data_9LNW
# 
_entry.id   9LNW 
# 
_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   9LNW         pdb_00009lnw 10.2210/pdb9lnw/pdb 
WWPDB D_1300056065 ?            ?                   
# 
_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                        9LNW 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              593672467@qq.com 
_pdbx_contact_author.name_first         Wang 
_pdbx_contact_author.name_last          Yuxi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   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-YQVB8 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 "GUANOSINE-5'-DIPHOSPHATE"             443.201   2 ? ? ? ? 
9  non-polymer syn "10'-bromovinblastine"                 889.870   1 ? ? ? ? 
10 water       nat water                                  18.015    9 ? ? ? ? 
# 
_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  "GUANOSINE-5'-DIPHOSPHATE"  GDP   
9  "10'-bromovinblastine"      A1EPS 
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 
A1EPS non-polymer         . "10'-bromovinblastine"      ? 'C46 H57 Br N4 O9'  889.870 
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        A1EPS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EPS 
_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  GDP   1 501 501 GDP   GDP D . 
N 8  GDP   1 501 501 GDP   GDP B . 
O 9  A1EPS 1 502 502 A1EPS LIG B . 
P 10 HOH   1 601 9   HOH   HOH C . 
P 10 HOH   2 602 4   HOH   HOH C . 
P 10 HOH   3 603 2   HOH   HOH C . 
P 10 HOH   4 604 5   HOH   HOH C . 
Q 10 HOH   1 601 1   HOH   HOH B . 
Q 10 HOH   2 602 3   HOH   HOH B . 
Q 10 HOH   3 603 6   HOH   HOH B . 
Q 10 HOH   4 604 7   HOH   HOH B . 
Q 10 HOH   5 605 8   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 1 A GLU 284 ? CG  ? A GLU 284 CG  
2  1 Y 1 A GLU 284 ? CD  ? A GLU 284 CD  
3  1 Y 1 A GLU 284 ? OE1 ? A GLU 284 OE1 
4  1 Y 1 A GLU 284 ? OE2 ? A GLU 284 OE2 
5  1 Y 0 C VAL 363 ? CA  B B VAL 363 CA  
6  1 Y 0 C VAL 363 ? CB  B B VAL 363 CB  
7  1 Y 0 C VAL 363 ? CG1 B B VAL 363 CG1 
8  1 Y 0 C VAL 363 ? CG2 B B VAL 363 CG2 
9  1 Y 0 D SER 155 ? CA  A C SER 153 CA  
10 1 Y 0 D SER 155 ? CB  A C SER 153 CB  
11 1 Y 0 D SER 155 ? OG  A C SER 153 OG  
12 1 Y 0 D THR 240 ? CA  A C THR 238 CA  
13 1 Y 0 D THR 240 ? CB  A C THR 238 CB  
14 1 Y 0 D THR 240 ? OG1 A C THR 238 OG1 
15 1 Y 0 D THR 240 ? CG2 A C THR 238 CG2 
16 1 Y 0 D ILE 318 ? CD1 ? C ILE 316 CD1 
17 1 Y 0 D ASN 334 ? CG  ? C ASN 332 CG  
18 1 Y 1 D LYS 338 ? CG  ? C LYS 336 CG  
19 1 Y 1 D LYS 338 ? CD  ? C LYS 336 CD  
20 1 Y 1 D LYS 338 ? CE  ? C LYS 336 CE  
21 1 Y 1 D LYS 338 ? NZ  ? C LYS 336 NZ  
22 1 Y 0 D ILE 384 ? CA  B C ILE 374 CA  
23 1 Y 0 D ILE 384 ? CB  B C ILE 374 CB  
24 1 Y 0 D ILE 384 ? CG1 B C ILE 374 CG1 
25 1 Y 0 D ILE 384 ? CG2 B C ILE 374 CG2 
26 1 Y 0 D ILE 384 ? CD1 B C ILE 374 CD1 
27 1 Y 0 F LEU 275 ? CA  B E LEU 275 CA  
28 1 Y 0 F LEU 275 ? CB  B E LEU 275 CB  
29 1 Y 0 F LEU 275 ? CG  B E LEU 275 CG  
30 1 Y 0 F LEU 275 ? CD1 B E LEU 275 CD1 
31 1 Y 0 F LEU 275 ? CD2 B E LEU 275 CD2 
32 1 Y 0 F THR 277 ? CA  B E THR 277 CA  
33 1 Y 0 F THR 277 ? CB  B E THR 277 CB  
34 1 Y 0 F THR 277 ? OG1 B E THR 277 OG1 
35 1 Y 0 F THR 277 ? CG2 B E THR 277 CG2 
36 1 Y 0 B THR 168 ? CA  B F THR 166 CA  
37 1 Y 0 B THR 168 ? CB  B F THR 166 CB  
38 1 Y 0 B THR 168 ? OG1 B F THR 166 OG1 
39 1 Y 0 B THR 168 ? CG2 B F THR 166 CG2 
40 1 Y 1 B SER 277 ? OG  ? F SER 275 OG  
41 1 Y 1 B SER 280 ? OG  ? F SER 278 OG  
42 1 Y 1 B GLN 281 ? CG  ? F GLN 279 CG  
43 1 Y 1 B GLN 281 ? CD  ? F GLN 279 CD  
44 1 Y 1 B GLN 281 ? OE1 ? F GLN 279 OE1 
45 1 Y 1 B GLN 281 ? NE2 ? F GLN 279 NE2 
46 1 Y 0 B ILE 318 ? CD1 ? F ILE 316 CD1 
47 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                     9LNW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.823 
_cell.length_a_esd                 ? 
_cell.length_b                     155.758 
_cell.length_b_esd                 ? 
_cell.length_c                     185.088 
_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                         9LNW 
_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                   9LNW 
_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             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.46 
_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                                       9LNW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               91.21 
_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                                     97144 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.81 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.3 
_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                                   0.970 
_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                                    2.55 
_reflns_shell.d_res_low                                     2.59 
_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                             4862 
_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                                  0.506 
_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                                 9LNW 
_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                            2.55 
_refine.ls_d_res_low                             91.21 
_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                     96971 
_refine.ls_number_reflns_R_free                  4873 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.63 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2286 
_refine.ls_R_factor_R_free                       0.2919 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2252 
_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                 31.76 
_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                            0.43 
_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             9 
_refine_hist.number_atoms_total               17449 
_refine_hist.d_res_high                       2.55 
_refine_hist.d_res_low                        91.21 
# 
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' ? 17.524 ? 6653 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 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' 2.55 2.58  . . 165 3076 99.00  . . . . 0.3155 . . . . . . . . . . . 0.3878 
'X-RAY DIFFRACTION' 2.58 2.61  . . 169 3073 99.00  . . . . 0.2964 . . . . . . . . . . . 0.3556 
'X-RAY DIFFRACTION' 2.61 2.64  . . 168 3055 98.00  . . . . 0.2898 . . . . . . . . . . . 0.3977 
'X-RAY DIFFRACTION' 2.64 2.67  . . 184 3004 99.00  . . . . 0.2902 . . . . . . . . . . . 0.3721 
'X-RAY DIFFRACTION' 2.67 2.71  . . 167 3041 98.00  . . . . 0.2896 . . . . . . . . . . . 0.3994 
'X-RAY DIFFRACTION' 2.71 2.75  . . 160 2917 93.00  . . . . 0.2875 . . . . . . . . . . . 0.3714 
'X-RAY DIFFRACTION' 2.75 2.79  . . 144 2833 91.00  . . . . 0.2692 . . . . . . . . . . . 0.3271 
'X-RAY DIFFRACTION' 2.79 2.83  . . 173 3063 99.00  . . . . 0.2600 . . . . . . . . . . . 0.3218 
'X-RAY DIFFRACTION' 2.83 2.87  . . 163 3100 99.00  . . . . 0.2562 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.87 2.92  . . 152 3067 98.00  . . . . 0.2691 . . . . . . . . . . . 0.3463 
'X-RAY DIFFRACTION' 2.92 2.97  . . 147 3112 100.00 . . . . 0.2668 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 2.97 3.02  . . 177 3075 99.00  . . . . 0.2619 . . . . . . . . . . . 0.3483 
'X-RAY DIFFRACTION' 3.02 3.08  . . 161 3082 99.00  . . . . 0.2511 . . . . . . . . . . . 0.3316 
'X-RAY DIFFRACTION' 3.08 3.14  . . 136 3137 100.00 . . . . 0.2627 . . . . . . . . . . . 0.3460 
'X-RAY DIFFRACTION' 3.14 3.21  . . 160 3067 99.00  . . . . 0.2469 . . . . . . . . . . . 0.3291 
'X-RAY DIFFRACTION' 3.21 3.29  . . 155 3133 99.00  . . . . 0.2467 . . . . . . . . . . . 0.3471 
'X-RAY DIFFRACTION' 3.29 3.37  . . 177 3104 99.00  . . . . 0.2518 . . . . . . . . . . . 0.3152 
'X-RAY DIFFRACTION' 3.37 3.46  . . 145 3093 99.00  . . . . 0.2355 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 3.46 3.56  . . 160 3001 96.00  . . . . 0.2379 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 3.56 3.68  . . 168 2806 90.00  . . . . 0.2237 . . . . . . . . . . . 0.3038 
'X-RAY DIFFRACTION' 3.68 3.81  . . 160 3140 100.00 . . . . 0.2223 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 3.81 3.96  . . 168 3124 100.00 . . . . 0.2037 . . . . . . . . . . . 0.2541 
'X-RAY DIFFRACTION' 3.96 4.14  . . 170 3135 100.00 . . . . 0.1967 . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 4.14 4.36  . . 143 3180 100.00 . . . . 0.1890 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 4.36 4.63  . . 171 3116 99.00  . . . . 0.1715 . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 4.63 4.99  . . 148 3166 98.00  . . . . 0.1689 . . . . . . . . . . . 0.2491 
'X-RAY DIFFRACTION' 4.99 5.49  . . 163 2848 90.00  . . . . 0.1883 . . . . . . . . . . . 0.2331 
'X-RAY DIFFRACTION' 5.49 6.29  . . 180 3181 100.00 . . . . 0.2104 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 6.29 7.92  . . 159 3195 98.00  . . . . 0.2187 . . . . . . . . . . . 0.2798 
'X-RAY DIFFRACTION' 7.92 91.21 . . 180 3174 94.00  . . . . 0.2159 . . . . . . . . . . . 0.2505 
# 
_struct.entry_id                     9LNW 
_struct.title                        'Crystal structure of T2R-TTL-YQVB8 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        9LNW 
_struct_keywords.text            'tubule inhibitor, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 8  ? 
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 9LNW A 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
2 1 9LNW C 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
3 2 9LNW D 1 ? 445 ? A0A8D1UIR5 1  ? 445 ? 1 455 
4 3 9LNW E 3 ? 143 ? P63042     49 ? 189 ? 5 145 
5 4 9LNW F 1 ? 378 ? A0A8V0Z8P0 1  ? 411 ? 1 378 
6 2 9LNW 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 9LNW MET E 1   ? UNP P63042     ?   ?  'initiating methionine' 3   1  
4 9LNW ALA E 2   ? UNP P63042     ?   ?  'expression tag'        4   2  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ALA 53 deletion                ?   3  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLU 54 deletion                ?   4  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 MET 55 deletion                ?   5  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLN 56 deletion                ?   6  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLN 57 deletion                ?   7  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLN 58 deletion                ?   8  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 LEU 59 deletion                ?   9  
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 LEU 60 deletion                ?   10 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLU 61 deletion                ?   11 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLY 62 deletion                ?   12 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ASP 63 deletion                ?   13 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLN 64 deletion                ?   14 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 THR 65 deletion                ?   15 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 LEU 66 deletion                ?   16 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 VAL 67 deletion                ?   17 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 LEU 68 deletion                ?   18 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ALA 69 deletion                ?   19 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 SER 70 deletion                ?   20 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 SER 71 deletion                ?   21 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 THR 72 deletion                ?   22 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 HIS 73 deletion                ?   23 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 PRO 74 deletion                ?   24 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLU 75 deletion                ?   25 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 SER 76 deletion                ?   26 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 VAL 77 deletion                ?   27 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ASP 78 deletion                ?   28 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 SER 79 deletion                ?   29 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ASP 80 deletion                ?   30 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 LYS 81 deletion                ?   31 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 ASN 82 deletion                ?   32 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 HIS 83 deletion                ?   33 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 GLY 84 deletion                ?   34 
5 9LNW ?   F ?   ? UNP A0A8V0Z8P0 PHE 85 deletion                ?   35 
5 9LNW HIS F 379 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        379 36 
5 9LNW HIS F 380 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        380 37 
5 9LNW HIS F 381 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        381 38 
5 9LNW HIS F 382 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        382 39 
5 9LNW HIS F 383 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        383 40 
5 9LNW 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  ? GLY A 29  ? GLY A 10  GLY A 29  1 ? 20 
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 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P5  AA5 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P6  AA6 GLY A 111 ? ASP A 127 ? GLY A 111 ASP A 127 1 ? 17 
HELX_P HELX_P7  AA7 GLY A 143 ? TYR A 161 ? GLY A 143 TYR A 161 1 ? 19 
HELX_P HELX_P8  AA8 VAL A 182 ? LEU A 195 ? VAL A 182 LEU A 195 1 ? 14 
HELX_P HELX_P9  AA9 GLU A 196 ? SER A 198 ? GLU A 196 SER A 198 5 ? 3  
HELX_P HELX_P10 AB1 ASN A 206 ? ASN A 216 ? ASN A 206 ASN A 216 1 ? 11 
HELX_P HELX_P11 AB2 THR A 223 ? PHE A 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P12 AB3 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P13 AB4 SER A 287 ? CYS A 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 296 ? GLN A 301 ? PHE A 296 GLN A 301 5 ? 6  
HELX_P HELX_P15 AB6 VAL A 324 ? ARG A 339 ? VAL A 324 ARG A 339 1 ? 16 
HELX_P HELX_P16 AB7 ILE A 384 ? ALA A 400 ? ILE A 384 ALA A 400 1 ? 17 
HELX_P HELX_P17 AB8 VAL A 405 ? GLY A 410 ? VAL A 405 GLY A 410 1 ? 6  
HELX_P HELX_P18 AB9 GLU A 414 ? VAL A 437 ? GLU A 414 VAL A 437 1 ? 24 
HELX_P HELX_P19 AC1 GLY B 10  ? GLY B 29  ? GLY C 10  GLY C 29  1 ? 20 
HELX_P HELX_P20 AC2 ASP B 47  ? THR B 51  ? ASP C 47  THR C 51  5 ? 5  
HELX_P HELX_P21 AC3 PRO B 72  ? GLY B 81  ? PRO C 72  GLY C 81  1 ? 10 
HELX_P HELX_P22 AC4 HIS B 88  ? GLU B 90  ? HIS C 88  GLU C 90  5 ? 3  
HELX_P HELX_P23 AC5 ASN B 102 ? TYR B 108 ? ASN C 102 TYR C 108 1 ? 7  
HELX_P HELX_P24 AC6 GLY B 111 ? GLN B 128 ? GLY C 111 GLN C 128 1 ? 18 
HELX_P HELX_P25 AC7 GLY B 143 ? GLY B 162 ? GLY C 143 GLY C 162 1 ? 20 
HELX_P HELX_P26 AC8 VAL B 182 ? LEU B 195 ? VAL C 182 LEU C 195 1 ? 14 
HELX_P HELX_P27 AC9 GLU B 196 ? SER B 198 ? GLU C 196 SER C 198 5 ? 3  
HELX_P HELX_P28 AD1 ASN B 206 ? ASP B 218 ? ASN C 206 ASP C 218 1 ? 13 
HELX_P HELX_P29 AD2 THR B 223 ? PHE B 244 ? THR C 223 PHE C 244 1 ? 22 
HELX_P HELX_P30 AD3 ASP B 251 ? VAL B 260 ? ASP C 251 VAL C 260 1 ? 10 
HELX_P HELX_P31 AD4 SER B 277 ? TYR B 282 ? SER C 277 TYR C 282 1 ? 6  
HELX_P HELX_P32 AD5 SER B 287 ? CYS B 295 ? SER C 287 CYS C 295 1 ? 9  
HELX_P HELX_P33 AD6 PHE B 296 ? GLN B 301 ? PHE C 296 GLN C 301 5 ? 6  
HELX_P HELX_P34 AD7 ASP B 306 ? GLY B 310 ? ASP C 306 GLY C 310 5 ? 5  
HELX_P HELX_P35 AD8 VAL B 324 ? LYS B 338 ? VAL C 324 LYS C 338 1 ? 15 
HELX_P HELX_P36 AD9 ILE B 384 ? LYS B 401 ? ILE C 384 LYS C 401 1 ? 18 
HELX_P HELX_P37 AE1 PHE B 404 ? GLY B 410 ? PHE C 404 GLY C 410 1 ? 7  
HELX_P HELX_P38 AE2 GLU B 414 ? VAL B 437 ? GLU C 414 VAL C 437 1 ? 24 
HELX_P HELX_P39 AE3 GLY C 10  ? GLY C 29  ? GLY D 10  GLY D 29  1 ? 20 
HELX_P HELX_P40 AE4 SER C 40  ? LEU C 44  ? SER D 40  LEU D 46  5 ? 5  
HELX_P HELX_P41 AE5 ARG C 46  ? VAL C 49  ? ARG D 48  VAL D 51  5 ? 4  
HELX_P HELX_P42 AE6 THR C 55  ? ASN C 57  ? THR D 57  ASN D 59  5 ? 3  
HELX_P HELX_P43 AE7 GLY C 71  ? GLY C 79  ? GLY D 73  GLY D 81  1 ? 9  
HELX_P HELX_P44 AE8 PHE C 81  ? PHE C 85  ? PHE D 83  PHE D 87  5 ? 5  
HELX_P HELX_P45 AE9 ASN C 100 ? TYR C 106 ? ASN D 102 TYR D 108 1 ? 7  
HELX_P HELX_P46 AF1 THR C 107 ? GLU C 125 ? THR D 109 GLU D 127 1 ? 19 
HELX_P HELX_P47 AF2 GLY C 142 ? TYR C 159 ? GLY D 144 TYR D 161 1 ? 18 
HELX_P HELX_P48 AF3 VAL C 180 ? THR C 196 ? VAL D 182 THR D 198 1 ? 17 
HELX_P HELX_P49 AF4 ASN C 204 ? ARG C 213 ? ASN D 206 ARG D 215 1 ? 10 
HELX_P HELX_P50 AF5 THR C 221 ? VAL C 236 ? THR D 223 VAL D 238 1 ? 16 
HELX_P HELX_P51 AF6 THR C 237 ? PHE C 242 ? THR D 239 PHE D 244 1 ? 6  
HELX_P HELX_P52 AF7 ASP C 249 ? VAL C 258 ? ASP D 251 VAL D 260 1 ? 10 
HELX_P HELX_P53 AF8 THR C 285 ? MET C 293 ? THR D 287 MET D 295 1 ? 9  
HELX_P HELX_P54 AF9 PHE C 294 ? MET C 299 ? PHE D 296 MET D 301 5 ? 6  
HELX_P HELX_P55 AG1 ASP C 304 ? GLY C 308 ? ASP D 306 GLY D 310 5 ? 5  
HELX_P HELX_P56 AG2 SER C 322 ? ASN C 337 ? SER D 324 ASN D 339 1 ? 16 
HELX_P HELX_P57 AG3 SER C 338 ? PHE C 341 ? SER D 340 PHE D 343 5 ? 4  
HELX_P HELX_P58 AG4 ILE C 374 ? ARG C 390 ? ILE D 384 ARG D 400 1 ? 17 
HELX_P HELX_P59 AG5 LEU C 395 ? GLY C 400 ? LEU D 405 GLY D 410 1 ? 6  
HELX_P HELX_P60 AG6 GLU C 405 ? ALA C 428 ? GLU D 415 ALA D 438 1 ? 24 
HELX_P HELX_P61 AG7 SER D 44  ? GLU D 136 ? SER E 46  GLU E 138 1 ? 93 
HELX_P HELX_P62 AG8 SER E 11  ? ALA E 23  ? SER F 11  ALA F 23  1 ? 13 
HELX_P HELX_P63 AG9 PRO E 48  ? LEU E 52  ? PRO F 48  LEU F 52  5 ? 5  
HELX_P HELX_P64 AH1 ALA E 68  ? ARG E 73  ? ALA F 68  ARG F 73  1 ? 6  
HELX_P HELX_P65 AH2 ARG E 73  ? THR E 83  ? ARG F 73  THR F 83  1 ? 11 
HELX_P HELX_P66 AH3 GLU E 127 ? ASN E 136 ? GLU F 127 ASN F 136 1 ? 10 
HELX_P HELX_P67 AH4 GLU E 165 ? ASP E 174 ? GLU F 165 ASP F 174 1 ? 10 
HELX_P HELX_P68 AH5 HIS E 243 ? LYS E 247 ? HIS F 243 LYS F 247 5 ? 5  
HELX_P HELX_P69 AH6 PHE E 264 ? ASN E 276 ? PHE F 264 ASN F 276 1 ? 13 
HELX_P HELX_P70 AH7 THR E 278 ? ILE E 283 ? THR F 278 ILE F 283 1 ? 6  
HELX_P HELX_P71 AH8 ILE E 283 ? SER E 303 ? ILE F 283 SER F 303 1 ? 21 
HELX_P HELX_P72 AH9 ALA E 339 ? LYS E 341 ? ALA F 339 LYS F 341 5 ? 3  
HELX_P HELX_P73 AI1 LEU E 342 ? ILE E 355 ? LEU F 342 ILE F 355 1 ? 14 
HELX_P HELX_P74 AI2 GLY F 10  ? HIS F 28  ? GLY B 10  HIS B 28  1 ? 19 
HELX_P HELX_P75 AI3 SER F 40  ? ARG F 46  ? SER B 40  ARG B 48  1 ? 7  
HELX_P HELX_P76 AI4 ILE F 47  ? VAL F 49  ? ILE B 49  VAL B 51  5 ? 3  
HELX_P HELX_P77 AI5 THR F 72  ? SER F 78  ? THR B 74  SER B 80  1 ? 7  
HELX_P HELX_P78 AI6 PHE F 81  ? PHE F 85  ? PHE B 83  PHE B 87  5 ? 5  
HELX_P HELX_P79 AI7 ARG F 86  ? ASP F 88  ? ARG B 88  ASP B 90  5 ? 3  
HELX_P HELX_P80 AI8 ASN F 100 ? TYR F 106 ? ASN B 102 TYR B 108 1 ? 7  
HELX_P HELX_P81 AI9 THR F 107 ? SER F 126 ? THR B 109 SER B 128 1 ? 20 
HELX_P HELX_P82 AJ1 GLY F 142 ? TYR F 159 ? GLY B 144 TYR B 161 1 ? 18 
HELX_P HELX_P83 AJ2 VAL F 180 ? THR F 196 ? VAL B 182 THR B 198 1 ? 17 
HELX_P HELX_P84 AJ3 ASN F 204 ? ARG F 213 ? ASN B 206 ARG B 215 1 ? 10 
HELX_P HELX_P85 AJ4 THR F 221 ? PHE F 242 ? THR B 223 PHE B 244 1 ? 22 
HELX_P HELX_P86 AJ5 ASP F 249 ? VAL F 258 ? ASP B 251 VAL B 260 1 ? 10 
HELX_P HELX_P87 AJ6 THR F 285 ? PHE F 294 ? THR B 287 PHE B 296 1 ? 10 
HELX_P HELX_P88 AJ7 ASP F 295 ? MET F 299 ? ASP B 297 MET B 301 5 ? 5  
HELX_P HELX_P89 AJ8 ASP F 304 ? GLY F 308 ? ASP B 306 GLY B 310 5 ? 5  
HELX_P HELX_P90 AJ9 SER F 322 ? ASN F 337 ? SER B 324 ASN B 339 1 ? 16 
HELX_P HELX_P91 AK1 SER F 338 ? PHE F 341 ? SER B 340 PHE B 343 5 ? 4  
HELX_P HELX_P92 AK2 ILE F 374 ? ARG F 390 ? ILE B 384 ARG B 400 1 ? 17 
HELX_P HELX_P93 AK3 LEU F 395 ? GLY F 400 ? LEU B 405 GLY B 410 1 ? 6  
HELX_P HELX_P94 AK4 ASP F 404 ? ASP F 427 ? ASP B 414 ASP B 437 1 ? 24 
# 
_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 OD1 ? ? ? 1_555 I CA . CA ? ? A ASP 39  A CA 503 1_555 ? ? ? ? ? ? ? 3.110 ? ? 
metalc2  metalc ? ? A ASP 39 OD2 ? ? ? 1_555 I CA . CA ? ? A ASP 39  A CA 503 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc3  metalc ? ? A THR 41 OG1 ? ? ? 1_555 I CA . CA ? ? A THR 41  A CA 503 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc4  metalc ? ? A GLY 44 O   ? ? ? 1_555 I CA . CA ? ? A GLY 44  A CA 503 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc5  metalc ? ? A ASP 47 OD2 ? ? ? 1_555 I CA . CA ? ? A ASP 47  A CA 503 1_555 ? ? ? ? ? ? ? 3.008 ? ? 
metalc6  metalc ? ? A ASN 50 OD1 ? ? ? 1_555 I CA . CA ? ? A ASN 50  A CA 503 1_555 ? ? ? ? ? ? ? 3.106 ? ? 
metalc7  metalc ? ? A GLU 55 OE2 ? ? ? 1_555 I CA . CA ? ? A GLU 55  A CA 503 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc8  metalc ? ? G GTP .  O3B ? ? ? 1_555 H MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.605 ? ? 
metalc9  metalc ? ? G GTP .  O1B ? ? ? 1_555 H MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc10 metalc ? ? B ASP 39 OD1 ? ? ? 1_555 L CA . CA ? ? C ASP 39  C CA 503 1_555 ? ? ? ? ? ? ? 2.795 ? ? 
metalc11 metalc ? ? B ASP 39 OD2 ? ? ? 1_555 L CA . CA ? ? C ASP 39  C CA 503 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc12 metalc ? ? B THR 41 OG1 ? ? ? 1_555 L CA . CA ? ? C THR 41  C CA 503 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc13 metalc ? ? B ASP 47 OD2 ? ? ? 1_555 L CA . CA ? ? C ASP 47  C CA 503 1_555 ? ? ? ? ? ? ? 2.670 ? ? 
metalc14 metalc ? ? B GLU 55 OE2 ? ? ? 1_555 L CA . CA ? ? C GLU 55  C CA 503 1_555 ? ? ? ? ? ? ? 2.707 ? ? 
metalc15 metalc ? ? J GTP .  O1G ? ? ? 1_555 K MG . MG ? ? C GTP 501 C MG 502 1_555 ? ? ? ? ? ? ? 2.897 ? ? 
# 
_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  OD1 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD2 ? A ASP 39 ? A ASP 39  ? 1_555 44.0  ? 
2  OD1 ? 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 47.0  ? 
3  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 68.3  ? 
4  OD1 ? 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 88.3  ? 
5  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 80.9  ? 
6  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 46.9  ? 
7  OD1 ? 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 90.3  ? 
8  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_555 126.5 ? 
9  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_555 103.3 ? 
10 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_555 133.0 ? 
11 OD1 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 159.3 ? 
12 OD2 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 128.1 ? 
13 OG1 ? A THR 41 ? A THR 41  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 153.7 ? 
14 O   ? A GLY 44 ? A GLY 44  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 110.5 ? 
15 OD2 ? A ASP 47 ? A ASP 47  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 83.3  ? 
16 OD1 ? A ASP 39 ? A ASP 39  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 114.1 ? 
17 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 73.0  ? 
18 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_555 100.2 ? 
19 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 60.4  ? 
20 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_555 154.0 ? 
21 OD1 ? A ASN 50 ? A ASN 50  ? 1_555 CA ? I CA . ? A CA 503 ? 1_555 OE2 ? A GLU 55 ? A GLU 55  ? 1_555 70.7  ? 
22 O3B ? G GTP .  ? A GTP 501 ? 1_555 MG ? H MG . ? A MG 502 ? 1_555 O1B ? G GTP .  ? A GTP 501 ? 1_555 63.6  ? 
23 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 48.2  ? 
24 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 57.3  ? 
25 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 59.5  ? 
26 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 88.0  ? 
27 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_555 134.9 ? 
28 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_555 109.8 ? 
29 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_555 119.0 ? 
30 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 78.4  ? 
31 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 72.4  ? 
32 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_555 144.2 ? 
# 
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 -4.44 
2 ALA 273 B . ? ALA 273 C PRO 274 B ? PRO 274 C 1 -2.52 
3 ALA 271 C . ? ALA 273 D PRO 272 C ? PRO 274 D 1 -3.80 
4 GLU 193 E . ? GLU 193 F PRO 194 E ? PRO 194 F 1 8.65  
5 ALA 271 F . ? ALA 273 B PRO 272 F ? PRO 274 B 1 -4.94 
# 
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 ? 2  ? 
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 
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  THR A 349 ? ASN A 356 ? THR A 349 ASN A 356 
AA3 5  GLY D 15  ? LYS D 23  ? GLY E 17  LYS E 25  
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  SER C 364 ? SER C 371 ? SER D 374 SER D 381 
AA7 9  TYR C 310 ? ARG C 318 ? TYR D 312 ARG D 320 
AA7 10 VAL C 349 ? CYS C 354 ? VAL D 351 CYS D 356 
AA8 1  TYR C 51  ? ALA C 54  ? TYR D 53  ALA D 56  
AA8 2  LYS C 58  ? PRO C 61  ? LYS D 60  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  SER E 97  ? ILE E 100 ? SER F 97  ILE F 100 
AB1 2  HIS E 180 ? GLN E 183 ? HIS F 180 GLN F 183 
AB2 1  TRP E 147 ? ILE E 148 ? TRP F 147 ILE F 148 
AB2 2  ILE E 162 ? SER E 163 ? ILE F 162 SER F 163 
AB3 1  GLU E 261 ? PHE E 263 ? GLU F 261 PHE F 263 
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 ? PHE E 263 ? GLU F 261 PHE F 263 
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 ? LEU E 378 ? PHE F 375 LEU F 378 
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 66  ? O VAL A 66  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 VAL A 137 ? N VAL A 137 O LEU A 167 ? O LEU A 167 
AA1 5 6  N SER A 170 ? N SER A 170 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 ALA A 374 ? O ALA A 374 N ARG A 320 ? N ARG A 320 
AA3 3 4  N TYR A 319 ? N TYR A 319 O GLY A 354 ? O GLY A 354 
AA3 4 5  N VAL A 353 ? N VAL A 353 O PHE D 18  ? O PHE E 20  
AA3 5 6  O GLU D 19  ? O GLU E 21  N ILE D 7   ? N ILE E 9   
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 PHE B 135 ? N PHE C 135 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 CYS B 376 ? O CYS C 376 N LEU B 318 ? N LEU C 318 
AA6 3 4  N LEU B 317 ? N LEU C 317 O LYS B 352 ? O LYS C 352 
AA7 1 2  O VAL C 91  ? O VAL D 93  N LEU C 65  ? N LEU D 67  
AA7 2 3  O VAL C 66  ? O VAL D 68  N GLN C 8   ? N GLN D 8   
AA7 3 4  N GLU C 3   ? N GLU D 3   O GLN C 131 ? O GLN D 133 
AA7 4 5  N LEU C 135 ? N LEU D 137 O PHE C 167 ? O PHE D 169 
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 SER C 364 ? O SER D 374 N ARG C 318 ? N ARG D 320 
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  N TRP E 147 ? N TRP F 147 O SER E 163 ? O SER F 163 
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 VAL E 205 ? N VAL F 205 O PHE E 315 ? O PHE F 315 
AB3 4 5  N MET E 320 ? N MET F 320 O TRP E 328 ? O TRP F 328 
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 GLY F 269 ? N GLY B 271 O PHE F 367 ? O PHE B 377 
AB5 8 9  O ASN F 370 ? O ASN B 380 N LEU F 311 ? N LEU B 313 
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                   9LNW 
_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   B THR 145 ? ? O2B   B GDP 501 ? ? 1.30 
2  1 N   D GLN 11  ? ? O1B   D GDP 501 ? ? 1.30 
3  1 N   A GLN 11  ? ? O2B   A GTP 501 ? ? 1.30 
4  1 OE2 C GLU 183 ? ? "O3'" C GTP 501 ? ? 1.96 
5  1 NE2 C GLN 285 ? ? OE1   C GLN 372 ? ? 1.97 
6  1 OH  B TYR 108 ? ? OE2   B GLU 417 ? ? 1.97 
7  1 OG1 A THR 41  ? ? O     A GLY 44  ? ? 1.98 
8  1 O   F THR 278 ? ? OG    F SER 282 ? ? 2.00 
9  1 OG  F SER 163 ? ? OE2   F GLU 168 ? ? 2.09 
10 1 OE1 A GLU 90  ? ? NZ    A LYS 124 ? ? 2.11 
11 1 OG  D SER 178 ? ? OE2   D GLU 183 ? ? 2.12 
12 1 NZ  E LYS 95  ? ? OE2   E GLU 99  ? ? 2.14 
13 1 OE2 B GLU 183 ? ? "O3'" B GDP 501 ? ? 2.16 
14 1 CA  B THR 145 ? ? O2B   B GDP 501 ? ? 2.17 
15 1 OE1 A GLN 285 ? ? N     A GLN 372 ? ? 2.17 
16 1 OE1 A GLU 97  ? ? NH2   B ARG 2   ? ? 2.19 
# 
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  ? ? -53.74  -7.28   
2  1 ARG A 64  ? ? -80.29  38.15   
3  1 LYS A 112 ? ? -22.10  -44.54  
4  1 TYR A 161 ? ? -157.23 41.40   
5  1 ALA A 281 ? ? -55.87  105.38  
6  1 TYR A 282 ? ? 37.30   125.68  
7  1 CYS A 305 ? ? 174.65  161.51  
8  1 HIS A 309 ? ? -103.70 78.38   
9  1 PHE A 404 ? ? 68.75   -6.96   
10 1 ASP A 438 ? ? -29.85  -95.14  
11 1 THR C 41  ? ? -52.25  100.32  
12 1 TYR C 108 ? ? -118.49 -81.26  
13 1 LYS C 164 ? ? -34.66  130.49  
14 1 VAL C 177 ? ? -141.19 20.45   
15 1 CYS C 200 ? ? -174.38 131.49  
16 1 PRO C 298 ? ? -52.33  -8.41   
17 1 ALA C 314 ? ? -179.18 149.71  
18 1 ILE C 341 ? ? -105.96 69.18   
19 1 THR C 349 ? ? 63.96   -128.00 
20 1 PHE C 404 ? ? 72.73   -6.91   
21 1 HIS D 37  ? ? -100.57 75.53   
22 1 ASP D 39  ? ? -138.63 -33.30  
23 1 THR D 57  ? ? -49.39  164.98  
24 1 ASN D 59  ? ? 80.84   22.23   
25 1 PRO D 63  ? ? -53.83  101.73  
26 1 ARG D 64  ? ? -52.93  71.00   
27 1 PRO D 72  ? ? -60.42  -109.93 
28 1 GLN D 96  ? ? -146.18 -50.92  
29 1 THR D 109 ? ? -129.39 -86.10  
30 1 CYS D 131 ? ? -172.98 79.03   
31 1 THR D 145 ? ? -76.57  -72.37  
32 1 LYS D 176 ? ? -68.09  2.97    
33 1 VAL D 177 ? ? -147.83 -12.32  
34 1 THR D 180 ? ? -53.48  106.84  
35 1 PHE D 214 ? ? -56.96  -84.26  
36 1 ARG D 215 ? ? -59.40  -128.39 
37 1 THR D 216 ? ? 9.15    -83.77  
38 1 LYS D 218 ? ? 80.48   50.62   
39 1 VAL D 238 ? ? -68.60  3.58    
40 1 ASN D 249 ? ? 36.90   55.65   
41 1 MET D 302 ? ? -67.89  4.90    
42 1 ALA D 304 ? ? -61.78  65.79   
43 1 ARG D 308 ? ? -58.25  -1.22   
44 1 ASN D 339 ? ? -97.20  31.27   
45 1 ARG D 369 ? ? -28.60  115.83  
46 1 MET D 373 ? ? -173.35 141.21  
47 1 ASN D 380 ? ? -101.45 66.59   
48 1 ILE D 384 ? ? -45.68  -16.56  
49 1 ILE D 384 ? ? -43.99  -18.30  
50 1 MET D 398 ? ? -133.93 -51.70  
51 1 LYS D 402 ? ? 48.29   12.33   
52 1 GLU E 10  ? ? 34.07   46.77   
53 1 PRO E 27  ? ? -67.13  -123.57 
54 1 LYS E 135 ? ? -79.76  33.64   
55 1 ASN E 136 ? ? -144.11 -40.91  
56 1 ALA F 23  ? ? -62.56  3.40    
57 1 ARG F 36  ? ? -106.34 59.05   
58 1 LEU F 87  ? ? -100.05 -78.88  
59 1 SER F 88  ? ? 44.02   -120.45 
60 1 PRO F 102 ? ? -61.62  99.55   
61 1 ALA F 133 ? ? -45.94  -73.18  
62 1 TYR F 135 ? ? -62.47  -75.71  
63 1 TRP F 147 ? ? -121.62 -168.35 
64 1 SER F 163 ? ? -153.73 -158.47 
65 1 SER F 164 ? ? -147.70 -10.15  
66 1 GLU F 175 ? ? -57.62  -90.25  
67 1 LEU F 190 ? ? -36.03  125.97  
68 1 SER F 230 ? ? -49.27  -106.58 
69 1 ASN F 232 ? ? 71.44   133.54  
70 1 GLN F 234 ? ? -163.43 -9.68   
71 1 LYS F 236 ? ? 62.93   -167.24 
72 1 THR F 237 ? ? 64.84   -62.75  
73 1 ILE F 245 ? ? -59.72  -9.54   
74 1 GLU F 248 ? ? 178.47  1.92    
75 1 TYR F 249 ? ? -150.08 3.05    
76 1 GLU F 258 ? ? -46.02  104.48  
77 1 MET F 272 ? ? -57.94  -74.70  
78 1 ILE F 330 ? ? -113.66 -76.33  
79 1 LEU F 361 ? ? -69.33  -179.81 
80 1 ARG B 2   ? ? 31.41   75.61   
81 1 SER B 40  ? ? -179.69 127.60  
82 1 THR B 74  ? ? 59.91   -74.75  
83 1 GLN B 96  ? ? -130.73 -35.88  
84 1 THR B 109 ? ? -120.15 -84.64  
85 1 ASN B 249 ? ? 27.43   59.54   
86 1 GLN B 281 ? ? 25.76   88.01   
87 1 LYS B 402 ? ? 48.97   29.62   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    89 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    90 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.22 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    E 
_pdbx_validate_planes.auth_seq_id     76 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.078 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 ? M GDP ?   
