F 2  175 ? 5.236   47.525  22.636  1.00 22.53  ? 177 VAL   B CG2   1 
ATOM   15344 N  N     . SER   F 2  176 ? 7.320   44.173  20.039  1.00 22.03  ? 178 SER   B N     1 
ATOM   15345 C  CA    . SER   F 2  176 ? 8.186   43.798  18.932  1.00 25.22  ? 178 SER   B CA    1 
ATOM   15346 C  C     . SER   F 2  176 ? 8.356   42.281  18.909  1.00 29.31  ? 178 SER   B C     1 
ATOM   15347 O  O     . SER   F 2  176 ? 8.088   41.599  19.902  1.00 29.03  ? 178 SER   B O     1 
ATOM   15348 C  CB    . SER   F 2  176 ? 9.525   44.528  19.017  1.00 18.29  ? 178 SER   B CB    1 
ATOM   15349 O  OG    . SER   F 2  176 ? 10.331  43.973  20.045  1.00 34.54  ? 178 SER   B OG    1 
ATOM   15350 N  N     . ASP   F 2  177 ? 8.791   41.752  17.745  1.00 21.51  ? 179 ASP   B N     1 
ATOM   15351 C  CA    . ASP   F 2  177 ? 8.847   40.306  17.510  1.00 29.92  ? 179 ASP   B CA    1 
ATOM   15352 C  C     . ASP   F 2  177 ? 10.198  39.829  16.948  1.00 30.80  ? 179 ASP   B C     1 
ATOM   15353 O  O     . ASP   F 2  177 ? 10.261  38.791  16.288  1.00 28.56  ? 179 ASP   B O     1 
ATOM   15354 C  CB    . ASP   F 2  177 ? 7.697   39.857  16.596  1.00 24.94  ? 179 ASP   B CB    1 
ATOM   15355 C  CG    . ASP   F 2  177 ? 7.606   40.660  15.274  1.00 33.00  ? 179 ASP   B CG    1 
ATOM   15356 O  OD1   . ASP   F 2  177 ? 8.593   41.275  14.834  1.00 31.77  ? 179 ASP   B OD1   1 
ATOM   15357 O  OD2   . ASP   F 2  177 ? 6.520   40.672  14.658  1.00 34.89  ? 179 ASP   B OD2   1 
ATOM   15358 N  N     . THR   F 2  178 ? 11.289  40.549  17.221  1.00 26.00  ? 180 THR   B N     1 
ATOM   15359 C  CA    . THR   F 2  178 ? 12.634  40.077  16.906  1.00 20.28  ? 180 THR   B CA    1 
ATOM   15360 C  C     . THR   F 2  178 ? 13.156  39.174  18.031  1.00 26.35  ? 180 THR   B C     1 
ATOM   15361 O  O     . THR   F 2  178 ? 13.241  39.581  19.192  1.00 27.26  ? 180 THR   B O     1 
ATOM   15362 C  CB    . THR   F 2  178 ? 13.569  41.264  16.701  1.00 30.84  ? 180 THR   B CB    1 
ATOM   15363 O  OG1   . THR   F 2  178 ? 13.125  42.067  15.590  1.00 26.52  ? 180 THR   B OG1   1 
ATOM   15364 C  CG2   . THR   F 2  178 ? 15.034  40.790  16.519  1.00 17.25  ? 180 THR   B CG2   1 
ATOM   15365 N  N     . VAL   F 2  179 ? 13.528  37.946  17.692  1.00 29.40  ? 181 VAL   B N     1 
ATOM   15366 C  CA    . VAL   F 2  179 ? 13.891  37.003  18.733  1.00 22.93  ? 181 VAL   B CA    1 
ATOM   15367 C  C     . VAL   F 2  179 ? 15.201  37.372  19.443  1.00 23.99  ? 181 VAL   B C     1 
ATOM   15368 O  O     . VAL   F 2  179 ? 15.406  36.960  20.593  1.00 25.73  ? 181 VAL   B O     1 
ATOM   15369 C  CB    . VAL   F 2  179 ? 13.939  35.602  18.102  1.00 19.53  ? 181 VAL   B CB    1 
ATOM   15370 C  CG1   . VAL   F 2  179 ? 15.262  35.405  17.341  1.00 16.77  ? 181 VAL   B CG1   1 
ATOM   15371 C  CG2   . VAL   F 2  179 ? 13.671  34.521  19.134  1.00 17.00  ? 181 VAL   B CG2   1 
ATOM   15372 N  N     . VAL   F 2  180 ? 16.098  38.147  18.816  1.00 23.13  ? 182 VAL   B N     1 
ATOM   15373 C  CA    . VAL   F 2  180 ? 17.406  38.385  19.431  1.00 20.27  ? 182 VAL   B CA    1 
ATOM   15374 C  C     . VAL   F 2  180 ? 17.439  39.614  20.337  1.00 24.59  ? 182 VAL   B C     1 
ATOM   15375 O  O     . VAL   F 2  180 ? 18.488  39.902  20.930  1.00 25.34  ? 182 VAL   B O     1 
ATOM   15376 C  CB    . VAL   F 2  180 ? 18.546  38.486  18.394  1.00 18.24  ? 182 VAL   B CB    1 
ATOM   15377 C  CG1   . VAL   F 2  180 ? 18.741  37.144  17.694  1.00 16.55  ? 182 VAL   B CG1   1 
ATOM   15378 C  CG2   . VAL   F 2  180 ? 18.354  39.648  17.414  1.00 12.82  ? 182 VAL   B CG2   1 
ATOM   15379 N  N     . GLU   F 2  181 ? 16.315  40.309  20.521  1.00 31.10  ? 183 GLU   B N     1 
ATOM   15380 C  CA    . GLU   F 2  181 ? 16.332  41.510  21.356  1.00 25.54  ? 183 GLU   B CA    1 
ATOM   15381 C  C     . GLU   F 2  181 ? 16.832  41.236  22.767  1.00 22.65  ? 183 GLU   B C     1 
ATOM   15382 O  O     . GLU   F 2  181 ? 17.589  42.068  23.288  1.00 27.65  ? 183 GLU   B O     1 
ATOM   15383 C  CB    . GLU   F 2  181 ? 14.941  42.170  21.367  1.00 20.17  ? 183 GLU   B CB    1 
ATOM   15384 C  CG    . GLU   F 2  181 ? 14.432  42.512  19.956  1.00 18.53  ? 183 GLU   B CG    1 
ATOM   15385 C  CD    . GLU   F 2  181 ? 13.628  43.781  19.868  1.00 22.32  ? 183 GLU   B CD    1 
ATOM   15386 O  OE1   . GLU   F 2  181 ? 13.467  44.491  20.864  1.00 27.53  ? 183 GLU   B OE1   1 
ATOM   15387 O  OE2   . GLU   F 2  181 ? 13.134  44.087  18.777  1.00 33.46  ? 183 GLU   B OE2   1 
ATOM   15388 N  N     . PRO   F 2  182 ? 16.474  40.133  23.429  1.00 23.72  ? 184 PRO   B N     1 
ATOM   15389 C  CA    . PRO   F 2  182 ? 17.017  39.887  24.772  1.00 20.17  ? 184 PRO   B CA    1 
ATOM   15390 C  C     . PRO   F 2  182 ? 18.524  39.772  24.805  1.00 21.28  ? 184 PRO   B C     1 
ATOM   15391 O  O     . PRO   F 2  182 ? 19.135  40.118  25.820  1.00 23.35  ? 184 PRO   B O     1 
ATOM   15392 C  CB    . PRO   F 2  182 ? 16.334  38.573  25.181  1.00 19.79  ? 184 PRO   B CB    1 
ATOM   15393 C  CG    . PRO   F 2  182 ? 15.074  38.621  24.526  1.00 17.21  ? 184 PRO   B CG    1 
ATOM   15394 C  CD    . PRO   F 2  182 ? 15.358  39.226  23.152  1.00 23.66  ? 184 PRO   B CD    1 
ATOM   15395 N  N     . TYR   F 2  183 ? 19.141  39.304  23.721  1.00 23.99  ? 185 TYR   B N     1 
ATOM   15396 C  CA    . TYR   F 2  183 ? 20.599  39.351  23.603  1.00 26.84  ? 185 TYR   B CA    1 
ATOM   15397 C  C     . TYR   F 2  183 ? 21.119  40.792  23.567  1.00 26.52  ? 185 TYR   B C     1 
ATOM   15398 O  O     . TYR   F 2  183 ? 22.011  41.167  24.342  1.00 21.42  ? 185 TYR   B O     1 
ATOM   15399 C  CB    . TYR   F 2  183 ? 21.041  38.600  22.351  1.00 26.25  ? 185 TYR   B CB    1 
ATOM   15400 C  CG    . TYR   F 2  183 ? 21.005  37.098  22.473  1.00 27.38  ? 185 TYR   B CG    1 
ATOM   15401 C  CD1   . TYR   F 2  183 ? 20.945  36.484  23.708  1.00 21.52  ? 185 TYR   B CD1   1 
ATOM   15402 C  CD2   . TYR   F 2  183 ? 21.049  36.296  21.343  1.00 26.35  ? 185 TYR   B CD2   1 
ATOM   15403 C  CE1   . TYR   F 2  183 ? 20.926  35.111  23.816  1.00 23.35  ? 185 TYR   B CE1   1 
ATOM   15404 C  CE2   . TYR   F 2  183 ? 21.035  34.913  21.443  1.00 29.78  ? 185 TYR   B CE2   1 
ATOM   15405 C  CZ    . TYR   F 2  183 ? 20.977  34.323  22.685  1.00 28.70  ? 185 TYR   B CZ    1 
ATOM   15406 O  OH    . TYR   F 2  183 ? 20.972  32.940  22.793  1.00 28.46  ? 185 TYR   B OH    1 
ATOM   15407 N  N     . ASN   F 2  184 ? 20.580  41.613  22.664  1.00 19.51  ? 186 ASN   B N     1 
ATOM   15408 C  CA    . ASN   F 2  184 ? 21.073  42.977  22.536  1.00 21.41  ? 186 ASN   B CA    1 
ATOM   15409 C  C     . ASN   F 2  184 ? 20.828  43.802  23.804  1.00 34.98  ? 186 ASN   B C     1 
ATOM   15410 O  O     . ASN   F 2  184 ? 21.602  44.724  24.115  1.00 35.45  ? 186 ASN   B O     1 
ATOM   15411 C  CB    . ASN   F 2  184 ? 20.425  43.650  21.328  1.00 30.44  ? 186 ASN   B CB    1 
ATOM   15412 C  CG    . ASN   F 2  184 ? 20.625  42.872  20.053  1.00 29.83  ? 186 ASN   B CG    1 
ATOM   15413 O  OD1   . ASN   F 2  184 ? 21.568  42.087  19.921  1.00 28.06  ? 186 ASN   B OD1   1 
ATOM   15414 N  ND2   . ASN   F 2  184 ? 19.731  43.073  19.109  1.00 22.49  ? 186 ASN   B ND2   1 
ATOM   15415 N  N     . ALA   F 2  185 ? 19.765  43.500  24.548  1.00 24.15  ? 187 ALA   B N     1 
ATOM   15416 C  CA    . ALA   F 2  185 ? 19.527  44.240  25.778  1.00 24.67  ? 187 ALA   B CA    1 
ATOM   15417 C  C     . ALA   F 2  185 ? 20.506  43.823  26.872  1.00 25.16  ? 187 ALA   B C     1 
ATOM   15418 O  O     . ALA   F 2  185 ? 21.021  44.678  27.598  1.00 33.60  ? 187 ALA   B O     1 
ATOM   15419 C  CB    . ALA   F 2  185 ? 18.073  44.059  26.235  1.00 27.23  ? 187 ALA   B CB    1 
ATOM   15420 N  N     . THR   F 2  186 ? 20.779  42.522  27.016  1.00 22.55  ? 188 THR   B N     1 
ATOM   15421 C  CA    . THR   F 2  186 ? 21.701  42.088  28.072  1.00 28.89  ? 188 THR   B CA    1 
ATOM   15422 C  C     . THR   F 2  186 ? 23.143  42.521  27.796  1.00 26.80  ? 188 THR   B C     1 
ATOM   15423 O  O     . THR   F 2  186 ? 23.889  42.828  28.729  1.00 31.19  ? 188 THR   B O     1 
ATOM   15424 C  CB    . THR   F 2  186 ? 21.640  40.570  28.260  1.00 27.44  ? 188 THR   B CB    1 
ATOM   15425 O  OG1   . THR   F 2  186 ? 20.266  40.155  28.334  1.00 27.88  ? 188 THR   B OG1   1 
ATOM   15426 C  CG2   . THR   F 2  186 ? 22.384  40.186  29.551  1.00 21.56  ? 188 THR   B CG2   1 
ATOM   15427 N  N     . LEU   F 2  187 ? 23.567  42.525  26.534  1.00 28.46  ? 189 LEU   B N     1 
ATOM   15428 C  CA    . LEU   F 2  187 ? 24.875  43.090  26.217  1.00 32.42  ? 189 LEU   B CA    1 
ATOM   15429 C  C     . LEU   F 2  187 ? 24.902  44.595  26.459  1.00 30.42  ? 189 LEU   B C     1 
ATOM   15430 O  O     . LEU   F 2  187 ? 25.930  45.136  26.894  1.00 32.63  ? 189 LEU   B O     1 
ATOM   15431 C  CB    . LEU   F 2  187 ? 25.268  42.751  24.770  1.00 30.97  ? 189 LEU   B CB    1 
ATOM   15432 C  CG    . LEU   F 2  187 ? 25.428  41.232  24.516  1.00 31.25  ? 189 LEU   B CG    1 
ATOM   15433 C  CD1   . LEU   F 2  187 ? 25.267  40.847  23.039  1.00 26.01  ? 189 LEU   B CD1   1 
ATOM   15434 C  CD2   . LEU   F 2  187 ? 26.758  40.713  25.069  1.00 17.04  ? 189 LEU   B CD2   1 
ATOM   15435 N  N     . SER   F 2  188 ? 23.789  45.286  26.210  1.00 25.08  ? 190 SER   B N     1 
ATOM   15436 C  CA    . SER   F 2  188 ? 23.756  46.719  26.480  1.00 21.25  ? 190 SER   B CA    1 
ATOM   15437 C  C     . SER   F 2  188 ? 23.703  47.008  27.968  1.00 23.54  ? 190 SER   B C     1 
ATOM   15438 O  O     . SER   F 2  188 ? 24.326  47.968  28.433  1.00 25.95  ? 190 SER   B O     1 
ATOM   15439 C  CB    . SER   F 2  188 ? 22.567  47.369  25.788  1.00 28.72  ? 190 SER   B CB    1 
ATOM   15440 O  OG    . SER   F 2  188 ? 22.864  47.550  24.417  1.00 37.06  ? 190 SER   B OG    1 
ATOM   15441 N  N     . VAL   F 2  189 ? 22.965  46.206  28.736  1.00 21.22  ? 191 VAL   B N     1 
ATOM   15442 C  CA    . VAL   F 2  189 ? 22.808  46.543  30.146  1.00 26.40  ? 191 VAL   B CA    1 
ATOM   15443 C  C     . VAL   F 2  189 ? 24.138  46.380  30.858  1.00 26.37  ? 191 VAL   B C     1 
ATOM   15444 O  O     . VAL   F 2  189 ? 24.525  47.206  31.688  1.00 32.19  ? 191 VAL   B O     1 
ATOM   15445 C  CB    . VAL   F 2  189 ? 21.683  45.710  30.793  1.00 26.78  ? 191 VAL   B CB    1 
ATOM   15446 C  CG1   . VAL   F 2  189 ? 21.786  45.741  32.321  1.00 20.64  ? 191 VAL   B CG1   1 
ATOM   15447 C  CG2   . VAL   F 2  189 ? 20.288  46.192  30.309  1.00 18.60  ? 191 VAL   B CG2   1 
ATOM   15448 N  N     . HIS   F 2  190 ? 24.874  45.335  30.509  1.00 29.16  ? 192 HIS   B N     1 
ATOM   15449 C  CA    . HIS   F 2  190 ? 26.220  45.140  31.029  1.00 23.43  ? 192 HIS   B CA    1 
ATOM   15450 C  C     . HIS   F 2  190 ? 27.058  46.391  30.831  1.00 33.69  ? 192 HIS   B C     1 
ATOM   15451 O  O     . HIS   F 2  190 ? 27.744  46.852  31.751  1.00 36.48  ? 192 HIS   B O     1 
ATOM   15452 C  CB    . HIS   F 2  190 ? 26.841  43.946  30.319  1.00 29.35  ? 192 HIS   B CB    1 
ATOM   15453 C  CG    . HIS   F 2  190 ? 28.248  43.672  30.718  1.00 40.50  ? 192 HIS   B CG    1 
ATOM   15454 N  ND1   . HIS   F 2  190 ? 28.661  43.692  32.034  1.00 36.99  ? 192 HIS   B ND1   1 
ATOM   15455 C  CD2   . HIS   F 2  190 ? 29.340  43.359  29.979  1.00 34.26  ? 192 HIS   B CD2   1 
ATOM   15456 C  CE1   . HIS   F 2  190 ? 29.952  43.418  32.089  1.00 47.56  ? 192 HIS   B CE1   1 
ATOM   15457 N  NE2   . HIS   F 2  190 ? 30.387  43.208  30.855  1.00 57.69  ? 192 HIS   B NE2   1 
ATOM   15458 N  N     . GLN   F 2  191 ? 26.988  46.967  29.629  1.00 30.16  ? 193 GLN   B N     1 
ATOM   15459 C  CA    . GLN   F 2  191 ? 27.714  48.190  29.329  1.00 19.09  ? 193 GLN   B CA    1 
ATOM   15460 C  C     . GLN   F 2  191 ? 27.234  49.341  30.195  1.00 31.55  ? 193 GLN   B C     1 
ATOM   15461 O  O     . GLN   F 2  191 ? 28.046  50.081  30.770  1.00 27.89  ? 193 GLN   B O     1 
ATOM   15462 C  CB    . GLN   F 2  191 ? 27.535  48.532  27.860  1.00 19.75  ? 193 GLN   B CB    1 
ATOM   15463 C  CG    . GLN   F 2  191 ? 28.079  47.504  26.916  1.00 26.68  ? 193 GLN   B CG    1 
ATOM   15464 C  CD    . GLN   F 2  191 ? 29.577  47.528  26.911  1.00 27.30  ? 193 GLN   B CD    1 
ATOM   15465 O  OE1   . GLN   F 2  191 ? 30.176  48.588  26.776  1.00 27.99  ? 193 GLN   B OE1   1 
ATOM   15466 N  NE2   . GLN   F 2  191 ? 30.196  46.366  27.091  1.00 22.22  ? 193 GLN   B NE2   1 
ATOM   15467 N  N     . LEU   F 2  192 ? 25.906  49.535  30.262  1.00 33.41  ? 194 LEU   B N     1 
ATOM   15468 C  CA    . LEU   F 2  192 ? 25.344  50.647  31.022  1.00 24.19  ? 194 LEU   B CA    1 
ATOM   15469 C  C     . LEU   F 2  192 ? 25.639  50.496  32.503  1.00 25.03  ? 194 LEU   B C     1 
ATOM   15470 O  O     . LEU   F 2  192 ? 25.841  51.496  33.207  1.00 30.41  ? 194 LEU   B O     1 
ATOM   15471 C  CB    . LEU   F 2  192 ? 23.839  50.741  30.799  1.00 26.27  ? 194 LEU   B CB    1 
ATOM   15472 C  CG    . LEU   F 2  192 ? 23.333  51.065  29.402  1.00 24.83  ? 194 LEU   B CG    1 
ATOM   15473 C  CD1   . LEU   F 2  192 ? 21.844  50.798  29.277  1.00 20.40  ? 194 LEU   B CD1   1 
ATOM   15474 C  CD2   . LEU   F 2  192 ? 23.632  52.523  29.086  1.00 32.22  ? 194 LEU   B CD2   1 
ATOM   15475 N  N     . VAL   F 2  193 ? 25.709  49.261  32.988  1.00 19.70  ? 195 VAL   B N     1 
ATOM   15476 C  CA    . VAL   F 2  193 ? 25.980  49.065  34.404  1.00 29.27  ? 195 VAL   B CA    1 
ATOM   15477 C  C     . VAL   F 2  193 ? 27.368  49.572  34.763  1.00 34.11  ? 195 VAL   B C     1 
ATOM   15478 O  O     . VAL   F 2  193 ? 27.609  49.985  35.902  1.00 40.72  ? 195 VAL   B O     1 
ATOM   15479 C  CB    . VAL   F 2  193 ? 25.784  47.583  34.786  1.00 28.32  ? 195 VAL   B CB    1 
ATOM   15480 C  CG1   . VAL   F 2  193 ? 26.753  47.167  35.858  1.00 31.08  ? 195 VAL   B CG1   1 
ATOM   15481 C  CG2   . VAL   F 2  193 ? 24.337  47.354  35.246  1.00 26.37  ? 195 VAL   B CG2   1 
ATOM   15482 N  N     . GLU   F 2  194 ? 28.289  49.580  33.801  1.00 40.80  ? 196 GLU   B N     1 
ATOM   15483 C  CA    . GLU   F 2  194 ? 29.689  49.910  34.027  1.00 30.18  ? 196 GLU   B CA    1 
ATOM   15484 C  C     . GLU   F 2  194 ? 30.048  51.350  33.691  1.00 29.93  ? 196 GLU   B C     1 
ATOM   15485 O  O     . GLU   F 2  194 ? 30.971  51.890  34.307  1.00 35.94  ? 196 GLU   B O     1 
ATOM   15486 C  CB    . GLU   F 2  194 ? 30.590  48.978  33.199  1.00 31.35  ? 196 GLU   B CB    1 
ATOM   15487 C  CG    . GLU   F 2  194 ? 30.426  47.488  33.478  1.00 37.28  ? 196 GLU   B CG    1 
ATOM   15488 C  CD    . GLU   F 2  194 ? 30.928  47.092  34.850  1.00 47.96  ? 196 GLU   B CD    1 
ATOM   15489 O  OE1   . GLU   F 2  194 ? 31.731  47.866  35.416  1.00 61.04  ? 196 GLU   B OE1   1 
ATOM   15490 O  OE2   . GLU   F 2  194 ? 30.516  46.021  35.371  1.00 49.39  ? 196 GLU   B OE2   1 
ATOM   15491 N  N     . ASN   F 2  195 ? 29.338  51.992  32.745  1.00 33.27  ? 197 ASN   B N     1 
ATOM   15492 C  CA    . ASN   F 2  195 ? 29.801  53.227  32.114  1.00 26.75  ? 197 ASN   B CA    1 
ATOM   15493 C  C     . ASN   F 2  195 ? 28.813  54.396  32.091  1.00 29.37  ? 197 ASN   B C     1 
ATOM   15494 O  O     . ASN   F 2  195 ? 29.074  55.369  31.381  1.00 30.88  ? 197 ASN   B O     1 
ATOM   15495 C  CB    . ASN   F 2  195 ? 30.209  52.954  30.662  1.00 28.77  ? 197 ASN   B CB    1 
ATOM   15496 C  CG    . ASN   F 2  195 ? 31.490  52.141  30.548  1.00 42.31  ? 197 ASN   B CG    1 
ATOM   15497 O  OD1   . ASN   F 2  195 ? 32.497  52.430  31.214  1.00 36.59  ? 197 ASN   B OD1   1 
ATOM   15498 N  ND2   . ASN   F 2  195 ? 31.457  51.107  29.692  1.00 28.63  ? 197 ASN   B ND2   1 
ATOM   15499 N  N     . THR   F 2  196 ? 27.674  54.345  32.773  1.00 19.14  ? 198 THR   B N     1 
ATOM   15500 C  CA    . THR   F 2  196 ? 26.836  55.540  32.836  1.00 24.53  ? 198 THR   B CA    1 
ATOM   15501 C  C     . THR   F 2  196 ? 26.604  55.940  34.291  1.00 27.95  ? 198 THR   B C     1 
ATOM   15502 O  O     . THR   F 2  196 ? 26.621  55.100  35.201  1.00 26.69  ? 198 THR   B O     1 
ATOM   15503 C  CB    . THR   F 2  196 ? 25.445  55.396  32.098  1.00 24.51  ? 198 THR   B CB    1 
ATOM   15504 O  OG1   . THR   F 2  196 ? 24.572  54.484  32.782  1.00 29.42  ? 198 THR   B OG1   1 
ATOM   15505 C  CG2   . THR   F 2  196 ? 25.599  54.957  30.669  1.00 17.19  ? 198 THR   B CG2   1 
ATOM   15506 N  N     . ASP   F 2  197 ? 26.377  57.238  34.500  1.00 29.75  ? 199 ASP   B N     1 
ATOM   15507 C  CA    . ASP   F 2  197 ? 26.052  57.759  35.825  1.00 27.10  ? 199 ASP   B CA    1 
ATOM   15508 C  C     . ASP   F 2  197 ? 24.558  57.722  36.134  1.00 31.26  ? 199 ASP   B C     1 
ATOM   15509 O  O     . ASP   F 2  197 ? 24.173  57.551  37.307  1.00 25.70  ? 199 ASP   B O     1 
ATOM   15510 C  CB    . ASP   F 2  197 ? 26.568  59.188  35.942  1.00 30.73  ? 199 ASP   B CB    1 
ATOM   15511 C  CG    . ASP   F 2  197 ? 28.030  59.285  35.636  1.00 30.52  ? 199 ASP   B CG    1 
ATOM   15512 O  OD1   . ASP   F 2  197 ? 28.793  58.631  36.375  1.00 32.21  ? 199 ASP   B OD1   1 
ATOM   15513 O  OD2   . ASP   F 2  197 ? 28.404  59.978  34.654  1.00 30.54  ? 199 ASP   B OD2   1 
ATOM   15514 N  N     . GLU   F 2  198 ? 23.719  57.876  35.103  1.00 25.04  ? 200 GLU   B N     1 
ATOM   15515 C  CA    . GLU   F 2  198 ? 22.271  57.828  35.241  1.00 29.23  ? 200 GLU   B CA    1 
ATOM   15516 C  C     . GLU   F 2  198 ? 21.674  57.234  33.982  1.00 26.91  ? 200 GLU   B C     1 
ATOM   15517 O  O     . GLU   F 2  198 ? 21.991  57.676  32.873  1.00 36.16  ? 200 GLU   B O     1 
ATOM   15518 C  CB    . GLU   F 2  198 ? 21.682  59.225  35.491  1.00 33.55  ? 200 GLU   B CB    1 
ATOM   15519 C  CG    . GLU   F 2  198 ? 22.284  59.947  36.697  1.00 33.23  ? 200 GLU   B CG    1 
ATOM   15520 C  CD    . GLU   F 2  198 ? 22.620  61.400  36.394  1.00 36.06  ? 200 GLU   B CD    1 
ATOM   15521 O  OE1   . GLU   F 2  198 ? 22.780  61.767  35.205  1.00 39.87  ? 200 GLU   B OE1   1 
ATOM   15522 O  OE2   . GLU   F 2  198 ? 22.718  62.186  37.352  1.00 37.37  ? 200 GLU   B OE2   1 
ATOM   15523 N  N     . THR   F 2  199 ? 20.785  56.263  34.147  1.00 22.96  ? 201 THR   B N     1 
ATOM   15524 C  CA    . THR   F 2  199 ? 20.029  55.724  33.021  1.00 28.15  ? 201 THR   B CA    1 
ATOM   15525 C  C     . THR   F 2  199 ? 18.541  55.716  33.358  1.00 27.36  ? 201 THR   B C     1 
ATOM   15526 O  O     . THR   F 2  199 ? 18.125  55.091  34.338  1.00 29.82  ? 201 THR   B O     1 
ATOM   15527 C  CB    . THR   F 2  199 ? 20.534  54.328  32.664  1.00 28.90  ? 201 THR   B CB    1 
ATOM   15528 O  OG1   . THR   F 2  199 ? 21.730  54.468  31.881  1.00 33.30  ? 201 THR   B OG1   1 
ATOM   15529 C  CG2   . THR   F 2  199 ? 19.484  53.543  31.890  1.00 22.75  ? 201 THR   B CG2   1 
ATOM   15530 N  N     . TYR   F 2  200 ? 17.746  56.443  32.580  1.00 25.30  ? 202 TYR   B N     1 
ATOM   15531 C  CA    . TYR   F 2  200 ? 16.297  56.358  32.705  1.00 23.94  ? 202 TYR   B CA    1 
ATOM   15532 C  C     . TYR   F 2  200 ? 15.826  55.122  31.956  1.00 26.05  ? 202 TYR   B C     1 
ATOM   15533 O  O     . TYR   F 2  200 ? 16.041  55.022  30.744  1.00 27.54  ? 202 TYR   B O     1 
ATOM   15534 C  CB    . TYR   F 2  200 ? 15.632  57.607  32.145  1.00 27.65  ? 202 TYR   B CB    1 
ATOM   15535 C  CG    . TYR   F 2  200 ? 15.974  58.889  32.882  1.00 30.97  ? 202 TYR   B CG    1 
ATOM   15536 C  CD1   . TYR   F 2  200 ? 15.493  59.124  34.166  1.00 32.09  ? 202 TYR   B CD1   1 
ATOM   15537 C  CD2   . TYR   F 2  200 ? 16.748  59.869  32.281  1.00 26.55  ? 202 TYR   B CD2   1 
ATOM   15538 C  CE1   . TYR   F 2  200 ? 15.791  60.295  34.846  1.00 29.91  ? 202 TYR   B CE1   1 
ATOM   15539 C  CE2   . TYR   F 2  200 ? 17.043  61.037  32.929  1.00 30.95  ? 202 TYR   B CE2   1 
ATOM   15540 C  CZ    . TYR   F 2  200 ? 16.566  61.258  34.222  1.00 38.54  ? 202 TYR   B CZ    1 
ATOM   15541 O  OH    . TYR   F 2  200 ? 16.884  62.438  34.883  1.00 27.91  ? 202 TYR   B OH    1 
ATOM   15542 N  N     . CYS   F 2  201 ? 15.218  54.164  32.667  1.00 26.26  ? 203 CYS   B N     1 
ATOM   15543 C  CA    . CYS   F 2  201 ? 14.698  52.957  32.017  1.00 22.37  ? 203 CYS   B CA    1 
ATOM   15544 C  C     . CYS   F 2  201 ? 13.316  53.242  31.448  1.00 27.57  ? 203 CYS   B C     1 
ATOM   15545 O  O     . CYS   F 2  201 ? 12.302  53.107  32.135  1.00 27.30  ? 203 CYS   B O     1 
ATOM   15546 C  CB    . CYS   F 2  201 ? 14.639  51.798  32.991  1.00 28.07  ? 203 CYS   B CB    1 
ATOM   15547 S  SG    . CYS   F 2  201 ? 16.193  51.487  33.769  1.00 49.27  ? 203 CYS   B SG    1 
ATOM   15548 N  N     . ILE   F 2  202 ? 13.273  53.634  30.175  1.00 23.85  ? 204 ILE   B N     1 
ATOM   15549 C  CA    . ILE   F 2  202 ? 12.010  53.717  29.440  1.00 32.04  ? 204 ILE   B CA    1 
ATOM   15550 C  C     . ILE   F 2  202 ? 11.674  52.327  28.906  1.00 21.29  ? 204 ILE   B C     1 
ATOM   15551 O  O     . ILE   F 2  202 ? 12.301  51.850  27.961  1.00 25.50  ? 204 ILE   B O     1 
ATOM   15552 C  CB    . ILE   F 2  202 ? 12.081  54.734  28.301  1.00 27.36  ? 204 ILE   B CB    1 
ATOM   15553 C  CG1   . ILE   F 2  202 ? 12.205  56.132  28.882  1.00 20.68  ? 204 ILE   B CG1   1 
ATOM   15554 C  CG2   . ILE   F 2  202 ? 10.878  54.585  27.408  1.00 21.88  ? 204 ILE   B CG2   1 
ATOM   15555 C  CD1   . ILE   F 2  202 ? 13.616  56.562  29.006  1.00 20.85  ? 204 ILE   B CD1   1 
ATOM   15556 N  N     . ASP   F 2  203 ? 10.698  51.675  29.525  1.00 21.37  ? 205 ASP   B N     1 
ATOM   15557 C  CA    . ASP   F 2  203 ? 10.349  50.291  29.227  1.00 23.07  ? 205 ASP   B CA    1 
ATOM   15558 C  C     . ASP   F 2  203 ? 9.207   50.259  28.214  1.00 25.77  ? 205 ASP   B C     1 
ATOM   15559 O  O     . ASP   F 2  203 ? 8.141   50.835  28.456  1.00 26.73  ? 205 ASP   B O     1 
ATOM   15560 C  CB    . ASP   F 2  203 ? 9.949   49.583  30.520  1.00 20.80  ? 205 ASP   B CB    1 
ATOM   15561 C  CG    . ASP   F 2  203 ? 9.779   48.098  30.356  1.00 25.02  ? 205 ASP   B CG    1 
ATOM   15562 O  OD1   . ASP   F 2  203 ? 10.006  47.567  29.250  1.00 25.62  ? 205 ASP   B OD1   1 
ATOM   15563 O  OD2   . ASP   F 2  203 ? 9.410   47.448  31.351  1.00 24.50  ? 205 ASP   B OD2   1 
ATOM   15564 N  N     . ASN   F 2  204 ? 9.424   49.592  27.078  1.00 22.53  ? 206 ASN   B N     1 
ATOM   15565 C  CA    . ASN   F 2  204 ? 8.338   49.456  26.109  1.00 26.11  ? 206 ASN   B CA    1 
ATOM   15566 C  C     . ASN   F 2  204 ? 7.204   48.559  26.607  1.00 26.22  ? 206 ASN   B C     1 
ATOM   15567 O  O     . ASN   F 2  204 ? 6.087   48.649  26.084  1.00 21.19  ? 206 ASN   B O     1 
ATOM   15568 C  CB    . ASN   F 2  204 ? 8.872   48.937  24.780  1.00 23.14  ? 206 ASN   B CB    1 
ATOM   15569 C  CG    . ASN   F 2  204 ? 9.281   50.063  23.843  1.00 26.78  ? 206 ASN   B CG    1 
ATOM   15570 O  OD1   . ASN   F 2  204 ? 9.252   51.252  24.192  1.00 21.33  ? 206 ASN   B OD1   1 
ATOM   15571 N  ND2   . ASN   F 2  204 ? 9.679   49.687  22.653  1.00 18.04  ? 206 ASN   B ND2   1 
ATOM   15572 N  N     . GLU   F 2  205 ? 7.451   47.716  27.609  1.00 17.58  ? 207 GLU   B N     1 
ATOM   15573 C  CA    . GLU   F 2  205 ? 6.345   46.999  28.226  1.00 23.86  ? 207 GLU   B CA    1 
ATOM   15574 C  C     . GLU   F 2  205 ? 5.403   47.961  28.926  1.00 40.60  ? 207 GLU   B C     1 
ATOM   15575 O  O     . GLU   F 2  205 ? 4.172   47.863  28.783  1.00 37.33  ? 207 GLU   B O     1 
ATOM   15576 C  CB    . GLU   F 2  205 ? 6.848   45.967  29.229  1.00 30.18  ? 207 GLU   B CB    1 
ATOM   15577 C  CG    . GLU   F 2  205 ? 5.740   45.064  29.723  1.00 34.20  ? 207 GLU   B CG    1 
ATOM   15578 C  CD    . GLU   F 2  205 ? 5.977   43.607  29.383  1.00 36.90  ? 207 GLU   B CD    1 
ATOM   15579 O  OE1   . GLU   F 2  205 ? 6.772   43.306  28.457  1.00 31.76  ? 207 GLU   B OE1   1 
ATOM   15580 O  OE2   . GLU   F 2  205 ? 5.380   42.761  30.073  1.00 35.45  ? 207 GLU   B OE2   1 
ATOM   15581 N  N     . ALA   F 2  206 ? 5.967   48.894  29.708  1.00 30.72  ? 208 ALA   B N     1 
ATOM   15582 C  CA    . ALA   F 2  206 ? 5.118   49.825  30.439  1.00 32.30  ? 208 ALA   B CA    1 
ATOM   15583 C  C     . ALA   F 2  206 ? 4.469   50.835  29.489  1.00 28.72  ? 208 ALA   B C     1 
ATOM   15584 O  O     . ALA   F 2  206 ? 3.276   51.127  29.616  1.00 34.46  ? 208 ALA   B O     1 
ATOM   15585 C  CB    . ALA   F 2  206 ? 5.919   50.510  31.557  1.00 23.93  ? 208 ALA   B CB    1 
ATOM   15586 N  N     . LEU   F 2  207 ? 5.215   51.354  28.509  1.00 30.69  ? 209 LEU   B N     1 
ATOM   15587 C  CA    . LEU   F 2  207 ? 4.594   52.265  27.549  1.00 28.64  ? 209 LEU   B CA    1 
ATOM   15588 C  C     . LEU   F 2  207 ? 3.445   51.585  26.806  1.00 33.09  ? 209 LEU   B C     1 
ATOM   15589 O  O     . LEU   F 2  207 ? 2.418   52.214  26.542  1.00 34.80  ? 209 LEU   B O     1 
ATOM   15590 C  CB    . LEU   F 2  207 ? 5.627   52.809  26.565  1.00 21.20  ? 209 LEU   B CB    1 
ATOM   15591 C  CG    . LEU   F 2  207 ? 6.857   53.505  27.149  1.00 26.34  ? 209 LEU   B CG    1 
ATOM   15592 C  CD1   . LEU   F 2  207 ? 7.815   53.886  26.033  1.00 22.31  ? 209 LEU   B CD1   1 
ATOM   15593 C  CD2   . LEU   F 2  207 ? 6.470   54.742  27.927  1.00 22.63  ? 209 LEU   B CD2   1 
ATOM   15594 N  N     . TYR   F 2  208 ? 3.583   50.290  26.486  1.00 33.75  ? 210 TYR   B N     1 
ATOM   15595 C  CA    . TYR   F 2  208 ? 2.504   49.591  25.792  1.00 29.99  ? 210 TYR   B CA    1 
ATOM   15596 C  C     . TYR   F 2  208 ? 1.261   49.480  26.673  1.00 36.96  ? 210 TYR   B C     1 
ATOM   15597 O  O     . TYR   F 2  208 ? 0.149   49.786  26.226  1.00 35.43  ? 210 TYR   B O     1 
ATOM   15598 C  CB    . TYR   F 2  208 ? 2.951   48.197  25.317  1.00 27.47  ? 210 TYR   B CB    1 
ATOM   15599 C  CG    . TYR   F 2  208 ? 1.775   47.354  24.843  1.00 29.80  ? 210 TYR   B CG    1 
ATOM   15600 C  CD1   . TYR   F 2  208 ? 1.318   47.416  23.524  1.00 26.68  ? 210 TYR   B CD1   1 
ATOM   15601 C  CD2   . TYR   F 2  208 ? 1.092   46.528  25.731  1.00 34.00  ? 210 TYR   B CD2   1 
ATOM   15602 C  CE1   . TYR   F 2  208 ? 0.217   46.656  23.107  1.00 27.51  ? 210 TYR   B CE1   1 
ATOM   15603 C  CE2   . TYR   F 2  208 ? 0.005   45.765  25.325  1.00 30.28  ? 210 TYR   B CE2   1 
ATOM   15604 C  CZ    . TYR   F 2  208 ? -0.443  45.835  24.021  1.00 32.44  ? 210 TYR   B CZ    1 
ATOM   15605 O  OH    . TYR   F 2  208 ? -1.545  45.070  23.661  1.00 29.18  ? 210 TYR   B OH    1 
ATOM   15606 N  N     . ASP   F 2  209 ? 1.422   49.041  27.929  1.00 33.05  ? 211 ASP   B N     1 
ATOM   15607 C  CA    . ASP   F 2  209 ? 0.260   48.892  28.798  1.00 26.26  ? 211 ASP   B CA    1 
ATOM   15608 C  C     . ASP   F 2  209 ? -0.451  50.225  28.983  1.00 35.68  ? 211 ASP   B C     1 
ATOM   15609 O  O     . ASP   F 2  209 ? -1.671  50.324  28.796  1.00 33.69  ? 211 ASP   B O     1 
ATOM   15610 C  CB    . ASP   F 2  209 ? 0.666   48.280  30.145  1.00 28.62  ? 211 ASP   B CB    1 
ATOM   15611 C  CG    . ASP   F 2  209 ? 1.118   46.797  30.017  1.00 49.65  ? 211 ASP   B CG    1 
ATOM   15612 O  OD1   . ASP   F 2  209 ? 0.405   45.960  29.400  1.00 54.33  ? 211 ASP   B OD1   1 
ATOM   15613 O  OD2   . ASP   F 2  209 ? 2.213   46.461  30.517  1.00 49.62  ? 211 ASP   B OD2   1 
ATOM   15614 N  N     . ILE   F 2  210 ? 0.300   51.274  29.333  1.00 33.86  ? 212 ILE   B N     1 
ATOM   15615 C  CA    . ILE   F 2  210 ? -0.307  52.593  29.515  1.00 29.72  ? 212 ILE   B CA    1 
ATOM   15616 C  C     . ILE   F 2  210 ? -1.158  52.950  28.298  1.00 39.92  ? 212 ILE   B C     1 
ATOM   15617 O  O     . ILE   F 2  210 ? -2.314  53.374  28.424  1.00 46.93  ? 212 ILE   B O     1 
ATOM   15618 C  CB    . ILE   F 2  210 ? 0.781   53.649  29.793  1.00 23.50  ? 212 ILE   B CB    1 
ATOM   15619 C  CG1   . ILE   F 2  210 ? 1.436   53.396  31.154  1.00 29.32  ? 212 ILE   B CG1   1 
ATOM   15620 C  CG2   . ILE   F 2  210 ? 0.205   55.031  29.789  1.00 25.14  ? 212 ILE   B CG2   1 
ATOM   15621 C  CD1   . ILE   F 2  210 ? 2.714   54.173  31.390  1.00 24.04  ? 212 ILE   B CD1   1 
ATOM   15622 N  N     . CYS   F 2  211 ? -0.614  52.736  27.099  1.00 31.08  ? 213 CYS   B N     1 
ATOM   15623 C  CA    . CYS   F 2  211 ? -1.329  53.089  25.873  1.00 34.04  ? 213 CYS   B CA    1 
ATOM   15624 C  C     . CYS   F 2  211 ? -2.554  52.199  25.633  1.00 44.74  ? 213 CYS   B C     1 
ATOM   15625 O  O     . CYS   F 2  211 ? -3.585  52.674  25.140  1.00 45.73  ? 213 CYS   B O     1 
ATOM   15626 C  CB    . CYS   F 2  211 ? -0.373  53.005  24.685  1.00 24.56  ? 213 CYS   B CB    1 
ATOM   15627 S  SG    . CYS   F 2  211 ? 0.731   54.398  24.610  1.00 31.28  ? 213 CYS   B SG    1 
ATOM   15628 N  N     . PHE   F 2  212 ? -2.461  50.907  25.950  1.00 43.88  ? 214 PHE   B N     1 
ATOM   15629 C  CA    . PHE   F 2  212 ? -3.495  49.943  25.560  1.00 36.40  ? 214 PHE   B CA    1 
ATOM   15630 C  C     . PHE   F 2  212 ? -4.607  49.894  26.605  1.00 38.27  ? 214 PHE   B C     1 
ATOM   15631 O  O     . PHE   F 2  212 ? -5.747  50.263  26.320  1.00 42.78  ? 214 PHE   B O     1 
ATOM   15632 C  CB    . PHE   F 2  212 ? -2.849  48.578  25.344  1.00 28.34  ? 214 PHE   B CB    1 
ATOM   15633 C  CG    . PHE   F 2  212 ? -3.750  47.580  24.708  1.00 33.79  ? 214 PHE   B CG    1 
ATOM   15634 C  CD1   . PHE   F 2  212 ? -4.259  47.804  23.441  1.00 33.76  ? 214 PHE   B CD1   1 
ATOM   15635 C  CD2   . PHE   F 2  212 ? -4.061  46.394  25.360  1.00 34.97  ? 214 PHE   B CD2   1 
ATOM   15636 C  CE1   . PHE   F 2  212 ? -5.084  46.875  22.838  1.00 35.38  ? 214 PHE   B CE1   1 
ATOM   15637 C  CE2   . PHE   F 2  212 ? -4.885  45.455  24.768  1.00 33.98  ? 214 PHE   B CE2   1 
ATOM   15638 C  CZ    . PHE   F 2  212 ? -5.403  45.699  23.507  1.00 38.74  ? 214 PHE   B CZ    1 
ATOM   15639 N  N     . ARG   F 2  213 ? -4.287  49.404  27.803  1.00 33.79  ? 215 ARG   B N     1 
ATOM   15640 C  CA    . ARG   F 2  213 ? -5.100  49.540  29.006  1.00 38.30  ? 215 ARG   B CA    1 
ATOM   15641 C  C     . ARG   F 2  213 ? -5.533  50.977  29.269  1.00 44.47  ? 215 ARG   B C     1 
ATOM   15642 O  O     . ARG   F 2  213 ? -6.617  51.412  28.880  1.00 46.38  ? 215 ARG   B O     1 
ATOM   15643 C  CB    . ARG   F 2  213 ? -4.314  49.087  30.238  1.00 47.02  ? 215 ARG   B CB    1 
ATOM   15644 C  CG    . ARG   F 2  213 ? -4.402  47.649  30.615  1.00 58.97  ? 215 ARG   B CG    1 
ATOM   15645 C  CD    . ARG   F 2  213 ? -4.052  47.487  32.096  1.00 60.53  ? 215 ARG   B CD    1 
ATOM   15646 N  NE    . ARG   F 2  213 ? -3.257  46.284  32.312  1.00 83.21  ? 215 ARG   B NE    1 
ATOM   15647 C  CZ    . ARG   F 2  213 ? -3.730  45.049  32.202  1.00 99.40  ? 215 ARG   B CZ    1 
ATOM   15648 N  NH1   . ARG   F 2  213 ? -5.000  44.818  31.905  1.00 93.05  ? 215 ARG   B NH1   1 
ATOM   15649 N  NH2   . ARG   F 2  213 ? -2.906  44.020  32.381  1.00 106.79 ? 215 ARG   B NH2   1 
ATOM   15650 N  N     . THR   F 2  214 ? -4.663  51.719  29.943  1.00 42.00  ? 216 THR   B N     1 
ATOM   15651 C  CA    . THR   F 2  214 ? -5.062  52.982  30.540  1.00 35.63  ? 216 THR   B CA    1 
ATOM   15652 C  C     . THR   F 2  214 ? -5.635  53.946  29.508  1.00 38.05  ? 216 THR   B C     1 
ATOM   15653 O  O     . THR   F 2  214 ? -6.712  54.514  29.714  1.00 41.49  ? 216 THR   B O     1 
ATOM   15654 C  CB    . THR   F 2  214 ? -3.868  53.591  31.263  1.00 31.90  ? 216 THR   B CB    1 
ATOM   15655 O  OG1   . THR   F 2  214 ? -3.548  52.772  32.392  1.00 43.05  ? 216 THR   B OG1   1 
ATOM   15656 C  CG2   . THR   F 2  214 ? -4.184  54.980  31.728  1.00 27.73  ? 216 THR   B CG2   1 
ATOM   15657 N  N     . LEU   F 2  215 ? -4.931  54.155  28.397  1.00 38.83  ? 217 LEU   B N     1 
ATOM   15658 C  CA    . LEU   F 2  215 ? -5.363  55.122  27.392  1.00 34.52  ? 217 LEU   B CA    1 
ATOM   15659 C  C     . LEU   F 2  215 ? -6.323  54.537  26.358  1.00 30.34  ? 217 LEU   B C     1 
ATOM   15660 O  O     . LEU   F 2  215 ? -6.708  55.238  25.425  1.00 29.69  ? 217 LEU   B O     1 
ATOM   15661 C  CB    . LEU   F 2  215 ? -4.150  55.737  26.675  1.00 29.85  ? 217 LEU   B CB    1 
ATOM   15662 C  CG    . LEU   F 2  215 ? -3.265  56.664  27.503  1.00 35.98  ? 217 LEU   B CG    1 
ATOM   15663 C  CD1   . LEU   F 2  215 ? -2.298  57.520  26.640  1.00 26.23  ? 217 LEU   B CD1   1 
ATOM   15664 C  CD2   . LEU   F 2  215 ? -4.149  57.538  28.389  1.00 33.18  ? 217 LEU   B CD2   1 
ATOM   15665 N  N     . LYS   F 2  216 ? -6.713  53.277  26.474  1.00 36.70  ? 218 LYS   B N     1 
ATOM   15666 C  CA    . LYS   F 2  216 ? -7.752  52.737  25.602  1.00 43.33  ? 218 LYS   B CA    1 
ATOM   15667 C  C     . LYS   F 2  216 ? -7.378  52.782  24.117  1.00 43.51  ? 218 LYS   B C     1 
ATOM   15668 O  O     . LYS   F 2  216 ? -8.273  52.811  23.267  1.00 39.30  ? 218 LYS   B O     1 
ATOM   15669 C  CB    . LYS   F 2  216 ? -9.071  53.486  25.819  1.00 35.45  ? 218 LYS   B CB    1 
ATOM   15670 C  CG    . LYS   F 2  216 ? -10.049 52.817  26.759  1.00 35.75  ? 218 LYS   B CG    1 
ATOM   15671 C  CD    . LYS   F 2  216 ? -9.390  52.298  28.037  1.00 45.47  ? 218 LYS   B CD    1 
ATOM   15672 C  CE    . LYS   F 2  216 ? -9.310  50.763  28.052  1.00 44.93  ? 218 LYS   B CE    1 
ATOM   15673 N  NZ    . LYS   F 2  216 ? -9.067  50.215  29.429  1.00 52.78  ? 218 LYS   B NZ    1 
ATOM   15674 N  N     . LEU   F 2  217 ? -6.076  52.803  23.788  1.00 42.35  ? 219 LEU   B N     1 
ATOM   15675 C  CA    . LEU   F 2  217 ? -5.577  52.898  22.408  1.00 29.95  ? 219 LEU   B CA    1 
ATOM   15676 C  C     . LEU   F 2  217 ? -5.280  51.489  21.908  1.00 41.56  ? 219 LEU   B C     1 
ATOM   15677 O  O     . LEU   F 2  217 ? -4.198  50.947  22.162  1.00 39.23  ? 219 LEU   B O     1 
ATOM   15678 C  CB    . LEU   F 2  217 ? -4.311  53.742  22.328  1.00 29.62  ? 219 LEU   B CB    1 
ATOM   15679 C  CG    . LEU   F 2  217 ? -4.323  55.244  22.561  1.00 40.14  ? 219 LEU   B CG    1 
ATOM   15680 C  CD1   . LEU   F 2  217 ? -2.896  55.776  22.604  1.00 31.01  ? 219 LEU   B CD1   1 
ATOM   15681 C  CD2   . LEU   F 2  217 ? -5.104  55.930  21.469  1.00 31.51  ? 219 LEU   B CD2   1 
ATOM   15682 N  N     . THR   F 2  218 ? -6.218  50.922  21.146  1.00 43.90  ? 220 THR   B N     1 
ATOM   15683 C  CA    . THR   F 2  218 ? -6.240  49.487  20.865  1.00 31.43  ? 220 THR   B CA    1 
ATOM   15684 C  C     . THR   F 2  218 ? -5.360  49.088  19.690  1.00 31.89  ? 220 THR   B C     1 
ATOM   15685 O  O     . THR   F 2  218 ? -5.136  47.887  19.497  1.00 37.18  ? 220 THR   B O     1 
ATOM   15686 C  CB    . THR   F 2  218 ? -7.691  49.025  20.615  1.00 35.71  ? 220 THR   B CB    1 
ATOM   15687 O  OG1   . THR   F 2  218 ? -8.382  49.975  19.779  1.00 23.71  ? 220 THR   B OG1   1 
ATOM   15688 C  CG2   . THR   F 2  218 ? -8.445  48.854  21.936  1.00 25.37  ? 220 THR   B CG2   1 
ATOM   15689 N  N     . THR   F 2  219 ? -4.887  50.047  18.892  1.00 27.71  ? 221 THR   B N     1 
ATOM   15690 C  CA    . THR   F 2  219 ? -3.878  49.802  17.859  1.00 29.64  ? 221 THR   B CA    1 
ATOM   15691 C  C     . THR   F 2  219 ? -2.759  50.815  18.072  1.00 33.24  ? 221 THR   B C     1 
ATOM   15692 O  O     . THR   F 2  219 ? -2.584  51.756  17.290  1.00 34.91  ? 221 THR   B O     1 
ATOM   15693 C  CB    . THR   F 2  219 ? -4.459  49.881  16.439  1.00 32.49  ? 221 THR   B CB    1 
ATOM   15694 O  OG1   . THR   F 2  219 ? -5.277  51.048  16.281  1.00 26.59  ? 221 THR   B OG1   1 
ATOM   15695 C  CG2   . THR   F 2  219 ? -5.300  48.666  16.123  1.00 32.15  ? 221 THR   B CG2   1 
ATOM   15696 N  N     . PRO   F 2  220 ? -1.982  50.652  19.140  1.00 33.33  ? 222 PRO   B N     1 
ATOM   15697 C  CA    . PRO   F 2  220 ? -0.943  51.641  19.457  1.00 33.42  ? 222 PRO   B CA    1 
ATOM   15698 C  C     . PRO   F 2  220 ? 0.149   51.734  18.397  1.00 38.47  ? 222 PRO   B C     1 
ATOM   15699 O  O     . PRO   F 2  220 ? 0.572   50.734  17.810  1.00 36.21  ? 222 PRO   B O     1 
ATOM   15700 C  CB    . PRO   F 2  220 ? -0.385  51.140  20.791  1.00 39.04  ? 222 PRO   B CB    1 
ATOM   15701 C  CG    . PRO   F 2  220 ? -0.873  49.721  20.932  1.00 28.44  ? 222 PRO   B CG    1 
ATOM   15702 C  CD    . PRO   F 2  220 ? -2.152  49.657  20.212  1.00 28.30  ? 222 PRO   B CD    1 
ATOM   15703 N  N     . THR   F 2  221 ? 0.613   52.958  18.159  1.00 38.71  ? 223 THR   B N     1 
ATOM   15704 C  CA    . THR   F 2  221 ? 1.742   53.200  17.272  1.00 34.71  ? 223 THR   B CA    1 
ATOM   15705 C  C     . THR   F 2  221 ? 2.938   53.684  18.073  1.00 35.04  ? 223 THR   B C     1 
ATOM   15706 O  O     . THR   F 2  221 ? 2.833   54.040  19.246  1.00 37.78  ? 223 THR   B O     1 
ATOM   15707 C  CB    . THR   F 2  221 ? 1.402   54.237  16.207  1.00 38.74  ? 223 THR   B CB    1 
ATOM   15708 O  OG1   . THR   F 2  221 ? 1.462   55.542  16.801  1.00 35.77  ? 223 THR   B OG1   1 
ATOM   15709 C  CG2   . THR   F 2  221 ? 0.018   53.951  15.609  1.00 24.88  ? 223 THR   B CG2   1 
ATOM   15710 N  N     . TYR   F 2  222 ? 4.099   53.702  17.425  1.00 38.93  ? 224 TYR   B N     1 
ATOM   15711 C  CA    . TYR   F 2  222 ? 5.266   54.236  18.120  1.00 36.89  ? 224 TYR   B CA    1 
ATOM   15712 C  C     . TYR   F 2  222 ? 5.067   55.710  18.469  1.00 30.20  ? 224 TYR   B C     1 
ATOM   15713 O  O     . TYR   F 2  222 ? 5.536   56.166  19.515  1.00 26.63  ? 224 TYR   B O     1 
ATOM   15714 C  CB    . TYR   F 2  222 ? 6.543   53.997  17.282  1.00 27.49  ? 224 TYR   B CB    1 
ATOM   15715 C  CG    . TYR   F 2  222 ? 7.155   52.631  17.532  1.00 20.42  ? 224 TYR   B CG    1 
ATOM   15716 C  CD1   . TYR   F 2  222 ? 7.335   52.142  18.845  1.00 22.40  ? 224 TYR   B CD1   1 
ATOM   15717 C  CD2   . TYR   F 2  222 ? 7.493   51.802  16.480  1.00 19.91  ? 224 TYR   B CD2   1 
ATOM   15718 C  CE1   . TYR   F 2  222 ? 7.872   50.857  19.088  1.00 17.33  ? 224 TYR   B CE1   1 
ATOM   15719 C  CE2   . TYR   F 2  222 ? 8.029   50.523  16.704  1.00 23.01  ? 224 TYR   B CE2   1 
ATOM   15720 C  CZ    . TYR   F 2  222 ? 8.210   50.058  17.988  1.00 25.91  ? 224 TYR   B CZ    1 
ATOM   15721 O  OH    . TYR   F 2  222 ? 8.738   48.804  18.151  1.00 32.67  ? 224 TYR   B OH    1 
ATOM   15722 N  N     . GLY   F 2  223 ? 4.347   56.460  17.628  1.00 35.49  ? 225 GLY   B N     1 
ATOM   15723 C  CA    . GLY   F 2  223 ? 4.067   57.849  17.949  1.00 29.16  ? 225 GLY   B CA    1 
ATOM   15724 C  C     . GLY   F 2  223 ? 3.296   57.997  19.243  1.00 37.20  ? 225 GLY   B C     1 
ATOM   15725 O  O     . GLY   F 2  223 ? 3.491   58.969  19.974  1.00 37.09  ? 225 GLY   B O     1 
ATOM   15726 N  N     . ASP   F 2  224 ? 2.411   57.039  19.541  1.00 33.52  ? 226 ASP   B N     1 
ATOM   15727 C  CA    . ASP   F 2  224 ? 1.720   57.020  20.823  1.00 31.31  ? 226 ASP   B CA    1 
ATOM   15728 C  C     . ASP   F 2  224 ? 2.704   56.799  21.955  1.00 34.61  ? 226 ASP   B C     1 
ATOM   15729 O  O     . ASP   F 2  224 ? 2.726   57.549  22.938  1.00 32.85  ? 226 ASP   B O     1 
ATOM   15730 C  CB    . ASP   F 2  224 ? 0.653   55.917  20.839  1.00 37.51  ? 226 ASP   B CB    1 
ATOM   15731 C  CG    . ASP   F 2  224 ? -0.462  56.176  19.860  1.00 49.65  ? 226 ASP   B CG    1 
ATOM   15732 O  OD1   . ASP   F 2  224 ? -0.783  57.370  19.679  1.00 49.84  ? 226 ASP   B OD1   1 
ATOM   15733 O  OD2   . ASP   F 2  224 ? -1.002  55.203  19.267  1.00 43.18  ? 226 ASP   B OD2   1 
ATOM   15734 N  N     . LEU   F 2  225 ? 3.490   55.729  21.855  1.00 37.18  ? 227 LEU   B N     1 
ATOM   15735 C  CA    . LEU   F 2  225 ? 4.533   55.463  22.836  1.00 34.25  ? 227 LEU   B CA    1 
ATOM   15736 C  C     . LEU   F 2  225 ? 5.421   56.687  23.026  1.00 32.55  ? 227 LEU   B C     1 
ATOM   15737 O  O     . LEU   F 2  225 ? 5.669   57.124  24.156  1.00 29.39  ? 227 LEU   B O     1 
ATOM   15738 C  CB    . LEU   F 2  225 ? 5.355   54.262  22.380  1.00 24.37  ? 227 LEU   B CB    1 
ATOM   15739 C  CG    . LEU   F 2  225 ? 4.833   52.906  22.820  1.00 32.02  ? 227 LEU   B CG    1 
ATOM   15740 C  CD1   . LEU   F 2  225 ? 3.328   52.755  22.602  1.00 25.37  ? 227 LEU   B CD1   1 
ATOM   15741 C  CD2   . LEU   F 2  225 ? 5.631   51.844  22.092  1.00 22.05  ? 227 LEU   B CD2   1 
ATOM   15742 N  N     . ASN   F 2  226 ? 5.879   57.272  21.916  1.00 29.94  ? 228 ASN   B N     1 
ATOM   15743 C  CA    . ASN   F 2  226 ? 6.819   58.378  21.981  1.00 25.35  ? 228 ASN   B CA    1 
ATOM   15744 C  C     . ASN   F 2  226 ? 6.166   59.623  22.526  1.00 29.35  ? 228 ASN   B C     1 
ATOM   15745 O  O     . ASN   F 2  226 ? 6.874   60.569  22.885  1.00 41.06  ? 228 ASN   B O     1 
ATOM   15746 C  CB    . ASN   F 2  226 ? 7.421   58.684  20.599  1.00 27.76  ? 228 ASN   B CB    1 
ATOM   15747 C  CG    . ASN   F 2  226 ? 8.292   57.551  20.049  1.00 25.77  ? 228 ASN   B CG    1 
ATOM   15748 O  OD1   . ASN   F 2  226 ? 8.595   56.570  20.730  1.00 31.04  ? 228 ASN   B OD1   1 
ATOM   15749 N  ND2   . ASN   F 2  226 ? 8.717   57.706  18.819  1.00 22.36  ? 228 ASN   B ND2   1 
ATOM   15750 N  N     . HIS   F 2  227 ? 4.836   59.668  22.559  1.00 29.46  ? 229 HIS   B N     1 
ATOM   15751 C  CA    . HIS   F 2  227 ? 4.163   60.786  23.208  1.00 26.35  ? 229 HIS   B CA    1 
ATOM   15752 C  C     . HIS   F 2  227 ? 4.405   60.739  24.710  1.00 32.95  ? 229 HIS   B C     1 
ATOM   15753 O  O     . HIS   F 2  227 ? 4.803   61.738  25.324  1.00 28.57  ? 229 HIS   B O     1 
ATOM   15754 C  CB    . HIS   F 2  227 ? 2.668   60.753  22.890  1.00 28.82  ? 229 HIS   B CB    1 
ATOM   15755 C  CG    . HIS   F 2  227 ? 1.893   61.879  23.496  1.00 31.27  ? 229 HIS   B CG    1 
ATOM   15756 N  ND1   . HIS   F 2  227 ? 1.051   61.708  24.577  1.00 29.75  ? 229 HIS   B ND1   1 
ATOM   15757 C  CD2   . HIS   F 2  227 ? 1.833   63.193  23.174  1.00 31.21  ? 229 HIS   B CD2   1 
ATOM   15758 C  CE1   . HIS   F 2  227 ? 0.504   62.871  24.890  1.00 29.42  ? 229 HIS   B CE1   1 
ATOM   15759 N  NE2   . HIS   F 2  227 ? 0.962   63.786  24.055  1.00 33.23  ? 229 HIS   B NE2   1 
ATOM   15760 N  N     . LEU   F 2  228 ? 4.204   59.563  25.312  1.00 28.44  ? 230 LEU   B N     1 
ATOM   15761 C  CA    . LEU   F 2  228 ? 4.557   59.373  26.708  1.00 22.08  ? 230 LEU   B CA    1 
ATOM   15762 C  C     . LEU   F 2  228 ? 6.058   59.579  26.939  1.00 31.53  ? 230 LEU   B C     1 
ATOM   15763 O  O     . LEU   F 2  228 ? 6.469   60.111  27.983  1.00 26.73  ? 230 LEU   B O     1 
ATOM   15764 C  CB    . LEU   F 2  228 ? 4.111   57.978  27.156  1.00 26.32  ? 230 LEU   B CB    1 
ATOM   15765 C  CG    . LEU   F 2  228 ? 2.617   57.647  26.974  1.00 24.22  ? 230 LEU   B CG    1 
ATOM   15766 C  CD1   . LEU   F 2  228 ? 2.298   56.175  27.259  1.00 16.78  ? 230 LEU   B CD1   1 
ATOM   15767 C  CD2   . LEU   F 2  228 ? 1.704   58.556  27.803  1.00 26.34  ? 230 LEU   B CD2   1 
ATOM   15768 N  N     . VAL   F 2  229 ? 6.893   59.181  25.969  1.00 25.83  ? 231 VAL   B N     1 
ATOM   15769 C  CA    . VAL   F 2  229 ? 8.331   59.238  26.192  1.00 22.25  ? 231 VAL   B CA    1 
ATOM   15770 C  C     . VAL   F 2  229 ? 8.843   60.675  26.174  1.00 32.82  ? 231 VAL   B C     1 
ATOM   15771 O  O     . VAL   F 2  229 ? 9.812   60.994  26.872  1.00 32.16  ? 231 VAL   B O     1 
ATOM   15772 C  CB    . VAL   F 2  229 ? 9.080   58.363  25.178  1.00 25.13  ? 231 VAL   B CB    1 
ATOM   15773 C  CG1   . VAL   F 2  229 ? 10.541  58.730  25.178  1.00 26.41  ? 231 VAL   B CG1   1 
ATOM   15774 C  CG2   . VAL   F 2  229 ? 8.922   56.905  25.549  1.00 27.00  ? 231 VAL   B CG2   1 
ATOM   15775 N  N     . SER   F 2  230 ? 8.215   61.570  25.406  1.00 26.37  ? 232 SER   B N     1 
ATOM   15776 C  CA    . SER   F 2  230 ? 8.696   62.943  25.388  1.00 22.69  ? 232 SER   B CA    1 
ATOM   15777 C  C     . SER   F 2  230 ? 8.113   63.787  26.511  1.00 28.48  ? 232 SER   B C     1 
ATOM   15778 O  O     . SER   F 2  230 ? 8.768   64.738  26.950  1.00 27.82  ? 232 SER   B O     1 
ATOM   15779 C  CB    . SER   F 2  230 ? 8.406   63.606  24.036  1.00 35.59  ? 232 SER   B CB    1 
ATOM   15780 O  OG    . SER   F 2  230 ? 7.021   63.813  23.859  1.00 41.57  ? 232 SER   B OG    1 
ATOM   15781 N  N     . ALA   F 2  231 ? 6.907   63.469  26.993  1.00 24.84  ? 233 ALA   B N     1 
ATOM   15782 C  CA    . ALA   F 2  231 ? 6.439   64.083  28.233  1.00 24.91  ? 233 ALA   B CA    1 
ATOM   15783 C  C     . ALA   F 2  231 ? 7.400   63.782  29.382  1.00 29.85  ? 233 ALA   B C     1 
ATOM   15784 O  O     . ALA   F 2  231 ? 7.775   64.679  30.151  1.00 28.57  ? 233 ALA   B O     1 
ATOM   15785 C  CB    . ALA   F 2  231 ? 5.023   63.605  28.574  1.00 22.77  ? 233 ALA   B CB    1 
ATOM   15786 N  N     . THR   F 2  232 ? 7.845   62.529  29.485  1.00 25.64  ? 234 THR   B N     1 
ATOM   15787 C  CA    . THR   F 2  232 ? 8.774   62.153  30.544  1.00 23.08  ? 234 THR   B CA    1 
ATOM   15788 C  C     . THR   F 2  232 ? 10.110  62.879  30.406  1.00 32.48  ? 234 THR   B C     1 
ATOM   15789 O  O     . THR   F 2  232 ? 10.635  63.436  31.382  1.00 29.46  ? 234 THR   B O     1 
ATOM   15790 C  CB    . THR   F 2  232 ? 8.977   60.653  30.517  1.00 20.04  ? 234 THR   B CB    1 
ATOM   15791 O  OG1   . THR   F 2  232 ? 7.736   60.016  30.855  1.00 27.49  ? 234 THR   B OG1   1 
ATOM   15792 C  CG2   . THR   F 2  232 ? 10.075  60.246  31.481  1.00 20.57  ? 234 THR   B CG2   1 
ATOM   15793 N  N     . MET   F 2  233 ? 10.679  62.873  29.196  1.00 28.10  ? 235 MET   B N     1 
ATOM   15794 C  CA    . MET   F 2  233 ? 11.990  63.471  28.988  1.00 24.37  ? 235 MET   B CA    1 
ATOM   15795 C  C     . MET   F 2  233 ? 11.951  64.956  29.293  1.00 33.21  ? 235 MET   B C     1 
ATOM   15796 O  O     . MET   F 2  233 ? 12.831  65.496  29.982  1.00 23.85  ? 235 MET   B O     1 
ATOM   15797 C  CB    . MET   F 2  233 ? 12.451  63.228  27.560  1.00 24.84  ? 235 MET   B CB    1 
ATOM   15798 C  CG    . MET   F 2  233 ? 12.837  61.788  27.287  1.00 30.20  ? 235 MET   B CG    1 
ATOM   15799 S  SD    . MET   F 2  233 ? 13.476  61.658  25.620  1.00 39.00  ? 235 MET   B SD    1 
ATOM   15800 C  CE    . MET   F 2  233 ? 15.033  62.547  25.831  1.00 30.39  ? 235 MET   B CE    1 
ATOM   15801 N  N     . SER   F 2  234 ? 10.924  65.635  28.788  1.00 32.91  ? 236 SER   B N     1 
ATOM   15802 C  CA    . SER   F 2  234 ? 10.694  67.006  29.209  1.00 33.74  ? 236 SER   B CA    1 
ATOM   15803 C  C     . SER   F 2  234 ? 10.653  67.106  30.733  1.00 35.59  ? 236 SER   B C     1 
ATOM   15804 O  O     . SER   F 2  234 ? 11.390  67.892  31.341  1.00 29.07  ? 236 SER   B O     1 
ATOM   15805 C  CB    . SER   F 2  234 ? 9.401   67.512  28.605  1.00 25.31  ? 236 SER   B CB    1 
ATOM   15806 O  OG    . SER   F 2  234 ? 9.052   68.715  29.228  1.00 33.77  ? 236 SER   B OG    1 
ATOM   15807 N  N     . GLY   F 2  235 ? 9.809   66.298  31.369  1.00 26.57  ? 237 GLY   B N     1 
ATOM   15808 C  CA    . GLY   F 2  235 ? 9.722   66.324  32.816  1.00 26.27  ? 237 GLY   B CA    1 
ATOM   15809 C  C     . GLY   F 2  235 ? 11.041  66.186  33.557  1.00 28.10  ? 237 GLY   B C     1 
ATOM   15810 O  O     . GLY   F 2  235 ? 11.401  67.041  34.367  1.00 30.76  ? 237 GLY   B O     1 
ATOM   15811 N  N     . VAL   F 2  236 ? 11.779  65.118  33.288  1.00 29.78  ? 238 VAL   B N     1 
ATOM   15812 C  CA    . VAL   F 2  236 ? 12.965  64.807  34.079  1.00 31.00  ? 238 VAL   B CA    1 
ATOM   15813 C  C     . VAL   F 2  236 ? 14.121  65.759  33.765  1.00 28.44  ? 238 VAL   B C     1 
ATOM   15814 O  O     . VAL   F 2  236 ? 15.189  65.669  34.378  1.00 33.76  ? 238 VAL   B O     1 
ATOM   15815 C  CB    . VAL   F 2  236 ? 13.372  63.331  33.881  1.00 31.98  ? 238 VAL   B CB    1 
ATOM   15816 C  CG1   . VAL   F 2  236 ? 12.137  62.430  34.017  1.00 26.09  ? 238 VAL   B CG1   1 
ATOM   15817 C  CG2   . VAL   F 2  236 ? 14.059  63.108  32.527  1.00 21.48  ? 238 VAL   B CG2   1 
ATOM   15818 N  N     . THR   F 2  237 ? 13.929  66.686  32.829  1.00 26.49  ? 239 THR   B N     1 
ATOM   15819 C  CA    . THR   F 2  237 ? 14.961  67.668  32.522  1.00 21.51  ? 239 THR   B CA    1 
ATOM   15820 C  C     . THR   F 2  237 ? 14.546  69.083  32.877  1.00 32.10  ? 239 THR   B C     1 
ATOM   15821 O  O     . THR   F 2  237 ? 15.353  70.001  32.689  1.00 31.35  ? 239 THR   B O     1 
ATOM   15822 C  CB    . THR   F 2  237 ? 15.384  67.625  31.037  1.00 23.52  ? 239 THR   B CB    1 
ATOM   15823 O  OG1   . THR   F 2  237 ? 14.252  67.778  30.175  1.00 26.79  ? 239 THR   B OG1   1 
ATOM   15824 C  CG2   . THR   F 2  237 ? 16.089  66.326  30.705  1.00 26.99  ? 239 THR   B CG2   1 
ATOM   15825 N  N     . THR   F 2  238 ? 13.325  69.285  33.395  1.00 26.30  ? 240 THR   B N     1 
ATOM   15826 C  CA    . THR   F 2  238 ? 12.917  70.618  33.836  1.00 29.58  ? 240 THR   B CA    1 
ATOM   15827 C  C     . THR   F 2  238 ? 14.008  71.262  34.688  1.00 32.52  ? 240 THR   B C     1 
ATOM   15828 O  O     . THR   F 2  238 ? 14.539  72.321  34.346  1.00 29.85  ? 240 THR   B O     1 
ATOM   15829 C  CB    . THR   F 2  238 ? 11.600  70.554  34.620  1.00 29.68  ? 240 THR   B CB    1 
ATOM   15830 O  OG1   . THR   F 2  238 ? 10.571  69.959  33.824  1.00 41.19  ? 240 THR   B OG1   1 
ATOM   15831 C  CG2   . THR   F 2  238 ? 11.147  71.929  34.971  1.00 37.81  ? 240 THR   B CG2   1 
ATOM   15832 N  N     . CYS   F 2  239 ? 14.385  70.592  35.784  1.00 29.92  ? 241 CYS   B N     1 
ATOM   15833 C  CA    . CYS   F 2  239 ? 15.363  71.106  36.738  1.00 32.42  ? 241 CYS   B CA    1 
ATOM   15834 C  C     . CYS   F 2  239 ? 16.690  71.518  36.113  1.00 41.86  ? 241 CYS   B C     1 
ATOM   15835 O  O     . CYS   F 2  239 ? 17.434  72.282  36.740  1.00 43.79  ? 241 CYS   B O     1 
ATOM   15836 C  CB    . CYS   F 2  239 ? 15.639  70.055  37.819  1.00 32.02  ? 241 CYS   B CB    1 
ATOM   15837 S  SG    . CYS   F 2  239 ? 14.340  69.898  39.081  1.00 45.33  ? 241 CYS   B SG    1 
ATOM   15838 N  N     . LEU   F 2  240 ? 17.027  71.006  34.919  1.00 42.49  ? 242 LEU   B N     1 
ATOM   15839 C  CA    . LEU   F 2  240 ? 18.255  71.387  34.223  1.00 38.45  ? 242 LEU   B CA    1 
ATOM   15840 C  C     . LEU   F 2  240 ? 18.072  72.571  33.283  1.00 36.69  ? 242 LEU   B C     1 
ATOM   15841 O  O     . LEU   F 2  240 ? 19.068  73.179  32.875  1.00 43.29  ? 242 LEU   B O     1 
ATOM   15842 C  CB    . LEU   F 2  240 ? 18.804  70.225  33.377  1.00 30.55  ? 242 LEU   B CB    1 
ATOM   15843 C  CG    . LEU   F 2  240 ? 18.946  68.826  33.947  1.00 26.76  ? 242 LEU   B CG    1 
ATOM   15844 C  CD1   . LEU   F 2  240 ? 18.969  67.828  32.821  1.00 22.75  ? 242 LEU   B CD1   1 
ATOM   15845 C  CD2   . LEU   F 2  240 ? 20.202  68.709  34.794  1.00 30.82  ? 242 LEU   B CD2   1 
ATOM   15846 N  N     . ARG   F 2  241 ? 16.838  72.888  32.903  1.00 32.77  ? 243 ARG   B N     1 
ATOM   15847 C  CA    . ARG   F 2  241 ? 16.582  73.825  31.819  1.00 37.29  ? 243 ARG   B CA    1 
ATOM   15848 C  C     . ARG   F 2  241 ? 15.949  75.130  32.272  1.00 38.86  ? 243 ARG   B C     1 
ATOM   15849 O  O     . ARG   F 2  241 ? 15.841  76.056  31.460  1.00 46.49  ? 243 ARG   B O     1 
ATOM   15850 C  CB    . ARG   F 2  241 ? 15.670  73.182  30.758  1.00 37.06  ? 243 ARG   B CB    1 
ATOM   15851 C  CG    . ARG   F 2  241 ? 16.159  71.852  30.220  1.00 34.21  ? 243 ARG   B CG    1 
ATOM   15852 C  CD    . ARG   F 2  241 ? 15.339  71.417  29.012  1.00 29.80  ? 243 ARG   B CD    1 
ATOM   15853 N  NE    . ARG   F 2  241 ? 14.087  70.753  29.351  1.00 33.01  ? 243 ARG   B NE    1 
ATOM   15854 C  CZ    . ARG   F 2  241 ? 12.881  71.304  29.245  1.00 41.76  ? 243 ARG   B CZ    1 
ATOM   15855 N  NH1   . ARG   F 2  241 ? 12.725  72.567  28.878  1.00 35.34  ? 243 ARG   B NH1   1 
ATOM   15856 N  NH2   . ARG   F 2  241 ? 11.803  70.566  29.513  1.00 33.40  ? 243 ARG   B NH2   1 
ATOM   15857 N  N     . PHE   F 2  242 ? 15.508  75.224  33.520  1.00 33.83  ? 244 PHE   B N     1 
ATOM   15858 C  CA    . PHE   F 2  242 ? 14.993  76.473  34.062  1.00 41.91  ? 244 PHE   B CA    1 
ATOM   15859 C  C     . PHE   F 2  242 ? 15.703  76.749  35.381  1.00 45.49  ? 244 PHE   B C     1 
ATOM   15860 O  O     . PHE   F 2  242 ? 16.517  75.928  35.817  1.00 46.71  ? 244 PHE   B O     1 
ATOM   15861 C  CB    . PHE   F 2  242 ? 13.479  76.409  34.256  1.00 41.57  ? 244 PHE   B CB    1 
ATOM   15862 C  CG    . PHE   F 2  242 ? 12.711  76.135  33.002  1.00 35.16  ? 244 PHE   B CG    1 
ATOM   15863 C  CD1   . PHE   F 2  242 ? 12.616  77.094  32.005  1.00 48.28  ? 244 PHE   B CD1   1 
ATOM   15864 C  CD2   . PHE   F 2  242 ? 12.054  74.933  32.830  1.00 39.08  ? 244 PHE   B CD2   1 
ATOM   15865 C  CE1   . PHE   F 2  242 ? 11.892  76.851  30.835  1.00 40.56  ? 244 PHE   B CE1   1 
ATOM   15866 C  CE2   . PHE   F 2  242 ? 11.329  74.682  31.672  1.00 40.20  ? 244 PHE   B CE2   1 
ATOM   15867 C  CZ    . PHE   F 2  242 ? 11.248  75.641  30.673  1.00 37.07  ? 244 PHE   B CZ    1 
ATOM   15868 N  N     . PRO   F 2  243 ? 15.436  77.879  36.040  1.00 49.19  ? 245 PRO   B N     1 
ATOM   15869 C  CA    . PRO   F 2  243 ? 16.144  78.193  37.290  1.00 37.83  ? 245 PRO   B CA    1 
ATOM   15870 C  C     . PRO   F 2  243 ? 15.555  77.449  38.479  1.00 41.01  ? 245 PRO   B C     1 
ATOM   15871 O  O     . PRO   F 2  243 ? 14.345  77.237  38.567  1.00 45.14  ? 245 PRO   B O     1 
ATOM   15872 C  CB    . PRO   F 2  243 ? 15.950  79.709  37.433  1.00 36.29  ? 245 PRO   B CB    1 
ATOM   15873 C  CG    . PRO   F 2  243 ? 15.427  80.179  36.101  1.00 49.97  ? 245 PRO   B CG    1 
ATOM   15874 C  CD    . PRO   F 2  243 ? 14.654  79.027  35.557  1.00 50.99  ? 245 PRO   B CD    1 
ATOM   15875 N  N     . GLY   F 2  244 ? 16.427  77.043  39.397  1.00 40.64  ? 246 GLY   B N     1 
ATOM   15876 C  CA    . GLY   F 2  244 ? 15.991  76.268  40.539  1.00 37.34  ? 246 GLY   B CA    1 
ATOM   15877 C  C     . GLY   F 2  244 ? 17.151  75.800  41.401  1.00 53.41  ? 246 GLY   B C     1 
ATOM   15878 O  O     . GLY   F 2  244 ? 18.332  76.027  41.103  1.00 41.40  ? 246 GLY   B O     1 
ATOM   15879 N  N     . GLN   F 2  245 ? 16.774  75.126  42.488  1.00 50.16  ? 247 GLN   B N     1 
ATOM   15880 C  CA    . GLN   F 2  245 ? 17.663  74.667  43.550  1.00 50.87  ? 247 GLN   B CA    1 
ATOM   15881 C  C     . GLN   F 2  245 ? 17.959  73.182  43.476  1.00 50.81  ? 247 GLN   B C     1 
ATOM   15882 O  O     . GLN   F 2  245 ? 19.101  72.771  43.692  1.00 64.43  ? 247 GLN   B O     1 
ATOM   15883 C  CB    . GLN   F 2  245 ? 17.040  74.956  44.923  1.00 49.61  ? 247 GLN   B CB    1 
ATOM   15884 C  CG    . GLN   F 2  245 ? 16.757  76.418  45.178  1.00 57.95  ? 247 GLN   B CG    1 
ATOM   15885 C  CD    . GLN   F 2  245 ? 18.037  77.195  45.376  1.00 59.51  ? 247 GLN   B CD    1 
ATOM   15886 O  OE1   . GLN   F 2  245 ? 18.826  76.886  46.284  1.00 55.08  ? 247 GLN   B OE1   1 
ATOM   15887 N  NE2   . GLN   F 2  245 ? 18.272  78.189  44.514  1.00 42.43  ? 247 GLN   B NE2   1 
ATOM   15888 N  N     . LEU   F 2  246 ? 16.942  72.374  43.206  1.00 41.88  ? 248 LEU   B N     1 
ATOM   15889 C  CA    . LEU   F 2  246 ? 17.081  70.931  43.227  1.00 40.70  ? 248 LEU   B CA    1 
ATOM   15890 C  C     . LEU   F 2  246 ? 17.624  70.421  41.897  1.00 37.96  ? 248 LEU   B C     1 
ATOM   15891 O  O     . LEU   F 2  246 ? 17.156  70.815  40.829  1.00 39.92  ? 248 LEU   B O     1 
ATOM   15892 C  CB    . LEU   F 2  246 ? 15.729  70.283  43.520  1.00 37.89  ? 248 LEU   B CB    1 
ATOM   15893 C  CG    . LEU   F 2  246 ? 15.841  68.801  43.858  1.00 44.84  ? 248 LEU   B CG    1 
ATOM   15894 C  CD1   . LEU   F 2  246 ? 16.713  68.611  45.104  1.00 37.55  ? 248 LEU   B CD1   1 
ATOM   15895 C  CD2   . LEU   F 2  246 ? 14.457  68.170  44.041  1.00 51.80  ? 248 LEU   B CD2   1 
ATOM   15896 N  N     . ASN   F 2  247 ? 18.615  69.551  41.961  1.00 42.50  ? 249 ASN   B N     1 
ATOM   15897 C  CA    . ASN   F 2  247 ? 18.978  68.736  40.816  1.00 33.99  ? 249 ASN   B CA    1 
ATOM   15898 C  C     . ASN   F 2  247 ? 19.142  69.574  39.542  1.00 33.60  ? 249 ASN   B C     1 
ATOM   15899 O  O     . ASN   F 2  247 ? 18.639  69.223  38.475  1.00 42.38  ? 249 ASN   B O     1 
ATOM   15900 C  CB    . ASN   F 2  247 ? 17.935  67.645  40.626  1.00 27.17  ? 249 ASN   B CB    1 
ATOM   15901 C  CG    . ASN   F 2  247 ? 17.860  66.690  41.807  1.00 32.99  ? 249 ASN   B CG    1 
ATOM   15902 O  OD1   . ASN   F 2  247 ? 18.871  66.367  42.429  1.00 35.67  ? 249 ASN   B OD1   1 
ATOM   15903 N  ND2   . ASN   F 2  247 ? 16.660  66.214  42.106  1.00 33.69  ? 249 ASN   B ND2   1 
ATOM   15904 N  N     . ALA   F 2  248 ? 19.873  70.685  39.643  1.00 28.54  ? 250 ALA   B N     1 
ATOM   15905 C  CA    . ALA   F 2  248 ? 19.919  71.608  38.516  1.00 39.08  ? 250 ALA   B CA    1 
ATOM   15906 C  C     . ALA   F 2  248 ? 21.014  71.284  37.516  1.00 37.26  ? 250 ALA   B C     1 
ATOM   15907 O  O     . ALA   F 2  248 ? 21.089  71.939  36.471  1.00 42.35  ? 250 ALA   B O     1 
ATOM   15908 C  CB    . ALA   F 2  248 ? 20.088  73.058  38.985  1.00 34.96  ? 250 ALA   B CB    1 
ATOM   15909 N  N     . ASP   F 2  249 ? 21.864  70.309  37.803  1.00 33.15  ? 251 ASP   B N     1 
ATOM   15910 C  CA    . ASP   F 2  249 ? 22.822  69.811  36.826  1.00 37.39  ? 251 ASP   B CA    1 
ATOM   15911 C  C     . ASP   F 2  249 ? 22.892  68.298  36.988  1.00 33.33  ? 251 ASP   B C     1 
ATOM   15912 O  O     . ASP   F 2  249 ? 22.273  67.723  37.886  1.00 35.37  ? 251 ASP   B O     1 