143 1 N 0 B GDP 501 ? N 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 
A1EPS C10    C  N N 1   
A1EPS C13    C  Y N 2   
A1EPS C15    C  Y N 3   
A1EPS C17    C  Y N 4   
A1EPS C20    C  N N 5   
A1EPS C21    C  N N 6   
A1EPS C22    C  N N 7   
A1EPS C26    C  N N 8   
A1EPS C02    C  N R 9   
A1EPS C03    C  N S 10  
A1EPS C04    C  N R 11  
A1EPS C05    C  N R 12  
A1EPS C06    C  N N 13  
A1EPS C07    C  N N 14  
A1EPS C08    C  N N 15  
A1EPS C11    C  N N 16  
A1EPS C12    C  N R 17  
A1EPS C14    C  Y N 18  
A1EPS C16    C  Y N 19  
A1EPS C18    C  Y N 20  
A1EPS C19    C  N R 21  
A1EPS C23    C  N N 22  
A1EPS C29    C  N N 23  
A1EPS C30    C  N N 24  
A1EPS C33    C  N N 25  
A1EPS C34    C  N N 26  
A1EPS C35    C  N R 27  
A1EPS C36    C  N N 28  
A1EPS C37    C  N R 29  
A1EPS C38    C  N N 30  
A1EPS C40    C  N N 31  
A1EPS C41    C  N N 32  
A1EPS C42    C  Y N 33  
A1EPS C43    C  Y N 34  
A1EPS C44    C  Y N 35  
A1EPS C45    C  Y N 36  
A1EPS C46    C  Y N 37  
A1EPS C47    C  Y N 38  
A1EPS C48    C  Y N 39  
A1EPS C50    C  Y N 40  
A1EPS C51    C  N S 41  
A1EPS C52    C  N N 42  
A1EPS C53    C  N N 43  
A1EPS C54    C  N N 44  
A1EPS C56    C  N N 45  
A1EPS C59    C  N N 46  
A1EPS N01    N  N N 47  
A1EPS N09    N  N N 48  
A1EPS N39    N  N R 49  
A1EPS N49    N  Y N 50  
A1EPS O24    O  N N 51  
A1EPS O25    O  N N 52  
A1EPS O27    O  N N 53  
A1EPS O28    O  N N 54  
A1EPS O31    O  N N 55  
A1EPS O32    O  N N 56  
A1EPS O55    O  N N 57  
A1EPS O57    O  N N 58  
A1EPS O58    O  N N 59  
A1EPS BR60   BR N N 60  
A1EPS H102   H  N N 61  
A1EPS H101   H  N N 62  
A1EPS H171   H  N N 63  
A1EPS H202   H  N N 64  
A1EPS H201   H  N N 65  
A1EPS H211   H  N N 66  
A1EPS H213   H  N N 67  
A1EPS H212   H  N N 68  
A1EPS H223   H  N N 69  
A1EPS H222   H  N N 70  
A1EPS H221   H  N N 71  
A1EPS H262   H  N N 72  
A1EPS H261   H  N N 73  
A1EPS H263   H  N N 74  
A1EPS H1     H  N N 75  
A1EPS H041   H  N N 76  
A1EPS H061   H  N N 77  
A1EPS H071   H  N N 78  
A1EPS H082   H  N N 79  
A1EPS H081   H  N N 80  
A1EPS H112   H  N N 81  
A1EPS H111   H  N N 82  
A1EPS H141   H  N N 83  
A1EPS H191   H  N N 84  
A1EPS H301   H  N N 85  
A1EPS H303   H  N N 86  
A1EPS H302   H  N N 87  
A1EPS H333   H  N N 88  
A1EPS H331   H  N N 89  
A1EPS H332   H  N N 90  
A1EPS H342   H  N N 91  
A1EPS H341   H  N N 92  
A1EPS H351   H  N N 93  
A1EPS H362   H  N N 94  
A1EPS H361   H  N N 95  
A1EPS H382   H  N N 96  
A1EPS H381   H  N N 97  
A1EPS H401   H  N N 98  
A1EPS H402   H  N N 99  
A1EPS H412   H  N N 100 
A1EPS H411   H  N N 101 
A1EPS H441   H  N N 102 
A1EPS H451   H  N N 103 
A1EPS H471   H  N N 104 
A1EPS H522   H  N N 105 
A1EPS H521   H  N N 106 
A1EPS H531   H  N N 107 
A1EPS H532   H  N N 108 
A1EPS H543   H  N N 109 
A1EPS H541   H  N N 110 
A1EPS H542   H  N N 111 
A1EPS H592   H  N N 112 
A1EPS H593   H  N N 113 
A1EPS H591   H  N N 114 
A1EPS H491   H  N N 115 
A1EPS H271   H  N N 116 
A1EPS H551   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 
A1EPS C10   C11    sing N N 1   
A1EPS C10   N09    sing N N 2   
A1EPS C13   C12    sing N N 3   
A1EPS C13   C14    doub Y N 4   
A1EPS C13   C18    sing Y N 5   
A1EPS C15   C14    sing Y N 6   
A1EPS C15   C16    doub Y N 7   
A1EPS C15   C51    sing N N 8   
A1EPS C17   C16    sing Y N 9   
A1EPS C17   C18    doub Y N 10  
A1EPS C20   C21    sing N N 11  
A1EPS C20   C05    sing N N 12  
A1EPS C22   N01    sing N N 13  
A1EPS C26   O25    sing N N 14  
A1EPS C02   C03    sing N N 15  
A1EPS C02   N01    sing N N 16  
A1EPS C03   C04    sing N N 17  
A1EPS C03   C23    sing N N 18  
A1EPS C03   O27    sing N N 19  
A1EPS C04   C05    sing N N 20  
A1EPS C04   O28    sing N N 21  
A1EPS C05   C06    sing N N 22  
A1EPS C05   C19    sing N N 23  
A1EPS C06   C07    doub N N 24  
A1EPS C07   C08    sing N N 25  
A1EPS C08   N09    sing N N 26  
A1EPS C11   C12    sing N N 27  
A1EPS C12   C19    sing N N 28  
A1EPS C16   O32    sing N N 29  
A1EPS C18   N01    sing N N 30  
A1EPS C19   N09    sing N N 31  
A1EPS C23   O24    doub N N 32  
A1EPS C23   O25    sing N N 33  
A1EPS C29   C30    sing N N 34  
A1EPS C29   O28    sing N N 35  
A1EPS C29   O31    doub N N 36  
A1EPS C33   O32    sing N N 37  
A1EPS C34   C35    sing N N 38  
A1EPS C34   C51    sing N N 39  
A1EPS C35   C36    sing N N 40  
A1EPS C35   C52    sing N N 41  
A1EPS C36   C37    sing N N 42  
A1EPS C37   C38    sing N N 43  
A1EPS C37   C53    sing N N 44  
A1EPS C37   O55    sing N N 45  
A1EPS C38   N39    sing N N 46  
A1EPS C40   C41    sing N N 47  
A1EPS C40   N39    sing N N 48  
A1EPS C41   C42    sing N N 49  
A1EPS C42   C43    sing Y N 50  
A1EPS C42   C50    doub Y N 51  
A1EPS C43   C44    doub Y N 52  
A1EPS C43   C48    sing Y N 53  
A1EPS C44   C45    sing Y N 54  
A1EPS C45   C46    doub Y N 55  
A1EPS C46   C47    sing Y N 56  
A1EPS C46   BR60   sing N N 57  
A1EPS C47   C48    doub Y N 58  
A1EPS C48   N49    sing Y N 59  
A1EPS C50   C51    sing N N 60  
A1EPS C50   N49    sing Y N 61  
A1EPS C51   C56    sing N N 62  
A1EPS C52   N39    sing N N 63  
A1EPS C53   C54    sing N N 64  
A1EPS C56   O57    doub N N 65  
A1EPS C56   O58    sing N N 66  
A1EPS C59   O58    sing N N 67  
A1EPS C10   H102   sing N N 68  
A1EPS C10   H101   sing N N 69  
A1EPS C17   H171   sing N N 70  
A1EPS C20   H202   sing N N 71  
A1EPS C20   H201   sing N N 72  
A1EPS C21   H211   sing N N 73  
A1EPS C21   H213   sing N N 74  
A1EPS C21   H212   sing N N 75  
A1EPS C22   H223   sing N N 76  
A1EPS C22   H222   sing N N 77  
A1EPS C22   H221   sing N N 78  
A1EPS C26   H262   sing N N 79  
A1EPS C26   H261   sing N N 80  
A1EPS C26   H263   sing N N 81  
A1EPS C02   H1     sing N N 82  
A1EPS C04   H041   sing N N 83  
A1EPS C06   H061   sing N N 84  
A1EPS C07   H071   sing N N 85  
A1EPS C08   H082   sing N N 86  
A1EPS C08   H081   sing N N 87  
A1EPS C11   H112   sing N N 88  
A1EPS C11   H111   sing N N 89  
A1EPS C14   H141   sing N N 90  
A1EPS C19   H191   sing N N 91  
A1EPS C30   H301   sing N N 92  
A1EPS C30   H303   sing N N 93  
A1EPS C30   H302   sing N N 94  
A1EPS C33   H333   sing N N 95  
A1EPS C33   H331   sing N N 96  
A1EPS C33   H332   sing N N 97  
A1EPS C34   H342   sing N N 98  
A1EPS C34   H341   sing N N 99  
A1EPS C35   H351   sing N N 100 
A1EPS C36   H362   sing N N 101 
A1EPS C36   H361   sing N N 102 
A1EPS C38   H382   sing N N 103 
A1EPS C38   H381   sing N N 104 
A1EPS C40   H401   sing N N 105 
A1EPS C40   H402   sing N N 106 
A1EPS C41   H412   sing N N 107 
A1EPS C41   H411   sing N N 108 
A1EPS C44   H441   sing N N 109 
A1EPS C45   H451   sing N N 110 
A1EPS C47   H471   sing N N 111 
A1EPS C52   H522   sing N N 112 
A1EPS C52   H521   sing N N 113 
A1EPS C53   H531   sing N N 114 
A1EPS C53   H532   sing N N 115 
A1EPS C54   H543   sing N N 116 
A1EPS C54   H541   sing N N 117 
A1EPS C54   H542   sing N N 118 
A1EPS C59   H592   sing N N 119 
A1EPS C59   H593   sing N N 120 
A1EPS C59   H591   sing N N 121 
A1EPS N49   H491   sing N N 122 
A1EPS O27   H271   sing N N 123 
A1EPS O55   H551   sing N N 124 
A1EPS C02   C12    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                    9LNW 
_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]   0.009540 
_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]   0.006420 
_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]   0.005403 
_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 
BR 
C  
CA 
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   ? -40.128 100.810 -68.216  1.00 57.33  ? 1   MET   A N     1 
ATOM   2     C  CA    . MET   A 1  1   ? -39.200 100.136 -67.302  1.00 68.25  ? 1   MET   A CA    1 
ATOM   3     C  C     . MET   A 1  1   ? -39.903 99.023  -66.515  1.00 68.97  ? 1   MET   A C     1 
ATOM   4     O  O     . MET   A 1  1   ? -41.045 99.173  -66.053  1.00 66.86  ? 1   MET   A O     1 
ATOM   5     C  CB    . MET   A 1  1   ? -38.548 101.146 -66.340  1.00 60.07  ? 1   MET   A CB    1 
ATOM   6     C  CG    . MET   A 1  1   ? -37.449 100.563 -65.435  1.00 51.78  ? 1   MET   A CG    1 
ATOM   7     S  SD    . MET   A 1  1   ? -38.084 99.853  -63.882  1.00 60.59  ? 1   MET   A SD    1 
ATOM   8     C  CE    . MET   A 1  1   ? -38.989 101.226 -63.181  1.00 55.60  ? 1   MET   A CE    1 
ATOM   9     N  N     . ARG   A 1  2   ? -39.205 97.903  -66.367  1.00 62.90  ? 2   ARG   A N     1 
ATOM   10    C  CA    . ARG   A 1  2   ? -39.734 96.725  -65.698  1.00 59.58  ? 2   ARG   A CA    1 
ATOM   11    C  C     . ARG   A 1  2   ? -38.687 96.173  -64.740  1.00 54.97  ? 2   ARG   A C     1 
ATOM   12    O  O     . ARG   A 1  2   ? -37.488 96.143  -65.050  1.00 49.20  ? 2   ARG   A O     1 
ATOM   13    C  CB    . ARG   A 1  2   ? -40.139 95.661  -66.717  1.00 56.09  ? 2   ARG   A CB    1 
ATOM   14    C  CG    . ARG   A 1  2   ? -41.027 96.186  -67.832  1.00 53.81  ? 2   ARG   A CG    1 
ATOM   15    C  CD    . ARG   A 1  2   ? -41.368 95.068  -68.800  1.00 65.93  ? 2   ARG   A CD    1 
ATOM   16    N  NE    . ARG   A 1  2   ? -42.205 94.039  -68.189  1.00 60.69  ? 2   ARG   A NE    1 
ATOM   17    C  CZ    . ARG   A 1  2   ? -42.380 92.825  -68.692  1.00 66.53  ? 2   ARG   A CZ    1 
ATOM   18    N  NH1   . ARG   A 1  2   ? -41.746 92.433  -69.790  1.00 65.24  ? 2   ARG   A NH1   1 
ATOM   19    N  NH2   . ARG   A 1  2   ? -43.208 91.981  -68.079  1.00 63.85  ? 2   ARG   A NH2   1 
ATOM   20    N  N     . GLU   A 1  3   ? -39.144 95.726  -63.581  1.00 55.93  ? 3   GLU   A N     1 
ATOM   21    C  CA    . GLU   A 1  3   ? -38.225 95.345  -62.522  1.00 51.90  ? 3   GLU   A CA    1 
ATOM   22    C  C     . GLU   A 1  3   ? -37.894 93.863  -62.595  1.00 46.32  ? 3   GLU   A C     1 
ATOM   23    O  O     . GLU   A 1  3   ? -38.655 93.048  -63.129  1.00 45.16  ? 3   GLU   A O     1 
ATOM   24    C  CB    . GLU   A 1  3   ? -38.807 95.686  -61.152  1.00 44.53  ? 3   GLU   A CB    1 
ATOM   25    C  CG    . GLU   A 1  3   ? -39.227 97.153  -61.011  1.00 48.36  ? 3   GLU   A CG    1 
ATOM   26    C  CD    . GLU   A 1  3   ? -40.660 97.422  -61.467  1.00 54.62  ? 3   GLU   A CD    1 
ATOM   27    O  OE1   . GLU   A 1  3   ? -41.312 96.500  -62.020  1.00 51.11  ? 3   GLU   A OE1   1 
ATOM   28    O  OE2   . GLU   A 1  3   ? -41.134 98.564  -61.260  1.00 55.37  ? 3   GLU   A OE2   1 
ATOM   29    N  N     . CYS   A 1  4   ? -36.723 93.532  -62.083  1.00 45.22  ? 4   CYS   A N     1 
ATOM   30    C  CA    . CYS   A 1  4   ? -36.341 92.154  -61.833  1.00 52.82  ? 4   CYS   A CA    1 
ATOM   31    C  C     . CYS   A 1  4   ? -36.098 91.999  -60.338  1.00 46.31  ? 4   CYS   A C     1 
ATOM   32    O  O     . CYS   A 1  4   ? -35.466 92.855  -59.701  1.00 42.82  ? 4   CYS   A O     1 
ATOM   33    C  CB    . CYS   A 1  4   ? -35.084 91.747  -62.635  1.00 43.15  ? 4   CYS   A CB    1 
ATOM   34    S  SG    . CYS   A 1  4   ? -35.228 91.906  -64.447  1.00 54.96  ? 4   CYS   A SG    1 
ATOM   35    N  N     . ILE   A 1  5   ? -36.613 90.920  -59.772  1.00 41.13  ? 5   ILE   A N     1 
ATOM   36    C  CA    . ILE   A 1  5   ? -36.341 90.588  -58.383  1.00 43.12  ? 5   ILE   A CA    1 
ATOM   37    C  C     . ILE   A 1  5   ? -35.337 89.445  -58.340  1.00 42.76  ? 5   ILE   A C     1 
ATOM   38    O  O     . ILE   A 1  5   ? -35.446 88.470  -59.105  1.00 40.32  ? 5   ILE   A O     1 
ATOM   39    C  CB    . ILE   A 1  5   ? -37.632 90.241  -57.634  1.00 40.94  ? 5   ILE   A CB    1 
ATOM   40    C  CG1   . ILE   A 1  5   ? -38.442 91.522  -57.414  1.00 35.10  ? 5   ILE   A CG1   1 
ATOM   41    C  CG2   . ILE   A 1  5   ? -37.290 89.568  -56.319  1.00 42.76  ? 5   ILE   A CG2   1 
ATOM   42    C  CD1   . ILE   A 1  5   ? -39.916 91.293  -57.354  1.00 41.21  ? 5   ILE   A CD1   1 
ATOM   43    N  N     . SER   A 1  6   ? -34.338 89.587  -57.476  1.00 44.12  ? 6   SER   A N     1 
ATOM   44    C  CA    . SER   A 1  6   ? -33.290 88.588  -57.306  1.00 49.02  ? 6   SER   A CA    1 
ATOM   45    C  C     . SER   A 1  6   ? -33.561 87.801  -56.031  1.00 48.22  ? 6   SER   A C     1 
ATOM   46    O  O     . SER   A 1  6   ? -33.849 88.395  -54.981  1.00 42.13  ? 6   SER   A O     1 
ATOM   47    C  CB    . SER   A 1  6   ? -31.910 89.247  -57.239  1.00 45.90  ? 6   SER   A CB    1 
ATOM   48    O  OG    . SER   A 1  6   ? -31.626 89.986  -58.413  1.00 41.91  ? 6   SER   A OG    1 
ATOM   49    N  N     . ILE   A 1  7   ? -33.483 86.472  -56.134  1.00 43.67  ? 7   ILE   A N     1 
ATOM   50    C  CA    . ILE   A 1  7   ? -33.704 85.559  -55.014  1.00 43.32  ? 7   ILE   A CA    1 
ATOM   51    C  C     . ILE   A 1  7   ? -32.427 84.757  -54.812  1.00 44.90  ? 7   ILE   A C     1 
ATOM   52    O  O     . ILE   A 1  7   ? -32.033 83.982  -55.693  1.00 45.28  ? 7   ILE   A O     1 
ATOM   53    C  CB    . ILE   A 1  7   ? -34.886 84.604  -55.255  1.00 37.75  ? 7   ILE   A CB    1 
ATOM   54    C  CG1   . ILE   A 1  7   ? -36.143 85.344  -55.703  1.00 34.87  ? 7   ILE   A CG1   1 
ATOM   55    C  CG2   . ILE   A 1  7   ? -35.172 83.766  -53.989  1.00 37.86  ? 7   ILE   A CG2   1 
ATOM   56    C  CD1   . ILE   A 1  7   ? -37.285 84.390  -56.114  1.00 35.17  ? 7   ILE   A CD1   1 
ATOM   57    N  N     . HIS   A 1  8   ? -31.800 84.916  -53.652  1.00 44.87  ? 8   HIS   A N     1 
ATOM   58    C  CA    . HIS   A 1  8   ? -30.576 84.198  -53.316  1.00 42.52  ? 8   HIS   A CA    1 
ATOM   59    C  C     . HIS   A 1  8   ? -30.891 83.136  -52.270  1.00 34.46  ? 8   HIS   A C     1 
ATOM   60    O  O     . HIS   A 1  8   ? -31.346 83.472  -51.177  1.00 36.41  ? 8   HIS   A O     1 
ATOM   61    C  CB    . HIS   A 1  8   ? -29.519 85.175  -52.814  1.00 37.16  ? 8   HIS   A CB    1 
ATOM   62    C  CG    . HIS   A 1  8   ? -29.431 86.427  -53.631  1.00 49.22  ? 8   HIS   A CG    1 
ATOM   63    N  ND1   . HIS   A 1  8   ? -28.393 86.679  -54.503  1.00 46.40  ? 8   HIS   A ND1   1 
ATOM   64    C  CD2   . HIS   A 1  8   ? -30.263 87.496  -53.718  1.00 51.84  ? 8   HIS   A CD2   1 
ATOM   65    C  CE1   . HIS   A 1  8   ? -28.584 87.851  -55.086  1.00 45.94  ? 8   HIS   A CE1   1 
ATOM   66    N  NE2   . HIS   A 1  8   ? -29.711 88.368  -54.626  1.00 45.15  ? 8   HIS   A NE2   1 
ATOM   67    N  N     . VAL   A 1  9   ? -30.637 81.866  -52.606  1.00 28.03  ? 9   VAL   A N     1 
ATOM   68    C  CA    . VAL   A 1  9   ? -31.044 80.711  -51.807  1.00 30.52  ? 9   VAL   A CA    1 
ATOM   69    C  C     . VAL   A 1  9   ? -29.814 79.867  -51.456  1.00 35.68  ? 9   VAL   A C     1 
ATOM   70    O  O     . VAL   A 1  9   ? -29.082 79.414  -52.350  1.00 37.26  ? 9   VAL   A O     1 
ATOM   71    C  CB    . VAL   A 1  9   ? -32.090 79.846  -52.529  1.00 37.32  ? 9   VAL   A CB    1 
ATOM   72    C  CG1   . VAL   A 1  9   ? -32.522 78.699  -51.619  1.00 43.36  ? 9   VAL   A CG1   1 
ATOM   73    C  CG2   . VAL   A 1  9   ? -33.303 80.660  -52.937  1.00 35.02  ? 9   VAL   A CG2   1 
ATOM   74    N  N     . GLY   A 1  10  ? -29.619 79.626  -50.150  1.00 29.08  ? 10  GLY   A N     1 
ATOM   75    C  CA    . GLY   A 1  10  ? -28.527 78.838  -49.625  1.00 29.04  ? 10  GLY   A CA    1 
ATOM   76    C  C     . GLY   A 1  10  ? -27.281 79.657  -49.341  1.00 34.66  ? 10  GLY   A C     1 
ATOM   77    O  O     . GLY   A 1  10  ? -27.183 80.840  -49.677  1.00 32.23  ? 10  GLY   A O     1 
ATOM   78    N  N     . GLN   A 1  11  ? -26.287 79.005  -48.712  1.00 24.97  ? 11  GLN   A N     1 
ATOM   79    C  CA    . GLN   A 1  11  ? -25.039 79.714  -48.457  1.00 28.22  ? 11  GLN   A CA    1 
ATOM   80    C  C     . GLN   A 1  11  ? -24.464 80.296  -49.756  1.00 39.26  ? 11  GLN   A C     1 
ATOM   81    O  O     . GLN   A 1  11  ? -24.104 81.480  -49.821  1.00 31.31  ? 11  GLN   A O     1 
ATOM   82    C  CB    . GLN   A 1  11  ? -24.022 78.793  -47.782  1.00 27.40  ? 11  GLN   A CB    1 
ATOM   83    C  CG    . GLN   A 1  11  ? -22.665 79.461  -47.593  1.00 28.67  ? 11  GLN   A CG    1 
ATOM   84    C  CD    . GLN   A 1  11  ? -21.661 78.601  -46.854  1.00 29.01  ? 11  GLN   A CD    1 
ATOM   85    O  OE1   . GLN   A 1  11  ? -21.815 78.347  -45.667  1.00 37.92  ? 11  GLN   A OE1   1 
ATOM   86    N  NE2   . GLN   A 1  11  ? -20.606 78.173  -47.546  1.00 28.74  ? 11  GLN   A NE2   1 
ATOM   87    N  N     . ALA   A 1  12  ? -24.383 79.471  -50.809  1.00 30.08  ? 12  ALA   A N     1 
ATOM   88    C  CA    . ALA   A 1  12  ? -23.718 79.911  -52.032  1.00 30.90  ? 12  ALA   A CA    1 
ATOM   89    C  C     . ALA   A 1  12  ? -24.488 81.039  -52.710  1.00 37.46  ? 12  ALA   A C     1 
ATOM   90    O  O     . ALA   A 1  12  ? -23.890 82.029  -53.154  1.00 36.73  ? 12  ALA   A O     1 
ATOM   91    C  CB    . ALA   A 1  12  ? -23.525 78.732  -52.987  1.00 24.14  ? 12  ALA   A CB    1 
ATOM   92    N  N     . GLY   A 1  13  ? -25.813 80.910  -52.804  1.00 38.19  ? 13  GLY   A N     1 
ATOM   93    C  CA    . GLY   A 1  13  ? -26.600 81.989  -53.375  1.00 33.41  ? 13  GLY   A CA    1 
ATOM   94    C  C     . GLY   A 1  13  ? -26.470 83.275  -52.585  1.00 38.17  ? 13  GLY   A C     1 
ATOM   95    O  O     . GLY   A 1  13  ? -26.330 84.358  -53.159  1.00 43.68  ? 13  GLY   A O     1 
ATOM   96    N  N     . VAL   A 1  14  ? -26.492 83.171  -51.257  1.00 39.62  ? 14  VAL   A N     1 
ATOM   97    C  CA    . VAL   A 1  14  ? -26.408 84.361  -50.423  1.00 41.13  ? 14  VAL   A CA    1 
ATOM   98    C  C     . VAL   A 1  14  ? -25.032 85.012  -50.553  1.00 42.41  ? 14  VAL   A C     1 
ATOM   99    O  O     . VAL   A 1  14  ? -24.921 86.229  -50.761  1.00 37.63  ? 14  VAL   A O     1 
ATOM   100   C  CB    . VAL   A 1  14  ? -26.762 84.010  -48.967  1.00 29.93  ? 14  VAL   A CB    1 
ATOM   101   C  CG1   . VAL   A 1  14  ? -26.651 85.230  -48.084  1.00 34.19  ? 14  VAL   A CG1   1 
ATOM   102   C  CG2   . VAL   A 1  14  ? -28.179 83.489  -48.917  1.00 32.66  ? 14  VAL   A CG2   1 
ATOM   103   N  N     . GLN   A 1  15  ? -23.963 84.218  -50.461  1.00 39.50  ? 15  GLN   A N     1 
ATOM   104   C  CA    . GLN   A 1  15  ? -22.631 84.818  -50.513  1.00 38.78  ? 15  GLN   A CA    1 
ATOM   105   C  C     . GLN   A 1  15  ? -22.331 85.358  -51.902  1.00 39.03  ? 15  GLN   A C     1 
ATOM   106   O  O     . GLN   A 1  15  ? -21.692 86.407  -52.038  1.00 35.33  ? 15  GLN   A O     1 
ATOM   107   C  CB    . GLN   A 1  15  ? -21.571 83.813  -50.066  1.00 28.66  ? 15  GLN   A CB    1 
ATOM   108   C  CG    . GLN   A 1  15  ? -21.900 83.277  -48.677  1.00 35.17  ? 15  GLN   A CG    1 
ATOM   109   C  CD    . GLN   A 1  15  ? -20.745 82.625  -47.961  1.00 30.56  ? 15  GLN   A CD    1 
ATOM   110   O  OE1   . GLN   A 1  15  ? -20.545 82.881  -46.774  1.00 34.76  ? 15  GLN   A OE1   1 
ATOM   111   N  NE2   . GLN   A 1  15  ? -19.985 81.765  -48.662  1.00 26.70  ? 15  GLN   A NE2   1 
ATOM   112   N  N     . ILE   A 1  16  ? -22.804 84.669  -52.940  1.00 35.68  ? 16  ILE   A N     1 
ATOM   113   C  CA    . ILE   A 1  16  ? -22.634 85.164  -54.299  1.00 32.94  ? 16  ILE   A CA    1 
ATOM   114   C  C     . ILE   A 1  16  ? -23.449 86.439  -54.491  1.00 42.49  ? 16  ILE   A C     1 
ATOM   115   O  O     . ILE   A 1  16  ? -22.904 87.507  -54.806  1.00 40.38  ? 16  ILE   A O     1 
ATOM   116   C  CB    . ILE   A 1  16  ? -22.994 84.063  -55.317  1.00 32.69  ? 16  ILE   A CB    1 
ATOM   117   C  CG1   . ILE   A 1  16  ? -21.864 83.036  -55.385  1.00 28.75  ? 16  ILE   A CG1   1 
ATOM   118   C  CG2   . ILE   A 1  16  ? -23.222 84.629  -56.707  1.00 32.14  ? 16  ILE   A CG2   1 
ATOM   119   C  CD1   . ILE   A 1  16  ? -22.213 81.838  -56.210  1.00 26.82  ? 16  ILE   A CD1   1 
ATOM   120   N  N     . GLY   A 1  17  ? -24.758 86.359  -54.249  1.00 37.66  ? 17  GLY   A N     1 
ATOM   121   C  CA    . GLY   A 1  17  ? -25.571 87.558  -54.145  1.00 42.05  ? 17  GLY   A CA    1 
ATOM   122   C  C     . GLY   A 1  17  ? -24.912 88.733  -53.430  1.00 43.28  ? 17  GLY   A C     1 
ATOM   123   O  O     . GLY   A 1  17  ? -25.049 89.884  -53.860  1.00 47.81  ? 17  GLY   A O     1 
ATOM   124   N  N     . ASN   A 1  18  ? -24.193 88.480  -52.339  1.00 36.22  ? 18  ASN   A N     1 
ATOM   125   C  CA    . ASN   A 1  18  ? -23.545 89.595  -51.661  1.00 41.37  ? 18  ASN   A CA    1 
ATOM   126   C  C     . ASN   A 1  18  ? -22.458 90.206  -52.525  1.00 43.43  ? 18  ASN   A C     1 
ATOM   127   O  O     . ASN   A 1  18  ? -22.313 91.432  -52.583  1.00 45.89  ? 18  ASN   A O     1 
ATOM   128   C  CB    . ASN   A 1  18  ? -22.972 89.151  -50.319  1.00 43.40  ? 18  ASN   A CB    1 
ATOM   129   C  CG    . ASN   A 1  18  ? -23.906 89.460  -49.192  1.00 48.82  ? 18  ASN   A CG    1 
ATOM   130   O  OD1   . ASN   A 1  18  ? -24.775 88.661  -48.888  1.00 51.83  ? 18  ASN   A OD1   1 
ATOM   131   N  ND2   . ASN   A 1  18  ? -23.773 90.649  -48.597  1.00 59.29  ? 18  ASN   A ND2   1 
ATOM   132   N  N     . ALA   A 1  19  ? -21.672 89.375  -53.194  1.00 41.77  ? 19  ALA   A N     1 
ATOM   133   C  CA    . ALA   A 1  19  ? -20.649 89.932  -54.050  1.00 38.14  ? 19  ALA   A CA    1 
ATOM   134   C  C     . ALA   A 1  19  ? -21.281 90.694  -55.210  1.00 45.69  ? 19  ALA   A C     1 
ATOM   135   O  O     . ALA   A 1  19  ? -20.737 91.710  -55.657  1.00 43.06  ? 19  ALA   A O     1 
ATOM   136   C  CB    . ALA   A 1  19  ? -19.726 88.817  -54.529  1.00 31.02  ? 19  ALA   A CB    1 
ATOM   137   N  N     . CYS   A 1  20  ? -22.445 90.241  -55.680  1.00 39.97  ? 20  CYS   A N     1 
ATOM   138   C  CA    . CYS   A 1  20  ? -23.081 90.902  -56.810  1.00 42.39  ? 20  CYS   A CA    1 
ATOM   139   C  C     . CYS   A 1  20  ? -23.589 92.281  -56.423  1.00 43.47  ? 20  CYS   A C     1 
ATOM   140   O  O     . CYS   A 1  20  ? -23.381 93.254  -57.159  1.00 44.01  ? 20  CYS   A O     1 
ATOM   141   C  CB    . CYS   A 1  20  ? -24.205 90.040  -57.368  1.00 28.65  ? 20  CYS   A CB    1 
ATOM   142   S  SG    . CYS   A 1  20  ? -23.541 88.582  -58.091  1.00 45.75  ? 20  CYS   A SG    1 
ATOM   143   N  N     . TRP   A 1  21  ? -24.258 92.393  -55.274  1.00 38.57  ? 21  TRP   A N     1 
ATOM   144   C  CA    . TRP   A 1  21  ? -24.743 93.709  -54.881  1.00 35.78  ? 21  TRP   A CA    1 
ATOM   145   C  C     . TRP   A 1  21  ? -23.587 94.613  -54.462  1.00 38.81  ? 21  TRP   A C     1 
ATOM   146   O  O     . TRP   A 1  21  ? -23.639 95.822  -54.702  1.00 47.40  ? 21  TRP   A O     1 
ATOM   147   C  CB    . TRP   A 1  21  ? -25.817 93.579  -53.796  1.00 36.04  ? 21  TRP   A CB    1 
ATOM   148   C  CG    . TRP   A 1  21  ? -27.040 92.835  -54.306  1.00 43.82  ? 21  TRP   A CG    1 
ATOM   149   C  CD1   . TRP   A 1  21  ? -27.336 91.519  -54.109  1.00 38.13  ? 21  TRP   A CD1   1 
ATOM   150   C  CD2   . TRP   A 1  21  ? -28.100 93.363  -55.137  1.00 35.37  ? 21  TRP   A CD2   1 
ATOM   151   N  NE1   . TRP   A 1  21  ? -28.510 91.192  -54.756  1.00 39.25  ? 21  TRP   A NE1   1 
ATOM   152   C  CE2   . TRP   A 1  21  ? -28.996 92.301  -55.397  1.00 33.76  ? 21  TRP   A CE2   1 
ATOM   153   C  CE3   . TRP   A 1  21  ? -28.372 94.622  -55.679  1.00 31.58  ? 21  TRP   A CE3   1 
ATOM   154   C  CZ2   . TRP   A 1  21  ? -30.156 92.463  -56.168  1.00 33.47  ? 21  TRP   A CZ2   1 
ATOM   155   C  CZ3   . TRP   A 1  21  ? -29.524 94.781  -56.460  1.00 40.70  ? 21  TRP   A CZ3   1 
ATOM   156   C  CH2   . TRP   A 1  21  ? -30.403 93.706  -56.691  1.00 32.41  ? 21  TRP   A CH2   1 
ATOM   157   N  N     . GLU   A 1  22  ? -22.515 94.059  -53.888  1.00 41.50  ? 22  GLU   A N     1 
ATOM   158   C  CA    . GLU   A 1  22  ? -21.331 94.882  -53.665  1.00 43.16  ? 22  GLU   A CA    1 
ATOM   159   C  C     . GLU   A 1  22  ? -20.881 95.507  -54.974  1.00 48.35  ? 22  GLU   A C     1 
ATOM   160   O  O     . GLU   A 1  22  ? -20.679 96.723  -55.061  1.00 48.37  ? 22  GLU   A O     1 
ATOM   161   C  CB    . GLU   A 1  22  ? -20.197 94.058  -53.056  1.00 46.17  ? 22  GLU   A CB    1 
ATOM   162   C  CG    . GLU   A 1  22  ? -18.871 94.835  -52.938  1.00 42.17  ? 22  GLU   A CG    1 
ATOM   163   C  CD    . GLU   A 1  22  ? -17.731 94.032  -52.289  1.00 60.64  ? 22  GLU   A CD    1 
ATOM   164   O  OE1   . GLU   A 1  22  ? -17.538 92.825  -52.598  1.00 51.61  ? 22  GLU   A OE1   1 
ATOM   165   O  OE2   . GLU   A 1  22  ? -17.007 94.626  -51.466  1.00 69.85  ? 22  GLU   A OE2   1 
ATOM   166   N  N     . LEU   A 1  23  ? -20.746 94.675  -56.011  1.00 48.44  ? 23  LEU   A N     1 
ATOM   167   C  CA    . LEU   A 1  23  ? -20.355 95.126  -57.341  1.00 44.60  ? 23  LEU   A CA    1 
ATOM   168   C  C     . LEU   A 1  23  ? -21.395 96.061  -57.951  1.00 44.97  ? 23  LEU   A C     1 
ATOM   169   O  O     . LEU   A 1  23  ? -21.079 97.197  -58.330  1.00 43.29  ? 23  LEU   A O     1 
ATOM   170   C  CB    . LEU   A 1  23  ? -20.149 93.917  -58.236  1.00 38.15  ? 23  LEU   A CB    1 
ATOM   171   C  CG    . LEU   A 1  23  ? -19.442 94.240  -59.530  1.00 39.93  ? 23  LEU   A CG    1 
ATOM   172   C  CD1   . LEU   A 1  23  ? -18.078 94.859  -59.207  1.00 41.47  ? 23  LEU   A CD1   1 
ATOM   173   C  CD2   . LEU   A 1  23  ? -19.313 92.960  -60.345  1.00 43.62  ? 23  LEU   A CD2   1 
ATOM   174   N  N     . TYR   A 1  24  ? -22.632 95.577  -58.105  1.00 38.12  ? 24  TYR   A N     1 
ATOM   175   C  CA    . TYR   A 1  24  ? -23.769 96.401  -58.518  1.00 39.97  ? 24  TYR   A CA    1 
ATOM   176   C  C     . TYR   A 1  24  ? -23.718 97.816  -57.950  1.00 50.29  ? 24  TYR   A C     1 
ATOM   177   O  O     . TYR   A 1  24  ? -24.000 98.792  -58.657  1.00 46.18  ? 24  TYR   A O     1 
ATOM   178   C  CB    . TYR   A 1  24  ? -25.081 95.766  -58.067  1.00 37.31  ? 24  TYR   A CB    1 
ATOM   179   C  CG    . TYR   A 1  24  ? -25.509 94.597  -58.881  1.00 39.09  ? 24  TYR   A CG    1 
ATOM   180   C  CD1   . TYR   A 1  24  ? -24.771 94.185  -59.992  1.00 39.44  ? 24  TYR   A CD1   1 
ATOM   181   C  CD2   . TYR   A 1  24  ? -26.661 93.903  -58.559  1.00 37.06  ? 24  TYR   A CD2   1 
ATOM   182   C  CE1   . TYR   A 1  24  ? -25.175 93.089  -60.756  1.00 33.80  ? 24  TYR   A CE1   1 
ATOM   183   C  CE2   . TYR   A 1  24  ? -27.070 92.825  -59.313  1.00 42.04  ? 24  TYR   A CE2   1 
ATOM   184   C  CZ    . TYR   A 1  24  ? -26.327 92.426  -60.410  1.00 29.92  ? 24  TYR   A CZ    1 
ATOM   185   O  OH    . TYR   A 1  24  ? -26.761 91.366  -61.144  1.00 38.34  ? 24  TYR   A OH    1 
ATOM   186   N  N     . CYS   A 1  25  ? -23.386 97.932  -56.658  1.00 44.88  ? 25  CYS   A N     1 
ATOM   187   C  CA    . CYS   A 1  25  ? -23.435 99.232  -55.998  1.00 47.59  ? 25  CYS   A CA    1 
ATOM   188   C  C     . CYS   A 1  25  ? -22.325 100.148 -56.498  1.00 50.21  ? 25  CYS   A C     1 
ATOM   189   O  O     . CYS   A 1  25  ? -22.560 101.333 -56.769  1.00 50.97  ? 25  CYS   A O     1 
ATOM   190   C  CB    . CYS   A 1  25  ? -23.355 99.052  -54.481  1.00 41.72  ? 25  CYS   A CB    1 
ATOM   191   S  SG    . CYS   A 1  25  ? -24.950 98.722  -53.728  1.00 50.20  ? 25  CYS   A SG    1 
ATOM   192   N  N     . LEU   A 1  26  ? -21.102 99.620  -56.601  1.00 45.21  ? 26  LEU   A N     1 
ATOM   193   C  CA    . LEU   A 1  26  ? -20.001 100.374 -57.186  1.00 49.42  ? 26  LEU   A CA    1 
ATOM   194   C  C     . LEU   A 1  26  ? -20.374 100.896 -58.565  1.00 50.20  ? 26  LEU   A C     1 
ATOM   195   O  O     . LEU   A 1  26  ? -20.229 102.090 -58.850  1.00 54.24  ? 26  LEU   A O     1 
ATOM   196   C  CB    . LEU   A 1  26  ? -18.754 99.498  -57.277  1.00 43.45  ? 26  LEU   A CB    1 
ATOM   197   C  CG    . LEU   A 1  26  ? -17.996 99.316  -55.984  1.00 44.97  ? 26  LEU   A CG    1 
ATOM   198   C  CD1   . LEU   A 1  26  ? -18.774 99.953  -54.878  1.00 45.91  ? 26  LEU   A CD1   1 
ATOM   199   C  CD2   . LEU   A 1  26  ? -17.776 97.840  -55.730  1.00 48.72  ? 26  LEU   A CD2   1 
ATOM   200   N  N     . GLU   A 1  27  ? -20.887 100.006 -59.424  1.00 46.04  ? 27  GLU   A N     1 
ATOM   201   C  CA    . GLU   A 1  27  ? -21.135 100.350 -60.822  1.00 50.28  ? 27  GLU   A CA    1 
ATOM   202   C  C     . GLU   A 1  27  ? -22.140 101.490 -60.959  1.00 46.34  ? 27  GLU   A C     1 
ATOM   203   O  O     . GLU   A 1  27  ? -21.947 102.399 -61.772  1.00 45.99  ? 27  GLU   A O     1 
ATOM   204   C  CB    . GLU   A 1  27  ? -21.616 99.113  -61.584  1.00 47.69  ? 27  GLU   A CB    1 
ATOM   205   C  CG    . GLU   A 1  27  ? -20.583 97.987  -61.660  1.00 44.78  ? 27  GLU   A CG    1 
ATOM   206   C  CD    . GLU   A 1  27  ? -21.057 96.816  -62.509  1.00 40.34  ? 27  GLU   A CD    1 
ATOM   207   O  OE1   . GLU   A 1  27  ? -22.251 96.792  -62.878  1.00 47.22  ? 27  GLU   A OE1   1 
ATOM   208   O  OE2   . GLU   A 1  27  ? -20.240 95.920  -62.808  1.00 41.34  ? 27  GLU   A OE2   1 
ATOM   209   N  N     . HIS   A 1  28  ? -23.213 101.466 -60.179  1.00 47.42  ? 28  HIS   A N     1 
ATOM   210   C  CA    . HIS   A 1  28  ? -24.225 102.505 -60.275  1.00 46.52  ? 28  HIS   A CA    1 
ATOM   211   C  C     . HIS   A 1  28  ? -23.952 103.692 -59.364  1.00 47.77  ? 28  HIS   A C     1 
ATOM   212   O  O     . HIS   A 1  28  ? -24.770 104.618 -59.323  1.00 46.35  ? 28  HIS   A O     1 
ATOM   213   C  CB    . HIS   A 1  28  ? -25.605 101.933 -59.950  1.00 41.97  ? 28  HIS   A CB    1 
ATOM   214   C  CG    . HIS   A 1  28  ? -26.083 100.914 -60.928  1.00 36.24  ? 28  HIS   A CG    1 
ATOM   215   N  ND1   . HIS   A 1  28  ? -26.350 101.219 -62.243  1.00 40.91  ? 28  HIS   A ND1   1 
ATOM   216   C  CD2   . HIS   A 1  28  ? -26.358 99.598  -60.783  1.00 33.63  ? 28  HIS   A CD2   1 
ATOM   217   C  CE1   . HIS   A 1  28  ? -26.766 100.133 -62.868  1.00 42.33  ? 28  HIS   A CE1   1 
ATOM   218   N  NE2   . HIS   A 1  28  ? -26.778 99.136  -62.005  1.00 43.30  ? 28  HIS   A NE2   1 
ATOM   219   N  N     . GLY   A 1  29  ? -22.849 103.687 -58.622  1.00 44.20  ? 29  GLY   A N     1 
ATOM   220   C  CA    . GLY   A 1  29  ? -22.579 104.781 -57.699  1.00 41.07  ? 29  GLY   A CA    1 
ATOM   221   C  C     . GLY   A 1  29  ? -23.534 104.889 -56.525  1.00 54.54  ? 29  GLY   A C     1 
ATOM   222   O  O     . GLY   A 1  29  ? -23.977 105.996 -56.187  1.00 59.69  ? 29  GLY   A O     1 
ATOM   223   N  N     . ILE   A 1  30  ? -23.868 103.765 -55.897  1.00 55.90  ? 30  ILE   A N     1 
ATOM   224   C  CA    . ILE   A 1  30  ? -24.685 103.732 -54.693  1.00 49.62  ? 30  ILE   A CA    1 
ATOM   225   C  C     . ILE   A 1  30  ? -23.773 103.406 -53.524  1.00 56.45  ? 30  ILE   A C     1 
ATOM   226   O  O     . ILE   A 1  30  ? -22.924 102.514 -53.623  1.00 59.73  ? 30  ILE   A O     1 
ATOM   227   C  CB    . ILE   A 1  30  ? -25.819 102.696 -54.805  1.00 54.45  ? 30  ILE   A CB    1 
ATOM   228   C  CG1   . ILE   A 1  30  ? -26.799 103.070 -55.923  1.00 44.73  ? 30  ILE   A CG1   1 
ATOM   229   C  CG2   . ILE   A 1  30  ? -26.512 102.527 -53.466  1.00 53.09  ? 30  ILE   A CG2   1 
ATOM   230   C  CD1   . ILE   A 1  30  ? -27.888 102.044 -56.121  1.00 44.02  ? 30  ILE   A CD1   1 
ATOM   231   N  N     . GLN   A 1  31  ? -23.949 104.120 -52.416  1.00 64.88  ? 31  GLN   A N     1 
ATOM   232   C  CA    . GLN   A 1  31  ? -23.070 103.958 -51.267  1.00 68.61  ? 31  GLN   A CA    1 
ATOM   233   C  C     . GLN   A 1  31  ? -23.639 102.950 -50.274  1.00 64.87  ? 31  GLN   A C     1 
ATOM   234   O  O     . GLN   A 1  31  ? -24.826 102.607 -50.322  1.00 61.52  ? 31  GLN   A O     1 
ATOM   235   C  CB    . GLN   A 1  31  ? -22.842 105.309 -50.584  1.00 73.09  ? 31  GLN   A CB    1 
ATOM   236   C  CG    . GLN   A 1  31  ? -21.616 106.073 -51.118  1.00 72.56  ? 31  GLN   A CG    1 
ATOM   237   C  CD    . GLN   A 1  31  ? -21.966 107.433 -51.713  1.00 85.26  ? 31  GLN   A CD    1 
ATOM   238   O  OE1   . GLN   A 1  31  ? -22.926 108.085 -51.289  1.00 85.02  ? 31  GLN   A OE1   1 
ATOM   239   N  NE2   . GLN   A 1  31  ? -21.188 107.865 -52.704  1.00 87.31  ? 31  GLN   A NE2   1 
ATOM   240   N  N     . PRO   A 1  32  ? -22.804 102.465 -49.332  1.00 70.84  ? 32  PRO   A N     1 
ATOM   241   C  CA    . PRO   A 1  32  ? -23.237 101.377 -48.438  1.00 68.37  ? 32  PRO   A CA    1 
ATOM   242   C  C     . PRO   A 1  32  ? -24.538 101.660 -47.703  1.00 68.49  ? 32  PRO   A C     1 
ATOM   243   O  O     . PRO   A 1  32  ? -25.071 100.775 -47.025  1.00 63.64  ? 32  PRO   A O     1 
ATOM   244   C  CB    . PRO   A 1  32  ? -22.071 101.253 -47.453  1.00 52.63  ? 32  PRO   A CB    1 
ATOM   245   C  CG    . PRO   A 1  32  ? -20.898 101.815 -48.185  1.00 56.44  ? 32  PRO   A CG    1 
ATOM   246   C  CD    . PRO   A 1  32  ? -21.435 102.917 -49.030  1.00 58.91  ? 32  PRO   A CD    1 
ATOM   247   N  N     . ASP   A 1  33  ? -25.052 102.888 -47.825  1.00 71.04  ? 33  ASP   A N     1 
ATOM   248   C  CA    . ASP   A 1  33  ? -26.244 103.319 -47.106  1.00 64.63  ? 33  ASP   A CA    1 
ATOM   249   C  C     . ASP   A 1  33  ? -27.392 103.664 -48.043  1.00 69.26  ? 33  ASP   A C     1 
ATOM   250   O  O     . ASP   A 1  33  ? -28.285 104.424 -47.656  1.00 73.46  ? 33  ASP   A O     1 
ATOM   251   C  CB    . ASP   A 1  33  ? -25.925 104.518 -46.212  1.00 59.56  ? 33  ASP   A CB    1 
ATOM   252   C  CG    . ASP   A 1  33  ? -25.635 105.778 -47.002  1.00 72.71  ? 33  ASP   A CG    1 
ATOM   253   O  OD1   . ASP   A 1  33  ? -25.515 105.685 -48.244  1.00 76.13  ? 33  ASP   A OD1   1 