ATOM   15913 C  CB    . ASP   F 2  249 ? 24.200  70.470  36.995  1.00 29.29  ? 251 ASP   B CB    1 
ATOM   15914 C  CG    . ASP   F 2  249 ? 24.894  70.021  38.260  1.00 35.45  ? 251 ASP   B CG    1 
ATOM   15915 O  OD1   . ASP   F 2  249 ? 25.337  68.844  38.304  1.00 33.02  ? 251 ASP   B OD1   1 
ATOM   15916 O  OD2   . ASP   F 2  249 ? 24.971  70.831  39.214  1.00 36.22  ? 251 ASP   B OD2   1 
ATOM   15917 N  N     . LEU   F 2  250 ? 23.676  67.642  36.134  1.00 30.44  ? 252 LEU   B N     1 
ATOM   15918 C  CA    . LEU   F 2  250 ? 23.701  66.186  36.174  1.00 29.58  ? 252 LEU   B CA    1 
ATOM   15919 C  C     . LEU   F 2  250 ? 24.478  65.648  37.379  1.00 35.10  ? 252 LEU   B C     1 
ATOM   15920 O  O     . LEU   F 2  250 ? 24.140  64.574  37.890  1.00 37.98  ? 252 LEU   B O     1 
ATOM   15921 C  CB    . LEU   F 2  250 ? 24.257  65.643  34.861  1.00 33.51  ? 252 LEU   B CB    1 
ATOM   15922 C  CG    . LEU   F 2  250 ? 23.443  66.108  33.651  1.00 35.19  ? 252 LEU   B CG    1 
ATOM   15923 C  CD1   . LEU   F 2  250 ? 24.292  66.032  32.408  1.00 33.02  ? 252 LEU   B CD1   1 
ATOM   15924 C  CD2   . LEU   F 2  250 ? 22.170  65.278  33.501  1.00 23.62  ? 252 LEU   B CD2   1 
ATOM   15925 N  N     . ARG   F 2  251 ? 25.500  66.363  37.872  1.00 33.85  ? 253 ARG   B N     1 
ATOM   15926 C  CA    . ARG   F 2  251 ? 26.216  65.807  39.017  1.00 32.40  ? 253 ARG   B CA    1 
ATOM   15927 C  C     . ARG   F 2  251 ? 25.390  65.970  40.284  1.00 33.57  ? 253 ARG   B C     1 
ATOM   15928 O  O     . ARG   F 2  251 ? 25.258  65.024  41.076  1.00 28.56  ? 253 ARG   B O     1 
ATOM   15929 C  CB    . ARG   F 2  251 ? 27.602  66.439  39.182  1.00 27.42  ? 253 ARG   B CB    1 
ATOM   15930 C  CG    . ARG   F 2  251 ? 28.504  65.577  40.062  1.00 26.58  ? 253 ARG   B CG    1 
ATOM   15931 C  CD    . ARG   F 2  251 ? 29.963  65.980  40.056  1.00 28.53  ? 253 ARG   B CD    1 
ATOM   15932 N  NE    . ARG   F 2  251 ? 30.417  66.454  38.759  1.00 31.01  ? 253 ARG   B NE    1 
ATOM   15933 C  CZ    . ARG   F 2  251 ? 30.984  65.685  37.842  1.00 46.17  ? 253 ARG   B CZ    1 
ATOM   15934 N  NH1   . ARG   F 2  251 ? 31.235  64.403  38.072  1.00 57.30  ? 253 ARG   B NH1   1 
ATOM   15935 N  NH2   . ARG   F 2  251 ? 31.292  66.210  36.658  1.00 48.45  ? 253 ARG   B NH2   1 
ATOM   15936 N  N     . LYS   F 2  252 ? 24.826  67.169  40.479  1.00 33.49  ? 254 LYS   B N     1 
ATOM   15937 C  CA    . LYS   F 2  252 ? 23.840  67.402  41.532  1.00 33.56  ? 254 LYS   B CA    1 
ATOM   15938 C  C     . LYS   F 2  252 ? 22.780  66.307  41.526  1.00 30.88  ? 254 LYS   B C     1 
ATOM   15939 O  O     . LYS   F 2  252 ? 22.486  65.693  42.560  1.00 26.59  ? 254 LYS   B O     1 
ATOM   15940 C  CB    . LYS   F 2  252 ? 23.191  68.780  41.330  1.00 38.50  ? 254 LYS   B CB    1 
ATOM   15941 C  CG    . LYS   F 2  252 ? 23.366  69.791  42.470  1.00 30.33  ? 254 LYS   B CG    1 
ATOM   15942 C  CD    . LYS   F 2  252 ? 24.825  70.055  42.793  1.00 37.14  ? 254 LYS   B CD    1 
ATOM   15943 C  CE    . LYS   F 2  252 ? 25.007  71.078  43.931  1.00 31.75  ? 254 LYS   B CE    1 
ATOM   15944 N  NZ    . LYS   F 2  252 ? 24.686  72.492  43.514  1.00 31.83  ? 254 LYS   B NZ    1 
ATOM   15945 N  N     . LEU   F 2  253 ? 22.215  66.020  40.349  1.00 31.77  ? 255 LEU   B N     1 
ATOM   15946 C  CA    . LEU   F 2  253 ? 21.202  64.976  40.271  1.00 28.91  ? 255 LEU   B CA    1 
ATOM   15947 C  C     . LEU   F 2  253 ? 21.769  63.627  40.699  1.00 27.23  ? 255 LEU   B C     1 
ATOM   15948 O  O     . LEU   F 2  253 ? 21.155  62.910  41.494  1.00 24.09  ? 255 LEU   B O     1 
ATOM   15949 C  CB    . LEU   F 2  253 ? 20.629  64.913  38.863  1.00 35.54  ? 255 LEU   B CB    1 
ATOM   15950 C  CG    . LEU   F 2  253 ? 19.692  63.730  38.632  1.00 29.28  ? 255 LEU   B CG    1 
ATOM   15951 C  CD1   . LEU   F 2  253 ? 18.506  63.792  39.548  1.00 24.52  ? 255 LEU   B CD1   1 
ATOM   15952 C  CD2   . LEU   F 2  253 ? 19.272  63.694  37.192  1.00 27.94  ? 255 LEU   B CD2   1 
ATOM   15953 N  N     . ALA   F 2  254 ? 22.967  63.280  40.214  1.00 28.09  ? 256 ALA   B N     1 
ATOM   15954 C  CA    . ALA   F 2  254 ? 23.532  61.971  40.535  1.00 27.88  ? 256 ALA   B CA    1 
ATOM   15955 C  C     . ALA   F 2  254 ? 23.831  61.831  42.023  1.00 25.69  ? 256 ALA   B C     1 
ATOM   15956 O  O     . ALA   F 2  254 ? 23.608  60.769  42.606  1.00 26.06  ? 256 ALA   B O     1 
ATOM   15957 C  CB    . ALA   F 2  254 ? 24.793  61.713  39.707  1.00 33.39  ? 256 ALA   B CB    1 
ATOM   15958 N  N     . VAL   F 2  255 ? 24.336  62.885  42.662  1.00 27.73  ? 257 VAL   B N     1 
ATOM   15959 C  CA    . VAL   F 2  255 ? 24.684  62.753  44.074  1.00 27.05  ? 257 VAL   B CA    1 
ATOM   15960 C  C     . VAL   F 2  255 ? 23.437  62.524  44.914  1.00 33.56  ? 257 VAL   B C     1 
ATOM   15961 O  O     . VAL   F 2  255 ? 23.512  61.923  45.999  1.00 29.00  ? 257 VAL   B O     1 
ATOM   15962 C  CB    . VAL   F 2  255 ? 25.454  63.987  44.568  1.00 24.22  ? 257 VAL   B CB    1 
ATOM   15963 C  CG1   . VAL   F 2  255 ? 25.752  63.835  46.056  1.00 19.52  ? 257 VAL   B CG1   1 
ATOM   15964 C  CG2   . VAL   F 2  255 ? 26.712  64.178  43.763  1.00 20.28  ? 257 VAL   B CG2   1 
ATOM   15965 N  N     . ASN   F 2  256 ? 22.278  63.004  44.431  1.00 31.48  ? 258 ASN   B N     1 
ATOM   15966 C  CA    . ASN   F 2  256 ? 21.004  62.834  45.130  1.00 30.43  ? 258 ASN   B CA    1 
ATOM   15967 C  C     . ASN   F 2  256 ? 20.359  61.482  44.846  1.00 32.42  ? 258 ASN   B C     1 
ATOM   15968 O  O     . ASN   F 2  256 ? 19.738  60.900  45.742  1.00 35.78  ? 258 ASN   B O     1 
ATOM   15969 C  CB    . ASN   F 2  256 ? 20.035  63.957  44.748  1.00 32.81  ? 258 ASN   B CB    1 
ATOM   15970 C  CG    . ASN   F 2  256 ? 20.149  65.151  45.655  1.00 34.94  ? 258 ASN   B CG    1 
ATOM   15971 O  OD1   . ASN   F 2  256 ? 20.565  65.023  46.801  1.00 35.69  ? 258 ASN   B OD1   1 
ATOM   15972 N  ND2   . ASN   F 2  256 ? 19.770  66.322  45.156  1.00 38.25  ? 258 ASN   B ND2   1 
ATOM   15973 N  N     . MET   F 2  257 ? 20.475  60.972  43.612  1.00 24.42  ? 259 MET   B N     1 
ATOM   15974 C  CA    . MET   F 2  257 ? 19.791  59.735  43.241  1.00 25.50  ? 259 MET   B CA    1 
ATOM   15975 C  C     . MET   F 2  257 ? 20.622  58.462  43.432  1.00 30.36  ? 259 MET   B C     1 
ATOM   15976 O  O     . MET   F 2  257 ? 20.047  57.386  43.645  1.00 35.78  ? 259 MET   B O     1 
ATOM   15977 C  CB    . MET   F 2  257 ? 19.331  59.810  41.784  1.00 25.93  ? 259 MET   B CB    1 
ATOM   15978 C  CG    . MET   F 2  257 ? 18.376  60.970  41.492  1.00 24.32  ? 259 MET   B CG    1 
ATOM   15979 S  SD    . MET   F 2  257 ? 16.912  60.881  42.526  1.00 35.74  ? 259 MET   B SD    1 
ATOM   15980 C  CE    . MET   F 2  257 ? 16.225  59.312  42.029  1.00 26.45  ? 259 MET   B CE    1 
ATOM   15981 N  N     . VAL   F 2  258 ? 21.946  58.525  43.371  1.00 29.42  ? 260 VAL   B N     1 
ATOM   15982 C  CA    . VAL   F 2  258 ? 22.725  57.291  43.225  1.00 31.58  ? 260 VAL   B CA    1 
ATOM   15983 C  C     . VAL   F 2  258 ? 23.508  57.004  44.504  1.00 27.39  ? 260 VAL   B C     1 
ATOM   15984 O  O     . VAL   F 2  258 ? 24.606  57.536  44.695  1.00 25.97  ? 260 VAL   B O     1 
ATOM   15985 C  CB    . VAL   F 2  258 ? 23.632  57.364  41.977  1.00 18.52  ? 260 VAL   B CB    1 
ATOM   15986 C  CG1   . VAL   F 2  258 ? 24.405  56.068  41.774  1.00 23.98  ? 260 VAL   B CG1   1 
ATOM   15987 C  CG2   . VAL   F 2  258 ? 22.769  57.583  40.790  1.00 20.36  ? 260 VAL   B CG2   1 
ATOM   15988 N  N     . PRO   F 2  259 ? 22.978  56.174  45.405  1.00 25.75  ? 261 PRO   B N     1 
ATOM   15989 C  CA    . PRO   F 2  259 ? 23.711  55.869  46.639  1.00 32.41  ? 261 PRO   B CA    1 
ATOM   15990 C  C     . PRO   F 2  259 ? 24.836  54.864  46.466  1.00 32.94  ? 261 PRO   B C     1 
ATOM   15991 O  O     . PRO   F 2  259 ? 25.748  54.825  47.305  1.00 37.72  ? 261 PRO   B O     1 
ATOM   15992 C  CB    . PRO   F 2  259 ? 22.618  55.304  47.555  1.00 29.73  ? 261 PRO   B CB    1 
ATOM   15993 C  CG    . PRO   F 2  259 ? 21.645  54.714  46.603  1.00 23.78  ? 261 PRO   B CG    1 
ATOM   15994 C  CD    . PRO   F 2  259 ? 21.592  55.686  45.468  1.00 25.18  ? 261 PRO   B CD    1 
ATOM   15995 N  N     . PHE   F 2  260 ? 24.783  54.033  45.433  1.00 34.51  ? 262 PHE   B N     1 
ATOM   15996 C  CA    . PHE   F 2  260 ? 25.818  53.057  45.136  1.00 28.21  ? 262 PHE   B CA    1 
ATOM   15997 C  C     . PHE   F 2  260 ? 26.021  53.093  43.629  1.00 28.64  ? 262 PHE   B C     1 
ATOM   15998 O  O     . PHE   F 2  260 ? 25.046  53.219  42.874  1.00 30.35  ? 262 PHE   B O     1 
ATOM   15999 C  CB    . PHE   F 2  260 ? 25.433  51.658  45.601  1.00 23.68  ? 262 PHE   B CB    1 
ATOM   16000 C  CG    . PHE   F 2  260 ? 25.003  51.603  47.026  1.00 29.12  ? 262 PHE   B CG    1 
ATOM   16001 C  CD1   . PHE   F 2  260 ? 25.941  51.681  48.055  1.00 33.50  ? 262 PHE   B CD1   1 
ATOM   16002 C  CD2   . PHE   F 2  260 ? 23.665  51.474  47.357  1.00 34.24  ? 262 PHE   B CD2   1 
ATOM   16003 C  CE1   . PHE   F 2  260 ? 25.549  51.625  49.408  1.00 31.52  ? 262 PHE   B CE1   1 
ATOM   16004 C  CE2   . PHE   F 2  260 ? 23.265  51.415  48.720  1.00 40.04  ? 262 PHE   B CE2   1 
ATOM   16005 C  CZ    . PHE   F 2  260 ? 24.216  51.489  49.739  1.00 26.52  ? 262 PHE   B CZ    1 
ATOM   16006 N  N     . PRO   F 2  261 ? 27.266  53.015  43.164  1.00 31.18  ? 263 PRO   B N     1 
ATOM   16007 C  CA    . PRO   F 2  261 ? 27.541  53.352  41.753  1.00 24.95  ? 263 PRO   B CA    1 
ATOM   16008 C  C     . PRO   F 2  261 ? 26.769  52.510  40.747  1.00 22.01  ? 263 PRO   B C     1 
ATOM   16009 O  O     . PRO   F 2  261 ? 26.387  53.023  39.688  1.00 21.58  ? 263 PRO   B O     1 
ATOM   16010 C  CB    . PRO   F 2  261 ? 29.051  53.134  41.625  1.00 13.22  ? 263 PRO   B CB    1 
ATOM   16011 C  CG    . PRO   F 2  261 ? 29.555  53.014  43.027  1.00 26.73  ? 263 PRO   B CG    1 
ATOM   16012 C  CD    . PRO   F 2  261 ? 28.463  52.572  43.896  1.00 28.83  ? 263 PRO   B CD    1 
ATOM   16013 N  N     . ARG   F 2  262 ? 26.515  51.234  41.031  1.00 21.73  ? 264 ARG   B N     1 
ATOM   16014 C  CA    . ARG   F 2  262 ? 25.846  50.438  40.007  1.00 26.52  ? 264 ARG   B CA    1 
ATOM   16015 C  C     . ARG   F 2  262 ? 24.332  50.635  40.014  1.00 25.01  ? 264 ARG   B C     1 
ATOM   16016 O  O     . ARG   F 2  262 ? 23.685  50.459  38.981  1.00 29.15  ? 264 ARG   B O     1 
ATOM   16017 C  CB    . ARG   F 2  262 ? 26.205  48.953  40.157  1.00 21.40  ? 264 ARG   B CB    1 
ATOM   16018 C  CG    . ARG   F 2  262 ? 27.722  48.687  40.204  1.00 24.35  ? 264 ARG   B CG    1 
ATOM   16019 C  CD    . ARG   F 2  262 ? 28.116  47.250  40.556  1.00 15.09  ? 264 ARG   B CD    1 
ATOM   16020 N  NE    . ARG   F 2  262 ? 27.930  46.365  39.414  1.00 26.82  ? 264 ARG   B NE    1 
ATOM   16021 C  CZ    . ARG   F 2  262 ? 27.216  45.250  39.433  1.00 35.32  ? 264 ARG   B CZ    1 
ATOM   16022 N  NH1   . ARG   F 2  262 ? 26.650  44.806  40.549  1.00 45.27  ? 264 ARG   B NH1   1 
ATOM   16023 N  NH2   . ARG   F 2  262 ? 27.090  44.545  38.315  1.00 30.74  ? 264 ARG   B NH2   1 
ATOM   16024 N  N     . LEU   F 2  263 ? 23.740  51.011  41.141  1.00 27.26  ? 265 LEU   B N     1 
ATOM   16025 C  CA    . LEU   F 2  263 ? 22.290  51.208  41.185  1.00 26.28  ? 265 LEU   B CA    1 
ATOM   16026 C  C     . LEU   F 2  263 ? 21.946  52.612  40.686  1.00 22.84  ? 265 LEU   B C     1 
ATOM   16027 O  O     . LEU   F 2  263 ? 21.547  53.504  41.431  1.00 20.94  ? 265 LEU   B O     1 
ATOM   16028 C  CB    . LEU   F 2  263 ? 21.769  50.944  42.585  1.00 27.24  ? 265 LEU   B CB    1 
ATOM   16029 C  CG    . LEU   F 2  263 ? 22.434  49.667  43.086  1.00 24.56  ? 265 LEU   B CG    1 
ATOM   16030 C  CD1   . LEU   F 2  263 ? 21.921  49.264  44.442  1.00 26.11  ? 265 LEU   B CD1   1 
ATOM   16031 C  CD2   . LEU   F 2  263 ? 22.228  48.573  42.072  1.00 26.72  ? 265 LEU   B CD2   1 
ATOM   16032 N  N     . HIS   F 2  264 ? 22.111  52.803  39.376  1.00 25.75  ? 266 HIS   B N     1 
ATOM   16033 C  CA    . HIS   F 2  264 ? 21.798  54.084  38.761  1.00 24.08  ? 266 HIS   B CA    1 
ATOM   16034 C  C     . HIS   F 2  264 ? 20.714  53.962  37.698  1.00 23.84  ? 266 HIS   B C     1 
ATOM   16035 O  O     . HIS   F 2  264 ? 20.676  54.743  36.740  1.00 24.09  ? 266 HIS   B O     1 
ATOM   16036 C  CB    . HIS   F 2  264 ? 23.051  54.754  38.198  1.00 27.15  ? 266 HIS   B CB    1 
ATOM   16037 C  CG    . HIS   F 2  264 ? 23.813  53.943  37.190  1.00 24.55  ? 266 HIS   B CG    1 
ATOM   16038 N  ND1   . HIS   F 2  264 ? 24.743  52.991  37.548  1.00 22.29  ? 266 HIS   B ND1   1 
ATOM   16039 C  CD2   . HIS   F 2  264 ? 23.862  54.026  35.839  1.00 23.73  ? 266 HIS   B CD2   1 
ATOM   16040 C  CE1   . HIS   F 2  264 ? 25.299  52.494  36.460  1.00 24.76  ? 266 HIS   B CE1   1 
ATOM   16041 N  NE2   . HIS   F 2  264 ? 24.790  53.111  35.411  1.00 22.84  ? 266 HIS   B NE2   1 
ATOM   16042 N  N     . PHE   F 2  265 ? 19.791  53.027  37.894  1.00 22.92  ? 267 PHE   B N     1 
ATOM   16043 C  CA    . PHE   F 2  265 ? 18.705  52.781  36.955  1.00 24.50  ? 267 PHE   B CA    1 
ATOM   16044 C  C     . PHE   F 2  265 ? 17.389  53.254  37.565  1.00 28.68  ? 267 PHE   B C     1 
ATOM   16045 O  O     . PHE   F 2  265 ? 16.981  52.784  38.633  1.00 31.17  ? 267 PHE   B O     1 
ATOM   16046 C  CB    . PHE   F 2  265 ? 18.656  51.303  36.580  1.00 30.05  ? 267 PHE   B CB    1 
ATOM   16047 C  CG    . PHE   F 2  265 ? 19.817  50.862  35.741  1.00 27.36  ? 267 PHE   B CG    1 
ATOM   16048 C  CD1   . PHE   F 2  265 ? 19.785  51.000  34.360  1.00 30.67  ? 267 PHE   B CD1   1 
ATOM   16049 C  CD2   . PHE   F 2  265 ? 20.958  50.341  36.324  1.00 26.48  ? 267 PHE   B CD2   1 
ATOM   16050 C  CE1   . PHE   F 2  265 ? 20.852  50.585  33.578  1.00 21.56  ? 267 PHE   B CE1   1 
ATOM   16051 C  CE2   . PHE   F 2  265 ? 22.039  49.941  35.531  1.00 24.45  ? 267 PHE   B CE2   1 
ATOM   16052 C  CZ    . PHE   F 2  265 ? 21.978  50.062  34.172  1.00 21.29  ? 267 PHE   B CZ    1 
ATOM   16053 N  N     . PHE   F 2  266 ? 16.728  54.172  36.874  1.00 22.61  ? 268 PHE   B N     1 
ATOM   16054 C  CA    . PHE   F 2  266 ? 15.648  54.964  37.423  1.00 19.86  ? 268 PHE   B CA    1 
ATOM   16055 C  C     . PHE   F 2  266 ? 14.311  54.586  36.807  1.00 22.80  ? 268 PHE   B C     1 
ATOM   16056 O  O     . PHE   F 2  266 ? 14.221  54.345  35.601  1.00 27.18  ? 268 PHE   B O     1 
ATOM   16057 C  CB    . PHE   F 2  266 ? 15.921  56.437  37.170  1.00 25.73  ? 268 PHE   B CB    1 
ATOM   16058 C  CG    . PHE   F 2  266 ? 17.164  56.949  37.834  1.00 26.44  ? 268 PHE   B CG    1 
ATOM   16059 C  CD1   . PHE   F 2  266 ? 17.736  56.263  38.892  1.00 26.32  ? 268 PHE   B CD1   1 
ATOM   16060 C  CD2   . PHE   F 2  266 ? 17.742  58.138  37.422  1.00 25.94  ? 268 PHE   B CD2   1 
ATOM   16061 C  CE1   . PHE   F 2  266 ? 18.877  56.742  39.526  1.00 21.29  ? 268 PHE   B CE1   1 
ATOM   16062 C  CE2   . PHE   F 2  266 ? 18.886  58.609  38.042  1.00 29.53  ? 268 PHE   B CE2   1 
ATOM   16063 C  CZ    . PHE   F 2  266 ? 19.449  57.902  39.098  1.00 24.50  ? 268 PHE   B CZ    1 
ATOM   16064 N  N     . MET   F 2  267 ? 13.271  54.549  37.638  1.00 20.53  ? 269 MET   B N     1 
ATOM   16065 C  CA    . MET   F 2  267 ? 11.904  54.450  37.152  1.00 21.88  ? 269 MET   B CA    1 
ATOM   16066 C  C     . MET   F 2  267 ? 11.354  55.850  36.944  1.00 20.95  ? 269 MET   B C     1 
ATOM   16067 O  O     . MET   F 2  267 ? 11.081  56.543  37.932  1.00 28.91  ? 269 MET   B O     1 
ATOM   16068 C  CB    . MET   F 2  267 ? 11.021  53.714  38.141  1.00 20.60  ? 269 MET   B CB    1 
ATOM   16069 C  CG    . MET   F 2  267 ? 11.520  52.399  38.630  1.00 31.72  ? 269 MET   B CG    1 
ATOM   16070 S  SD    . MET   F 2  267 ? 10.156  51.617  39.512  1.00 47.44  ? 269 MET   B SD    1 
ATOM   16071 C  CE    . MET   F 2  267 ? 8.795   52.106  38.460  1.00 26.54  ? 269 MET   B CE    1 
ATOM   16072 N  N     . PRO   F 2  268 ? 11.145  56.301  35.716  1.00 17.78  ? 270 PRO   B N     1 
ATOM   16073 C  CA    . PRO   F 2  268 ? 10.400  57.542  35.519  1.00 18.42  ? 270 PRO   B CA    1 
ATOM   16074 C  C     . PRO   F 2  268 ? 8.913   57.291  35.712  1.00 24.61  ? 270 PRO   B C     1 
ATOM   16075 O  O     . PRO   F 2  268 ? 8.429   56.165  35.623  1.00 27.78  ? 270 PRO   B O     1 
ATOM   16076 C  CB    . PRO   F 2  268 ? 10.721  57.935  34.068  1.00 23.09  ? 270 PRO   B CB    1 
ATOM   16077 C  CG    . PRO   F 2  268 ? 11.616  56.776  33.509  1.00 17.95  ? 270 PRO   B CG    1 
ATOM   16078 C  CD    . PRO   F 2  268 ? 11.435  55.630  34.439  1.00 21.06  ? 270 PRO   B CD    1 
ATOM   16079 N  N     . GLY   F 2  269 ? 8.195   58.368  36.010  1.00 30.47  ? 271 GLY   B N     1 
ATOM   16080 C  CA    . GLY   F 2  269 ? 6.746   58.328  36.116  1.00 29.69  ? 271 GLY   B CA    1 
ATOM   16081 C  C     . GLY   F 2  269 ? 6.204   59.701  35.792  1.00 32.68  ? 271 GLY   B C     1 
ATOM   16082 O  O     . GLY   F 2  269 ? 6.938   60.692  35.819  1.00 31.35  ? 271 GLY   B O     1 
ATOM   16083 N  N     . PHE   F 2  270 ? 4.909   59.759  35.484  1.00 35.88  ? 272 PHE   B N     1 
ATOM   16084 C  CA    . PHE   F 2  270 ? 4.363   61.010  34.965  1.00 33.77  ? 272 PHE   B CA    1 
ATOM   16085 C  C     . PHE   F 2  270 ? 2.854   61.087  35.190  1.00 33.69  ? 272 PHE   B C     1 
ATOM   16086 O  O     . PHE   F 2  270 ? 2.165   60.068  35.230  1.00 33.00  ? 272 PHE   B O     1 
ATOM   16087 C  CB    . PHE   F 2  270 ? 4.694   61.134  33.484  1.00 23.79  ? 272 PHE   B CB    1 
ATOM   16088 C  CG    . PHE   F 2  270 ? 4.304   62.429  32.892  1.00 35.51  ? 272 PHE   B CG    1 
ATOM   16089 C  CD1   . PHE   F 2  270 ? 3.028   62.611  32.372  1.00 34.15  ? 272 PHE   B CD1   1 
ATOM   16090 C  CD2   . PHE   F 2  270 ? 5.217   63.479  32.829  1.00 38.91  ? 272 PHE   B CD2   1 
ATOM   16091 C  CE1   . PHE   F 2  270 ? 2.660   63.832  31.806  1.00 34.99  ? 272 PHE   B CE1   1 
ATOM   16092 C  CE2   . PHE   F 2  270 ? 4.863   64.705  32.262  1.00 38.93  ? 272 PHE   B CE2   1 
ATOM   16093 C  CZ    . PHE   F 2  270 ? 3.579   64.880  31.749  1.00 38.56  ? 272 PHE   B CZ    1 
ATOM   16094 N  N     . ALA   F 2  271 ? 2.344   62.310  35.337  1.00 37.01  ? 273 ALA   B N     1 
ATOM   16095 C  CA    . ALA   F 2  271 ? 0.895   62.466  35.447  1.00 33.83  ? 273 ALA   B CA    1 
ATOM   16096 C  C     . ALA   F 2  271 ? 0.507   63.893  35.113  1.00 36.59  ? 273 ALA   B C     1 
ATOM   16097 O  O     . ALA   F 2  271 ? 1.265   64.820  35.431  1.00 31.36  ? 273 ALA   B O     1 
ATOM   16098 C  CB    . ALA   F 2  271 ? 0.373   62.108  36.838  1.00 24.58  ? 273 ALA   B CB    1 
ATOM   16099 N  N     . PRO   F 2  272 ? -0.640  64.108  34.464  1.00 39.94  ? 274 PRO   B N     1 
ATOM   16100 C  CA    . PRO   F 2  272 ? -1.585  63.088  33.969  1.00 30.66  ? 274 PRO   B CA    1 
ATOM   16101 C  C     . PRO   F 2  272 ? -1.082  62.365  32.733  1.00 27.35  ? 274 PRO   B C     1 
ATOM   16102 O  O     . PRO   F 2  272 ? -0.358  62.958  31.968  1.00 34.76  ? 274 PRO   B O     1 
ATOM   16103 C  CB    . PRO   F 2  272 ? -2.813  63.921  33.620  1.00 28.40  ? 274 PRO   B CB    1 
ATOM   16104 C  CG    . PRO   F 2  272 ? -2.212  65.219  33.155  1.00 31.15  ? 274 PRO   B CG    1 
ATOM   16105 C  CD    . PRO   F 2  272 ? -1.087  65.470  34.118  1.00 29.02  ? 274 PRO   B CD    1 
ATOM   16106 N  N     . LEU   F 2  273 ? -1.458  61.113  32.492  1.00 34.43  ? 275 LEU   B N     1 
ATOM   16107 C  CA    . LEU   F 2  273 ? -1.184  60.458  31.219  1.00 30.12  ? 275 LEU   B CA    1 
ATOM   16108 C  C     . LEU   F 2  273 ? -2.206  60.917  30.193  1.00 33.40  ? 275 LEU   B C     1 
ATOM   16109 O  O     . LEU   F 2  273 ? -3.344  61.235  30.540  1.00 40.40  ? 275 LEU   B O     1 
ATOM   16110 C  CB    . LEU   F 2  273 ? -1.232  58.936  31.376  1.00 27.65  ? 275 LEU   B CB    1 
ATOM   16111 C  CG    . LEU   F 2  273 ? -0.331  58.380  32.486  1.00 28.18  ? 275 LEU   B CG    1 
ATOM   16112 C  CD1   . LEU   F 2  273 ? -0.841  57.029  32.952  1.00 33.49  ? 275 LEU   B CD1   1 
ATOM   16113 C  CD2   . LEU   F 2  273 ? 1.122   58.262  32.041  1.00 20.52  ? 275 LEU   B CD2   1 
ATOM   16114 N  N     . THR   F 2  274 ? -1.789  60.979  28.924  1.00 40.41  ? 276 THR   B N     1 
ATOM   16115 C  CA    . THR   F 2  274 ? -2.638  61.571  27.894  1.00 35.29  ? 276 THR   B CA    1 
ATOM   16116 C  C     . THR   F 2  274 ? -2.254  61.077  26.508  1.00 45.89  ? 276 THR   B C     1 
ATOM   16117 O  O     . THR   F 2  274 ? -1.066  61.015  26.174  1.00 44.15  ? 276 THR   B O     1 
ATOM   16118 C  CB    . THR   F 2  274 ? -2.544  63.094  27.895  1.00 28.28  ? 276 THR   B CB    1 
ATOM   16119 O  OG1   . THR   F 2  274 ? -1.183  63.482  27.641  1.00 37.35  ? 276 THR   B OG1   1 
ATOM   16120 C  CG2   . THR   F 2  274 ? -3.024  63.639  29.232  1.00 30.20  ? 276 THR   B CG2   1 
ATOM   16121 N  N     . SER   F 2  275 ? -3.276  60.777  25.699  1.00 42.46  ? 277 SER   B N     1 
ATOM   16122 C  CA    . SER   F 2  275 ? -3.079  60.411  24.302  1.00 36.59  ? 277 SER   B CA    1 
ATOM   16123 C  C     . SER   F 2  275 ? -2.668  61.635  23.498  1.00 38.48  ? 277 SER   B C     1 
ATOM   16124 O  O     . SER   F 2  275 ? -3.186  62.730  23.705  1.00 42.91  ? 277 SER   B O     1 
ATOM   16125 C  CB    . SER   F 2  275 ? -4.370  59.822  23.720  1.00 24.29  ? 277 SER   B CB    1 
ATOM   16126 N  N     . ARG   F 2  276 ? -1.734  61.460  22.572  1.00 45.39  ? 278 ARG   B N     1 
ATOM   16127 C  CA    . ARG   F 2  276 ? -1.499  62.537  21.626  1.00 46.77  ? 278 ARG   B CA    1 
ATOM   16128 C  C     . ARG   F 2  276 ? -2.845  62.898  20.996  1.00 60.90  ? 278 ARG   B C     1 
ATOM   16129 O  O     . ARG   F 2  276 ? -3.628  62.016  20.620  1.00 46.45  ? 278 ARG   B O     1 
ATOM   16130 C  CB    . ARG   F 2  276 ? -0.452  62.127  20.572  1.00 47.84  ? 278 ARG   B CB    1 
ATOM   16131 C  CG    . ARG   F 2  276 ? -0.854  60.956  19.676  1.00 63.12  ? 278 ARG   B CG    1 
ATOM   16132 C  CD    . ARG   F 2  276 ? 0.242   60.462  18.710  1.00 42.84  ? 278 ARG   B CD    1 
ATOM   16133 N  NE    . ARG   F 2  276 ? 0.803   61.513  17.870  1.00 60.73  ? 278 ARG   B NE    1 
ATOM   16134 C  CZ    . ARG   F 2  276 ? 2.091   61.843  17.860  1.00 76.45  ? 278 ARG   B CZ    1 
ATOM   16135 N  NH1   . ARG   F 2  276 ? 2.963   61.240  18.653  1.00 73.78  ? 278 ARG   B NH1   1 
ATOM   16136 N  NH2   . ARG   F 2  276 ? 2.519   62.790  17.024  1.00 59.68  ? 278 ARG   B NH2   1 
ATOM   16137 N  N     . GLY   F 2  277 ? -3.158  64.197  20.983  1.00 64.59  ? 279 GLY   B N     1 
ATOM   16138 C  CA    . GLY   F 2  277 ? -4.442  64.670  20.508  1.00 52.88  ? 279 GLY   B CA    1 
ATOM   16139 C  C     . GLY   F 2  277 ? -5.562  64.700  21.534  1.00 63.80  ? 279 GLY   B C     1 
ATOM   16140 O  O     . GLY   F 2  277 ? -6.639  65.223  21.220  1.00 69.36  ? 279 GLY   B O     1 
ATOM   16141 N  N     . SER   F 2  278 ? -5.352  64.151  22.744  1.00 73.06  ? 280 SER   B N     1 
ATOM   16142 C  CA    . SER   F 2  278 ? -6.332  64.176  23.839  1.00 60.69  ? 280 SER   B CA    1 
ATOM   16143 C  C     . SER   F 2  278 ? -6.661  65.594  24.282  1.00 71.65  ? 280 SER   B C     1 
ATOM   16144 O  O     . SER   F 2  278 ? -5.824  66.251  24.906  1.00 89.87  ? 280 SER   B O     1 
ATOM   16145 C  CB    . SER   F 2  278 ? -5.816  63.399  25.060  1.00 45.15  ? 280 SER   B CB    1 
ATOM   16146 N  N     . GLN   F 2  279 ? -7.863  66.078  23.984  1.00 73.27  ? 281 GLN   B N     1 
ATOM   16147 C  CA    . GLN   F 2  279 ? -8.282  67.365  24.521  1.00 74.40  ? 281 GLN   B CA    1 
ATOM   16148 C  C     . GLN   F 2  279 ? -8.357  67.275  26.039  1.00 82.02  ? 281 GLN   B C     1 
ATOM   16149 O  O     . GLN   F 2  279 ? -8.968  66.352  26.586  1.00 88.27  ? 281 GLN   B O     1 
ATOM   16150 C  CB    . GLN   F 2  279 ? -9.636  67.771  23.939  1.00 78.11  ? 281 GLN   B CB    1 
ATOM   16151 N  N     . GLN   F 2  280 ? -7.715  68.221  26.725  1.00 81.76  ? 282 GLN   B N     1 
ATOM   16152 C  CA    . GLN   F 2  280 ? -7.640  68.201  28.184  1.00 93.42  ? 282 GLN   B CA    1 
ATOM   16153 C  C     . GLN   F 2  280 ? -8.620  69.225  28.752  1.00 87.69  ? 282 GLN   B C     1 
ATOM   16154 O  O     . GLN   F 2  280 ? -8.550  70.417  28.423  1.00 70.25  ? 282 GLN   B O     1 
ATOM   16155 C  CB    . GLN   F 2  280 ? -6.211  68.455  28.677  1.00 89.07  ? 282 GLN   B CB    1 
ATOM   16156 C  CG    . GLN   F 2  280 ? -5.453  67.174  29.092  1.00 79.31  ? 282 GLN   B CG    1 
ATOM   16157 C  CD    . GLN   F 2  280 ? -6.202  66.344  30.147  1.00 93.47  ? 282 GLN   B CD    1 
ATOM   16158 O  OE1   . GLN   F 2  280 ? -7.377  66.008  29.971  1.00 101.69 ? 282 GLN   B OE1   1 
ATOM   16159 N  NE2   . GLN   F 2  280 ? -5.521  66.017  31.248  1.00 74.94  ? 282 GLN   B NE2   1 
ATOM   16160 N  N     . TYR   F 2  281 ? -9.529  68.750  29.608  1.00 82.20  ? 283 TYR   B N     1 
ATOM   16161 C  CA    . TYR   F 2  281 ? -10.703 69.511  30.018  1.00 77.14  ? 283 TYR   B CA    1 
ATOM   16162 C  C     . TYR   F 2  281 ? -10.584 70.102  31.410  1.00 67.00  ? 283 TYR   B C     1 
ATOM   16163 O  O     . TYR   F 2  281 ? -11.010 71.242  31.621  1.00 69.85  ? 283 TYR   B O     1 
ATOM   16164 C  CB    . TYR   F 2  281 ? -11.958 68.633  29.938  1.00 75.78  ? 283 TYR   B CB    1 
ATOM   16165 C  CG    . TYR   F 2  281 ? -12.333 68.328  28.513  1.00 76.19  ? 283 TYR   B CG    1 
ATOM   16166 C  CD1   . TYR   F 2  281 ? -12.161 69.288  27.526  1.00 74.84  ? 283 TYR   B CD1   1 
ATOM   16167 C  CD2   . TYR   F 2  281 ? -12.823 67.076  28.143  1.00 77.46  ? 283 TYR   B CD2   1 
ATOM   16168 C  CE1   . TYR   F 2  281 ? -12.477 69.026  26.215  1.00 85.29  ? 283 TYR   B CE1   1 
ATOM   16169 C  CE2   . TYR   F 2  281 ? -13.151 66.799  26.830  1.00 74.69  ? 283 TYR   B CE2   1 
ATOM   16170 C  CZ    . TYR   F 2  281 ? -12.973 67.783  25.865  1.00 90.82  ? 283 TYR   B CZ    1 
ATOM   16171 O  OH    . TYR   F 2  281 ? -13.286 67.547  24.541  1.00 94.18  ? 283 TYR   B OH    1 
ATOM   16172 N  N     . ARG   F 2  282 ? -10.019 69.373  32.367  1.00 64.09  ? 284 ARG   B N     1 
ATOM   16173 C  CA    . ARG   F 2  282 ? -9.780  69.962  33.675  1.00 71.81  ? 284 ARG   B CA    1 
ATOM   16174 C  C     . ARG   F 2  282 ? -8.424  69.538  34.209  1.00 63.30  ? 284 ARG   B C     1 
ATOM   16175 O  O     . ARG   F 2  282 ? -8.035  68.371  34.090  1.00 54.75  ? 284 ARG   B O     1 
ATOM   16176 C  CB    . ARG   F 2  282 ? -10.865 69.583  34.684  1.00 62.77  ? 284 ARG   B CB    1 
ATOM   16177 C  CG    . ARG   F 2  282 ? -10.729 68.201  35.244  1.00 51.56  ? 284 ARG   B CG    1 
ATOM   16178 C  CD    . ARG   F 2  282 ? -11.258 68.198  36.670  1.00 58.51  ? 284 ARG   B CD    1 
ATOM   16179 N  NE    . ARG   F 2  282 ? -10.925 66.967  37.377  1.00 65.53  ? 284 ARG   B NE    1 
ATOM   16180 C  CZ    . ARG   F 2  282 ? -9.827  66.782  38.101  1.00 55.90  ? 284 ARG   B CZ    1 
ATOM   16181 N  NH1   . ARG   F 2  282 ? -8.910  67.730  38.229  1.00 49.52  ? 284 ARG   B NH1   1 
ATOM   16182 N  NH2   . ARG   F 2  282 ? -9.644  65.617  38.712  1.00 60.12  ? 284 ARG   B NH2   1 
ATOM   16183 N  N     . ALA   F 2  283 ? -7.721  70.507  34.803  1.00 56.07  ? 285 ALA   B N     1 
ATOM   16184 C  CA    . ALA   F 2  283 ? -6.477  70.288  35.527  1.00 48.01  ? 285 ALA   B CA    1 
ATOM   16185 C  C     . ALA   F 2  283 ? -6.614  69.232  36.617  1.00 56.47  ? 285 ALA   B C     1 
ATOM   16186 O  O     . ALA   F 2  283 ? -7.722  68.914  37.062  1.00 53.44  ? 285 ALA   B O     1 
ATOM   16187 C  CB    . ALA   F 2  283 ? -5.999  71.596  36.157  1.00 53.43  ? 285 ALA   B CB    1 
ATOM   16188 N  N     . LEU   F 2  284 ? -5.492  68.682  37.061  1.00 53.28  ? 286 LEU   B N     1 
ATOM   16189 C  CA    . LEU   F 2  284 ? -5.492  67.883  38.272  1.00 44.94  ? 286 LEU   B CA    1 
ATOM   16190 C  C     . LEU   F 2  284 ? -5.302  68.785  39.488  1.00 41.81  ? 286 LEU   B C     1 
ATOM   16191 O  O     . LEU   F 2  284 ? -4.641  69.823  39.415  1.00 47.45  ? 286 LEU   B O     1 
ATOM   16192 C  CB    . LEU   F 2  284 ? -4.376  66.843  38.235  1.00 42.29  ? 286 LEU   B CB    1 
ATOM   16193 C  CG    . LEU   F 2  284 ? -4.264  65.832  37.110  1.00 45.17  ? 286 LEU   B CG    1 
ATOM   16194 C  CD1   . LEU   F 2  284 ? -4.013  64.474  37.759  1.00 38.45  ? 286 LEU   B CD1   1 
ATOM   16195 C  CD2   . LEU   F 2  284 ? -5.496  65.832  36.201  1.00 34.81  ? 286 LEU   B CD2   1 
ATOM   16196 N  N     . THR   F 2  285 ? -5.891  68.380  40.606  1.00 38.06  ? 287 THR   B N     1 
ATOM   16197 C  CA    . THR   F 2  285 ? -5.530  68.963  41.889  1.00 38.70  ? 287 THR   B CA    1 