ATOM   254   O  OD2   . ASP   A 1  33  ? -25.527 106.864 -46.381  1.00 67.85  ? 33  ASP   A OD2   1 
ATOM   255   N  N     . GLY   A 1  34  ? -27.375 103.138 -49.273  1.00 62.84  ? 34  GLY   A N     1 
ATOM   256   C  CA    . GLY   A 1  34  ? -28.443 103.353 -50.231  1.00 68.74  ? 34  GLY   A CA    1 
ATOM   257   C  C     . GLY   A 1  34  ? -28.432 104.690 -50.949  1.00 66.99  ? 34  GLY   A C     1 
ATOM   258   O  O     . GLY   A 1  34  ? -29.191 104.861 -51.919  1.00 57.33  ? 34  GLY   A O     1 
ATOM   259   N  N     . GLN   A 1  35  ? -27.593 105.634 -50.523  1.00 67.92  ? 35  GLN   A N     1 
ATOM   260   C  CA    . GLN   A 1  35  ? -27.585 106.974 -51.097  1.00 70.31  ? 35  GLN   A CA    1 
ATOM   261   C  C     . GLN   A 1  35  ? -26.780 107.015 -52.393  1.00 71.63  ? 35  GLN   A C     1 
ATOM   262   O  O     . GLN   A 1  35  ? -25.743 106.358 -52.523  1.00 67.21  ? 35  GLN   A O     1 
ATOM   263   C  CB    . GLN   A 1  35  ? -27.025 107.979 -50.089  1.00 61.85  ? 35  GLN   A CB    1 
ATOM   264   C  CG    . GLN   A 1  35  ? -28.026 108.412 -49.032  1.00 54.84  ? 35  GLN   A CG    1 
ATOM   265   C  CD    . GLN   A 1  35  ? -29.181 109.219 -49.603  1.00 62.95  ? 35  GLN   A CD    1 
ATOM   266   O  OE1   . GLN   A 1  35  ? -30.349 108.857 -49.443  1.00 62.00  ? 35  GLN   A OE1   1 
ATOM   267   N  NE2   . GLN   A 1  35  ? -28.860 110.328 -50.262  1.00 69.31  ? 35  GLN   A NE2   1 
ATOM   268   N  N     . MET   A 1  36  ? -27.259 107.817 -53.344  1.00 73.33  ? 36  MET   A N     1 
ATOM   269   C  CA    . MET   A 1  36  ? -26.774 107.791 -54.722  1.00 58.30  ? 36  MET   A CA    1 
ATOM   270   C  C     . MET   A 1  36  ? -26.781 109.215 -55.261  1.00 61.81  ? 36  MET   A C     1 
ATOM   271   O  O     . MET   A 1  36  ? -27.793 109.681 -55.800  1.00 60.65  ? 36  MET   A O     1 
ATOM   272   C  CB    . MET   A 1  36  ? -27.651 106.867 -55.568  1.00 59.38  ? 36  MET   A CB    1 
ATOM   273   C  CG    . MET   A 1  36  ? -27.279 106.693 -57.041  1.00 63.83  ? 36  MET   A CG    1 
ATOM   274   S  SD    . MET   A 1  36  ? -28.584 105.772 -57.917  1.00 67.41  ? 36  MET   A SD    1 
ATOM   275   C  CE    . MET   A 1  36  ? -27.739 105.358 -59.446  1.00 56.17  ? 36  MET   A CE    1 
ATOM   276   N  N     . PRO   A 1  37  ? -25.666 109.951 -55.117  1.00 71.59  ? 37  PRO   A N     1 
ATOM   277   C  CA    . PRO   A 1  37  ? -25.629 111.334 -55.644  1.00 66.41  ? 37  PRO   A CA    1 
ATOM   278   C  C     . PRO   A 1  37  ? -26.033 111.430 -57.102  1.00 63.49  ? 37  PRO   A C     1 
ATOM   279   O  O     . PRO   A 1  37  ? -26.633 112.433 -57.507  1.00 73.87  ? 37  PRO   A O     1 
ATOM   280   C  CB    . PRO   A 1  37  ? -24.167 111.759 -55.437  1.00 56.50  ? 37  PRO   A CB    1 
ATOM   281   C  CG    . PRO   A 1  37  ? -23.668 110.891 -54.320  1.00 73.32  ? 37  PRO   A CG    1 
ATOM   282   C  CD    . PRO   A 1  37  ? -24.399 109.570 -54.464  1.00 73.51  ? 37  PRO   A CD    1 
ATOM   283   N  N     . SER   A 1  38  ? -25.742 110.397 -57.894  1.00 67.43  ? 38  SER   A N     1 
ATOM   284   C  CA    . SER   A 1  38  ? -26.121 110.370 -59.304  1.00 60.07  ? 38  SER   A CA    1 
ATOM   285   C  C     . SER   A 1  38  ? -27.615 110.607 -59.510  1.00 60.12  ? 38  SER   A C     1 
ATOM   286   O  O     . SER   A 1  38  ? -28.008 111.307 -60.450  1.00 68.20  ? 38  SER   A O     1 
ATOM   287   C  CB    . SER   A 1  38  ? -25.696 109.032 -59.921  1.00 65.32  ? 38  SER   A CB    1 
ATOM   288   O  OG    . SER   A 1  38  ? -26.410 108.741 -61.114  1.00 64.25  ? 38  SER   A OG    1 
ATOM   289   N  N     . ASP   A 1  39  ? -28.468 110.030 -58.662  1.00 61.40  ? 39  ASP   A N     1 
ATOM   290   C  CA    . ASP   A 1  39  ? -29.907 110.119 -58.899  1.00 63.06  ? 39  ASP   A CA    1 
ATOM   291   C  C     . ASP   A 1  39  ? -30.413 111.479 -58.444  1.00 65.78  ? 39  ASP   A C     1 
ATOM   292   O  O     . ASP   A 1  39  ? -30.345 111.802 -57.254  1.00 69.15  ? 39  ASP   A O     1 
ATOM   293   C  CB    . ASP   A 1  39  ? -30.688 109.005 -58.194  1.00 53.72  ? 39  ASP   A CB    1 
ATOM   294   C  CG    . ASP   A 1  39  ? -32.144 108.920 -58.685  1.00 60.91  ? 39  ASP   A CG    1 
ATOM   295   O  OD1   . ASP   A 1  39  ? -32.551 109.812 -59.448  1.00 67.02  ? 39  ASP   A OD1   1 
ATOM   296   O  OD2   . ASP   A 1  39  ? -32.892 107.982 -58.340  1.00 55.08  ? 39  ASP   A OD2   1 
ATOM   297   N  N     . LYS   A 1  40  ? -30.910 112.277 -59.393  1.00 66.16  ? 40  LYS   A N     1 
ATOM   298   C  CA    . LYS   A 1  40  ? -31.618 113.511 -59.086  1.00 59.43  ? 40  LYS   A CA    1 
ATOM   299   C  C     . LYS   A 1  40  ? -33.129 113.321 -59.102  1.00 66.86  ? 40  LYS   A C     1 
ATOM   300   O  O     . LYS   A 1  40  ? -33.868 114.280 -58.858  1.00 75.16  ? 40  LYS   A O     1 
ATOM   301   C  CB    . LYS   A 1  40  ? -31.214 114.627 -60.053  1.00 58.31  ? 40  LYS   A CB    1 
ATOM   302   C  CG    . LYS   A 1  40  ? -29.969 114.343 -60.894  1.00 59.78  ? 40  LYS   A CG    1 
ATOM   303   C  CD    . LYS   A 1  40  ? -28.715 114.146 -60.060  1.00 65.39  ? 40  LYS   A CD    1 
ATOM   304   C  CE    . LYS   A 1  40  ? -28.280 115.425 -59.364  1.00 70.23  ? 40  LYS   A CE    1 
ATOM   305   N  NZ    . LYS   A 1  40  ? -26.916 115.280 -58.758  1.00 62.61  ? 40  LYS   A NZ    1 
ATOM   306   N  N     . THR   A 1  41  ? -33.596 112.099 -59.370  1.00 63.26  ? 41  THR   A N     1 
ATOM   307   C  CA    . THR   A 1  41  ? -34.989 111.697 -59.160  1.00 62.47  ? 41  THR   A CA    1 
ATOM   308   C  C     . THR   A 1  41  ? -35.211 111.264 -57.705  1.00 62.14  ? 41  THR   A C     1 
ATOM   309   O  O     . THR   A 1  41  ? -35.596 110.131 -57.421  1.00 65.75  ? 41  THR   A O     1 
ATOM   310   C  CB    . THR   A 1  41  ? -35.344 110.558 -60.111  1.00 65.39  ? 41  THR   A CB    1 
ATOM   311   O  OG1   . THR   A 1  41  ? -34.771 109.320 -59.629  1.00 67.63  ? 41  THR   A OG1   1 
ATOM   312   C  CG2   . THR   A 1  41  ? -34.797 110.833 -61.490  1.00 56.60  ? 41  THR   A CG2   1 
ATOM   313   N  N     . ILE   A 1  42  ? -34.946 112.182 -56.767  1.00 69.28  ? 42  ILE   A N     1 
ATOM   314   C  CA    . ILE   A 1  42  ? -34.949 111.820 -55.343  1.00 68.90  ? 42  ILE   A CA    1 
ATOM   315   C  C     . ILE   A 1  42  ? -36.329 111.308 -54.952  1.00 57.74  ? 42  ILE   A C     1 
ATOM   316   O  O     . ILE   A 1  42  ? -37.338 112.005 -55.110  1.00 60.14  ? 42  ILE   A O     1 
ATOM   317   C  CB    . ILE   A 1  42  ? -34.528 113.006 -54.463  1.00 59.73  ? 42  ILE   A CB    1 
ATOM   318   C  CG1   . ILE   A 1  42  ? -33.374 113.792 -55.099  1.00 52.94  ? 42  ILE   A CG1   1 
ATOM   319   C  CG2   . ILE   A 1  42  ? -34.125 112.509 -53.094  1.00 47.86  ? 42  ILE   A CG2   1 
ATOM   320   C  CD1   . ILE   A 1  42  ? -32.004 113.498 -54.520  1.00 46.90  ? 42  ILE   A CD1   1 
ATOM   321   N  N     . GLY   A 1  43  ? -36.385 110.086 -54.442  1.00 52.22  ? 43  GLY   A N     1 
ATOM   322   C  CA    . GLY   A 1  43  ? -37.650 109.441 -54.178  1.00 55.46  ? 43  GLY   A CA    1 
ATOM   323   C  C     . GLY   A 1  43  ? -38.126 108.474 -55.249  1.00 60.50  ? 43  GLY   A C     1 
ATOM   324   O  O     . GLY   A 1  43  ? -39.064 107.708 -54.989  1.00 57.69  ? 43  GLY   A O     1 
ATOM   325   N  N     . GLY   A 1  44  ? -37.520 108.469 -56.435  1.00 68.13  ? 44  GLY   A N     1 
ATOM   326   C  CA    . GLY   A 1  44  ? -37.929 107.480 -57.424  1.00 66.97  ? 44  GLY   A CA    1 
ATOM   327   C  C     . GLY   A 1  44  ? -37.280 107.668 -58.780  1.00 59.07  ? 44  GLY   A C     1 
ATOM   328   O  O     . GLY   A 1  44  ? -36.110 108.063 -58.886  1.00 53.65  ? 44  GLY   A O     1 
ATOM   329   N  N     . GLY   A 1  45  ? -38.055 107.344 -59.814  1.00 55.17  ? 45  GLY   A N     1 
ATOM   330   C  CA    . GLY   A 1  45  ? -37.578 107.364 -61.181  1.00 69.23  ? 45  GLY   A CA    1 
ATOM   331   C  C     . GLY   A 1  45  ? -37.785 106.044 -61.903  1.00 64.09  ? 45  GLY   A C     1 
ATOM   332   O  O     . GLY   A 1  45  ? -37.881 104.981 -61.276  1.00 66.36  ? 45  GLY   A O     1 
ATOM   333   N  N     . ASP   A 1  46  ? -37.874 106.102 -63.227  1.00 61.63  ? 46  ASP   A N     1 
ATOM   334   C  CA    . ASP   A 1  46  ? -37.985 104.917 -64.068  1.00 60.44  ? 46  ASP   A CA    1 
ATOM   335   C  C     . ASP   A 1  46  ? -36.707 104.727 -64.885  1.00 59.96  ? 46  ASP   A C     1 
ATOM   336   O  O     . ASP   A 1  46  ? -36.746 104.398 -66.070  1.00 59.71  ? 46  ASP   A O     1 
ATOM   337   C  CB    . ASP   A 1  46  ? -39.210 105.000 -64.977  1.00 57.13  ? 46  ASP   A CB    1 
ATOM   338   C  CG    . ASP   A 1  46  ? -39.195 106.236 -65.855  1.00 71.54  ? 46  ASP   A CG    1 
ATOM   339   O  OD1   . ASP   A 1  46  ? -38.552 107.231 -65.435  1.00 70.27  ? 46  ASP   A OD1   1 
ATOM   340   O  OD2   . ASP   A 1  46  ? -39.807 106.217 -66.957  1.00 63.69  ? 46  ASP   A OD2   1 
ATOM   341   N  N     . ASP   A 1  47  ? -35.557 104.935 -64.250  1.00 49.06  ? 47  ASP   A N     1 
ATOM   342   C  CA    . ASP   A 1  47  ? -34.284 104.763 -64.920  1.00 53.69  ? 47  ASP   A CA    1 
ATOM   343   C  C     . ASP   A 1  47  ? -33.937 103.281 -65.077  1.00 58.38  ? 47  ASP   A C     1 
ATOM   344   O  O     . ASP   A 1  47  ? -34.520 102.401 -64.436  1.00 50.22  ? 47  ASP   A O     1 
ATOM   345   C  CB    . ASP   A 1  47  ? -33.201 105.503 -64.154  1.00 47.88  ? 47  ASP   A CB    1 
ATOM   346   C  CG    . ASP   A 1  47  ? -33.414 106.989 -64.194  1.00 58.92  ? 47  ASP   A CG    1 
ATOM   347   O  OD1   . ASP   A 1  47  ? -33.797 107.466 -65.281  1.00 70.58  ? 47  ASP   A OD1   1 
ATOM   348   O  OD2   . ASP   A 1  47  ? -33.238 107.675 -63.159  1.00 57.25  ? 47  ASP   A OD2   1 
ATOM   349   N  N     . SER   A 1  48  ? -32.976 103.012 -65.967  1.00 50.31  ? 48  SER   A N     1 
ATOM   350   C  CA    . SER   A 1  48  ? -32.614 101.631 -66.262  1.00 52.82  ? 48  SER   A CA    1 
ATOM   351   C  C     . SER   A 1  48  ? -32.158 100.892 -65.004  1.00 53.23  ? 48  SER   A C     1 
ATOM   352   O  O     . SER   A 1  48  ? -32.420 99.689  -64.851  1.00 44.23  ? 48  SER   A O     1 
ATOM   353   C  CB    . SER   A 1  48  ? -31.532 101.586 -67.350  1.00 40.60  ? 48  SER   A CB    1 
ATOM   354   O  OG    . SER   A 1  48  ? -32.123 101.423 -68.635  1.00 48.51  ? 48  SER   A OG    1 
ATOM   355   N  N     . PHE   A 1  49  ? -31.474 101.587 -64.091  1.00 45.16  ? 49  PHE   A N     1 
ATOM   356   C  CA    . PHE   A 1  49  ? -30.967 100.883 -62.927  1.00 47.29  ? 49  PHE   A CA    1 
ATOM   357   C  C     . PHE   A 1  49  ? -32.063 100.577 -61.925  1.00 49.95  ? 49  PHE   A C     1 
ATOM   358   O  O     . PHE   A 1  49  ? -31.884 99.688  -61.087  1.00 48.44  ? 49  PHE   A O     1 
ATOM   359   C  CB    . PHE   A 1  49  ? -29.823 101.657 -62.259  1.00 52.45  ? 49  PHE   A CB    1 
ATOM   360   C  CG    . PHE   A 1  49  ? -30.243 102.901 -61.526  1.00 50.76  ? 49  PHE   A CG    1 
ATOM   361   C  CD1   . PHE   A 1  49  ? -30.930 102.823 -60.321  1.00 54.86  ? 49  PHE   A CD1   1 
ATOM   362   C  CD2   . PHE   A 1  49  ? -29.892 104.149 -62.010  1.00 45.69  ? 49  PHE   A CD2   1 
ATOM   363   C  CE1   . PHE   A 1  49  ? -31.302 103.977 -59.632  1.00 61.46  ? 49  PHE   A CE1   1 
ATOM   364   C  CE2   . PHE   A 1  49  ? -30.255 105.300 -61.330  1.00 59.36  ? 49  PHE   A CE2   1 
ATOM   365   C  CZ    . PHE   A 1  49  ? -30.964 105.214 -60.134  1.00 57.94  ? 49  PHE   A CZ    1 
ATOM   366   N  N     . ASN   A 1  50  ? -33.195 101.273 -62.006  1.00 49.71  ? 50  ASN   A N     1 
ATOM   367   C  CA    . ASN   A 1  50  ? -34.293 100.999 -61.089  1.00 49.66  ? 50  ASN   A CA    1 
ATOM   368   C  C     . ASN   A 1  50  ? -34.916 99.632  -61.322  1.00 48.79  ? 50  ASN   A C     1 
ATOM   369   O  O     . ASN   A 1  50  ? -35.731 99.196  -60.504  1.00 50.43  ? 50  ASN   A O     1 
ATOM   370   C  CB    . ASN   A 1  50  ? -35.365 102.086 -61.185  1.00 45.20  ? 50  ASN   A CB    1 
ATOM   371   C  CG    . ASN   A 1  50  ? -34.922 103.383 -60.568  1.00 51.28  ? 50  ASN   A CG    1 
ATOM   372   O  OD1   . ASN   A 1  50  ? -34.525 104.318 -61.265  1.00 59.52  ? 50  ASN   A OD1   1 
ATOM   373   N  ND2   . ASN   A 1  50  ? -34.975 103.451 -59.246  1.00 64.65  ? 50  ASN   A ND2   1 
ATOM   374   N  N     . THR   A 1  51  ? -34.563 98.938  -62.403  1.00 46.53  ? 51  THR   A N     1 
ATOM   375   C  CA    A THR   A 1  51  ? -35.047 97.571  -62.542  0.64 48.55  ? 51  THR   A CA    1 
ATOM   376   C  CA    B THR   A 1  51  ? -35.013 97.559  -62.560  0.36 48.52  ? 51  THR   A CA    1 
ATOM   377   C  C     . THR   A 1  51  ? -34.551 96.698  -61.392  1.00 47.29  ? 51  THR   A C     1 
ATOM   378   O  O     . THR   A 1  51  ? -35.223 95.726  -61.021  1.00 45.47  ? 51  THR   A O     1 
ATOM   379   C  CB    A THR   A 1  51  ? -34.644 96.988  -63.904  0.64 47.44  ? 51  THR   A CB    1 
ATOM   380   C  CB    B THR   A 1  51  ? -34.498 96.987  -63.884  0.36 47.44  ? 51  THR   A CB    1 
ATOM   381   O  OG1   A THR   A 1  51  ? -33.225 96.806  -63.968  0.64 44.13  ? 51  THR   A OG1   1 
ATOM   382   O  OG1   B THR   A 1  51  ? -34.989 97.779  -64.972  0.36 49.03  ? 51  THR   A OG1   1 
ATOM   383   C  CG2   A THR   A 1  51  ? -35.071 97.923  -65.025  0.64 49.07  ? 51  THR   A CG2   1 
ATOM   384   C  CG2   B THR   A 1  51  ? -34.951 95.546  -64.062  0.36 46.65  ? 51  THR   A CG2   1 
ATOM   385   N  N     . PHE   A 1  52  ? -33.405 97.053  -60.795  1.00 46.27  ? 52  PHE   A N     1 
ATOM   386   C  CA    . PHE   A 1  52  ? -32.808 96.344  -59.670  1.00 45.27  ? 52  PHE   A CA    1 
ATOM   387   C  C     . PHE   A 1  52  ? -32.863 97.107  -58.354  1.00 43.70  ? 52  PHE   A C     1 
ATOM   388   O  O     . PHE   A 1  52  ? -32.600 96.508  -57.316  1.00 43.99  ? 52  PHE   A O     1 
ATOM   389   C  CB    . PHE   A 1  52  ? -31.333 96.005  -59.960  1.00 36.68  ? 52  PHE   A CB    1 
ATOM   390   C  CG    . PHE   A 1  52  ? -31.142 94.802  -60.845  1.00 43.55  ? 52  PHE   A CG    1 
ATOM   391   C  CD1   . PHE   A 1  52  ? -31.846 94.675  -62.040  1.00 42.87  ? 52  PHE   A CD1   1 
ATOM   392   C  CD2   . PHE   A 1  52  ? -30.244 93.799  -60.489  1.00 44.70  ? 52  PHE   A CD2   1 
ATOM   393   C  CE1   . PHE   A 1  52  ? -31.659 93.576  -62.858  1.00 45.04  ? 52  PHE   A CE1   1 
ATOM   394   C  CE2   . PHE   A 1  52  ? -30.050 92.702  -61.296  1.00 35.28  ? 52  PHE   A CE2   1 
ATOM   395   C  CZ    . PHE   A 1  52  ? -30.764 92.579  -62.479  1.00 43.31  ? 52  PHE   A CZ    1 
ATOM   396   N  N     . PHE   A 1  53  ? -33.160 98.405  -58.357  1.00 46.91  ? 53  PHE   A N     1 
ATOM   397   C  CA    . PHE   A 1  53  ? -33.263 99.169  -57.117  1.00 45.37  ? 53  PHE   A CA    1 
ATOM   398   C  C     . PHE   A 1  53  ? -34.546 99.983  -57.121  1.00 52.60  ? 53  PHE   A C     1 
ATOM   399   O  O     . PHE   A 1  53  ? -34.782 100.761 -58.051  1.00 54.53  ? 53  PHE   A O     1 
ATOM   400   C  CB    . PHE   A 1  53  ? -32.087 100.119 -56.921  1.00 32.88  ? 53  PHE   A CB    1 
ATOM   401   C  CG    . PHE   A 1  53  ? -30.760 99.444  -56.853  1.00 48.90  ? 53  PHE   A CG    1 
ATOM   402   C  CD1   . PHE   A 1  53  ? -30.216 98.830  -57.973  1.00 48.78  ? 53  PHE   A CD1   1 
ATOM   403   C  CD2   . PHE   A 1  53  ? -30.029 99.444  -55.677  1.00 53.21  ? 53  PHE   A CD2   1 
ATOM   404   C  CE1   . PHE   A 1  53  ? -28.978 98.219  -57.913  1.00 42.82  ? 53  PHE   A CE1   1 
ATOM   405   C  CE2   . PHE   A 1  53  ? -28.782 98.832  -55.615  1.00 49.33  ? 53  PHE   A CE2   1 
ATOM   406   C  CZ    . PHE   A 1  53  ? -28.258 98.220  -56.737  1.00 43.07  ? 53  PHE   A CZ    1 
ATOM   407   N  N     . SER   A 1  54  ? -35.365 99.812  -56.083  1.00 47.26  ? 54  SER   A N     1 
ATOM   408   C  CA    . SER   A 1  54  ? -36.428 100.764 -55.806  1.00 51.58  ? 54  SER   A CA    1 
ATOM   409   C  C     . SER   A 1  54  ? -35.868 101.889 -54.936  1.00 52.19  ? 54  SER   A C     1 
ATOM   410   O  O     . SER   A 1  54  ? -34.739 101.819 -54.445  1.00 54.13  ? 54  SER   A O     1 
ATOM   411   C  CB    . SER   A 1  54  ? -37.625 100.081 -55.148  1.00 42.62  ? 54  SER   A CB    1 
ATOM   412   O  OG    . SER   A 1  54  ? -37.248 99.408  -53.961  1.00 53.69  ? 54  SER   A OG    1 
ATOM   413   N  N     . GLU   A 1  55  ? -36.652 102.955 -54.768  1.00 55.69  ? 55  GLU   A N     1 
ATOM   414   C  CA    . GLU   A 1  55  ? -36.133 104.175 -54.157  1.00 59.52  ? 55  GLU   A CA    1 
ATOM   415   C  C     . GLU   A 1  55  ? -37.003 104.605 -52.990  1.00 59.36  ? 55  GLU   A C     1 
ATOM   416   O  O     . GLU   A 1  55  ? -38.236 104.572 -53.061  1.00 55.69  ? 55  GLU   A O     1 
ATOM   417   C  CB    . GLU   A 1  55  ? -36.022 105.321 -55.177  1.00 57.96  ? 55  GLU   A CB    1 
ATOM   418   C  CG    . GLU   A 1  55  ? -35.000 105.048 -56.283  1.00 61.15  ? 55  GLU   A CG    1 
ATOM   419   C  CD    . GLU   A 1  55  ? -34.871 106.184 -57.262  1.00 63.84  ? 55  GLU   A CD    1 
ATOM   420   O  OE1   . GLU   A 1  55  ? -34.805 107.348 -56.822  1.00 66.84  ? 55  GLU   A OE1   1 
ATOM   421   O  OE2   . GLU   A 1  55  ? -34.847 105.919 -58.479  1.00 69.32  ? 55  GLU   A OE2   1 
ATOM   422   N  N     . THR   A 1  56  ? -36.343 105.020 -51.922  1.00 64.17  ? 56  THR   A N     1 
ATOM   423   C  CA    . THR   A 1  56  ? -37.001 105.394 -50.682  1.00 63.63  ? 56  THR   A CA    1 
ATOM   424   C  C     . THR   A 1  56  ? -37.099 106.909 -50.551  1.00 61.16  ? 56  THR   A C     1 
ATOM   425   O  O     . THR   A 1  56  ? -36.135 107.629 -50.842  1.00 57.82  ? 56  THR   A O     1 
ATOM   426   C  CB    . THR   A 1  56  ? -36.236 104.810 -49.502  1.00 56.64  ? 56  THR   A CB    1 
ATOM   427   O  OG1   . THR   A 1  56  ? -37.085 103.888 -48.816  1.00 63.99  ? 56  THR   A OG1   1 
ATOM   428   C  CG2   . THR   A 1  56  ? -35.748 105.912 -48.566  1.00 53.84  ? 56  THR   A CG2   1 
ATOM   429   N  N     . GLY   A 1  57  ? -38.271 107.384 -50.110  1.00 56.43  ? 57  GLY   A N     1 
ATOM   430   C  CA    . GLY   A 1  57  ? -38.499 108.797 -49.850  1.00 51.67  ? 57  GLY   A CA    1 
ATOM   431   C  C     . GLY   A 1  57  ? -37.287 109.551 -49.326  1.00 56.49  ? 57  GLY   A C     1 
ATOM   432   O  O     . GLY   A 1  57  ? -37.018 110.675 -49.760  1.00 55.20  ? 57  GLY   A O     1 
ATOM   433   N  N     . ALA   A 1  58  ? -36.537 108.940 -48.406  1.00 57.15  ? 58  ALA   A N     1 
ATOM   434   C  CA    . ALA   A 1  58  ? -35.340 109.553 -47.835  1.00 60.89  ? 58  ALA   A CA    1 
ATOM   435   C  C     . ALA   A 1  58  ? -34.135 109.490 -48.766  1.00 66.54  ? 58  ALA   A C     1 
ATOM   436   O  O     . ALA   A 1  58  ? -33.056 109.965 -48.383  1.00 62.56  ? 58  ALA   A O     1 
ATOM   437   C  CB    . ALA   A 1  58  ? -34.987 108.886 -46.496  1.00 53.51  ? 58  ALA   A CB    1 
ATOM   438   N  N     . GLY   A 1  59  ? -34.286 108.916 -49.960  1.00 60.09  ? 59  GLY   A N     1 
ATOM   439   C  CA    . GLY   A 1  59  ? -33.198 108.806 -50.907  1.00 61.33  ? 59  GLY   A CA    1 
ATOM   440   C  C     . GLY   A 1  59  ? -32.468 107.482 -50.910  1.00 62.57  ? 59  GLY   A C     1 
ATOM   441   O  O     . GLY   A 1  59  ? -31.421 107.371 -51.557  1.00 63.20  ? 59  GLY   A O     1 
ATOM   442   N  N     . LYS   A 1  60  ? -32.976 106.477 -50.211  1.00 66.38  ? 60  LYS   A N     1 
ATOM   443   C  CA    . LYS   A 1  60  ? -32.298 105.192 -50.153  1.00 67.87  ? 60  LYS   A CA    1 
ATOM   444   C  C     . LYS   A 1  60  ? -32.669 104.362 -51.379  1.00 58.66  ? 60  LYS   A C     1 
ATOM   445   O  O     . LYS   A 1  60  ? -33.850 104.243 -51.737  1.00 48.84  ? 60  LYS   A O     1 
ATOM   446   C  CB    . LYS   A 1  60  ? -32.645 104.456 -48.848  1.00 65.05  ? 60  LYS   A CB    1 
ATOM   447   C  CG    . LYS   A 1  60  ? -32.095 103.015 -48.724  1.00 68.50  ? 60  LYS   A CG    1 
ATOM   448   C  CD    . LYS   A 1  60  ? -30.842 102.893 -47.836  1.00 61.94  ? 60  LYS   A CD    1 
ATOM   449   C  CE    . LYS   A 1  60  ? -31.171 103.030 -46.355  1.00 61.59  ? 60  LYS   A CE    1 
ATOM   450   N  NZ    . LYS   A 1  60  ? -32.386 102.255 -45.965  1.00 52.60  ? 60  LYS   A NZ    1 
ATOM   451   N  N     . HIS   A 1  61  ? -31.647 103.819 -52.036  1.00 55.68  ? 61  HIS   A N     1 
ATOM   452   C  CA    . HIS   A 1  61  ? -31.819 102.884 -53.137  1.00 61.34  ? 61  HIS   A CA    1 
ATOM   453   C  C     . HIS   A 1  61  ? -31.609 101.481 -52.595  1.00 55.11  ? 61  HIS   A C     1 
ATOM   454   O  O     . HIS   A 1  61  ? -30.535 101.168 -52.069  1.00 59.76  ? 61  HIS   A O     1 
ATOM   455   C  CB    . HIS   A 1  61  ? -30.851 103.194 -54.278  1.00 61.38  ? 61  HIS   A CB    1 
ATOM   456   C  CG    . HIS   A 1  61  ? -31.056 104.552 -54.863  1.00 58.56  ? 61  HIS   A CG    1 
ATOM   457   N  ND1   . HIS   A 1  61  ? -30.364 105.663 -54.428  1.00 60.71  ? 61  HIS   A ND1   1 
ATOM   458   C  CD2   . HIS   A 1  61  ? -31.916 104.988 -55.811  1.00 57.91  ? 61  HIS   A CD2   1 
ATOM   459   C  CE1   . HIS   A 1  61  ? -30.767 106.719 -55.109  1.00 66.22  ? 61  HIS   A CE1   1 
ATOM   460   N  NE2   . HIS   A 1  61  ? -31.711 106.337 -55.952  1.00 66.61  ? 61  HIS   A NE2   1 
ATOM   461   N  N     . VAL   A 1  62  ? -32.632 100.648 -52.721  1.00 51.33  ? 62  VAL   A N     1 
ATOM   462   C  CA    . VAL   A 1  62  ? -32.729 99.387  -52.000  1.00 59.29  ? 62  VAL   A CA    1 
ATOM   463   C  C     . VAL   A 1  62  ? -32.775 98.240  -53.004  1.00 52.93  ? 62  VAL   A C     1 
ATOM   464   O  O     . VAL   A 1  62  ? -33.695 98.174  -53.826  1.00 44.90  ? 62  VAL   A O     1 
ATOM   465   C  CB    . VAL   A 1  62  ? -33.964 99.348  -51.086  1.00 56.65  ? 62  VAL   A CB    1 
ATOM   466   C  CG1   . VAL   A 1  62  ? -35.231 99.573  -51.907  1.00 50.44  ? 62  VAL   A CG1   1 
ATOM   467   C  CG2   . VAL   A 1  62  ? -34.018 98.017  -50.371  1.00 55.02  ? 62  VAL   A CG2   1 
ATOM   468   N  N     . PRO   A 1  63  ? -31.827 97.309  -52.966  1.00 45.40  ? 63  PRO   A N     1 
ATOM   469   C  CA    . PRO   A 1  63  ? -31.919 96.141  -53.834  1.00 37.77  ? 63  PRO   A CA    1 
ATOM   470   C  C     . PRO   A 1  63  ? -33.313 95.535  -53.797  1.00 44.34  ? 63  PRO   A C     1 
ATOM   471   O  O     . PRO   A 1  63  ? -33.952 95.452  -52.746  1.00 49.95  ? 63  PRO   A O     1 
ATOM   472   C  CB    . PRO   A 1  63  ? -30.871 95.195  -53.252  1.00 35.45  ? 63  PRO   A CB    1 
ATOM   473   C  CG    . PRO   A 1  63  ? -29.844 96.119  -52.688  1.00 42.89  ? 63  PRO   A CG    1 
ATOM   474   C  CD    . PRO   A 1  63  ? -30.599 97.296  -52.151  1.00 46.14  ? 63  PRO   A CD    1 
ATOM   475   N  N     . ARG   A 1  64  ? -33.793 95.136  -54.968  1.00 40.32  ? 64  ARG   A N     1 
ATOM   476   C  CA    . ARG   A 1  64  ? -35.013 94.348  -55.076  1.00 44.37  ? 64  ARG   A CA    1 
ATOM   477   C  C     . ARG   A 1  64  ? -34.726 92.890  -54.784  1.00 42.07  ? 64  ARG   A C     1 
ATOM   478   O  O     . ARG   A 1  64  ? -35.261 91.975  -55.413  1.00 49.71  ? 64  ARG   A O     1 
ATOM   479   C  CB    . ARG   A 1  64  ? -35.631 94.549  -56.461  1.00 44.89  ? 64  ARG   A CB    1 
ATOM   480   C  CG    . ARG   A 1  64  ? -35.813 96.044  -56.809  1.00 45.96  ? 64  ARG   A CG    1 
ATOM   481   C  CD    . ARG   A 1  64  ? -36.350 96.289  -58.231  1.00 50.04  ? 64  ARG   A CD    1 
ATOM   482   N  NE    . ARG   A 1  64  ? -37.761 96.631  -58.188  1.00 51.33  ? 64  ARG   A NE    1 
ATOM   483   C  CZ    . ARG   A 1  64  ? -38.244 97.862  -58.086  1.00 49.84  ? 64  ARG   A CZ    1 
ATOM   484   N  NH1   . ARG   A 1  64  ? -37.468 98.926  -58.214  1.00 45.83  ? 64  ARG   A NH1   1 
ATOM   485   N  NH2   . ARG   A 1  64  ? -39.538 98.027  -57.827  1.00 50.47  ? 64  ARG   A NH2   1 
ATOM   486   N  N     . ALA   A 1  65  ? -33.851 92.672  -53.817  1.00 48.70  ? 65  ALA   A N     1 
ATOM   487   C  CA    . ALA   A 1  65  ? -33.310 91.366  -53.491  1.00 46.20  ? 65  ALA   A CA    1 
ATOM   488   C  C     . ALA   A 1  65  ? -34.059 90.714  -52.333  1.00 44.27  ? 65  ALA   A C     1 
ATOM   489   O  O     . ALA   A 1  65  ? -34.599 91.379  -51.442  1.00 37.60  ? 65  ALA   A O     1 
ATOM   490   C  CB    . ALA   A 1  65  ? -31.826 91.490  -53.143  1.00 38.36  ? 65  ALA   A CB    1 
ATOM   491   N  N     . VAL   A 1  66  ? -34.087 89.391  -52.367  1.00 47.17  ? 66  VAL   A N     1 
ATOM   492   C  CA    A VAL   A 1  66  ? -34.621 88.581  -51.281  0.20 45.88  ? 66  VAL   A CA    1 
ATOM   493   C  CA    B VAL   A 1  66  ? -34.635 88.569  -51.296  0.80 45.93  ? 66  VAL   A CA    1 
ATOM   494   C  C     . VAL   A 1  66  ? -33.636 87.450  -51.031  1.00 43.64  ? 66  VAL   A C     1 
ATOM   495   O  O     . VAL   A 1  66  ? -33.342 86.661  -51.939  1.00 42.44  ? 66  VAL   A O     1 
ATOM   496   C  CB    A VAL   A 1  66  ? -36.024 88.028  -51.585  0.20 43.22  ? 66  VAL   A CB    1 
ATOM   497   C  CB    B VAL   A 1  66  ? -36.013 87.999  -51.674  0.80 43.16  ? 66  VAL   A CB    1 
ATOM   498   C  CG1   A VAL   A 1  66  ? -35.990 87.087  -52.775  0.20 42.49  ? 66  VAL   A CG1   1 
ATOM   499   C  CG1   B VAL   A 1  66  ? -36.263 86.684  -50.977  0.80 42.75  ? 66  VAL   A CG1   1 
ATOM   500   C  CG2   A VAL   A 1  66  ? -36.588 87.322  -50.361  0.20 44.78  ? 66  VAL   A CG2   1 
ATOM   501   C  CG2   B VAL   A 1  66  ? -37.107 89.010  -51.355  0.80 43.84  ? 66  VAL   A CG2   1 
ATOM   502   N  N     . PHE   A 1  67  ? -33.101 87.392  -49.813  1.00 45.69  ? 67  PHE   A N     1 
ATOM   503   C  CA    . PHE   A 1  67  ? -32.232 86.302  -49.382  1.00 46.89  ? 67  PHE   A CA    1 
ATOM   504   C  C     . PHE   A 1  67  ? -33.001 85.316  -48.500  1.00 47.10  ? 67  PHE   A C     1 
ATOM   505   O  O     . PHE   A 1  67  ? -33.916 85.700  -47.761  1.00 44.88  ? 67  PHE   A O     1 
ATOM   506   C  CB    . PHE   A 1  67  ? -31.029 86.818  -48.599  1.00 47.49  ? 67  PHE   A CB    1 
ATOM   507   C  CG    . PHE   A 1  67  ? -30.130 87.742  -49.369  1.00 46.55  ? 67  PHE   A CG    1 
ATOM   508   C  CD1   . PHE   A 1  67  ? -30.600 88.937  -49.871  1.00 48.38  ? 67  PHE   A CD1   1 
ATOM   509   C  CD2   . PHE   A 1  67  ? -28.788 87.440  -49.522  1.00 44.10  ? 67  PHE   A CD2   1 
ATOM   510   C  CE1   . PHE   A 1  67  ? -29.754 89.791  -50.542  1.00 48.21  ? 67  PHE   A CE1   1 
ATOM   511   C  CE2   . PHE   A 1  67  ? -27.946 88.289  -50.186  1.00 41.48  ? 67  PHE   A CE2   1 
ATOM   512   C  CZ    . PHE   A 1  67  ? -28.423 89.461  -50.693  1.00 45.05  ? 67  PHE   A CZ    1 
ATOM   513   N  N     . VAL   A 1  68  ? -32.605 84.037  -48.575  1.00 41.64  ? 68  VAL   A N     1 
ATOM   514   C  CA    A VAL   A 1  68  ? -33.255 82.964  -47.829  0.31 39.59  ? 68  VAL   A CA    1 
ATOM   515   C  CA    B VAL   A 1  68  ? -33.253 82.966  -47.820  0.69 39.61  ? 68  VAL   A CA    1 
ATOM   516   C  C     . VAL   A 1  68  ? -32.293 81.798  -47.629  1.00 41.74  ? 68  VAL   A C     1 
ATOM   517   O  O     . VAL   A 1  68  ? -31.869 81.151  -48.597  1.00 33.45  ? 68  VAL   A O     1 
ATOM   518   C  CB    A VAL   A 1  68  ? -34.536 82.493  -48.542  0.31 38.07  ? 68  VAL   A CB    1 
ATOM   519   C  CB    B VAL   A 1  68  ? -34.548 82.489  -48.505  0.69 38.01  ? 68  VAL   A CB    1 
ATOM   520   C  CG1   A VAL   A 1  68  ? -34.974 81.135  -48.012  0.31 34.71  ? 68  VAL   A CG1   1 
ATOM   521   C  CG1   B VAL   A 1  68  ? -34.343 82.346  -49.989  0.69 39.38  ? 68  VAL   A CG1   1 
ATOM   522   C  CG2   A VAL   A 1  68  ? -35.646 83.518  -48.369  0.31 42.05  ? 68  VAL   A CG2   1 
ATOM   523   C  CG2   B VAL   A 1  68  ? -34.999 81.157  -47.923  0.69 34.47  ? 68  VAL   A CG2   1 
ATOM   524   N  N     . ASP   A 1  69  ? -31.956 81.513  -46.378  1.00 35.82  ? 69  ASP   A N     1 
ATOM   525   C  CA    . ASP   A 1  69  ? -31.163 80.345  -46.028  1.00 38.06  ? 69  ASP   A CA    1 
ATOM   526   C  C     . ASP   A 1  69  ? -31.869 79.589  -44.905  1.00 41.29  ? 69  ASP   A C     1 
ATOM   527   O  O     . ASP   A 1  69  ? -32.423 80.204  -43.990  1.00 34.81  ? 69  ASP   A O     1 
ATOM   528   C  CB    . ASP   A 1  69  ? -29.751 80.756  -45.619  1.00 36.81  ? 69  ASP   A CB    1 
ATOM   529   C  CG    . ASP   A 1  69  ? -28.808 79.593  -45.575  1.00 35.22  ? 69  ASP   A CG    1 
ATOM   530   O  OD1   . ASP   A 1  69  ? -29.287 78.494  -45.870  1.00 41.85  ? 69  ASP   A OD1   1 
ATOM   531   O  OD2   . ASP   A 1  69  ? -27.607 79.765  -45.237  1.00 41.03  ? 69  ASP   A OD2   1 
ATOM   532   N  N     . LEU   A 1  70  ? -31.882 78.254  -44.986  1.00 43.00  ? 70  LEU   A N     1 
ATOM   533   C  CA    . LEU   A 1  70  ? -32.602 77.465  -43.988  1.00 40.68  ? 70  LEU   A CA    1 
ATOM   534   C  C     . LEU   A 1  70  ? -31.876 77.473  -42.649  1.00 47.91  ? 70  LEU   A C     1 
ATOM   535   O  O     . LEU   A 1  70  ? -32.137 76.626  -41.794  1.00 53.66  ? 70  LEU   A O     1 
ATOM   536   C  CB    . LEU   A 1  70  ? -32.801 76.030  -44.459  1.00 29.04  ? 70  LEU   A CB    1 
ATOM   537   C  CG    . LEU   A 1  70  ? -33.808 75.933  -45.588  1.00 45.30  ? 70  LEU   A CG    1 
ATOM   538   C  CD1   . LEU   A 1  70  ? -34.220 74.488  -45.902  1.00 39.01  ? 70  LEU   A CD1   1 
ATOM   539   C  CD2   . LEU   A 1  70  ? -35.016 76.801  -45.251  1.00 53.67  ? 70  LEU   A CD2   1 
ATOM   540   N  N     . GLU   A 1  71  ? -30.957 78.412  -42.460  1.00 44.45  ? 71  GLU   A N     1 
ATOM   541   C  CA    . GLU   A 1  71  ? -30.264 78.572  -41.193  1.00 43.79  ? 71  GLU   A CA    1 
ATOM   542   C  C     . GLU   A 1  71  ? -29.646 79.965  -41.162  1.00 45.45  ? 71  GLU   A C     1 
ATOM   543   O  O     . GLU   A 1  71  ? -29.465 80.594  -42.208  1.00 50.07  ? 71  GLU   A O     1 
ATOM   544   C  CB    . GLU   A 1  71  ? -29.203 77.471  -40.989  1.00 49.20  ? 71  GLU   A CB    1 
ATOM   545   C  CG    . GLU   A 1  71  ? -27.901 77.646  -41.771  1.00 53.30  ? 71  GLU   A CG    1 
ATOM   546   C  CD    . GLU   A 1  71  ? -26.748 78.061  -40.882  1.00 44.85  ? 71  GLU   A CD    1 
ATOM   547   O  OE1   . GLU   A 1  71  ? -26.333 77.260  -40.013  1.00 64.39  ? 71  GLU   A OE1   1 
ATOM   548   O  OE2   . GLU   A 1  71  ? -26.272 79.193  -41.034  1.00 44.51  ? 71  GLU   A OE2   1 
ATOM   549   N  N     . PRO   A 1  72  ? -29.337 80.487  -39.976  1.00 48.09  ? 72  PRO   A N     1 
ATOM   550   C  CA    . PRO   A 1  72  ? -29.148 81.929  -39.844  1.00 42.01  ? 72  PRO   A CA    1 
ATOM   551   C  C     . PRO   A 1  72  ? -27.721 82.399  -39.996  1.00 44.70  ? 72  PRO   A C     1 
ATOM   552   O  O     . PRO   A 1  72  ? -27.505 83.615  -40.101  1.00 44.24  ? 72  PRO   A O     1 
ATOM   553   C  CB    . PRO   A 1  72  ? -29.643 82.185  -38.417  1.00 48.95  ? 72  PRO   A CB    1 
ATOM   554   C  CG    . PRO   A 1  72  ? -29.217 80.932  -37.671  1.00 40.27  ? 72  PRO   A CG    1 
ATOM   555   C  CD    . PRO   A 1  72  ? -29.333 79.802  -38.666  1.00 50.21  ? 72  PRO   A CD    1 
ATOM   556   N  N     . THR   A 1  73  ? -26.756 81.479  -40.002  1.00 47.36  ? 73  THR   A N     1 
ATOM   557   C  CA    . THR   A 1  73  ? -25.358 81.858  -39.803  1.00 48.66  ? 73  THR   A CA    1 
ATOM   558   C  C     . THR   A 1  73  ? -24.869 82.791  -40.899  1.00 51.80  ? 73  THR   A C     1 
ATOM   559   O  O     . THR   A 1  73  ? -24.244 83.823  -40.618  1.00 48.64  ? 73  THR   A O     1 
ATOM   560   C  CB    . THR   A 1  73  ? -24.485 80.607  -39.746  1.00 52.70  ? 73  THR   A CB    1 
ATOM   561   O  OG1   . THR   A 1  73  ? -24.584 80.033  -38.444  1.00 54.05  ? 73  THR   A OG1   1 
ATOM   562   C  CG2   . THR   A 1  73  ? -23.035 80.931  -40.071  1.00 53.98  ? 73  THR   A CG2   1 
ATOM   563   N  N     . VAL   A 1  74  ? -25.140 82.437  -42.159  1.00 50.06  ? 74  VAL   A N     1 
ATOM   564   C  CA    . VAL   A 1  74  ? -24.557 83.173  -43.278  1.00 56.67  ? 74  VAL   A CA    1 
ATOM   565   C  C     . VAL   A 1  74  ? -25.270 84.505  -43.490  1.00 49.02  ? 74  VAL   A C     1 
ATOM   566   O  O     . VAL   A 1  74  ? -24.636 85.563  -43.535  1.00 44.26  ? 74  VAL   A O     1 
ATOM   567   C  CB    . VAL   A 1  74  ? -24.581 82.315  -44.553  1.00 44.79  ? 74  VAL   A CB    1 
ATOM   568   C  CG1   . VAL   A 1  74  ? -23.635 82.892  -45.517  1.00 37.23  ? 74  VAL   A CG1   1 
ATOM   569   C  CG2   . VAL   A 1  74  ? -24.232 80.852  -44.235  1.00 42.94  ? 74  VAL   A CG2   1 
ATOM   570   N  N     . ILE   A 1  75  ? -26.598 84.472  -43.626  1.00 41.82  ? 75  ILE   A N     1 
ATOM   571   C  CA    . ILE   A 1  75  ? -27.358 85.708  -43.772  1.00 44.44  ? 75  ILE   A CA    1 
ATOM   572   C  C     . ILE   A 1  75  ? -27.142 86.631  -42.573  1.00 48.38  ? 75  ILE   A C     1 
ATOM   573   O  O     . ILE   A 1  75  ? -27.156 87.858  -42.713  1.00 42.19  ? 75  ILE   A O     1 
ATOM   574   C  CB    . ILE   A 1  75  ? -28.849 85.376  -43.987  1.00 43.56  ? 75  ILE   A CB    1 
ATOM   575   C  CG1   . ILE   A 1  75  ? -29.058 84.725  -45.367  1.00 38.38  ? 75  ILE   A CG1   1 
ATOM   576   C  CG2   . ILE   A 1  75  ? -29.705 86.624  -43.798  1.00 45.38  ? 75  ILE   A CG2   1 
ATOM   577   C  CD1   . ILE   A 1  75  ? -30.475 84.155  -45.618  1.00 40.29  ? 75  ILE   A CD1   1 
ATOM   578   N  N     . ASP   A 1  76  ? -26.930 86.064  -41.381  1.00 53.89  ? 76  ASP   A N     1 
ATOM   579   C  CA    . ASP   A 1  76  ? -26.607 86.884  -40.217  1.00 56.25  ? 76  ASP   A CA    1 
ATOM   580   C  C     . ASP   A 1  76  ? -25.454 87.820  -40.506  1.00 54.88  ? 76  ASP   A C     1 
ATOM   581   O  O     . ASP   A 1  76  ? -25.379 88.914  -39.936  1.00 58.71  ? 76  ASP   A O     1 
ATOM   582   C  CB    . ASP   A 1  76  ? -26.251 86.005  -39.022  1.00 53.72  ? 76  ASP   A CB    1 
ATOM   583   C  CG    . ASP   A 1  76  ? -27.391 85.848  -38.070  1.00 49.28  ? 76  ASP   A CG    1 
ATOM   584   O  OD1   . ASP   A 1  76  ? -28.376 86.605  -38.210  1.00 45.16  ? 76  ASP   A OD1   1 
ATOM   585   O  OD2   . ASP   A 1  76  ? -27.299 84.962  -37.195  1.00 56.04  ? 76  ASP   A OD2   1 
ATOM   586   N  N     . GLU   A 1  77  ? -24.537 87.396  -41.375  1.00 59.42  ? 77  GLU   A N     1 
ATOM   587   C  CA    . GLU   A 1  77  ? -23.433 88.254  -41.778  1.00 59.82  ? 77  GLU   A CA    1 
ATOM   588   C  C     . GLU   A 1  77  ? -23.916 89.415  -42.643  1.00 58.48  ? 77  GLU   A C     1 
ATOM   589   O  O     . GLU   A 1  77  ? -23.369 90.517  -42.548  1.00 58.83  ? 77  GLU   A O     1 
ATOM   590   C  CB    . GLU   A 1  77  ? -22.375 87.418  -42.505  1.00 65.93  ? 77  GLU   A CB    1 
ATOM   591   C  CG    . GLU   A 1  77  ? -21.858 86.199  -41.708  1.00 62.25  ? 77  GLU   A CG    1 
ATOM   592   C  CD    . GLU   A 1  77  ? -20.518 86.447  -40.999  1.00 78.66  ? 77  GLU   A CD    1 
ATOM   593   O  OE1   . GLU   A 1  77  ? -20.348 87.494  -40.321  1.00 72.43  ? 77  GLU   A OE1   1 
ATOM   594   O  OE2   . GLU   A 1  77  ? -19.627 85.579  -41.126  1.00 78.62  ? 77  GLU   A OE2   1 
ATOM   595   N  N     . VAL   A 1  78  ? -24.944 89.197  -43.470  1.00 54.75  ? 78  VAL   A N     1 
ATOM   596   C  CA    . VAL   A 1  78  ? -25.526 90.294  -44.241  1.00 59.74  ? 78  VAL   A CA    1 
ATOM   597   C  C     . VAL   A 1  78  ? -26.265 91.269  -43.329  1.00 56.96  ? 78  VAL   A C     1 
ATOM   598   O  O     . VAL   A 1  78  ? -26.157 92.488  -43.497  1.00 61.54  ? 78  VAL   A O     1 
ATOM   599   C  CB    . VAL   A 1  78  ? -26.447 89.753  -45.352  1.00 56.17  ? 78  VAL   A CB    1 
ATOM   600   C  CG1   . VAL   A 1  78  ? -27.059 90.902  -46.146  1.00 45.70  ? 78  VAL   A CG1   1 
ATOM   601   C  CG2   . VAL   A 1  78  ? -25.673 88.841  -46.274  1.00 35.16  ? 78  VAL   A CG2   1 
ATOM   602   N  N     . ARG   A 1  79  ? -27.027 90.759  -42.354  1.00 57.85  ? 79  ARG   A N     1 
ATOM   603   C  CA    . ARG   A 1  79  ? -27.705 91.640  -41.399  1.00 55.39  ? 79  ARG   A CA    1 
ATOM   604   C  C     . ARG   A 1  79  ? -26.703 92.524  -40.667  1.00 65.80  ? 79  ARG   A C     1 
ATOM   605   O  O     . ARG   A 1  79  ? -26.917 93.733  -40.504  1.00 60.92  ? 79  ARG   A O     1 
ATOM   606   C  CB    . ARG   A 1  79  ? -28.515 90.824  -40.388  1.00 46.32  ? 79  ARG   A CB    1 
ATOM   607   C  CG    . ARG   A 1  79  ? -29.550 89.888  -41.005  1.00 54.07  ? 79  ARG   A CG    1 
ATOM   608   C  CD    . ARG   A 1  79  ? -30.321 89.100  -39.941  1.00 51.05  ? 79  ARG   A CD    1 
ATOM   609   N  NE    . ARG   A 1  79  ? -31.543 88.517  -40.492  1.00 48.49  ? 79  ARG   A NE    1 
ATOM   610   C  CZ    . ARG   A 1  79  ? -31.859 87.227  -40.445  1.00 54.62  ? 79  ARG   A CZ    1 
ATOM   611   N  NH1   . ARG   A 1  79  ? -31.117 86.355  -39.778  1.00 52.49  ? 79  ARG   A NH1   1 
ATOM   612   N  NH2   . ARG   A 1  79  ? -32.951 86.802  -41.079  1.00 48.59  ? 79  ARG   A NH2   1 
ATOM   613   N  N     . THR   A 1  80  ? -25.601 91.928  -40.212  1.00 60.90  ? 80  THR   A N     1 
ATOM   614   C  CA    . THR   A 1  80  ? -24.592 92.636  -39.439  1.00 61.92  ? 80  THR   A CA    1 
ATOM   615   C  C     . THR   A 1  80  ? -23.528 93.279  -40.311  1.00 65.84  ? 80  THR   A C     1 
ATOM   616   O  O     . THR   A 1  80  ? -22.918 94.269  -39.898  1.00 70.99  ? 80  THR   A O     1 
ATOM   617   C  CB    . THR   A 1  80  ? -23.901 91.673  -38.466  1.00 63.43  ? 80  THR   A CB    1 
ATOM   618   O  OG1   . THR   A 1  80  ? -23.175 90.693  -39.219  1.00 60.98  ? 80  THR   A OG1   1 
ATOM   619   C  CG2   . THR   A 1  80  ? -24.918 90.968  -37.581  1.00 56.77  ? 80  THR   A CG2   1 
ATOM   620   N  N     . GLY   A 1  81  ? -23.294 92.732  -41.501  1.00 70.69  ? 81  GLY   A N     1 
ATOM   621   C  CA    . GLY   A 1  81  ? -22.153 93.084  -42.326  1.00 66.10  ? 81  GLY   A CA    1 
ATOM   622   C  C     . GLY   A 1  81  ? -22.032 94.524  -42.773  1.00 63.88  ? 81  GLY   A C     1 
ATOM   623   O  O     . GLY   A 1  81  ? -22.592 95.438  -42.162  1.00 62.54  ? 81  GLY   A O     1 
ATOM   624   N  N     . THR   A 1  82  ? -21.290 94.734  -43.858  1.00 62.41  ? 82  THR   A N     1 
ATOM   625   C  CA    . THR   A 1  82  ? -20.922 96.082  -44.261  1.00 56.74  ? 82  THR   A CA    1 
ATOM   626   C  C     . THR   A 1  82  ? -22.028 96.792  -45.039  1.00 56.50  ? 82  THR   A C     1 
ATOM   627   O  O     . THR   A 1  82  ? -22.037 98.027  -45.090  1.00 61.63  ? 82  THR   A O     1 
ATOM   628   C  CB    . THR   A 1  82  ? -19.600 96.016  -45.048  1.00 56.81  ? 82  THR   A CB    1 
ATOM   629   O  OG1   . THR   A 1  82  ? -19.734 96.634  -46.331  1.00 59.20  ? 82  THR   A OG1   1 
ATOM   630   C  CG2   . THR   A 1  82  ? -19.167 94.559  -45.234  1.00 66.13  ? 82  THR   A CG2   1 
ATOM   631   N  N     . TYR   A 1  83  ? -22.983 96.052  -45.605  1.00 58.67  ? 83  TYR   A N     1 
ATOM   632   C  CA    . TYR   A 1  83  ? -24.088 96.625  -46.370  1.00 61.83  ? 83  TYR   A CA    1 
ATOM   633   C  C     . TYR   A 1  83  ? -25.427 96.485  -45.641  1.00 66.62  ? 83  TYR   A C     1 
ATOM   634   O  O     . TYR   A 1  83  ? -26.479 96.375  -46.279  1.00 63.29  ? 83  TYR   A O     1 
ATOM   635   C  CB    . TYR   A 1  83  ? -24.167 95.983  -47.762  1.00 61.16  ? 83  TYR   A CB    1 
ATOM   636   C  CG    . TYR   A 1  83  ? -23.109 96.481  -48.741  1.00 61.55  ? 83  TYR   A CG    1 
ATOM   637   C  CD1   . TYR   A 1  83  ? -23.359 97.572  -49.576  1.00 57.39  ? 83  TYR   A CD1   1 
ATOM   638   C  CD2   . TYR   A 1  83  ? -21.857 95.863  -48.825  1.00 57.21  ? 83  TYR   A CD2   1 
ATOM   639   C  CE1   . TYR   A 1  83  ? -22.394 98.029  -50.464  1.00 58.53  ? 83  TYR   A CE1   1 
ATOM   640   C  CE2   . TYR   A 1  83  ? -20.880 96.317  -49.714  1.00 48.04  ? 83  TYR   A CE2   1 
ATOM   641   C  CZ    . TYR   A 1  83  ? -21.156 97.395  -50.527  1.00 54.91  ? 83  TYR   A CZ    1 
ATOM   642   O  OH    . TYR   A 1  83  ? -20.191 97.850  -51.406  1.00 64.64  ? 83  TYR   A OH    1 
ATOM   643   N  N     . ARG   A 1  84  ? -25.402 96.512  -44.301  1.00 70.21  ? 84  ARG   A N     1 
ATOM   644   C  CA    . ARG   A 1  84  ? -26.604 96.242  -43.510  1.00 64.79  ? 84  ARG   A CA    1 
ATOM   645   C  C     . ARG   A 1  84  ? -27.718 97.247  -43.799  1.00 68.68  ? 84  ARG   A C     1 
ATOM   646   O  O     . ARG   A 1  84  ? -28.903 96.882  -43.822  1.00 58.63  ? 84  ARG   A O     1 
ATOM   647   C  CB    . ARG   A 1  84  ? -26.259 96.233  -42.016  1.00 64.48  ? 84  ARG   A CB    1 
ATOM   648   C  CG    . ARG   A 1  84  ? -25.722 97.543  -41.479  1.00 63.89  ? 84  ARG   A CG    1 
ATOM   649   C  CD    . ARG   A 1  84  ? -24.999 97.368  -40.141  1.00 71.06  ? 84  ARG   A CD    1 
ATOM   650   N  NE    . ARG   A 1  84  ? -24.255 98.571  -39.772  1.00 85.42  ? 84  ARG   A NE    1 
ATOM   651   C  CZ    . ARG   A 1  84  ? -23.002 98.824  -40.133  1.00 84.41  ? 84  ARG   A CZ    1 
ATOM   652   N  NH1   . ARG   A 1  84  ? -22.287 97.945  -40.818  1.00 78.95  ? 84  ARG   A NH1   1 
ATOM   653   N  NH2   . ARG   A 1  84  ? -22.454 99.994  -39.806  1.00 84.88  ? 84  ARG   A NH2   1 
ATOM   654   N  N     . GLN   A 1  85  ? -27.361 98.519  -44.020  1.00 69.31  ? 85  GLN   A N     1 
ATOM   655   C  CA    . GLN   A 1  85  ? -28.370 99.541  -44.285  1.00 68.68  ? 85  GLN   A CA    1 
ATOM   656   C  C     . GLN   A 1  85  ? -29.055 99.343  -45.630  1.00 65.44  ? 85  GLN   A C     1 
ATOM   657   O  O     . GLN   A 1  85  ? -30.187 99.803  -45.817  1.00 66.25  ? 85  GLN   A O     1 
ATOM   658   C  CB    . GLN   A 1  85  ? -27.742 100.933 -44.238  1.00 64.39  ? 85  GLN   A CB    1 
ATOM   659   C  CG    . GLN   A 1  85  ? -26.922 101.220 -42.996  1.00 56.73  ? 85  GLN   A CG    1 
ATOM   660   C  CD    . GLN   A 1  85  ? -25.503 101.644 -43.340  1.00 71.07  ? 85  GLN   A CD    1 
ATOM   661   O  OE1   . GLN   A 1  85  ? -25.152 102.822 -43.234  1.00 67.45  ? 85  GLN   A OE1   1 
ATOM   662   N  NE2   . GLN   A 1  85  ? -24.680 100.683 -43.771  1.00 70.16  ? 85  GLN   A NE2   1 
ATOM   663   N  N     . LEU   A 1  86  ? -28.398 98.651  -46.556  1.00 66.08  ? 86  LEU   A N     1 
ATOM   664   C  CA    . LEU   A 1  86  ? -28.908 98.542  -47.915  1.00 65.35  ? 86  LEU   A CA    1 
ATOM   665   C  C     . LEU   A 1  86  ? -30.244 97.798  -47.971  1.00 54.31  ? 86  LEU   A C     1 
ATOM   666   O  O     . LEU   A 1  86  ? -31.150 98.208  -48.701  1.00 62.23  ? 86  LEU   A O     1 
ATOM   667   C  CB    . LEU   A 1  86  ? -27.853 97.859  -48.785  1.00 67.14  ? 86  LEU   A CB    1 
ATOM   668   C  CG    . LEU   A 1  86  ? -27.723 98.192  -50.269  1.00 61.02  ? 86  LEU   A CG    1 
ATOM   669   C  CD1   . LEU   A 1  86  ? -27.654 99.692  -50.476  1.00 57.05  ? 86  LEU   A CD1   1 
ATOM   670   C  CD2   . LEU   A 1  86  ? -26.479 97.513  -50.808  1.00 56.22  ? 86  LEU   A CD2   1 
ATOM   671   N  N     . PHE   A 1  87  ? -30.394 96.715  -47.209  1.00 59.17  ? 87  PHE   A N     1 
ATOM   672   C  CA    . PHE   A 1  87  ? -31.563 95.842  -47.316  1.00 60.43  ? 87  PHE   A CA    1 
ATOM   673   C  C     . PHE   A 1  87  ? -32.576 96.108  -46.205  1.00 65.98  ? 87  PHE   A C     1 
ATOM   674   O  O     . PHE   A 1  87  ? -32.203 96.417  -45.068  1.00 64.14  ? 87  PHE   A O     1 
ATOM   675   C  CB    . PHE   A 1  87  ? -31.149 94.373  -47.252  1.00 47.32  ? 87  PHE   A CB    1 
ATOM   676   C  CG    . PHE   A 1  87  ? -29.992 94.026  -48.137  1.00 57.08  ? 87  PHE   A CG    1 
ATOM   677   C  CD1   . PHE   A 1  87  ? -30.207 93.580  -49.442  1.00 51.73  ? 87  PHE   A CD1   1 
ATOM   678   C  CD2   . PHE   A 1  87  ? -28.682 94.129  -47.665  1.00 48.78  ? 87  PHE   A CD2   1 
ATOM   679   C  CE1   . PHE   A 1  87  ? -29.133 93.248  -50.273  1.00 52.41  ? 87  PHE   A CE1   1 
ATOM   680   C  CE2   . PHE   A 1  87  ? -27.595 93.798  -48.493  1.00 56.49  ? 87  PHE   A CE2   1 
ATOM   681   C  CZ    . PHE   A 1  87  ? -27.821 93.357  -49.800  1.00 49.63  ? 87  PHE   A CZ    1 
ATOM   682   N  N     . HIS   A 1  88  ? -33.915 95.960  -46.542  1.00 65.00  ? 88  HIS   A N     1 
ATOM   683   C  CA    . HIS   A 1  88  ? -34.822 95.999  -45.395  1.00 65.48  ? 88  HIS   A CA    1 
ATOM   684   C  C     . HIS   A 1  88  ? -34.897 94.618  -44.738  1.00 63.97  ? 88  HIS   A C     1 
ATOM   685   O  O     . HIS   A 1  88  ? -34.840 93.593  -45.423  1.00 64.12  ? 88  HIS   A O     1 
ATOM   686   C  CB    . HIS   A 1  88  ? -36.248 96.489  -45.750  1.00 65.42  ? 88  HIS   A CB    1 
ATOM   687   C  CG    . HIS   A 1  88  ? -36.575 96.545  -47.217  1.00 88.35  ? 88  HIS   A CG    1 
ATOM   688   N  ND1   . HIS   A 1  88  ? -36.669 97.734  -47.915  1.00 91.12  ? 88  HIS   A ND1   1 
ATOM   689   C  CD2   . HIS   A 1  88  ? -36.929 95.571  -48.093  1.00 84.02  ? 88  HIS   A CD2   1 
ATOM   690   C  CE1   . HIS   A 1  88  ? -37.015 97.485  -49.169  1.00 74.28  ? 88  HIS   A CE1   1 
ATOM   691   N  NE2   . HIS   A 1  88  ? -37.174 96.180  -49.305  1.00 66.32  ? 88  HIS   A NE2   1 
ATOM   692   N  N     . PRO   A 1  89  ? -34.995 94.566  -43.412  1.00 59.23  ? 89  PRO   A N     1 
ATOM   693   C  CA    . PRO   A 1  89  ? -34.936 93.267  -42.728  1.00 57.25  ? 89  PRO   A CA    1 
ATOM   694   C  C     . PRO   A 1  89  ? -35.857 92.214  -43.308  1.00 52.68  ? 89  PRO   A C     1 
ATOM   695   O  O     . PRO   A 1  89  ? -35.476 91.042  -43.357  1.00 56.33  ? 89  PRO   A O     1 
ATOM   696   C  CB    . PRO   A 1  89  ? -35.317 93.636  -41.291  1.00 52.85  ? 89  PRO   A CB    1 
ATOM   697   C  CG    . PRO   A 1  89  ? -34.700 95.019  -41.122  1.00 57.49  ? 89  PRO   A CG    1 
ATOM   698   C  CD    . PRO   A 1  89  ? -34.930 95.695  -42.463  1.00 62.53  ? 89  PRO   A CD    1 
ATOM   699   N  N     . GLU   A 1  90  ? -37.052 92.590  -43.755  1.00 52.41  ? 90  GLU   A N     1 
ATOM   700   C  CA    . GLU   A 1  90  ? -38.017 91.606  -44.224  1.00 48.87  ? 90  GLU   A CA    1 
ATOM   701   C  C     . GLU   A 1  90  ? -37.530 90.802  -45.422  1.00 56.79  ? 90  GLU   A C     1 
ATOM   702   O  O     . GLU   A 1  90  ? -38.141 89.777  -45.747  1.00 54.15  ? 90  GLU   A O     1 
ATOM   703   C  CB    . GLU   A 1  90  ? -39.322 92.294  -44.596  1.00 66.44  ? 90  GLU   A CB    1 
ATOM   704   C  CG    . GLU   A 1  90  ? -40.044 92.941  -43.445  1.00 76.06  ? 90  GLU   A CG    1 
ATOM   705   C  CD    . GLU   A 1  90  ? -41.061 93.945  -43.926  1.00 100.49 ? 90  GLU   A CD    1 
ATOM   706   O  OE1   . GLU   A 1  90  ? -40.700 94.767  -44.803  1.00 103.66 ? 90  GLU   A OE1   1 
ATOM   707   O  OE2   . GLU   A 1  90  ? -42.216 93.904  -43.443  1.00 101.67 ? 90  GLU   A OE2   1 
ATOM   708   N  N     . GLN   A 1  91  ? -36.471 91.231  -46.100  1.00 57.28  ? 91  GLN   A N     1 
ATOM   709   C  CA    . GLN   A 1  91  ? -36.004 90.514  -47.278  1.00 54.78  ? 91  GLN   A CA    1 
ATOM   710   C  C     . GLN   A 1  91  ? -34.806 89.614  -46.993  1.00 53.46  ? 91  GLN   A C     1 
ATOM   711   O  O     . GLN   A 1  91  ? -34.286 88.984  -47.921  1.00 50.89  ? 91  GLN   A O     1 
ATOM   712   C  CB    . GLN   A 1  91  ? -35.681 91.503  -48.403  1.00 58.24  ? 91  GLN   A CB    1 
ATOM   713   C  CG    . GLN   A 1  91  ? -34.704 92.605  -48.039  1.00 60.64  ? 91  GLN   A CG    1 
ATOM   714   C  CD    . GLN   A 1  91  ? -34.648 93.699  -49.103  1.00 66.63  ? 91  GLN   A CD    1 
ATOM   715   O  OE1   . GLN   A 1  91  ? -34.393 94.863  -48.793  1.00 62.56  ? 91  GLN   A OE1   1 
ATOM   716   N  NE2   . GLN   A 1  91  ? -34.885 93.325  -50.364  1.00 58.42  ? 91  GLN   A NE2   1 
ATOM   717   N  N     . LEU   A 1  92  ? -34.374 89.530  -45.734  1.00 55.01  ? 92  LEU   A N     1 
ATOM   718   C  CA    . LEU   A 1  92  ? -33.322 88.623  -45.276  1.00 44.79  ? 92  LEU   A CA    1 
ATOM   719   C  C     . LEU   A 1  92  ? -33.979 87.564  -44.385  1.00 47.91  ? 92  LEU   A C     1 
ATOM   720   O  O     . LEU   A 1  92  ? -34.082 87.730  -43.170  1.00 55.21  ? 92  LEU   A O     1 
ATOM   721   C  CB    . LEU   A 1  92  ? -32.250 89.399  -44.535  1.00 43.75  ? 92  LEU   A CB    1 
ATOM   722   C  CG    . LEU   A 1  92  ? -31.695 90.626  -45.253  1.00 43.66  ? 92  LEU   A CG    1 
ATOM   723   C  CD1   . LEU   A 1  92  ? -30.516 91.192  -44.489  1.00 38.99  ? 92  LEU   A CD1   1 
ATOM   724   C  CD2   . LEU   A 1  92  ? -31.286 90.264  -46.677  1.00 39.93  ? 92  LEU   A CD2   1 
ATOM   725   N  N     . ILE   A 1  93  ? -34.412 86.467  -44.997  1.00 40.84  ? 93  ILE   A N     1 
ATOM   726   C  CA    . ILE   A 1  93  ? -35.256 85.468  -44.353  1.00 35.39  ? 93  ILE   A CA    1 
ATOM   727   C  C     . ILE   A 1  93  ? -34.414 84.255  -43.962  1.00 43.36  ? 93  ILE   A C     1 
ATOM   728   O  O     . ILE   A 1  93  ? -33.936 83.522  -44.833  1.00 45.38  ? 93  ILE   A O     1 
ATOM   729   C  CB    . ILE   A 1  93  ? -36.396 85.044  -45.285  1.00 35.99  ? 93  ILE   A CB    1 
ATOM   730   C  CG1   . ILE   A 1  93  ? -37.223 86.255  -45.707  1.00 43.16  ? 93  ILE   A CG1   1 
ATOM   731   C  CG2   . ILE   A 1  93  ? -37.269 84.000  -44.645  1.00 39.70  ? 93  ILE   A CG2   1 
ATOM   732   C  CD1   . ILE   A 1  93  ? -37.982 86.018  -47.026  1.00 42.49  ? 93  ILE   A CD1   1 
ATOM   733   N  N     . THR   A 1  94  ? -34.292 83.988  -42.659  1.00 49.73  ? 94  THR   A N     1 
ATOM   734   C  CA    . THR   A 1  94  ? -33.568 82.817  -42.162  1.00 48.03  ? 94  THR   A CA    1 
ATOM   735   C  C     . THR   A 1  94  ? -34.465 81.884  -41.353  1.00 38.59  ? 94  THR   A C     1 
ATOM   736   O  O     . THR   A 1  94  ? -35.312 82.335  -40.578  1.00 45.46  ? 94  THR   A O     1 
ATOM   737   C  CB    . THR   A 1  94  ? -32.388 83.219  -41.282  1.00 47.55  ? 94  THR   A CB    1 
ATOM   738   O  OG1   . THR   A 1  94  ? -32.883 83.712  -40.030  1.00 47.13  ? 94  THR   A OG1   1 
ATOM   739   C  CG2   . THR   A 1  94  ? -31.551 84.297  -41.978  1.00 47.28  ? 94  THR   A CG2   1 
ATOM   740   N  N     . GLY   A 1  95  ? -34.261 80.581  -41.546  1.00 47.67  ? 95  GLY   A N     1 
ATOM   741   C  CA    . GLY   A 1  95  ? -34.728 79.555  -40.635  1.00 47.17  ? 95  GLY   A CA    1 
ATOM   742   C  C     . GLY   A 1  95  ? -33.752 79.305  -39.497  1.00 49.77  ? 95  GLY   A C     1 
ATOM   743   O  O     . GLY   A 1  95  ? -32.927 80.153  -39.142  1.00 46.15  ? 95  GLY   A O     1 
ATOM   744   N  N     . LYS   A 1  96  ? -33.853 78.111  -38.914  1.00 56.35  ? 96  LYS   A N     1 
ATOM   745   C  CA    . LYS   A 1  96  ? -33.136 77.779  -37.687  1.00 47.54  ? 96  LYS   A CA    1 
ATOM   746   C  C     . LYS   A 1  96  ? -32.091 76.690  -37.897  1.00 43.93  ? 96  LYS   A C     1 
ATOM   747   O  O     . LYS   A 1  96  ? -30.918 76.905  -37.589  1.00 54.51  ? 96  LYS   A O     1 
ATOM   748   C  CB    . LYS   A 1  96  ? -34.136 77.364  -36.590  1.00 50.32  ? 96  LYS   A CB    1 
ATOM   749   C  CG    . LYS   A 1  96  ? -35.608 77.263  -37.044  1.00 62.74  ? 96  LYS   A CG    1 
ATOM   750   C  CD    . LYS   A 1  96  ? -35.878 76.061  -37.955  1.00 61.66  ? 96  LYS   A CD    1 
ATOM   751   C  CE    . LYS   A 1  96  ? -37.334 76.026  -38.446  1.00 65.84  ? 96  LYS   A CE    1 
ATOM   752   N  NZ    . LYS   A 1  96  ? -37.707 77.026  -39.519  1.00 56.99  ? 96  LYS   A NZ    1 
ATOM   753   N  N     . GLU   A 1  97  ? -32.490 75.514  -38.377  1.00 41.44  ? 97  GLU   A N     1 
ATOM   754   C  CA    . GLU   A 1  97  ? -31.580 74.436  -38.729  1.00 44.02  ? 97  GLU   A CA    1 
ATOM   755   C  C     . GLU   A 1  97  ? -31.710 74.168  -40.223  1.00 47.72  ? 97  GLU   A C     1 
ATOM   756   O  O     . GLU   A 1  97  ? -32.740 74.472  -40.828  1.00 47.59  ? 97  GLU   A O     1 
ATOM   757   C  CB    . GLU   A 1  97  ? -31.849 73.149  -37.909  1.00 39.82  ? 97  GLU   A CB    1 
ATOM   758   C  CG    . GLU   A 1  97  ? -33.184 72.452  -38.135  1.00 48.05  ? 97  GLU   A CG    1 
ATOM   759   C  CD    . GLU   A 1  97  ? -33.337 71.129  -37.335  1.00 65.13  ? 97  GLU   A CD    1 
ATOM   760   O  OE1   . GLU   A 1  97  ? -32.329 70.563  -36.843  1.00 50.72  ? 97  GLU   A OE1   1 
ATOM   761   O  OE2   . GLU   A 1  97  ? -34.487 70.649  -37.194  1.00 71.14  ? 97  GLU   A OE2   1 
ATOM   762   N  N     . ASP   A 1  98  ? -30.654 73.598  -40.823  1.00 53.59  ? 98  ASP   A N     1 
ATOM   763   C  CA    . ASP   A 1  98  ? -30.500 73.605  -42.276  1.00 39.04  ? 98  ASP   A CA    1 
ATOM   764   C  C     . ASP   A 1  98  ? -30.772 72.233  -42.856  1.00 32.44  ? 98  ASP   A C     1 
ATOM   765   O  O     . ASP   A 1  98  ? -31.129 71.296  -42.146  1.00 44.88  ? 98  ASP   A O     1 
ATOM   766   C  CB    . ASP   A 1  98  ? -29.117 74.119  -42.683  1.00 34.67  ? 98  ASP   A CB    1 
ATOM   767   C  CG    . ASP   A 1  98  ? -28.003 73.126  -42.437  1.00 26.86  ? 98  ASP   A CG    1 
ATOM   768   O  OD1   . ASP   A 1  98  ? -28.096 71.960  -42.869  1.00 31.03  ? 98  ASP   A OD1   1 
ATOM   769   O  OD2   . ASP   A 1  98  ? -26.991 73.547  -41.871  1.00 27.88  ? 98  ASP   A OD2   1 
ATOM   770   N  N     . ALA   A 1  99  ? -30.618 72.127  -44.172  1.00 31.21  ? 99  ALA   A N     1 
ATOM   771   C  CA    . ALA   A 1  99  ? -31.021 70.915  -44.884  1.00 32.45  ? 99  ALA   A CA    1 
ATOM   772   C  C     . ALA   A 1  99  ? -30.014 69.783  -44.761  1.00 33.35  ? 99  ALA   A C     1 
ATOM   773   O  O     . ALA   A 1  99  ? -30.247 68.699  -45.326  1.00 28.35  ? 99  ALA   A O     1 
ATOM   774   C  CB    . ALA   A 1  99  ? -31.258 71.213  -46.365  1.00 21.18  ? 99  ALA   A CB    1 
ATOM   775   N  N     . ALA   A 1  100 ? -28.892 70.005  -44.079  1.00 25.27  ? 100 ALA   A N     1 
ATOM   776   C  CA    . ALA   A 1  100 ? -27.909 68.937  -43.864  1.00 38.22  ? 100 ALA   A CA    1 
ATOM   777   C  C     . ALA   A 1  100 ? -27.383 68.351  -45.175  1.00 32.47  ? 100 ALA   A C     1 
ATOM   778   O  O     . ALA   A 1  100 ? -27.161 67.149  -45.278  1.00 29.86  ? 100 ALA   A O     1 
ATOM   779   C  CB    . ALA   A 1  100 ? -28.500 67.819  -42.994  1.00 27.93  ? 100 ALA   A CB    1 
ATOM   780   N  N     . ASN   A 1  101 ? -27.183 69.192  -46.193  1.00 37.72  ? 101 ASN   A N     1 
ATOM   781   C  CA    . ASN   A 1  101 ? -26.705 68.710  -47.498  1.00 34.44  ? 101 ASN   A CA    1 
ATOM   782   C  C     . ASN   A 1  101 ? -27.619 67.632  -48.076  1.00 30.81  ? 101 ASN   A C     1 
ATOM   783   O  O     . ASN   A 1  101 ? -27.202 66.772  -48.863  1.00 29.31  ? 101 ASN   A O     1 
ATOM   784   C  CB    . ASN   A 1  101 ? -25.277 68.182  -47.392  1.00 36.32  ? 101 ASN   A CB    1 
ATOM   785   C  CG    . ASN   A 1  101 ? -24.298 69.265  -47.099  1.00 36.69  ? 101 ASN   A CG    1 
ATOM   786   O  OD1   . ASN   A 1  101 ? -23.494 69.153  -46.180  1.00 39.86  ? 101 ASN   A OD1   1 
ATOM   787   N  ND2   . ASN   A 1  101 ? -24.367 70.347  -47.875  1.00 38.43  ? 101 ASN   A ND2   1 
ATOM   788   N  N     . ASN   A 1  102 ? -28.876 67.681  -47.689  1.00 32.56  ? 102 ASN   A N     1 
ATOM   789   C  CA    . ASN   A 1  102 ? -29.855 66.667  -48.025  1.00 34.03  ? 102 ASN   A CA    1 
ATOM   790   C  C     . ASN   A 1  102 ? -30.942 67.314  -48.883  1.00 37.47  ? 102 ASN   A C     1 
ATOM   791   O  O     . ASN   A 1  102 ? -31.784 68.055  -48.359  1.00 32.58  ? 102 ASN   A O     1 
ATOM   792   C  CB    . ASN   A 1  102 ? -30.418 66.086  -46.735  1.00 26.00  ? 102 ASN   A CB    1 
ATOM   793   C  CG    . ASN   A 1  102 ? -31.332 64.931  -46.971  1.00 26.96  ? 102 ASN   A CG    1 
ATOM   794   O  OD1   . ASN   A 1  102 ? -31.945 64.813  -48.031  1.00 33.76  ? 102 ASN   A OD1   1 
ATOM   795   N  ND2   . ASN   A 1  102 ? -31.440 64.056  -45.976  1.00 32.92  ? 102 ASN   A ND2   1 
ATOM   796   N  N     . TYR   A 1  103 ? -30.944 67.029  -50.195  1.00 30.76  ? 103 TYR   A N     1 
ATOM   797   C  CA    . TYR   A 1  103 ? -32.003 67.572  -51.046  1.00 32.98  ? 103 TYR   A CA    1 
ATOM   798   C  C     . TYR   A 1  103 ? -33.390 67.328  -50.436  1.00 31.60  ? 103 TYR   A C     1 
ATOM   799   O  O     . TYR   A 1  103 ? -34.158 68.267  -50.217  1.00 27.65  ? 103 TYR   A O     1 
ATOM   800   C  CB    . TYR   A 1  103 ? -31.919 66.988  -52.462  1.00 32.34  ? 103 TYR   A CB    1 
ATOM   801   C  CG    . TYR   A 1  103 ? -33.091 67.410  -53.326  1.00 34.80  ? 103 TYR   A CG    1 
ATOM   802   C  CD1   . TYR   A 1  103 ? -33.083 68.624  -53.991  1.00 30.73  ? 103 TYR   A CD1   1 
ATOM   803   C  CD2   . TYR   A 1  103 ? -34.222 66.606  -53.447  1.00 38.81  ? 103 TYR   A CD2   1 
ATOM   804   C  CE1   . TYR   A 1  103 ? -34.156 69.034  -54.749  1.00 33.54  ? 103 TYR   A CE1   1 
ATOM   805   C  CE2   . TYR   A 1  103 ? -35.304 66.995  -54.223  1.00 34.87  ? 103 TYR   A CE2   1 
ATOM   806   C  CZ    . TYR   A 1  103 ? -35.268 68.217  -54.875  1.00 43.46  ? 103 TYR   A CZ    1 
ATOM   807   O  OH    . TYR   A 1  103 ? -36.345 68.630  -55.652  1.00 43.92  ? 103 TYR   A OH    1 
ATOM   808   N  N     . ALA   A 1  104 ? -33.712 66.067  -50.121  1.00 41.49  ? 104 ALA   A N     1 
ATOM   809   C  CA    . ALA   A 1  104 ? -35.030 65.732  -49.573  1.00 39.02  ? 104 ALA   A CA    1 
ATOM   810   C  C     . ALA   A 1  104 ? -35.379 66.597  -48.370  1.00 35.99  ? 104 ALA   A C     1 
ATOM   811   O  O     . ALA   A 1  104 ? -36.498 67.096  -48.250  1.00 38.11  ? 104 ALA   A O     1 
ATOM   812   C  CB    . ALA   A 1  104 ? -35.083 64.255  -49.188  1.00 35.80  ? 104 ALA   A CB    1 
ATOM   813   N  N     . ARG   A 1  105 ? -34.424 66.808  -47.481  1.00 34.22  ? 105 ARG   A N     1 
ATOM   814   C  CA    . ARG   A 1  105 ? -34.719 67.554  -46.265  1.00 35.39  ? 105 ARG   A CA    1 
ATOM   815   C  C     . ARG   A 1  105 ? -35.017 69.021  -46.553  1.00 38.85  ? 105 ARG   A C     1 
ATOM   816   O  O     . ARG   A 1  105 ? -35.720 69.677  -45.773  1.00 42.19  ? 105 ARG   A O     1 
ATOM   817   C  CB    . ARG   A 1  105 ? -33.543 67.386  -45.299  1.00 31.44  ? 105 ARG   A CB    1 
ATOM   818   C  CG    . ARG   A 1  105 ? -33.545 68.218  -44.080  1.00 28.14  ? 105 ARG   A CG    1 
ATOM   819   C  CD    . ARG   A 1  105 ? -32.384 67.790  -43.202  1.00 28.65  ? 105 ARG   A CD    1 
ATOM   820   N  NE    . ARG   A 1  105 ? -32.511 68.356  -41.862  1.00 44.04  ? 105 ARG   A NE    1 
ATOM   821   C  CZ    . ARG   A 1  105 ? -33.125 67.746  -40.857  1.00 39.03  ? 105 ARG   A CZ    1 
ATOM   822   N  NH1   . ARG   A 1  105 ? -33.617 66.522  -40.991  1.00 27.74  ? 105 ARG   A NH1   1 
ATOM   823   N  NH2   . ARG   A 1  105 ? -33.261 68.384  -39.699  1.00 46.70  ? 105 ARG   A NH2   1 
ATOM   824   N  N     . GLY   A 1  106 ? -34.487 69.557  -47.652  1.00 44.37  ? 106 GLY   A N     1 
ATOM   825   C  CA    . GLY   A 1  106 ? -34.687 70.954  -47.990  1.00 36.49  ? 106 GLY   A CA    1 
ATOM   826   C  C     . GLY   A 1  106 ? -35.938 71.155  -48.827  1.00 39.79  ? 106 GLY   A C     1 
ATOM   827   O  O     . GLY   A 1  106 ? -36.631 72.172  -48.704  1.00 36.71  ? 106 GLY   A O     1 
ATOM   828   N  N     . HIS   A 1  107 ? -36.235 70.185  -49.691  1.00 32.71  ? 107 HIS   A N     1 
ATOM   829   C  CA    . HIS   A 1  107 ? -37.485 70.230  -50.435  1.00 38.65  ? 107 HIS   A CA    1 
ATOM   830   C  C     . HIS   A 1  107 ? -38.677 69.878  -49.544  1.00 51.22  ? 107 HIS   A C     1 
ATOM   831   O  O     . HIS   A 1  107 ? -39.606 70.682  -49.370  1.00 50.97  ? 107 HIS   A O     1 
ATOM   832   C  CB    . HIS   A 1  107 ? -37.429 69.280  -51.623  1.00 38.95  ? 107 HIS   A CB    1 
ATOM   833   C  CG    . HIS   A 1  107 ? -38.531 69.507  -52.610  1.00 48.51  ? 107 HIS   A CG    1 
ATOM   834   N  ND1   . HIS   A 1  107 ? -38.507 70.540  -53.520  1.00 40.76  ? 107 HIS   A ND1   1 
ATOM   835   C  CD2   . HIS   A 1  107 ? -39.702 68.856  -52.805  1.00 45.25  ? 107 HIS   A CD2   1 
ATOM   836   C  CE1   . HIS   A 1  107 ? -39.606 70.502  -54.249  1.00 50.92  ? 107 HIS   A CE1   1 
ATOM   837   N  NE2   . HIS   A 1  107 ? -40.349 69.490  -53.834  1.00 53.77  ? 107 HIS   A NE2   1 
ATOM   838   N  N     . TYR   A 1  108 ? -38.671 68.673  -48.972  1.00 38.62  ? 108 TYR   A N     1 
ATOM   839   C  CA    . TYR   A 1  108 ? -39.874 68.154  -48.342  1.00 32.50  ? 108 TYR   A CA    1 
ATOM   840   C  C     . TYR   A 1  108 ? -39.968 68.613  -46.888  1.00 41.03  ? 108 TYR   A C     1 
ATOM   841   O  O     . TYR   A 1  108 ? -40.859 69.390  -46.535  1.00 48.61  ? 108 TYR   A O     1 
ATOM   842   C  CB    . TYR   A 1  108 ? -39.920 66.622  -48.488  1.00 32.47  ? 108 TYR   A CB    1 
ATOM   843   C  CG    . TYR   A 1  108 ? -40.033 66.136  -49.932  1.00 32.31  ? 108 TYR   A CG    1 
ATOM   844   C  CD1   . TYR   A 1  108 ? -41.227 66.236  -50.646  1.00 43.01  ? 108 TYR   A CD1   1 
ATOM   845   C  CD2   . TYR   A 1  108 ? -38.936 65.630  -50.591  1.00 35.41  ? 108 TYR   A CD2   1 
ATOM   846   C  CE1   . TYR   A 1  108 ? -41.314 65.826  -51.974  1.00 34.65  ? 108 TYR   A CE1   1 
ATOM   847   C  CE2   . TYR   A 1  108 ? -39.011 65.215  -51.897  1.00 38.16  ? 108 TYR   A CE2   1 
ATOM   848   C  CZ    . TYR   A 1  108 ? -40.196 65.305  -52.585  1.00 43.60  ? 108 TYR   A CZ    1 
ATOM   849   O  OH    . TYR   A 1  108 ? -40.222 64.868  -53.890  1.00 37.99  ? 108 TYR   A OH    1 
ATOM   850   N  N     . THR   A 1  109 ? -39.022 68.193  -46.052  1.00 42.26  ? 109 THR   A N     1 
ATOM   851   C  CA    . THR   A 1  109 ? -39.174 68.357  -44.611  1.00 37.70  ? 109 THR   A CA    1 
ATOM   852   C  C     . THR   A 1  109 ? -39.252 69.825  -44.215  1.00 42.74  ? 109 THR   A C     1 
ATOM   853   O  O     . THR   A 1  109 ? -40.201 70.245  -43.545  1.00 51.68  ? 109 THR   A O     1 
ATOM   854   C  CB    . THR   A 1  109 ? -38.034 67.665  -43.869  1.00 39.37  ? 109 THR   A CB    1 
ATOM   855   O  OG1   . THR   A 1  109 ? -38.145 66.241  -44.015  1.00 48.01  ? 109 THR   A OG1   1 
ATOM   856   C  CG2   . THR   A 1  109 ? -38.098 68.023  -42.410  1.00 43.95  ? 109 THR   A CG2   1 
ATOM   857   N  N     . ILE   A 1  110 ? -38.249 70.623  -44.590  1.00 48.82  ? 110 ILE   A N     1 
ATOM   858   C  CA    . ILE   A 1  110 ? -38.204 72.025  -44.162  1.00 50.87  ? 110 ILE   A CA    1 
ATOM   859   C  C     . ILE   A 1  110 ? -38.739 72.989  -45.213  1.00 51.36  ? 110 ILE   A C     1 
ATOM   860   O  O     . ILE   A 1  110 ? -38.979 74.170  -44.893  1.00 47.92  ? 110 ILE   A O     1 
ATOM   861   C  CB    . ILE   A 1  110 ? -36.781 72.451  -43.752  1.00 41.44  ? 110 ILE   A CB    1 
ATOM   862   C  CG1   . ILE   A 1  110 ? -36.083 71.323  -42.997  1.00 43.04  ? 110 ILE   A CG1   1 
ATOM   863   C  CG2   . ILE   A 1  110 ? -36.855 73.680  -42.887  1.00 41.36  ? 110 ILE   A CG2   1 
ATOM   864   C  CD1   . ILE   A 1  110 ? -35.049 71.822  -42.023  1.00 46.43  ? 110 ILE   A CD1   1 
ATOM   865   N  N     . GLY   A 1  111 ? -38.913 72.537  -46.456  1.00 44.04  ? 111 GLY   A N     1 
ATOM   866   C  CA    . GLY   A 1  111 ? -39.620 73.321  -47.445  1.00 54.57  ? 111 GLY   A CA    1 
ATOM   867   C  C     . GLY   A 1  111 ? -40.932 73.789  -46.858  1.00 61.22  ? 111 GLY   A C     1 
ATOM   868   O  O     . GLY   A 1  111 ? -40.996 74.902  -46.322  1.00 62.49  ? 111 GLY   A O     1 
ATOM   869   N  N     . LYS   A 1  112 ? -41.957 72.920  -46.906  1.00 58.14  ? 112 LYS   A N     1 
ATOM   870   C  CA    . LYS   A 1  112 ? -43.268 73.157  -46.309  1.00 53.72  ? 112 LYS   A CA    1 
ATOM   871   C  C     . LYS   A 1  112 ? -43.214 74.195  -45.202  1.00 46.12  ? 112 LYS   A C     1 
ATOM   872   O  O     . LYS   A 1  112 ? -44.041 75.109  -45.145  1.00 62.04  ? 112 LYS   A O     1 
ATOM   873   C  CB    . LYS   A 1  112 ? -43.846 71.856  -45.746  1.00 51.33  ? 112 LYS   A CB    1 
ATOM   874   C  CG    . LYS   A 1  112 ? -44.412 70.916  -46.789  1.00 53.67  ? 112 LYS   A CG    1 
ATOM   875   C  CD    . LYS   A 1  112 ? -45.151 69.741  -46.153  1.00 59.19  ? 112 LYS   A CD    1 
ATOM   876   C  CE    . LYS   A 1  112 ? -46.585 70.079  -45.737  1.00 66.64  ? 112 LYS   A CE    1 
ATOM   877   N  NZ    . LYS   A 1  112 ? -46.700 70.710  -44.385  1.00 65.24  ? 112 LYS   A NZ    1 
ATOM   878   N  N     . GLU   A 1  113 ? -42.213 74.076  -44.343  1.00 41.92  ? 113 GLU   A N     1 
ATOM   879   C  CA    . GLU   A 1  113 ? -42.151 74.871  -43.127  1.00 49.61  ? 113 GLU   A CA    1 
ATOM   880   C  C     . GLU   A 1  113 ? -41.836 76.332  -43.403  1.00 56.88  ? 113 GLU   A C     1 
ATOM   881   O  O     . GLU   A 1  113 ? -42.003 77.168  -42.509  1.00 60.54  ? 113 GLU   A O     1 
ATOM   882   C  CB    . GLU   A 1  113 ? -41.095 74.276  -42.184  1.00 44.02  ? 113 GLU   A CB    1 
ATOM   883   C  CG    . GLU   A 1  113 ? -41.384 74.366  -40.695  1.00 55.48  ? 113 GLU   A CG    1 
ATOM   884   C  CD    . GLU   A 1  113 ? -40.101 74.334  -39.834  1.00 77.94  ? 113 GLU   A CD    1 
ATOM   885   O  OE1   . GLU   A 1  113 ? -39.393 73.284  -39.774  1.00 56.18  ? 113 GLU   A OE1   1 
ATOM   886   O  OE2   . GLU   A 1  113 ? -39.798 75.384  -39.221  1.00 80.57  ? 113 GLU   A OE2   1 
ATOM   887   N  N     . ILE   A 1  114 ? -41.361 76.675  -44.595  1.00 47.96  ? 114 ILE   A N     1 
ATOM   888   C  CA    . ILE   A 1  114 ? -40.914 78.051  -44.772  1.00 53.09  ? 114 ILE   A CA    1 
ATOM   889   C  C     . ILE   A 1  114 ? -41.353 78.586  -46.129  1.00 50.81  ? 114 ILE   A C     1 
ATOM   890   O  O     . ILE   A 1  114 ? -41.228 79.784  -46.407  1.00 47.17  ? 114 ILE   A O     1 
ATOM   891   C  CB    . ILE   A 1  114 ? -39.392 78.154  -44.579  1.00 52.51  ? 114 ILE   A CB    1 
ATOM   892   C  CG1   . ILE   A 1  114 ? -39.032 79.484  -43.933  1.00 46.59  ? 114 ILE   A CG1   1 
ATOM   893   C  CG2   . ILE   A 1  114 ? -38.661 77.984  -45.901  1.00 47.81  ? 114 ILE   A CG2   1 
ATOM   894   C  CD1   . ILE   A 1  114 ? -37.589 79.565  -43.567  1.00 49.04  ? 114 ILE   A CD1   1 
ATOM   895   N  N     . ILE   A 1  115 ? -41.907 77.705  -46.964  1.00 48.97  ? 115 ILE   A N     1 
ATOM   896   C  CA    . ILE   A 1  115 ? -42.318 78.105  -48.307  1.00 53.34  ? 115 ILE   A CA    1 
ATOM   897   C  C     . ILE   A 1  115 ? -43.252 79.307  -48.230  1.00 53.97  ? 115 ILE   A C     1 
ATOM   898   O  O     . ILE   A 1  115 ? -42.925 80.400  -48.705  1.00 58.68  ? 115 ILE   A O     1 
ATOM   899   C  CB    . ILE   A 1  115 ? -42.963 76.922  -49.053  1.00 56.91  ? 115 ILE   A CB    1 
ATOM   900   C  CG1   . ILE   A 1  115 ? -43.223 77.282  -50.519  1.00 51.41  ? 115 ILE   A CG1   1 
ATOM   901   C  CG2   . ILE   A 1  115 ? -44.249 76.465  -48.365  1.00 56.55  ? 115 ILE   A CG2   1 
ATOM   902   C  CD1   . ILE   A 1  115 ? -41.986 77.671  -51.294  1.00 47.50  ? 115 ILE   A CD1   1 
ATOM   903   N  N     . ASP   A 1  116 ? -44.413 79.133  -47.593  1.00 51.66  ? 116 ASP   A N     1 
ATOM   904   C  CA    . ASP   A 1  116 ? -45.405 80.205  -47.569  1.00 55.08  ? 116 ASP   A CA    1 
ATOM   905   C  C     . ASP   A 1  116 ? -44.779 81.535  -47.144  1.00 52.97  ? 116 ASP   A C     1 
ATOM   906   O  O     . ASP   A 1  116 ? -45.019 82.574  -47.770  1.00 49.37  ? 116 ASP   A O     1 
ATOM   907   C  CB    . ASP   A 1  116 ? -46.567 79.819  -46.651  1.00 43.66  ? 116 ASP   A CB    1 
ATOM   908   C  CG    . ASP   A 1  116 ? -47.389 78.658  -47.195  1.00 51.90  ? 116 ASP   A CG    1 