ATOM   16198 C  C     . THR   F 2  285 ? -4.147  68.476  42.310  1.00 41.76  ? 287 THR   B C     1 
ATOM   16199 O  O     . THR   F 2  285 ? -3.667  67.414  41.874  1.00 33.78  ? 287 THR   B O     1 
ATOM   16200 C  CB    . THR   F 2  285 ? -6.553  68.598  42.972  1.00 47.77  ? 287 THR   B CB    1 
ATOM   16201 O  OG1   . THR   F 2  285 ? -6.350  67.243  43.422  1.00 44.18  ? 287 THR   B OG1   1 
ATOM   16202 C  CG2   . THR   F 2  285 ? -7.965  68.745  42.437  1.00 34.11  ? 287 THR   B CG2   1 
ATOM   16203 N  N     . VAL   F 2  286 ? -3.483  69.264  43.173  1.00 44.08  ? 288 VAL   B N     1 
ATOM   16204 C  CA    . VAL   F 2  286 ? -2.152  68.885  43.639  1.00 43.78  ? 288 VAL   B CA    1 
ATOM   16205 C  C     . VAL   F 2  286 ? -2.195  67.485  44.243  1.00 44.54  ? 288 VAL   B C     1 
ATOM   16206 O  O     . VAL   F 2  286 ? -1.269  66.701  43.998  1.00 41.60  ? 288 VAL   B O     1 
ATOM   16207 C  CB    . VAL   F 2  286 ? -1.590  69.952  44.585  1.00 36.29  ? 288 VAL   B CB    1 
ATOM   16208 C  CG1   . VAL   F 2  286 ? -0.469  69.377  45.452  1.00 38.11  ? 288 VAL   B CG1   1 
ATOM   16209 C  CG2   . VAL   F 2  286 ? -1.059  71.145  43.804  1.00 33.64  ? 288 VAL   B CG2   1 
ATOM   16210 N  N     . PRO   F 2  287 ? -3.232  67.106  44.995  1.00 46.25  ? 289 PRO   B N     1 
ATOM   16211 C  CA    . PRO   F 2  287 ? -3.289  65.731  45.511  1.00 36.26  ? 289 PRO   B CA    1 
ATOM   16212 C  C     . PRO   F 2  287 ? -3.505  64.697  44.430  1.00 44.64  ? 289 PRO   B C     1 
ATOM   16213 O  O     . PRO   F 2  287 ? -3.082  63.547  44.605  1.00 49.80  ? 289 PRO   B O     1 
ATOM   16214 C  CB    . PRO   F 2  287 ? -4.474  65.778  46.487  1.00 27.84  ? 289 PRO   B CB    1 
ATOM   16215 C  CG    . PRO   F 2  287 ? -4.639  67.225  46.810  1.00 31.88  ? 289 PRO   B CG    1 
ATOM   16216 C  CD    . PRO   F 2  287 ? -4.271  67.965  45.584  1.00 32.17  ? 289 PRO   B CD    1 
ATOM   16217 N  N     . GLU   F 2  288 ? -4.172  65.038  43.327  1.00 46.25  ? 290 GLU   B N     1 
ATOM   16218 C  CA    . GLU   F 2  288 ? -4.272  64.062  42.249  1.00 42.28  ? 290 GLU   B CA    1 
ATOM   16219 C  C     . GLU   F 2  288 ? -2.930  63.889  41.562  1.00 39.11  ? 290 GLU   B C     1 
ATOM   16220 O  O     . GLU   F 2  288 ? -2.526  62.766  41.242  1.00 38.65  ? 290 GLU   B O     1 
ATOM   16221 C  CB    . GLU   F 2  288 ? -5.326  64.477  41.237  1.00 42.70  ? 290 GLU   B CB    1 
ATOM   16222 C  CG    . GLU   F 2  288 ? -6.684  64.668  41.819  1.00 50.58  ? 290 GLU   B CG    1 
ATOM   16223 C  CD    . GLU   F 2  288 ? -7.679  65.136  40.777  1.00 53.47  ? 290 GLU   B CD    1 
ATOM   16224 O  OE1   . GLU   F 2  288 ? -7.551  66.291  40.311  1.00 41.21  ? 290 GLU   B OE1   1 
ATOM   16225 O  OE2   . GLU   F 2  288 ? -8.574  64.335  40.412  1.00 58.23  ? 290 GLU   B OE2   1 
ATOM   16226 N  N     . LEU   F 2  289 ? -2.236  64.999  41.309  1.00 44.21  ? 291 LEU   B N     1 
ATOM   16227 C  CA    . LEU   F 2  289 ? -0.874  64.914  40.800  1.00 40.77  ? 291 LEU   B CA    1 
ATOM   16228 C  C     . LEU   F 2  289 ? -0.068  63.898  41.584  1.00 39.55  ? 291 LEU   B C     1 
ATOM   16229 O  O     . LEU   F 2  289 ? 0.641   63.071  40.997  1.00 40.10  ? 291 LEU   B O     1 
ATOM   16230 C  CB    . LEU   F 2  289 ? -0.201  66.278  40.881  1.00 37.42  ? 291 LEU   B CB    1 
ATOM   16231 C  CG    . LEU   F 2  289 ? -0.529  67.091  39.664  1.00 30.53  ? 291 LEU   B CG    1 
ATOM   16232 C  CD1   . LEU   F 2  289 ? 0.522   68.168  39.480  1.00 31.35  ? 291 LEU   B CD1   1 
ATOM   16233 C  CD2   . LEU   F 2  289 ? -0.495  66.093  38.581  1.00 34.55  ? 291 LEU   B CD2   1 
ATOM   16234 N  N     . THR   F 2  290 ? -0.191  63.931  42.915  1.00 30.42  ? 292 THR   B N     1 
ATOM   16235 C  CA    . THR   F 2  290 ? 0.726   63.191  43.775  1.00 41.05  ? 292 THR   B CA    1 
ATOM   16236 C  C     . THR   F 2  290 ? 0.397   61.704  43.837  1.00 35.99  ? 292 THR   B C     1 
ATOM   16237 O  O     . THR   F 2  290 ? 1.245   60.864  43.520  1.00 40.25  ? 292 THR   B O     1 
ATOM   16238 C  CB    . THR   F 2  290 ? 0.745   63.785  45.180  1.00 37.68  ? 292 THR   B CB    1 
ATOM   16239 O  OG1   . THR   F 2  290 ? 1.246   65.126  45.118  1.00 37.82  ? 292 THR   B OG1   1 
ATOM   16240 C  CG2   . THR   F 2  290 ? 1.654   62.992  46.002  1.00 31.85  ? 292 THR   B CG2   1 
ATOM   16241 N  N     . GLN   F 2  291 ? -0.817  61.347  44.264  1.00 42.59  ? 293 GLN   B N     1 
ATOM   16242 C  CA    . GLN   F 2  291 ? -1.124  59.921  44.375  1.00 43.97  ? 293 GLN   B CA    1 
ATOM   16243 C  C     . GLN   F 2  291 ? -0.908  59.225  43.037  1.00 39.68  ? 293 GLN   B C     1 
ATOM   16244 O  O     . GLN   F 2  291 ? -0.420  58.085  42.993  1.00 28.33  ? 293 GLN   B O     1 
ATOM   16245 C  CB    . GLN   F 2  291 ? -2.556  59.703  44.893  1.00 38.54  ? 293 GLN   B CB    1 
ATOM   16246 C  CG    . GLN   F 2  291 ? -2.942  60.505  46.190  1.00 63.45  ? 293 GLN   B CG    1 
ATOM   16247 C  CD    . GLN   F 2  291 ? -1.978  60.331  47.411  1.00 65.02  ? 293 GLN   B CD    1 
ATOM   16248 O  OE1   . GLN   F 2  291 ? -1.766  59.221  47.913  1.00 61.64  ? 293 GLN   B OE1   1 
ATOM   16249 N  NE2   . GLN   F 2  291 ? -1.419  61.451  47.892  1.00 60.15  ? 293 GLN   B NE2   1 
ATOM   16250 N  N     . GLN   F 2  292 ? -1.196  59.936  41.946  1.00 32.72  ? 294 GLN   B N     1 
ATOM   16251 C  CA    . GLN   F 2  292 ? -1.139  59.363  40.609  1.00 30.00  ? 294 GLN   B CA    1 
ATOM   16252 C  C     . GLN   F 2  292 ? 0.292   59.101  40.186  1.00 39.60  ? 294 GLN   B C     1 
ATOM   16253 O  O     . GLN   F 2  292 ? 0.607   58.033  39.647  1.00 36.62  ? 294 GLN   B O     1 
ATOM   16254 C  CB    . GLN   F 2  292 ? -1.798  60.319  39.619  1.00 33.86  ? 294 GLN   B CB    1 
ATOM   16255 C  CG    . GLN   F 2  292 ? -2.959  59.766  38.829  1.00 34.01  ? 294 GLN   B CG    1 
ATOM   16256 C  CD    . GLN   F 2  292 ? -3.885  60.869  38.358  1.00 35.30  ? 294 GLN   B CD    1 
ATOM   16257 O  OE1   . GLN   F 2  292 ? -3.697  61.435  37.280  1.00 32.02  ? 294 GLN   B OE1   1 
ATOM   16258 N  NE2   . GLN   F 2  292 ? -4.880  61.200  39.181  1.00 38.01  ? 294 GLN   B NE2   1 
ATOM   16259 N  N     . MET   F 2  293 ? 1.173   60.081  40.398  1.00 38.54  ? 295 MET   B N     1 
ATOM   16260 C  CA    . MET   F 2  293 ? 2.532   59.963  39.890  1.00 36.88  ? 295 MET   B CA    1 
ATOM   16261 C  C     . MET   F 2  293 ? 3.351   58.928  40.646  1.00 37.54  ? 295 MET   B C     1 
ATOM   16262 O  O     . MET   F 2  293 ? 4.384   58.494  40.128  1.00 46.78  ? 295 MET   B O     1 
ATOM   16263 C  CB    . MET   F 2  293 ? 3.234   61.311  39.945  1.00 38.24  ? 295 MET   B CB    1 
ATOM   16264 C  CG    . MET   F 2  293 ? 3.893   61.569  41.271  1.00 37.12  ? 295 MET   B CG    1 
ATOM   16265 S  SD    . MET   F 2  293 ? 4.576   63.219  41.341  1.00 46.93  ? 295 MET   B SD    1 
ATOM   16266 C  CE    . MET   F 2  293 ? 5.536   63.090  42.850  1.00 47.05  ? 295 MET   B CE    1 
ATOM   16267 N  N     . PHE   F 2  294 ? 2.927   58.532  41.853  1.00 32.22  ? 296 PHE   B N     1 
ATOM   16268 C  CA    . PHE   F 2  294 ? 3.508   57.395  42.567  1.00 24.50  ? 296 PHE   B CA    1 
ATOM   16269 C  C     . PHE   F 2  294 ? 2.798   56.091  42.246  1.00 32.33  ? 296 PHE   B C     1 
ATOM   16270 O  O     . PHE   F 2  294 ? 3.236   55.030  42.707  1.00 31.98  ? 296 PHE   B O     1 
ATOM   16271 C  CB    . PHE   F 2  294 ? 3.452   57.611  44.084  1.00 26.46  ? 296 PHE   B CB    1 
ATOM   16272 C  CG    . PHE   F 2  294 ? 4.486   58.568  44.619  1.00 34.54  ? 296 PHE   B CG    1 
ATOM   16273 C  CD1   . PHE   F 2  294 ? 4.324   59.931  44.495  1.00 28.02  ? 296 PHE   B CD1   1 
ATOM   16274 C  CD2   . PHE   F 2  294 ? 5.605   58.093  45.289  1.00 36.70  ? 296 PHE   B CD2   1 
ATOM   16275 C  CE1   . PHE   F 2  294 ? 5.276   60.794  44.984  1.00 38.41  ? 296 PHE   B CE1   1 
ATOM   16276 C  CE2   . PHE   F 2  294 ? 6.563   58.962  45.793  1.00 34.85  ? 296 PHE   B CE2   1 
ATOM   16277 C  CZ    . PHE   F 2  294 ? 6.401   60.309  45.640  1.00 34.17  ? 296 PHE   B CZ    1 
ATOM   16278 N  N     . ASP   F 2  295 ? 1.688   56.170  41.516  1.00 26.97  ? 297 ASP   B N     1 
ATOM   16279 C  CA    . ASP   F 2  295 ? 0.910   55.003  41.127  1.00 37.28  ? 297 ASP   B CA    1 
ATOM   16280 C  C     . ASP   F 2  295 ? 1.723   54.135  40.174  1.00 39.06  ? 297 ASP   B C     1 
ATOM   16281 O  O     . ASP   F 2  295 ? 2.491   54.644  39.348  1.00 35.53  ? 297 ASP   B O     1 
ATOM   16282 C  CB    . ASP   F 2  295 ? -0.401  55.475  40.459  1.00 42.62  ? 297 ASP   B CB    1 
ATOM   16283 C  CG    . ASP   F 2  295 ? -1.423  54.350  40.215  1.00 40.81  ? 297 ASP   B CG    1 
ATOM   16284 O  OD1   . ASP   F 2  295 ? -1.071  53.152  40.155  1.00 47.63  ? 297 ASP   B OD1   1 
ATOM   16285 O  OD2   . ASP   F 2  295 ? -2.610  54.688  40.062  1.00 47.66  ? 297 ASP   B OD2   1 
ATOM   16286 N  N     . SER   F 2  296 ? 1.551   52.818  40.277  1.00 35.12  ? 298 SER   B N     1 
ATOM   16287 C  CA    . SER   F 2  296 ? 2.274   51.947  39.359  1.00 33.65  ? 298 SER   B CA    1 
ATOM   16288 C  C     . SER   F 2  296 ? 1.793   52.130  37.927  1.00 31.75  ? 298 SER   B C     1 
ATOM   16289 O  O     . SER   F 2  296 ? 2.600   52.086  36.997  1.00 38.60  ? 298 SER   B O     1 
ATOM   16290 C  CB    . SER   F 2  296 ? 2.125   50.496  39.765  1.00 28.32  ? 298 SER   B CB    1 
ATOM   16291 O  OG    . SER   F 2  296 ? 0.878   50.033  39.299  1.00 52.32  ? 298 SER   B OG    1 
ATOM   16292 N  N     . LYS   F 2  297 ? 0.487   52.337  37.725  1.00 36.51  ? 299 LYS   B N     1 
ATOM   16293 C  CA    . LYS   F 2  297 ? -0.055  52.552  36.381  1.00 36.54  ? 299 LYS   B CA    1 
ATOM   16294 C  C     . LYS   F 2  297 ? 0.572   53.741  35.654  1.00 30.21  ? 299 LYS   B C     1 
ATOM   16295 O  O     . LYS   F 2  297 ? 0.336   53.902  34.453  1.00 35.96  ? 299 LYS   B O     1 
ATOM   16296 C  CB    . LYS   F 2  297 ? -1.574  52.761  36.435  1.00 39.85  ? 299 LYS   B CB    1 
ATOM   16297 C  CG    . LYS   F 2  297 ? -2.387  51.559  36.912  1.00 42.59  ? 299 LYS   B CG    1 
ATOM   16298 C  CD    . LYS   F 2  297 ? -3.895  51.799  36.718  1.00 55.76  ? 299 LYS   B CD    1 
ATOM   16299 C  CE    . LYS   F 2  297 ? -4.529  52.683  37.804  1.00 55.58  ? 299 LYS   B CE    1 
ATOM   16300 N  NZ    . LYS   F 2  297 ? -4.821  51.927  39.085  1.00 50.00  ? 299 LYS   B NZ    1 
ATOM   16301 N  N     . ASN   F 2  298 ? 1.344   54.583  36.339  1.00 36.98  ? 300 ASN   B N     1 
ATOM   16302 C  CA    . ASN   F 2  298 ? 1.951   55.761  35.728  1.00 34.80  ? 300 ASN   B CA    1 
ATOM   16303 C  C     . ASN   F 2  298 ? 3.447   55.613  35.531  1.00 29.35  ? 300 ASN   B C     1 
ATOM   16304 O  O     . ASN   F 2  298 ? 4.084   56.559  35.060  1.00 32.81  ? 300 ASN   B O     1 
ATOM   16305 C  CB    . ASN   F 2  298 ? 1.697   57.021  36.577  1.00 35.85  ? 300 ASN   B CB    1 
ATOM   16306 C  CG    . ASN   F 2  298 ? 0.274   57.525  36.496  1.00 30.61  ? 300 ASN   B CG    1 
ATOM   16307 O  OD1   . ASN   F 2  298 ? -0.652  56.937  37.058  1.00 40.58  ? 300 ASN   B OD1   1 
ATOM   16308 N  ND2   . ASN   F 2  298 ? 0.101   58.646  35.840  1.00 34.18  ? 300 ASN   B ND2   1 
ATOM   16309 N  N     . MET   F 2  299 ? 4.022   54.476  35.914  1.00 29.65  ? 301 MET   B N     1 
ATOM   16310 C  CA    . MET   F 2  299 ? 5.452   54.228  35.750  1.00 33.00  ? 301 MET   B CA    1 
ATOM   16311 C  C     . MET   F 2  299 ? 5.797   53.894  34.296  1.00 31.23  ? 301 MET   B C     1 
ATOM   16312 O  O     . MET   F 2  299 ? 5.019   53.243  33.596  1.00 32.16  ? 301 MET   B O     1 
ATOM   16313 C  CB    . MET   F 2  299 ? 5.901   53.085  36.668  1.00 25.02  ? 301 MET   B CB    1 
ATOM   16314 C  CG    . MET   F 2  299 ? 5.599   53.308  38.135  1.00 25.87  ? 301 MET   B CG    1 
ATOM   16315 S  SD    . MET   F 2  299 ? 6.479   54.733  38.813  1.00 38.21  ? 301 MET   B SD    1 
ATOM   16316 C  CE    . MET   F 2  299 ? 5.714   54.865  40.435  1.00 34.84  ? 301 MET   B CE    1 
ATOM   16317 N  N     . MET   F 2  300 ? 6.974   54.350  33.851  1.00 27.08  ? 302 MET   B N     1 
ATOM   16318 C  CA    . MET   F 2  300 ? 7.498   54.103  32.513  1.00 24.83  ? 302 MET   B CA    1 
ATOM   16319 C  C     . MET   F 2  300 ? 8.436   52.899  32.451  1.00 28.92  ? 302 MET   B C     1 
ATOM   16320 O  O     . MET   F 2  300 ? 8.906   52.543  31.364  1.00 29.70  ? 302 MET   B O     1 
ATOM   16321 C  CB    . MET   F 2  300 ? 8.239   55.339  31.986  1.00 33.03  ? 302 MET   B CB    1 
ATOM   16322 C  CG    . MET   F 2  300 ? 7.479   56.637  32.085  1.00 31.61  ? 302 MET   B CG    1 
ATOM   16323 S  SD    . MET   F 2  300 ? 6.125   56.674  30.928  1.00 34.44  ? 302 MET   B SD    1 
ATOM   16324 C  CE    . MET   F 2  300 ? 5.178   58.035  31.612  1.00 35.77  ? 302 MET   B CE    1 
ATOM   16325 N  N     . ALA   F 2  301 ? 8.754   52.290  33.579  1.00 23.02  ? 303 ALA   B N     1 
ATOM   16326 C  CA    . ALA   F 2  301 ? 9.310   50.949  33.601  1.00 28.38  ? 303 ALA   B CA    1 
ATOM   16327 C  C     . ALA   F 2  301 ? 8.237   50.032  34.155  1.00 31.38  ? 303 ALA   B C     1 
ATOM   16328 O  O     . ALA   F 2  301 ? 7.548   50.407  35.106  1.00 32.29  ? 303 ALA   B O     1 
ATOM   16329 C  CB    . ALA   F 2  301 ? 10.576  50.872  34.469  1.00 33.89  ? 303 ALA   B CB    1 
ATOM   16330 N  N     . ALA   F 2  302 ? 8.084   48.834  33.573  1.00 25.81  ? 304 ALA   B N     1 
ATOM   16331 C  CA    . ALA   F 2  302 ? 7.033   47.921  34.035  1.00 25.73  ? 304 ALA   B CA    1 
ATOM   16332 C  C     . ALA   F 2  302 ? 7.516   47.150  35.261  1.00 31.52  ? 304 ALA   B C     1 
ATOM   16333 O  O     . ALA   F 2  302 ? 7.966   46.006  35.177  1.00 31.98  ? 304 ALA   B O     1 
ATOM   16334 C  CB    . ALA   F 2  302 ? 6.597   46.981  32.932  1.00 20.94  ? 304 ALA   B CB    1 
ATOM   16335 N  N     . CYS   F 2  303 ? 7.383   47.796  36.428  1.00 26.88  ? 305 CYS   B N     1 
ATOM   16336 C  CA    . CYS   F 2  303 ? 7.739   47.226  37.721  1.00 28.61  ? 305 CYS   B CA    1 
ATOM   16337 C  C     . CYS   F 2  303 ? 6.728   47.669  38.768  1.00 37.22  ? 305 CYS   B C     1 
ATOM   16338 O  O     . CYS   F 2  303 ? 6.117   48.737  38.654  1.00 41.56  ? 305 CYS   B O     1 
ATOM   16339 C  CB    . CYS   F 2  303 ? 9.144   47.663  38.153  1.00 39.89  ? 305 CYS   B CB    1 
ATOM   16340 S  SG    . CYS   F 2  303 ? 10.372  47.498  36.817  1.00 42.34  ? 305 CYS   B SG    1 
ATOM   16341 N  N     . ASP   F 2  304 ? 6.567   46.845  39.804  1.00 40.62  ? 306 ASP   B N     1 
ATOM   16342 C  CA    . ASP   F 2  304 ? 5.635   47.143  40.889  1.00 37.81  ? 306 ASP   B CA    1 
ATOM   16343 C  C     . ASP   F 2  304 ? 6.371   47.863  42.016  1.00 33.54  ? 306 ASP   B C     1 
ATOM   16344 O  O     . ASP   F 2  304 ? 7.204   47.238  42.695  1.00 32.07  ? 306 ASP   B O     1 
ATOM   16345 C  CB    . ASP   F 2  304 ? 5.003   45.858  41.411  1.00 39.00  ? 306 ASP   B CB    1 
ATOM   16346 C  CG    . ASP   F 2  304 ? 3.738   46.106  42.229  1.00 45.52  ? 306 ASP   B CG    1 
ATOM   16347 O  OD1   . ASP   F 2  304 ? 3.619   47.189  42.853  1.00 51.09  ? 306 ASP   B OD1   1 
ATOM   16348 O  OD2   . ASP   F 2  304 ? 2.860   45.210  42.236  1.00 41.11  ? 306 ASP   B OD2   1 
ATOM   16349 N  N     . PRO   F 2  305 ? 6.102   49.145  42.265  1.00 30.27  ? 307 PRO   B N     1 
ATOM   16350 C  CA    . PRO   F 2  305 ? 6.790   49.810  43.382  1.00 30.13  ? 307 PRO   B CA    1 
ATOM   16351 C  C     . PRO   F 2  305 ? 6.558   49.116  44.716  1.00 33.52  ? 307 PRO   B C     1 
ATOM   16352 O  O     . PRO   F 2  305 ? 7.509   48.918  45.480  1.00 30.85  ? 307 PRO   B O     1 
ATOM   16353 C  CB    . PRO   F 2  305 ? 6.209   51.232  43.348  1.00 37.08  ? 307 PRO   B CB    1 
ATOM   16354 C  CG    . PRO   F 2  305 ? 5.683   51.431  41.961  1.00 28.04  ? 307 PRO   B CG    1 
ATOM   16355 C  CD    . PRO   F 2  305 ? 5.221   50.062  41.523  1.00 39.76  ? 307 PRO   B CD    1 
ATOM   16356 N  N     . ARG   F 2  306 ? 5.329   48.694  45.006  1.00 37.40  ? 308 ARG   B N     1 
ATOM   16357 C  CA    . ARG   F 2  306 ? 5.060   47.989  46.257  1.00 35.03  ? 308 ARG   B CA    1 
ATOM   16358 C  C     . ARG   F 2  306 ? 5.780   46.646  46.346  1.00 36.18  ? 308 ARG   B C     1 
ATOM   16359 O  O     . ARG   F 2  306 ? 5.648   45.950  47.352  1.00 43.46  ? 308 ARG   B O     1 
ATOM   16360 C  CB    . ARG   F 2  306 ? 3.556   47.747  46.456  1.00 44.10  ? 308 ARG   B CB    1 
ATOM   16361 C  CG    . ARG   F 2  306 ? 2.728   48.931  46.964  1.00 45.38  ? 308 ARG   B CG    1 
ATOM   16362 C  CD    . ARG   F 2  306 ? 1.233   48.726  46.667  1.00 57.75  ? 308 ARG   B CD    1 
ATOM   16363 N  NE    . ARG   F 2  306 ? 0.645   47.597  47.388  1.00 77.93  ? 308 ARG   B NE    1 
ATOM   16364 C  CZ    . ARG   F 2  306 ? -0.517  47.022  47.084  1.00 92.97  ? 308 ARG   B CZ    1 
ATOM   16365 N  NH1   . ARG   F 2  306 ? -1.243  47.424  46.046  1.00 81.80  ? 308 ARG   B NH1   1 
ATOM   16366 N  NH2   . ARG   F 2  306 ? -0.960  46.012  47.835  1.00 69.75  ? 308 ARG   B NH2   1 
ATOM   16367 N  N     . HIS   F 2  307 ? 6.499   46.236  45.298  1.00 36.31  ? 309 HIS   B N     1 
ATOM   16368 C  CA    . HIS   F 2  307 ? 7.331   45.040  45.384  1.00 33.90  ? 309 HIS   B CA    1 
ATOM   16369 C  C     . HIS   F 2  307 ? 8.766   45.367  45.770  1.00 49.26  ? 309 HIS   B C     1 
ATOM   16370 O  O     . HIS   F 2  307 ? 9.594   44.451  45.857  1.00 45.37  ? 309 HIS   B O     1 
ATOM   16371 C  CB    . HIS   F 2  307 ? 7.333   44.266  44.064  1.00 42.33  ? 309 HIS   B CB    1 
ATOM   16372 C  CG    . HIS   F 2  307 ? 6.196   43.305  43.921  1.00 49.89  ? 309 HIS   B CG    1 
ATOM   16373 N  ND1   . HIS   F 2  307 ? 4.973   43.672  43.406  1.00 51.42  ? 309 HIS   B ND1   1 
ATOM   16374 C  CD2   . HIS   F 2  307 ? 6.095   41.991  44.229  1.00 52.92  ? 309 HIS   B CD2   1 
ATOM   16375 C  CE1   . HIS   F 2  307 ? 4.163   42.628  43.406  1.00 51.01  ? 309 HIS   B CE1   1 
ATOM   16376 N  NE2   . HIS   F 2  307 ? 4.822   41.595  43.898  1.00 62.77  ? 309 HIS   B NE2   1 
ATOM   16377 N  N     . GLY   F 2  308 ? 9.076   46.646  45.993  1.00 35.03  ? 310 GLY   B N     1 
ATOM   16378 C  CA    . GLY   F 2  308 ? 10.401  47.036  46.411  1.00 27.94  ? 310 GLY   B CA    1 
ATOM   16379 C  C     . GLY   F 2  308 ? 10.420  48.122  47.472  1.00 36.24  ? 310 GLY   B C     1 
ATOM   16380 O  O     . GLY   F 2  308 ? 9.447   48.335  48.202  1.00 31.39  ? 310 GLY   B O     1 
ATOM   16381 N  N     . ARG   F 2  309 ? 11.561  48.793  47.583  1.00 34.83  ? 311 ARG   B N     1 
ATOM   16382 C  CA    . ARG   F 2  309 ? 11.715  49.967  48.421  1.00 27.82  ? 311 ARG   B CA    1 
ATOM   16383 C  C     . ARG   F 2  309 ? 12.395  51.043  47.590  1.00 32.93  ? 311 ARG   B C     1 
ATOM   16384 O  O     . ARG   F 2  309 ? 13.234  50.751  46.731  1.00 29.63  ? 311 ARG   B O     1 
ATOM   16385 C  CB    . ARG   F 2  309 ? 12.519  49.653  49.693  1.00 33.32  ? 311 ARG   B CB    1 
ATOM   16386 C  CG    . ARG   F 2  309 ? 12.136  48.301  50.312  1.00 41.52  ? 311 ARG   B CG    1 
ATOM   16387 C  CD    . ARG   F 2  309 ? 11.684  48.434  51.748  1.00 34.19  ? 311 ARG   B CD    1 
ATOM   16388 N  NE    . ARG   F 2  309 ? 12.836  48.522  52.633  1.00 48.12  ? 311 ARG   B NE    1 
ATOM   16389 C  CZ    . ARG   F 2  309 ? 12.874  49.251  53.743  1.00 52.58  ? 311 ARG   B CZ    1 
ATOM   16390 N  NH1   . ARG   F 2  309 ? 11.829  49.971  54.140  1.00 42.44  ? 311 ARG   B NH1   1 
ATOM   16391 N  NH2   . ARG   F 2  309 ? 13.991  49.267  54.467  1.00 48.65  ? 311 ARG   B NH2   1 
ATOM   16392 N  N     . TYR   F 2  310 ? 11.974  52.280  47.811  1.00 31.09  ? 312 TYR   B N     1 
ATOM   16393 C  CA    . TYR   F 2  310 ? 12.591  53.427  47.184  1.00 25.11  ? 312 TYR   B CA    1 
ATOM   16394 C  C     . TYR   F 2  310 ? 13.886  53.797  47.909  1.00 33.81  ? 312 TYR   B C     1 
ATOM   16395 O  O     . TYR   F 2  310 ? 13.899  53.968  49.138  1.00 29.12  ? 312 TYR   B O     1 
ATOM   16396 C  CB    . TYR   F 2  310 ? 11.617  54.586  47.209  1.00 26.86  ? 312 TYR   B CB    1 
ATOM   16397 C  CG    . TYR   F 2  310 ? 10.500  54.470  46.221  1.00 33.77  ? 312 TYR   B CG    1 
ATOM   16398 C  CD1   . TYR   F 2  310 ? 10.759  54.446  44.857  1.00 29.88  ? 312 TYR   B CD1   1 
ATOM   16399 C  CD2   . TYR   F 2  310 ? 9.184   54.409  46.645  1.00 28.74  ? 312 TYR   B CD2   1 
ATOM   16400 C  CE1   . TYR   F 2  310 ? 9.733   54.338  43.940  1.00 29.19  ? 312 TYR   B CE1   1 
ATOM   16401 C  CE2   . TYR   F 2  310 ? 8.160   54.316  45.745  1.00 31.53  ? 312 TYR   B CE2   1 
ATOM   16402 C  CZ    . TYR   F 2  310 ? 8.431   54.287  44.384  1.00 35.52  ? 312 TYR   B CZ    1 
ATOM   16403 O  OH    . TYR   F 2  310 ? 7.387   54.196  43.473  1.00 41.75  ? 312 TYR   B OH    1 
ATOM   16404 N  N     . LEU   F 2  311 ? 14.979  53.895  47.144  1.00 25.39  ? 313 LEU   B N     1 
ATOM   16405 C  CA    . LEU   F 2  311 ? 16.259  54.351  47.683  1.00 27.40  ? 313 LEU   B CA    1 
ATOM   16406 C  C     . LEU   F 2  311 ? 16.335  55.878  47.717  1.00 29.37  ? 313 LEU   B C     1 
ATOM   16407 O  O     . LEU   F 2  311 ? 16.441  56.485  48.789  1.00 28.41  ? 313 LEU   B O     1 
ATOM   16408 C  CB    . LEU   F 2  311 ? 17.407  53.771  46.848  1.00 27.08  ? 313 LEU   B CB    1 
ATOM   16409 C  CG    . LEU   F 2  311 ? 17.545  52.254  46.865  1.00 31.85  ? 313 LEU   B CG    1 
ATOM   16410 C  CD1   . LEU   F 2  311 ? 18.789  51.846  46.102  1.00 34.02  ? 313 LEU   B CD1   1 
ATOM   16411 C  CD2   . LEU   F 2  311 ? 17.589  51.737  48.311  1.00 29.57  ? 313 LEU   B CD2   1 
ATOM   16412 N  N     . THR   F 2  312 ? 16.285  56.512  46.547  1.00 21.72  ? 314 THR   B N     1 
ATOM   16413 C  CA    . THR   F 2  312 ? 16.091  57.945  46.437  1.00 21.18  ? 314 THR   B CA    1 
ATOM   16414 C  C     . THR   F 2  312 ? 14.904  58.194  45.514  1.00 22.69  ? 314 THR   B C     1 
ATOM   16415 O  O     . THR   F 2  312 ? 14.468  57.285  44.802  1.00 29.10  ? 314 THR   B O     1 
ATOM   16416 C  CB    . THR   F 2  312 ? 17.359  58.626  45.903  1.00 32.66  ? 314 THR   B CB    1 
ATOM   16417 O  OG1   . THR   F 2  312 ? 17.645  58.132  44.587  1.00 36.75  ? 314 THR   B OG1   1 
ATOM   16418 C  CG2   . THR   F 2  312 ? 18.531  58.321  46.807  1.00 23.31  ? 314 THR   B CG2   1 
ATOM   16419 N  N     . VAL   F 2  313 ? 14.384  59.429  45.539  1.00 21.12  ? 315 VAL   B N     1 
ATOM   16420 C  CA    . VAL   F 2  313 ? 13.238  59.877  44.730  1.00 21.96  ? 315 VAL   B CA    1 
ATOM   16421 C  C     . VAL   F 2  313 ? 13.351  61.379  44.478  1.00 18.75  ? 315 VAL   B C     1 
ATOM   16422 O  O     . VAL   F 2  313 ? 13.600  62.156  45.403  1.00 26.09  ? 315 VAL   B O     1 
ATOM   16423 C  CB    . VAL   F 2  313 ? 11.868  59.594  45.404  1.00 20.75  ? 315 VAL   B CB    1 
ATOM   16424 C  CG1   . VAL   F 2  313 ? 10.810  60.476  44.772  1.00 17.39  ? 315 VAL   B CG1   1 
ATOM   16425 C  CG2   . VAL   F 2  313 ? 11.455  58.136  45.293  1.00 20.84  ? 315 VAL   B CG2   1 
ATOM   16426 N  N     . ALA   F 2  314 ? 13.105  61.792  43.231  1.00 30.36  ? 316 ALA   B N     1 
ATOM   16427 C  CA    . ALA   F 2  314 ? 12.976  63.200  42.830  1.00 28.86  ? 316 ALA   B CA    1 
ATOM   16428 C  C     . ALA   F 2  314 ? 11.581  63.457  42.272  1.00 28.30  ? 316 ALA   B C     1 
ATOM   16429 O  O     . ALA   F 2  314 ? 11.117  62.723  41.391  1.00 30.99  ? 316 ALA   B O     1 
ATOM   16430 C  CB    . ALA   F 2  314 ? 14.011  63.569  41.760  1.00 26.33  ? 316 ALA   B CB    1 
ATOM   16431 N  N     . ALA   F 2  315 ? 10.919  64.503  42.747  1.00 25.87  ? 317 ALA   B N     1 
ATOM   16432 C  CA    . ALA   F 2  315 ? 9.593   64.849  42.242  1.00 28.22  ? 317 ALA   B CA    1 
ATOM   16433 C  C     . ALA   F 2  315 ? 9.622   66.260  41.674  1.00 24.43  ? 317 ALA   B C     1 
ATOM   16434 O  O     . ALA   F 2  315 ? 10.220  67.162  42.262  1.00 27.21  ? 317 ALA   B O     1 
ATOM   16435 C  CB    . ALA   F 2  315 ? 8.503   64.718  43.332  1.00 22.73  ? 317 ALA   B CB    1 
ATOM   16436 N  N     . ILE   F 2  316 ? 9.000   66.440  40.509  1.00 32.17  ? 318 ILE   B N     1 
ATOM   16437 C  CA    . ILE   F 2  316 ? 8.973   67.730  39.821  1.00 27.87  ? 318 ILE   B CA    1 
ATOM   16438 C  C     . ILE   F 2  316 ? 7.520   68.067  39.515  1.00 30.15  ? 318 ILE   B C     1 
ATOM   16439 O  O     . ILE   F 2  316 ? 6.800   67.260  38.917  1.00 33.76  ? 318 ILE   B O     1 
ATOM   16440 C  CB    . ILE   F 2  316 ? 9.809   67.730  38.532  1.00 24.37  ? 318 ILE   B CB    1 
ATOM   16441 C  CG1   . ILE   F 2  316 ? 11.120  66.972  38.726  1.00 33.15  ? 318 ILE   B CG1   1 
ATOM   16442 C  CG2   . ILE   F 2  316 ? 10.133  69.150  38.111  1.00 28.37  ? 318 ILE   B CG2   1 
ATOM   16443 C  CD1   . ILE   F 2  316 ? 10.995  65.467  38.595  0.00 29.42  ? 318 ILE   B CD1   1 
ATOM   16444 N  N     . PHE   F 2  317 ? 7.073   69.227  39.969  1.00 30.11  ? 319 PHE   B N     1 
ATOM   16445 C  CA    . PHE   F 2  317 ? 5.734   69.709  39.690  1.00 26.89  ? 319 PHE   B CA    1 
ATOM   16446 C  C     . PHE   F 2  317 ? 5.852   70.886  38.742  1.00 36.04  ? 319 PHE   B C     1 
ATOM   16447 O  O     . PHE   F 2  317 ? 6.822   71.650  38.790  1.00 36.44  ? 319 PHE   B O     1 
ATOM   16448 C  CB    . PHE   F 2  317 ? 4.994   70.129  40.961  1.00 22.81  ? 319 PHE   B CB    1 
ATOM   16449 C  CG    . PHE   F 2  317 ? 4.703   68.997  41.897  1.00 24.21  ? 319 PHE   B CG    1 
ATOM   16450 C  CD1   . PHE   F 2  317 ? 5.701   68.467  42.704  1.00 24.73  ? 319 PHE   B CD1   1 
ATOM   16451 C  CD2   . PHE   F 2  317 ? 3.435   68.451  41.967  1.00 20.26  ? 319 PHE   B CD2   1 
ATOM   16452 C  CE1   . PHE   F 2  317 ? 5.419   67.408  43.565  1.00 35.60  ? 319 PHE   B CE1   1 
ATOM   16453 C  CE2   . PHE   F 2  317 ? 3.155   67.407  42.819  1.00 20.27  ? 319 PHE   B CE2   1 
ATOM   16454 C  CZ    . PHE   F 2  317 ? 4.137   66.883  43.615  1.00 26.71  ? 319 PHE   B CZ    1 
ATOM   16455 N  N     . ARG   F 2  318 ? 4.867   71.010  37.861  1.00 35.94  ? 320 ARG   B N     1 
ATOM   16456 C  CA    . ARG   F 2  318 ? 4.891   72.059  36.862  1.00 39.56  ? 320 ARG   B CA    1 
ATOM   16457 C  C     . ARG   F 2  318 ? 3.515   72.694  36.758  1.00 46.54  ? 320 ARG   B C     1 
ATOM   16458 O  O     . ARG   F 2  318 ? 2.490   71.994  36.782  1.00 39.91  ? 320 ARG   B O     1 
ATOM   16459 C  CB    . ARG   F 2  318 ? 5.368   71.490  35.526  1.00 47.83  ? 320 ARG   B CB    1 
ATOM   16460 C  CG    . ARG   F 2  318 ? 6.731   70.846  35.666  1.00 40.92  ? 320 ARG   B CG    1 
ATOM   16461 C  CD    . ARG   F 2  318 ? 7.263   70.451  34.344  1.00 43.19  ? 320 ARG   B CD    1 
ATOM   16462 N  NE    . ARG   F 2  318 ? 7.512   71.599  33.488  1.00 41.38  ? 320 ARG   B NE    1 
ATOM   16463 C  CZ    . ARG   F 2  318 ? 7.693   71.502  32.179  1.00 48.87  ? 320 ARG   B CZ    1 
ATOM   16464 N  NH1   . ARG   F 2  318 ? 7.611   70.334  31.558  1.00 50.93  ? 320 ARG   B NH1   1 
ATOM   16465 N  NH2   . ARG   F 2  318 ? 7.965   72.598  31.477  1.00 38.33  ? 320 ARG   B NH2   1 
ATOM   16466 N  N     . GLY   F 2  319 ? 3.512   74.018  36.652  1.00 39.09  ? 321 GLY   B N     1 
ATOM   16467 C  CA    . GLY   F 2  319 ? 2.310   74.823  36.622  1.00 39.05  ? 321 GLY   B CA    1 
ATOM   16468 C  C     . GLY   F 2  319 ? 2.158   75.675  37.874  1.00 47.48  ? 321 GLY   B C     1 
ATOM   16469 O  O     . GLY   F 2  319 ? 2.884   75.540  38.860  1.00 51.09  ? 321 GLY   B O     1 
ATOM   16470 N  N     . ARG   F 2  320 ? 1.177   76.573  37.810  1.00 57.49  ? 322 ARG   B N     1 
ATOM   16471 C  CA    . ARG   F 2  320 ? 0.846   77.457  38.924  1.00 45.17  ? 322 ARG   B CA    1 
ATOM   16472 C  C     . ARG   F 2  320 ? 0.121   76.665  40.008  1.00 43.29  ? 322 ARG   B C     1 
ATOM   16473 O  O     . ARG   F 2  320 ? -1.011  76.214  39.808  1.00 52.99  ? 322 ARG   B O     1 
ATOM   16474 C  CB    . ARG   F 2  320 ? -0.011  78.614  38.418  1.00 55.56  ? 322 ARG   B CB    1 
ATOM   16475 C  CG    . ARG   F 2  320 ? 0.014   79.851  39.306  1.00 87.98  ? 322 ARG   B CG    1 
ATOM   16476 C  CD    . ARG   F 2  320 ? 1.269   80.701  39.072  1.00 91.76  ? 322 ARG   B CD    1 
ATOM   16477 N  NE    . ARG   F 2  320 ? 1.181   81.451  37.825  1.00 87.61  ? 322 ARG   B NE    1 
ATOM   16478 C  CZ    . ARG   F 2  320 ? 1.577   80.993  36.646  1.00 87.66  ? 322 ARG   B CZ    1 
ATOM   16479 N  NH1   . ARG   F 2  320 ? 2.130   79.798  36.517  1.00 71.69  ? 322 ARG   B NH1   1 
ATOM   16480 N  NH2   . ARG   F 2  320 ? 1.410   81.754  35.567  1.00 111.38 ? 322 ARG   B NH2   1 
ATOM   16481 N  N     . MET   F 2  321 ? 0.767   76.473  41.153  1.00 34.97  ? 323 MET   B N     1 
ATOM   16482 C  CA    . MET   F 2  321 ? 0.161   75.711  42.230  1.00 21.86  ? 323 MET   B CA    1 