ATOM   909   O  OD1   . ASP   A 1  116 ? -47.137 78.203  -48.327  1.00 57.81  ? 116 ASP   A OD1   1 
ATOM   910   O  OD2   . ASP   A 1  116 ? -48.304 78.195  -46.483  1.00 70.91  ? 116 ASP   A OD2   1 
ATOM   911   N  N     . LEU   A 1  117 ? -43.944 81.519  -46.108  1.00 44.60  ? 117 LEU   A N     1 
ATOM   912   C  CA    . LEU   A 1  117 ? -43.361 82.763  -45.626  1.00 44.95  ? 117 LEU   A CA    1 
ATOM   913   C  C     . LEU   A 1  117 ? -42.470 83.411  -46.682  1.00 63.32  ? 117 LEU   A C     1 
ATOM   914   O  O     . LEU   A 1  117 ? -42.419 84.649  -46.789  1.00 57.40  ? 117 LEU   A O     1 
ATOM   915   C  CB    . LEU   A 1  117 ? -42.569 82.494  -44.361  1.00 40.95  ? 117 LEU   A CB    1 
ATOM   916   C  CG    . LEU   A 1  117 ? -41.451 83.483  -44.094  1.00 50.88  ? 117 LEU   A CG    1 
ATOM   917   C  CD1   . LEU   A 1  117 ? -41.994 84.732  -43.439  1.00 54.70  ? 117 LEU   A CD1   1 
ATOM   918   C  CD2   . LEU   A 1  117 ? -40.415 82.807  -43.217  1.00 61.08  ? 117 LEU   A CD2   1 
ATOM   919   N  N     . VAL   A 1  118 ? -41.738 82.591  -47.451  1.00 53.03  ? 118 VAL   A N     1 
ATOM   920   C  CA    . VAL   A 1  118 ? -40.867 83.120  -48.500  1.00 52.18  ? 118 VAL   A CA    1 
ATOM   921   C  C     . VAL   A 1  118 ? -41.706 83.690  -49.639  1.00 48.25  ? 118 VAL   A C     1 
ATOM   922   O  O     . VAL   A 1  118 ? -41.478 84.814  -50.100  1.00 44.81  ? 118 VAL   A O     1 
ATOM   923   C  CB    . VAL   A 1  118 ? -39.887 82.033  -49.000  1.00 47.00  ? 118 VAL   A CB    1 
ATOM   924   C  CG1   . VAL   A 1  118 ? -39.453 82.318  -50.432  1.00 47.32  ? 118 VAL   A CG1   1 
ATOM   925   C  CG2   . VAL   A 1  118 ? -38.645 81.967  -48.128  1.00 42.06  ? 118 VAL   A CG2   1 
ATOM   926   N  N     . LEU   A 1  119 ? -42.684 82.914  -50.115  1.00 44.80  ? 119 LEU   A N     1 
ATOM   927   C  CA    . LEU   A 1  119 ? -43.617 83.412  -51.114  1.00 42.36  ? 119 LEU   A CA    1 
ATOM   928   C  C     . LEU   A 1  119 ? -44.267 84.713  -50.663  1.00 52.58  ? 119 LEU   A C     1 
ATOM   929   O  O     . LEU   A 1  119 ? -44.505 85.615  -51.475  1.00 53.00  ? 119 LEU   A O     1 
ATOM   930   C  CB    . LEU   A 1  119 ? -44.676 82.357  -51.397  1.00 36.77  ? 119 LEU   A CB    1 
ATOM   931   C  CG    . LEU   A 1  119 ? -44.182 81.156  -52.188  1.00 47.47  ? 119 LEU   A CG    1 
ATOM   932   C  CD1   . LEU   A 1  119 ? -45.297 80.157  -52.330  1.00 45.33  ? 119 LEU   A CD1   1 
ATOM   933   C  CD2   . LEU   A 1  119 ? -43.667 81.615  -53.557  1.00 43.39  ? 119 LEU   A CD2   1 
ATOM   934   N  N     . ASP   A 1  120 ? -44.545 84.837  -49.365  1.00 53.63  ? 120 ASP   A N     1 
ATOM   935   C  CA    . ASP   A 1  120 ? -45.143 86.060  -48.850  1.00 51.09  ? 120 ASP   A CA    1 
ATOM   936   C  C     . ASP   A 1  120 ? -44.195 87.242  -49.000  1.00 56.46  ? 120 ASP   A C     1 
ATOM   937   O  O     . ASP   A 1  120 ? -44.498 88.207  -49.712  1.00 59.58  ? 120 ASP   A O     1 
ATOM   938   C  CB    . ASP   A 1  120 ? -45.536 85.871  -47.391  1.00 61.31  ? 120 ASP   A CB    1 
ATOM   939   C  CG    . ASP   A 1  120 ? -46.937 86.343  -47.109  1.00 70.93  ? 120 ASP   A CG    1 
ATOM   940   O  OD1   . ASP   A 1  120 ? -47.884 85.699  -47.624  1.00 71.46  ? 120 ASP   A OD1   1 
ATOM   941   O  OD2   . ASP   A 1  120 ? -47.082 87.351  -46.378  1.00 71.83  ? 120 ASP   A OD2   1 
ATOM   942   N  N     . ARG   A 1  121 ? -43.041 87.190  -48.319  1.00 58.14  ? 121 ARG   A N     1 
ATOM   943   C  CA    . ARG   A 1  121 ? -42.020 88.233  -48.440  1.00 53.34  ? 121 ARG   A CA    1 
ATOM   944   C  C     . ARG   A 1  121 ? -41.656 88.551  -49.891  1.00 57.85  ? 121 ARG   A C     1 
ATOM   945   O  O     . ARG   A 1  121 ? -41.183 89.659  -50.186  1.00 54.61  ? 121 ARG   A O     1 
ATOM   946   C  CB    . ARG   A 1  121 ? -40.770 87.808  -47.676  1.00 47.45  ? 121 ARG   A CB    1 
ATOM   947   C  CG    . ARG   A 1  121 ? -40.968 87.805  -46.175  1.00 59.45  ? 121 ARG   A CG    1 
ATOM   948   C  CD    . ARG   A 1  121 ? -40.695 89.183  -45.596  1.00 56.80  ? 121 ARG   A CD    1 
ATOM   949   N  NE    . ARG   A 1  121 ? -41.321 89.368  -44.296  1.00 67.16  ? 121 ARG   A NE    1 
ATOM   950   C  CZ    . ARG   A 1  121 ? -41.056 88.628  -43.227  1.00 72.04  ? 121 ARG   A CZ    1 
ATOM   951   N  NH1   . ARG   A 1  121 ? -40.173 87.642  -43.274  1.00 60.23  ? 121 ARG   A NH1   1 
ATOM   952   N  NH2   . ARG   A 1  121 ? -41.705 88.873  -42.088  1.00 55.58  ? 121 ARG   A NH2   1 
ATOM   953   N  N     . ILE   A 1  122 ? -41.849 87.594  -50.800  1.00 53.42  ? 122 ILE   A N     1 
ATOM   954   C  CA    . ILE   A 1  122 ? -41.571 87.815  -52.216  1.00 48.88  ? 122 ILE   A CA    1 
ATOM   955   C  C     . ILE   A 1  122 ? -42.690 88.625  -52.866  1.00 57.54  ? 122 ILE   A C     1 
ATOM   956   O  O     . ILE   A 1  122 ? -42.444 89.695  -53.436  1.00 53.05  ? 122 ILE   A O     1 
ATOM   957   C  CB    . ILE   A 1  122 ? -41.347 86.465  -52.929  1.00 54.17  ? 122 ILE   A CB    1 
ATOM   958   C  CG1   . ILE   A 1  122 ? -39.866 86.055  -52.852  1.00 45.56  ? 122 ILE   A CG1   1 
ATOM   959   C  CG2   . ILE   A 1  122 ? -41.885 86.492  -54.380  1.00 44.49  ? 122 ILE   A CG2   1 
ATOM   960   C  CD1   . ILE   A 1  122 ? -39.578 84.697  -53.481  1.00 44.27  ? 122 ILE   A CD1   1 
ATOM   961   N  N     . ARG   A 1  123 ? -43.937 88.121  -52.791  1.00 60.91  ? 123 ARG   A N     1 
ATOM   962   C  CA    . ARG   A 1  123 ? -45.109 88.904  -53.195  1.00 57.85  ? 123 ARG   A CA    1 
ATOM   963   C  C     . ARG   A 1  123 ? -45.083 90.319  -52.622  1.00 55.84  ? 123 ARG   A C     1 
ATOM   964   O  O     . ARG   A 1  123 ? -45.639 91.241  -53.223  1.00 56.39  ? 123 ARG   A O     1 
ATOM   965   C  CB    . ARG   A 1  123 ? -46.400 88.209  -52.756  1.00 63.04  ? 123 ARG   A CB    1 
ATOM   966   C  CG    . ARG   A 1  123 ? -47.676 88.995  -53.066  1.00 53.70  ? 123 ARG   A CG    1 
ATOM   967   C  CD    . ARG   A 1  123 ? -48.163 88.688  -54.473  1.00 57.87  ? 123 ARG   A CD    1 
ATOM   968   N  NE    . ARG   A 1  123 ? -48.472 87.270  -54.634  1.00 65.15  ? 123 ARG   A NE    1 
ATOM   969   C  CZ    . ARG   A 1  123 ? -48.454 86.611  -55.788  1.00 62.18  ? 123 ARG   A CZ    1 
ATOM   970   N  NH1   . ARG   A 1  123 ? -48.128 87.209  -56.924  1.00 56.88  ? 123 ARG   A NH1   1 
ATOM   971   N  NH2   . ARG   A 1  123 ? -48.754 85.313  -55.800  1.00 65.33  ? 123 ARG   A NH2   1 
ATOM   972   N  N     . LYS   A 1  124 ? -44.440 90.513  -51.472  1.00 52.88  ? 124 LYS   A N     1 
ATOM   973   C  CA    . LYS   A 1  124 ? -44.279 91.858  -50.930  1.00 50.81  ? 124 LYS   A CA    1 
ATOM   974   C  C     . LYS   A 1  124 ? -43.460 92.754  -51.858  1.00 59.02  ? 124 LYS   A C     1 
ATOM   975   O  O     . LYS   A 1  124 ? -43.660 93.978  -51.868  1.00 56.56  ? 124 LYS   A O     1 
ATOM   976   C  CB    . LYS   A 1  124 ? -43.637 91.772  -49.544  1.00 48.59  ? 124 LYS   A CB    1 
ATOM   977   C  CG    . LYS   A 1  124 ? -43.363 93.100  -48.853  1.00 61.53  ? 124 LYS   A CG    1 
ATOM   978   C  CD    . LYS   A 1  124 ? -42.783 92.853  -47.455  1.00 72.44  ? 124 LYS   A CD    1 
ATOM   979   C  CE    . LYS   A 1  124 ? -42.672 94.125  -46.640  1.00 78.40  ? 124 LYS   A CE    1 
ATOM   980   N  NZ    . LYS   A 1  124 ? -41.351 94.795  -46.812  1.00 82.62  ? 124 LYS   A NZ    1 
ATOM   981   N  N     . LEU   A 1  125 ? -42.526 92.178  -52.631  1.00 56.95  ? 125 LEU   A N     1 
ATOM   982   C  CA    . LEU   A 1  125 ? -41.747 92.966  -53.587  1.00 55.30  ? 125 LEU   A CA    1 
ATOM   983   C  C     . LEU   A 1  125 ? -42.454 93.121  -54.932  1.00 54.75  ? 125 LEU   A C     1 
ATOM   984   O  O     . LEU   A 1  125 ? -42.406 94.202  -55.529  1.00 62.17  ? 125 LEU   A O     1 
ATOM   985   C  CB    . LEU   A 1  125 ? -40.360 92.348  -53.814  1.00 52.42  ? 125 LEU   A CB    1 
ATOM   986   C  CG    . LEU   A 1  125 ? -39.246 92.425  -52.761  1.00 49.16  ? 125 LEU   A CG    1 
ATOM   987   C  CD1   . LEU   A 1  125 ? -38.022 91.696  -53.289  1.00 42.97  ? 125 LEU   A CD1   1 
ATOM   988   C  CD2   . LEU   A 1  125 ? -38.875 93.848  -52.342  1.00 39.55  ? 125 LEU   A CD2   1 
ATOM   989   N  N     . ALA   A 1  126 ? -43.100 92.066  -55.438  1.00 47.76  ? 126 ALA   A N     1 
ATOM   990   C  CA    . ALA   A 1  126 ? -43.869 92.201  -56.672  1.00 53.51  ? 126 ALA   A CA    1 
ATOM   991   C  C     . ALA   A 1  126 ? -44.902 93.326  -56.560  1.00 60.91  ? 126 ALA   A C     1 
ATOM   992   O  O     . ALA   A 1  126 ? -44.993 94.189  -57.438  1.00 62.17  ? 126 ALA   A O     1 
ATOM   993   C  CB    . ALA   A 1  126 ? -44.539 90.870  -57.017  1.00 46.09  ? 126 ALA   A CB    1 
ATOM   994   N  N     . ASP   A 1  127 ? -45.677 93.337  -55.467  1.00 65.56  ? 127 ASP   A N     1 
ATOM   995   C  CA    . ASP   A 1  127 ? -46.660 94.394  -55.225  1.00 54.42  ? 127 ASP   A CA    1 
ATOM   996   C  C     . ASP   A 1  127 ? -46.074 95.789  -55.434  1.00 63.30  ? 127 ASP   A C     1 
ATOM   997   O  O     . ASP   A 1  127 ? -46.775 96.689  -55.909  1.00 75.26  ? 127 ASP   A O     1 
ATOM   998   C  CB    . ASP   A 1  127 ? -47.223 94.273  -53.808  1.00 46.39  ? 127 ASP   A CB    1 
ATOM   999   C  CG    . ASP   A 1  127 ? -48.123 93.054  -53.638  1.00 62.83  ? 127 ASP   A CG    1 
ATOM   1000  O  OD1   . ASP   A 1  127 ? -48.439 92.415  -54.671  1.00 66.84  ? 127 ASP   A OD1   1 
ATOM   1001  O  OD2   . ASP   A 1  127 ? -48.510 92.732  -52.481  1.00 54.04  ? 127 ASP   A OD2   1 
ATOM   1002  N  N     . GLN   A 1  128 ? -44.797 95.993  -55.081  1.00 59.10  ? 128 GLN   A N     1 
ATOM   1003  C  CA    . GLN   A 1  128 ? -44.104 97.273  -55.249  1.00 59.63  ? 128 GLN   A CA    1 
ATOM   1004  C  C     . GLN   A 1  128 ? -43.528 97.497  -56.666  1.00 64.90  ? 128 GLN   A C     1 
ATOM   1005  O  O     . GLN   A 1  128 ? -42.748 98.443  -56.851  1.00 52.87  ? 128 GLN   A O     1 
ATOM   1006  C  CB    . GLN   A 1  128 ? -42.972 97.388  -54.221  1.00 64.26  ? 128 GLN   A CB    1 
ATOM   1007  C  CG    . GLN   A 1  128 ? -42.994 98.657  -53.365  1.00 80.10  ? 128 GLN   A CG    1 
ATOM   1008  C  CD    . GLN   A 1  128 ? -41.708 98.840  -52.563  1.00 85.00  ? 128 GLN   A CD    1 
ATOM   1009  O  OE1   . GLN   A 1  128 ? -40.738 98.094  -52.740  1.00 70.38  ? 128 GLN   A OE1   1 
ATOM   1010  N  NE2   . GLN   A 1  128 ? -41.695 99.836  -51.679  1.00 90.77  ? 128 GLN   A NE2   1 
ATOM   1011  N  N     . CYS   A 1  129 ? -43.889 96.668  -57.652  1.00 55.44  ? 129 CYS   A N     1 
ATOM   1012  C  CA    . CYS   A 1  129 ? -43.357 96.735  -59.012  1.00 59.35  ? 129 CYS   A CA    1 
ATOM   1013  C  C     . CYS   A 1  129 ? -44.447 97.160  -59.998  1.00 63.18  ? 129 CYS   A C     1 
ATOM   1014  O  O     . CYS   A 1  129 ? -45.530 96.557  -60.032  1.00 55.93  ? 129 CYS   A O     1 
ATOM   1015  C  CB    . CYS   A 1  129 ? -42.785 95.372  -59.446  1.00 61.05  ? 129 CYS   A CB    1 
ATOM   1016  S  SG    . CYS   A 1  129 ? -41.386 94.683  -58.468  1.00 60.84  ? 129 CYS   A SG    1 
ATOM   1017  N  N     . THR   A 1  130 ? -44.142 98.166  -60.833  1.00 56.78  ? 130 THR   A N     1 
ATOM   1018  C  CA    . THR   A 1  130 ? -45.086 98.598  -61.874  1.00 46.79  ? 130 THR   A CA    1 
ATOM   1019  C  C     . THR   A 1  130 ? -45.223 97.564  -62.991  1.00 49.99  ? 130 THR   A C     1 
ATOM   1020  O  O     . THR   A 1  130 ? -46.308 97.390  -63.552  1.00 59.46  ? 130 THR   A O     1 
ATOM   1021  C  CB    . THR   A 1  130 ? -44.660 99.950  -62.458  1.00 45.32  ? 130 THR   A CB    1 
ATOM   1022  O  OG1   . THR   A 1  130 ? -43.524 99.790  -63.327  1.00 56.21  ? 130 THR   A OG1   1 
ATOM   1023  C  CG2   . THR   A 1  130 ? -44.276 100.909 -61.347  1.00 52.22  ? 130 THR   A CG2   1 
ATOM   1024  N  N     . GLY   A 1  131 ? -44.141 96.874  -63.340  1.00 56.07  ? 131 GLY   A N     1 
ATOM   1025  C  CA    . GLY   A 1  131 ? -44.172 95.925  -64.434  1.00 46.92  ? 131 GLY   A CA    1 
ATOM   1026  C  C     . GLY   A 1  131 ? -43.125 94.840  -64.276  1.00 58.39  ? 131 GLY   A C     1 
ATOM   1027  O  O     . GLY   A 1  131 ? -42.271 94.641  -65.146  1.00 55.24  ? 131 GLY   A O     1 
ATOM   1028  N  N     . LEU   A 1  132 ? -43.189 94.138  -63.148  1.00 60.91  ? 132 LEU   A N     1 
ATOM   1029  C  CA    . LEU   A 1  132 ? -42.345 92.979  -62.890  1.00 55.47  ? 132 LEU   A CA    1 
ATOM   1030  C  C     . LEU   A 1  132 ? -42.237 92.066  -64.106  1.00 49.59  ? 132 LEU   A C     1 
ATOM   1031  O  O     . LEU   A 1  132 ? -43.241 91.687  -64.711  1.00 47.69  ? 132 LEU   A O     1 
ATOM   1032  C  CB    . LEU   A 1  132 ? -42.917 92.194  -61.711  1.00 57.23  ? 132 LEU   A CB    1 
ATOM   1033  C  CG    . LEU   A 1  132 ? -42.231 90.847  -61.510  1.00 53.62  ? 132 LEU   A CG    1 
ATOM   1034  C  CD1   . LEU   A 1  132 ? -40.854 91.077  -60.891  1.00 51.48  ? 132 LEU   A CD1   1 
ATOM   1035  C  CD2   . LEU   A 1  132 ? -43.079 89.910  -60.681  1.00 34.85  ? 132 LEU   A CD2   1 
ATOM   1036  N  N     . GLN   A 1  133 ? -41.010 91.675  -64.433  1.00 44.79  ? 133 GLN   A N     1 
ATOM   1037  C  CA    . GLN   A 1  133 ? -40.792 90.736  -65.518  1.00 49.19  ? 133 GLN   A CA    1 
ATOM   1038  C  C     . GLN   A 1  133 ? -40.400 89.340  -65.067  1.00 50.84  ? 133 GLN   A C     1 
ATOM   1039  O  O     . GLN   A 1  133 ? -40.605 88.382  -65.822  1.00 42.31  ? 133 GLN   A O     1 
ATOM   1040  C  CB    . GLN   A 1  133 ? -39.708 91.258  -66.464  1.00 48.43  ? 133 GLN   A CB    1 
ATOM   1041  C  CG    . GLN   A 1  133 ? -38.475 91.821  -65.785  1.00 46.62  ? 133 GLN   A CG    1 
ATOM   1042  C  CD    . GLN   A 1  133 ? -37.635 92.597  -66.784  1.00 51.28  ? 133 GLN   A CD    1 
ATOM   1043  O  OE1   . GLN   A 1  133 ? -37.243 92.059  -67.824  1.00 55.85  ? 133 GLN   A OE1   1 
ATOM   1044  N  NE2   . GLN   A 1  133 ? -37.395 93.879  -66.500  1.00 48.26  ? 133 GLN   A NE2   1 
ATOM   1045  N  N     . GLY   A 1  134 ? -39.832 89.194  -63.890  1.00 58.73  ? 134 GLY   A N     1 
ATOM   1046  C  CA    . GLY   A 1  134 ? -39.397 87.886  -63.467  1.00 53.28  ? 134 GLY   A CA    1 
ATOM   1047  C  C     . GLY   A 1  134 ? -38.260 87.977  -62.472  1.00 50.64  ? 134 GLY   A C     1 
ATOM   1048  O  O     . GLY   A 1  134 ? -37.991 89.038  -61.888  1.00 44.13  ? 134 GLY   A O     1 
ATOM   1049  N  N     . PHE   A 1  135 ? -37.604 86.829  -62.307  1.00 39.80  ? 135 PHE   A N     1 
ATOM   1050  C  CA    . PHE   A 1  135 ? -36.749 86.589  -61.160  1.00 41.20  ? 135 PHE   A CA    1 
ATOM   1051  C  C     . PHE   A 1  135 ? -35.387 86.102  -61.612  1.00 37.77  ? 135 PHE   A C     1 
ATOM   1052  O  O     . PHE   A 1  135 ? -35.270 85.355  -62.586  1.00 36.97  ? 135 PHE   A O     1 
ATOM   1053  C  CB    . PHE   A 1  135 ? -37.381 85.550  -60.200  1.00 38.88  ? 135 PHE   A CB    1 
ATOM   1054  C  CG    . PHE   A 1  135 ? -38.812 85.844  -59.836  1.00 35.28  ? 135 PHE   A CG    1 
ATOM   1055  C  CD1   . PHE   A 1  135 ? -39.120 86.848  -58.923  1.00 37.55  ? 135 PHE   A CD1   1 
ATOM   1056  C  CD2   . PHE   A 1  135 ? -39.848 85.125  -60.415  1.00 41.69  ? 135 PHE   A CD2   1 
ATOM   1057  C  CE1   . PHE   A 1  135 ? -40.444 87.128  -58.602  1.00 46.44  ? 135 PHE   A CE1   1 
ATOM   1058  C  CE2   . PHE   A 1  135 ? -41.184 85.399  -60.093  1.00 45.34  ? 135 PHE   A CE2   1 
ATOM   1059  C  CZ    . PHE   A 1  135 ? -41.483 86.395  -59.189  1.00 38.26  ? 135 PHE   A CZ    1 
ATOM   1060  N  N     . LEU   A 1  136 ? -34.367 86.546  -60.902  1.00 36.80  ? 136 LEU   A N     1 
ATOM   1061  C  CA    A LEU   A 1  136 ? -33.023 85.998  -61.014  0.64 41.15  ? 136 LEU   A CA    1 
ATOM   1062  C  CA    B LEU   A 1  136 ? -33.021 86.000  -61.015  0.36 41.07  ? 136 LEU   A CA    1 
ATOM   1063  C  C     . LEU   A 1  136 ? -32.758 85.178  -59.754  1.00 37.93  ? 136 LEU   A C     1 
ATOM   1064  O  O     . LEU   A 1  136 ? -32.674 85.736  -58.655  1.00 43.62  ? 136 LEU   A O     1 
ATOM   1065  C  CB    A LEU   A 1  136 ? -31.995 87.115  -61.188  0.64 41.02  ? 136 LEU   A CB    1 
ATOM   1066  C  CB    B LEU   A 1  136 ? -31.997 87.121  -61.188  0.36 40.95  ? 136 LEU   A CB    1 
ATOM   1067  C  CG    A LEU   A 1  136 ? -31.913 87.828  -62.541  0.64 38.59  ? 136 LEU   A CG    1 
ATOM   1068  C  CG    B LEU   A 1  136 ? -32.091 87.995  -62.445  0.36 38.67  ? 136 LEU   A CG    1 
ATOM   1069  C  CD1   A LEU   A 1  136 ? -32.509 86.974  -63.652  0.64 39.62  ? 136 LEU   A CD1   1 
ATOM   1070  C  CD1   B LEU   A 1  136 ? -33.358 88.833  -62.454  0.36 40.54  ? 136 LEU   A CD1   1 
ATOM   1071  C  CD2   A LEU   A 1  136 ? -32.562 89.199  -62.485  0.64 38.97  ? 136 LEU   A CD2   1 
ATOM   1072  C  CD2   B LEU   A 1  136 ? -30.865 88.889  -62.577  0.36 37.53  ? 136 LEU   A CD2   1 
ATOM   1073  N  N     . VAL   A 1  137 ? -32.643 83.856  -59.904  1.00 36.09  ? 137 VAL   A N     1 
ATOM   1074  C  CA    . VAL   A 1  137 ? -32.544 82.935  -58.756  1.00 39.00  ? 137 VAL   A CA    1 
ATOM   1075  C  C     . VAL   A 1  137 ? -31.134 82.349  -58.674  1.00 39.23  ? 137 VAL   A C     1 
ATOM   1076  O  O     . VAL   A 1  137 ? -30.720 81.571  -59.549  1.00 35.27  ? 137 VAL   A O     1 
ATOM   1077  C  CB    . VAL   A 1  137 ? -33.595 81.817  -58.835  1.00 36.90  ? 137 VAL   A CB    1 
ATOM   1078  C  CG1   . VAL   A 1  137 ? -33.403 80.820  -57.695  1.00 37.84  ? 137 VAL   A CG1   1 
ATOM   1079  C  CG2   . VAL   A 1  137 ? -34.990 82.414  -58.789  1.00 34.69  ? 137 VAL   A CG2   1 
ATOM   1080  N  N     . PHE   A 1  138 ? -30.416 82.699  -57.595  1.00 38.85  ? 138 PHE   A N     1 
ATOM   1081  C  CA    . PHE   A 1  138 ? -29.026 82.304  -57.338  1.00 37.09  ? 138 PHE   A CA    1 
ATOM   1082  C  C     . PHE   A 1  138 ? -28.975 81.158  -56.332  1.00 39.54  ? 138 PHE   A C     1 
ATOM   1083  O  O     . PHE   A 1  138 ? -29.581 81.249  -55.263  1.00 42.48  ? 138 PHE   A O     1 
ATOM   1084  C  CB    . PHE   A 1  138 ? -28.219 83.475  -56.765  1.00 34.54  ? 138 PHE   A CB    1 
ATOM   1085  C  CG    . PHE   A 1  138 ? -28.069 84.633  -57.700  1.00 44.12  ? 138 PHE   A CG    1 
ATOM   1086  C  CD1   . PHE   A 1  138 ? -29.171 85.417  -58.050  1.00 41.48  ? 138 PHE   A CD1   1 
ATOM   1087  C  CD2   . PHE   A 1  138 ? -26.825 84.959  -58.223  1.00 40.87  ? 138 PHE   A CD2   1 
ATOM   1088  C  CE1   . PHE   A 1  138 ? -29.036 86.494  -58.904  1.00 34.66  ? 138 PHE   A CE1   1 
ATOM   1089  C  CE2   . PHE   A 1  138 ? -26.683 86.043  -59.090  1.00 43.28  ? 138 PHE   A CE2   1 
ATOM   1090  C  CZ    . PHE   A 1  138 ? -27.791 86.811  -59.425  1.00 40.43  ? 138 PHE   A CZ    1 
ATOM   1091  N  N     . HIS   A 1  139 ? -28.206 80.115  -56.631  1.00 30.76  ? 139 HIS   A N     1 
ATOM   1092  C  CA    . HIS   A 1  139 ? -28.197 78.977  -55.727  1.00 30.69  ? 139 HIS   A CA    1 
ATOM   1093  C  C     . HIS   A 1  139 ? -27.124 77.974  -56.134  1.00 39.02  ? 139 HIS   A C     1 
ATOM   1094  O  O     . HIS   A 1  139 ? -26.664 77.951  -57.285  1.00 34.07  ? 139 HIS   A O     1 
ATOM   1095  C  CB    . HIS   A 1  139 ? -29.570 78.292  -55.698  1.00 35.36  ? 139 HIS   A CB    1 
ATOM   1096  C  CG    . HIS   A 1  139 ? -29.939 77.593  -56.975  1.00 32.60  ? 139 HIS   A CG    1 
ATOM   1097  N  ND1   . HIS   A 1  139 ? -29.731 76.244  -57.173  1.00 25.95  ? 139 HIS   A ND1   1 
ATOM   1098  C  CD2   . HIS   A 1  139 ? -30.524 78.051  -58.110  1.00 30.08  ? 139 HIS   A CD2   1 
ATOM   1099  C  CE1   . HIS   A 1  139 ? -30.164 75.900  -58.374  1.00 30.46  ? 139 HIS   A CE1   1 
ATOM   1100  N  NE2   . HIS   A 1  139 ? -30.651 76.977  -58.963  1.00 30.06  ? 139 HIS   A NE2   1 
ATOM   1101  N  N     . SER   A 1  140 ? -26.754 77.122  -55.175  1.00 34.78  ? 140 SER   A N     1 
ATOM   1102  C  CA    . SER   A 1  140 ? -25.874 75.991  -55.427  1.00 29.34  ? 140 SER   A CA    1 
ATOM   1103  C  C     . SER   A 1  140 ? -26.715 74.777  -55.794  1.00 32.85  ? 140 SER   A C     1 
ATOM   1104  O  O     . SER   A 1  140 ? -27.872 74.667  -55.388  1.00 31.03  ? 140 SER   A O     1 
ATOM   1105  C  CB    . SER   A 1  140 ? -25.013 75.670  -54.207  1.00 31.27  ? 140 SER   A CB    1 
ATOM   1106  O  OG    . SER   A 1  140 ? -25.755 74.962  -53.205  1.00 30.68  ? 140 SER   A OG    1 
ATOM   1107  N  N     . PHE   A 1  141 ? -26.131 73.895  -56.620  1.00 33.46  ? 141 PHE   A N     1 
ATOM   1108  C  CA    . PHE   A 1  141 ? -26.687 72.573  -56.888  1.00 29.22  ? 141 PHE   A CA    1 
ATOM   1109  C  C     . PHE   A 1  141 ? -26.534 71.613  -55.701  1.00 29.28  ? 141 PHE   A C     1 
ATOM   1110  O  O     . PHE   A 1  141 ? -27.362 70.724  -55.532  1.00 23.71  ? 141 PHE   A O     1 
ATOM   1111  C  CB    . PHE   A 1  141 ? -25.984 71.939  -58.089  1.00 33.24  ? 141 PHE   A CB    1 
ATOM   1112  C  CG    . PHE   A 1  141 ? -26.557 72.301  -59.412  1.00 27.10  ? 141 PHE   A CG    1 
ATOM   1113  C  CD1   . PHE   A 1  141 ? -27.590 73.213  -59.523  1.00 37.03  ? 141 PHE   A CD1   1 
ATOM   1114  C  CD2   . PHE   A 1  141 ? -26.051 71.726  -60.555  1.00 27.40  ? 141 PHE   A CD2   1 
ATOM   1115  C  CE1   . PHE   A 1  141 ? -28.111 73.535  -60.774  1.00 33.12  ? 141 PHE   A CE1   1 
ATOM   1116  C  CE2   . PHE   A 1  141 ? -26.560 72.050  -61.817  1.00 35.45  ? 141 PHE   A CE2   1 
ATOM   1117  C  CZ    . PHE   A 1  141 ? -27.589 72.945  -61.928  1.00 27.11  ? 141 PHE   A CZ    1 
ATOM   1118  N  N     . GLY   A 1  142 ? -25.467 71.746  -54.899  1.00 37.83  ? 142 GLY   A N     1 
ATOM   1119  C  CA    . GLY   A 1  142 ? -25.003 70.668  -54.032  1.00 23.67  ? 142 GLY   A CA    1 
ATOM   1120  C  C     . GLY   A 1  142 ? -25.439 70.678  -52.578  1.00 29.58  ? 142 GLY   A C     1 
ATOM   1121  O  O     . GLY   A 1  142 ? -25.458 69.625  -51.949  1.00 30.50  ? 142 GLY   A O     1 
ATOM   1122  N  N     . GLY   A 1  143 ? -25.766 71.844  -52.017  1.00 27.82  ? 143 GLY   A N     1 
ATOM   1123  C  CA    . GLY   A 1  143 ? -26.339 71.899  -50.692  1.00 23.98  ? 143 GLY   A CA    1 
ATOM   1124  C  C     . GLY   A 1  143 ? -27.822 71.499  -50.645  1.00 31.23  ? 143 GLY   A C     1 
ATOM   1125  O  O     . GLY   A 1  143 ? -28.524 71.389  -51.649  1.00 33.30  ? 143 GLY   A O     1 
ATOM   1126  N  N     . GLY   A 1  144 ? -28.310 71.274  -49.425  1.00 34.82  ? 144 GLY   A N     1 
ATOM   1127  C  CA    . GLY   A 1  144 ? -29.691 70.850  -49.266  1.00 32.07  ? 144 GLY   A CA    1 
ATOM   1128  C  C     . GLY   A 1  144 ? -30.679 71.968  -49.547  1.00 37.29  ? 144 GLY   A C     1 
ATOM   1129  O  O     . GLY   A 1  144 ? -31.721 71.743  -50.181  1.00 31.13  ? 144 GLY   A O     1 
ATOM   1130  N  N     . THR   A 1  145 ? -30.377 73.180  -49.056  1.00 27.82  ? 145 THR   A N     1 
ATOM   1131  C  CA    . THR   A 1  145 ? -31.212 74.345  -49.335  1.00 29.54  ? 145 THR   A CA    1 
ATOM   1132  C  C     . THR   A 1  145 ? -31.122 74.724  -50.807  1.00 31.52  ? 145 THR   A C     1 
ATOM   1133  O  O     . THR   A 1  145 ? -32.133 74.773  -51.515  1.00 32.52  ? 145 THR   A O     1 
ATOM   1134  C  CB    . THR   A 1  145 ? -30.783 75.532  -48.464  1.00 29.51  ? 145 THR   A CB    1 
ATOM   1135  O  OG1   . THR   A 1  145 ? -30.778 75.167  -47.085  1.00 30.44  ? 145 THR   A OG1   1 
ATOM   1136  C  CG2   . THR   A 1  145 ? -31.728 76.691  -48.642  1.00 39.50  ? 145 THR   A CG2   1 
ATOM   1137  N  N     . GLY   A 1  146 ? -29.902 74.991  -51.282  1.00 36.06  ? 146 GLY   A N     1 
ATOM   1138  C  CA    . GLY   A 1  146 ? -29.719 75.419  -52.660  1.00 29.41  ? 146 GLY   A CA    1 
ATOM   1139  C  C     . GLY   A 1  146 ? -30.344 74.478  -53.665  1.00 30.24  ? 146 GLY   A C     1 
ATOM   1140  O  O     . GLY   A 1  146 ? -30.911 74.915  -54.668  1.00 37.80  ? 146 GLY   A O     1 
ATOM   1141  N  N     . SER   A 1  147 ? -30.277 73.177  -53.409  1.00 31.64  ? 147 SER   A N     1 
ATOM   1142  C  CA    . SER   A 1  147 ? -30.946 72.265  -54.328  1.00 33.93  ? 147 SER   A CA    1 
ATOM   1143  C  C     . SER   A 1  147 ? -32.431 72.122  -53.999  1.00 31.36  ? 147 SER   A C     1 
ATOM   1144  O  O     . SER   A 1  147 ? -33.284 72.331  -54.870  1.00 29.92  ? 147 SER   A O     1 
ATOM   1145  C  CB    . SER   A 1  147 ? -30.253 70.899  -54.327  1.00 34.32  ? 147 SER   A CB    1 
ATOM   1146  O  OG    . SER   A 1  147 ? -29.967 70.443  -53.014  1.00 34.72  ? 147 SER   A OG    1 
ATOM   1147  N  N     . GLY   A 1  148 ? -32.763 71.754  -52.761  1.00 33.51  ? 148 GLY   A N     1 
ATOM   1148  C  CA    . GLY   A 1  148 ? -34.104 71.277  -52.447  1.00 25.17  ? 148 GLY   A CA    1 
ATOM   1149  C  C     . GLY   A 1  148 ? -35.134 72.382  -52.314  1.00 33.13  ? 148 GLY   A C     1 
ATOM   1150  O  O     . GLY   A 1  148 ? -36.223 72.304  -52.894  1.00 41.74  ? 148 GLY   A O     1 
ATOM   1151  N  N     . PHE   A 1  149 ? -34.822 73.417  -51.536  1.00 22.79  ? 149 PHE   A N     1 
ATOM   1152  C  CA    . PHE   A 1  149 ? -35.736 74.540  -51.422  1.00 30.41  ? 149 PHE   A CA    1 
ATOM   1153  C  C     . PHE   A 1  149 ? -35.925 75.240  -52.771  1.00 39.54  ? 149 PHE   A C     1 
ATOM   1154  O  O     . PHE   A 1  149 ? -37.059 75.515  -53.184  1.00 35.70  ? 149 PHE   A O     1 
ATOM   1155  C  CB    . PHE   A 1  149 ? -35.233 75.522  -50.365  1.00 31.87  ? 149 PHE   A CB    1 
ATOM   1156  C  CG    . PHE   A 1  149 ? -36.237 76.580  -50.010  1.00 42.67  ? 149 PHE   A CG    1 
ATOM   1157  C  CD1   . PHE   A 1  149 ? -37.494 76.226  -49.516  1.00 46.17  ? 149 PHE   A CD1   1 
ATOM   1158  C  CD2   . PHE   A 1  149 ? -35.938 77.925  -50.161  1.00 41.22  ? 149 PHE   A CD2   1 
ATOM   1159  C  CE1   . PHE   A 1  149 ? -38.433 77.198  -49.178  1.00 46.79  ? 149 PHE   A CE1   1 
ATOM   1160  C  CE2   . PHE   A 1  149 ? -36.875 78.906  -49.821  1.00 41.09  ? 149 PHE   A CE2   1 
ATOM   1161  C  CZ    . PHE   A 1  149 ? -38.123 78.534  -49.329  1.00 44.80  ? 149 PHE   A CZ    1 
ATOM   1162  N  N     . THR   A 1  150 ? -34.819 75.529  -53.475  1.00 36.82  ? 150 THR   A N     1 
ATOM   1163  C  CA    . THR   A 1  150 ? -34.887 76.213  -54.764  1.00 33.28  ? 150 THR   A CA    1 
ATOM   1164  C  C     . THR   A 1  150 ? -35.860 75.529  -55.721  1.00 32.19  ? 150 THR   A C     1 
ATOM   1165  O  O     . THR   A 1  150 ? -36.666 76.193  -56.375  1.00 38.01  ? 150 THR   A O     1 
ATOM   1166  C  CB    . THR   A 1  150 ? -33.489 76.299  -55.392  1.00 37.33  ? 150 THR   A CB    1 
ATOM   1167  O  OG1   . THR   A 1  150 ? -32.724 77.302  -54.722  1.00 33.31  ? 150 THR   A OG1   1 
ATOM   1168  C  CG2   . THR   A 1  150 ? -33.579 76.643  -56.854  1.00 33.49  ? 150 THR   A CG2   1 
ATOM   1169  N  N     . SER   A 1  151 ? -35.807 74.200  -55.822  1.00 31.94  ? 151 SER   A N     1 
ATOM   1170  C  CA    . SER   A 1  151 ? -36.771 73.527  -56.692  1.00 37.08  ? 151 SER   A CA    1 
ATOM   1171  C  C     . SER   A 1  151 ? -38.194 73.669  -56.150  1.00 43.60  ? 151 SER   A C     1 
ATOM   1172  O  O     . SER   A 1  151 ? -39.163 73.681  -56.918  1.00 42.88  ? 151 SER   A O     1 
ATOM   1173  C  CB    . SER   A 1  151 ? -36.389 72.050  -56.879  1.00 33.76  ? 151 SER   A CB    1 
ATOM   1174  O  OG    . SER   A 1  151 ? -36.882 71.210  -55.845  1.00 35.84  ? 151 SER   A OG    1 
ATOM   1175  N  N     . LEU   A 1  152 ? -38.340 73.786  -54.832  1.00 49.01  ? 152 LEU   A N     1 
ATOM   1176  C  CA    . LEU   A 1  152 ? -39.654 74.037  -54.256  1.00 46.76  ? 152 LEU   A CA    1 
ATOM   1177  C  C     . LEU   A 1  152 ? -40.110 75.456  -54.571  1.00 48.12  ? 152 LEU   A C     1 
ATOM   1178  O  O     . LEU   A 1  152 ? -41.224 75.669  -55.072  1.00 44.04  ? 152 LEU   A O     1 
ATOM   1179  C  CB    . LEU   A 1  152 ? -39.602 73.799  -52.749  1.00 42.11  ? 152 LEU   A CB    1 
ATOM   1180  C  CG    . LEU   A 1  152 ? -40.876 74.079  -51.957  1.00 52.72  ? 152 LEU   A CG    1 
ATOM   1181  C  CD1   . LEU   A 1  152 ? -41.840 72.909  -52.087  1.00 45.58  ? 152 LEU   A CD1   1 
ATOM   1182  C  CD2   . LEU   A 1  152 ? -40.528 74.366  -50.495  1.00 52.52  ? 152 LEU   A CD2   1 
ATOM   1183  N  N     . LEU   A 1  153 ? -39.244 76.438  -54.296  1.00 40.54  ? 153 LEU   A N     1 
ATOM   1184  C  CA    . LEU   A 1  153 ? -39.563 77.828  -54.597  1.00 40.77  ? 153 LEU   A CA    1 
ATOM   1185  C  C     . LEU   A 1  153 ? -39.886 78.010  -56.074  1.00 41.29  ? 153 LEU   A C     1 
ATOM   1186  O  O     . LEU   A 1  153 ? -40.831 78.726  -56.423  1.00 44.64  ? 153 LEU   A O     1 
ATOM   1187  C  CB    . LEU   A 1  153 ? -38.406 78.738  -54.183  1.00 31.71  ? 153 LEU   A CB    1 
ATOM   1188  C  CG    . LEU   A 1  153 ? -38.683 80.217  -54.438  1.00 41.19  ? 153 LEU   A CG    1 
ATOM   1189  C  CD1   . LEU   A 1  153 ? -40.008 80.606  -53.806  1.00 41.06  ? 153 LEU   A CD1   1 
ATOM   1190  C  CD2   . LEU   A 1  153 ? -37.564 81.119  -53.925  1.00 42.98  ? 153 LEU   A CD2   1 
ATOM   1191  N  N     . MET   A 1  154 ? -39.124 77.359  -56.954  1.00 31.79  ? 154 MET   A N     1 
ATOM   1192  C  CA    . MET   A 1  154 ? -39.358 77.524  -58.384  1.00 42.74  ? 154 MET   A CA    1 
ATOM   1193  C  C     . MET   A 1  154 ? -40.771 77.083  -58.764  1.00 46.85  ? 154 MET   A C     1 
ATOM   1194  O  O     . MET   A 1  154 ? -41.432 77.731  -59.585  1.00 46.25  ? 154 MET   A O     1 
ATOM   1195  C  CB    . MET   A 1  154 ? -38.306 76.754  -59.198  1.00 36.02  ? 154 MET   A CB    1 
ATOM   1196  C  CG    . MET   A 1  154 ? -36.904 77.385  -59.272  1.00 40.13  ? 154 MET   A CG    1 
ATOM   1197  S  SD    . MET   A 1  154 ? -36.654 78.808  -60.394  1.00 44.15  ? 154 MET   A SD    1 
ATOM   1198  C  CE    . MET   A 1  154 ? -36.863 80.114  -59.209  1.00 41.84  ? 154 MET   A CE    1 
ATOM   1199  N  N     . GLU   A 1  155 ? -41.259 75.992  -58.176  1.00 48.29  ? 155 GLU   A N     1 
ATOM   1200  C  CA    . GLU   A 1  155 ? -42.595 75.520  -58.535  1.00 52.92  ? 155 GLU   A CA    1 
ATOM   1201  C  C     . GLU   A 1  155 ? -43.683 76.460  -58.023  1.00 47.39  ? 155 GLU   A C     1 
ATOM   1202  O  O     . GLU   A 1  155 ? -44.691 76.675  -58.704  1.00 47.60  ? 155 GLU   A O     1 
ATOM   1203  C  CB    . GLU   A 1  155 ? -42.816 74.111  -58.006  1.00 44.22  ? 155 GLU   A CB    1 
ATOM   1204  C  CG    . GLU   A 1  155 ? -42.149 73.040  -58.830  1.00 52.89  ? 155 GLU   A CG    1 
ATOM   1205  C  CD    . GLU   A 1  155 ? -42.373 71.679  -58.227  1.00 55.97  ? 155 GLU   A CD    1 
ATOM   1206  O  OE1   . GLU   A 1  155 ? -42.567 71.629  -56.989  1.00 44.42  ? 155 GLU   A OE1   1 
ATOM   1207  O  OE2   . GLU   A 1  155 ? -42.385 70.682  -58.986  1.00 57.60  ? 155 GLU   A OE2   1 
ATOM   1208  N  N     . ARG   A 1  156 ? -43.509 77.017  -56.823  1.00 43.64  ? 156 ARG   A N     1 
ATOM   1209  C  CA    . ARG   A 1  156 ? -44.469 78.001  -56.329  1.00 53.40  ? 156 ARG   A CA    1 
ATOM   1210  C  C     . ARG   A 1  156 ? -44.430 79.278  -57.158  1.00 55.66  ? 156 ARG   A C     1 
ATOM   1211  O  O     . ARG   A 1  156 ? -45.463 79.938  -57.339  1.00 53.98  ? 156 ARG   A O     1 
ATOM   1212  C  CB    . ARG   A 1  156 ? -44.204 78.326  -54.851  1.00 50.28  ? 156 ARG   A CB    1 
ATOM   1213  C  CG    . ARG   A 1  156 ? -44.477 77.174  -53.897  1.00 49.20  ? 156 ARG   A CG    1 
ATOM   1214  C  CD    . ARG   A 1  156 ? -45.889 76.610  -54.078  1.00 55.35  ? 156 ARG   A CD    1 
ATOM   1215  N  NE    . ARG   A 1  156 ? -46.911 77.637  -53.901  1.00 64.75  ? 156 ARG   A NE    1 
ATOM   1216  C  CZ    . ARG   A 1  156 ? -47.417 78.001  -52.728  1.00 69.75  ? 156 ARG   A CZ    1 
ATOM   1217  N  NH1   . ARG   A 1  156 ? -47.020 77.435  -51.596  1.00 59.08  ? 156 ARG   A NH1   1 
ATOM   1218  N  NH2   . ARG   A 1  156 ? -48.337 78.963  -52.688  1.00 69.85  ? 156 ARG   A NH2   1 
ATOM   1219  N  N     . LEU   A 1  157 ? -43.253 79.648  -57.663  1.00 52.23  ? 157 LEU   A N     1 
ATOM   1220  C  CA    . LEU   A 1  157 ? -43.171 80.852  -58.472  1.00 50.71  ? 157 LEU   A CA    1 
ATOM   1221  C  C     . LEU   A 1  157 ? -43.929 80.682  -59.796  1.00 51.70  ? 157 LEU   A C     1 
ATOM   1222  O  O     . LEU   A 1  157 ? -44.684 81.578  -60.196  1.00 45.46  ? 157 LEU   A O     1 
ATOM   1223  C  CB    . LEU   A 1  157 ? -41.700 81.224  -58.670  1.00 49.86  ? 157 LEU   A CB    1 
ATOM   1224  C  CG    . LEU   A 1  157 ? -40.974 81.799  -57.435  1.00 43.37  ? 157 LEU   A CG    1 
ATOM   1225  C  CD1   . LEU   A 1  157 ? -39.532 82.197  -57.743  1.00 35.49  ? 157 LEU   A CD1   1 
ATOM   1226  C  CD2   . LEU   A 1  157 ? -41.717 82.995  -56.854  1.00 45.98  ? 157 LEU   A CD2   1 
ATOM   1227  N  N     . SER   A 1  158 ? -43.789 79.523  -60.460  1.00 41.48  ? 158 SER   A N     1 
ATOM   1228  C  CA    . SER   A 1  158 ? -44.521 79.273  -61.704  1.00 44.48  ? 158 SER   A CA    1 
ATOM   1229  C  C     . SER   A 1  158 ? -46.034 79.254  -61.485  1.00 57.99  ? 158 SER   A C     1 
ATOM   1230  O  O     . SER   A 1  158 ? -46.805 79.679  -62.358  1.00 54.91  ? 158 SER   A O     1 
ATOM   1231  C  CB    . SER   A 1  158 ? -44.078 77.950  -62.329  1.00 42.61  ? 158 SER   A CB    1 
ATOM   1232  O  OG    . SER   A 1  158 ? -42.720 77.993  -62.717  1.00 51.38  ? 158 SER   A OG    1 
ATOM   1233  N  N     . VAL   A 1  159 ? -46.478 78.733  -60.341  1.00 57.83  ? 159 VAL   A N     1 
ATOM   1234  C  CA    . VAL   A 1  159 ? -47.900 78.736  -60.024  1.00 51.82  ? 159 VAL   A CA    1 
ATOM   1235  C  C     . VAL   A 1  159 ? -48.381 80.150  -59.708  1.00 55.06  ? 159 VAL   A C     1 
ATOM   1236  O  O     . VAL   A 1  159 ? -49.498 80.529  -60.073  1.00 66.80  ? 159 VAL   A O     1 
ATOM   1237  C  CB    . VAL   A 1  159 ? -48.188 77.764  -58.862  1.00 60.31  ? 159 VAL   A CB    1 
ATOM   1238  C  CG1   . VAL   A 1  159 ? -49.634 77.908  -58.408  1.00 55.94  ? 159 VAL   A CG1   1 
ATOM   1239  C  CG2   . VAL   A 1  159 ? -47.892 76.311  -59.266  1.00 46.74  ? 159 VAL   A CG2   1 
ATOM   1240  N  N     . ASP   A 1  160 ? -47.556 80.951  -59.030  1.00 51.78  ? 160 ASP   A N     1 
ATOM   1241  C  CA    . ASP   A 1  160 ? -47.932 82.293  -58.592  1.00 49.32  ? 160 ASP   A CA    1 
ATOM   1242  C  C     . ASP   A 1  160 ? -47.493 83.409  -59.542  1.00 58.82  ? 160 ASP   A C     1 
ATOM   1243  O  O     . ASP   A 1  160 ? -47.710 84.589  -59.223  1.00 52.21  ? 160 ASP   A O     1 
ATOM   1244  C  CB    . ASP   A 1  160 ? -47.352 82.588  -57.199  1.00 51.59  ? 160 ASP   A CB    1 
ATOM   1245  C  CG    . ASP   A 1  160 ? -47.874 81.649  -56.135  1.00 60.52  ? 160 ASP   A CG    1 
ATOM   1246  O  OD1   . ASP   A 1  160 ? -48.448 80.596  -56.493  1.00 63.88  ? 160 ASP   A OD1   1 
ATOM   1247  O  OD2   . ASP   A 1  160 ? -47.710 81.969  -54.939  1.00 54.69  ? 160 ASP   A OD2   1 
ATOM   1248  N  N     . TYR   A 1  161 ? -46.850 83.087  -60.671  1.00 55.61  ? 161 TYR   A N     1 
ATOM   1249  C  CA    . TYR   A 1  161 ? -46.458 84.116  -61.635  1.00 48.29  ? 161 TYR   A CA    1 
ATOM   1250  C  C     . TYR   A 1  161 ? -46.261 83.555  -63.039  1.00 53.38  ? 161 TYR   A C     1 
ATOM   1251  O  O     . TYR   A 1  161 ? -45.305 83.941  -63.718  1.00 60.49  ? 161 TYR   A O     1 
ATOM   1252  C  CB    . TYR   A 1  161 ? -45.155 84.807  -61.224  1.00 44.12  ? 161 TYR   A CB    1 
ATOM   1253  C  CG    . TYR   A 1  161 ? -45.094 85.412  -59.844  1.00 40.82  ? 161 TYR   A CG    1 
ATOM   1254  C  CD1   . TYR   A 1  161 ? -44.762 84.636  -58.733  1.00 47.10  ? 161 TYR   A CD1   1 
ATOM   1255  C  CD2   . TYR   A 1  161 ? -45.309 86.765  -59.656  1.00 34.81  ? 161 TYR   A CD2   1 
ATOM   1256  C  CE1   . TYR   A 1  161 ? -44.679 85.194  -57.462  1.00 42.92  ? 161 TYR   A CE1   1 
ATOM   1257  C  CE2   . TYR   A 1  161 ? -45.231 87.341  -58.389  1.00 43.97  ? 161 TYR   A CE2   1 
ATOM   1258  C  CZ    . TYR   A 1  161 ? -44.914 86.551  -57.296  1.00 49.19  ? 161 TYR   A CZ    1 
ATOM   1259  O  OH    . TYR   A 1  161 ? -44.841 87.123  -56.042  1.00 51.33  ? 161 TYR   A OH    1 
ATOM   1260  N  N     . GLY   A 1  162 ? -47.133 82.654  -63.491  1.00 49.13  ? 162 GLY   A N     1 
ATOM   1261  C  CA    . GLY   A 1  162 ? -46.967 82.034  -64.795  1.00 50.46  ? 162 GLY   A CA    1 
ATOM   1262  C  C     . GLY   A 1  162 ? -46.551 82.979  -65.911  1.00 63.24  ? 162 GLY   A C     1 
ATOM   1263  O  O     . GLY   A 1  162 ? -45.913 82.566  -66.883  1.00 64.31  ? 162 GLY   A O     1 
ATOM   1264  N  N     . LYS   A 1  163 ? -46.903 84.261  -65.776  1.00 67.41  ? 163 LYS   A N     1 
ATOM   1265  C  CA    . LYS   A 1  163 ? -46.599 85.249  -66.807  1.00 76.99  ? 163 LYS   A CA    1 
ATOM   1266  C  C     . LYS   A 1  163 ? -45.112 85.618  -66.851  1.00 81.34  ? 163 LYS   A C     1 
ATOM   1267  O  O     . LYS   A 1  163 ? -44.617 86.040  -67.909  1.00 74.45  ? 163 LYS   A O     1 
ATOM   1268  C  CB    . LYS   A 1  163 ? -47.446 86.516  -66.586  1.00 70.53  ? 163 LYS   A CB    1 
ATOM   1269  C  CG    . LYS   A 1  163 ? -48.973 86.306  -66.559  1.00 79.81  ? 163 LYS   A CG    1 
ATOM   1270  C  CD    . LYS   A 1  163 ? -49.472 85.632  -65.257  1.00 82.46  ? 163 LYS   A CD    1 
ATOM   1271  C  CE    . LYS   A 1  163 ? -51.000 85.428  -65.272  1.00 86.28  ? 163 LYS   A CE    1 
ATOM   1272  N  NZ    . LYS   A 1  163 ? -51.493 84.362  -64.334  1.00 65.48  ? 163 LYS   A NZ    1 
ATOM   1273  N  N     . LYS   A 1  164 ? -44.392 85.450  -65.740  1.00 70.40  ? 164 LYS   A N     1 
ATOM   1274  C  CA    . LYS   A 1  164 ? -43.058 86.006  -65.567  1.00 61.50  ? 164 LYS   A CA    1 
ATOM   1275  C  C     . LYS   A 1  164 ? -41.960 85.002  -65.953  1.00 53.03  ? 164 LYS   A C     1 
ATOM   1276  O  O     . LYS   A 1  164 ? -42.198 83.806  -66.131  1.00 49.51  ? 164 LYS   A O     1 
ATOM   1277  C  CB    . LYS   A 1  164 ? -42.871 86.479  -64.123  1.00 51.21  ? 164 LYS   A CB    1 
ATOM   1278  C  CG    . LYS   A 1  164 ? -43.714 87.682  -63.719  1.00 53.17  ? 164 LYS   A CG    1 
ATOM   1279  C  CD    . LYS   A 1  164 ? -45.200 87.356  -63.634  1.00 64.39  ? 164 LYS   A CD    1 
ATOM   1280  C  CE    . LYS   A 1  164 ? -46.001 88.572  -63.173  1.00 62.51  ? 164 LYS   A CE    1 
ATOM   1281  N  NZ    . LYS   A 1  164 ? -45.659 89.790  -63.974  1.00 57.63  ? 164 LYS   A NZ    1 
ATOM   1282  N  N     . SER   A 1  165 ? -40.743 85.528  -66.087  1.00 45.79  ? 165 SER   A N     1 
ATOM   1283  C  CA    . SER   A 1  165 ? -39.548 84.804  -66.498  1.00 43.95  ? 165 SER   A CA    1 
ATOM   1284  C  C     . SER   A 1  165 ? -38.734 84.399  -65.273  1.00 41.95  ? 165 SER   A C     1 
ATOM   1285  O  O     . SER   A 1  165 ? -38.729 85.096  -64.258  1.00 44.56  ? 165 SER   A O     1 
ATOM   1286  C  CB    . SER   A 1  165 ? -38.680 85.680  -67.415  1.00 50.62  ? 165 SER   A CB    1 
ATOM   1287  O  OG    . SER   A 1  165 ? -38.899 85.425  -68.789  1.00 41.98  ? 165 SER   A OG    1 
ATOM   1288  N  N     . LYS   A 1  166 ? -38.025 83.273  -65.375  1.00 44.40  ? 166 LYS   A N     1 
ATOM   1289  C  CA    . LYS   A 1  166 ? -37.160 82.810  -64.289  1.00 48.65  ? 166 LYS   A CA    1 
ATOM   1290  C  C     . LYS   A 1  166 ? -35.793 82.420  -64.851  1.00 40.81  ? 166 LYS   A C     1 
ATOM   1291  O  O     . LYS   A 1  166 ? -35.685 81.478  -65.640  1.00 37.55  ? 166 LYS   A O     1 
ATOM   1292  C  CB    . LYS   A 1  166 ? -37.823 81.651  -63.526  1.00 46.44  ? 166 LYS   A CB    1 
ATOM   1293  C  CG    . LYS   A 1  166 ? -39.066 82.118  -62.723  1.00 49.56  ? 166 LYS   A CG    1 
ATOM   1294  C  CD    . LYS   A 1  166 ? -39.532 81.174  -61.612  1.00 37.34  ? 166 LYS   A CD    1 
ATOM   1295  C  CE    . LYS   A 1  166 ? -40.145 79.876  -62.140  1.00 43.45  ? 166 LYS   A CE    1 
ATOM   1296  N  NZ    . LYS   A 1  166 ? -41.399 80.006  -62.939  1.00 41.58  ? 166 LYS   A NZ    1 
ATOM   1297  N  N     . LEU   A 1  167 ? -34.763 83.173  -64.468  1.00 46.24  ? 167 LEU   A N     1 
ATOM   1298  C  CA    . LEU   A 1  167 ? -33.366 82.889  -64.793  1.00 40.58  ? 167 LEU   A CA    1 
ATOM   1299  C  C     . LEU   A 1  167 ? -32.652 82.321  -63.572  1.00 40.04  ? 167 LEU   A C     1 
ATOM   1300  O  O     . LEU   A 1  167 ? -32.860 82.791  -62.444  1.00 37.82  ? 167 LEU   A O     1 
ATOM   1301  C  CB    . LEU   A 1  167 ? -32.624 84.154  -65.242  1.00 34.30  ? 167 LEU   A CB    1 
ATOM   1302  C  CG    . LEU   A 1  167 ? -32.484 84.587  -66.707  1.00 39.14  ? 167 LEU   A CG    1 
ATOM   1303  C  CD1   . LEU   A 1  167 ? -33.828 84.741  -67.387  1.00 36.41  ? 167 LEU   A CD1   1 
ATOM   1304  C  CD2   . LEU   A 1  167 ? -31.691 85.895  -66.781  1.00 38.40  ? 167 LEU   A CD2   1 
ATOM   1305  N  N     . GLU   A 1  168 ? -31.788 81.334  -63.805  1.00 34.88  ? 168 GLU   A N     1 
ATOM   1306  C  CA    . GLU   A 1  168 ? -30.958 80.749  -62.759  1.00 33.46  ? 168 GLU   A CA    1 
ATOM   1307  C  C     . GLU   A 1  168 ? -29.501 81.121  -62.974  1.00 36.07  ? 168 GLU   A C     1 
ATOM   1308  O  O     . GLU   A 1  168 ? -28.999 81.098  -64.108  1.00 39.53  ? 168 GLU   A O     1 
ATOM   1309  C  CB    . GLU   A 1  168 ? -31.055 79.218  -62.734  1.00 36.82  ? 168 GLU   A CB    1 
ATOM   1310  C  CG    . GLU   A 1  168 ? -32.327 78.611  -62.178  1.00 25.24  ? 168 GLU   A CG    1 
ATOM   1311  C  CD    . GLU   A 1  168 ? -32.317 77.096  -62.287  1.00 35.28  ? 168 GLU   A CD    1 
ATOM   1312  O  OE1   . GLU   A 1  168 ? -32.688 76.560  -63.360  1.00 32.95  ? 168 GLU   A OE1   1 
ATOM   1313  O  OE2   . GLU   A 1  168 ? -31.907 76.431  -61.304  1.00 41.76  ? 168 GLU   A OE2   1 
ATOM   1314  N  N     . PHE   A 1  169 ? -28.825 81.446  -61.875  1.00 36.00  ? 169 PHE   A N     1 
ATOM   1315  C  CA    . PHE   A 1  169 ? -27.374 81.341  -61.764  1.00 27.26  ? 169 PHE   A CA    1 
ATOM   1316  C  C     . PHE   A 1  169 ? -27.098 80.193  -60.803  1.00 35.20  ? 169 PHE   A C     1 
ATOM   1317  O  O     . PHE   A 1  169 ? -27.317 80.327  -59.595  1.00 38.34  ? 169 PHE   A O     1 
ATOM   1318  C  CB    . PHE   A 1  169 ? -26.760 82.643  -61.278  1.00 29.40  ? 169 PHE   A CB    1 
ATOM   1319  C  CG    . PHE   A 1  169 ? -26.937 83.783  -62.236  1.00 34.60  ? 169 PHE   A CG    1 
ATOM   1320  C  CD1   . PHE   A 1  169 ? -28.087 84.557  -62.204  1.00 41.09  ? 169 PHE   A CD1   1 
ATOM   1321  C  CD2   . PHE   A 1  169 ? -25.951 84.078  -63.173  1.00 36.21  ? 169 PHE   A CD2   1 
ATOM   1322  C  CE1   . PHE   A 1  169 ? -28.256 85.610  -63.090  1.00 41.36  ? 169 PHE   A CE1   1 
ATOM   1323  C  CE2   . PHE   A 1  169 ? -26.100 85.125  -64.043  1.00 35.49  ? 169 PHE   A CE2   1 
ATOM   1324  C  CZ    . PHE   A 1  169 ? -27.261 85.892  -64.008  1.00 33.97  ? 169 PHE   A CZ    1 
ATOM   1325  N  N     . SER   A 1  170 ? -26.657 79.057  -61.347  1.00 36.57  ? 170 SER   A N     1 
ATOM   1326  C  CA    . SER   A 1  170 ? -26.472 77.816  -60.607  1.00 28.52  ? 170 SER   A CA    1 
ATOM   1327  C  C     . SER   A 1  170 ? -24.991 77.483  -60.481  1.00 32.60  ? 170 SER   A C     1 
ATOM   1328  O  O     . SER   A 1  170 ? -24.236 77.603  -61.450  1.00 40.67  ? 170 SER   A O     1 
ATOM   1329  C  CB    . SER   A 1  170 ? -27.194 76.668  -61.303  1.00 28.23  ? 170 SER   A CB    1 
ATOM   1330  O  OG    . SER   A 1  170 ? -28.542 77.022  -61.556  1.00 42.32  ? 170 SER   A OG    1 
ATOM   1331  N  N     . ILE   A 1  171 ? -24.583 77.052  -59.288  1.00 33.93  ? 171 ILE   A N     1 
ATOM   1332  C  CA    . ILE   A 1  171 ? -23.197 76.696  -58.988  1.00 26.97  ? 171 ILE   A CA    1 
ATOM   1333  C  C     . ILE   A 1  171 ? -23.081 75.176  -59.001  1.00 28.23  ? 171 ILE   A C     1 
ATOM   1334  O  O     . ILE   A 1  171 ? -23.747 74.488  -58.219  1.00 30.06  ? 171 ILE   A O     1 
ATOM   1335  C  CB    . ILE   A 1  171 ? -22.762 77.285  -57.637  1.00 32.95  ? 171 ILE   A CB    1 
ATOM   1336  C  CG1   . ILE   A 1  171 ? -22.892 78.818  -57.669  1.00 24.54  ? 171 ILE   A CG1   1 
ATOM   1337  C  CG2   . ILE   A 1  171 ? -21.337 76.823  -57.267  1.00 28.00  ? 171 ILE   A CG2   1 
ATOM   1338  C  CD1   . ILE   A 1  171 ? -21.774 79.514  -58.411  1.00 21.70  ? 171 ILE   A CD1   1 
ATOM   1339  N  N     . TYR   A 1  172 ? -22.271 74.644  -59.910  1.00 24.20  ? 172 TYR   A N     1 
ATOM   1340  C  CA    . TYR   A 1  172 ? -22.138 73.216  -60.197  1.00 24.87  ? 172 TYR   A CA    1 
ATOM   1341  C  C     . TYR   A 1  172 ? -21.061 72.630  -59.292  1.00 23.39  ? 172 TYR   A C     1 
ATOM   1342  O  O     . TYR   A 1  172 ? -20.067 73.290  -59.036  1.00 19.02  ? 172 TYR   A O     1 
ATOM   1343  C  CB    . TYR   A 1  172 ? -21.784 73.030  -61.673  1.00 27.60  ? 172 TYR   A CB    1 
ATOM   1344  C  CG    . TYR   A 1  172 ? -21.528 71.639  -62.229  1.00 29.20  ? 172 TYR   A CG    1 
ATOM   1345  C  CD1   . TYR   A 1  172 ? -20.333 70.972  -61.981  1.00 24.73  ? 172 TYR   A CD1   1 
ATOM   1346  C  CD2   . TYR   A 1  172 ? -22.442 71.030  -63.080  1.00 23.51  ? 172 TYR   A CD2   1 
ATOM   1347  C  CE1   . TYR   A 1  172 ? -20.082 69.735  -62.530  1.00 20.56  ? 172 TYR   A CE1   1 
ATOM   1348  C  CE2   . TYR   A 1  172 ? -22.188 69.776  -63.641  1.00 24.40  ? 172 TYR   A CE2   1 
ATOM   1349  C  CZ    . TYR   A 1  172 ? -21.007 69.138  -63.357  1.00 26.97  ? 172 TYR   A CZ    1 
ATOM   1350  O  OH    . TYR   A 1  172 ? -20.738 67.893  -63.891  1.00 31.60  ? 172 TYR   A OH    1 
ATOM   1351  N  N     . PRO   A 1  173 ? -21.230 71.427  -58.735  1.00 33.88  ? 173 PRO   A N     1 
ATOM   1352  C  CA    . PRO   A 1  173 ? -20.381 71.009  -57.603  1.00 23.44  ? 173 PRO   A CA    1 
ATOM   1353  C  C     . PRO   A 1  173 ? -18.990 70.574  -58.042  1.00 22.37  ? 173 PRO   A C     1 
ATOM   1354  O  O     . PRO   A 1  173 ? -18.835 69.872  -59.038  1.00 30.26  ? 173 PRO   A O     1 
ATOM   1355  C  CB    . PRO   A 1  173 ? -21.165 69.848  -56.987  1.00 16.64  ? 173 PRO   A CB    1 
ATOM   1356  C  CG    . PRO   A 1  173 ? -21.994 69.329  -58.082  1.00 25.98  ? 173 PRO   A CG    1 
ATOM   1357  C  CD    . PRO   A 1  173 ? -22.280 70.440  -59.041  1.00 26.36  ? 173 PRO   A CD    1 
ATOM   1358  N  N     . ALA   A 1  174 ? -17.964 71.037  -57.312  1.00 23.15  ? 174 ALA   A N     1 
ATOM   1359  C  CA    . ALA   A 1  174 ? -16.579 70.648  -57.588  1.00 19.96  ? 174 ALA   A CA    1 
ATOM   1360  C  C     . ALA   A 1  174 ? -15.883 70.132  -56.330  1.00 27.14  ? 174 ALA   A C     1 
ATOM   1361  O  O     . ALA   A 1  174 ? -15.855 70.827  -55.295  1.00 20.56  ? 174 ALA   A O     1 
ATOM   1362  C  CB    . ALA   A 1  174 ? -15.777 71.807  -58.177  1.00 20.91  ? 174 ALA   A CB    1 
ATOM   1363  N  N     . PRO   A 1  175 ? -15.280 68.943  -56.390  1.00 32.10  ? 175 PRO   A N     1 
ATOM   1364  C  CA    . PRO   A 1  175 ? -14.554 68.393  -55.224  1.00 19.91  ? 175 PRO   A CA    1 
ATOM   1365  C  C     . PRO   A 1  175 ? -13.607 69.364  -54.547  1.00 30.90  ? 175 PRO   A C     1 
ATOM   1366  O  O     . PRO   A 1  175 ? -13.460 69.311  -53.321  1.00 38.20  ? 175 PRO   A O     1 
ATOM   1367  C  CB    . PRO   A 1  175 ? -13.789 67.220  -55.836  1.00 31.04  ? 175 PRO   A CB    1 
ATOM   1368  C  CG    . PRO   A 1  175 ? -14.605 66.793  -57.027  1.00 26.42  ? 175 PRO   A CG    1 
ATOM   1369  C  CD    . PRO   A 1  175 ? -15.243 68.049  -57.560  1.00 18.21  ? 175 PRO   A CD    1 
ATOM   1370  N  N     . GLN   A 1  176 ? -12.959 70.260  -55.291  1.00 36.31  ? 176 GLN   A N     1 
ATOM   1371  C  CA    . GLN   A 1  176 ? -11.988 71.159  -54.668  1.00 31.58  ? 176 GLN   A CA    1 
ATOM   1372  C  C     . GLN   A 1  176 ? -12.589 72.014  -53.555  1.00 29.24  ? 176 GLN   A C     1 
ATOM   1373  O  O     . GLN   A 1  176 ? -11.840 72.491  -52.701  1.00 33.85  ? 176 GLN   A O     1 
ATOM   1374  C  CB    . GLN   A 1  176 ? -11.343 72.058  -55.741  1.00 32.00  ? 176 GLN   A CB    1 
ATOM   1375  C  CG    . GLN   A 1  176 ? -9.912  71.668  -56.098  1.00 34.07  ? 176 GLN   A CG    1 
ATOM   1376  C  CD    . GLN   A 1  176 ? -9.647  71.593  -57.596  1.00 47.00  ? 176 GLN   A CD    1 
ATOM   1377  O  OE1   . GLN   A 1  176 ? -10.581 71.555  -58.410  1.00 50.26  ? 176 GLN   A OE1   1 
ATOM   1378  N  NE2   . GLN   A 1  176 ? -8.364  71.568  -57.970  1.00 39.87  ? 176 GLN   A NE2   1 
ATOM   1379  N  N     . VAL   A 1  177 ? -13.908 72.240  -53.542  1.00 32.64  ? 177 VAL   A N     1 
ATOM   1380  C  CA    . VAL   A 1  177 ? -14.529 73.074  -52.507  1.00 34.75  ? 177 VAL   A CA    1 
ATOM   1381  C  C     . VAL   A 1  177 ? -15.831 72.493  -51.947  1.00 34.01  ? 177 VAL   A C     1 
ATOM   1382  O  O     . VAL   A 1  177 ? -16.386 73.038  -50.990  1.00 35.94  ? 177 VAL   A O     1 
ATOM   1383  C  CB    . VAL   A 1  177 ? -14.775 74.513  -53.014  1.00 30.79  ? 177 VAL   A CB    1 
ATOM   1384  C  CG1   . VAL   A 1  177 ? -13.485 75.281  -53.046  1.00 31.27  ? 177 VAL   A CG1   1 
ATOM   1385  C  CG2   . VAL   A 1  177 ? -15.468 74.511  -54.401  1.00 24.84  ? 177 VAL   A CG2   1 
ATOM   1386  N  N     . SER   A 1  178 ? -16.326 71.392  -52.514  1.00 36.27  ? 178 SER   A N     1 
ATOM   1387  C  CA    . SER   A 1  178 ? -17.545 70.757  -52.005  1.00 44.14  ? 178 SER   A CA    1 
ATOM   1388  C  C     . SER   A 1  178 ? -17.401 70.314  -50.538  1.00 48.42  ? 178 SER   A C     1 
ATOM   1389  O  O     . SER   A 1  178 ? -16.311 69.978  -50.068  1.00 35.28  ? 178 SER   A O     1 
ATOM   1390  C  CB    . SER   A 1  178 ? -17.901 69.538  -52.866  1.00 42.45  ? 178 SER   A CB    1 
ATOM   1391  O  OG    . SER   A 1  178 ? -17.117 68.426  -52.453  1.00 45.56  ? 178 SER   A OG    1 
ATOM   1392  N  N     . THR   A 1  179 ? -18.538 70.268  -49.821  1.00 50.19  ? 179 THR   A N     1 
ATOM   1393  C  CA    . THR   A 1  179 ? -18.598 69.824  -48.427  1.00 42.30  ? 179 THR   A CA    1 
ATOM   1394  C  C     . THR   A 1  179 ? -19.543 68.635  -48.233  1.00 48.15  ? 179 THR   A C     1 
ATOM   1395  O  O     . THR   A 1  179 ? -20.092 68.450  -47.140  1.00 45.26  ? 179 THR   A O     1 
ATOM   1396  C  CB    . THR   A 1  179 ? -19.036 70.961  -47.497  1.00 44.35  ? 179 THR   A CB    1 
ATOM   1397  O  OG1   . THR   A 1  179 ? -19.660 72.002  -48.256  1.00 40.76  ? 179 THR   A OG1   1 
ATOM   1398  C  CG2   . THR   A 1  179 ? -17.867 71.525  -46.713  1.00 46.17  ? 179 THR   A CG2   1 
ATOM   1399  N  N     . ALA   A 1  180 ? -19.762 67.823  -49.272  1.00 44.81  ? 180 ALA   A N     1 
ATOM   1400  C  CA    . ALA   A 1  180 ? -20.662 66.684  -49.118  1.00 37.03  ? 180 ALA   A CA    1 
ATOM   1401  C  C     . ALA   A 1  180 ? -20.524 65.700  -50.265  1.00 35.97  ? 180 ALA   A C     1 
ATOM   1402  O  O     . ALA   A 1  180 ? -20.547 66.103  -51.430  1.00 39.64  ? 180 ALA   A O     1 
ATOM   1403  C  CB    . ALA   A 1  180 ? -22.116 67.152  -49.008  1.00 35.73  ? 180 ALA   A CB    1 
ATOM   1404  N  N     . VAL   A 1  181 ? -20.394 64.409  -49.944  1.00 28.24  ? 181 VAL   A N     1 
ATOM   1405  C  CA    . VAL   A 1  181 ? -20.258 63.378  -50.966  1.00 28.74  ? 181 VAL   A CA    1 
ATOM   1406  C  C     . VAL   A 1  181 ? -21.546 63.200  -51.786  1.00 28.98  ? 181 VAL   A C     1 
ATOM   1407  O  O     . VAL   A 1  181 ? -21.509 62.600  -52.865  1.00 29.88  ? 181 VAL   A O     1 
ATOM   1408  C  CB    . VAL   A 1  181 ? -19.797 62.062  -50.279  1.00 32.99  ? 181 VAL   A CB    1 
ATOM   1409  C  CG1   . VAL   A 1  181 ? -20.810 61.621  -49.246  1.00 42.18  ? 181 VAL   A CG1   1 
ATOM   1410  C  CG2   . VAL   A 1  181 ? -19.601 60.920  -51.273  1.00 26.97  ? 181 VAL   A CG2   1 
ATOM   1411  N  N     . VAL   A 1  182 ? -22.690 63.718  -51.319  1.00 31.87  ? 182 VAL   A N     1 
ATOM   1412  C  CA    . VAL   A 1  182 ? -23.974 63.456  -51.971  1.00 32.21  ? 182 VAL   A CA    1 
ATOM   1413  C  C     . VAL   A 1  182 ? -24.369 64.521  -53.002  1.00 35.72  ? 182 VAL   A C     1 
ATOM   1414  O  O     . VAL   A 1  182 ? -25.420 64.379  -53.648  1.00 27.12  ? 182 VAL   A O     1 
ATOM   1415  C  CB    . VAL   A 1  182 ? -25.129 63.312  -50.946  1.00 22.29  ? 182 VAL   A CB    1 
ATOM   1416  C  CG1   . VAL   A 1  182 ? -24.975 62.048  -50.182  1.00 25.91  ? 182 VAL   A CG1   1 
ATOM   1417  C  CG2   . VAL   A 1  182 ? -25.207 64.511  -50.012  1.00 21.24  ? 182 VAL   A CG2   1 
ATOM   1418  N  N     . GLU   A 1  183 ? -23.556 65.566  -53.189  1.00 39.32  ? 183 GLU   A N     1 
ATOM   1419  C  CA    . GLU   A 1  183 ? -23.836 66.633  -54.157  1.00 32.51  ? 183 GLU   A CA    1 
ATOM   1420  C  C     . GLU   A 1  183 ? -24.369 66.152  -55.503  1.00 28.04  ? 183 GLU   A C     1 
ATOM   1421  O  O     . GLU   A 1  183 ? -25.355 66.731  -55.981  1.00 32.96  ? 183 GLU   A O     1 
ATOM   1422  C  CB    . GLU   A 1  183 ? -22.559 67.463  -54.349  1.00 35.36  ? 183 GLU   A CB    1 
ATOM   1423  C  CG    . GLU   A 1  183 ? -21.910 67.787  -53.042  1.00 38.28  ? 183 GLU   A CG    1 
ATOM   1424  C  CD    . GLU   A 1  183 ? -21.496 69.217  -52.926  1.00 42.27  ? 183 GLU   A CD    1 
ATOM   1425  O  OE1   . GLU   A 1  183 ? -21.923 70.003  -53.780  1.00 41.34  ? 183 GLU   A OE1   1 
ATOM   1426  O  OE2   . GLU   A 1  183 ? -20.741 69.552  -51.977  1.00 50.75  ? 183 GLU   A OE2   1 
ATOM   1427  N  N     . PRO   A 1  184 ? -23.818 65.118  -56.148  1.00 30.42  ? 184 PRO   A N     1 
ATOM   1428  C  CA    . PRO   A 1  184 ? -24.440 64.651  -57.413  1.00 31.13  ? 184 PRO   A CA    1 
ATOM   1429  C  C     . PRO   A 1  184 ? -25.885 64.191  -57.246  1.00 30.69  ? 184 PRO   A C     1 
ATOM   1430  O  O     . PRO   A 1  184 ? -26.678 64.345  -58.175  1.00 36.99  ? 184 PRO   A O     1 
ATOM   1431  C  CB    . PRO   A 1  184 ? -23.535 63.494  -57.877  1.00 16.89  ? 184 PRO   A CB    1 
ATOM   1432  C  CG    . PRO   A 1  184 ? -22.291 63.602  -57.070  1.00 22.46  ? 184 PRO   A CG    1 
ATOM   1433  C  CD    . PRO   A 1  184 ? -22.644 64.311  -55.766  1.00 27.31  ? 184 PRO   A CD    1 
ATOM   1434  N  N     . TYR   A 1  185 ? -26.248 63.602  -56.109  1.00 22.82  ? 185 TYR   A N     1 
ATOM   1435  C  CA    . TYR   A 1  185 ? -27.652 63.322  -55.841  1.00 29.29  ? 185 TYR   A CA    1 
ATOM   1436  C  C     . TYR   A 1  185 ? -28.473 64.601  -55.866  1.00 30.43  ? 185 TYR   A C     1 
ATOM   1437  O  O     . TYR   A 1  185 ? -29.414 64.738  -56.647  1.00 32.26  ? 185 TYR   A O     1 
ATOM   1438  C  CB    . TYR   A 1  185 ? -27.800 62.648  -54.478  1.00 33.05  ? 185 TYR   A CB    1 
ATOM   1439  C  CG    . TYR   A 1  185 ? -27.515 61.173  -54.451  1.00 29.15  ? 185 TYR   A CG    1 
ATOM   1440  C  CD1   . TYR   A 1  185 ? -27.355 60.459  -55.635  1.00 22.28  ? 185 TYR   A CD1   1 
ATOM   1441  C  CD2   . TYR   A 1  185 ? -27.429 60.486  -53.225  1.00 26.37  ? 185 TYR   A CD2   1 
ATOM   1442  C  CE1   . TYR   A 1  185 ? -27.118 59.096  -55.618  1.00 31.18  ? 185 TYR   A CE1   1 
ATOM   1443  C  CE2   . TYR   A 1  185 ? -27.197 59.115  -53.190  1.00 24.49  ? 185 TYR   A CE2   1 
ATOM   1444  C  CZ    . TYR   A 1  185 ? -27.033 58.429  -54.388  1.00 30.00  ? 185 TYR   A CZ    1 
ATOM   1445  O  OH    . TYR   A 1  185 ? -26.797 57.085  -54.374  1.00 27.40  ? 185 TYR   A OH    1 
ATOM   1446  N  N     . ASN   A 1  186 ? -28.138 65.542  -54.984  1.00 30.24  ? 186 ASN   A N     1 
ATOM   1447  C  CA    . ASN   A 1  186 ? -28.871 66.793  -54.899  1.00 29.93  ? 186 ASN   A CA    1 
ATOM   1448  C  C     . ASN   A 1  186 ? -28.857 67.553  -56.215  1.00 36.07  ? 186 ASN   A C     1 
ATOM   1449  O  O     . ASN   A 1  186 ? -29.804 68.294  -56.511  1.00 36.80  ? 186 ASN   A O     1 
ATOM   1450  C  CB    . ASN   A 1  186 ? -28.284 67.658  -53.790  1.00 31.61  ? 186 ASN   A CB    1 
ATOM   1451  C  CG    . ASN   A 1  186 ? -28.318 66.974  -52.432  1.00 33.74  ? 186 ASN   A CG    1 
ATOM   1452  O  OD1   . ASN   A 1  186 ? -29.073 66.020  -52.212  1.00 30.06  ? 186 ASN   A OD1   1 
ATOM   1453  N  ND2   . ASN   A 1  186 ? -27.514 67.477  -51.506  1.00 28.23  ? 186 ASN   A ND2   1 
ATOM   1454  N  N     . SER   A 1  187 ? -27.796 67.401  -57.009  1.00 31.69  ? 187 SER   A N     1 
ATOM   1455  C  CA    . SER   A 1  187 ? -27.701 68.160  -58.249  1.00 33.73  ? 187 SER   A CA    1 
ATOM   1456  C  C     . SER   A 1  187 ? -28.665 67.623  -59.296  1.00 33.05  ? 187 SER   A C     1 
ATOM   1457  O  O     . SER   A 1  187 ? -29.338 68.397  -59.980  1.00 33.30  ? 187 SER   A O     1 
ATOM   1458  C  CB    . SER   A 1  187 ? -26.265 68.149  -58.782  1.00 27.42  ? 187 SER   A CB    1 
ATOM   1459  O  OG    . SER   A 1  187 ? -25.477 69.035  -58.015  1.00 28.92  ? 187 SER   A OG    1 
ATOM   1460  N  N     . ILE   A 1  188 ? -28.718 66.297  -59.459  1.00 33.99  ? 188 ILE   A N     1 
ATOM   1461  C  CA    . ILE   A 1  188 ? -29.648 65.704  -60.415  1.00 34.71  ? 188 ILE   A CA    1 
ATOM   1462  C  C     . ILE   A 1  188 ? -31.090 65.899  -59.942  1.00 40.54  ? 188 ILE   A C     1 
ATOM   1463  O  O     . ILE   A 1  188 ? -31.971 66.276  -60.725  1.00 38.56  ? 188 ILE   A O     1 
ATOM   1464  C  CB    . ILE   A 1  188 ? -29.304 64.221  -60.643  1.00 29.79  ? 188 ILE   A CB    1 
ATOM   1465  C  CG1   . ILE   A 1  188 ? -28.226 64.065  -61.710  1.00 36.74  ? 188 ILE   A CG1   1 
ATOM   1466  C  CG2   . ILE   A 1  188 ? -30.511 63.459  -61.122  1.00 39.75  ? 188 ILE   A CG2   1 
ATOM   1467  C  CD1   . ILE   A 1  188 ? -26.929 64.740  -61.382  1.00 40.91  ? 188 ILE   A CD1   1 
ATOM   1468  N  N     . LEU   A 1  189 ? -31.337 65.698  -58.644  1.00 40.63  ? 189 LEU   A N     1 
ATOM   1469  C  CA    . LEU   A 1  189 ? -32.664 65.918  -58.071  1.00 36.31  ? 189 LEU   A CA    1 
ATOM   1470  C  C     . LEU   A 1  189 ? -33.201 67.304  -58.400  1.00 39.55  ? 189 LEU   A C     1 
ATOM   1471  O  O     . LEU   A 1  189 ? -34.313 67.442  -58.926  1.00 37.98  ? 189 LEU   A O     1 
ATOM   1472  C  CB    . LEU   A 1  189 ? -32.622 65.707  -56.558  1.00 31.99  ? 189 LEU   A CB    1 
ATOM   1473  C  CG    . LEU   A 1  189 ? -32.556 64.239  -56.079  1.00 33.27  ? 189 LEU   A CG    1 
ATOM   1474  C  CD1   . LEU   A 1  189 ? -32.320 64.185  -54.578  1.00 31.88  ? 189 LEU   A CD1   1 
ATOM   1475  C  CD2   . LEU   A 1  189 ? -33.834 63.489  -56.449  1.00 26.03  ? 189 LEU   A CD2   1 
ATOM   1476  N  N     . THR   A 1  190 ? -32.414 68.347  -58.117  1.00 38.37  ? 190 THR   A N     1 
ATOM   1477  C  CA    . THR   A 1  190 ? -32.918 69.709  -58.293  1.00 37.63  ? 190 THR   A CA    1 
ATOM   1478  C  C     . THR   A 1  190 ? -32.995 70.130  -59.758  1.00 39.32  ? 190 THR   A C     1 
ATOM   1479  O  O     . THR   A 1  190 ? -33.829 70.974  -60.107  1.00 36.89  ? 190 THR   A O     1 
ATOM   1480  C  CB    . THR   A 1  190 ? -32.046 70.695  -57.554  1.00 32.14  ? 190 THR   A CB    1 
ATOM   1481  O  OG1   . THR   A 1  190 ? -32.788 71.893  -57.364  1.00 26.24  ? 190 THR   A OG1   1 
ATOM   1482  C  CG2   . THR   A 1  190 ? -30.821 70.988  -58.389  1.00 33.97  ? 190 THR   A CG2   1 
ATOM   1483  N  N     . THR   A 1  191 ? -32.127 69.583  -60.618  1.00 36.66  ? 191 THR   A N     1 
ATOM   1484  C  CA    . THR   A 1  191 ? -32.209 69.886  -62.046  1.00 41.68  ? 191 THR   A CA    1 
ATOM   1485  C  C     . THR   A 1  191 ? -33.465 69.279  -62.648  1.00 32.90  ? 191 THR   A C     1 
ATOM   1486  O  O     . THR   A 1  191 ? -34.154 69.919  -63.445  1.00 44.99  ? 191 THR   A O     1 
ATOM   1487  C  CB    . THR   A 1  191 ? -30.961 69.377  -62.795  1.00 35.18  ? 191 THR   A CB    1 
ATOM   1488  O  OG1   . THR   A 1  191 ? -29.769 69.900  -62.200  1.00 36.38  ? 191 THR   A OG1   1 
ATOM   1489  C  CG2   . THR   A 1  191 ? -30.976 69.809  -64.234  1.00 26.75  ? 191 THR   A CG2   1 
ATOM   1490  N  N     . HIS   A 1  192 ? -33.780 68.046  -62.276  1.00 41.61  ? 192 HIS   A N     1 
ATOM   1491  C  CA    . HIS   A 1  192 ? -34.962 67.392  -62.823  1.00 44.23  ? 192 HIS   A CA    1 
ATOM   1492  C  C     . HIS   A 1  192 ? -36.240 68.123  -62.414  1.00 41.32  ? 192 HIS   A C     1 
ATOM   1493  O  O     . HIS   A 1  192 ? -37.182 68.226  -63.200  1.00 52.52  ? 192 HIS   A O     1 
ATOM   1494  C  CB    . HIS   A 1  192 ? -34.990 65.930  -62.373  1.00 36.03  ? 192 HIS   A CB    1 
ATOM   1495  C  CG    . HIS   A 1  192 ? -36.365 65.344  -62.290  1.00 48.23  ? 192 HIS   A CG    1 
ATOM   1496  N  ND1   . HIS   A 1  192 ? -37.221 65.294  -63.369  1.00 47.89  ? 192 HIS   A ND1   1 
ATOM   1497  C  CD2   . HIS   A 1  192 ? -37.028 64.774  -61.256  1.00 50.00  ? 192 HIS   A CD2   1 
ATOM   1498  C  CE1   . HIS   A 1  192 ? -38.354 64.724  -62.999  1.00 47.47  ? 192 HIS   A CE1   1 
ATOM   1499  N  NE2   . HIS   A 1  192 ? -38.263 64.398  -61.723  1.00 43.59  ? 192 HIS   A NE2   1 
ATOM   1500  N  N     . THR   A 1  193 ? -36.283 68.661  -61.210  1.00 39.59  ? 193 THR   A N     1 
ATOM   1501  C  CA    . THR   A 1  193 ? -37.519 69.255  -60.724  1.00 40.07  ? 193 THR   A CA    1 
ATOM   1502  C  C     . THR   A 1  193 ? -37.632 70.722  -61.081  1.00 40.09  ? 193 THR   A C     1 
ATOM   1503  O  O     . THR   A 1  193 ? -38.742 71.220  -61.278  1.00 42.12  ? 193 THR   A O     1 
ATOM   1504  C  CB    . THR   A 1  193 ? -37.629 69.053  -59.206  1.00 37.34  ? 193 THR   A CB    1 
ATOM   1505  O  OG1   . THR   A 1  193 ? -37.987 67.685  -58.944  1.00 36.93  ? 193 THR   A OG1   1 
ATOM   1506  C  CG2   . THR   A 1  193 ? -38.667 69.999  -58.583  1.00 44.72  ? 193 THR   A CG2   1 
ATOM   1507  N  N     . THR   A 1  194 ? -36.507 71.415  -61.197  1.00 40.55  ? 194 THR   A N     1 
ATOM   1508  C  CA    . THR   A 1  194 ? -36.509 72.792  -61.666  1.00 39.54  ? 194 THR   A CA    1 
ATOM   1509  C  C     . THR   A 1  194 ? -36.573 72.911  -63.192  1.00 38.78  ? 194 THR   A C     1 
ATOM   1510  O  O     . THR   A 1  194 ? -36.918 73.985  -63.696  1.00 37.90  ? 194 THR   A O     1 
ATOM   1511  C  CB    . THR   A 1  194 ? -35.262 73.493  -61.130  1.00 32.89  ? 194 THR   A CB    1 
ATOM   1512  O  OG1   . THR   A 1  194 ? -35.089 73.114  -59.764  1.00 39.60  ? 194 THR   A OG1   1 
ATOM   1513  C  CG2   . THR   A 1  194 ? -35.399 74.988  -61.216  1.00 27.78  ? 194 THR   A CG2   1 
ATOM   1514  N  N     . LEU   A 1  195 ? -36.290 71.836  -63.937  1.00 35.36  ? 195 LEU   A N     1 
ATOM   1515  C  CA    . LEU   A 1  195 ? -36.038 71.969  -65.370  1.00 40.19  ? 195 LEU   A CA    1 
ATOM   1516  C  C     . LEU   A 1  195 ? -37.155 72.739  -66.074  1.00 39.67  ? 195 LEU   A C     1 
ATOM   1517  O  O     . LEU   A 1  195 ? -36.919 73.794  -66.669  1.00 49.62  ? 195 LEU   A O     1 
ATOM   1518  C  CB    . LEU   A 1  195 ? -35.831 70.593  -66.006  1.00 33.30  ? 195 LEU   A CB    1 
ATOM   1519  C  CG    . LEU   A 1  195 ? -35.028 70.696  -67.308  1.00 47.68  ? 195 LEU   A CG    1 
ATOM   1520  C  CD1   . LEU   A 1  195 ? -33.926 71.726  -67.143  1.00 47.58  ? 195 LEU   A CD1   1 
ATOM   1521  C  CD2   . LEU   A 1  195 ? -34.420 69.365  -67.763  1.00 44.14  ? 195 LEU   A CD2   1 
ATOM   1522  N  N     . GLU   A 1  196 ? -38.382 72.232  -66.014  1.00 40.82  ? 196 GLU   A N     1 
ATOM   1523  C  CA    . GLU   A 1  196 ? -39.462 72.864  -66.758  1.00 40.68  ? 196 GLU   A CA    1 
ATOM   1524  C  C     . GLU   A 1  196 ? -39.832 74.233  -66.202  1.00 44.93  ? 196 GLU   A C     1 
ATOM   1525  O  O     . GLU   A 1  196 ? -40.510 74.998  -66.892  1.00 53.09  ? 196 GLU   A O     1 
ATOM   1526  C  CB    . GLU   A 1  196 ? -40.692 71.953  -66.791  1.00 34.59  ? 196 GLU   A CB    1 
ATOM   1527  C  CG    . GLU   A 1  196 ? -41.774 72.370  -67.787  1.00 70.27  ? 196 GLU   A CG    1 
ATOM   1528  C  CD    . GLU   A 1  196 ? -41.506 71.914  -69.225  1.00 87.12  ? 196 GLU   A CD    1 
ATOM   1529  O  OE1   . GLU   A 1  196 ? -41.200 70.715  -69.429  1.00 90.18  ? 196 GLU   A OE1   1 
ATOM   1530  O  OE2   . GLU   A 1  196 ? -41.615 72.754  -70.152  1.00 79.57  ? 196 GLU   A OE2   1 
ATOM   1531  N  N     . HIS   A 1  197 ? -39.371 74.594  -65.016  1.00 36.61  ? 197 HIS   A N     1 
ATOM   1532  C  CA    . HIS   A 1  197 ? -39.749 75.868  -64.434  1.00 34.79  ? 197 HIS   A CA    1 
ATOM   1533  C  C     . HIS   A 1  197 ? -38.708 76.966  -64.618  1.00 40.34  ? 197 HIS   A C     1 
ATOM   1534  O  O     . HIS   A 1  197 ? -38.956 78.098  -64.204  1.00 34.32  ? 197 HIS   A O     1 
ATOM   1535  C  CB    . HIS   A 1  197 ? -40.056 75.689  -62.952  1.00 35.36  ? 197 HIS   A CB    1 
ATOM   1536  C  CG    . HIS   A 1  197 ? -41.078 74.635  -62.682  1.00 42.84  ? 197 HIS   A CG    1 
ATOM   1537  N  ND1   . HIS   A 1  197 ? -40.768 73.292  -62.637  1.00 42.98  ? 197 HIS   A ND1   1 
ATOM   1538  C  CD2   . HIS   A 1  197 ? -42.409 74.721  -62.454  1.00 42.62  ? 197 HIS   A CD2   1 
ATOM   1539  C  CE1   . HIS   A 1  197 ? -41.861 72.598  -62.370  1.00 45.97  ? 197 HIS   A CE1   1 
ATOM   1540  N  NE2   . HIS   A 1  197 ? -42.871 73.441  -62.264  1.00 47.63  ? 197 HIS   A NE2   1 
ATOM   1541  N  N     . SER   A 1  198 ? -37.567 76.676  -65.233  1.00 43.44  ? 198 SER   A N     1 
ATOM   1542  C  CA    . SER   A 1  198 ? -36.541 77.676  -65.497  1.00 44.36  ? 198 SER   A CA    1 
ATOM   1543  C  C     . SER   A 1  198 ? -36.457 77.968  -66.999  1.00 45.31  ? 198 SER   A C     1 
ATOM   1544  O  O     . SER   A 1  198 ? -36.618 77.065  -67.832  1.00 44.37  ? 198 SER   A O     1 
ATOM   1545  C  CB    . SER   A 1  198 ? -35.183 77.204  -64.962  1.00 43.06  ? 198 SER   A CB    1 
ATOM   1546  O  OG    . SER   A 1  198 ? -34.184 78.216  -65.055  1.00 40.97  ? 198 SER   A OG    1 
ATOM   1547  N  N     . ASP   A 1  199 ? -36.203 79.232  -67.344  1.00 27.49  ? 199 ASP   A N     1 
ATOM   1548  C  CA    . ASP   A 1  199 ? -36.129 79.642  -68.740  1.00 35.58  ? 199 ASP   A CA    1 
ATOM   1549  C  C     . ASP   A 1  199 ? -34.703 79.740  -69.245  1.00 41.15  ? 199 ASP   A C     1 
ATOM   1550  O  O     . ASP   A 1  199 ? -34.447 79.507  -70.431  1.00 36.30  ? 199 ASP   A O     1 
ATOM   1551  C  CB    . ASP   A 1  199 ? -36.811 81.000  -68.941  1.00 38.42  ? 199 ASP   A CB    1 
ATOM   1552  C  CG    . ASP   A 1  199 ? -38.264 81.006  -68.493  1.00 42.07  ? 199 ASP   A CG    1 
ATOM   1553  O  OD1   . ASP   A 1  199 ? -39.036 80.176  -69.025  1.00 34.92  ? 199 ASP   A OD1   1 
ATOM   1554  O  OD2   . ASP   A 1  199 ? -38.618 81.844  -67.610  1.00 34.82  ? 199 ASP   A OD2   1 
ATOM   1555  N  N     . CYS   A 1  200 ? -33.770 80.086  -68.372  1.00 37.00  ? 200 CYS   A N     1 
ATOM   1556  C  CA    . CYS   A 1  200 ? -32.390 80.252  -68.788  1.00 35.19  ? 200 CYS   A CA    1 
ATOM   1557  C  C     . CYS   A 1  200 ? -31.527 80.033  -67.562  1.00 35.55  ? 200 CYS   A C     1 
ATOM   1558  O  O     . CYS   A 1  200 ? -31.701 80.728  -66.552  1.00 35.25  ? 200 CYS   A O     1 
ATOM   1559  C  CB    . CYS   A 1  200 ? -32.173 81.645  -69.384  1.00 34.73  ? 200 CYS   A CB    1 
ATOM   1560  S  SG    . CYS   A 1  200 ? -30.625 81.811  -70.276  1.00 31.09  ? 200 CYS   A SG    1 
ATOM   1561  N  N     . ALA   A 1  201 ? -30.608 79.079  -67.628  1.00 29.36  ? 201 ALA   A N     1 
ATOM   1562  C  CA    . ALA   A 1  201 ? -29.774 78.784  -66.468  1.00 34.05  ? 201 ALA   A CA    1 
ATOM   1563  C  C     . ALA   A 1  201 ? -28.307 78.983  -66.823  1.00 32.95  ? 201 ALA   A C     1 