ATOM   16483 C  C     . MET   F 2  321 ? 0.808   76.148  43.537  1.00 35.64  ? 323 MET   B C     1 
ATOM   16484 O  O     . MET   F 2  321 ? 1.742   76.952  43.544  1.00 33.85  ? 323 MET   B O     1 
ATOM   16485 C  CB    . MET   F 2  321 ? 0.313   74.221  41.995  1.00 32.14  ? 323 MET   B CB    1 
ATOM   16486 C  CG    . MET   F 2  321 ? 1.752   73.744  42.083  1.00 37.76  ? 323 MET   B CG    1 
ATOM   16487 S  SD    . MET   F 2  321 ? 1.923   72.066  41.478  1.00 39.62  ? 323 MET   B SD    1 
ATOM   16488 C  CE    . MET   F 2  321 ? 2.340   72.460  39.791  1.00 34.07  ? 323 MET   B CE    1 
ATOM   16489 N  N     . SER   F 2  322 ? 0.291   75.624  44.654  1.00 28.75  ? 324 SER   B N     1 
ATOM   16490 C  CA    . SER   F 2  322 ? 0.699   76.093  45.973  1.00 27.09  ? 324 SER   B CA    1 
ATOM   16491 C  C     . SER   F 2  322 ? 1.813   75.207  46.529  1.00 37.97  ? 324 SER   B C     1 
ATOM   16492 O  O     . SER   F 2  322 ? 1.615   74.011  46.777  1.00 32.52  ? 324 SER   B O     1 
ATOM   16493 C  CB    . SER   F 2  322 ? -0.493  76.151  46.939  1.00 24.30  ? 324 SER   B CB    1 
ATOM   16494 O  OG    . SER   F 2  322 ? -0.443  75.159  47.968  1.00 32.02  ? 324 SER   B OG    1 
ATOM   16495 N  N     . MET   F 2  323 ? 2.988   75.806  46.711  1.00 40.46  ? 325 MET   B N     1 
ATOM   16496 C  CA    . MET   F 2  323 ? 4.067   75.188  47.468  1.00 39.15  ? 325 MET   B CA    1 
ATOM   16497 C  C     . MET   F 2  323 ? 3.567   74.492  48.720  1.00 40.25  ? 325 MET   B C     1 
ATOM   16498 O  O     . MET   F 2  323 ? 3.920   73.336  48.988  1.00 38.89  ? 325 MET   B O     1 
ATOM   16499 C  CB    . MET   F 2  323 ? 5.085   76.264  47.842  1.00 52.09  ? 325 MET   B CB    1 
ATOM   16500 C  CG    . MET   F 2  323 ? 5.641   77.006  46.648  1.00 61.97  ? 325 MET   B CG    1 
ATOM   16501 S  SD    . MET   F 2  323 ? 6.790   75.901  45.847  1.00 80.80  ? 325 MET   B SD    1 
ATOM   16502 C  CE    . MET   F 2  323 ? 7.636   75.252  47.297  1.00 48.74  ? 325 MET   B CE    1 
ATOM   16503 N  N     . LYS   F 2  324 ? 2.747   75.190  49.514  1.00 45.77  ? 326 LYS   B N     1 
ATOM   16504 C  CA    . LYS   F 2  324 ? 2.287   74.592  50.763  1.00 42.49  ? 326 LYS   B CA    1 
ATOM   16505 C  C     . LYS   F 2  324 ? 1.598   73.251  50.517  1.00 37.84  ? 326 LYS   B C     1 
ATOM   16506 O  O     . LYS   F 2  324 ? 1.858   72.272  51.226  1.00 42.29  ? 326 LYS   B O     1 
ATOM   16507 C  CB    . LYS   F 2  324 ? 1.353   75.542  51.512  1.00 41.48  ? 326 LYS   B CB    1 
ATOM   16508 C  CG    . LYS   F 2  324 ? 1.000   75.005  52.898  1.00 48.85  ? 326 LYS   B CG    1 
ATOM   16509 C  CD    . LYS   F 2  324 ? -0.212  75.668  53.489  1.00 59.02  ? 326 LYS   B CD    1 
ATOM   16510 C  CE    . LYS   F 2  324 ? -0.459  75.167  54.907  1.00 55.66  ? 326 LYS   B CE    1 
ATOM   16511 N  NZ    . LYS   F 2  324 ? -1.819  75.550  55.388  1.00 55.87  ? 326 LYS   B NZ    1 
ATOM   16512 N  N     . GLU   F 2  325 ? 0.737   73.176  49.499  1.00 36.14  ? 327 GLU   B N     1 
ATOM   16513 C  CA    . GLU   F 2  325 ? -0.024  71.953  49.275  1.00 35.83  ? 327 GLU   B CA    1 
ATOM   16514 C  C     . GLU   F 2  325 ? 0.854   70.840  48.684  1.00 37.29  ? 327 GLU   B C     1 
ATOM   16515 O  O     . GLU   F 2  325 ? 0.717   69.667  49.059  1.00 35.71  ? 327 GLU   B O     1 
ATOM   16516 C  CB    . GLU   F 2  325 ? -1.224  72.277  48.389  1.00 30.73  ? 327 GLU   B CB    1 
ATOM   16517 C  CG    . GLU   F 2  325 ? -2.314  71.231  48.404  1.00 34.21  ? 327 GLU   B CG    1 
ATOM   16518 C  CD    . GLU   F 2  325 ? -3.429  71.564  47.435  1.00 48.80  ? 327 GLU   B CD    1 
ATOM   16519 O  OE1   . GLU   F 2  325 ? -3.246  72.527  46.645  1.00 45.33  ? 327 GLU   B OE1   1 
ATOM   16520 O  OE2   . GLU   F 2  325 ? -4.484  70.879  47.476  1.00 50.93  ? 327 GLU   B OE2   1 
ATOM   16521 N  N     . VAL   F 2  326 ? 1.766   71.182  47.766  1.00 30.78  ? 328 VAL   B N     1 
ATOM   16522 C  CA    . VAL   F 2  326 ? 2.732   70.191  47.286  1.00 34.52  ? 328 VAL   B CA    1 
ATOM   16523 C  C     . VAL   F 2  326 ? 3.461   69.576  48.470  1.00 37.50  ? 328 VAL   B C     1 
ATOM   16524 O  O     . VAL   F 2  326 ? 3.487   68.348  48.649  1.00 29.22  ? 328 VAL   B O     1 
ATOM   16525 C  CB    . VAL   F 2  326 ? 3.741   70.817  46.303  1.00 39.29  ? 328 VAL   B CB    1 
ATOM   16526 C  CG1   . VAL   F 2  326 ? 4.766   69.757  45.857  1.00 24.31  ? 328 VAL   B CG1   1 
ATOM   16527 C  CG2   . VAL   F 2  326 ? 3.060   71.431  45.094  1.00 31.22  ? 328 VAL   B CG2   1 
ATOM   16528 N  N     . ASP   F 2  327 ? 4.068   70.441  49.295  1.00 34.74  ? 329 ASP   B N     1 
ATOM   16529 C  CA    . ASP   F 2  327 ? 4.831   69.979  50.450  1.00 34.78  ? 329 ASP   B CA    1 
ATOM   16530 C  C     . ASP   F 2  327 ? 3.970   69.144  51.387  1.00 33.49  ? 329 ASP   B C     1 
ATOM   16531 O  O     . ASP   F 2  327 ? 4.398   68.074  51.846  1.00 36.34  ? 329 ASP   B O     1 
ATOM   16532 C  CB    . ASP   F 2  327 ? 5.449   71.174  51.179  1.00 26.47  ? 329 ASP   B CB    1 
ATOM   16533 C  CG    . ASP   F 2  327 ? 6.556   71.865  50.352  1.00 43.11  ? 329 ASP   B CG    1 
ATOM   16534 O  OD1   . ASP   F 2  327 ? 7.067   71.273  49.357  1.00 35.62  ? 329 ASP   B OD1   1 
ATOM   16535 O  OD2   . ASP   F 2  327 ? 6.935   73.004  50.709  1.00 41.10  ? 329 ASP   B OD2   1 
ATOM   16536 N  N     . GLU   F 2  328 ? 2.739   69.588  51.659  1.00 32.45  ? 330 GLU   B N     1 
ATOM   16537 C  CA    . GLU   F 2  328 ? 1.850   68.765  52.475  1.00 36.20  ? 330 GLU   B CA    1 
ATOM   16538 C  C     . GLU   F 2  328 ? 1.572   67.424  51.814  1.00 36.10  ? 330 GLU   B C     1 
ATOM   16539 O  O     . GLU   F 2  328 ? 1.545   66.389  52.490  1.00 37.24  ? 330 GLU   B O     1 
ATOM   16540 C  CB    . GLU   F 2  328 ? 0.550   69.504  52.752  1.00 43.34  ? 330 GLU   B CB    1 
ATOM   16541 C  CG    . GLU   F 2  328 ? 0.789   70.821  53.425  1.00 49.65  ? 330 GLU   B CG    1 
ATOM   16542 C  CD    . GLU   F 2  328 ? -0.453  71.408  54.005  1.00 51.91  ? 330 GLU   B CD    1 
ATOM   16543 O  OE1   . GLU   F 2  328 ? -1.552  71.015  53.558  1.00 60.62  ? 330 GLU   B OE1   1 
ATOM   16544 O  OE2   . GLU   F 2  328 ? -0.322  72.258  54.911  1.00 59.36  ? 330 GLU   B OE2   1 
ATOM   16545 N  N     . GLN   F 2  329 ? 1.397   67.415  50.486  1.00 31.10  ? 331 GLN   B N     1 
ATOM   16546 C  CA    . GLN   F 2  329 ? 1.037   66.179  49.800  1.00 32.50  ? 331 GLN   B CA    1 
ATOM   16547 C  C     . GLN   F 2  329 ? 2.230   65.232  49.632  1.00 37.56  ? 331 GLN   B C     1 
ATOM   16548 O  O     . GLN   F 2  329 ? 2.081   64.011  49.778  1.00 30.32  ? 331 GLN   B O     1 
ATOM   16549 C  CB    . GLN   F 2  329 ? 0.396   66.522  48.462  1.00 37.20  ? 331 GLN   B CB    1 
ATOM   16550 C  CG    . GLN   F 2  329 ? -1.080  66.856  48.584  1.00 38.55  ? 331 GLN   B CG    1 
ATOM   16551 C  CD    . GLN   F 2  329 ? -1.872  65.681  49.135  1.00 42.77  ? 331 GLN   B CD    1 
ATOM   16552 O  OE1   . GLN   F 2  329 ? -1.497  64.517  48.949  1.00 53.70  ? 331 GLN   B OE1   1 
ATOM   16553 N  NE2   . GLN   F 2  329 ? -2.957  65.977  49.832  1.00 38.64  ? 331 GLN   B NE2   1 
ATOM   16554 N  N     . MET   F 2  330 ? 3.416   65.765  49.320  1.00 32.89  ? 332 MET   B N     1 
ATOM   16555 C  CA    . MET   F 2  330 ? 4.611   64.927  49.324  1.00 33.91  ? 332 MET   B CA    1 
ATOM   16556 C  C     . MET   F 2  330 ? 4.865   64.325  50.710  1.00 37.84  ? 332 MET   B C     1 
ATOM   16557 O  O     . MET   F 2  330 ? 5.313   63.171  50.826  1.00 27.68  ? 332 MET   B O     1 
ATOM   16558 C  CB    . MET   F 2  330 ? 5.825   65.731  48.836  1.00 18.89  ? 332 MET   B CB    1 
ATOM   16559 C  CG    . MET   F 2  330 ? 5.764   66.123  47.353  1.00 27.48  ? 332 MET   B CG    1 
ATOM   16560 S  SD    . MET   F 2  330 ? 5.435   64.744  46.210  1.00 36.75  ? 332 MET   B SD    1 
ATOM   16561 C  CE    . MET   F 2  330 ? 6.700   63.609  46.776  1.00 29.52  ? 332 MET   B CE    1 
ATOM   16562 N  N     . LEU   F 2  331 ? 4.573   65.084  51.779  1.00 32.27  ? 333 LEU   B N     1 
ATOM   16563 C  CA    . LEU   F 2  331 ? 4.812   64.562  53.121  1.00 25.28  ? 333 LEU   B CA    1 
ATOM   16564 C  C     . LEU   F 2  331 ? 3.826   63.453  53.464  1.00 33.47  ? 333 LEU   B C     1 
ATOM   16565 O  O     . LEU   F 2  331 ? 4.213   62.422  54.030  1.00 36.81  ? 333 LEU   B O     1 
ATOM   16566 C  CB    . LEU   F 2  331 ? 4.754   65.698  54.138  1.00 30.68  ? 333 LEU   B CB    1 
ATOM   16567 C  CG    . LEU   F 2  331 ? 6.035   66.536  54.180  1.00 33.36  ? 333 LEU   B CG    1 
ATOM   16568 C  CD1   . LEU   F 2  331 ? 5.914   67.689  55.152  1.00 26.39  ? 333 LEU   B CD1   1 
ATOM   16569 C  CD2   . LEU   F 2  331 ? 7.203   65.637  54.554  1.00 26.76  ? 333 LEU   B CD2   1 
ATOM   16570 N  N     . ASN   F 2  332 ? 2.555   63.628  53.099  1.00 29.03  ? 334 ASN   B N     1 
ATOM   16571 C  CA    . ASN   F 2  332 ? 1.571   62.588  53.364  1.00 26.92  ? 334 ASN   B CA    1 
ATOM   16572 C  C     . ASN   F 2  332 ? 1.935   61.291  52.662  1.00 31.37  ? 334 ASN   B C     1 
ATOM   16573 O  O     . ASN   F 2  332 ? 1.811   60.208  53.244  1.00 40.47  ? 334 ASN   B O     1 
ATOM   16574 C  CB    . ASN   F 2  332 ? 0.172   63.049  52.941  1.00 30.66  ? 334 ASN   B CB    1 
ATOM   16575 C  CG    . ASN   F 2  332 ? -0.801  61.901  52.883  0.00 38.63  ? 334 ASN   B CG    1 
ATOM   16576 O  OD1   . ASN   F 2  332 ? -1.225  61.391  53.922  0.86 40.65  ? 334 ASN   B OD1   1 
ATOM   16577 N  ND2   . ASN   F 2  332 ? -1.134  61.456  51.668  1.00 45.40  ? 334 ASN   B ND2   1 
ATOM   16578 N  N     . VAL   F 2  333 ? 2.387   61.376  51.408  1.00 33.77  ? 335 VAL   B N     1 
ATOM   16579 C  CA    . VAL   F 2  333 ? 2.795   60.179  50.672  1.00 36.34  ? 335 VAL   B CA    1 
ATOM   16580 C  C     . VAL   F 2  333 ? 3.799   59.376  51.491  1.00 38.63  ? 335 VAL   B C     1 
ATOM   16581 O  O     . VAL   F 2  333 ? 3.627   58.171  51.728  1.00 35.88  ? 335 VAL   B O     1 
ATOM   16582 C  CB    . VAL   F 2  333 ? 3.375   60.570  49.299  1.00 41.17  ? 335 VAL   B CB    1 
ATOM   16583 C  CG1   . VAL   F 2  333 ? 3.583   59.360  48.451  1.00 34.60  ? 335 VAL   B CG1   1 
ATOM   16584 C  CG2   . VAL   F 2  333 ? 2.474   61.555  48.590  1.00 37.02  ? 335 VAL   B CG2   1 
ATOM   16585 N  N     . GLN   F 2  334 ? 4.859   60.047  51.953  1.00 31.73  ? 336 GLN   B N     1 
ATOM   16586 C  CA    . GLN   F 2  334 ? 5.913   59.347  52.679  1.00 41.75  ? 336 GLN   B CA    1 
ATOM   16587 C  C     . GLN   F 2  334 ? 5.426   58.883  54.038  1.00 42.71  ? 336 GLN   B C     1 
ATOM   16588 O  O     . GLN   F 2  334 ? 5.819   57.812  54.514  1.00 42.68  ? 336 GLN   B O     1 
ATOM   16589 C  CB    . GLN   F 2  334 ? 7.136   60.253  52.824  1.00 40.04  ? 336 GLN   B CB    1 
ATOM   16590 C  CG    . GLN   F 2  334 ? 7.340   61.129  51.611  1.00 30.52  ? 336 GLN   B CG    1 
ATOM   16591 C  CD    . GLN   F 2  334 ? 8.626   61.873  51.658  1.00 31.18  ? 336 GLN   B CD    1 
ATOM   16592 O  OE1   . GLN   F 2  334 ? 9.682   61.267  51.723  1.00 34.47  ? 336 GLN   B OE1   1 
ATOM   16593 N  NE2   . GLN   F 2  334 ? 8.558   63.207  51.616  1.00 38.20  ? 336 GLN   B NE2   1 
ATOM   16594 N  N     . ASN   F 2  335 ? 4.557   59.662  54.666  1.00 45.90  ? 337 ASN   B N     1 
ATOM   16595 C  CA    . ASN   F 2  335 ? 4.053   59.261  55.967  1.00 44.23  ? 337 ASN   B CA    1 
ATOM   16596 C  C     . ASN   F 2  335 ? 3.034   58.116  55.864  1.00 41.71  ? 337 ASN   B C     1 
ATOM   16597 O  O     . ASN   F 2  335 ? 3.031   57.222  56.716  1.00 40.36  ? 337 ASN   B O     1 
ATOM   16598 C  CB    . ASN   F 2  335 ? 3.502   60.504  56.664  1.00 43.86  ? 337 ASN   B CB    1 
ATOM   16599 C  CG    . ASN   F 2  335 ? 4.622   61.484  57.075  0.57 44.08  ? 337 ASN   B CG    1 
ATOM   16600 O  OD1   . ASN   F 2  335 ? 5.763   61.068  57.310  1.00 42.15  ? 337 ASN   B OD1   1 
ATOM   16601 N  ND2   . ASN   F 2  335 ? 4.298   62.778  57.161  1.00 44.03  ? 337 ASN   B ND2   1 
ATOM   16602 N  N     . LYS   F 2  336 ? 2.213   58.081  54.810  1.00 38.07  ? 338 LYS   B N     1 
ATOM   16603 C  CA    . LYS   F 2  336 ? 1.187   57.044  54.686  1.00 46.92  ? 338 LYS   B CA    1 
ATOM   16604 C  C     . LYS   F 2  336 ? 1.700   55.725  54.105  1.00 44.08  ? 338 LYS   B C     1 
ATOM   16605 O  O     . LYS   F 2  336 ? 1.031   54.699  54.250  1.00 38.91  ? 338 LYS   B O     1 
ATOM   16606 C  CB    . LYS   F 2  336 ? 0.023   57.541  53.816  1.00 43.02  ? 338 LYS   B CB    1 
ATOM   16607 C  CG    . LYS   F 2  336 ? -0.927  58.529  54.506  1.00 40.63  ? 338 LYS   B CG    1 
ATOM   16608 C  CD    . LYS   F 2  336 ? -1.585  57.918  55.751  1.00 47.70  ? 338 LYS   B CD    1 
ATOM   16609 C  CE    . LYS   F 2  336 ? -2.536  58.911  56.407  1.00 50.02  ? 338 LYS   B CE    1 
ATOM   16610 N  NZ    . LYS   F 2  336 ? -3.120  59.821  55.376  1.00 46.89  ? 338 LYS   B NZ    1 
ATOM   16611 N  N     . ASN   F 2  337 ? 2.844   55.725  53.431  1.00 46.33  ? 339 ASN   B N     1 
ATOM   16612 C  CA    . ASN   F 2  337 ? 3.393   54.516  52.823  1.00 40.31  ? 339 ASN   B CA    1 
ATOM   16613 C  C     . ASN   F 2  337 ? 4.884   54.423  53.124  1.00 45.84  ? 339 ASN   B C     1 
ATOM   16614 O  O     . ASN   F 2  337 ? 5.708   54.194  52.233  1.00 38.29  ? 339 ASN   B O     1 
ATOM   16615 C  CB    . ASN   F 2  337 ? 3.163   54.509  51.322  1.00 39.07  ? 339 ASN   B CB    1 
ATOM   16616 C  CG    . ASN   F 2  337 ? 1.775   54.912  50.959  1.00 48.92  ? 339 ASN   B CG    1 
ATOM   16617 O  OD1   . ASN   F 2  337 ? 1.469   56.113  50.884  1.00 33.71  ? 339 ASN   B OD1   1 
ATOM   16618 N  ND2   . ASN   F 2  337 ? 0.904   53.913  50.724  1.00 41.70  ? 339 ASN   B ND2   1 
ATOM   16619 N  N     . SER   F 2  338 ? 5.232   54.590  54.408  1.00 34.61  ? 340 SER   B N     1 
ATOM   16620 C  CA    . SER   F 2  338 ? 6.593   54.945  54.786  1.00 37.06  ? 340 SER   B CA    1 
ATOM   16621 C  C     . SER   F 2  338 ? 7.531   53.759  54.784  1.00 32.49  ? 340 SER   B C     1 
ATOM   16622 O  O     . SER   F 2  338 ? 8.749   53.959  54.789  1.00 33.09  ? 340 SER   B O     1 
ATOM   16623 C  CB    . SER   F 2  338 ? 6.611   55.594  56.168  1.00 41.01  ? 340 SER   B CB    1 
ATOM   16624 O  OG    . SER   F 2  338 ? 6.376   54.619  57.160  1.00 35.90  ? 340 SER   B OG    1 
ATOM   16625 N  N     . SER   F 2  339 ? 6.995   52.541  54.786  1.00 30.67  ? 341 SER   B N     1 
ATOM   16626 C  CA    . SER   F 2  339 ? 7.853   51.365  54.716  1.00 37.72  ? 341 SER   B CA    1 
ATOM   16627 C  C     . SER   F 2  339 ? 8.409   51.156  53.319  1.00 39.23  ? 341 SER   B C     1 
ATOM   16628 O  O     . SER   F 2  339 ? 9.318   50.338  53.139  1.00 45.22  ? 341 SER   B O     1 
ATOM   16629 C  CB    . SER   F 2  339 ? 7.094   50.114  55.153  1.00 31.06  ? 341 SER   B CB    1 
ATOM   16630 O  OG    . SER   F 2  339 ? 6.293   49.603  54.091  1.00 33.99  ? 341 SER   B OG    1 
ATOM   16631 N  N     . TYR   F 2  340 ? 7.885   51.872  52.341  1.00 27.92  ? 342 TYR   B N     1 
ATOM   16632 C  CA    . TYR   F 2  340 ? 8.384   51.771  50.982  1.00 39.34  ? 342 TYR   B CA    1 
ATOM   16633 C  C     . TYR   F 2  340 ? 9.606   52.653  50.708  1.00 39.70  ? 342 TYR   B C     1 
ATOM   16634 O  O     . TYR   F 2  340 ? 10.119  52.623  49.585  1.00 45.87  ? 342 TYR   B O     1 
ATOM   16635 C  CB    . TYR   F 2  340 ? 7.236   52.086  50.018  1.00 38.07  ? 342 TYR   B CB    1 
ATOM   16636 C  CG    . TYR   F 2  340 ? 6.253   50.944  50.002  1.00 42.00  ? 342 TYR   B CG    1 
ATOM   16637 C  CD1   . TYR   F 2  340 ? 6.615   49.720  49.435  1.00 40.16  ? 342 TYR   B CD1   1 
ATOM   16638 C  CD2   . TYR   F 2  340 ? 5.001   51.051  50.601  1.00 36.45  ? 342 TYR   B CD2   1 
ATOM   16639 C  CE1   . TYR   F 2  340 ? 5.760   48.647  49.430  1.00 36.75  ? 342 TYR   B CE1   1 
ATOM   16640 C  CE2   . TYR   F 2  340 ? 4.118   49.961  50.607  1.00 34.10  ? 342 TYR   B CE2   1 
ATOM   16641 C  CZ    . TYR   F 2  340 ? 4.511   48.765  50.012  1.00 40.06  ? 342 TYR   B CZ    1 
ATOM   16642 O  OH    . TYR   F 2  340 ? 3.678   47.673  49.981  1.00 34.49  ? 342 TYR   B OH    1 
ATOM   16643 N  N     . PHE   F 2  341 ? 10.093  53.414  51.690  1.00 31.04  ? 343 PHE   B N     1 
ATOM   16644 C  CA    . PHE   F 2  341 ? 11.300  54.224  51.550  1.00 33.91  ? 343 PHE   B CA    1 
ATOM   16645 C  C     . PHE   F 2  341 ? 12.308  53.745  52.582  1.00 36.57  ? 343 PHE   B C     1 
ATOM   16646 O  O     . PHE   F 2  341 ? 12.040  53.823  53.785  1.00 38.15  ? 343 PHE   B O     1 
ATOM   16647 C  CB    . PHE   F 2  341 ? 11.032  55.719  51.759  1.00 28.15  ? 343 PHE   B CB    1 
ATOM   16648 C  CG    . PHE   F 2  341 ? 9.897   56.272  50.947  1.00 29.98  ? 343 PHE   B CG    1 
ATOM   16649 C  CD1   . PHE   F 2  341 ? 8.581   56.156  51.394  1.00 36.01  ? 343 PHE   B CD1   1 
ATOM   16650 C  CD2   . PHE   F 2  341 ? 10.142  56.957  49.778  1.00 24.51  ? 343 PHE   B CD2   1 
ATOM   16651 C  CE1   . PHE   F 2  341 ? 7.535   56.692  50.676  1.00 33.91  ? 343 PHE   B CE1   1 
ATOM   16652 C  CE2   . PHE   F 2  341 ? 9.110   57.488  49.025  1.00 27.30  ? 343 PHE   B CE2   1 
ATOM   16653 C  CZ    . PHE   F 2  341 ? 7.797   57.361  49.476  1.00 41.04  ? 343 PHE   B CZ    1 
ATOM   16654 N  N     . VAL   F 2  342 ? 13.469  53.271  52.119  1.00 36.41  ? 344 VAL   B N     1 
ATOM   16655 C  CA    . VAL   F 2  342 ? 14.454  52.727  53.048  1.00 40.49  ? 344 VAL   B CA    1 
ATOM   16656 C  C     . VAL   F 2  342 ? 14.660  53.695  54.218  1.00 27.76  ? 344 VAL   B C     1 
ATOM   16657 O  O     . VAL   F 2  342 ? 14.889  54.893  54.030  1.00 25.61  ? 344 VAL   B O     1 
ATOM   16658 C  CB    . VAL   F 2  342 ? 15.774  52.389  52.314  1.00 30.59  ? 344 VAL   B CB    1 
ATOM   16659 C  CG1   . VAL   F 2  342 ? 15.554  51.276  51.336  1.00 25.56  ? 344 VAL   B CG1   1 
ATOM   16660 C  CG2   . VAL   F 2  342 ? 16.397  53.612  51.617  1.00 26.35  ? 344 VAL   B CG2   1 
ATOM   16661 N  N     . GLU   F 2  343 ? 14.551  53.168  55.439  1.00 28.91  ? 345 GLU   B N     1 
ATOM   16662 C  CA    . GLU   F 2  343 ? 14.753  53.980  56.631  1.00 39.63  ? 345 GLU   B CA    1 
ATOM   16663 C  C     . GLU   F 2  343 ? 16.197  54.432  56.804  1.00 39.25  ? 345 GLU   B C     1 
ATOM   16664 O  O     . GLU   F 2  343 ? 16.448  55.341  57.601  1.00 38.03  ? 345 GLU   B O     1 
ATOM   16665 C  CB    . GLU   F 2  343 ? 14.341  53.213  57.889  1.00 41.69  ? 345 GLU   B CB    1 
ATOM   16666 C  CG    . GLU   F 2  343 ? 15.266  52.069  58.211  1.00 32.12  ? 345 GLU   B CG    1 
ATOM   16667 C  CD    . GLU   F 2  343 ? 14.892  50.829  57.429  1.00 56.62  ? 345 GLU   B CD    1 
ATOM   16668 O  OE1   . GLU   F 2  343 ? 13.898  50.905  56.673  1.00 47.62  ? 345 GLU   B OE1   1 
ATOM   16669 O  OE2   . GLU   F 2  343 ? 15.576  49.785  57.561  1.00 61.92  ? 345 GLU   B OE2   1 
ATOM   16670 N  N     . TRP   F 2  344 ? 17.148  53.817  56.103  1.00 31.58  ? 346 TRP   B N     1 
ATOM   16671 C  CA    . TRP   F 2  344 ? 18.548  54.159  56.271  1.00 26.18  ? 346 TRP   B CA    1 
ATOM   16672 C  C     . TRP   F 2  344 ? 19.040  55.171  55.251  1.00 36.33  ? 346 TRP   B C     1 
ATOM   16673 O  O     . TRP   F 2  344 ? 20.257  55.365  55.128  1.00 38.44  ? 346 TRP   B O     1 
ATOM   16674 C  CB    . TRP   F 2  344 ? 19.428  52.905  56.242  1.00 30.39  ? 346 TRP   B CB    1 
ATOM   16675 C  CG    . TRP   F 2  344 ? 19.120  51.893  55.155  1.00 33.23  ? 346 TRP   B CG    1 
ATOM   16676 C  CD1   . TRP   F 2  344 ? 18.312  50.794  55.261  1.00 31.13  ? 346 TRP   B CD1   1 
ATOM   16677 C  CD2   . TRP   F 2  344 ? 19.632  51.884  53.815  1.00 33.60  ? 346 TRP   B CD2   1 
ATOM   16678 N  NE1   . TRP   F 2  344 ? 18.287  50.110  54.077  1.00 36.69  ? 346 TRP   B NE1   1 
ATOM   16679 C  CE2   . TRP   F 2  344 ? 19.091  50.753  53.172  1.00 29.08  ? 346 TRP   B CE2   1 
ATOM   16680 C  CE3   . TRP   F 2  344 ? 20.486  52.730  53.092  1.00 32.06  ? 346 TRP   B CE3   1 
ATOM   16681 C  CZ2   . TRP   F 2  344 ? 19.378  50.443  51.847  1.00 23.11  ? 346 TRP   B CZ2   1 
ATOM   16682 C  CZ3   . TRP   F 2  344 ? 20.776  52.414  51.776  1.00 27.06  ? 346 TRP   B CZ3   1 
ATOM   16683 C  CH2   . TRP   F 2  344 ? 20.220  51.283  51.168  1.00 26.14  ? 346 TRP   B CH2   1 
ATOM   16684 N  N     . ILE   F 2  345 ? 18.136  55.805  54.503  1.00 35.00  ? 347 ILE   B N     1 
ATOM   16685 C  CA    . ILE   F 2  345 ? 18.459  57.064  53.828  1.00 31.70  ? 347 ILE   B CA    1 
ATOM   16686 C  C     . ILE   F 2  345 ? 17.443  58.098  54.301  1.00 31.62  ? 347 ILE   B C     1 
ATOM   16687 O  O     . ILE   F 2  345 ? 16.402  58.293  53.657  1.00 29.75  ? 347 ILE   B O     1 
ATOM   16688 C  CB    . ILE   F 2  345 ? 18.466  56.941  52.294  1.00 23.35  ? 347 ILE   B CB    1 
ATOM   16689 C  CG1   . ILE   F 2  345 ? 19.387  55.809  51.849  1.00 25.66  ? 347 ILE   B CG1   1 
ATOM   16690 C  CG2   . ILE   F 2  345 ? 18.926  58.259  51.648  1.00 18.72  ? 347 ILE   B CG2   1 
ATOM   16691 C  CD1   . ILE   F 2  345 ? 19.688  55.815  50.346  1.00 23.27  ? 347 ILE   B CD1   1 
ATOM   16692 N  N     . PRO   F 2  346 ? 17.694  58.779  55.413  1.00 32.69  ? 348 PRO   B N     1 
ATOM   16693 C  CA    . PRO   F 2  346 ? 16.711  59.752  55.898  1.00 32.29  ? 348 PRO   B CA    1 
ATOM   16694 C  C     . PRO   F 2  346 ? 16.371  60.735  54.790  1.00 32.39  ? 348 PRO   B C     1 
ATOM   16695 O  O     . PRO   F 2  346 ? 17.218  61.079  53.964  1.00 25.35  ? 348 PRO   B O     1 
ATOM   16696 C  CB    . PRO   F 2  346 ? 17.417  60.431  57.079  1.00 25.43  ? 348 PRO   B CB    1 
ATOM   16697 C  CG    . PRO   F 2  346 ? 18.515  59.452  57.488  1.00 33.22  ? 348 PRO   B CG    1 
ATOM   16698 C  CD    . PRO   F 2  346 ? 18.937  58.783  56.207  1.00 33.38  ? 348 PRO   B CD    1 
ATOM   16699 N  N     . ASN   F 2  347 ? 15.098  61.135  54.745  1.00 39.83  ? 349 ASN   B N     1 
ATOM   16700 C  CA    . ASN   F 2  347 ? 14.647  62.234  53.895  1.00 34.87  ? 349 ASN   B CA    1 
ATOM   16701 C  C     . ASN   F 2  347 ? 15.100  62.061  52.454  1.00 28.16  ? 349 ASN   B C     1 
ATOM   16702 O  O     . ASN   F 2  347 ? 15.695  62.963  51.862  1.00 33.20  ? 349 ASN   B O     1 
ATOM   16703 C  CB    . ASN   F 2  347 ? 15.145  63.572  54.447  1.00 35.47  ? 349 ASN   B CB    1 
ATOM   16704 C  CG    . ASN   F 2  347 ? 14.793  63.767  55.913  1.00 35.59  ? 349 ASN   B CG    1 
ATOM   16705 O  OD1   . ASN   F 2  347 ? 15.651  64.112  56.723  1.00 33.89  ? 349 ASN   B OD1   1 
ATOM   16706 N  ND2   . ASN   F 2  347 ? 13.525  63.542  56.256  1.00 29.71  ? 349 ASN   B ND2   1 
ATOM   16707 N  N     . ASN   F 2  348 ? 14.803  60.893  51.880  1.00 27.23  ? 350 ASN   B N     1 
ATOM   16708 C  CA    . ASN   F 2  348 ? 15.343  60.504  50.577  1.00 26.62  ? 350 ASN   B CA    1 
ATOM   16709 C  C     . ASN   F 2  348 ? 14.494  60.975  49.392  1.00 24.17  ? 350 ASN   B C     1 
ATOM   16710 O  O     . ASN   F 2  348 ? 14.766  60.576  48.253  1.00 30.87  ? 350 ASN   B O     1 
ATOM   16711 C  CB    . ASN   F 2  348 ? 15.524  58.986  50.518  1.00 22.67  ? 350 ASN   B CB    1 
ATOM   16712 C  CG    . ASN   F 2  348 ? 14.235  58.257  50.693  1.00 28.65  ? 350 ASN   B CG    1 
ATOM   16713 O  OD1   . ASN   F 2  348 ? 13.216  58.852  51.051  1.00 33.79  ? 350 ASN   B OD1   1 
ATOM   16714 N  ND2   . ASN   F 2  348 ? 14.257  56.965  50.454  1.00 29.47  ? 350 ASN   B ND2   1 
ATOM   16715 N  N     . VAL   F 2  349 ? 13.517  61.844  49.624  1.00 25.46  ? 351 VAL   B N     1 
ATOM   16716 C  CA    . VAL   F 2  349 ? 12.587  62.325  48.602  1.00 29.82  ? 351 VAL   B CA    1 
ATOM   16717 C  C     . VAL   F 2  349 ? 12.757  63.834  48.483  1.00 28.87  ? 351 VAL   B C     1 
ATOM   16718 O  O     . VAL   F 2  349 ? 12.452  64.568  49.430  1.00 27.29  ? 351 VAL   B O     1 
ATOM   16719 C  CB    . VAL   F 2  349 ? 11.137  61.976  48.945  1.00 22.85  ? 351 VAL   B CB    1 
ATOM   16720 C  CG1   . VAL   F 2  349 ? 10.243  62.516  47.901  1.00 25.08  ? 351 VAL   B CG1   1 
ATOM   16721 C  CG2   . VAL   F 2  349 ? 10.961  60.463  49.087  1.00 19.70  ? 351 VAL   B CG2   1 
ATOM   16722 N  N     . LYS   F 2  350 ? 13.230  64.303  47.326  1.00 29.92  ? 352 LYS   B N     1 
ATOM   16723 C  CA    . LYS   F 2  350 ? 13.473  65.724  47.083  1.00 28.52  ? 352 LYS   B CA    1 
ATOM   16724 C  C     . LYS   F 2  350 ? 12.516  66.256  46.025  1.00 27.80  ? 352 LYS   B C     1 
ATOM   16725 O  O     . LYS   F 2  350 ? 12.233  65.594  45.024  1.00 36.48  ? 352 LYS   B O     1 
ATOM   16726 C  CB    . LYS   F 2  350 ? 14.919  65.996  46.654  1.00 25.81  ? 352 LYS   B CB    1 
ATOM   16727 C  CG    . LYS   F 2  350 ? 15.967  65.697  47.723  1.00 25.68  ? 352 LYS   B CG    1 
ATOM   16728 C  CD    . LYS   F 2  350 ? 15.532  66.190  49.085  1.00 27.78  ? 352 LYS   B CD    1 
ATOM   16729 C  CE    . LYS   F 2  350 ? 16.707  66.319  50.045  1.00 38.03  ? 352 LYS   B CE    1 
ATOM   16730 N  NZ    . LYS   F 2  350 ? 16.522  65.508  51.296  1.00 34.73  ? 352 LYS   B NZ    1 
ATOM   16731 N  N     . THR   F 2  351 ? 12.011  67.451  46.262  1.00 39.46  ? 353 THR   B N     1 
ATOM   16732 C  CA    . THR   F 2  351 ? 10.907  67.997  45.497  1.00 33.04  ? 353 THR   B CA    1 
ATOM   16733 C  C     . THR   F 2  351 ? 11.291  69.355  44.949  1.00 35.78  ? 353 THR   B C     1 
ATOM   16734 O  O     . THR   F 2  351 ? 11.858  70.190  45.660  1.00 46.17  ? 353 THR   B O     1 
ATOM   16735 C  CB    . THR   F 2  351 ? 9.651   68.131  46.361  1.00 30.07  ? 353 THR   B CB    1 
ATOM   16736 O  OG1   . THR   F 2  351 ? 9.167   66.826  46.694  1.00 31.16  ? 353 THR   B OG1   1 
ATOM   16737 C  CG2   . THR   F 2  351 ? 8.571   68.944  45.636  1.00 25.88  ? 353 THR   B CG2   1 
ATOM   16738 N  N     . ALA   F 2  352 ? 10.971  69.561  43.684  1.00 28.04  ? 354 ALA   B N     1 
ATOM   16739 C  CA    . ALA   F 2  352 ? 11.111  70.842  43.027  1.00 25.94  ? 354 ALA   B CA    1 
ATOM   16740 C  C     . ALA   F 2  352 ? 9.772   71.224  42.415  1.00 36.42  ? 354 ALA   B C     1 
ATOM   16741 O  O     . ALA   F 2  352 ? 8.968   70.366  42.033  1.00 29.49  ? 354 ALA   B O     1 
ATOM   16742 C  CB    . ALA   F 2  352 ? 12.186  70.793  41.936  1.00 36.60  ? 354 ALA   B CB    1 
ATOM   16743 N  N     . VAL   F 2  353 ? 9.537   72.522  42.318  1.00 32.98  ? 355 VAL   B N     1 
ATOM   16744 C  CA    . VAL   F 2  353 ? 8.359   73.029  41.644  1.00 34.81  ? 355 VAL   B CA    1 
ATOM   16745 C  C     . VAL   F 2  353 ? 8.810   74.044  40.616  1.00 33.22  ? 355 VAL   B C     1 
ATOM   16746 O  O     . VAL   F 2  353 ? 9.472   75.022  40.970  1.00 41.26  ? 355 VAL   B O     1 
ATOM   16747 C  CB    . VAL   F 2  353 ? 7.368   73.671  42.619  1.00 41.37  ? 355 VAL   B CB    1 
ATOM   16748 C  CG1   . VAL   F 2  353 ? 6.353   74.495  41.830  1.00 40.54  ? 355 VAL   B CG1   1 
ATOM   16749 C  CG2   . VAL   F 2  353 ? 6.696   72.598  43.464  1.00 27.03  ? 355 VAL   B CG2   1 
ATOM   16750 N  N     . CYS   F 2  354 ? 8.448   73.821  39.354  1.00 33.99  ? 356 CYS   B N     1 
ATOM   16751 C  CA    . CYS   F 2  354 ? 8.650   74.802  38.299  1.00 31.94  ? 356 CYS   B CA    1 
ATOM   16752 C  C     . CYS   F 2  354 ? 7.308   75.405  37.862  1.00 36.58  ? 356 CYS   B C     1 
ATOM   16753 O  O     . CYS   F 2  354 ? 6.301   74.704  37.742  1.00 36.23  ? 356 CYS   B O     1 
ATOM   16754 C  CB    . CYS   F 2  354 ? 9.385   74.167  37.125  1.00 24.49  ? 356 CYS   B CB    1 
ATOM   16755 S  SG    . CYS   F 2  354 ? 9.463   75.244  35.707  1.00 46.78  ? 356 CYS   B SG    1 
ATOM   16756 N  N     . ASP   F 2  355 ? 7.295   76.717  37.643  1.00 37.21  ? 357 ASP   B N     1 
ATOM   16757 C  CA    . ASP   F 2  355 ? 6.046   77.426  37.373  1.00 43.87  ? 357 ASP   B CA    1 
ATOM   16758 C  C     . ASP   F 2  355 ? 5.539   77.180  35.959  1.00 51.53  ? 357 ASP   B C     1 
ATOM   16759 O  O     . ASP   F 2  355 ? 4.323   77.093  35.736  1.00 46.00  ? 357 ASP   B O     1 
ATOM   16760 C  CB    . ASP   F 2  355 ? 6.231   78.932  37.580  1.00 46.99  ? 357 ASP   B CB    1 
ATOM   16761 C  CG    . ASP   F 2  355 ? 6.110   79.351  39.035  1.00 63.24  ? 357 ASP   B CG    1 
ATOM   16762 O  OD1   . ASP   F 2  355 ? 6.091   78.473  39.934  1.00 54.38  ? 357 ASP   B OD1   1 
ATOM   16763 O  OD2   . ASP   F 2  355 ? 6.029   80.574  39.274  1.00 64.15  ? 357 ASP   B OD2   1 
ATOM   16764 N  N     . ILE   F 2  356 ? 6.449   77.103  34.992  1.00 44.24  ? 358 ILE   B N     1 
ATOM   16765 C  CA    . ILE   F 2  356 ? 6.069   76.942  33.592  1.00 48.11  ? 358 ILE   B CA    1 
ATOM   16766 C  C     . ILE   F 2  356 ? 5.513   75.546  33.337  1.00 43.21  ? 358 ILE   B C     1 
ATOM   16767 O  O     . ILE   F 2  356 ? 6.254   74.560  33.447  1.00 44.41  ? 358 ILE   B O     1 