ATOM   1564  O  O     . ALA   A 1  201 ? -27.810 78.388  -67.792  1.00 31.67  ? 201 ALA   A O     1 
ATOM   1565  C  CB    . ALA   A 1  201 ? -30.034 77.367  -65.962  1.00 34.14  ? 201 ALA   A CB    1 
ATOM   1566  N  N     . PHE   A 1  202 ? -27.621 79.825  -66.038  1.00 29.42  ? 202 PHE   A N     1 
ATOM   1567  C  CA    . PHE   A 1  202 ? -26.191 80.086  -66.215  1.00 31.52  ? 202 PHE   A CA    1 
ATOM   1568  C  C     . PHE   A 1  202 ? -25.415 79.261  -65.190  1.00 34.92  ? 202 PHE   A C     1 
ATOM   1569  O  O     . PHE   A 1  202 ? -25.358 79.601  -64.003  1.00 29.03  ? 202 PHE   A O     1 
ATOM   1570  C  CB    . PHE   A 1  202 ? -25.900 81.580  -66.109  1.00 32.21  ? 202 PHE   A CB    1 
ATOM   1571  C  CG    . PHE   A 1  202 ? -26.526 82.376  -67.211  1.00 33.60  ? 202 PHE   A CG    1 
ATOM   1572  C  CD1   . PHE   A 1  202 ? -26.074 82.238  -68.522  1.00 32.56  ? 202 PHE   A CD1   1 
ATOM   1573  C  CD2   . PHE   A 1  202 ? -27.583 83.223  -66.953  1.00 24.82  ? 202 PHE   A CD2   1 
ATOM   1574  C  CE1   . PHE   A 1  202 ? -26.657 82.954  -69.555  1.00 35.97  ? 202 PHE   A CE1   1 
ATOM   1575  C  CE2   . PHE   A 1  202 ? -28.176 83.934  -67.975  1.00 34.77  ? 202 PHE   A CE2   1 
ATOM   1576  C  CZ    . PHE   A 1  202 ? -27.709 83.805  -69.285  1.00 34.36  ? 202 PHE   A CZ    1 
ATOM   1577  N  N     . MET   A 1  203 ? -24.840 78.161  -65.661  1.00 26.81  ? 203 MET   A N     1 
ATOM   1578  C  CA    . MET   A 1  203 ? -24.185 77.183  -64.811  1.00 34.50  ? 203 MET   A CA    1 
ATOM   1579  C  C     . MET   A 1  203 ? -22.732 77.572  -64.617  1.00 37.49  ? 203 MET   A C     1 
ATOM   1580  O  O     . MET   A 1  203 ? -21.972 77.661  -65.586  1.00 35.99  ? 203 MET   A O     1 
ATOM   1581  C  CB    . MET   A 1  203 ? -24.256 75.789  -65.432  1.00 39.47  ? 203 MET   A CB    1 
ATOM   1582  C  CG    . MET   A 1  203 ? -25.424 74.954  -64.992  1.00 32.94  ? 203 MET   A CG    1 
ATOM   1583  S  SD    . MET   A 1  203 ? -24.904 73.235  -64.942  1.00 43.93  ? 203 MET   A SD    1 
ATOM   1584  C  CE    . MET   A 1  203 ? -24.494 72.903  -66.635  1.00 33.19  ? 203 MET   A CE    1 
ATOM   1585  N  N     . VAL   A 1  204 ? -22.330 77.752  -63.372  1.00 29.99  ? 204 VAL   A N     1 
ATOM   1586  C  CA    . VAL   A 1  204 ? -20.943 78.056  -63.058  1.00 32.34  ? 204 VAL   A CA    1 
ATOM   1587  C  C     . VAL   A 1  204 ? -20.356 76.851  -62.326  1.00 33.14  ? 204 VAL   A C     1 
ATOM   1588  O  O     . VAL   A 1  204 ? -20.770 76.513  -61.206  1.00 29.21  ? 204 VAL   A O     1 
ATOM   1589  C  CB    . VAL   A 1  204 ? -20.822 79.354  -62.250  1.00 30.87  ? 204 VAL   A CB    1 
ATOM   1590  C  CG1   . VAL   A 1  204 ? -19.390 79.561  -61.772  1.00 29.14  ? 204 VAL   A CG1   1 
ATOM   1591  C  CG2   . VAL   A 1  204 ? -21.267 80.523  -63.120  1.00 26.99  ? 204 VAL   A CG2   1 
ATOM   1592  N  N     . ASP   A 1  205 ? -19.405 76.187  -62.980  1.00 30.51  ? 205 ASP   A N     1 
ATOM   1593  C  CA    . ASP   A 1  205 ? -18.676 75.070  -62.390  1.00 26.76  ? 205 ASP   A CA    1 
ATOM   1594  C  C     . ASP   A 1  205 ? -17.601 75.613  -61.466  1.00 28.49  ? 205 ASP   A C     1 
ATOM   1595  O  O     . ASP   A 1  205 ? -16.619 76.214  -61.923  1.00 25.70  ? 205 ASP   A O     1 
ATOM   1596  C  CB    . ASP   A 1  205 ? -18.049 74.205  -63.472  1.00 23.51  ? 205 ASP   A CB    1 
ATOM   1597  C  CG    . ASP   A 1  205 ? -17.557 72.888  -62.931  1.00 25.73  ? 205 ASP   A CG    1 
ATOM   1598  O  OD1   . ASP   A 1  205 ? -17.285 72.840  -61.716  1.00 39.53  ? 205 ASP   A OD1   1 
ATOM   1599  O  OD2   . ASP   A 1  205 ? -17.447 71.899  -63.696  1.00 24.17  ? 205 ASP   A OD2   1 
ATOM   1600  N  N     . ASN   A 1  206 ? -17.773 75.379  -60.166  1.00 30.19  ? 206 ASN   A N     1 
ATOM   1601  C  CA    . ASN   A 1  206 ? -16.763 75.798  -59.200  1.00 27.50  ? 206 ASN   A CA    1 
ATOM   1602  C  C     . ASN   A 1  206 ? -15.365 75.387  -59.635  1.00 26.86  ? 206 ASN   A C     1 
ATOM   1603  O  O     . ASN   A 1  206 ? -14.406 76.125  -59.411  1.00 26.19  ? 206 ASN   A O     1 
ATOM   1604  C  CB    . ASN   A 1  206 ? -17.081 75.224  -57.832  1.00 19.90  ? 206 ASN   A CB    1 
ATOM   1605  C  CG    . ASN   A 1  206 ? -17.770 76.222  -56.945  1.00 25.02  ? 206 ASN   A CG    1 
ATOM   1606  O  OD1   . ASN   A 1  206 ? -18.040 77.349  -57.359  1.00 27.60  ? 206 ASN   A OD1   1 
ATOM   1607  N  ND2   . ASN   A 1  206 ? -18.065 75.820  -55.716  1.00 24.12  ? 206 ASN   A ND2   1 
ATOM   1608  N  N     . GLU   A 1  207 ? -15.229 74.223  -60.276  1.00 24.24  ? 207 GLU   A N     1 
ATOM   1609  C  CA    . GLU   A 1  207 ? -13.913 73.804  -60.746  1.00 31.30  ? 207 GLU   A CA    1 
ATOM   1610  C  C     . GLU   A 1  207 ? -13.324 74.820  -61.729  1.00 36.37  ? 207 GLU   A C     1 
ATOM   1611  O  O     . GLU   A 1  207 ? -12.165 75.237  -61.591  1.00 32.65  ? 207 GLU   A O     1 
ATOM   1612  C  CB    . GLU   A 1  207 ? -13.998 72.427  -61.392  1.00 32.98  ? 207 GLU   A CB    1 
ATOM   1613  C  CG    . GLU   A 1  207 ? -12.789 72.090  -62.250  1.00 28.95  ? 207 GLU   A CG    1 
ATOM   1614  C  CD    . GLU   A 1  207 ? -13.032 70.896  -63.145  1.00 34.82  ? 207 GLU   A CD    1 
ATOM   1615  O  OE1   . GLU   A 1  207 ? -13.753 71.038  -64.162  1.00 39.23  ? 207 GLU   A OE1   1 
ATOM   1616  O  OE2   . GLU   A 1  207 ? -12.509 69.805  -62.826  1.00 42.16  ? 207 GLU   A OE2   1 
ATOM   1617  N  N     . ALA   A 1  208 ? -14.112 75.237  -62.726  1.00 31.85  ? 208 ALA   A N     1 
ATOM   1618  C  CA    . ALA   A 1  208 ? -13.614 76.206  -63.698  1.00 27.90  ? 208 ALA   A CA    1 
ATOM   1619  C  C     . ALA   A 1  208 ? -13.152 77.485  -63.009  1.00 30.14  ? 208 ALA   A C     1 
ATOM   1620  O  O     . ALA   A 1  208 ? -12.036 77.964  -63.250  1.00 21.79  ? 208 ALA   A O     1 
ATOM   1621  C  CB    . ALA   A 1  208 ? -14.682 76.506  -64.749  1.00 22.32  ? 208 ALA   A CB    1 
ATOM   1622  N  N     . ILE   A 1  209 ? -13.995 78.045  -62.133  1.00 29.10  ? 209 ILE   A N     1 
ATOM   1623  C  CA    . ILE   A 1  209 ? -13.631 79.275  -61.437  1.00 22.37  ? 209 ILE   A CA    1 
ATOM   1624  C  C     . ILE   A 1  209 ? -12.389 79.050  -60.605  1.00 34.29  ? 209 ILE   A C     1 
ATOM   1625  O  O     . ILE   A 1  209 ? -11.530 79.934  -60.474  1.00 36.38  ? 209 ILE   A O     1 
ATOM   1626  C  CB    . ILE   A 1  209 ? -14.793 79.768  -60.560  1.00 31.18  ? 209 ILE   A CB    1 
ATOM   1627  C  CG1   . ILE   A 1  209 ? -16.010 80.034  -61.426  1.00 38.71  ? 209 ILE   A CG1   1 
ATOM   1628  C  CG2   . ILE   A 1  209 ? -14.390 81.038  -59.866  1.00 37.11  ? 209 ILE   A CG2   1 
ATOM   1629  C  CD1   . ILE   A 1  209 ? -15.611 80.618  -62.746  1.00 31.82  ? 209 ILE   A CD1   1 
ATOM   1630  N  N     . TYR   A 1  210 ? -12.279 77.861  -60.018  1.00 34.11  ? 210 TYR   A N     1 
ATOM   1631  C  CA    . TYR   A 1  210 ? -11.174 77.585  -59.117  1.00 34.62  ? 210 TYR   A CA    1 
ATOM   1632  C  C     . TYR   A 1  210 ? -9.846  77.678  -59.842  1.00 36.84  ? 210 TYR   A C     1 
ATOM   1633  O  O     . TYR   A 1  210 ? -8.901  78.288  -59.332  1.00 37.07  ? 210 TYR   A O     1 
ATOM   1634  C  CB    . TYR   A 1  210 ? -11.355 76.206  -58.501  1.00 34.64  ? 210 TYR   A CB    1 
ATOM   1635  C  CG    . TYR   A 1  210 ? -10.446 75.940  -57.351  1.00 30.77  ? 210 TYR   A CG    1 
ATOM   1636  C  CD1   . TYR   A 1  210 ? -10.677 76.517  -56.121  1.00 31.06  ? 210 TYR   A CD1   1 
ATOM   1637  C  CD2   . TYR   A 1  210 ? -9.355  75.091  -57.493  1.00 38.86  ? 210 TYR   A CD2   1 
ATOM   1638  C  CE1   . TYR   A 1  210 ? -9.846  76.259  -55.046  1.00 40.10  ? 210 TYR   A CE1   1 
ATOM   1639  C  CE2   . TYR   A 1  210 ? -8.518  74.825  -56.441  1.00 35.43  ? 210 TYR   A CE2   1 
ATOM   1640  C  CZ    . TYR   A 1  210 ? -8.768  75.409  -55.213  1.00 39.63  ? 210 TYR   A CZ    1 
ATOM   1641  O  OH    . TYR   A 1  210 ? -7.924  75.148  -54.160  1.00 38.96  ? 210 TYR   A OH    1 
ATOM   1642  N  N     . ASP   A 1  211 ? -9.773  77.091  -61.051  1.00 33.94  ? 211 ASP   A N     1 
ATOM   1643  C  CA    . ASP   A 1  211 ? -8.540  77.078  -61.838  1.00 36.95  ? 211 ASP   A CA    1 
ATOM   1644  C  C     . ASP   A 1  211 ? -8.231  78.427  -62.468  1.00 34.18  ? 211 ASP   A C     1 
ATOM   1645  O  O     . ASP   A 1  211 ? -7.052  78.765  -62.616  1.00 40.47  ? 211 ASP   A O     1 
ATOM   1646  C  CB    . ASP   A 1  211 ? -8.601  76.003  -62.925  1.00 36.66  ? 211 ASP   A CB    1 
ATOM   1647  C  CG    . ASP   A 1  211 ? -8.456  74.605  -62.359  1.00 54.27  ? 211 ASP   A CG    1 
ATOM   1648  O  OD1   . ASP   A 1  211 ? -8.226  74.495  -61.121  1.00 54.85  ? 211 ASP   A OD1   1 
ATOM   1649  O  OD2   . ASP   A 1  211 ? -8.582  73.620  -63.137  1.00 54.60  ? 211 ASP   A OD2   1 
ATOM   1650  N  N     . ILE   A 1  212 ? -9.251  79.201  -62.857  1.00 32.51  ? 212 ILE   A N     1 
ATOM   1651  C  CA    . ILE   A 1  212 ? -9.001  80.576  -63.296  1.00 37.70  ? 212 ILE   A CA    1 
ATOM   1652  C  C     . ILE   A 1  212 ? -8.367  81.383  -62.168  1.00 36.88  ? 212 ILE   A C     1 
ATOM   1653  O  O     . ILE   A 1  212 ? -7.459  82.190  -62.398  1.00 43.57  ? 212 ILE   A O     1 
ATOM   1654  C  CB    . ILE   A 1  212 ? -10.295 81.239  -63.814  1.00 30.54  ? 212 ILE   A CB    1 
ATOM   1655  C  CG1   . ILE   A 1  212 ? -10.653 80.708  -65.207  1.00 30.67  ? 212 ILE   A CG1   1 
ATOM   1656  C  CG2   . ILE   A 1  212 ? -10.115 82.732  -63.892  1.00 22.55  ? 212 ILE   A CG2   1 
ATOM   1657  C  CD1   . ILE   A 1  212 ? -12.126 80.745  -65.515  1.00 23.51  ? 212 ILE   A CD1   1 
ATOM   1658  N  N     . CYS   A 1  213 ? -8.811  81.154  -60.926  1.00 41.60  ? 213 CYS   A N     1 
ATOM   1659  C  CA    . CYS   A 1  213 ? -8.224  81.840  -59.777  1.00 41.84  ? 213 CYS   A CA    1 
ATOM   1660  C  C     . CYS   A 1  213 ? -6.775  81.415  -59.539  1.00 36.91  ? 213 CYS   A C     1 
ATOM   1661  O  O     . CYS   A 1  213 ? -5.940  82.245  -59.165  1.00 37.87  ? 213 CYS   A O     1 
ATOM   1662  C  CB    . CYS   A 1  213 ? -9.069  81.586  -58.524  1.00 32.57  ? 213 CYS   A CB    1 
ATOM   1663  S  SG    . CYS   A 1  213 ? -10.612 82.481  -58.525  1.00 32.09  ? 213 CYS   A SG    1 
ATOM   1664  N  N     . ARG   A 1  214 ? -6.455  80.132  -59.715  1.00 28.07  ? 214 ARG   A N     1 
ATOM   1665  C  CA    . ARG   A 1  214 ? -5.063  79.709  -59.549  1.00 42.90  ? 214 ARG   A CA    1 
ATOM   1666  C  C     . ARG   A 1  214 ? -4.213  80.137  -60.733  1.00 36.06  ? 214 ARG   A C     1 
ATOM   1667  O  O     . ARG   A 1  214 ? -3.157  80.746  -60.551  1.00 42.53  ? 214 ARG   A O     1 
ATOM   1668  C  CB    . ARG   A 1  214 ? -4.951  78.194  -59.372  1.00 46.09  ? 214 ARG   A CB    1 
ATOM   1669  C  CG    . ARG   A 1  214 ? -5.288  77.674  -58.010  1.00 33.83  ? 214 ARG   A CG    1 
ATOM   1670  C  CD    . ARG   A 1  214 ? -5.959  76.327  -58.189  1.00 48.11  ? 214 ARG   A CD    1 
ATOM   1671  N  NE    . ARG   A 1  214 ? -5.114  75.200  -57.809  1.00 45.61  ? 214 ARG   A NE    1 
ATOM   1672  C  CZ    . ARG   A 1  214 ? -5.281  73.964  -58.253  1.00 39.75  ? 214 ARG   A CZ    1 
ATOM   1673  N  NH1   . ARG   A 1  214 ? -6.224  73.667  -59.135  1.00 42.25  ? 214 ARG   A NH1   1 
ATOM   1674  N  NH2   . ARG   A 1  214 ? -4.472  73.006  -57.820  1.00 49.90  ? 214 ARG   A NH2   1 
ATOM   1675  N  N     . ARG   A 1  215 ? -4.668  79.840  -61.958  1.00 35.24  ? 215 ARG   A N     1 
ATOM   1676  C  CA    . ARG   A 1  215 ? -3.829  80.034  -63.138  1.00 36.27  ? 215 ARG   A CA    1 
ATOM   1677  C  C     . ARG   A 1  215 ? -3.660  81.507  -63.493  1.00 35.37  ? 215 ARG   A C     1 
ATOM   1678  O  O     . ARG   A 1  215 ? -2.568  81.923  -63.888  1.00 40.32  ? 215 ARG   A O     1 
ATOM   1679  C  CB    . ARG   A 1  215 ? -4.394  79.263  -64.331  1.00 34.11  ? 215 ARG   A CB    1 
ATOM   1680  C  CG    . ARG   A 1  215 ? -4.227  77.741  -64.275  1.00 31.82  ? 215 ARG   A CG    1 
ATOM   1681  C  CD    . ARG   A 1  215 ? -4.940  77.102  -65.470  1.00 56.51  ? 215 ARG   A CD    1 
ATOM   1682  N  NE    . ARG   A 1  215 ? -5.594  78.122  -66.296  1.00 62.09  ? 215 ARG   A NE    1 
ATOM   1683  C  CZ    . ARG   A 1  215 ? -6.908  78.244  -66.475  1.00 51.90  ? 215 ARG   A CZ    1 
ATOM   1684  N  NH1   . ARG   A 1  215 ? -7.765  77.352  -65.987  1.00 43.75  ? 215 ARG   A NH1   1 
ATOM   1685  N  NH2   . ARG   A 1  215 ? -7.374  79.294  -67.151  1.00 42.12  ? 215 ARG   A NH2   1 
ATOM   1686  N  N     . ASN   A 1  216 ? -4.714  82.316  -63.368  1.00 34.88  ? 216 ASN   A N     1 
ATOM   1687  C  CA    . ASN   A 1  216 ? -4.654  83.685  -63.858  1.00 33.77  ? 216 ASN   A CA    1 
ATOM   1688  C  C     . ASN   A 1  216 ? -4.587  84.743  -62.779  1.00 42.75  ? 216 ASN   A C     1 
ATOM   1689  O  O     . ASN   A 1  216 ? -4.110  85.850  -63.060  1.00 37.43  ? 216 ASN   A O     1 
ATOM   1690  C  CB    . ASN   A 1  216 ? -5.853  83.993  -64.753  1.00 36.05  ? 216 ASN   A CB    1 
ATOM   1691  C  CG    . ASN   A 1  216 ? -5.913  83.079  -65.929  1.00 37.07  ? 216 ASN   A CG    1 
ATOM   1692  O  OD1   . ASN   A 1  216 ? -4.897  82.526  -66.338  1.00 44.06  ? 216 ASN   A OD1   1 
ATOM   1693  N  ND2   . ASN   A 1  216 ? -7.097  82.888  -66.471  1.00 34.75  ? 216 ASN   A ND2   1 
ATOM   1694  N  N     . LEU   A 1  217 ? -5.069  84.459  -61.576  1.00 39.47  ? 217 LEU   A N     1 
ATOM   1695  C  CA    . LEU   A 1  217 ? -4.936  85.406  -60.479  1.00 37.00  ? 217 LEU   A CA    1 
ATOM   1696  C  C     . LEU   A 1  217 ? -3.797  85.040  -59.542  1.00 40.06  ? 217 LEU   A C     1 
ATOM   1697  O  O     . LEU   A 1  217 ? -3.517  85.791  -58.604  1.00 37.36  ? 217 LEU   A O     1 
ATOM   1698  C  CB    . LEU   A 1  217 ? -6.249  85.508  -59.700  1.00 42.78  ? 217 LEU   A CB    1 
ATOM   1699  C  CG    . LEU   A 1  217 ? -7.437  86.022  -60.517  1.00 46.42  ? 217 LEU   A CG    1 
ATOM   1700  C  CD1   . LEU   A 1  217 ? -8.684  86.182  -59.651  1.00 37.94  ? 217 LEU   A CD1   1 
ATOM   1701  C  CD2   . LEU   A 1  217 ? -7.072  87.330  -61.190  1.00 35.31  ? 217 LEU   A CD2   1 
ATOM   1702  N  N     . ASP   A 1  218 ? -3.124  83.915  -59.783  1.00 37.46  ? 218 ASP   A N     1 
ATOM   1703  C  CA    . ASP   A 1  218 ? -2.035  83.417  -58.944  1.00 45.63  ? 218 ASP   A CA    1 
ATOM   1704  C  C     . ASP   A 1  218 ? -2.483  83.020  -57.544  1.00 40.59  ? 218 ASP   A C     1 
ATOM   1705  O  O     . ASP   A 1  218 ? -1.637  82.763  -56.699  1.00 43.41  ? 218 ASP   A O     1 
ATOM   1706  C  CB    . ASP   A 1  218 ? -0.896  84.436  -58.839  1.00 40.34  ? 218 ASP   A CB    1 
ATOM   1707  C  CG    . ASP   A 1  218 ? -0.389  84.867  -60.199  1.00 49.92  ? 218 ASP   A CG    1 
ATOM   1708  O  OD1   . ASP   A 1  218 ? -0.190  83.972  -61.053  1.00 51.52  ? 218 ASP   A OD1   1 
ATOM   1709  O  OD2   . ASP   A 1  218 ? -0.217  86.091  -60.427  1.00 53.91  ? 218 ASP   A OD2   1 
ATOM   1710  N  N     . ILE   A 1  219 ? -3.790  82.959  -57.281  1.00 47.06  ? 219 ILE   A N     1 
ATOM   1711  C  CA    . ILE   A 1  219 ? -4.302  82.545  -55.977  1.00 47.34  ? 219 ILE   A CA    1 
ATOM   1712  C  C     . ILE   A 1  219 ? -3.933  81.083  -55.739  1.00 46.38  ? 219 ILE   A C     1 
ATOM   1713  O  O     . ILE   A 1  219 ? -4.330  80.193  -56.500  1.00 43.87  ? 219 ILE   A O     1 
ATOM   1714  C  CB    . ILE   A 1  219 ? -5.820  82.747  -55.895  1.00 46.81  ? 219 ILE   A CB    1 
ATOM   1715  C  CG1   . ILE   A 1  219 ? -6.224  84.123  -56.443  1.00 47.63  ? 219 ILE   A CG1   1 
ATOM   1716  C  CG2   . ILE   A 1  219 ? -6.287  82.564  -54.459  1.00 37.69  ? 219 ILE   A CG2   1 
ATOM   1717  C  CD1   . ILE   A 1  219 ? -5.946  85.276  -55.501  1.00 35.44  ? 219 ILE   A CD1   1 
ATOM   1718  N  N     . GLU   A 1  220 ? -3.190  80.822  -54.665  1.00 46.15  ? 220 GLU   A N     1 
ATOM   1719  C  CA    . GLU   A 1  220 ? -2.620  79.491  -54.491  1.00 48.17  ? 220 GLU   A CA    1 
ATOM   1720  C  C     . GLU   A 1  220 ? -3.674  78.477  -54.066  1.00 53.38  ? 220 GLU   A C     1 
ATOM   1721  O  O     . GLU   A 1  220 ? -3.658  77.327  -54.527  1.00 52.83  ? 220 GLU   A O     1 
ATOM   1722  C  CB    . GLU   A 1  220 ? -1.476  79.536  -53.482  1.00 54.20  ? 220 GLU   A CB    1 
ATOM   1723  C  CG    . GLU   A 1  220 ? -0.481  78.411  -53.690  1.00 64.57  ? 220 GLU   A CG    1 
ATOM   1724  C  CD    . GLU   A 1  220 ? 0.900   78.761  -53.192  1.00 74.56  ? 220 GLU   A CD    1 
ATOM   1725  O  OE1   . GLU   A 1  220 ? 0.968   79.494  -52.176  1.00 74.91  ? 220 GLU   A OE1   1 
ATOM   1726  O  OE2   . GLU   A 1  220 ? 1.901   78.314  -53.820  1.00 60.54  ? 220 GLU   A OE2   1 
ATOM   1727  N  N     . ARG   A 1  221 ? -4.589  78.875  -53.182  1.00 50.76  ? 221 ARG   A N     1 
ATOM   1728  C  CA    . ARG   A 1  221 ? -5.711  78.027  -52.788  1.00 40.36  ? 221 ARG   A CA    1 
ATOM   1729  C  C     . ARG   A 1  221 ? -6.935  78.927  -52.656  1.00 33.51  ? 221 ARG   A C     1 
ATOM   1730  O  O     . ARG   A 1  221 ? -7.231  79.446  -51.578  1.00 32.87  ? 221 ARG   A O     1 
ATOM   1731  C  CB    . ARG   A 1  221 ? -5.396  77.256  -51.501  1.00 40.79  ? 221 ARG   A CB    1 
ATOM   1732  C  CG    . ARG   A 1  221 ? -6.598  76.718  -50.726  1.00 48.59  ? 221 ARG   A CG    1 
ATOM   1733  C  CD    . ARG   A 1  221 ? -7.356  75.634  -51.476  1.00 47.09  ? 221 ARG   A CD    1 
ATOM   1734  N  NE    . ARG   A 1  221 ? -8.289  74.920  -50.609  1.00 43.20  ? 221 ARG   A NE    1 
ATOM   1735  C  CZ    . ARG   A 1  221 ? -9.606  75.095  -50.587  1.00 46.23  ? 221 ARG   A CZ    1 
ATOM   1736  N  NH1   . ARG   A 1  221 ? -10.215 75.911  -51.430  1.00 45.59  ? 221 ARG   A NH1   1 
ATOM   1737  N  NH2   . ARG   A 1  221 ? -10.331 74.435  -49.689  1.00 53.14  ? 221 ARG   A NH2   1 
ATOM   1738  N  N     . PRO   A 1  222 ? -7.666  79.140  -53.750  1.00 40.66  ? 222 PRO   A N     1 
ATOM   1739  C  CA    . PRO   A 1  222 ? -8.793  80.084  -53.727  1.00 36.28  ? 222 PRO   A CA    1 
ATOM   1740  C  C     . PRO   A 1  222 ? -9.824  79.780  -52.650  1.00 37.25  ? 222 PRO   A C     1 
ATOM   1741  O  O     . PRO   A 1  222 ? -10.209 78.633  -52.423  1.00 40.24  ? 222 PRO   A O     1 
ATOM   1742  C  CB    . PRO   A 1  222 ? -9.404  79.932  -55.119  1.00 30.78  ? 222 PRO   A CB    1 
ATOM   1743  C  CG    . PRO   A 1  222 ? -8.267  79.471  -55.968  1.00 38.80  ? 222 PRO   A CG    1 
ATOM   1744  C  CD    . PRO   A 1  222 ? -7.380  78.645  -55.107  1.00 40.46  ? 222 PRO   A CD    1 
ATOM   1745  N  N     . THR   A 1  223 ? -10.298 80.833  -52.010  1.00 33.90  ? 223 THR   A N     1 
ATOM   1746  C  CA    . THR   A 1  223 ? -11.422 80.749  -51.096  1.00 32.80  ? 223 THR   A CA    1 
ATOM   1747  C  C     . THR   A 1  223 ? -12.708 81.125  -51.826  1.00 32.53  ? 223 THR   A C     1 
ATOM   1748  O  O     . THR   A 1  223 ? -12.712 81.484  -53.009  1.00 27.96  ? 223 THR   A O     1 
ATOM   1749  C  CB    . THR   A 1  223 ? -11.205 81.675  -49.895  1.00 41.14  ? 223 THR   A CB    1 
ATOM   1750  O  OG1   . THR   A 1  223 ? -11.163 83.042  -50.345  1.00 41.87  ? 223 THR   A OG1   1 
ATOM   1751  C  CG2   . THR   A 1  223 ? -9.893  81.335  -49.185  1.00 43.63  ? 223 THR   A CG2   1 
ATOM   1752  N  N     . TYR   A 1  224 ? -13.817 81.060  -51.092  1.00 29.14  ? 224 TYR   A N     1 
ATOM   1753  C  CA    . TYR   A 1  224 ? -15.085 81.508  -51.642  1.00 23.50  ? 224 TYR   A CA    1 
ATOM   1754  C  C     . TYR   A 1  224 ? -15.072 83.009  -51.952  1.00 32.31  ? 224 TYR   A C     1 
ATOM   1755  O  O     . TYR   A 1  224 ? -15.783 83.459  -52.852  1.00 32.47  ? 224 TYR   A O     1 
ATOM   1756  C  CB    . TYR   A 1  224 ? -16.215 81.178  -50.678  1.00 25.01  ? 224 TYR   A CB    1 
ATOM   1757  C  CG    . TYR   A 1  224 ? -16.619 79.722  -50.557  1.00 23.04  ? 224 TYR   A CG    1 
ATOM   1758  C  CD1   . TYR   A 1  224 ? -16.658 78.879  -51.650  1.00 23.84  ? 224 TYR   A CD1   1 
ATOM   1759  C  CD2   . TYR   A 1  224 ? -17.000 79.210  -49.329  1.00 26.13  ? 224 TYR   A CD2   1 
ATOM   1760  C  CE1   . TYR   A 1  224 ? -17.057 77.562  -51.507  1.00 22.45  ? 224 TYR   A CE1   1 
ATOM   1761  C  CE2   . TYR   A 1  224 ? -17.384 77.918  -49.176  1.00 23.99  ? 224 TYR   A CE2   1 
ATOM   1762  C  CZ    . TYR   A 1  224 ? -17.418 77.089  -50.256  1.00 29.40  ? 224 TYR   A CZ    1 
ATOM   1763  O  OH    . TYR   A 1  224 ? -17.804 75.767  -50.047  1.00 34.41  ? 224 TYR   A OH    1 
ATOM   1764  N  N     . THR   A 1  225 ? -14.267 83.807  -51.252  1.00 33.02  ? 225 THR   A N     1 
ATOM   1765  C  CA    . THR   A 1  225 ? -14.219 85.226  -51.603  1.00 36.53  ? 225 THR   A CA    1 
ATOM   1766  C  C     . THR   A 1  225 ? -13.584 85.440  -52.985  1.00 38.75  ? 225 THR   A C     1 
ATOM   1767  O  O     . THR   A 1  225 ? -14.140 86.153  -53.825  1.00 36.44  ? 225 THR   A O     1 
ATOM   1768  C  CB    . THR   A 1  225 ? -13.493 86.022  -50.511  1.00 38.65  ? 225 THR   A CB    1 
ATOM   1769  O  OG1   . THR   A 1  225 ? -12.335 85.294  -50.097  1.00 64.11  ? 225 THR   A OG1   1 
ATOM   1770  C  CG2   . THR   A 1  225 ? -14.391 86.218  -49.285  1.00 25.47  ? 225 THR   A CG2   1 
ATOM   1771  N  N     . ASN   A 1  226 ? -12.425 84.831  -53.257  1.00 38.24  ? 226 ASN   A N     1 
ATOM   1772  C  CA    . ASN   A 1  226 ? -11.913 84.865  -54.627  1.00 33.02  ? 226 ASN   A CA    1 
ATOM   1773  C  C     . ASN   A 1  226 ? -12.975 84.367  -55.601  1.00 34.39  ? 226 ASN   A C     1 
ATOM   1774  O  O     . ASN   A 1  226 ? -13.351 85.063  -56.546  1.00 37.15  ? 226 ASN   A O     1 
ATOM   1775  C  CB    . ASN   A 1  226 ? -10.652 84.009  -54.776  1.00 32.17  ? 226 ASN   A CB    1 
ATOM   1776  C  CG    . ASN   A 1  226 ? -9.652  84.242  -53.683  1.00 38.27  ? 226 ASN   A CG    1 
ATOM   1777  O  OD1   . ASN   A 1  226 ? -9.218  83.294  -53.009  1.00 34.57  ? 226 ASN   A OD1   1 
ATOM   1778  N  ND2   . ASN   A 1  226 ? -9.275  85.508  -53.487  1.00 36.57  ? 226 ASN   A ND2   1 
ATOM   1779  N  N     . LEU   A 1  227 ? -13.468 83.148  -55.370  1.00 31.69  ? 227 LEU   A N     1 
ATOM   1780  C  CA    . LEU   A 1  227 ? -14.454 82.554  -56.261  1.00 30.16  ? 227 LEU   A CA    1 
ATOM   1781  C  C     . LEU   A 1  227 ? -15.587 83.520  -56.554  1.00 35.75  ? 227 LEU   A C     1 
ATOM   1782  O  O     . LEU   A 1  227 ? -16.000 83.662  -57.713  1.00 33.38  ? 227 LEU   A O     1 
ATOM   1783  C  CB    . LEU   A 1  227 ? -15.006 81.261  -55.654  1.00 27.91  ? 227 LEU   A CB    1 
ATOM   1784  C  CG    . LEU   A 1  227 ? -14.021 80.098  -55.460  1.00 31.38  ? 227 LEU   A CG    1 
ATOM   1785  C  CD1   . LEU   A 1  227 ? -14.653 78.749  -55.825  1.00 28.85  ? 227 LEU   A CD1   1 
ATOM   1786  C  CD2   . LEU   A 1  227 ? -12.767 80.340  -56.271  1.00 30.18  ? 227 LEU   A CD2   1 
ATOM   1787  N  N     . ASN   A 1  228 ? -16.094 84.210  -55.516  1.00 32.59  ? 228 ASN   A N     1 
ATOM   1788  C  CA    . ASN   A 1  228 ? -17.351 84.949  -55.645  1.00 28.15  ? 228 ASN   A CA    1 
ATOM   1789  C  C     . ASN   A 1  228 ? -17.161 86.296  -56.305  1.00 28.89  ? 228 ASN   A C     1 
ATOM   1790  O  O     . ASN   A 1  228 ? -18.080 86.791  -56.967  1.00 35.65  ? 228 ASN   A O     1 
ATOM   1791  C  CB    . ASN   A 1  228 ? -18.018 85.155  -54.285  1.00 30.38  ? 228 ASN   A CB    1 
ATOM   1792  C  CG    . ASN   A 1  228 ? -18.528 83.862  -53.680  1.00 30.34  ? 228 ASN   A CG    1 
ATOM   1793  O  OD1   . ASN   A 1  228 ? -18.571 82.820  -54.339  1.00 25.19  ? 228 ASN   A OD1   1 
ATOM   1794  N  ND2   . ASN   A 1  228 ? -18.920 83.928  -52.409  1.00 34.94  ? 228 ASN   A ND2   1 
ATOM   1795  N  N     . ARG   A 1  229 ? -15.992 86.898  -56.133  1.00 27.42  ? 229 ARG   A N     1 
ATOM   1796  C  CA    . ARG   A 1  229 ? -15.694 88.139  -56.830  1.00 31.89  ? 229 ARG   A CA    1 
ATOM   1797  C  C     . ARG   A 1  229 ? -15.646 87.923  -58.335  1.00 38.25  ? 229 ARG   A C     1 
ATOM   1798  O  O     . ARG   A 1  229 ? -16.174 88.738  -59.098  1.00 37.88  ? 229 ARG   A O     1 
ATOM   1799  C  CB    . ARG   A 1  229 ? -14.378 88.716  -56.325  1.00 31.16  ? 229 ARG   A CB    1 
ATOM   1800  C  CG    . ARG   A 1  229 ? -14.466 89.194  -54.892  1.00 42.20  ? 229 ARG   A CG    1 
ATOM   1801  C  CD    . ARG   A 1  229 ? -13.490 90.314  -54.657  1.00 53.72  ? 229 ARG   A CD    1 
ATOM   1802  N  NE    . ARG   A 1  229 ? -13.976 91.201  -53.620  1.00 43.52  ? 229 ARG   A NE    1 
ATOM   1803  C  CZ    . ARG   A 1  229 ? -13.529 91.188  -52.377  1.00 52.41  ? 229 ARG   A CZ    1 
ATOM   1804  N  NH1   . ARG   A 1  229 ? -12.503 90.425  -52.024  1.00 44.16  ? 229 ARG   A NH1   1 
ATOM   1805  N  NH2   . ARG   A 1  229 ? -14.137 91.948  -51.466  1.00 47.68  ? 229 ARG   A NH2   1 
ATOM   1806  N  N     . LEU   A 1  230 ? -15.023 86.829  -58.782  1.00 28.81  ? 230 LEU   A N     1 
ATOM   1807  C  CA    . LEU   A 1  230 ? -15.000 86.548  -60.208  1.00 32.19  ? 230 LEU   A CA    1 
ATOM   1808  C  C     . LEU   A 1  230 ? -16.403 86.245  -60.720  1.00 33.08  ? 230 LEU   A C     1 
ATOM   1809  O  O     . LEU   A 1  230 ? -16.813 86.763  -61.765  1.00 35.33  ? 230 LEU   A O     1 
ATOM   1810  C  CB    . LEU   A 1  230 ? -14.036 85.397  -60.508  1.00 31.93  ? 230 LEU   A CB    1 
ATOM   1811  C  CG    . LEU   A 1  230 ? -13.780 85.080  -61.973  1.00 27.24  ? 230 LEU   A CG    1 
ATOM   1812  C  CD1   . LEU   A 1  230 ? -13.181 86.296  -62.680  1.00 26.43  ? 230 LEU   A CD1   1 
ATOM   1813  C  CD2   . LEU   A 1  230 ? -12.872 83.895  -62.100  1.00 28.29  ? 230 LEU   A CD2   1 
ATOM   1814  N  N     . ILE   A 1  231 ? -17.165 85.428  -59.988  1.00 31.86  ? 231 ILE   A N     1 
ATOM   1815  C  CA    . ILE   A 1  231 ? -18.521 85.118  -60.429  1.00 31.03  ? 231 ILE   A CA    1 
ATOM   1816  C  C     . ILE   A 1  231 ? -19.373 86.373  -60.490  1.00 31.89  ? 231 ILE   A C     1 
ATOM   1817  O  O     . ILE   A 1  231 ? -20.277 86.473  -61.327  1.00 34.69  ? 231 ILE   A O     1 
ATOM   1818  C  CB    . ILE   A 1  231 ? -19.172 84.071  -59.512  1.00 37.97  ? 231 ILE   A CB    1 
ATOM   1819  C  CG1   . ILE   A 1  231 ? -18.470 82.730  -59.665  1.00 34.71  ? 231 ILE   A CG1   1 
ATOM   1820  C  CG2   . ILE   A 1  231 ? -20.665 83.957  -59.816  1.00 22.68  ? 231 ILE   A CG2   1 
ATOM   1821  C  CD1   . ILE   A 1  231 ? -18.749 81.827  -58.520  1.00 28.62  ? 231 ILE   A CD1   1 
ATOM   1822  N  N     . SER   A 1  232 ? -19.125 87.336  -59.596  1.00 36.98  ? 232 SER   A N     1 
ATOM   1823  C  CA    . SER   A 1  232 ? -19.889 88.583  -59.600  1.00 31.17  ? 232 SER   A CA    1 
ATOM   1824  C  C     . SER   A 1  232 ? -19.538 89.442  -60.799  1.00 35.07  ? 232 SER   A C     1 
ATOM   1825  O  O     . SER   A 1  232 ? -20.407 90.103  -61.374  1.00 41.28  ? 232 SER   A O     1 
ATOM   1826  C  CB    . SER   A 1  232 ? -19.636 89.349  -58.307  1.00 43.96  ? 232 SER   A CB    1 
ATOM   1827  O  OG    . SER   A 1  232 ? -20.564 88.953  -57.309  1.00 50.10  ? 232 SER   A OG    1 
ATOM   1828  N  N     . GLN   A 1  233 ? -18.260 89.461  -61.171  1.00 38.43  ? 233 GLN   A N     1 
ATOM   1829  C  CA    . GLN   A 1  233 ? -17.844 89.960  -62.475  1.00 39.74  ? 233 GLN   A CA    1 
ATOM   1830  C  C     . GLN   A 1  233 ? -18.676 89.352  -63.604  1.00 38.43  ? 233 GLN   A C     1 
ATOM   1831  O  O     . GLN   A 1  233 ? -19.298 90.068  -64.394  1.00 38.05  ? 233 GLN   A O     1 
ATOM   1832  C  CB    . GLN   A 1  233 ? -16.363 89.646  -62.683  1.00 37.66  ? 233 GLN   A CB    1 
ATOM   1833  C  CG    . GLN   A 1  233 ? -15.448 90.522  -61.915  1.00 42.02  ? 233 GLN   A CG    1 
ATOM   1834  C  CD    . GLN   A 1  233 ? -15.468 91.907  -62.461  1.00 51.68  ? 233 GLN   A CD    1 
ATOM   1835  O  OE1   . GLN   A 1  233 ? -14.817 92.196  -63.477  1.00 60.21  ? 233 GLN   A OE1   1 
ATOM   1836  N  NE2   . GLN   A 1  233 ? -16.236 92.779  -61.821  1.00 46.40  ? 233 GLN   A NE2   1 
ATOM   1837  N  N     . ILE   A 1  234 ? -18.655 88.024  -63.730  1.00 27.91  ? 234 ILE   A N     1 
ATOM   1838  C  CA    . ILE   A 1  234 ? -19.344 87.405  -64.854  1.00 34.23  ? 234 ILE   A CA    1 
ATOM   1839  C  C     . ILE   A 1  234 ? -20.842 87.674  -64.769  1.00 37.96  ? 234 ILE   A C     1 
ATOM   1840  O  O     . ILE   A 1  234 ? -21.488 87.997  -65.774  1.00 30.50  ? 234 ILE   A O     1 
ATOM   1841  C  CB    . ILE   A 1  234 ? -19.021 85.900  -64.908  1.00 33.91  ? 234 ILE   A CB    1 
ATOM   1842  C  CG1   . ILE   A 1  234 ? -17.536 85.701  -65.199  1.00 33.40  ? 234 ILE   A CG1   1 
ATOM   1843  C  CG2   . ILE   A 1  234 ? -19.887 85.206  -65.916  1.00 28.81  ? 234 ILE   A CG2   1 
ATOM   1844  C  CD1   . ILE   A 1  234 ? -16.821 84.844  -64.171  1.00 31.43  ? 234 ILE   A CD1   1 
ATOM   1845  N  N     . VAL   A 1  235 ? -21.413 87.579  -63.562  1.00 35.48  ? 235 VAL   A N     1 
ATOM   1846  C  CA    . VAL   A 1  235 ? -22.848 87.815  -63.396  1.00 33.66  ? 235 VAL   A CA    1 
ATOM   1847  C  C     . VAL   A 1  235 ? -23.193 89.245  -63.784  1.00 30.43  ? 235 VAL   A C     1 
ATOM   1848  O  O     . VAL   A 1  235 ? -24.167 89.497  -64.502  1.00 34.28  ? 235 VAL   A O     1 
ATOM   1849  C  CB    . VAL   A 1  235 ? -23.290 87.493  -61.956  1.00 32.05  ? 235 VAL   A CB    1 
ATOM   1850  C  CG1   . VAL   A 1  235 ? -24.649 88.141  -61.656  1.00 31.22  ? 235 VAL   A CG1   1 
ATOM   1851  C  CG2   . VAL   A 1  235 ? -23.336 85.971  -61.732  1.00 27.83  ? 235 VAL   A CG2   1 
ATOM   1852  N  N     . SER   A 1  236 ? -22.398 90.202  -63.311  1.00 33.79  ? 236 SER   A N     1 
ATOM   1853  C  CA    . SER   A 1  236 ? -22.577 91.594  -63.718  1.00 35.69  ? 236 SER   A CA    1 
ATOM   1854  C  C     . SER   A 1  236 ? -22.612 91.742  -65.235  1.00 40.82  ? 236 SER   A C     1 
ATOM   1855  O  O     . SER   A 1  236 ? -23.453 92.478  -65.767  1.00 44.35  ? 236 SER   A O     1 
ATOM   1856  C  CB    . SER   A 1  236 ? -21.467 92.464  -63.140  1.00 37.85  ? 236 SER   A CB    1 
ATOM   1857  O  OG    . SER   A 1  236 ? -21.585 93.773  -63.655  1.00 44.91  ? 236 SER   A OG    1 
ATOM   1858  N  N     . SER   A 1  237 ? -21.710 91.055  -65.958  1.00 34.65  ? 237 SER   A N     1 
ATOM   1859  C  CA    . SER   A 1  237 ? -21.694 91.192  -67.418  1.00 39.79  ? 237 SER   A CA    1 
ATOM   1860  C  C     . SER   A 1  237 ? -23.019 90.756  -68.029  1.00 38.24  ? 237 SER   A C     1 
ATOM   1861  O  O     . SER   A 1  237 ? -23.537 91.415  -68.940  1.00 45.78  ? 237 SER   A O     1 
ATOM   1862  C  CB    . SER   A 1  237 ? -20.557 90.380  -68.034  1.00 35.50  ? 237 SER   A CB    1 
ATOM   1863  O  OG    . SER   A 1  237 ? -19.332 90.717  -67.448  1.00 41.90  ? 237 SER   A OG    1 
ATOM   1864  N  N     . ILE   A 1  238 ? -23.573 89.640  -67.542  1.00 42.12  ? 238 ILE   A N     1 
ATOM   1865  C  CA    . ILE   A 1  238 ? -24.805 89.080  -68.082  1.00 39.47  ? 238 ILE   A CA    1 
ATOM   1866  C  C     . ILE   A 1  238 ? -26.009 89.949  -67.761  1.00 37.35  ? 238 ILE   A C     1 
ATOM   1867  O  O     . ILE   A 1  238 ? -27.025 89.872  -68.462  1.00 40.65  ? 238 ILE   A O     1 
ATOM   1868  C  CB    . ILE   A 1  238 ? -24.992 87.650  -67.544  1.00 35.98  ? 238 ILE   A CB    1 
ATOM   1869  C  CG1   . ILE   A 1  238 ? -23.682 86.887  -67.737  1.00 35.69  ? 238 ILE   A CG1   1 
ATOM   1870  C  CG2   . ILE   A 1  238 ? -26.177 86.938  -68.240  1.00 34.17  ? 238 ILE   A CG2   1 
ATOM   1871  C  CD1   . ILE   A 1  238 ? -23.686 85.474  -67.210  1.00 33.40  ? 238 ILE   A CD1   1 
ATOM   1872  N  N     . THR   A 1  239 ? -25.922 90.787  -66.730  1.00 29.15  ? 239 THR   A N     1 
ATOM   1873  C  CA    . THR   A 1  239 ? -27.050 91.603  -66.325  1.00 33.61  ? 239 THR   A CA    1 
ATOM   1874  C  C     . THR   A 1  239 ? -26.893 93.066  -66.710  1.00 44.33  ? 239 THR   A C     1 
ATOM   1875  O  O     . THR   A 1  239 ? -27.903 93.780  -66.769  1.00 44.81  ? 239 THR   A O     1 
ATOM   1876  C  CB    . THR   A 1  239 ? -27.289 91.502  -64.799  1.00 41.68  ? 239 THR   A CB    1 
ATOM   1877  O  OG1   . THR   A 1  239 ? -26.293 92.234  -64.077  1.00 39.54  ? 239 THR   A OG1   1 
ATOM   1878  C  CG2   . THR   A 1  239 ? -27.247 90.054  -64.312  1.00 42.84  ? 239 THR   A CG2   1 
ATOM   1879  N  N     . ALA   A 1  240 ? -25.662 93.523  -66.975  1.00 41.04  ? 240 ALA   A N     1 
ATOM   1880  C  CA    . ALA   A 1  240 ? -25.393 94.897  -67.381  1.00 36.01  ? 240 ALA   A CA    1 
ATOM   1881  C  C     . ALA   A 1  240 ? -26.524 95.419  -68.252  1.00 36.35  ? 240 ALA   A C     1 
ATOM   1882  O  O     . ALA   A 1  240 ? -26.972 96.561  -68.094  1.00 38.64  ? 240 ALA   A O     1 
ATOM   1883  C  CB    . ALA   A 1  240 ? -24.060 94.980  -68.132  1.00 36.36  ? 240 ALA   A CB    1 
ATOM   1884  N  N     . SER   A 1  241 ? -27.019 94.563  -69.143  1.00 30.12  ? 241 SER   A N     1 
ATOM   1885  C  CA    . SER   A 1  241 ? -28.015 94.966  -70.119  1.00 29.00  ? 241 SER   A CA    1 
ATOM   1886  C  C     . SER   A 1  241 ? -29.381 95.243  -69.511  1.00 39.80  ? 241 SER   A C     1 
ATOM   1887  O  O     . SER   A 1  241 ? -30.286 95.661  -70.235  1.00 43.40  ? 241 SER   A O     1 
ATOM   1888  C  CB    . SER   A 1  241 ? -28.156 93.889  -71.189  1.00 36.20  ? 241 SER   A CB    1 
ATOM   1889  O  OG    . SER   A 1  241 ? -28.616 92.669  -70.639  1.00 38.75  ? 241 SER   A OG    1 
ATOM   1890  N  N     . LEU   A 1  242 ? -29.588 94.987  -68.230  1.00 41.27  ? 242 LEU   A N     1 