ATOM   16768 C  CB    . ILE   F 2  356 ? 7.261   77.221  32.678  1.00 42.36  ? 358 ILE   B CB    1 
ATOM   16769 C  CG1   . ILE   F 2  356 ? 7.982   78.465  33.175  1.00 48.53  ? 358 ILE   B CG1   1 
ATOM   16770 C  CG2   . ILE   F 2  356 ? 6.771   77.378  31.276  1.00 35.61  ? 358 ILE   B CG2   1 
ATOM   16771 C  CD1   . ILE   F 2  356 ? 9.174   78.867  32.324  1.00 62.90  ? 358 ILE   B CD1   1 
ATOM   16772 N  N     . PRO   F 2  357 ? 4.236   75.407  32.993  1.00 49.75  ? 359 PRO   B N     1 
ATOM   16773 C  CA    . PRO   F 2  357 ? 3.682   74.080  32.746  1.00 50.90  ? 359 PRO   B CA    1 
ATOM   16774 C  C     . PRO   F 2  357 ? 4.127   73.577  31.388  1.00 47.09  ? 359 PRO   B C     1 
ATOM   16775 O  O     . PRO   F 2  357 ? 4.521   74.374  30.523  1.00 45.13  ? 359 PRO   B O     1 
ATOM   16776 C  CB    . PRO   F 2  357 ? 2.165   74.322  32.781  1.00 43.73  ? 359 PRO   B CB    1 
ATOM   16777 C  CG    . PRO   F 2  357 ? 2.034   75.670  32.186  1.00 42.16  ? 359 PRO   B CG    1 
ATOM   16778 C  CD    . PRO   F 2  357 ? 3.250   76.459  32.686  1.00 46.86  ? 359 PRO   B CD    1 
ATOM   16779 N  N     . PRO   F 2  358 ? 4.089   72.268  31.166  1.00 50.31  ? 360 PRO   B N     1 
ATOM   16780 C  CA    . PRO   F 2  358 ? 4.426   71.734  29.843  1.00 53.62  ? 360 PRO   B CA    1 
ATOM   16781 C  C     . PRO   F 2  358 ? 3.358   72.056  28.806  1.00 55.12  ? 360 PRO   B C     1 
ATOM   16782 O  O     . PRO   F 2  358 ? 2.301   72.602  29.137  1.00 46.10  ? 360 PRO   B O     1 
ATOM   16783 C  CB    . PRO   F 2  358 ? 4.511   70.228  30.103  1.00 43.43  ? 360 PRO   B CB    1 
ATOM   16784 C  CG    . PRO   F 2  358 ? 3.497   70.012  31.156  1.00 30.52  ? 360 PRO   B CG    1 
ATOM   16785 C  CD    . PRO   F 2  358 ? 3.679   71.195  32.089  1.00 44.91  ? 360 PRO   B CD    1 
ATOM   16786 N  N     . ARG   F 2  359 ? 3.621   71.693  27.552  1.00 58.28  ? 369 ARG   B N     1 
ATOM   16787 C  CA    . ARG   F 2  359 ? 2.705   71.991  26.457  1.00 63.52  ? 369 ARG   B CA    1 
ATOM   16788 C  C     . ARG   F 2  359 ? 1.330   71.389  26.715  1.00 54.85  ? 369 ARG   B C     1 
ATOM   16789 O  O     . ARG   F 2  359 ? 1.205   70.188  26.958  1.00 58.25  ? 369 ARG   B O     1 
ATOM   16790 C  CB    . ARG   F 2  359 ? 3.292   71.454  25.150  1.00 75.38  ? 369 ARG   B CB    1 
ATOM   16791 C  CG    . ARG   F 2  359 ? 2.287   71.175  24.041  1.00 63.83  ? 369 ARG   B CG    1 
ATOM   16792 C  CD    . ARG   F 2  359 ? 1.574   72.431  23.580  1.00 69.94  ? 369 ARG   B CD    1 
ATOM   16793 N  NE    . ARG   F 2  359 ? 2.444   73.430  22.969  1.00 65.69  ? 369 ARG   B NE    1 
ATOM   16794 C  CZ    . ARG   F 2  359 ? 2.044   74.655  22.641  1.00 84.84  ? 369 ARG   B CZ    1 
ATOM   16795 N  NH1   . ARG   F 2  359 ? 0.792   75.049  22.835  1.00 86.84  ? 369 ARG   B NH1   1 
ATOM   16796 N  NH2   . ARG   F 2  359 ? 2.922   75.510  22.115  1.00 70.76  ? 369 ARG   B NH2   1 
ATOM   16797 N  N     . GLY   F 2  360 ? 0.297   72.222  26.677  1.00 39.55  ? 370 GLY   B N     1 
ATOM   16798 C  CA    . GLY   F 2  360 ? -1.058  71.719  26.725  1.00 48.94  ? 370 GLY   B CA    1 
ATOM   16799 C  C     . GLY   F 2  360 ? -1.590  71.324  28.088  1.00 52.13  ? 370 GLY   B C     1 
ATOM   16800 O  O     . GLY   F 2  360 ? -2.791  71.059  28.207  1.00 50.47  ? 370 GLY   B O     1 
ATOM   16801 N  N     . LEU   F 2  361 ? -0.760  71.268  29.121  1.00 53.42  ? 371 LEU   B N     1 
ATOM   16802 C  CA    . LEU   F 2  361 ? -1.235  71.018  30.473  1.00 39.45  ? 371 LEU   B CA    1 
ATOM   16803 C  C     . LEU   F 2  361 ? -1.175  72.297  31.298  1.00 42.78  ? 371 LEU   B C     1 
ATOM   16804 O  O     . LEU   F 2  361 ? -0.276  73.125  31.121  1.00 52.55  ? 371 LEU   B O     1 
ATOM   16805 C  CB    . LEU   F 2  361 ? -0.413  69.922  31.149  1.00 51.63  ? 371 LEU   B CB    1 
ATOM   16806 C  CG    . LEU   F 2  361 ? -0.658  68.478  30.702  1.00 43.92  ? 371 LEU   B CG    1 
ATOM   16807 C  CD1   . LEU   F 2  361 ? 0.639   67.692  30.726  1.00 33.14  ? 371 LEU   B CD1   1 
ATOM   16808 C  CD2   . LEU   F 2  361 ? -1.670  67.834  31.620  1.00 41.99  ? 371 LEU   B CD2   1 
ATOM   16809 N  N     . LYS   F 2  362 ? -2.166  72.476  32.170  1.00 46.21  ? 372 LYS   B N     1 
ATOM   16810 C  CA    . LYS   F 2  362 ? -2.082  73.497  33.203  1.00 43.57  ? 372 LYS   B CA    1 
ATOM   16811 C  C     . LYS   F 2  362 ? -1.287  73.012  34.399  1.00 46.88  ? 372 LYS   B C     1 
ATOM   16812 O  O     . LYS   F 2  362 ? -0.832  73.832  35.204  1.00 43.04  ? 372 LYS   B O     1 
ATOM   16813 C  CB    . LYS   F 2  362 ? -3.479  73.913  33.671  1.00 53.09  ? 372 LYS   B CB    1 
ATOM   16814 C  CG    . LYS   F 2  362 ? -4.196  74.904  32.771  1.00 61.12  ? 372 LYS   B CG    1 
ATOM   16815 C  CD    . LYS   F 2  362 ? -5.700  74.777  32.967  1.00 75.48  ? 372 LYS   B CD    1 
ATOM   16816 C  CE    . LYS   F 2  362 ? -6.086  73.298  33.067  1.00 74.82  ? 372 LYS   B CE    1 
ATOM   16817 N  NZ    . LYS   F 2  362 ? -7.549  73.046  32.908  1.00 83.41  ? 372 LYS   B NZ    1 
ATOM   16818 N  N     . MET   F 2  363 ? -1.115  71.696  34.529  1.00 45.39  ? 373 MET   B N     1 
ATOM   16819 C  CA    . MET   F 2  363 ? -0.436  71.125  35.678  1.00 40.37  ? 373 MET   B CA    1 
ATOM   16820 C  C     . MET   F 2  363 ? -0.040  69.675  35.447  1.00 41.82  ? 373 MET   B C     1 
ATOM   16821 O  O     . MET   F 2  363 ? -0.863  68.852  35.033  1.00 40.92  ? 373 MET   B O     1 
ATOM   16822 C  CB    . MET   F 2  363 ? -1.323  71.245  36.910  1.00 43.97  ? 373 MET   B CB    1 
ATOM   16823 C  CG    . MET   F 2  363 ? -1.044  72.500  37.706  1.00 48.24  ? 373 MET   B CG    1 
ATOM   16824 S  SD    . MET   F 2  363 ? -2.028  72.488  39.184  1.00 47.16  ? 373 MET   B SD    1 
ATOM   16825 C  CE    . MET   F 2  363 ? -3.638  72.894  38.485  1.00 54.92  ? 373 MET   B CE    1 
ATOM   16826 N  N     . SER   F 2  364 ? 1.223   69.358  35.730  1.00 44.10  ? 374 SER   B N     1 
ATOM   16827 C  CA    . SER   F 2  364 ? 1.746   68.011  35.588  1.00 33.77  ? 374 SER   B CA    1 
ATOM   16828 C  C     . SER   F 2  364 ? 2.710   67.712  36.731  1.00 36.22  ? 374 SER   B C     1 
ATOM   16829 O  O     . SER   F 2  364 ? 3.181   68.601  37.443  1.00 33.35  ? 374 SER   B O     1 
ATOM   16830 C  CB    . SER   F 2  364 ? 2.455   67.826  34.236  1.00 33.64  ? 374 SER   B CB    1 
ATOM   16831 O  OG    . SER   F 2  364 ? 3.607   68.644  34.155  1.00 38.62  ? 374 SER   B OG    1 
ATOM   16832 N  N     . ALA   F 2  365 ? 3.023   66.435  36.879  1.00 36.42  ? 375 ALA   B N     1 
ATOM   16833 C  CA    . ALA   F 2  365 ? 4.003   65.994  37.853  1.00 34.89  ? 375 ALA   B CA    1 
ATOM   16834 C  C     . ALA   F 2  365 ? 4.867   64.916  37.206  1.00 35.58  ? 375 ALA   B C     1 
ATOM   16835 O  O     . ALA   F 2  365 ? 4.348   64.023  36.526  1.00 34.17  ? 375 ALA   B O     1 
ATOM   16836 C  CB    . ALA   F 2  365 ? 3.308   65.475  39.117  1.00 28.50  ? 375 ALA   B CB    1 
ATOM   16837 N  N     . THR   F 2  366 ? 6.181   65.017  37.392  1.00 33.31  ? 376 THR   B N     1 
ATOM   16838 C  CA    . THR   F 2  366 ? 7.121   64.023  36.894  1.00 30.68  ? 376 THR   B CA    1 
ATOM   16839 C  C     . THR   F 2  366 ? 7.875   63.408  38.067  1.00 29.27  ? 376 THR   B C     1 
ATOM   16840 O  O     . THR   F 2  366 ? 8.359   64.121  38.954  1.00 25.85  ? 376 THR   B O     1 
ATOM   16841 C  CB    . THR   F 2  366 ? 8.102   64.616  35.868  1.00 31.46  ? 376 THR   B CB    1 
ATOM   16842 O  OG1   . THR   F 2  366 ? 7.399   64.979  34.662  1.00 27.34  ? 376 THR   B OG1   1 
ATOM   16843 C  CG2   . THR   F 2  366 ? 9.177   63.593  35.538  1.00 24.01  ? 376 THR   B CG2   1 
ATOM   16844 N  N     . PHE   F 2  367 ? 7.954   62.083  38.054  1.00 25.75  ? 377 PHE   B N     1 
ATOM   16845 C  CA    . PHE   F 2  367 ? 8.536   61.265  39.105  1.00 33.22  ? 377 PHE   B CA    1 
ATOM   16846 C  C     . PHE   F 2  367 ? 9.809   60.595  38.575  1.00 29.53  ? 377 PHE   B C     1 
ATOM   16847 O  O     . PHE   F 2  367 ? 9.867   60.183  37.416  1.00 23.48  ? 377 PHE   B O     1 
ATOM   16848 C  CB    . PHE   F 2  367 ? 7.477   60.241  39.564  1.00 33.93  ? 377 PHE   B CB    1 
ATOM   16849 C  CG    . PHE   F 2  367 ? 7.989   59.142  40.466  1.00 31.57  ? 377 PHE   B CG    1 
ATOM   16850 C  CD1   . PHE   F 2  367 ? 8.004   59.305  41.847  1.00 32.99  ? 377 PHE   B CD1   1 
ATOM   16851 C  CD2   . PHE   F 2  367 ? 8.388   57.917  39.937  1.00 31.99  ? 377 PHE   B CD2   1 
ATOM   16852 C  CE1   . PHE   F 2  367 ? 8.458   58.272  42.700  1.00 37.77  ? 377 PHE   B CE1   1 
ATOM   16853 C  CE2   . PHE   F 2  367 ? 8.855   56.882  40.779  1.00 41.01  ? 377 PHE   B CE2   1 
ATOM   16854 C  CZ    . PHE   F 2  367 ? 8.884   57.055  42.164  1.00 27.21  ? 377 PHE   B CZ    1 
ATOM   16855 N  N     . ILE   F 2  368 ? 10.845  60.526  39.402  1.00 26.00  ? 378 ILE   B N     1 
ATOM   16856 C  CA    . ILE   F 2  368 ? 12.074  59.809  39.070  1.00 23.92  ? 378 ILE   B CA    1 
ATOM   16857 C  C     . ILE   F 2  368 ? 12.427  59.005  40.301  1.00 26.97  ? 378 ILE   B C     1 
ATOM   16858 O  O     . ILE   F 2  368 ? 12.891  59.566  41.300  1.00 32.13  ? 378 ILE   B O     1 
ATOM   16859 C  CB    . ILE   F 2  368 ? 13.237  60.743  38.691  1.00 24.69  ? 378 ILE   B CB    1 
ATOM   16860 C  CG1   . ILE   F 2  368 ? 12.921  61.570  37.457  1.00 26.59  ? 378 ILE   B CG1   1 
ATOM   16861 C  CG2   . ILE   F 2  368 ? 14.454  59.956  38.402  1.00 20.85  ? 378 ILE   B CG2   1 
ATOM   16862 C  CD1   . ILE   F 2  368 ? 13.397  62.974  37.571  1.00 27.63  ? 378 ILE   B CD1   1 
ATOM   16863 N  N     . GLY   F 2  369 ? 12.215  57.706  40.251  1.00 23.26  ? 379 GLY   B N     1 
ATOM   16864 C  CA    . GLY   F 2  369 ? 12.461  56.849  41.399  1.00 26.99  ? 379 GLY   B CA    1 
ATOM   16865 C  C     . GLY   F 2  369 ? 13.633  55.916  41.151  1.00 26.13  ? 379 GLY   B C     1 
ATOM   16866 O  O     . GLY   F 2  369 ? 13.772  55.354  40.066  1.00 28.70  ? 379 GLY   B O     1 
ATOM   16867 N  N     . ASN   F 2  370 ? 14.488  55.784  42.146  1.00 27.42  ? 380 ASN   B N     1 
ATOM   16868 C  CA    . ASN   F 2  370 ? 15.528  54.772  42.143  1.00 16.89  ? 380 ASN   B CA    1 
ATOM   16869 C  C     . ASN   F 2  370 ? 15.021  53.728  43.126  1.00 23.91  ? 380 ASN   B C     1 
ATOM   16870 O  O     . ASN   F 2  370 ? 15.312  53.790  44.321  1.00 28.35  ? 380 ASN   B O     1 
ATOM   16871 C  CB    . ASN   F 2  370 ? 16.868  55.359  42.521  1.00 23.10  ? 380 ASN   B CB    1 
ATOM   16872 C  CG    . ASN   F 2  370 ? 17.998  54.339  42.504  1.00 27.13  ? 380 ASN   B CG    1 
ATOM   16873 O  OD1   . ASN   F 2  370 ? 17.793  53.123  42.616  1.00 25.00  ? 380 ASN   B OD1   1 
ATOM   16874 N  ND2   . ASN   F 2  370 ? 19.216  54.846  42.385  1.00 26.99  ? 380 ASN   B ND2   1 
ATOM   16875 N  N     . SER   F 2  371 ? 14.213  52.800  42.611  1.00 26.94  ? 381 SER   B N     1 
ATOM   16876 C  CA    . SER   F 2  371 ? 13.552  51.756  43.383  1.00 21.26  ? 381 SER   B CA    1 
ATOM   16877 C  C     . SER   F 2  371 ? 14.217  50.408  43.153  1.00 23.62  ? 381 SER   B C     1 
ATOM   16878 O  O     . SER   F 2  371 ? 14.527  50.057  42.015  1.00 25.95  ? 381 SER   B O     1 
ATOM   16879 C  CB    . SER   F 2  371 ? 12.084  51.636  42.987  1.00 22.89  ? 381 SER   B CB    1 
ATOM   16880 O  OG    . SER   F 2  371 ? 11.546  50.415  43.488  1.00 34.59  ? 381 SER   B OG    1 
ATOM   16881 N  N     . THR   F 2  372 ? 14.413  49.636  44.231  1.00 26.63  ? 382 THR   B N     1 
ATOM   16882 C  CA    . THR   F 2  372 ? 14.891  48.268  44.051  1.00 26.41  ? 382 THR   B CA    1 
ATOM   16883 C  C     . THR   F 2  372 ? 13.889  47.419  43.268  1.00 28.14  ? 382 THR   B C     1 
ATOM   16884 O  O     . THR   F 2  372 ? 14.254  46.365  42.743  1.00 31.19  ? 382 THR   B O     1 
ATOM   16885 C  CB    . THR   F 2  372 ? 15.227  47.607  45.406  1.00 35.39  ? 382 THR   B CB    1 
ATOM   16886 O  OG1   . THR   F 2  372 ? 14.034  47.375  46.170  1.00 31.54  ? 382 THR   B OG1   1 
ATOM   16887 C  CG2   . THR   F 2  372 ? 16.211  48.470  46.219  1.00 29.70  ? 382 THR   B CG2   1 
ATOM   16888 N  N     . ALA   F 2  373 ? 12.643  47.865  43.142  1.00 24.51  ? 383 ALA   B N     1 
ATOM   16889 C  CA    . ALA   F 2  373 ? 11.694  47.115  42.340  1.00 24.73  ? 383 ALA   B CA    1 
ATOM   16890 C  C     . ALA   F 2  373 ? 12.085  47.039  40.860  1.00 23.23  ? 383 ALA   B C     1 
ATOM   16891 O  O     . ALA   F 2  373 ? 11.531  46.219  40.128  1.00 26.15  ? 383 ALA   B O     1 
ATOM   16892 C  CB    . ALA   F 2  373 ? 10.304  47.731  42.512  1.00 27.83  ? 383 ALA   B CB    1 
ATOM   16893 N  N     . ILE   F 2  374 ? 13.026  47.851  40.382  1.00 26.57  ? 384 ILE   B N     1 
ATOM   16894 C  CA    . ILE   F 2  374 ? 13.428  47.715  38.985  1.00 24.14  ? 384 ILE   B CA    1 
ATOM   16895 C  C     . ILE   F 2  374 ? 14.183  46.426  38.710  1.00 27.73  ? 384 ILE   B C     1 
ATOM   16896 O  O     . ILE   F 2  374 ? 14.437  46.104  37.549  1.00 29.63  ? 384 ILE   B O     1 
ATOM   16897 C  CB    . ILE   F 2  374 ? 14.274  48.905  38.500  1.00 22.21  ? 384 ILE   B CB    1 
ATOM   16898 C  CG1   . ILE   F 2  374 ? 14.028  49.115  37.023  1.00 17.63  ? 384 ILE   B CG1   1 
ATOM   16899 C  CG2   . ILE   F 2  374 ? 15.748  48.674  38.751  1.00 26.31  ? 384 ILE   B CG2   1 
ATOM   16900 C  CD1   . ILE   F 2  374 ? 14.568  50.391  36.507  1.00 23.67  ? 384 ILE   B CD1   1 
ATOM   16901 N  N     . GLN   F 2  375 ? 14.550  45.670  39.740  1.00 29.20  ? 385 GLN   B N     1 
ATOM   16902 C  CA    . GLN   F 2  375 ? 15.081  44.347  39.470  1.00 24.13  ? 385 GLN   B CA    1 
ATOM   16903 C  C     . GLN   F 2  375 ? 14.087  43.514  38.679  1.00 31.57  ? 385 GLN   B C     1 
ATOM   16904 O  O     . GLN   F 2  375 ? 14.491  42.645  37.901  1.00 34.96  ? 385 GLN   B O     1 
ATOM   16905 C  CB    . GLN   F 2  375 ? 15.453  43.650  40.771  1.00 27.48  ? 385 GLN   B CB    1 
ATOM   16906 C  CG    . GLN   F 2  375 ? 14.301  42.966  41.469  1.00 30.42  ? 385 GLN   B CG    1 
ATOM   16907 C  CD    . GLN   F 2  375 ? 14.728  42.380  42.806  1.00 37.90  ? 385 GLN   B CD    1 
ATOM   16908 O  OE1   . GLN   F 2  375 ? 15.105  41.208  42.900  1.00 42.24  ? 385 GLN   B OE1   1 
ATOM   16909 N  NE2   . GLN   F 2  375 ? 14.680  43.203  43.852  1.00 36.45  ? 385 GLN   B NE2   1 
ATOM   16910 N  N     . GLU   F 2  376 ? 12.783  43.752  38.857  1.00 33.59  ? 386 GLU   B N     1 
ATOM   16911 C  CA    . GLU   F 2  376 ? 11.804  43.025  38.051  1.00 26.83  ? 386 GLU   B CA    1 
ATOM   16912 C  C     . GLU   F 2  376 ? 12.045  43.225  36.561  1.00 30.68  ? 386 GLU   B C     1 
ATOM   16913 O  O     . GLU   F 2  376 ? 11.798  42.306  35.768  1.00 34.98  ? 386 GLU   B O     1 
ATOM   16914 C  CB    . GLU   F 2  376 ? 10.387  43.450  38.421  1.00 22.48  ? 386 GLU   B CB    1 
ATOM   16915 C  CG    . GLU   F 2  376 ? 9.964   42.982  39.802  1.00 20.35  ? 386 GLU   B CG    1 
ATOM   16916 C  CD    . GLU   F 2  376 ? 8.582   43.452  40.172  1.00 33.14  ? 386 GLU   B CD    1 
ATOM   16917 O  OE1   . GLU   F 2  376 ? 8.082   44.384  39.492  1.00 39.02  ? 386 GLU   B OE1   1 
ATOM   16918 O  OE2   . GLU   F 2  376 ? 7.999   42.896  41.135  1.00 37.36  ? 386 GLU   B OE2   1 
ATOM   16919 N  N     . LEU   F 2  377 ? 12.525  44.411  36.160  1.00 25.84  ? 387 LEU   B N     1 
ATOM   16920 C  CA    . LEU   F 2  377 ? 12.820  44.660  34.751  1.00 21.63  ? 387 LEU   B CA    1 
ATOM   16921 C  C     . LEU   F 2  377 ? 13.982  43.791  34.283  1.00 28.87  ? 387 LEU   B C     1 
ATOM   16922 O  O     . LEU   F 2  377 ? 13.898  43.112  33.251  1.00 30.28  ? 387 LEU   B O     1 
ATOM   16923 C  CB    . LEU   F 2  377 ? 13.124  46.140  34.519  1.00 23.24  ? 387 LEU   B CB    1 
ATOM   16924 C  CG    . LEU   F 2  377 ? 12.907  46.663  33.087  1.00 25.99  ? 387 LEU   B CG    1 
ATOM   16925 C  CD1   . LEU   F 2  377 ? 13.121  48.150  33.033  1.00 31.56  ? 387 LEU   B CD1   1 
ATOM   16926 C  CD2   . LEU   F 2  377 ? 13.863  46.035  32.134  1.00 27.33  ? 387 LEU   B CD2   1 
ATOM   16927 N  N     . PHE   F 2  378 ? 15.060  43.764  35.058  1.00 27.64  ? 388 PHE   B N     1 
ATOM   16928 C  CA    . PHE   F 2  378 ? 16.226  43.004  34.655  1.00 22.29  ? 388 PHE   B CA    1 
ATOM   16929 C  C     . PHE   F 2  378 ? 15.965  41.513  34.708  1.00 24.78  ? 388 PHE   B C     1 
ATOM   16930 O  O     . PHE   F 2  378 ? 16.522  40.778  33.890  1.00 27.67  ? 388 PHE   B O     1 
ATOM   16931 C  CB    . PHE   F 2  378 ? 17.415  43.442  35.503  1.00 18.49  ? 388 PHE   B CB    1 
ATOM   16932 C  CG    . PHE   F 2  378 ? 17.730  44.910  35.329  1.00 23.53  ? 388 PHE   B CG    1 
ATOM   16933 C  CD1   . PHE   F 2  378 ? 18.041  45.416  34.064  1.00 25.46  ? 388 PHE   B CD1   1 
ATOM   16934 C  CD2   . PHE   F 2  378 ? 17.661  45.799  36.400  1.00 26.16  ? 388 PHE   B CD2   1 
ATOM   16935 C  CE1   . PHE   F 2  378 ? 18.315  46.776  33.878  1.00 27.56  ? 388 PHE   B CE1   1 
ATOM   16936 C  CE2   . PHE   F 2  378 ? 17.923  47.159  36.224  1.00 24.36  ? 388 PHE   B CE2   1 
ATOM   16937 C  CZ    . PHE   F 2  378 ? 18.252  47.652  34.958  1.00 22.12  ? 388 PHE   B CZ    1 
ATOM   16938 N  N     . LYS   F 2  379 ? 15.094  41.051  35.620  1.00 23.86  ? 389 LYS   B N     1 
ATOM   16939 C  CA    . LYS   F 2  379 ? 14.755  39.627  35.662  1.00 24.26  ? 389 LYS   B CA    1 
ATOM   16940 C  C     . LYS   F 2  379 ? 13.963  39.213  34.436  1.00 35.70  ? 389 LYS   B C     1 
ATOM   16941 O  O     . LYS   F 2  379 ? 14.091  38.074  33.974  1.00 35.06  ? 389 LYS   B O     1 
ATOM   16942 C  CB    . LYS   F 2  379 ? 13.930  39.259  36.896  1.00 25.63  ? 389 LYS   B CB    1 
ATOM   16943 C  CG    . LYS   F 2  379 ? 14.452  39.800  38.204  1.00 41.74  ? 389 LYS   B CG    1 
ATOM   16944 C  CD    . LYS   F 2  379 ? 14.154  38.866  39.355  1.00 24.97  ? 389 LYS   B CD    1 
ATOM   16945 C  CE    . LYS   F 2  379 ? 14.265  39.609  40.685  1.00 46.46  ? 389 LYS   B CE    1 
ATOM   16946 N  NZ    . LYS   F 2  379 ? 14.421  38.691  41.855  1.00 48.42  ? 389 LYS   B NZ    1 
ATOM   16947 N  N     . ARG   F 2  380 ? 13.118  40.110  33.919  1.00 29.98  ? 390 ARG   B N     1 
ATOM   16948 C  CA    . ARG   F 2  380 ? 12.319  39.768  32.754  1.00 25.70  ? 390 ARG   B CA    1 
ATOM   16949 C  C     . ARG   F 2  380 ? 13.211  39.540  31.553  1.00 31.69  ? 390 ARG   B C     1 
ATOM   16950 O  O     . ARG   F 2  380 ? 13.022  38.576  30.799  1.00 32.33  ? 390 ARG   B O     1 
ATOM   16951 C  CB    . ARG   F 2  380 ? 11.317  40.880  32.467  1.00 25.51  ? 390 ARG   B CB    1 
ATOM   16952 C  CG    . ARG   F 2  380 ? 10.335  40.566  31.374  1.00 16.08  ? 390 ARG   B CG    1 
ATOM   16953 C  CD    . ARG   F 2  380 ? 9.465   41.752  31.083  1.00 17.51  ? 390 ARG   B CD    1 
ATOM   16954 N  NE    . ARG   F 2  380 ? 10.143  42.710  30.224  1.00 27.38  ? 390 ARG   B NE    1 
ATOM   16955 C  CZ    . ARG   F 2  380 ? 10.027  44.030  30.307  1.00 32.22  ? 390 ARG   B CZ    1 
ATOM   16956 N  NH1   . ARG   F 2  380 ? 9.266   44.608  31.228  1.00 25.87  ? 390 ARG   B NH1   1 
ATOM   16957 N  NH2   . ARG   F 2  380 ? 10.706  44.791  29.455  1.00 25.40  ? 390 ARG   B NH2   1 
ATOM   16958 N  N     . ILE   F 2  381 ? 14.195  40.421  31.368  1.00 30.31  ? 391 ILE   B N     1 
ATOM   16959 C  CA    . ILE   F 2  381 ? 15.094  40.296  30.233  1.00 29.01  ? 391 ILE   B CA    1 
ATOM   16960 C  C     . ILE   F 2  381 ? 16.016  39.107  30.423  1.00 26.17  ? 391 ILE   B C     1 
ATOM   16961 O  O     . ILE   F 2  381 ? 16.263  38.345  29.483  1.00 26.43  ? 391 ILE   B O     1 
ATOM   16962 C  CB    . ILE   F 2  381 ? 15.872  41.607  30.029  1.00 31.26  ? 391 ILE   B CB    1 
ATOM   16963 C  CG1   . ILE   F 2  381 ? 14.919  42.700  29.528  1.00 24.37  ? 391 ILE   B CG1   1 
ATOM   16964 C  CG2   . ILE   F 2  381 ? 17.048  41.388  29.079  1.00 28.57  ? 391 ILE   B CG2   1 
ATOM   16965 C  CD1   . ILE   F 2  381 ? 15.424  44.080  29.817  1.00 20.08  ? 391 ILE   B CD1   1 
ATOM   16966 N  N     . SER   F 2  382 ? 16.517  38.916  31.651  1.00 31.72  ? 392 SER   B N     1 
ATOM   16967 C  CA    . SER   F 2  382 ? 17.407  37.791  31.942  1.00 31.05  ? 392 SER   B CA    1 
ATOM   16968 C  C     . SER   F 2  382 ? 16.713  36.453  31.697  1.00 34.68  ? 392 SER   B C     1 
ATOM   16969 O  O     . SER   F 2  382 ? 17.337  35.506  31.207  1.00 29.38  ? 392 SER   B O     1 
ATOM   16970 C  CB    . SER   F 2  382 ? 17.908  37.880  33.385  1.00 29.10  ? 392 SER   B CB    1 
ATOM   16971 O  OG    . SER   F 2  382 ? 18.716  36.765  33.752  1.00 28.85  ? 392 SER   B OG    1 
ATOM   16972 N  N     . GLU   F 2  383 ? 15.424  36.349  32.041  1.00 34.16  ? 393 GLU   B N     1 
ATOM   16973 C  CA    . GLU   F 2  383 ? 14.704  35.111  31.779  1.00 31.79  ? 393 GLU   B CA    1 
ATOM   16974 C  C     . GLU   F 2  383 ? 14.568  34.867  30.272  1.00 33.88  ? 393 GLU   B C     1 
ATOM   16975 O  O     . GLU   F 2  383 ? 14.753  33.735  29.804  1.00 31.92  ? 393 GLU   B O     1 
ATOM   16976 C  CB    . GLU   F 2  383 ? 13.339  35.123  32.490  1.00 36.00  ? 393 GLU   B CB    1 
ATOM   16977 C  CG    . GLU   F 2  383 ? 12.221  35.974  31.804  1.00 60.24  ? 393 GLU   B CG    1 
ATOM   16978 C  CD    . GLU   F 2  383 ? 10.800  35.776  32.406  1.00 75.41  ? 393 GLU   B CD    1 
ATOM   16979 O  OE1   . GLU   F 2  383 ? 10.261  34.642  32.354  1.00 83.85  ? 393 GLU   B OE1   1 
ATOM   16980 O  OE2   . GLU   F 2  383 ? 10.214  36.762  32.924  1.00 66.18  ? 393 GLU   B OE2   1 
ATOM   16981 N  N     . GLN   F 2  384 ? 14.300  35.916  29.490  1.00 22.79  ? 394 GLN   B N     1 
ATOM   16982 C  CA    . GLN   F 2  384 ? 14.248  35.736  28.041  1.00 29.62  ? 394 GLN   B CA    1 
ATOM   16983 C  C     . GLN   F 2  384 ? 15.627  35.355  27.485  1.00 36.86  ? 394 GLN   B C     1 
ATOM   16984 O  O     . GLN   F 2  384 ? 15.748  34.437  26.659  1.00 35.60  ? 394 GLN   B O     1 
ATOM   16985 C  CB    . GLN   F 2  384 ? 13.707  37.004  27.365  1.00 23.15  ? 394 GLN   B CB    1 
ATOM   16986 C  CG    . GLN   F 2  384 ? 12.331  37.470  27.854  1.00 27.19  ? 394 GLN   B CG    1 
ATOM   16987 C  CD    . GLN   F 2  384 ? 11.846  38.796  27.221  1.00 36.34  ? 394 GLN   B CD    1 
ATOM   16988 O  OE1   . GLN   F 2  384 ? 11.445  38.842  26.053  1.00 43.92  ? 394 GLN   B OE1   1 
ATOM   16989 N  NE2   . GLN   F 2  384 ? 11.875  39.866  27.997  1.00 29.24  ? 394 GLN   B NE2   1 
ATOM   16990 N  N     . PHE   F 2  385 ? 16.673  36.043  27.941  1.00 29.55  ? 395 PHE   B N     1 
ATOM   16991 C  CA    . PHE   F 2  385 ? 18.047  35.708  27.585  1.00 27.55  ? 395 PHE   B CA    1 
ATOM   16992 C  C     . PHE   F 2  385 ? 18.387  34.250  27.890  1.00 30.38  ? 395 PHE   B C     1 
ATOM   16993 O  O     . PHE   F 2  385 ? 18.959  33.541  27.058  1.00 32.91  ? 395 PHE   B O     1 
ATOM   16994 C  CB    . PHE   F 2  385 ? 18.988  36.642  28.349  1.00 29.40  ? 395 PHE   B CB    1 
ATOM   16995 C  CG    . PHE   F 2  385 ? 20.444  36.408  28.078  1.00 28.46  ? 395 PHE   B CG    1 
ATOM   16996 C  CD1   . PHE   F 2  385 ? 21.113  35.356  28.671  1.00 26.14  ? 395 PHE   B CD1   1 
ATOM   16997 C  CD2   . PHE   F 2  385 ? 21.152  37.271  27.251  1.00 26.86  ? 395 PHE   B CD2   1 
ATOM   16998 C  CE1   . PHE   F 2  385 ? 22.448  35.157  28.430  1.00 30.32  ? 395 PHE   B CE1   1 
ATOM   16999 C  CE2   . PHE   F 2  385 ? 22.494  37.069  27.000  1.00 23.67  ? 395 PHE   B CE2   1 
ATOM   17000 C  CZ    . PHE   F 2  385 ? 23.147  36.016  27.594  1.00 23.56  ? 395 PHE   B CZ    1 
ATOM   17001 N  N     . THR   F 2  386 ? 18.102  33.803  29.108  1.00 36.88  ? 396 THR   B N     1 
ATOM   17002 C  CA    . THR   F 2  386 ? 18.562  32.481  29.522  1.00 36.16  ? 396 THR   B CA    1 
ATOM   17003 C  C     . THR   F 2  386 ? 17.933  31.392  28.675  1.00 30.95  ? 396 THR   B C     1 
ATOM   17004 O  O     . THR   F 2  386 ? 18.617  30.446  28.273  1.00 34.36  ? 396 THR   B O     1 
ATOM   17005 C  CB    . THR   F 2  386 ? 18.261  32.262  31.006  1.00 36.77  ? 396 THR   B CB    1 
ATOM   17006 O  OG1   . THR   F 2  386 ? 18.946  33.279  31.757  1.00 52.30  ? 396 THR   B OG1   1 
ATOM   17007 C  CG2   . THR   F 2  386 ? 18.736  30.881  31.475  1.00 23.31  ? 396 THR   B CG2   1 
ATOM   17008 N  N     . ALA   F 2  387 ? 16.635  31.519  28.383  1.00 31.25  ? 397 ALA   B N     1 
ATOM   17009 C  CA    . ALA   F 2  387 ? 15.924  30.485  27.635  1.00 32.06  ? 397 ALA   B CA    1 
ATOM   17010 C  C     . ALA   F 2  387 ? 16.581  30.218  26.284  1.00 29.69  ? 397 ALA   B C     1 
ATOM   17011 O  O     . ALA   F 2  387 ? 16.629  29.077  25.823  1.00 28.27  ? 397 ALA   B O     1 
ATOM   17012 C  CB    . ALA   F 2  387 ? 14.464  30.893  27.447  1.00 31.13  ? 397 ALA   B CB    1 
ATOM   17013 N  N     . MET   F 2  388 ? 17.073  31.259  25.626  1.00 25.84  ? 398 MET   B N     1 
ATOM   17014 C  CA    . MET   F 2  388 ? 17.771  31.048  24.373  1.00 27.80  ? 398 MET   B CA    1 
ATOM   17015 C  C     . MET   F 2  388 ? 19.198  30.610  24.622  1.00 28.03  ? 398 MET   B C     1 
ATOM   17016 O  O     . MET   F 2  388 ? 19.683  29.673  23.973  1.00 26.88  ? 398 MET   B O     1 
ATOM   17017 C  CB    . MET   F 2  388 ? 17.766  32.322  23.523  1.00 23.78  ? 398 MET   B CB    1 
ATOM   17018 C  CG    . MET   F 2  388 ? 16.416  32.800  23.166  1.00 25.50  ? 398 MET   B CG    1 
ATOM   17019 S  SD    . MET   F 2  388 ? 16.504  34.186  22.049  1.00 32.14  ? 398 MET   B SD    1 
ATOM   17020 C  CE    . MET   F 2  388 ? 17.301  35.354  23.083  1.00 18.64  ? 398 MET   B CE    1 
ATOM   17021 N  N     . PHE   F 2  389 ? 19.886  31.289  25.552  1.00 18.41  ? 399 PHE   B N     1 
ATOM   17022 C  CA    . PHE   F 2  389 ? 21.329  31.111  25.650  1.00 21.16  ? 399 PHE   B CA    1 
ATOM   17023 C  C     . PHE   F 2  389 ? 21.704  29.738  26.195  1.00 24.87  ? 399 PHE   B C     1 
ATOM   17024 O  O     . PHE   F 2  389 ? 22.741  29.192  25.803  1.00 23.99  ? 399 PHE   B O     1 
ATOM   17025 C  CB    . PHE   F 2  389 ? 21.949  32.220  26.486  1.00 25.10  ? 399 PHE   B CB    1 
ATOM   17026 C  CG    . PHE   F 2  389 ? 23.449  32.205  26.495  1.00 23.08  ? 399 PHE   B CG    1 
ATOM   17027 C  CD1   . PHE   F 2  389 ? 24.166  32.503  25.346  1.00 24.34  ? 399 PHE   B CD1   1 
ATOM   17028 C  CD2   . PHE   F 2  389 ? 24.148  31.918  27.662  1.00 23.80  ? 399 PHE   B CD2   1 
ATOM   17029 C  CE1   . PHE   F 2  389 ? 25.557  32.490  25.340  1.00 22.49  ? 399 PHE   B CE1   1 
ATOM   17030 C  CE2   . PHE   F 2  389 ? 25.536  31.919  27.674  1.00 25.05  ? 399 PHE   B CE2   1 
ATOM   17031 C  CZ    . PHE   F 2  389 ? 26.243  32.194  26.507  1.00 26.00  ? 399 PHE   B CZ    1 
ATOM   17032 N  N     . ARG   F 2  390 ? 20.854  29.137  27.040  1.00 23.61  ? 400 ARG   B N     1 
ATOM   17033 C  CA    . ARG   F 2  390 ? 21.142  27.793  27.527  1.00 24.96  ? 400 ARG   B CA    1 
ATOM   17034 C  C     . ARG   F 2  390 ? 21.214  26.774  26.389  1.00 32.19  ? 400 ARG   B C     1 
ATOM   17035 O  O     . ARG   F 2  390 ? 21.832  25.719  26.555  1.00 31.73  ? 400 ARG   B O     1 
ATOM   17036 C  CB    . ARG   F 2  390 ? 20.113  27.364  28.594  1.00 32.39  ? 400 ARG   B CB    1 
ATOM   17037 C  CG    . ARG   F 2  390 ? 18.731  26.970  28.052  1.00 48.04  ? 400 ARG   B CG    1 
ATOM   17038 C  CD    . ARG   F 2  390 ? 17.702  26.625  29.164  1.00 59.28  ? 400 ARG   B CD    1 
ATOM   17039 N  NE    . ARG   F 2  390 ? 17.788  27.517  30.319  1.00 70.09  ? 400 ARG   B NE    1 
ATOM   17040 C  CZ    . ARG   F 2  390 ? 18.242  27.161  31.516  1.00 76.78  ? 400 ARG   B CZ    1 
ATOM   17041 N  NH1   . ARG   F 2  390 ? 18.595  25.909  31.779  1.00 80.38  ? 400 ARG   B NH1   1 
ATOM   17042 N  NH2   . ARG   F 2  390 ? 18.340  28.082  32.475  1.00 52.05  ? 400 ARG   B NH2   1 
ATOM   17043 N  N     . ARG   F 2  391 ? 20.619  27.062  25.229  1.00 30.71  ? 401 ARG   B N     1 
ATOM   17044 C  CA    . ARG   F 2  391 ? 20.861  26.264  24.033  1.00 25.45  ? 401 ARG   B CA    1 
ATOM   17045 C  C     . ARG   F 2  391 ? 21.678  27.025  22.997  1.00 26.42  ? 401 ARG   B C     1 
ATOM   17046 O  O     . ARG   F 2  391 ? 21.720  26.630  21.828  1.00 25.29  ? 401 ARG   B O     1 
ATOM   17047 C  CB    . ARG   F 2  391 ? 19.547  25.787  23.424  1.00 26.22  ? 401 ARG   B CB    1 
ATOM   17048 C  CG    . ARG   F 2  391 ? 18.591  25.212  24.425  1.00 29.19  ? 401 ARG   B CG    1 
ATOM   17049 C  CD    . ARG   F 2  391 ? 19.061  23.865  24.871  1.00 21.19  ? 401 ARG   B CD    1 
ATOM   17050 N  NE    . ARG   F 2  391 ? 18.922  22.897  23.796  1.00 21.20  ? 401 ARG   B NE    1 
ATOM   17051 C  CZ    . ARG   F 2  391 ? 17.865  22.115  23.626  1.00 28.29  ? 401 ARG   B CZ    1 
ATOM   17052 N  NH1   . ARG   F 2  391 ? 16.829  22.165  24.448  1.00 29.92  ? 401 ARG   B NH1   1 
ATOM   17053 N  NH2   . ARG   F 2  391 ? 17.845  21.260  22.606  1.00 23.14  ? 401 ARG   B NH2   1 
ATOM   17054 N  N     . LYS   F 2  392 ? 22.329  28.111  23.399  1.00 20.78  ? 402 LYS   B N     1 
ATOM   17055 C  CA    . LYS   F 2  392 ? 23.159  28.879  22.477  1.00 27.45  ? 402 LYS   B CA    1 
ATOM   17056 C  C     . LYS   F 2  392 ? 22.408  29.242  21.185  1.00 28.44  ? 402 LYS   B C     1 
ATOM   17057 O  O     . LYS   F 2  392 ? 23.011  29.462  20.134  1.00 27.60  ? 402 LYS   B O     1 
ATOM   17058 C  CB    . LYS   F 2  392 ? 24.449  28.120  22.188  1.00 20.39  ? 402 LYS   B CB    1 
ATOM   17059 C  CG    . LYS   F 2  392 ? 25.314  27.987  23.435  1.00 31.68  ? 402 LYS   B CG    1 
ATOM   17060 C  CD    . LYS   F 2  392 ? 26.276  26.804  23.347  1.00 38.85  ? 402 LYS   B CD    1 
ATOM   17061 C  CE    . LYS   F 2  392 ? 27.442  26.995  24.321  1.00 63.04  ? 402 LYS   B CE    1 
ATOM   17062 N  NZ    . LYS   F 2  392 ? 28.644  26.149  24.014  1.00 55.68  ? 402 LYS   B NZ    1 
ATOM   17063 N  N     . ALA   F 2  393 ? 21.089  29.372  21.261  1.00 19.34  ? 403 ALA   B N     1 
ATOM   17064 C  CA    . ALA   F 2  393 ? 20.311  29.658  20.071  1.00 24.53  ? 403 ALA   B CA    1 
ATOM   17065 C  C     . ALA   F 2  393 ? 20.563  31.073  19.569  1.00 25.12  ? 403 ALA   B C     1 
ATOM   17066 O  O     . ALA   F 2  393 ? 20.592  32.030  20.341  1.00 29.03  ? 403 ALA   B O     1 
ATOM   17067 C  CB    . ALA   F 2  393 ? 18.819  29.471  20.352  1.00 29.09  ? 403 ALA   B CB    1 
ATOM   17068 N  N     . PHE   F 2  394 ? 20.685  31.207  18.255  1.00 25.36  ? 404 PHE   B N     1 
ATOM   17069 C  CA    . PHE   F 2  394 ? 20.865  32.479  17.569  1.00 29.09  ? 404 PHE   B CA    1 
ATOM   17070 C  C     . PHE   F 2  394 ? 22.239  33.069  17.801  1.00 26.84  ? 404 PHE   B C     1 
ATOM   17071 O  O     . PHE   F 2  394 ? 22.500  34.199  17.357  1.00 26.87  ? 404 PHE   B O     1 
ATOM   17072 C  CB    . PHE   F 2  394 ? 19.774  33.483  17.966  1.00 24.28  ? 404 PHE   B CB    1 
ATOM   17073 C  CG    . PHE   F 2  394 ? 18.417  32.948  17.738  1.00 26.11  ? 404 PHE   B CG    1 
ATOM   17074 C  CD1   . PHE   F 2  394 ? 17.937  32.802  16.453  1.00 21.94  ? 404 PHE   B CD1   1 
ATOM   17075 C  CD2   . PHE   F 2  394 ? 17.644  32.502  18.797  1.00 31.47  ? 404 PHE   B CD2   1 
ATOM   17076 C  CE1   . PHE   F 2  394 ? 16.695  32.254  16.225  1.00 21.53  ? 404 PHE   B CE1   1 
ATOM   17077 C  CE2   . PHE   F 2  394 ? 16.392  31.956  18.572  1.00 28.76  ? 404 PHE   B CE2   1 
ATOM   17078 C  CZ    . PHE   F 2  394 ? 15.920  31.829  17.281  1.00 18.70  ? 404 PHE   B CZ    1 
ATOM   17079 N  N     . LEU   F 2  395 ? 23.136  32.331  18.455  1.00 19.76  ? 405 LEU   B N     1 
ATOM   17080 C  CA    . LEU   F 2  395 ? 24.450  32.889  18.746  1.00 20.37  ? 405 LEU   B CA    1 
ATOM   17081 C  C     . LEU   F 2  395 ? 25.284  33.159  17.492  1.00 19.29  ? 405 LEU   B C     1 
ATOM   17082 O  O     . LEU   F 2  395 ? 26.157  34.028  17.533  1.00 23.26  ? 405 LEU   B O     1 
ATOM   17083 C  CB    . LEU   F 2  395 ? 25.196  31.964  19.687  1.00 13.46  ? 405 LEU   B CB    1 
ATOM   17084 C  CG    . LEU   F 2  395 ? 25.860  32.526  20.925  1.00 21.14  ? 405 LEU   B CG    1 
ATOM   17085 C  CD1   . LEU   F 2  395 ? 24.995  33.582  21.592  1.00 21.59  ? 405 LEU   B CD1   1 
ATOM   17086 C  CD2   . LEU   F 2  395 ? 26.078  31.336  21.867  1.00 31.35  ? 405 LEU   B CD2   1 
ATOM   17087 N  N     . HIS   F 2  396 ? 25.024  32.470  16.378  1.00 20.26  ? 406 HIS   B N     1 
ATOM   17088 C  CA    . HIS   F 2  396 ? 25.888  32.599  15.201  1.00 21.32  ? 406 HIS   B CA    1 
ATOM   17089 C  C     . HIS   F 2  396 ? 25.772  33.959  14.530  1.00 23.76  ? 406 HIS   B C     1 
ATOM   17090 O  O     . HIS   F 2  396 ? 26.710  34.374  13.839  1.00 26.09  ? 406 HIS   B O     1 
ATOM   17091 C  CB    . HIS   F 2  396 ? 25.589  31.497  14.164  1.00 22.04  ? 406 HIS   B CB    1 
ATOM   17092 C  CG    . HIS   F 2  396 ? 24.257  31.638  13.485  1.00 22.77  ? 406 HIS   B CG    1 
ATOM   17093 N  ND1   . HIS   F 2  396 ? 24.107  32.219  12.244  1.00 30.55  ? 406 HIS   B ND1   1 
ATOM   17094 C  CD2   . HIS   F 2  396 ? 23.015  31.275  13.881  1.00 25.36  ? 406 HIS   B CD2   1 
ATOM   17095 C  CE1   . HIS   F 2  396 ? 22.830  32.212  11.910  1.00 26.47  ? 406 HIS   B CE1   1 
ATOM   17096 N  NE2   . HIS   F 2  396 ? 22.149  31.631  12.880  1.00 27.02  ? 406 HIS   B NE2   1 
ATOM   17097 N  N     . TRP   F 2  397 ? 24.645  34.654  14.699  1.00 22.01  ? 407 TRP   B N     1 
ATOM   17098 C  CA    . TRP   F 2  397 ? 24.555  36.030  14.212  1.00 24.70  ? 407 TRP   B CA    1 
ATOM   17099 C  C     . TRP   F 2  397 ? 25.600  36.922  14.878  1.00 28.73  ? 407 TRP   B C     1 
ATOM   17100 O  O     . TRP   F 2  397 ? 25.998  37.947  14.301  1.00 24.00  ? 407 TRP   B O     1 
ATOM   17101 C  CB    . TRP   F 2  397 ? 23.158  36.599  14.459  1.00 22.25  ? 407 TRP   B CB    1 
ATOM   17102 C  CG    . TRP   F 2  397 ? 22.058  35.844  13.790  1.00 28.72  ? 407 TRP   B CG    1 
ATOM   17103 C  CD1   . TRP   F 2  397 ? 20.993  35.238  14.393  1.00 26.34  ? 407 TRP   B CD1   1 
ATOM   17104 C  CD2   . TRP   F 2  397 ? 21.916  35.601  12.386  1.00 27.33  ? 407 TRP   B CD2   1 
ATOM   17105 N  NE1   . TRP   F 2  397 ? 20.197  34.647  13.455  1.00 27.61  ? 407 TRP   B NE1   1 
ATOM   17106 C  CE2   . TRP   F 2  397 ? 20.736  34.855  12.214  1.00 23.93  ? 407 TRP   B CE2   1 
ATOM   17107 C  CE3   . TRP   F 2  397 ? 22.657  35.968  11.256  1.00 24.76  ? 407 TRP   B CE3   1 
ATOM   17108 C  CZ2   . TRP   F 2  397 ? 20.291  34.442  10.960  1.00 28.30  ? 407 TRP   B CZ2   1 
ATOM   17109 C  CZ3   . TRP   F 2  397 ? 22.223  35.557  10.016  1.00 25.41  ? 407 TRP   B CZ3   1 
ATOM   17110 C  CH2   . TRP   F 2  397 ? 21.053  34.796  9.873   1.00 30.39  ? 407 TRP   B CH2   1 
ATOM   17111 N  N     . TYR   F 2  398 ? 26.046  36.543  16.090  1.00 18.73  ? 408 TYR   B N     1 
ATOM   17112 C  CA    . TYR   F 2  398 ? 27.035  37.238  16.912  1.00 22.52  ? 408 TYR   B CA    1 
ATOM   17113 C  C     . TYR   F 2  398 ? 28.431  36.635  16.801  1.00 33.77  ? 408 TYR   B C     1 
ATOM   17114 O  O     . TYR   F 2  398 ? 29.410  37.372  16.608  1.00 29.97  ? 408 TYR   B O     1 
ATOM   17115 C  CB    . TYR   F 2  398 ? 26.590  37.240  18.376  1.00 24.08  ? 408 TYR   B CB    1 
ATOM   17116 C  CG    . TYR   F 2  398 ? 25.229  37.867  18.543  1.00 31.53  ? 408 TYR   B CG    1 
ATOM   17117 C  CD1   . TYR   F 2  398 ? 25.102  39.226  18.759  1.00 22.79  ? 408 TYR   B CD1   1 
ATOM   17118 C  CD2   . TYR   F 2  398 ? 24.073  37.107  18.438  1.00 26.82  ? 408 TYR   B CD2   1 
ATOM   17119 C  CE1   . TYR   F 2  398 ? 23.876  39.804  18.895  1.00 27.33  ? 408 TYR   B CE1   1 
ATOM   17120 C  CE2   . TYR   F 2  398 ? 22.831  37.685  18.561  1.00 27.16  ? 408 TYR   B CE2   1 
ATOM   17121 C  CZ    . TYR   F 2  398 ? 22.736  39.035  18.792  1.00 28.66  ? 408 TYR   B CZ    1 
ATOM   17122 O  OH    . TYR   F 2  398 ? 21.509  39.633  18.933  1.00 23.10  ? 408 TYR   B OH    1 
ATOM   17123 N  N     . THR   F 2  399 ? 28.557  35.308  16.911  1.00 24.10  ? 409 THR   B N     1 
ATOM   17124 C  CA    . THR   F 2  399 ? 29.887  34.749  16.761  1.00 23.62  ? 409 THR   B CA    1 
ATOM   17125 C  C     . THR   F 2  399 ? 30.450  35.032  15.372  1.00 24.72  ? 409 THR   B C     1 
ATOM   17126 O  O     . THR   F 2  399 ? 31.673  35.083  15.212  1.00 31.07  ? 409 THR   B O     1 
ATOM   17127 C  CB    . THR   F 2  399 ? 29.905  33.244  17.079  1.00 19.36  ? 409 THR   B CB    1 
ATOM   17128 O  OG1   . THR   F 2  399 ? 28.928  32.565  16.300  1.00 30.10  ? 409 THR   B OG1   1 
ATOM   17129 C  CG2   . THR   F 2  399 ? 29.642  32.993  18.544  1.00 13.08  ? 409 THR   B CG2   1 
ATOM   17130 N  N     . GLY   F 2  400 ? 29.594  35.269  14.378  1.00 23.79  ? 410 GLY   B N     1 
ATOM   17131 C  CA    . GLY   F 2  400 ? 30.062  35.587  13.040  1.00 19.07  ? 410 GLY   B CA    1 
ATOM   17132 C  C     . GLY   F 2  400 ? 30.532  37.011  12.839  1.00 27.11  ? 410 GLY   B C     1 
ATOM   17133 O  O     . GLY   F 2  400 ? 31.150  37.323  11.811  1.00 28.56  ? 410 GLY   B O     1 
ATOM   17134 N  N     . GLU   F 2  401 ? 30.221  37.891  13.779  1.00 28.73  ? 411 GLU   B N     1 
ATOM   17135 C  CA    . GLU   F 2  401 ? 30.832  39.207  13.837  1.00 31.88  ? 411 GLU   B CA    1 
ATOM   17136 C  C     . GLU   F 2  401 ? 32.121  39.199  14.628  1.00 21.76  ? 411 GLU   B C     1 
ATOM   17137 O  O     . GLU   F 2  401 ? 32.701  40.261  14.850  1.00 25.20  ? 411 GLU   B O     1 
ATOM   17138 C  CB    . GLU   F 2  401 ? 29.869  40.224  14.460  1.00 27.37  ? 411 GLU   B CB    1 
ATOM   17139 C  CG    . GLU   F 2  401 ? 28.583  40.317  13.708  1.00 29.99  ? 411 GLU   B CG    1 
ATOM   17140 C  CD    . GLU   F 2  401 ? 28.812  40.442  12.220  1.00 31.85  ? 411 GLU   B CD    1 
ATOM   17141 O  OE1   . GLU   F 2  401 ? 29.580  41.353  11.813  1.00 27.48  ? 411 GLU   B OE1   1 
ATOM   17142 O  OE2   . GLU   F 2  401 ? 28.219  39.625  11.474  1.00 31.96  ? 411 GLU   B OE2   1 
ATOM   17143 N  N     . GLY   F 2  402 ? 32.557  38.045  15.088  1.00 22.24  ? 412 GLY   B N     1 
ATOM   17144 C  CA    . GLY   F 2  402 ? 33.777  37.950  15.865  1.00 36.65  ? 412 GLY   B CA    1 
ATOM   17145 C  C     . GLY   F 2  402 ? 33.574  37.710  17.341  1.00 33.66  ? 412 GLY   B C     1 
ATOM   17146 O  O     . GLY   F 2  402 ? 34.548  37.404  18.033  1.00 39.48  ? 412 GLY   B O     1 
ATOM   17147 N  N     . MET   F 2  403 ? 32.350  37.824  17.848  1.00 31.05  ? 413 MET   B N     1 
ATOM   17148 C  CA    . MET   F 2  403 ? 32.165  37.663  19.274  1.00 27.32  ? 413 MET   B CA    1 
ATOM   17149 C  C     . MET   F 2  403 ? 32.327  36.208  19.703  1.00 33.24  ? 413 MET   B C     1 
ATOM   17150 O  O     . MET   F 2  403 ? 32.193  35.256  18.920  1.00 29.72  ? 413 MET   B O     1 
ATOM   17151 C  CB    . MET   F 2  403 ? 30.796  38.156  19.719  1.00 21.78  ? 413 MET   B CB    1 
ATOM   17152 C  CG    . MET   F 2  403 ? 30.652  39.627  19.746  1.00 26.21  ? 413 MET   B CG    1 
ATOM   17153 S  SD    . MET   F 2  403 ? 29.022  40.038  20.370  1.00 30.36  ? 413 MET   B SD    1 
ATOM   17154 C  CE    . MET   F 2  403 ? 29.179  39.482  22.056  1.00 25.42  ? 413 MET   B CE    1 
ATOM   17155 N  N     . ASP   F 2  404 ? 32.571  36.062  21.000  1.00 33.29  ? 414 ASP   B N     1 
ATOM   17156 C  CA    . ASP   F 2  404 ? 32.791  34.799  21.662  1.00 23.45  ? 414 ASP   B CA    1 
ATOM   17157 C  C     . ASP   F 2  404 ? 31.673  34.606  22.678  1.00 32.93  ? 414 ASP   B C     1 
ATOM   17158 O  O     . ASP   F 2  404 ? 31.176  35.579  23.248  1.00 40.41  ? 414 ASP   B O     1 
ATOM   17159 C  CB    . ASP   F 2  404 ? 34.194  34.826  22.306  1.00 28.97  ? 414 ASP   B CB    1 
ATOM   17160 C  CG    . ASP   F 2  404 ? 34.563  33.526  22.987  1.00 49.06  ? 414 ASP   B CG    1 
ATOM   17161 O  OD1   . ASP   F 2  404 ? 33.896  33.184  23.985  1.00 49.55  ? 414 ASP   B OD1   1 
ATOM   17162 O  OD2   . ASP   F 2  404 ? 35.527  32.855  22.537  1.00 56.70  ? 414 ASP   B OD2   1 
ATOM   17163 N  N     . GLU   F 2  405 ? 31.253  33.354  22.885  1.00 31.74  ? 415 GLU   B N     1 
ATOM   17164 C  CA    . GLU   F 2  405 ? 30.259  33.068  23.919  1.00 27.60  ? 415 GLU   B CA    1 
ATOM   17165 C  C     . GLU   F 2  405 ? 30.614  33.707  25.250  1.00 34.36  ? 415 GLU   B C     1 
ATOM   17166 O  O     . GLU   F 2  405 ? 29.737  34.228  25.951  1.00 36.10  ? 415 GLU   B O     1 
ATOM   17167 C  CB    . GLU   F 2  405 ? 30.113  31.569  24.133  1.00 27.08  ? 415 GLU   B CB    1 
ATOM   17168 C  CG    . GLU   F 2  405 ? 29.609  30.826  22.942  1.00 56.20  ? 415 GLU   B CG    1 
ATOM   17169 C  CD    . GLU   F 2  405 ? 29.380  29.365  23.249  1.00 56.84  ? 415 GLU   B CD    1 
ATOM   17170 O  OE1   . GLU   F 2  405 ? 29.507  28.973  24.439  1.00 39.98  ? 415 GLU   B OE1   1 
ATOM   17171 O  OE2   . GLU   F 2  405 ? 29.069  28.626  22.290  1.00 52.44  ? 415 GLU   B OE2   1 
ATOM   17172 N  N     . MET   F 2  406 ? 31.887  33.630  25.646  1.00 43.45  ? 416 MET   B N     1 
ATOM   17173 C  CA    . MET   F 2  406 ? 32.276  34.091  26.978  1.00 47.87  ? 416 MET   B CA    1 
ATOM   17174 C  C     . MET   F 2  406 ? 31.755  35.500  27.247  1.00 44.61  ? 416 MET   B C     1 
ATOM   17175 O  O     . MET   F 2  406 ? 31.302  35.814  28.356  1.00 41.14  ? 416 MET   B O     1 
ATOM   17176 C  CB    . MET   F 2  406 ? 33.796  34.032  27.129  1.00 44.62  ? 416 MET   B CB    1 
ATOM   17177 C  CG    . MET   F 2  406 ? 34.264  33.958  28.576  1.00 65.98  ? 416 MET   B CG    1 
ATOM   17178 S  SD    . MET   F 2  406 ? 33.257  32.858  29.619  1.00 104.76 ? 416 MET   B SD    1 
ATOM   17179 C  CE    . MET   F 2  406 ? 33.746  31.234  29.031  1.00 85.61  ? 416 MET   B CE    1 
ATOM   17180 N  N     . GLU   F 2  407 ? 31.779  36.351  26.227  1.00 40.04  ? 417 GLU   B N     1 
ATOM   17181 C  CA    . GLU   F 2  407 ? 31.270  37.703  26.385  1.00 37.74  ? 417 GLU   B CA    1 
ATOM   17182 C  C     . GLU   F 2  407 ? 29.787  37.713  26.760  1.00 39.11  ? 417 GLU   B C     1 
ATOM   17183 O  O     . GLU   F 2  407 ? 29.328  38.631  27.454  1.00 33.41  ? 417 GLU   B O     1 
ATOM   17184 C  CB    . GLU   F 2  407 ? 31.519  38.459  25.094  1.00 23.48  ? 417 GLU   B CB    1 
ATOM   17185 C  CG    . GLU   F 2  407 ? 31.412  39.923  25.225  1.00 25.86  ? 417 GLU   B CG    1 
ATOM   17186 C  CD    . GLU   F 2  407 ? 32.046  40.629  24.072  1.00 28.15  ? 417 GLU   B CD    1 
ATOM   17187 O  OE1   . GLU   F 2  407 ? 33.037  40.107  23.491  1.00 24.56  ? 417 GLU   B OE1   1 
ATOM   17188 O  OE2   . GLU   F 2  407 ? 31.541  41.717  23.757  1.00 28.97  ? 417 GLU   B OE2   1 
ATOM   17189 N  N     . PHE   F 2  408 ? 29.031  36.708  26.298  1.00 33.03  ? 418 PHE   B N     1 
ATOM   17190 C  CA    . PHE   F 2  408 ? 27.628  36.557  26.686  1.00 30.27  ? 418 PHE   B CA    1 
ATOM   17191 C  C     . PHE   F 2  408 ? 27.505  36.134  28.141  1.00 27.47  ? 418 PHE   B C     1 
ATOM   17192 O  O     . PHE   F 2  408 ? 26.738  36.721  28.906  1.00 31.27  ? 418 PHE   B O     1 
ATOM   17193 C  CB    . PHE   F 2  408 ? 26.929  35.532  25.781  1.00 23.11  ? 418 PHE   B CB    1 
ATOM   17194 C  CG    . PHE   F 2  408 ? 26.540  36.073  24.454  1.00 27.21  ? 418 PHE   B CG    1 
ATOM   17195 C  CD1   . PHE   F 2  408 ? 27.509  36.414  23.520  1.00 30.15  ? 418 PHE   B CD1   1 
ATOM   17196 C  CD2   . PHE   F 2  408 ? 25.199  36.239  24.122  1.00 26.91  ? 418 PHE   B CD2   1 
ATOM   17197 C  CE1   . PHE   F 2  408 ? 27.152  36.931  22.286  1.00 25.15  ? 418 PHE   B CE1   1 
ATOM   17198 C  CE2   . PHE   F 2  408 ? 24.840  36.735  22.895  1.00 25.10  ? 418 PHE   B CE2   1 
ATOM   17199 C  CZ    . PHE   F 2  408 ? 25.824  37.094  21.971  1.00 23.13  ? 418 PHE   B CZ    1 
ATOM   17200 N  N     . THR   F 2  409 ? 28.243  35.096  28.531  1.00 34.64  ? 419 THR   B N     1 
ATOM   17201 C  CA    . THR   F 2  409 ? 28.277  34.670  29.925  1.00 33.41  ? 419 THR   B CA    1 
ATOM   17202 C  C     . THR   F 2  409 ? 28.612  35.826  30.870  1.00 27.89  ? 419 THR   B C     1 
ATOM   17203 O  O     . THR   F 2  409 ? 28.105  35.877  31.991  1.00 34.13  ? 419 THR   B O     1 
ATOM   17204 C  CB    . THR   F 2  409 ? 29.277  33.509  30.074  1.00 32.69  ? 419 THR   B CB    1 
ATOM   17205 O  OG1   . THR   F 2  409 ? 28.648  32.271  29.701  1.00 33.39  ? 419 THR   B OG1   1 
ATOM   17206 C  CG2   . THR   F 2  409 ? 29.778  33.399  31.475  1.00 25.69  ? 419 THR   B CG2   1 
ATOM   17207 N  N     . GLU   F 2  410 ? 29.421  36.782  30.431  1.00 27.67  ? 420 GLU   B N     1 
ATOM   17208 C  CA    . GLU   F 2  410 ? 29.801  37.871  31.322  1.00 31.86  ? 420 GLU   B CA    1 
ATOM   17209 C  C     . GLU   F 2  410 ? 28.680  38.902  31.479  1.00 34.01  ? 420 GLU   B C     1 
ATOM   17210 O  O     . GLU   F 2  410 ? 28.375  39.321  32.603  1.00 26.86  ? 420 GLU   B O     1 
ATOM   17211 C  CB    . GLU   F 2  410 ? 31.094  38.526  30.827  1.00 38.06  ? 420 GLU   B CB    1 
ATOM   17212 C  CG    . GLU   F 2  410 ? 32.367  37.774  31.225  1.00 44.73  ? 420 GLU   B CG    1 
ATOM   17213 C  CD    . GLU   F 2  410 ? 33.510  37.954  30.207  1.00 66.68  ? 420 GLU   B CD    1 
ATOM   17214 O  OE1   . GLU   F 2  410 ? 33.437  38.881  29.353  1.00 52.01  ? 420 GLU   B OE1   1 
ATOM   17215 O  OE2   . GLU   F 2  410 ? 34.479  37.155  30.261  1.00 61.81  ? 420 GLU   B OE2   1 
ATOM   17216 N  N     . ALA   F 2  411 ? 28.078  39.346  30.362  1.00 32.72  ? 421 ALA   B N     1 
ATOM   17217 C  CA    . ALA   F 2  411 ? 26.878  40.178  30.436  1.00 24.76  ? 421 ALA   B CA    1 
ATOM   17218 C  C     . ALA   F 2  411 ? 25.823  39.515  31.317  1.00 33.24  ? 421 ALA   B C     1 
ATOM   17219 O  O     . ALA   F 2  411 ? 25.307  40.121  32.262  1.00 28.21  ? 421 ALA   B O     1 
ATOM   17220 C  CB    . ALA   F 2  411 ? 26.308  40.431  29.039  1.00 20.04  ? 421 ALA   B CB    1 
ATOM   17221 N  N     . GLU   F 2  412 ? 25.497  38.257  31.025  1.00 26.33  ? 422 GLU   B N     1 
ATOM   17222 C  CA    . GLU   F 2  412 ? 24.481  37.589  31.810  1.00 28.76  ? 422 GLU   B CA    1 
ATOM   17223 C  C     . GLU   F 2  412 ? 24.845  37.604  33.287  1.00 34.56  ? 422 GLU   B C     1 
ATOM   17224 O  O     . GLU   F 2  412 ? 23.969  37.751  34.148  1.00 27.52  ? 422 GLU   B O     1 
ATOM   17225 C  CB    . GLU   F 2  412 ? 24.291  36.164  31.313  1.00 31.11  ? 422 GLU   B CB    1 
ATOM   17226 C  CG    . GLU   F 2  412 ? 23.241  35.424  32.099  1.00 35.98  ? 422 GLU   B CG    1 
ATOM   17227 C  CD    . GLU   F 2  412 ? 23.091  33.997  31.661  1.00 31.51  ? 422 GLU   B CD    1 
ATOM   17228 O  OE1   . GLU   F 2  412 ? 24.113  33.289  31.570  1.00 39.05  ? 422 GLU   B OE1   1 
ATOM   17229 O  OE2   . GLU   F 2  412 ? 21.949  33.584  31.406  1.00 44.05  ? 422 GLU   B OE2   1 
ATOM   17230 N  N     . SER   F 2  413 ? 26.139  37.467  33.597  1.00 30.15  ? 423 SER   B N     1 
ATOM   17231 C  CA    A SER   F 2  413 ? 26.562  37.433  34.994  0.26 31.32  ? 423 SER   B CA    1 
ATOM   17232 C  CA    B SER   F 2  413 ? 26.570  37.434  34.992  0.74 31.45  ? 423 SER   B CA    1 
ATOM   17233 C  C     . SER   F 2  413 ? 26.455  38.811  35.635  1.00 33.65  ? 423 SER   B C     1 
ATOM   17234 O  O     . SER   F 2  413 ? 25.943  38.949  36.751  1.00 32.57  ? 423 SER   B O     1 
ATOM   17235 C  CB    A SER   F 2  413 ? 27.991  36.895  35.096  0.26 28.94  ? 423 SER   B CB    1 
ATOM   17236 C  CB    B SER   F 2  413 ? 28.009  36.918  35.085  0.74 29.07  ? 423 SER   B CB    1 
ATOM   17237 O  OG    A SER   F 2  413 ? 28.476  36.983  36.426  0.26 27.92  ? 423 SER   B OG    1 
ATOM   17238 O  OG    B SER   F 2  413 ? 28.058  35.567  35.497  0.74 26.25  ? 423 SER   B OG    1 
ATOM   17239 N  N     . ASN   F 2  414 ? 26.930  39.845  34.939  1.00 26.28  ? 424 ASN   B N     1 
ATOM   17240 C  CA    . ASN   F 2  414 ? 26.907  41.183  35.503  1.00 32.25  ? 424 ASN   B CA    1 
ATOM   17241 C  C     . ASN   F 2  414 ? 25.490  41.706  35.684  1.00 34.62  ? 424 ASN   B C     1 
ATOM   17242 O  O     . ASN   F 2  414 ? 25.266  42.586  36.514  1.00 37.91  ? 424 ASN   B O     1 
ATOM   17243 C  CB    . ASN   F 2  414 ? 27.699  42.143  34.620  1.00 32.79  ? 424 ASN   B CB    1 
ATOM   17244 C  CG    . ASN   F 2  414 ? 28.118  43.368  35.368  1.00 31.35  ? 424 ASN   B CG    1 
ATOM   17245 O  OD1   . ASN   F 2  414 ? 28.104  43.369  36.591  1.00 37.42  ? 424 ASN   B OD1   1 
ATOM   17246 N  ND2   . ASN   F 2  414 ? 28.488  44.417  34.656  1.00 40.94  ? 424 ASN   B ND2   1 
ATOM   17247 N  N     . MET   F 2  415 ? 24.532  41.216  34.897  1.00 33.49  ? 425 MET   B N     1 
ATOM   17248 C  CA    . MET   F 2  415 ? 23.155  41.659  35.075  1.00 27.90  ? 425 MET   B CA    1 
ATOM   17249 C  C     . MET   F 2  415 ? 22.455  40.850  36.159  1.00 30.18  ? 425 MET   B C     1 
ATOM   17250 O  O     . MET   F 2  415 ? 21.646  41.400  36.915  1.00 34.30  ? 425 MET   B O     1 
ATOM   17251 C  CB    . MET   F 2  415 ? 22.394  41.577  33.758  1.00 28.21  ? 425 MET   B CB    1 
ATOM   17252 C  CG    . MET   F 2  415 ? 21.099  42.346  33.722  1.00 22.02  ? 425 MET   B CG    1 
ATOM   17253 S  SD    . MET   F 2  415 ? 20.100  41.710  32.395  1.00 38.52  ? 425 MET   B SD    1 
ATOM   17254 C  CE    . MET   F 2  415 ? 20.168  43.060  31.247  1.00 26.07  ? 425 MET   B CE    1 
ATOM   17255 N  N     . ASN   F 2  416 ? 22.759  39.552  36.272  1.00 28.26  ? 426 ASN   B N     1 
ATOM   17256 C  CA    . ASN   F 2  416 ? 22.233  38.792  37.410  1.00 33.95  ? 426 ASN   B CA    1 
ATOM   17257 C  C     . ASN   F 2  416 ? 22.780  39.328  38.736  1.00 36.48  ? 426 ASN   B C     1 
ATOM   17258 O  O     . ASN   F 2  416 ? 22.062  39.334  39.749  1.00 33.95  ? 426 ASN   B O     1 
ATOM   17259 C  CB    . ASN   F 2  416 ? 22.527  37.291  37.250  1.00 22.86  ? 426 ASN   B CB    1 
ATOM   17260 C  CG    . ASN   F 2  416 ? 21.688  36.625  36.119  1.00 32.11  ? 426 ASN   B CG    1 
ATOM   17261 O  OD1   . ASN   F 2  416 ? 20.601  37.094  35.735  1.00 23.98  ? 426 ASN   B OD1   1 
ATOM   17262 N  ND2   . ASN   F 2  416 ? 22.215  35.534  35.582  1.00 44.95  ? 426 ASN   B ND2   1 
ATOM   17263 N  N     . ASP   F 2  417 ? 24.030  39.817  38.734  1.00 32.44  ? 427 ASP   B N     1 
ATOM   17264 C  CA    . ASP   F 2  417 ? 24.592  40.482  39.908  1.00 31.23  ? 427 ASP   B CA    1 
ATOM   17265 C  C     . ASP   F 2  417 ? 23.865  41.780  40.223  1.00 32.30  ? 427 ASP   B C     1 
ATOM   17266 O  O     . ASP   F 2  417 ? 23.641  42.099  41.394  1.00 39.41  ? 427 ASP   B O     1 
ATOM   17267 C  CB    . ASP   F 2  417 ? 26.066  40.790  39.691  1.00 27.35  ? 427 ASP   B CB    1 
ATOM   17268 C  CG    . ASP   F 2  417 ? 26.943  39.591  39.802  1.00 19.58  ? 427 ASP   B CG    1 
ATOM   17269 O  OD1   . ASP   F 2  417 ? 26.459  38.471  40.043  1.00 37.55  ? 427 ASP   B OD1   1 
ATOM   17270 O  OD2   . ASP   F 2  417 ? 28.148  39.776  39.621  1.00 30.36  ? 427 ASP   B OD2   1 
ATOM   17271 N  N     . LEU   F 2  418 ? 23.544  42.569  39.197  1.00 25.51  ? 428 LEU   B N     1 
ATOM   17272 C  CA    . LEU   F 2  418 ? 22.769  43.784  39.420  1.00 34.91  ? 428 LEU   B CA    1 
ATOM   17273 C  C     . LEU   F 2  418 ? 21.434  43.471  40.088  1.00 37.84  ? 428 LEU   B C     1 
ATOM   17274 O  O     . LEU   F 2  418 ? 20.965  44.225  40.947  1.00 36.73  ? 428 LEU   B O     1 
ATOM   17275 C  CB    . LEU   F 2  418 ? 22.537  44.521  38.102  1.00 31.50  ? 428 LEU   B CB    1 
ATOM   17276 C  CG    . LEU   F 2  418 ? 21.812  45.857  38.279  1.00 23.02  ? 428 LEU   B CG    1 
ATOM   17277 C  CD1   . LEU   F 2  418 ? 22.751  46.902  38.814  1.00 23.00  ? 428 LEU   B CD1   1 
ATOM   17278 C  CD2   . LEU   F 2  418 ? 21.214  46.333  36.988  1.00 25.62  ? 428 LEU   B CD2   1 
ATOM   17279 N  N     . VAL   F 2  419 ? 20.799  42.372  39.704  1.00 32.67  ? 429 VAL   B N     1 
ATOM   17280 C  CA    . VAL   F 2  419 ? 19.545  42.024  40.347  1.00 34.29  ? 429 VAL   B CA    1 
ATOM   17281 C  C     . VAL   F 2  419 ? 19.793  41.619  41.791  1.00 30.51  ? 429 VAL   B C     1 
ATOM   17282 O  O     . VAL   F 2  419 ? 19.144  42.125  42.714  1.00 30.79  ? 429 VAL   B O     1 
ATOM   17283 C  CB    . VAL   F 2  419 ? 18.814  40.920  39.560  1.00 36.73  ? 429 VAL   B CB    1 
ATOM   17284 C  CG1   . VAL   F 2  419 ? 17.612  40.399  40.365  1.00 20.90  ? 429 VAL   B CG1   1 
ATOM   17285 C  CG2   . VAL   F 2  419 ? 18.369  41.461  38.207  1.00 30.92  ? 429 VAL   B CG2   1 
ATOM   17286 N  N     . SER   F 2  420 ? 20.727  40.696  42.015  1.00 32.59  ? 430 SER   B N     1 
ATOM   17287 C  CA    . SER   F 2  420 ? 20.951  40.261  43.389  1.00 43.83  ? 430 SER   B CA    1 
ATOM   17288 C  C     . SER   F 2  420 ? 21.388  41.423  44.263  1.00 36.86  ? 430 SER   B C     1 
ATOM   17289 O  O     . SER   F 2  420 ? 21.172  41.392  45.481  1.00 37.15  ? 430 SER   B O     1 
ATOM   17290 C  CB    . SER   F 2  420 ? 21.993  39.153  43.459  1.00 29.81  ? 430 SER   B CB    1 
ATOM   17291 O  OG    . SER   F 2  420 ? 23.275  39.742  43.439  1.00 52.37  ? 430 SER   B OG    1 
ATOM   17292 N  N     . GLU   F 2  421 ? 21.963  42.454  43.642  1.00 33.52  ? 431 GLU   B N     1 
ATOM   17293 C  CA    . GLU   F 2  421 ? 22.432  43.634  44.351  1.00 29.57  ? 431 GLU   B CA    1 
ATOM   17294 C  C     . GLU   F 2  421 ? 21.275  44.517  44.808  1.00 29.17  ? 431 GLU   B C     1 
ATOM   17295 O  O     . GLU   F 2  421 ? 21.285  45.047  45.922  1.00 37.41  ? 431 GLU   B O     1 
ATOM   17296 C  CB    . GLU   F 2  421 ? 23.381  44.385  43.435  1.00 31.44  ? 431 GLU   B CB    1 
ATOM   17297 C  CG    . GLU   F 2  421 ? 24.087  45.537  44.062  1.00 45.37  ? 431 GLU   B CG    1 
ATOM   17298 C  CD    . GLU   F 2  421 ? 25.287  45.928  43.244  1.00 51.39  ? 431 GLU   B CD    1 
ATOM   17299 O  OE1   . GLU   F 2  421 ? 25.776  45.025  42.484  1.00 33.74  ? 431 GLU   B OE1   1 
ATOM   17300 O  OE2   . GLU   F 2  421 ? 25.710  47.118  43.380  1.00 42.33  ? 431 GLU   B OE2   1 
ATOM   17301 N  N     . TYR   F 2  422 ? 20.270  44.685  43.961  1.00 34.04  ? 432 TYR   B N     1 
ATOM   17302 C  CA    . TYR   F 2  422 ? 19.053  45.366  44.376  1.00 35.55  ? 432 TYR   B CA    1 
ATOM   17303 C  C     . TYR   F 2  422 ? 18.345  44.598  45.485  1.00 35.36  ? 432 TYR   B C     1 
ATOM   17304 O  O     . TYR   F 2  422 ? 17.807  45.196  46.424  1.00 41.58  ? 432 TYR   B O     1 
ATOM   17305 C  CB    . TYR   F 2  422 ? 18.125  45.537  43.175  1.00 31.33  ? 432 TYR   B CB    1 
ATOM   17306 C  CG    . TYR   F 2  422 ? 18.411  46.744  42.316  1.00 27.72  ? 432 TYR   B CG    1 
ATOM   17307 C  CD1   . TYR   F 2  422 ? 18.306  48.026  42.851  1.00 23.25  ? 432 TYR   B CD1   1 
ATOM   17308 C  CD2   . TYR   F 2  422 ? 18.751  46.610  40.956  1.00 22.43  ? 432 TYR   B CD2   1 
ATOM   17309 C  CE1   . TYR   F 2  422 ? 18.535  49.153  42.072  1.00 26.46  ? 432 TYR   B CE1   1 
ATOM   17310 C  CE2   . TYR   F 2  422 ? 18.994  47.742  40.155  1.00 22.46  ? 432 TYR   B CE2   1 
ATOM   17311 C  CZ    . TYR   F 2  422 ? 18.884  49.008  40.727  1.00 28.88  ? 432 TYR   B CZ    1 
ATOM   17312 O  OH    . TYR   F 2  422 ? 19.098  50.153  39.986  1.00 40.61  ? 432 TYR   B OH    1 
ATOM   17313 N  N     . GLN   F 2  423 ? 18.326  43.271  45.387  1.00 34.59  ? 433 GLN   B N     1 
ATOM   17314 C  CA    . GLN   F 2  423 ? 17.649  42.463  46.395  1.00 38.87  ? 433 GLN   B CA    1 
ATOM   17315 C  C     . GLN   F 2  423 ? 18.290  42.647  47.765  1.00 39.58  ? 433 GLN   B C     1 
ATOM   17316 O  O     . GLN   F 2  423 ? 17.595  42.750  48.785  1.00 39.10  ? 433 GLN   B O     1 
ATOM   17317 C  CB    . GLN   F 2  423 ? 17.669  40.990  45.966  1.00 37.61  ? 433 GLN   B CB    1 
ATOM   17318 C  CG    . GLN   F 2  423 ? 16.822  40.055  46.821  1.00 28.93  ? 433 GLN   B CG    1 
ATOM   17319 C  CD    . GLN   F 2  423 ? 15.397  40.581  47.064  1.00 42.56  ? 433 GLN   B CD    1 
ATOM   17320 O  OE1   . GLN   F 2  423 ? 14.830  41.338  46.252  1.00 32.52  ? 433 GLN   B OE1   1 
ATOM   17321 N  NE2   . GLN   F 2  423 ? 14.824  40.190  48.200  1.00 33.15  ? 433 GLN   B NE2   1 
ATOM   17322 N  N     . GLN   F 2  424 ? 19.623  42.696  47.801  1.00 46.26  ? 434 GLN   B N     1 
ATOM   17323 C  CA    . GLN   F 2  424 ? 20.350  42.986  49.032  1.00 37.68  ? 434 GLN   B CA    1 
ATOM   17324 C  C     . GLN   F 2  424 ? 19.798  44.226  49.739  1.00 39.81  ? 434 GLN   B C     1 
ATOM   17325 O  O     . GLN   F 2  424 ? 19.476  44.189  50.933  1.00 43.18  ? 434 GLN   B O     1 
ATOM   17326 C  CB    . GLN   F 2  424 ? 21.831  43.166  48.698  1.00 34.10  ? 434 GLN   B CB    1 
ATOM   17327 C  CG    . GLN   F 2  424 ? 22.681  43.721  49.827  1.00 47.22  ? 434 GLN   B CG    1 
ATOM   17328 C  CD    . GLN   F 2  424 ? 24.106  43.971  49.398  1.00 53.96  ? 434 GLN   B CD    1 
ATOM   17329 O  OE1   . GLN   F 2  424 ? 24.437  43.867  48.207  1.00 55.26  ? 434 GLN   B OE1   1 
ATOM   17330 N  NE2   . GLN   F 2  424 ? 24.964  44.304  50.359  1.00 53.16  ? 434 GLN   B NE2   1 
ATOM   17331 N  N     . TYR   F 2  425 ? 19.706  45.345  49.025  1.00 41.60  ? 435 TYR   B N     1 
ATOM   17332 C  CA    . TYR   F 2  425 ? 19.349  46.585  49.694  1.00 42.06  ? 435 TYR   B CA    1 
ATOM   17333 C  C     . TYR   F 2  425 ? 17.858  46.715  49.892  1.00 43.79  ? 435 TYR   B C     1 
ATOM   17334 O  O     . TYR   F 2  425 ? 17.419  47.672  50.539  1.00 45.92  ? 435 TYR   B O     1 
ATOM   17335 C  CB    . TYR   F 2  425 ? 19.881  47.787  48.922  1.00 31.64  ? 435 TYR   B CB    1 
ATOM   17336 C  CG    . TYR   F 2  425 ? 21.381  47.898  48.964  1.00 28.76  ? 435 TYR   B CG    1 
ATOM   17337 C  CD1   . TYR   F 2  425 ? 22.031  48.310  50.116  1.00 34.36  ? 435 TYR   B CD1   1 
ATOM   17338 C  CD2   . TYR   F 2  425 ? 22.150  47.595  47.852  1.00 36.49  ? 435 TYR   B CD2   1 
ATOM   17339 C  CE1   . TYR   F 2  425 ? 23.415  48.420  50.165  1.00 41.40  ? 435 TYR   B CE1   1 
ATOM   17340 C  CE2   . TYR   F 2  425 ? 23.540  47.699  47.887  1.00 41.73  ? 435 TYR   B CE2   1 
ATOM   17341 C  CZ    . TYR   F 2  425 ? 24.163  48.115  49.049  1.00 45.33  ? 435 TYR   B CZ    1 
ATOM   17342 O  OH    . TYR   F 2  425 ? 25.536  48.222  49.094  1.00 53.07  ? 435 TYR   B OH    1 
ATOM   17343 N  N     . GLN   F 2  426 ? 17.090  45.774  49.354  1.00 37.73  ? 436 GLN   B N     1 
ATOM   17344 C  CA    . GLN   F 2  426 ? 15.647  45.727  49.530  1.00 35.60  ? 436 GLN   B CA    1 
ATOM   17345 C  C     . GLN   F 2  426 ? 15.270  45.001  50.799  1.00 43.59  ? 436 GLN   B C     1 
ATOM   17346 O  O     . GLN   F 2  426 ? 14.273  45.356  51.438  1.00 52.86  ? 436 GLN   B O     1 
ATOM   17347 C  CB    . GLN   F 2  426 ? 15.008  45.032  48.332  1.00 42.77  ? 436 GLN   B CB    1 
ATOM   17348 C  CG    . GLN   F 2  426 ? 13.512  45.085  48.246  1.00 41.99  ? 436 GLN   B CG    1 
ATOM   17349 C  CD    . GLN   F 2  426 ? 13.024  44.484  46.927  1.00 50.51  ? 436 GLN   B CD    1 
ATOM   17350 O  OE1   . GLN   F 2  426 ? 13.072  45.138  45.862  1.00 33.02  ? 436 GLN   B OE1   1 
ATOM   17351 N  NE2   . GLN   F 2  426 ? 12.576  43.222  46.985  1.00 41.72  ? 436 GLN   B NE2   1 
ATOM   17352 N  N     . ASP   F 2  427 ? 16.061  43.995  51.173  1.00 48.63  ? 437 ASP   B N     1 
ATOM   17353 C  CA    . ASP   F 2  427 ? 15.945  43.329  52.465  1.00 57.26  ? 437 ASP   B CA    1 
ATOM   17354 C  C     . ASP   F 2  427 ? 16.410  44.254  53.585  1.00 54.90  ? 437 ASP   B C     1 
ATOM   17355 O  O     . ASP   F 2  427 ? 15.595  44.687  54.412  1.00 62.36  ? 437 ASP   B O     1 
ATOM   17356 C  CB    . ASP   F 2  427 ? 16.758  42.029  52.474  1.00 59.91  ? 437 ASP   B CB    1 
ATOM   17357 C  CG    . ASP   F 2  427 ? 16.126  40.934  51.626  1.00 61.26  ? 437 ASP   B CG    1 
ATOM   17358 O  OD1   . ASP   F 2  427 ? 15.315  41.254  50.725  1.00 50.86  ? 437 ASP   B OD1   1 
ATOM   17359 O  OD2   . ASP   F 2  427 ? 16.434  39.748  51.877  1.00 72.14  ? 437 ASP   B OD2   1 
ATOM   17360 N  N     . ALA   F 2  428 ? 17.710  44.564  53.601  1.00 41.75  ? 438 ALA   B N     1 
ATOM   17361 C  CA    . ALA   F 2  428 ? 18.341  45.504  54.556  1.00 57.58  ? 438 ALA   B CA    1 
ATOM   17362 C  C     . ALA   F 2  428 ? 17.397  46.529  55.200  1.00 51.83  ? 438 ALA   B C     1 
ATOM   17363 O  O     . ALA   F 2  428 ? 17.651  47.005  56.313  1.00 57.26  ? 438 ALA   B O     1 
ATOM   17364 C  CB    . ALA   F 2  428 ? 19.489  46.249  53.864  1.00 48.53  ? 438 ALA   B CB    1 
HETATM 17365 P  PG    . GTP   G 5  .   ? 27.501  74.006  46.606  0.00 32.50  ? 501 GTP   A PG    1 
HETATM 17366 O  O1G   . GTP   G 5  .   ? 28.351  73.135  47.498  0.00 32.59  ? 501 GTP   A O1G   1 
HETATM 17367 O  O2G   . GTP   G 5  .   ? 28.140  74.088  45.241  0.00 32.06  ? 501 GTP   A O2G   1 
HETATM 17368 O  O3G   . GTP   G 5  .   ? 26.112  73.421  46.499  0.00 32.74  ? 501 GTP   A O3G   1 
HETATM 17369 O  O3B   . GTP   G 5  .   ? 27.426  75.476  47.258  0.00 33.34  ? 501 GTP   A O3B   1 
HETATM 17370 P  PB    . GTP   G 5  .   ? 26.069  75.976  47.963  0.00 33.26  ? 501 GTP   A PB    1 
HETATM 17371 O  O1B   . GTP   G 5  .   ? 24.967  76.077  46.937  0.00 33.40  ? 501 GTP   A O1B   1 
HETATM 17372 O  O2B   . GTP   G 5  .   ? 26.291  77.301  48.653  0.00 33.38  ? 501 GTP   A O2B   1 
HETATM 17373 O  O3A   . GTP   G 5  .   ? 25.714  74.834  49.041  0.00 33.31  ? 501 GTP   A O3A   1 
HETATM 17374 P  PA    . GTP   G 5  .   ? 24.655  75.155  50.210  0.00 32.87  ? 501 GTP   A PA    1 
HETATM 17375 O  O1A   . GTP   G 5  .   ? 23.645  76.155  49.702  0.00 32.13  ? 501 GTP   A O1A   1 
HETATM 17376 O  O2A   . GTP   G 5  .   ? 25.354  75.671  51.444  0.00 32.19  ? 501 GTP   A O2A   1 
HETATM 17377 O  "O5'" . GTP   G 5  .   ? 23.920  73.748  50.487  0.00 34.00  ? 501 GTP   A "O5'" 1 
HETATM 17378 C  "C5'" . GTP   G 5  .   ? 22.512  73.649  50.534  0.00 34.68  ? 501 GTP   A "C5'" 1 
HETATM 17379 C  "C4'" . GTP   G 5  .   ? 22.006  74.013  51.924  0.00 34.42  ? 501 GTP   A "C4'" 1 
HETATM 17380 O  "O4'" . GTP   G 5  .   ? 22.382  75.339  52.233  0.00 32.63  ? 501 GTP   A "O4'" 1 
HETATM 17381 C  "C3'" . GTP   G 5  .   ? 20.491  73.966  52.015  0.00 35.55  ? 501 GTP   A "C3'" 1 
HETATM 17382 O  "O3'" . GTP   G 5  .   ? 20.064  72.763  52.612  0.00 37.76  ? 501 GTP   A "O3'" 1 
HETATM 17383 C  "C2'" . GTP   G 5  .   ? 20.121  75.147  52.889  0.00 31.98  ? 501 GTP   A "C2'" 1 
HETATM 17384 O  "O2'" . GTP   G 5  .   ? 19.756  74.705  54.175  0.00 30.54  ? 501 GTP   A "O2'" 1 
HETATM 17385 C  "C1'" . GTP   G 5  .   ? 21.373  76.009  52.963  0.00 31.26  ? 501 GTP   A "C1'" 1 
HETATM 17386 N  N9    . GTP   G 5  .   ? 21.110  77.312  52.327  0.00 30.12  ? 501 GTP   A N9    1 
HETATM 17387 C  C8    . GTP   G 5  .   ? 21.582  77.720  51.107  0.00 30.25  ? 501 GTP   A C8    1 
HETATM 17388 N  N7    . GTP   G 5  .   ? 21.138  78.974  50.870  0.00 29.30  ? 501 GTP   A N7    1 
HETATM 17389 C  C5    . GTP   G 5  .   ? 20.396  79.377  51.924  0.00 28.99  ? 501 GTP   A C5    1 
HETATM 17390 C  C6    . GTP   G 5  .   ? 19.720  80.561  52.190  0.00 28.74  ? 501 GTP   A C6    1 
HETATM 17391 O  O6    . GTP   G 5  .   ? 19.738  81.480  51.373  0.00 29.45  ? 501 GTP   A O6    1 
HETATM 17392 N  N1    . GTP   G 5  .   ? 19.029  80.698  53.376  0.00 28.79  ? 501 GTP   A N1    1 
HETATM 17393 C  C2    . GTP   G 5  .   ? 19.015  79.661  54.287  0.00 27.90  ? 501 GTP   A C2    1 
HETATM 17394 N  N2    . GTP   G 5  .   ? 18.349  79.793  55.430  0.00 27.17  ? 501 GTP   A N2    1 
HETATM 17395 N  N3    . GTP   G 5  .   ? 19.690  78.487  54.015  0.00 28.10  ? 501 GTP   A N3    1 
HETATM 17396 C  C4    . GTP   G 5  .   ? 20.372  78.345  52.851  0.00 28.87  ? 501 GTP   A C4    1 
HETATM 17397 MG MG    . MG    H 6  .   ? 25.993  76.583  45.165  0.00 35.96  ? 502 MG    A MG    1 
HETATM 17398 CA CA    . CA    I 7  .   ? 34.364  107.700 60.170  0.00 67.50  ? 503 CA    A CA    1 
HETATM 17399 P  PG    . GTP   J 5  .   ? 19.444  18.076  -16.277 0.00 26.55  ? 501 GTP   C PG    1 
HETATM 17400 O  O1G   . GTP   J 5  .   ? 18.240  17.790  -17.141 0.00 27.21  ? 501 GTP   C O1G   1 
HETATM 17401 O  O2G   . GTP   J 5  .   ? 20.214  16.799  -16.041 0.00 26.71  ? 501 GTP   C O2G   1 
HETATM 17402 O  O3G   . GTP   J 5  .   ? 20.332  19.089  -16.960 0.00 26.48  ? 501 GTP   C O3G   1 
HETATM 17403 O  O3B   . GTP   J 5  .   ? 18.931  18.665  -14.869 0.00 26.93  ? 501 GTP   C O3B   1 
HETATM 17404 P  PB    . GTP   J 5  .   ? 18.246  20.119  -14.791 0.00 26.43  ? 501 GTP   C PB    1 
HETATM 17405 O  O1B   . GTP   J 5  .   ? 19.128  21.132  -15.481 0.00 26.58  ? 501 GTP   C O1B   1 
HETATM 17406 O  O2B   . GTP   J 5  .   ? 17.984  20.519  -13.359 0.00 26.57  ? 501 GTP   C O2B   1 
HETATM 17407 O  O3A   . GTP   J 5  .   ? 16.866  19.976  -15.608 0.00 26.58  ? 501 GTP   C O3A   1 
HETATM 17408 P  PA    . GTP   J 5  .   ? 15.492  19.561  -14.877 0.00 26.74  ? 501 GTP   C PA    1 
HETATM 17409 O  O1A   . GTP   J 5  .   ? 14.479  19.097  -15.896 0.00 27.40  ? 501 GTP   C O1A   1 
HETATM 17410 O  O2A   . GTP   J 5  .   ? 14.976  20.744  -14.094 0.00 26.16  ? 501 GTP   C O2A   1 
HETATM 17411 O  "O5'" . GTP   J 5  .   ? 15.860  18.351  -13.879 0.00 27.97  ? 501 GTP   C "O5'" 1 
HETATM 17412 C  "C5'" . GTP   J 5  .   ? 14.884  17.383  -13.549 0.00 29.19  ? 501 GTP   C "C5'" 1 
HETATM 17413 C  "C4'" . GTP   J 5  .   ? 14.069  17.815  -12.335 0.00 29.40  ? 501 GTP   C "C4'" 1 
HETATM 17414 O  "O4'" . GTP   J 5  .   ? 13.796  19.199  -12.395 0.00 27.52  ? 501 GTP   C "O4'" 1 
HETATM 17415 C  "C3'" . GTP   J 5  .   ? 12.715  17.127  -12.280 0.00 31.07  ? 501 GTP   C "C3'" 1 
HETATM 17416 O  "O3'" . GTP   J 5  .   ? 12.749  16.024  -11.405 0.00 33.25  ? 501 GTP   C "O3'" 1 
HETATM 17417 C  "C2'" . GTP   J 5  .   ? 11.763  18.185  -11.756 0.00 28.92  ? 501 GTP   C "C2'" 1 
HETATM 17418 O  "O2'" . GTP   J 5  .   ? 11.410  17.903  -10.422 0.00 29.12  ? 501 GTP   C "O2'" 1 
HETATM 17419 C  "C1'" . GTP   J 5  .   ? 12.532  19.496  -11.831 0.00 26.98  ? 501 GTP   C "C1'" 1 
HETATM 17420 N  N9    . GTP   J 5  .   ? 11.822  20.455  -12.699 0.00 26.12  ? 501 GTP   C N9    1 
HETATM 17421 C  C8    . GTP   J 5  .   ? 12.158  20.778  -13.987 0.00 25.56  ? 501 GTP   C C8    1 
HETATM 17422 N  N7    . GTP   J 5  .   ? 11.284  21.700  -14.447 0.00 24.83  ? 501 GTP   C N7    1 
HETATM 17423 C  C5    . GTP   J 5  .   ? 10.399  21.980  -13.467 0.00 24.64  ? 501 GTP   C C5    1 
HETATM 17424 C  C6    . GTP   J 5  .   ? 9.315   22.846  -13.411 0.00 24.89  ? 501 GTP   C C6    1 
HETATM 17425 O  O6    . GTP   J 5  .   ? 9.019   23.530  -14.390 0.00 25.60  ? 501 GTP   C O6    1 
HETATM 17426 N  N1    . GTP   J 5  .   ? 8.569   22.929  -12.254 0.00 25.43  ? 501 GTP   C N1    1 
HETATM 17427 C  C2    . GTP   J 5  .   ? 8.907   22.155  -11.162 0.00 24.89  ? 501 GTP   C C2    1 
HETATM 17428 N  N2    . GTP   J 5  .   ? 8.189   22.236  -10.046 0.00 25.23  ? 501 GTP   C N2    1 
HETATM 17429 N  N3    . GTP   J 5  .   ? 9.989   21.298  -11.225 0.00 24.80  ? 501 GTP   C N3    1 
HETATM 17430 C  C4    . GTP   J 5  .   ? 10.726  21.209  -12.359 0.00 25.12  ? 501 GTP   C C4    1 
HETATM 17431 MG MG    . MG    K 6  .   ? 17.994  20.222  -18.772 0.00 29.27  ? 502 MG    C MG    1 
HETATM 17432 CA CA    . CA    L 7  .   ? 12.893  53.894  -10.303 0.00 46.81  ? 503 CA    C CA    1 
HETATM 17433 C  C10   . A1EPR M 8  .   ? 4.480   41.036  18.490  1.00 28.86  ? 504 A1EPR C C10   1 
HETATM 17434 C  C13   . A1EPR M 8  .   ? 1.347   42.748  19.090  1.00 29.81  ? 504 A1EPR C C13   1 
HETATM 17435 C  C15   . A1EPR M 8  .   ? 0.146   44.962  18.045  1.00 28.31  ? 504 A1EPR C C15   1 
HETATM 17436 C  C17   . A1EPR M 8  .   ? -0.578  44.085  20.471  1.00 28.47  ? 504 A1EPR C C17   1 
HETATM 17437 C  C20   . A1EPR M 8  .   ? 0.024   40.117  17.148  1.00 32.97  ? 504 A1EPR C C20   1 
HETATM 17438 C  C21   . A1EPR M 8  .   ? 0.547   40.139  15.684  1.00 30.09  ? 504 A1EPR C C21   1 
HETATM 17439 C  C22   . A1EPR M 8  .   ? 0.697   42.199  22.782  1.00 31.56  ? 504 A1EPR C C22   1 
HETATM 17440 C  C26   . A1EPR M 8  .   ? 1.744   39.290  23.987  1.00 44.73  ? 504 A1EPR C C26   1 
HETATM 17441 C  C02   . A1EPR M 8  .   ? 1.687   40.952  20.854  1.00 27.23  ? 504 A1EPR C C02   1 
HETATM 17442 C  C03   . A1EPR M 8  .   ? 1.131   39.521  20.644  1.00 34.18  ? 504 A1EPR C C03   1 
HETATM 17443 C  C04   . A1EPR M 8  .   ? 0.353   39.537  19.479  1.00 36.03  ? 504 A1EPR C C04   1 
HETATM 17444 C  C05   . A1EPR M 8  .   ? 1.043   39.591  18.220  1.00 30.04  ? 504 A1EPR C C05   1 
HETATM 17445 C  C06   . A1EPR M 8  .   ? 1.397   38.078  17.747  1.00 26.86  ? 504 A1EPR C C06   1 
HETATM 17446 C  C07   . A1EPR M 8  .   ? 2.734   37.938  16.964  1.00 36.75  ? 504 A1EPR C C07   1 
HETATM 17447 C  C08   . A1EPR M 8  .   ? 3.925   38.955  17.303  1.00 24.34  ? 504 A1EPR C C08   1 
HETATM 17448 C  C11   . A1EPR M 8  .   ? 3.492   42.293  19.042  1.00 29.84  ? 504 A1EPR C C11   1 
HETATM 17449 C  C12   . A1EPR M 8  .   ? 2.181   41.566  19.337  1.00 29.06  ? 504 A1EPR C C12   1 
HETATM 17450 C  C14   . A1EPR M 8  .   ? 1.158   43.793  17.943  1.00 28.99  ? 504 A1EPR C C14   1 
HETATM 17451 C  C16   . A1EPR M 8  .   ? -0.743  45.127  19.325  1.00 30.94  ? 504 A1EPR C C16   1 
HETATM 17452 C  C18   . A1EPR M 8  .   ? 0.441   42.941  20.320  1.00 24.11  ? 504 A1EPR C C18   1 
HETATM 17453 C  C19   . A1EPR M 8  .   ? 2.172   40.458  18.191  1.00 30.01  ? 504 A1EPR C C19   1 
HETATM 17454 C  C23   . A1EPR M 8  .   ? 0.339   39.134  22.036  1.00 37.69  ? 504 A1EPR C C23   1 
HETATM 17455 C  C29   . A1EPR M 8  .   ? -1.841  38.320  19.333  1.00 32.88  ? 504 A1EPR C C29   1 
HETATM 17456 C  C30   . A1EPR M 8  .   ? -2.617  39.654  19.471  1.00 41.03  ? 504 A1EPR C C30   1 
HETATM 17457 C  C33   . A1EPR M 8  .   ? -2.528  46.083  20.586  1.00 40.53  ? 504 A1EPR C C33   1 
HETATM 17458 C  C34   . A1EPR M 8  .   ? 0.931   47.161  17.486  1.00 32.23  ? 504 A1EPR C C34   1 
HETATM 17459 C  C35   . A1EPR M 8  .   ? 2.347   46.802  18.058  1.00 37.05  ? 504 A1EPR C C35   1 
HETATM 17460 C  C36   . A1EPR M 8  .   ? 2.976   48.140  18.664  1.00 28.00  ? 504 A1EPR C C36   1 
HETATM 17461 C  C37   . A1EPR M 8  .   ? 3.683   49.001  17.609  1.00 32.56  ? 504 A1EPR C C37   1 
HETATM 17462 C  C38   . A1EPR M 8  .   ? 4.636   48.080  16.865  1.00 27.15  ? 504 A1EPR C C38   1 
HETATM 17463 C  C40   . A1EPR M 8  .   ? 3.428   46.954  14.720  1.00 36.29  ? 504 A1EPR C C40   1 
HETATM 17464 C  C41   . A1EPR M 8  .   ? 1.909   47.168  14.536  1.00 28.00  ? 504 A1EPR C C41   1 
HETATM 17465 C  C42   . A1EPR M 8  .   ? 1.111   45.850  14.447  1.00 33.78  ? 504 A1EPR C C42   1 
HETATM 17466 C  C43   . A1EPR M 8  .   ? 0.976   44.907  13.434  1.00 31.57  ? 504 A1EPR C C43   1 
HETATM 17467 C  C44   . A1EPR M 8  .   ? 1.618   44.897  12.006  1.00 27.09  ? 504 A1EPR C C44   1 
HETATM 17468 C  C45   . A1EPR M 8  .   ? 1.331   43.763  11.065  1.00 26.18  ? 504 A1EPR C C45   1 
HETATM 17469 C  C46   . A1EPR M 8  .   ? 0.422   42.677  11.488  1.00 25.53  ? 504 A1EPR C C46   1 
HETATM 17470 C  C47   . A1EPR M 8  .   ? -0.200  42.682  12.864  1.00 31.66  ? 504 A1EPR C C47   1 
HETATM 17471 C  C48   . A1EPR M 8  .   ? 0.128   43.870  13.831  1.00 28.59  ? 504 A1EPR C C48   1 
HETATM 17472 C  C50   . A1EPR M 8  .   ? 0.297   45.353  15.539  1.00 29.18  ? 504 A1EPR C C50   1 
HETATM 17473 C  C51   . A1EPR M 8  .   ? 0.048   46.021  16.916  1.00 31.77  ? 504 A1EPR C C51   1 
HETATM 17474 C  C52   . A1EPR M 8  .   ? 3.258   46.116  17.047  1.00 33.60  ? 504 A1EPR C C52   1 
HETATM 17475 C  C53   . A1EPR M 8  .   ? 4.594   50.126  18.189  1.00 28.71  ? 504 A1EPR C C53   1 
HETATM 17476 C  C54   . A1EPR M 8  .   ? 3.949   50.917  19.346  1.00 25.90  ? 504 A1EPR C C54   1 
HETATM 17477 C  C56   . A1EPR M 8  .   ? -1.412  46.474  16.797  1.00 38.05  ? 504 A1EPR C C56   1 
HETATM 17478 C  C59   . A1EPR M 8  .   ? -3.702  45.687  16.566  1.00 36.83  ? 504 A1EPR C C59   1 
HETATM 17479 F  F60   . A1EPR M 8  .   ? 0.167   41.661  10.634  1.00 35.45  ? 504 A1EPR C F60   1 
HETATM 17480 N  N01   . A1EPR M 8  .   ? 0.735   41.816  21.381  1.00 25.54  ? 504 A1EPR C N01   1 
HETATM 17481 N  N09   . A1EPR M 8  .   ? 3.587   39.837  18.387  1.00 33.06  ? 504 A1EPR C N09   1 
HETATM 17482 N  N39   . A1EPR M 8  .   ? 3.888   47.040  16.116  1.00 36.23  ? 504 A1EPR C N39   1 
HETATM 17483 N  N49   . A1EPR M 8  .   ? -0.295  44.160  15.121  1.00 31.99  ? 504 A1EPR C N49   1 
HETATM 17484 O  O24   . A1EPR M 8  .   ? -0.805  39.411  22.245  1.00 37.09  ? 504 A1EPR C O24   1 
HETATM 17485 O  O25   . A1EPR M 8  .   ? 1.062   38.448  23.056  1.00 39.15  ? 504 A1EPR C O25   1 
HETATM 17486 O  O27   . A1EPR M 8  .   ? 2.184   38.586  20.492  1.00 34.66  ? 504 A1EPR C O27   1 
HETATM 17487 O  O28   . A1EPR M 8  .   ? -0.459  38.220  19.516  1.00 32.43  ? 504 A1EPR C O28   1 
HETATM 17488 O  O31   . A1EPR M 8  .   ? -2.397  37.307  19.087  1.00 44.64  ? 504 A1EPR C O31   1 
HETATM 17489 O  O32   . A1EPR M 8  .   ? -1.689  46.188  19.447  1.00 34.96  ? 504 A1EPR C O32   1 
HETATM 17490 O  O55   . A1EPR M 8  .   ? 2.712   49.538  16.731  1.00 35.02  ? 504 A1EPR C O55   1 
HETATM 17491 O  O57   . A1EPR M 8  .   ? -1.689  47.618  16.545  1.00 34.07  ? 504 A1EPR C O57   1 
HETATM 17492 O  O58   . A1EPR M 8  .   ? -2.380  45.436  17.024  1.00 29.85  ? 504 A1EPR C O58   1 
HETATM 17493 H  H102  . A1EPR M 8  .   ? 5.281   40.847  19.204  1.00 34.63  ? 504 A1EPR C H102  1 
HETATM 17494 H  H101  . A1EPR M 8  .   ? 4.890   41.284  17.511  1.00 34.63  ? 504 A1EPR C H101  1 
HETATM 17495 H  H171  . A1EPR M 8  .   ? -1.177  44.165  21.371  1.00 34.16  ? 504 A1EPR C H171  1 
HETATM 17496 H  H201  . A1EPR M 8  .   ? -0.848  39.485  17.179  1.00 39.56  ? 504 A1EPR C H201  1 
HETATM 17497 H  H202  . A1EPR M 8  .   ? -0.252  41.123  17.417  1.00 39.56  ? 504 A1EPR C H202  1 
HETATM 17498 H  H213  . A1EPR M 8  .   ? -0.080  39.499  15.065  1.00 36.11  ? 504 A1EPR C H213  1 
HETATM 17499 H  H212  . A1EPR M 8  .   ? 1.573   39.774  15.660  1.00 36.11  ? 504 A1EPR C H212  1 
HETATM 17500 H  H211  . A1EPR M 8  .   ? 0.515   41.158  15.302  1.00 36.11  ? 504 A1EPR C H211  1 
HETATM 17501 H  H223  . A1EPR M 8  .   ? 1.664   41.997  23.240  1.00 37.87  ? 504 A1EPR C H223  1 
HETATM 17502 H  H221  . A1EPR M 8  .   ? 0.473   43.262  22.861  1.00 37.87  ? 504 A1EPR C H221  1 
HETATM 17503 H  H222  . A1EPR M 8  .   ? -0.075  41.626  23.294  1.00 37.87  ? 504 A1EPR C H222  1 
HETATM 17504 H  H262  . A1EPR M 8  .   ? 2.122   38.687  24.815  1.00 53.68  ? 504 A1EPR C H262  1 
HETATM 17505 H  H263  . A1EPR M 8  .   ? 1.052   40.043  24.371  1.00 53.68  ? 504 A1EPR C H263  1 
HETATM 17506 H  H261  . A1EPR M 8  .   ? 2.579   39.784  23.487  1.00 53.68  ? 504 A1EPR C H261  1 
HETATM 17507 H  H1    . A1EPR M 8  .   ? 2.500   40.965  21.581  1.00 32.68  ? 504 A1EPR C H1    1 
HETATM 17508 H  H041  . A1EPR M 8  .   ? -0.262  40.439  19.505  1.00 43.24  ? 504 A1EPR C H041  1 
HETATM 17509 H  H061  . A1EPR M 8  .   ? 0.625   37.311  17.686  1.00 32.23  ? 504 A1EPR C H061  1 
HETATM 17510 H  H071  . A1EPR M 8  .   ? 2.857   37.167  16.203  1.00 44.10  ? 504 A1EPR C H071  1 
HETATM 17511 H  H081  . A1EPR M 8  .   ? 4.143   39.550  16.418  1.00 29.20  ? 504 A1EPR C H081  1 
HETATM 17512 H  H112  . A1EPR M 8  .   ? 3.346   43.030  18.257  1.00 35.81  ? 504 A1EPR C H112  1 
HETATM 17513 H  H111  . A1EPR M 8  .   ? 3.900   42.719  19.955  1.00 35.81  ? 504 A1EPR C H111  1 
HETATM 17514 H  H141  . A1EPR M 8  .   ? 1.757   43.696  17.042  1.00 34.79  ? 504 A1EPR C H141  1 
HETATM 17515 H  H191  . A1EPR M 8  .   ? 2.118   40.876  17.185  1.00 36.01  ? 504 A1EPR C H191  1 
HETATM 17516 H  H301  . A1EPR M 8  .   ? -2.309  40.160  20.384  1.00 49.24  ? 504 A1EPR C H301  1 
HETATM 17517 H  H302  . A1EPR M 8  .   ? -3.686  39.449  19.512  1.00 49.24  ? 504 A1EPR C H302  1 
HETATM 17518 H  H303  . A1EPR M 8  .   ? -2.402  40.289  18.613  1.00 49.24  ? 504 A1EPR C H303  1 
HETATM 17519 H  H332  . A1EPR M 8  .   ? -3.259  46.888  20.573  1.00 48.64  ? 504 A1EPR C H332  1 
HETATM 17520 H  H333  . A1EPR M 8  .   ? -1.924  46.155  21.488  1.00 48.64  ? 504 A1EPR C H333  1 
HETATM 17521 H  H331  . A1EPR M 8  .   ? -3.042  45.124  20.570  1.00 48.64  ? 504 A1EPR C H331  1 
HETATM 17522 H  H341  . A1EPR M 8  .   ? 1.080   47.881  16.687  1.00 38.68  ? 504 A1EPR C H341  1 
HETATM 17523 H  H342  . A1EPR M 8  .   ? 0.370   47.631  18.288  1.00 38.68  ? 504 A1EPR C H342  1 
HETATM 17524 H  H351  . A1EPR M 8  .   ? 2.262   46.091  18.885  1.00 44.46  ? 504 A1EPR C H351  1 
HETATM 17525 H  H361  . A1EPR M 8  .   ? 3.704   47.865  19.433  1.00 33.60  ? 504 A1EPR C H361  1 
HETATM 17526 H  H362  . A1EPR M 8  .   ? 2.172   48.731  19.112  1.00 33.60  ? 504 A1EPR C H362  1 
HETATM 17527 H  H382  . A1EPR M 8  .   ? 5.298   47.594  17.587  1.00 32.58  ? 504 A1EPR C H382  1 
HETATM 17528 H  H381  . A1EPR M 8  .   ? 5.228   48.671  16.162  1.00 32.58  ? 504 A1EPR C H381  1 
HETATM 17529 H  H401  . A1EPR M 8  .   ? 3.957   47.715  14.135  1.00 43.55  ? 504 A1EPR C H401  1 
HETATM 17530 H  H402  . A1EPR M 8  .   ? 3.686   45.961  14.333  1.00 43.55  ? 504 A1EPR C H402  1 
HETATM 17531 H  H411  . A1EPR M 8  .   ? 1.751   47.724  13.631  1.00 33.59  ? 504 A1EPR C H411  1 
HETATM 17532 H  H412  . A1EPR M 8  .   ? 1.542   47.733  15.372  1.00 33.59  ? 504 A1EPR C H412  1 
HETATM 17533 H  H441  . A1EPR M 8  .   ? 2.270   45.710  11.696  1.00 32.51  ? 504 A1EPR C H441  1 
HETATM 17534 H  H451  . A1EPR M 8  .   ? 1.793   43.741  10.073  1.00 31.42  ? 504 A1EPR C H451  1 
HETATM 17535 H  H471  . A1EPR M 8  .   ? -0.862  41.876  13.178  1.00 37.99  ? 504 A1EPR C H471  1 
HETATM 17536 H  H522  . A1EPR M 8  .   ? 2.666   45.395  16.476  1.00 40.32  ? 504 A1EPR C H522  1 
HETATM 17537 H  H521  . A1EPR M 8  .   ? 4.041   45.579  17.590  1.00 40.32  ? 504 A1EPR C H521  1 
HETATM 17538 H  H531  . A1EPR M 8  .   ? 4.832   50.826  17.385  1.00 34.46  ? 504 A1EPR C H531  1 
HETATM 17539 H  H532  . A1EPR M 8  .   ? 5.515   49.668  18.558  1.00 34.46  ? 504 A1EPR C H532  1 
HETATM 17540 H  H543  . A1EPR M 8  .   ? 2.894   51.060  19.142  1.00 31.08  ? 504 A1EPR C H543  1 
HETATM 17541 H  H541  . A1EPR M 8  .   ? 4.434   51.883  19.437  1.00 31.08  ? 504 A1EPR C H541  1 
HETATM 17542 H  H542  . A1EPR M 8  .   ? 4.067   50.365  20.271  1.00 31.08  ? 504 A1EPR C H542  1 
HETATM 17543 H  H591  . A1EPR M 8  .   ? -4.209  44.737  16.382  1.00 44.19  ? 504 A1EPR C H591  1 
HETATM 17544 H  H593  . A1EPR M 8  .   ? -3.663  46.264  15.640  1.00 44.19  ? 504 A1EPR C H593  1 
HETATM 17545 H  H592  . A1EPR M 8  .   ? -4.249  46.251  17.324  1.00 44.19  ? 504 A1EPR C H592  1 
HETATM 17546 H  H491  . A1EPR M 8  .   ? -0.927  43.600  15.667  1.00 38.39  ? 504 A1EPR C H491  1 
HETATM 17547 H  H271  . A1EPR M 8  .   ? 2.811   38.700  21.192  1.00 41.59  ? 504 A1EPR C H271  1 
HETATM 17548 H  H551  . A1EPR M 8  .   ? 2.544   50.448  16.948  1.00 42.02  ? 504 A1EPR C H551  1 
HETATM 17549 H  H2    . A1EPR M 8  .   ? 4.810   38.383  17.575  1.00 29.20  ? 504 A1EPR C H2    1 
HETATM 17550 H  H091  . A1EPR M 8  .   ? 3.600   39.296  19.234  1.00 39.67  ? 504 A1EPR C H091  1 
HETATM 17551 P  PB    . GDP   N 9  .   ? 24.696  -10.729 -42.575 0.00 64.47  ? 501 GDP   D PB    1 
HETATM 17552 O  O1B   . GDP   N 9  .   ? 23.680  -9.687  -42.983 0.00 63.84  ? 501 GDP   D O1B   1 
HETATM 17553 O  O2B   . GDP   N 9  .   ? 25.848  -10.057 -41.868 0.00 61.53  ? 501 GDP   D O2B   1 
HETATM 17554 O  O3B   . GDP   N 9  .   ? 25.208  -11.442 -43.804 0.00 65.93  ? 501 GDP   D O3B   1 
HETATM 17555 O  O3A   . GDP   N 9  .   ? 24.016  -11.796 -41.579 0.00 65.71  ? 501 GDP   D O3A   1 
HETATM 17556 P  PA    . GDP   N 9  .   ? 22.745  -12.669 -42.043 0.00 67.96  ? 501 GDP   D PA    1 
HETATM 17557 O  O1A   . GDP   N 9  .   ? 23.082  -13.524 -43.241 0.00 69.03  ? 501 GDP   D O1A   1 
HETATM 17558 O  O2A   . GDP   N 9  .   ? 21.565  -11.774 -42.332 0.00 68.30  ? 501 GDP   D O2A   1 
HETATM 17559 O  "O5'" . GDP   N 9  .   ? 22.421  -13.580 -40.758 0.00 67.67  ? 501 GDP   D "O5'" 1 
HETATM 17560 C  "C5'" . GDP   N 9  .   ? 21.456  -14.626 -40.835 0.00 68.69  ? 501 GDP   D "C5'" 1 
HETATM 17561 C  "C4'" . GDP   N 9  .   ? 20.532  -14.508 -39.633 0.00 68.51  ? 501 GDP   D "C4'" 1 
HETATM 17562 O  "O4'" . GDP   N 9  .   ? 20.005  -13.181 -39.616 0.00 67.73  ? 501 GDP   D "O4'" 1 
HETATM 17563 C  "C3'" . GDP   N 9  .   ? 19.360  -15.469 -39.732 0.00 69.60  ? 501 GDP   D "C3'" 1 
HETATM 17564 O  "O3'" . GDP   N 9  .   ? 19.403  -16.406 -38.652 0.00 70.10  ? 501 GDP   D "O3'" 1 
HETATM 17565 C  "C2'" . GDP   N 9  .   ? 18.108  -14.621 -39.630 0.00 68.88  ? 501 GDP   D "C2'" 1 
HETATM 17566 O  "O2'" . GDP   N 9  .   ? 17.338  -15.012 -38.491 0.00 68.30  ? 501 GDP   D "O2'" 1 
HETATM 17567 C  "C1'" . GDP   N 9  .   ? 18.585  -13.187 -39.468 0.00 67.59  ? 501 GDP   D "C1'" 1 
HETATM 17568 N  N9    . GDP   N 9  .   ? 17.975  -12.332 -40.515 0.00 67.08  ? 501 GDP   D N9    1 
HETATM 17569 C  C8    . GDP   N 9  .   ? 18.459  -12.136 -41.756 0.00 67.63  ? 501 GDP   D C8    1 
HETATM 17570 N  N7    . GDP   N 9  .   ? 17.661  -11.297 -42.466 0.00 66.97  ? 501 GDP   D N7    1 
HETATM 17571 C  C5    . GDP   N 9  .   ? 16.639  -10.942 -41.666 0.00 65.67  ? 501 GDP   D C5    1 
HETATM 17572 C  C6    . GDP   N 9  .   ? 15.439  -10.081 -41.781 0.00 64.61  ? 501 GDP   D C6    1 
HETATM 17573 O  O6    . GDP   N 9  .   ? 15.187  -9.464  -42.839 0.00 64.99  ? 501 GDP   D O6    1 
HETATM 17574 N  N1    . GDP   N 9  .   ? 14.635  -9.986  -40.716 0.00 64.53  ? 501 GDP   D N1    1 
HETATM 17575 C  C2    . GDP   N 9  .   ? 14.878  -10.637 -39.562 0.00 64.36  ? 501 GDP   D C2    1 
HETATM 17576 N  N2    . GDP   N 9  .   ? 14.008  -10.481 -38.535 0.00 63.27  ? 501 GDP   D N2    1 
HETATM 17577 N  N3    . GDP   N 9  .   ? 15.956  -11.441 -39.386 0.00 65.50  ? 501 GDP   D N3    1 
HETATM 17578 C  C4    . GDP   N 9  .   ? 16.851  -11.627 -40.382 0.00 66.30  ? 501 GDP   D C4    1 
HETATM 17579 P  PB    . GDP   O 9  .   ? 18.582  50.150  16.031  0.00 26.60  ? 501 GDP   B PB    1 
HETATM 17580 O  O1B   . GDP   O 9  .   ? 18.764  49.136  14.927  0.00 26.30  ? 501 GDP   B O1B   1 
HETATM 17581 O  O2B   . GDP   O 9  .   ? 19.913  50.426  16.687  0.00 26.41  ? 501 GDP   B O2B   1 
HETATM 17582 O  O3B   . GDP   O 9  .   ? 18.030  51.431  15.452  0.00 27.56  ? 501 GDP   B O3B   1 
HETATM 17583 O  O3A   . GDP   O 9  .   ? 17.557  49.570  17.128  0.00 26.34  ? 501 GDP   B O3A   1 
HETATM 17584 P  PA    . GDP   O 9  .   ? 16.041  49.215  16.719  0.00 27.03  ? 501 GDP   B PA    1 
HETATM 17585 O  O1A   . GDP   O 9  .   ? 16.010  48.207  15.596  0.00 27.58  ? 501 GDP   B O1A   1 
HETATM 17586 O  O2A   . GDP   O 9  .   ? 15.293  50.467  16.326  0.00 27.99  ? 501 GDP   B O2A   1 
HETATM 17587 O  "O5'" . GDP   O 9  .   ? 15.422  48.590  18.068  0.00 26.11  ? 501 GDP   B "O5'" 1 
HETATM 17588 C  "C5'" . GDP   O 9  .   ? 14.164  47.920  18.042  0.00 25.93  ? 501 GDP   B "C5'" 1 
HETATM 17589 C  "C4'" . GDP   O 9  .   ? 13.499  48.055  19.405  0.00 25.95  ? 501 GDP   B "C4'" 1 
HETATM 17590 O  "O4'" . GDP   O 9  .   ? 13.428  49.441  19.740  0.00 25.59  ? 501 GDP   B "O4'" 1 
HETATM 17591 C  "C3'" . GDP   O 9  .   ? 12.077  47.517  19.384  0.00 26.03  ? 501 GDP   B "C3'" 1 
HETATM 17592 O  "O3'" . GDP   O 9  .   ? 11.969  46.381  20.247  0.00 25.82  ? 501 GDP   B "O3'" 1 
HETATM 17593 C  "C2'" . GDP   O 9  .   ? 11.193  48.640  19.889  0.00 25.43  ? 501 GDP   B "C2'" 1 
HETATM 17594 O  "O2'" . GDP   O 9  .   ? 10.508  48.230  21.076  0.00 24.93  ? 501 GDP   B "O2'" 1 
HETATM 17595 C  "C1'" . GDP   O 9  .   ? 12.124  49.802  20.199  0.00 25.07  ? 501 GDP   B "C1'" 1 
HETATM 17596 N  N9    . GDP   O 9  .   ? 11.675  51.023  19.485  0.00 24.89  ? 501 GDP   B N9    1 
HETATM 17597 C  C8    . GDP   O 9  .   ? 11.971  51.333  18.208  0.00 25.46  ? 501 GDP   B C8    1 
HETATM 17598 N  N7    . GDP   O 9  .   ? 11.415  52.517  17.849  0.00 25.87  ? 501 GDP   B N7    1 
HETATM 17599 C  C5    . GDP   O 9  .   ? 10.745  52.988  18.916  0.00 25.03  ? 501 GDP   B C5    1 
HETATM 17600 C  C6    . GDP   O 9  .   ? 9.933   54.189  19.221  0.00 25.49  ? 501 GDP   B C6    1 
HETATM 17601 O  O6    . GDP   O 9  .   ? 9.739   55.071  18.357  0.00 26.74  ? 501 GDP   B O6    1 
HETATM 17602 N  N1    . GDP   O 9  .   ? 9.412   54.299  20.450  0.00 25.68  ? 501 GDP   B N1    1 
HETATM 17603 C  C2    . GDP   O 9  .   ? 9.604   53.364  21.400  0.00 24.92  ? 501 GDP   B C2    1 
HETATM 17604 N  N2    . GDP   O 9  .   ? 9.041   53.553  22.618  0.00 25.30  ? 501 GDP   B N2    1 
HETATM 17605 N  N3    . GDP   O 9  .   ? 10.336  52.239  21.190  0.00 24.52  ? 501 GDP   B N3    1 
HETATM 17606 C  C4    . GDP   O 9  .   ? 10.919  52.000  19.992  0.00 24.60  ? 501 GDP   B C4    1 
HETATM 17607 O  O     . HOH   P 10 .   ? 5.396   35.846  19.470  1.00 37.53  ? 601 HOH   C O     1 
HETATM 17608 O  O     . HOH   P 10 .   ? 7.813   35.933  23.220  1.00 37.76  ? 602 HOH   C O     1 
HETATM 17609 O  O     . HOH   P 10 .   ? -0.848  49.965  15.477  1.00 34.46  ? 603 HOH   C O     1 
HETATM 17610 O  O     . HOH   P 10 .   ? 6.975   31.859  22.355  1.00 50.89  ? 604 HOH   C O     1 
HETATM 17611 O  O     . HOH   P 10 .   ? 9.407   44.534  13.582  1.00 24.39  ? 605 HOH   C O     1 
HETATM 17612 O  O     . HOH   P 10 .   ? -4.226  41.910  20.922  1.00 24.76  ? 606 HOH   C O     1 
HETATM 17613 O  O     . HOH   Q 10 .   ? 4.876   61.166  19.361  1.00 40.37  ? 601 HOH   B O     1 
HETATM 17614 O  O     . HOH   Q 10 .   ? 11.256  42.309  27.683  1.00 27.39  ? 602 HOH   B O     1 
HETATM 17615 O  O     . HOH   Q 10 .   ? 19.450  49.703  19.302  1.00 28.04  ? 603 HOH   B O     1 
HETATM 17616 O  O     . HOH   Q 10 .   ? 17.927  53.389  18.908  1.00 25.12  ? 604 HOH   B O     1 
HETATM 17617 O  O     . HOH   Q 10 .   ? 14.566  47.881  23.008  1.00 20.97  ? 605 HOH   B O     1 
HETATM 17618 O  O     . HOH   Q 10 .   ? 9.134   39.311  28.504  1.00 42.96  ? 606 HOH   B O     1 
HETATM 17619 O  O     . HOH   Q 10 .   ? 7.273   59.374  17.006  1.00 28.26  ? 607 HOH   B O     1 
HETATM 17620 O  O     . HOH   Q 10 .   ? 3.773   55.714  14.770  1.00 37.08  ? 608 HOH   B O     1 
HETATM 17621 O  O     . HOH   Q 10 .   ? -2.257  42.640  25.830  1.00 32.50  ? 609 HOH   B O     1 
# 