ATOM   1891  C  CA    . LEU   A 1  242 ? -30.880 95.294  -67.643  1.00 38.80  ? 242 LEU   A CA    1 
ATOM   1892  C  C     . LEU   A 1  242 ? -30.823 96.491  -66.719  1.00 37.60  ? 242 LEU   A C     1 
ATOM   1893  O  O     . LEU   A 1  242 ? -31.880 96.968  -66.296  1.00 32.13  ? 242 LEU   A O     1 
ATOM   1894  C  CB    . LEU   A 1  242 ? -31.426 94.093  -66.871  1.00 34.66  ? 242 LEU   A CB    1 
ATOM   1895  C  CG    . LEU   A 1  242 ? -31.309 92.692  -67.431  1.00 35.43  ? 242 LEU   A CG    1 
ATOM   1896  C  CD1   . LEU   A 1  242 ? -31.026 91.759  -66.250  1.00 39.27  ? 242 LEU   A CD1   1 
ATOM   1897  C  CD2   . LEU   A 1  242 ? -32.608 92.317  -68.105  1.00 41.54  ? 242 LEU   A CD2   1 
ATOM   1898  N  N     . ARG   A 1  243 ? -29.616 96.968  -66.394  1.00 37.13  ? 243 ARG   A N     1 
ATOM   1899  C  CA    . ARG   A 1  243 ? -29.383 98.057  -65.457  1.00 42.68  ? 243 ARG   A CA    1 
ATOM   1900  C  C     . ARG   A 1  243 ? -28.805 99.286  -66.142  1.00 43.54  ? 243 ARG   A C     1 
ATOM   1901  O  O     . ARG   A 1  243 ? -28.530 100.287 -65.471  1.00 43.78  ? 243 ARG   A O     1 
ATOM   1902  C  CB    . ARG   A 1  243 ? -28.423 97.606  -64.335  1.00 35.00  ? 243 ARG   A CB    1 
ATOM   1903  C  CG    . ARG   A 1  243 ? -28.616 96.185  -63.877  1.00 36.10  ? 243 ARG   A CG    1 
ATOM   1904  C  CD    . ARG   A 1  243 ? -27.662 95.818  -62.724  1.00 43.82  ? 243 ARG   A CD    1 
ATOM   1905  N  NE    . ARG   A 1  243 ? -26.452 95.144  -63.182  1.00 33.64  ? 243 ARG   A NE    1 
ATOM   1906  C  CZ    . ARG   A 1  243 ? -25.242 95.686  -63.163  1.00 37.54  ? 243 ARG   A CZ    1 
ATOM   1907  N  NH1   . ARG   A 1  243 ? -25.034 96.894  -62.662  1.00 36.26  ? 243 ARG   A NH1   1 
ATOM   1908  N  NH2   . ARG   A 1  243 ? -24.215 95.001  -63.664  1.00 35.37  ? 243 ARG   A NH2   1 
ATOM   1909  N  N     . PHE   A 1  244 ? -28.578 99.230  -67.449  1.00 41.97  ? 244 PHE   A N     1 
ATOM   1910  C  CA    . PHE   A 1  244 ? -27.988 100.353 -68.155  1.00 46.72  ? 244 PHE   A CA    1 
ATOM   1911  C  C     . PHE   A 1  244 ? -28.707 100.557 -69.478  1.00 46.09  ? 244 PHE   A C     1 
ATOM   1912  O  O     . PHE   A 1  244 ? -29.452 99.699  -69.957  1.00 54.71  ? 244 PHE   A O     1 
ATOM   1913  C  CB    . PHE   A 1  244 ? -26.490 100.148 -68.415  1.00 52.08  ? 244 PHE   A CB    1 
ATOM   1914  C  CG    . PHE   A 1  244 ? -25.636 100.035 -67.161  1.00 44.57  ? 244 PHE   A CG    1 
ATOM   1915  C  CD1   . PHE   A 1  244 ? -25.306 101.155 -66.429  1.00 41.56  ? 244 PHE   A CD1   1 
ATOM   1916  C  CD2   . PHE   A 1  244 ? -25.115 98.810  -66.767  1.00 38.18  ? 244 PHE   A CD2   1 
ATOM   1917  C  CE1   . PHE   A 1  244 ? -24.505 101.058 -65.301  1.00 47.01  ? 244 PHE   A CE1   1 
ATOM   1918  C  CE2   . PHE   A 1  244 ? -24.310 98.712  -65.650  1.00 42.69  ? 244 PHE   A CE2   1 
ATOM   1919  C  CZ    . PHE   A 1  244 ? -24.009 99.839  -64.910  1.00 41.16  ? 244 PHE   A CZ    1 
ATOM   1920  N  N     . ASP   A 1  245 ? -28.463 101.716 -70.069  1.00 53.68  ? 245 ASP   A N     1 
ATOM   1921  C  CA    . ASP   A 1  245 ? -28.953 102.014 -71.407  1.00 54.68  ? 245 ASP   A CA    1 
ATOM   1922  C  C     . ASP   A 1  245 ? -28.413 101.010 -72.423  1.00 57.43  ? 245 ASP   A C     1 
ATOM   1923  O  O     . ASP   A 1  245 ? -27.206 100.742 -72.472  1.00 54.53  ? 245 ASP   A O     1 
ATOM   1924  C  CB    . ASP   A 1  245 ? -28.513 103.425 -71.788  1.00 53.17  ? 245 ASP   A CB    1 
ATOM   1925  C  CG    . ASP   A 1  245 ? -29.508 104.135 -72.657  1.00 50.30  ? 245 ASP   A CG    1 
ATOM   1926  O  OD1   . ASP   A 1  245 ? -30.554 103.535 -72.991  1.00 46.22  ? 245 ASP   A OD1   1 
ATOM   1927  O  OD2   . ASP   A 1  245 ? -29.227 105.307 -72.995  1.00 56.39  ? 245 ASP   A OD2   1 
ATOM   1928  N  N     . GLY   A 1  246 ? -29.301 100.478 -73.254  1.00 48.80  ? 246 GLY   A N     1 
ATOM   1929  C  CA    . GLY   A 1  246 ? -28.879 99.603  -74.332  1.00 36.11  ? 246 GLY   A CA    1 
ATOM   1930  C  C     . GLY   A 1  246 ? -30.080 99.115  -75.112  1.00 49.91  ? 246 GLY   A C     1 
ATOM   1931  O  O     . GLY   A 1  246 ? -31.237 99.312  -74.721  1.00 50.20  ? 246 GLY   A O     1 
ATOM   1932  N  N     . ALA   A 1  247 ? -29.785 98.473  -76.238  1.00 55.72  ? 247 ALA   A N     1 
ATOM   1933  C  CA    . ALA   A 1  247 ? -30.814 97.911  -77.104  1.00 53.30  ? 247 ALA   A CA    1 
ATOM   1934  C  C     . ALA   A 1  247 ? -30.663 96.401  -77.274  1.00 58.25  ? 247 ALA   A C     1 
ATOM   1935  O  O     . ALA   A 1  247 ? -31.292 95.821  -78.171  1.00 63.40  ? 247 ALA   A O     1 
ATOM   1936  C  CB    . ALA   A 1  247 ? -30.797 98.608  -78.470  1.00 44.82  ? 247 ALA   A CB    1 
ATOM   1937  N  N     . LEU   A 1  248 ? -29.861 95.749  -76.429  1.00 47.78  ? 248 LEU   A N     1 
ATOM   1938  C  CA    . LEU   A 1  248 ? -29.609 94.318  -76.512  1.00 48.86  ? 248 LEU   A CA    1 
ATOM   1939  C  C     . LEU   A 1  248 ? -29.860 93.669  -75.158  1.00 45.37  ? 248 LEU   A C     1 
ATOM   1940  O  O     . LEU   A 1  248 ? -29.340 94.137  -74.135  1.00 42.06  ? 248 LEU   A O     1 
ATOM   1941  C  CB    . LEU   A 1  248 ? -28.170 94.043  -76.966  1.00 45.07  ? 248 LEU   A CB    1 
ATOM   1942  C  CG    . LEU   A 1  248 ? -27.705 92.588  -76.905  1.00 34.82  ? 248 LEU   A CG    1 
ATOM   1943  C  CD1   . LEU   A 1  248 ? -28.701 91.719  -77.631  1.00 31.29  ? 248 LEU   A CD1   1 
ATOM   1944  C  CD2   . LEU   A 1  248 ? -26.333 92.451  -77.515  1.00 39.13  ? 248 LEU   A CD2   1 
ATOM   1945  N  N     . ASN   A 1  249 ? -30.624 92.572  -75.162  1.00 37.90  ? 249 ASN   A N     1 
ATOM   1946  C  CA    . ASN   A 1  249 ? -30.927 91.814  -73.939  1.00 50.98  ? 249 ASN   A CA    1 
ATOM   1947  C  C     . ASN   A 1  249 ? -31.515 92.726  -72.855  1.00 50.82  ? 249 ASN   A C     1 
ATOM   1948  O  O     . ASN   A 1  249 ? -31.069 92.723  -71.700  1.00 40.37  ? 249 ASN   A O     1 
ATOM   1949  C  CB    . ASN   A 1  249 ? -29.681 91.073  -73.417  1.00 34.29  ? 249 ASN   A CB    1 
ATOM   1950  C  CG    . ASN   A 1  249 ? -29.355 89.812  -74.224  1.00 37.92  ? 249 ASN   A CG    1 
ATOM   1951  O  OD1   . ASN   A 1  249 ? -30.228 89.215  -74.859  1.00 43.12  ? 249 ASN   A OD1   1 
ATOM   1952  N  ND2   . ASN   A 1  249 ? -28.091 89.403  -74.199  1.00 37.38  ? 249 ASN   A ND2   1 
ATOM   1953  N  N     . VAL   A 1  250 ? -32.545 93.501  -73.243  1.00 48.51  ? 250 VAL   A N     1 
ATOM   1954  C  CA    . VAL   A 1  250 ? -33.087 94.575  -72.401  1.00 43.17  ? 250 VAL   A CA    1 
ATOM   1955  C  C     . VAL   A 1  250 ? -34.153 94.111  -71.412  1.00 44.30  ? 250 VAL   A C     1 
ATOM   1956  O  O     . VAL   A 1  250 ? -34.505 94.878  -70.507  1.00 47.84  ? 250 VAL   A O     1 
ATOM   1957  C  CB    . VAL   A 1  250 ? -33.706 95.723  -73.232  1.00 46.05  ? 250 VAL   A CB    1 
ATOM   1958  C  CG1   . VAL   A 1  250 ? -32.646 96.553  -73.928  1.00 46.66  ? 250 VAL   A CG1   1 
ATOM   1959  C  CG2   . VAL   A 1  250 ? -34.713 95.186  -74.241  1.00 46.06  ? 250 VAL   A CG2   1 
ATOM   1960  N  N     . ASP   A 1  251 ? -34.717 92.914  -71.589  1.00 42.16  ? 251 ASP   A N     1 
ATOM   1961  C  CA    . ASP   A 1  251 ? -35.549 92.291  -70.566  1.00 46.13  ? 251 ASP   A CA    1 
ATOM   1962  C  C     . ASP   A 1  251 ? -35.340 90.780  -70.628  1.00 48.90  ? 251 ASP   A C     1 
ATOM   1963  O  O     . ASP   A 1  251 ? -34.782 90.249  -71.597  1.00 44.56  ? 251 ASP   A O     1 
ATOM   1964  C  CB    . ASP   A 1  251 ? -37.038 92.689  -70.705  1.00 51.88  ? 251 ASP   A CB    1 
ATOM   1965  C  CG    . ASP   A 1  251 ? -37.772 91.956  -71.840  1.00 60.11  ? 251 ASP   A CG    1 
ATOM   1966  O  OD1   . ASP   A 1  251 ? -37.165 91.147  -72.576  1.00 54.98  ? 251 ASP   A OD1   1 
ATOM   1967  O  OD2   . ASP   A 1  251 ? -38.988 92.203  -71.996  1.00 71.53  ? 251 ASP   A OD2   1 
ATOM   1968  N  N     . LEU   A 1  252 ? -35.820 90.088  -69.581  1.00 47.35  ? 252 LEU   A N     1 
ATOM   1969  C  CA    . LEU   A 1  252 ? -35.498 88.671  -69.378  1.00 50.88  ? 252 LEU   A CA    1 
ATOM   1970  C  C     . LEU   A 1  252 ? -35.993 87.790  -70.524  1.00 48.62  ? 252 LEU   A C     1 
ATOM   1971  O  O     . LEU   A 1  252 ? -35.344 86.793  -70.866  1.00 50.69  ? 252 LEU   A O     1 
ATOM   1972  C  CB    . LEU   A 1  252 ? -36.092 88.166  -68.059  1.00 55.12  ? 252 LEU   A CB    1 
ATOM   1973  C  CG    . LEU   A 1  252 ? -35.837 88.895  -66.745  1.00 41.70  ? 252 LEU   A CG    1 
ATOM   1974  C  CD1   . LEU   A 1  252 ? -36.605 88.192  -65.657  1.00 46.14  ? 252 LEU   A CD1   1 
ATOM   1975  C  CD2   . LEU   A 1  252 ? -34.361 88.934  -66.434  1.00 43.10  ? 252 LEU   A CD2   1 
ATOM   1976  N  N     . THR   A 1  253 ? -37.151 88.114  -71.110  1.00 43.53  ? 253 THR   A N     1 
ATOM   1977  C  CA    . THR   A 1  253 ? -37.628 87.325  -72.244  1.00 43.18  ? 253 THR   A CA    1 
ATOM   1978  C  C     . THR   A 1  253 ? -36.595 87.283  -73.357  1.00 41.32  ? 253 THR   A C     1 
ATOM   1979  O  O     . THR   A 1  253 ? -36.457 86.266  -74.048  1.00 48.61  ? 253 THR   A O     1 
ATOM   1980  C  CB    . THR   A 1  253 ? -38.952 87.881  -72.784  1.00 43.76  ? 253 THR   A CB    1 
ATOM   1981  O  OG1   . THR   A 1  253 ? -39.715 88.450  -71.717  1.00 55.49  ? 253 THR   A OG1   1 
ATOM   1982  C  CG2   . THR   A 1  253 ? -39.768 86.770  -73.420  1.00 45.64  ? 253 THR   A CG2   1 
ATOM   1983  N  N     . GLU   A 1  254 ? -35.854 88.369  -73.541  1.00 46.07  ? 254 GLU   A N     1 
ATOM   1984  C  CA    . GLU   A 1  254 ? -34.879 88.421  -74.623  1.00 44.74  ? 254 GLU   A CA    1 
ATOM   1985  C  C     . GLU   A 1  254 ? -33.748 87.425  -74.412  1.00 48.99  ? 254 GLU   A C     1 
ATOM   1986  O  O     . GLU   A 1  254 ? -33.219 86.883  -75.390  1.00 49.99  ? 254 GLU   A O     1 
ATOM   1987  C  CB    . GLU   A 1  254 ? -34.324 89.831  -74.734  1.00 49.55  ? 254 GLU   A CB    1 
ATOM   1988  C  CG    . GLU   A 1  254 ? -34.105 90.317  -76.131  1.00 42.39  ? 254 GLU   A CG    1 
ATOM   1989  C  CD    . GLU   A 1  254 ? -33.497 91.701  -76.137  1.00 50.35  ? 254 GLU   A CD    1 
ATOM   1990  O  OE1   . GLU   A 1  254 ? -34.063 92.601  -75.476  1.00 57.05  ? 254 GLU   A OE1   1 
ATOM   1991  O  OE2   . GLU   A 1  254 ? -32.433 91.882  -76.775  1.00 58.23  ? 254 GLU   A OE2   1 
ATOM   1992  N  N     . PHE   A 1  255 ? -33.352 87.184  -73.153  1.00 51.81  ? 255 PHE   A N     1 
ATOM   1993  C  CA    . PHE   A 1  255 ? -32.340 86.165  -72.860  1.00 49.52  ? 255 PHE   A CA    1 
ATOM   1994  C  C     . PHE   A 1  255 ? -32.754 84.811  -73.425  1.00 49.67  ? 255 PHE   A C     1 
ATOM   1995  O  O     . PHE   A 1  255 ? -31.959 84.110  -74.073  1.00 42.03  ? 255 PHE   A O     1 
ATOM   1996  C  CB    . PHE   A 1  255 ? -32.114 86.057  -71.345  1.00 44.86  ? 255 PHE   A CB    1 
ATOM   1997  C  CG    . PHE   A 1  255 ? -31.341 87.195  -70.761  1.00 39.29  ? 255 PHE   A CG    1 
ATOM   1998  C  CD1   . PHE   A 1  255 ? -31.986 88.322  -70.311  1.00 40.60  ? 255 PHE   A CD1   1 
ATOM   1999  C  CD2   . PHE   A 1  255 ? -29.967 87.134  -70.662  1.00 40.05  ? 255 PHE   A CD2   1 
ATOM   2000  C  CE1   . PHE   A 1  255 ? -31.273 89.383  -69.783  1.00 38.58  ? 255 PHE   A CE1   1 
ATOM   2001  C  CE2   . PHE   A 1  255 ? -29.248 88.191  -70.123  1.00 39.94  ? 255 PHE   A CE2   1 
ATOM   2002  C  CZ    . PHE   A 1  255 ? -29.902 89.312  -69.684  1.00 32.71  ? 255 PHE   A CZ    1 
ATOM   2003  N  N     . GLN   A 1  256 ? -33.999 84.421  -73.166  1.00 43.08  ? 256 GLN   A N     1 
ATOM   2004  C  CA    . GLN   A 1  256 ? -34.514 83.173  -73.700  1.00 42.65  ? 256 GLN   A CA    1 
ATOM   2005  C  C     . GLN   A 1  256 ? -34.608 83.244  -75.214  1.00 43.79  ? 256 GLN   A C     1 
ATOM   2006  O  O     . GLN   A 1  256 ? -34.150 82.332  -75.911  1.00 47.92  ? 256 GLN   A O     1 
ATOM   2007  C  CB    . GLN   A 1  256 ? -35.862 82.898  -73.042  1.00 51.88  ? 256 GLN   A CB    1 
ATOM   2008  C  CG    . GLN   A 1  256 ? -36.769 81.865  -73.640  1.00 48.00  ? 256 GLN   A CG    1 
ATOM   2009  C  CD    . GLN   A 1  256 ? -38.113 81.882  -72.917  1.00 62.78  ? 256 GLN   A CD    1 
ATOM   2010  O  OE1   . GLN   A 1  256 ? -38.481 82.885  -72.284  1.00 56.78  ? 256 GLN   A OE1   1 
ATOM   2011  N  NE2   . GLN   A 1  256 ? -38.837 80.769  -72.979  1.00 69.28  ? 256 GLN   A NE2   1 
ATOM   2012  N  N     . THR   A 1  257 ? -35.127 84.354  -75.747  1.00 46.09  ? 257 THR   A N     1 
ATOM   2013  C  CA    . THR   A 1  257 ? -35.273 84.470  -77.198  1.00 47.44  ? 257 THR   A CA    1 
ATOM   2014  C  C     . THR   A 1  257 ? -33.920 84.442  -77.905  1.00 44.20  ? 257 THR   A C     1 
ATOM   2015  O  O     . THR   A 1  257 ? -33.765 83.758  -78.919  1.00 49.70  ? 257 THR   A O     1 
ATOM   2016  C  CB    . THR   A 1  257 ? -36.058 85.738  -77.563  1.00 38.34  ? 257 THR   A CB    1 
ATOM   2017  O  OG1   . THR   A 1  257 ? -37.243 85.357  -78.266  1.00 44.32  ? 257 THR   A OG1   1 
ATOM   2018  C  CG2   . THR   A 1  257 ? -35.260 86.634  -78.464  1.00 33.01  ? 257 THR   A CG2   1 
ATOM   2019  N  N     . ASN   A 1  258 ? -32.929 85.176  -77.391  1.00 42.77  ? 258 ASN   A N     1 
ATOM   2020  C  CA    . ASN   A 1  258 ? -31.618 85.199  -78.035  1.00 41.31  ? 258 ASN   A CA    1 
ATOM   2021  C  C     . ASN   A 1  258 ? -30.803 83.953  -77.747  1.00 41.11  ? 258 ASN   A C     1 
ATOM   2022  O  O     . ASN   A 1  258 ? -30.001 83.548  -78.587  1.00 49.79  ? 258 ASN   A O     1 
ATOM   2023  C  CB    . ASN   A 1  258 ? -30.807 86.411  -77.584  1.00 45.70  ? 258 ASN   A CB    1 
ATOM   2024  C  CG    . ASN   A 1  258 ? -31.340 87.700  -78.139  1.00 45.66  ? 258 ASN   A CG    1 
ATOM   2025  O  OD1   . ASN   A 1  258 ? -31.996 87.706  -79.171  1.00 51.74  ? 258 ASN   A OD1   1 
ATOM   2026  N  ND2   . ASN   A 1  258 ? -31.053 88.803  -77.467  1.00 34.82  ? 258 ASN   A ND2   1 
ATOM   2027  N  N     . LEU   A 1  259 ? -30.974 83.346  -76.573  1.00 42.51  ? 259 LEU   A N     1 
ATOM   2028  C  CA    . LEU   A 1  259 ? -30.102 82.270  -76.128  1.00 41.16  ? 259 LEU   A CA    1 
ATOM   2029  C  C     . LEU   A 1  259 ? -30.736 80.890  -76.193  1.00 42.38  ? 259 LEU   A C     1 
ATOM   2030  O  O     . LEU   A 1  259 ? -29.999 79.906  -76.311  1.00 42.46  ? 259 LEU   A O     1 
ATOM   2031  C  CB    . LEU   A 1  259 ? -29.634 82.525  -74.681  1.00 41.95  ? 259 LEU   A CB    1 
ATOM   2032  C  CG    . LEU   A 1  259 ? -28.294 83.225  -74.380  1.00 39.90  ? 259 LEU   A CG    1 
ATOM   2033  C  CD1   . LEU   A 1  259 ? -27.518 83.580  -75.635  1.00 37.14  ? 259 LEU   A CD1   1 
ATOM   2034  C  CD2   . LEU   A 1  259 ? -28.447 84.456  -73.487  1.00 34.66  ? 259 LEU   A CD2   1 
ATOM   2035  N  N     . VAL   A 1  260 ? -32.063 80.787  -76.142  1.00 43.17  ? 260 VAL   A N     1 
ATOM   2036  C  CA    . VAL   A 1  260 ? -32.707 79.496  -75.890  1.00 49.80  ? 260 VAL   A CA    1 
ATOM   2037  C  C     . VAL   A 1  260 ? -33.812 79.172  -76.889  1.00 46.57  ? 260 VAL   A C     1 
ATOM   2038  O  O     . VAL   A 1  260 ? -34.998 79.283  -76.547  1.00 50.34  ? 260 VAL   A O     1 
ATOM   2039  C  CB    . VAL   A 1  260 ? -33.271 79.436  -74.462  1.00 40.43  ? 260 VAL   A CB    1 
ATOM   2040  C  CG1   . VAL   A 1  260 ? -33.876 78.058  -74.188  1.00 32.37  ? 260 VAL   A CG1   1 
ATOM   2041  C  CG2   . VAL   A 1  260 ? -32.167 79.748  -73.475  1.00 38.85  ? 260 VAL   A CG2   1 
ATOM   2042  N  N     . PRO   A 1  261 ? -33.482 78.721  -78.100  1.00 45.89  ? 261 PRO   A N     1 
ATOM   2043  C  CA    . PRO   A 1  261 ? -34.541 78.232  -78.999  1.00 46.62  ? 261 PRO   A CA    1 
ATOM   2044  C  C     . PRO   A 1  261 ? -35.269 77.001  -78.475  1.00 47.75  ? 261 PRO   A C     1 
ATOM   2045  O  O     . PRO   A 1  261 ? -36.478 76.861  -78.702  1.00 50.70  ? 261 PRO   A O     1 
ATOM   2046  C  CB    . PRO   A 1  261 ? -33.780 77.942  -80.307  1.00 49.65  ? 261 PRO   A CB    1 
ATOM   2047  C  CG    . PRO   A 1  261 ? -32.370 77.763  -79.918  1.00 44.29  ? 261 PRO   A CG    1 
ATOM   2048  C  CD    . PRO   A 1  261 ? -32.153 78.676  -78.727  1.00 48.02  ? 261 PRO   A CD    1 
ATOM   2049  N  N     . TYR   A 1  262 ? -34.563 76.095  -77.787  1.00 54.64  ? 262 TYR   A N     1 
ATOM   2050  C  CA    . TYR   A 1  262 ? -35.154 74.886  -77.211  1.00 46.74  ? 262 TYR   A CA    1 
ATOM   2051  C  C     . TYR   A 1  262 ? -35.344 75.059  -75.712  1.00 51.85  ? 262 TYR   A C     1 
ATOM   2052  O  O     . TYR   A 1  262 ? -34.371 75.352  -74.999  1.00 48.34  ? 262 TYR   A O     1 
ATOM   2053  C  CB    . TYR   A 1  262 ? -34.267 73.687  -77.486  1.00 56.17  ? 262 TYR   A CB    1 
ATOM   2054  C  CG    . TYR   A 1  262 ? -34.532 73.058  -78.820  1.00 68.89  ? 262 TYR   A CG    1 
ATOM   2055  C  CD1   . TYR   A 1  262 ? -34.580 73.834  -79.974  1.00 74.73  ? 262 TYR   A CD1   1 
ATOM   2056  C  CD2   . TYR   A 1  262 ? -34.748 71.685  -78.931  1.00 82.72  ? 262 TYR   A CD2   1 
ATOM   2057  C  CE1   . TYR   A 1  262 ? -34.838 73.261  -81.212  1.00 80.88  ? 262 TYR   A CE1   1 
ATOM   2058  C  CE2   . TYR   A 1  262 ? -35.000 71.100  -80.163  1.00 90.39  ? 262 TYR   A CE2   1 
ATOM   2059  C  CZ    . TYR   A 1  262 ? -35.041 71.896  -81.304  1.00 92.47  ? 262 TYR   A CZ    1 
ATOM   2060  O  OH    . TYR   A 1  262 ? -35.286 71.332  -82.538  1.00 91.53  ? 262 TYR   A OH    1 
ATOM   2061  N  N     . PRO   A 1  263 ? -36.555 74.879  -75.188  1.00 53.43  ? 263 PRO   A N     1 
ATOM   2062  C  CA    A PRO   A 1  263 ? -36.766 75.131  -73.752  0.99 49.03  ? 263 PRO   A CA    1 
ATOM   2063  C  CA    B PRO   A 1  263 ? -36.768 75.127  -73.749  0.01 49.16  ? 263 PRO   A CA    1 
ATOM   2064  C  C     . PRO   A 1  263 ? -35.848 74.329  -72.836  1.00 46.67  ? 263 PRO   A C     1 
ATOM   2065  O  O     . PRO   A 1  263 ? -35.285 74.894  -71.886  1.00 45.73  ? 263 PRO   A O     1 
ATOM   2066  C  CB    A PRO   A 1  263 ? -38.246 74.761  -73.557  0.99 52.29  ? 263 PRO   A CB    1 
ATOM   2067  C  CB    B PRO   A 1  263 ? -38.243 74.748  -73.552  0.01 52.24  ? 263 PRO   A CB    1 
ATOM   2068  C  CG    A PRO   A 1  263 ? -38.863 74.985  -74.896  0.99 55.26  ? 263 PRO   A CG    1 
ATOM   2069  C  CG    B PRO   A 1  263 ? -38.862 74.914  -74.901  0.01 55.04  ? 263 PRO   A CG    1 
ATOM   2070  C  CD    A PRO   A 1  263 ? -37.812 74.603  -75.905  0.99 53.66  ? 263 PRO   A CD    1 
ATOM   2071  C  CD    B PRO   A 1  263 ? -37.800 74.508  -75.880  0.01 53.59  ? 263 PRO   A CD    1 
ATOM   2072  N  N     . ARG   A 1  264 ? -35.679 73.020  -73.081  1.00 45.16  ? 264 ARG   A N     1 
ATOM   2073  C  CA    . ARG   A 1  264 ? -34.898 72.196  -72.148  1.00 45.82  ? 264 ARG   A CA    1 
ATOM   2074  C  C     . ARG   A 1  264 ? -33.403 72.471  -72.254  1.00 52.27  ? 264 ARG   A C     1 
ATOM   2075  O  O     . ARG   A 1  264 ? -32.701 72.508  -71.233  1.00 45.91  ? 264 ARG   A O     1 
ATOM   2076  C  CB    . ARG   A 1  264 ? -35.167 70.713  -72.381  1.00 49.12  ? 264 ARG   A CB    1 
ATOM   2077  C  CG    . ARG   A 1  264 ? -36.504 70.230  -71.838  1.00 41.00  ? 264 ARG   A CG    1 
ATOM   2078  C  CD    . ARG   A 1  264 ? -36.799 68.851  -72.363  1.00 40.43  ? 264 ARG   A CD    1 
ATOM   2079  N  NE    . ARG   A 1  264 ? -35.813 67.847  -71.962  1.00 48.39  ? 264 ARG   A NE    1 
ATOM   2080  C  CZ    . ARG   A 1  264 ? -35.802 67.249  -70.774  1.00 45.16  ? 264 ARG   A CZ    1 
ATOM   2081  N  NH1   . ARG   A 1  264 ? -36.613 67.638  -69.796  1.00 37.25  ? 264 ARG   A NH1   1 
ATOM   2082  N  NH2   . ARG   A 1  264 ? -34.972 66.226  -70.570  1.00 37.10  ? 264 ARG   A NH2   1 
ATOM   2083  N  N     . ILE   A 1  265 ? -32.898 72.631  -73.480  1.00 43.07  ? 265 ILE   A N     1 
ATOM   2084  C  CA    . ILE   A 1  265 ? -31.538 73.073  -73.755  1.00 32.54  ? 265 ILE   A CA    1 
ATOM   2085  C  C     . ILE   A 1  265 ? -31.410 74.560  -73.424  1.00 37.22  ? 265 ILE   A C     1 
ATOM   2086  O  O     . ILE   A 1  265 ? -31.105 75.384  -74.301  1.00 39.85  ? 265 ILE   A O     1 
ATOM   2087  C  CB    . ILE   A 1  265 ? -31.197 72.809  -75.237  1.00 47.15  ? 265 ILE   A CB    1 
ATOM   2088  C  CG1   . ILE   A 1  265 ? -31.812 71.494  -75.696  1.00 43.73  ? 265 ILE   A CG1   1 
ATOM   2089  C  CG2   . ILE   A 1  265 ? -29.691 72.784  -75.478  1.00 37.47  ? 265 ILE   A CG2   1 
ATOM   2090  C  CD1   . ILE   A 1  265 ? -31.027 70.295  -75.274  1.00 38.82  ? 265 ILE   A CD1   1 
ATOM   2091  N  N     . HIS   A 1  266 ? -31.640 74.935  -72.176  1.00 33.95  ? 266 HIS   A N     1 
ATOM   2092  C  CA    . HIS   A 1  266 ? -31.616 76.345  -71.796  1.00 32.90  ? 266 HIS   A CA    1 
ATOM   2093  C  C     . HIS   A 1  266 ? -30.415 76.708  -70.919  1.00 31.28  ? 266 HIS   A C     1 
ATOM   2094  O  O     . HIS   A 1  266 ? -30.518 77.555  -70.026  1.00 35.00  ? 266 HIS   A O     1 
ATOM   2095  C  CB    . HIS   A 1  266 ? -32.928 76.718  -71.110  1.00 36.51  ? 266 HIS   A CB    1 
ATOM   2096  C  CG    . HIS   A 1  266 ? -33.200 75.968  -69.836  1.00 42.72  ? 266 HIS   A CG    1 
ATOM   2097  N  ND1   . HIS   A 1  266 ? -34.461 75.550  -69.481  1.00 38.48  ? 266 HIS   A ND1   1 
ATOM   2098  C  CD2   . HIS   A 1  266 ? -32.383 75.602  -68.815  1.00 42.48  ? 266 HIS   A CD2   1 
ATOM   2099  C  CE1   . HIS   A 1  266 ? -34.410 74.946  -68.306  1.00 40.97  ? 266 HIS   A CE1   1 
ATOM   2100  N  NE2   . HIS   A 1  266 ? -33.162 74.969  -67.878  1.00 38.47  ? 266 HIS   A NE2   1 
ATOM   2101  N  N     . PHE   A 1  267 ? -29.255 76.074  -71.158  1.00 29.98  ? 267 PHE   A N     1 
ATOM   2102  C  CA    . PHE   A 1  267 ? -28.076 76.191  -70.292  1.00 36.18  ? 267 PHE   A CA    1 
ATOM   2103  C  C     . PHE   A 1  267 ? -26.931 76.754  -71.126  1.00 36.86  ? 267 PHE   A C     1 
ATOM   2104  O  O     . PHE   A 1  267 ? -26.098 76.001  -71.654  1.00 31.33  ? 267 PHE   A O     1 
ATOM   2105  C  CB    . PHE   A 1  267 ? -27.670 74.850  -69.668  1.00 25.77  ? 267 PHE   A CB    1 
ATOM   2106  C  CG    . PHE   A 1  267 ? -28.679 74.285  -68.707  1.00 30.67  ? 267 PHE   A CG    1 
ATOM   2107  C  CD1   . PHE   A 1  267 ? -28.657 74.637  -67.358  1.00 30.30  ? 267 PHE   A CD1   1 
ATOM   2108  C  CD2   . PHE   A 1  267 ? -29.652 73.396  -69.141  1.00 39.04  ? 267 PHE   A CD2   1 
ATOM   2109  C  CE1   . PHE   A 1  267 ? -29.573 74.116  -66.476  1.00 31.49  ? 267 PHE   A CE1   1 
ATOM   2110  C  CE2   . PHE   A 1  267 ? -30.605 72.861  -68.238  1.00 35.24  ? 267 PHE   A CE2   1 
ATOM   2111  C  CZ    . PHE   A 1  267 ? -30.557 73.218  -66.918  1.00 34.58  ? 267 PHE   A CZ    1 
ATOM   2112  N  N     . PRO   A 1  268 ? -26.850 78.070  -71.259  1.00 30.59  ? 268 PRO   A N     1 
ATOM   2113  C  CA    . PRO   A 1  268 ? -25.806 78.651  -72.100  1.00 30.57  ? 268 PRO   A CA    1 
ATOM   2114  C  C     . PRO   A 1  268 ? -24.464 78.761  -71.385  1.00 29.18  ? 268 PRO   A C     1 
ATOM   2115  O  O     . PRO   A 1  268 ? -24.371 79.099  -70.205  1.00 29.32  ? 268 PRO   A O     1 
ATOM   2116  C  CB    . PRO   A 1  268 ? -26.375 80.031  -72.471  1.00 35.03  ? 268 PRO   A CB    1 
ATOM   2117  C  CG    . PRO   A 1  268 ? -27.386 80.328  -71.464  1.00 31.27  ? 268 PRO   A CG    1 
ATOM   2118  C  CD    . PRO   A 1  268 ? -27.896 79.041  -70.902  1.00 34.96  ? 268 PRO   A CD    1 
ATOM   2119  N  N     . LEU   A 1  269 ? -23.420 78.460  -72.139  1.00 26.57  ? 269 LEU   A N     1 
ATOM   2120  C  CA    . LEU   A 1  269 ? -22.054 78.546  -71.666  1.00 25.89  ? 269 LEU   A CA    1 
ATOM   2121  C  C     . LEU   A 1  269 ? -21.609 79.998  -71.583  1.00 22.38  ? 269 LEU   A C     1 
ATOM   2122  O  O     . LEU   A 1  269 ? -21.878 80.806  -72.468  1.00 30.64  ? 269 LEU   A O     1 
ATOM   2123  C  CB    . LEU   A 1  269 ? -21.139 77.759  -72.612  1.00 25.53  ? 269 LEU   A CB    1 
ATOM   2124  C  CG    . LEU   A 1  269 ? -19.682 77.683  -72.196  1.00 29.93  ? 269 LEU   A CG    1 
ATOM   2125  C  CD1   . LEU   A 1  269 ? -19.561 76.852  -70.925  1.00 25.74  ? 269 LEU   A CD1   1 
ATOM   2126  C  CD2   . LEU   A 1  269 ? -18.815 77.113  -73.305  1.00 20.39  ? 269 LEU   A CD2   1 
ATOM   2127  N  N     . ALA   A 1  270 ? -20.924 80.332  -70.516  1.00 23.73  ? 270 ALA   A N     1 
ATOM   2128  C  CA    . ALA   A 1  270 ? -20.401 81.672  -70.321  1.00 27.94  ? 270 ALA   A CA    1 
ATOM   2129  C  C     . ALA   A 1  270 ? -18.891 81.587  -70.444  1.00 30.14  ? 270 ALA   A C     1 
ATOM   2130  O  O     . ALA   A 1  270 ? -18.279 80.612  -69.990  1.00 30.99  ? 270 ALA   A O     1 
ATOM   2131  C  CB    . ALA   A 1  270 ? -20.807 82.242  -68.949  1.00 18.95  ? 270 ALA   A CB    1 
ATOM   2132  N  N     . THR   A 1  271 ? -18.290 82.574  -71.100  1.00 24.26  ? 271 THR   A N     1 
ATOM   2133  C  CA    . THR   A 1  271 ? -16.841 82.607  -71.187  1.00 22.04  ? 271 THR   A CA    1 
ATOM   2134  C  C     . THR   A 1  271 ? -16.440 84.055  -71.079  1.00 31.30  ? 271 THR   A C     1 
ATOM   2135  O  O     . THR   A 1  271 ? -17.031 84.909  -71.745  1.00 31.78  ? 271 THR   A O     1 
ATOM   2136  C  CB    . THR   A 1  271 ? -16.308 81.988  -72.483  1.00 29.03  ? 271 THR   A CB    1 
ATOM   2137  O  OG1   . THR   A 1  271 ? -16.900 80.694  -72.680  1.00 31.21  ? 271 THR   A OG1   1 
ATOM   2138  C  CG2   . THR   A 1  271 ? -14.795 81.830  -72.391  1.00 27.14  ? 271 THR   A CG2   1 
ATOM   2139  N  N     . TYR   A 1  272 ? -15.448 84.323  -70.230  1.00 29.11  ? 272 TYR   A N     1 
ATOM   2140  C  CA    . TYR   A 1  272 ? -15.120 85.675  -69.823  1.00 22.35  ? 272 TYR   A CA    1 
ATOM   2141  C  C     . TYR   A 1  272 ? -13.629 85.893  -69.993  1.00 26.09  ? 272 TYR   A C     1 
ATOM   2142  O  O     . TYR   A 1  272 ? -12.842 84.953  -69.916  1.00 27.82  ? 272 TYR   A O     1 
ATOM   2143  C  CB    . TYR   A 1  272 ? -15.548 85.904  -68.378  1.00 21.13  ? 272 TYR   A CB    1 
ATOM   2144  C  CG    . TYR   A 1  272 ? -15.344 87.295  -67.876  1.00 23.52  ? 272 TYR   A CG    1 
ATOM   2145  C  CD1   . TYR   A 1  272 ? -16.234 88.305  -68.203  1.00 24.43  ? 272 TYR   A CD1   1 
ATOM   2146  C  CD2   . TYR   A 1  272 ? -14.270 87.601  -67.055  1.00 25.54  ? 272 TYR   A CD2   1 
ATOM   2147  C  CE1   . TYR   A 1  272 ? -16.042 89.598  -67.739  1.00 34.08  ? 272 TYR   A CE1   1 
ATOM   2148  C  CE2   . TYR   A 1  272 ? -14.074 88.883  -66.581  1.00 25.68  ? 272 TYR   A CE2   1 
ATOM   2149  C  CZ    . TYR   A 1  272 ? -14.962 89.881  -66.924  1.00 33.30  ? 272 TYR   A CZ    1 
ATOM   2150  O  OH    . TYR   A 1  272 ? -14.771 91.160  -66.456  1.00 37.34  ? 272 TYR   A OH    1 
ATOM   2151  N  N     . ALA   A 1  273 ? -13.254 87.142  -70.251  1.00 30.00  ? 273 ALA   A N     1 
ATOM   2152  C  CA    . ALA   A 1  273 ? -11.868 87.531  -70.450  1.00 31.18  ? 273 ALA   A CA    1 
ATOM   2153  C  C     . ALA   A 1  273 ? -11.782 89.047  -70.477  1.00 32.97  ? 273 ALA   A C     1 
ATOM   2154  O  O     . ALA   A 1  273 ? -12.731 89.719  -70.900  1.00 37.51  ? 273 ALA   A O     1 
ATOM   2155  C  CB    . ALA   A 1  273 ? -11.298 86.948  -71.750  1.00 27.22  ? 273 ALA   A CB    1 
ATOM   2156  N  N     . PRO   A 1  274 ? -10.656 89.619  -70.058  1.00 35.13  ? 274 PRO   A N     1 
ATOM   2157  C  CA    . PRO   A 1  274 ? -9.501  88.933  -69.479  1.00 34.61  ? 274 PRO   A CA    1 
ATOM   2158  C  C     . PRO   A 1  274 ? -9.567  88.898  -67.954  1.00 31.93  ? 274 PRO   A C     1 
ATOM   2159  O  O     . PRO   A 1  274 ? -10.051 89.821  -67.299  1.00 31.02  ? 274 PRO   A O     1 
ATOM   2160  C  CB    . PRO   A 1  274 ? -8.326  89.786  -69.968  1.00 27.37  ? 274 PRO   A CB    1 
ATOM   2161  C  CG    . PRO   A 1  274 ? -8.896  91.187  -69.909  1.00 34.62  ? 274 PRO   A CG    1 
ATOM   2162  C  CD    . PRO   A 1  274 ? -10.342 91.029  -70.370  1.00 36.26  ? 274 PRO   A CD    1 
ATOM   2163  N  N     . VAL   A 1  275 ? -9.078  87.818  -67.370  1.00 24.26  ? 275 VAL   A N     1 
ATOM   2164  C  CA    . VAL   A 1  275 ? -8.851  87.727  -65.937  1.00 28.91  ? 275 VAL   A CA    1 
ATOM   2165  C  C     . VAL   A 1  275 ? -7.362  87.945  -65.716  1.00 24.19  ? 275 VAL   A C     1 
ATOM   2166  O  O     . VAL   A 1  275 ? -6.549  87.086  -66.067  1.00 27.97  ? 275 VAL   A O     1 
ATOM   2167  C  CB    . VAL   A 1  275 ? -9.313  86.375  -65.376  1.00 25.18  ? 275 VAL   A CB    1 
ATOM   2168  C  CG1   . VAL   A 1  275 ? -9.164  86.352  -63.873  1.00 35.09  ? 275 VAL   A CG1   1 
ATOM   2169  C  CG2   . VAL   A 1  275 ? -10.731 86.133  -65.770  1.00 23.09  ? 275 VAL   A CG2   1 
ATOM   2170  N  N     . ILE   A 1  276 ? -7.017  89.095  -65.138  1.00 29.41  ? 276 ILE   A N     1 
ATOM   2171  C  CA    . ILE   A 1  276 ? -5.650  89.542  -64.900  1.00 27.48  ? 276 ILE   A CA    1 
ATOM   2172  C  C     . ILE   A 1  276 ? -5.474  89.852  -63.415  1.00 36.73  ? 276 ILE   A C     1 
ATOM   2173  O  O     . ILE   A 1  276 ? -6.309  90.540  -62.813  1.00 44.01  ? 276 ILE   A O     1 
ATOM   2174  C  CB    . ILE   A 1  276 ? -5.325  90.806  -65.726  1.00 37.60  ? 276 ILE   A CB    1 
ATOM   2175  C  CG1   . ILE   A 1  276 ? -5.561  90.588  -67.236  1.00 35.17  ? 276 ILE   A CG1   1 
ATOM   2176  C  CG2   . ILE   A 1  276 ? -3.932  91.315  -65.378  1.00 31.83  ? 276 ILE   A CG2   1 
ATOM   2177  C  CD1   . ILE   A 1  276 ? -4.594  89.621  -67.884  1.00 43.62  ? 276 ILE   A CD1   1 
ATOM   2178  N  N     . SER   A 1  277 ? -4.357  89.406  -62.845  1.00 35.72  ? 277 SER   A N     1 
ATOM   2179  C  CA    . SER   A 1  277 ? -4.045  89.684  -61.445  1.00 30.52  ? 277 SER   A CA    1 
ATOM   2180  C  C     . SER   A 1  277 ? -3.740  91.159  -61.225  1.00 42.52  ? 277 SER   A C     1 
ATOM   2181  O  O     . SER   A 1  277 ? -2.867  91.728  -61.889  1.00 47.63  ? 277 SER   A O     1 
ATOM   2182  C  CB    . SER   A 1  277 ? -2.848  88.845  -60.999  1.00 36.85  ? 277 SER   A CB    1 
ATOM   2183  O  OG    . SER   A 1  277 ? -2.318  89.328  -59.780  1.00 47.14  ? 277 SER   A OG    1 
ATOM   2184  N  N     . ALA   A 1  278 ? -4.434  91.777  -60.265  1.00 41.61  ? 278 ALA   A N     1 
ATOM   2185  C  CA    . ALA   A 1  278 ? -4.116  93.157  -59.912  1.00 49.76  ? 278 ALA   A CA    1 
ATOM   2186  C  C     . ALA   A 1  278 ? -2.714  93.300  -59.318  1.00 51.60  ? 278 ALA   A C     1 
ATOM   2187  O  O     . ALA   A 1  278 ? -2.166  94.406  -59.321  1.00 58.93  ? 278 ALA   A O     1 
ATOM   2188  C  CB    . ALA   A 1  278 ? -5.154  93.722  -58.939  1.00 44.24  ? 278 ALA   A CB    1 
ATOM   2189  N  N     . GLU   A 1  279 ? -2.112  92.219  -58.820  1.00 46.86  ? 279 GLU   A N     1 
ATOM   2190  C  CA    . GLU   A 1  279 ? -0.758  92.270  -58.284  1.00 54.99  ? 279 GLU   A CA    1 
ATOM   2191  C  C     . GLU   A 1  279 ? 0.307   92.035  -59.347  1.00 53.80  ? 279 GLU   A C     1 
ATOM   2192  O  O     . GLU   A 1  279 ? 1.452   91.742  -58.998  1.00 62.59  ? 279 GLU   A O     1 
ATOM   2193  C  CB    . GLU   A 1  279 ? -0.576  91.242  -57.158  1.00 55.97  ? 279 GLU   A CB    1 
ATOM   2194  C  CG    . GLU   A 1  279 ? -1.520  91.386  -55.971  1.00 63.36  ? 279 GLU   A CG    1 
ATOM   2195  C  CD    . GLU   A 1  279 ? -1.206  92.590  -55.093  1.00 75.69  ? 279 GLU   A CD    1 
ATOM   2196  O  OE1   . GLU   A 1  279 ? -0.262  92.501  -54.271  1.00 70.80  ? 279 GLU   A OE1   1 
ATOM   2197  O  OE2   . GLU   A 1  279 ? -1.908  93.623  -55.230  1.00 67.04  ? 279 GLU   A OE2   1 
ATOM   2198  N  N     . LYS   A 1  280 ? -0.041  92.131  -60.626  1.00 56.57  ? 280 LYS   A N     1 
ATOM   2199  C  CA    . LYS   A 1  280 ? 0.873   91.785  -61.716  1.00 62.58  ? 280 LYS   A CA    1 
ATOM   2200  C  C     . LYS   A 1  280 ? 1.528   93.067  -62.219  1.00 69.88  ? 280 LYS   A C     1 
ATOM   2201  O  O     . LYS   A 1  280 ? 0.850   93.939  -62.780  1.00 68.37  ? 280 LYS   A O     1 
ATOM   2202  C  CB    . LYS   A 1  280 ? 0.141   91.046  -62.840  1.00 53.94  ? 280 LYS   A CB    1 
ATOM   2203  C  CG    . LYS   A 1  280 ? 0.874   91.021  -64.171  1.00 58.59  ? 280 LYS   A CG    1 
ATOM   2204  C  CD    . LYS   A 1  280 ? 0.258   90.033  -65.159  1.00 47.19  ? 280 LYS   A CD    1 
ATOM   2205  C  CE    . LYS   A 1  280 ? 0.809   88.613  -64.976  1.00 67.01  ? 280 LYS   A CE    1 
ATOM   2206  N  NZ    . LYS   A 1  280 ? 0.303   87.876  -63.760  1.00 59.94  ? 280 LYS   A NZ    1 
ATOM   2207  N  N     . ALA   A 1  281 ? 2.844   93.179  -62.002  1.00 74.61  ? 281 ALA   A N     1 
ATOM   2208  C  CA    . ALA   A 1  281 ? 3.626   94.355  -62.376  1.00 74.95  ? 281 ALA   A CA    1 
ATOM   2209  C  C     . ALA   A 1  281 ? 3.467   94.652  -63.861  1.00 93.01  ? 281 ALA   A C     1 
ATOM   2210  O  O     . ALA   A 1  281 ? 4.045   93.957  -64.706  1.00 92.96  ? 281 ALA   A O     1 
ATOM   2211  C  CB    . ALA   A 1  281 ? 5.105   94.163  -62.021  1.00 65.04  ? 281 ALA   A CB    1 
ATOM   2212  N  N     . TYR   A 1  282 ? 2.691   95.696  -64.170  1.00 91.78  ? 282 TYR   A N     1 
ATOM   2213  C  CA    . TYR   A 1  282 ? 2.245   96.050  -65.515  1.00 88.89  ? 282 TYR   A CA    1 
ATOM   2214  C  C     . TYR   A 1  282 ? 1.914   94.856  -66.407  1.00 83.19  ? 282 TYR   A C     1 
ATOM   2215  O  O     . TYR   A 1  282 ? 2.744   93.965  -66.628  1.00 72.16  ? 282 TYR   A O     1 
ATOM   2216  C  CB    . TYR   A 1  282 ? 3.275   96.920  -66.233  1.00 92.26  ? 282 TYR   A CB    1 
ATOM   2217  C  CG    . TYR   A 1  282 ? 2.740   97.396  -67.561  1.00 87.77  ? 282 TYR   A CG    1 
ATOM   2218  C  CD1   . TYR   A 1  282 ? 1.994   98.569  -67.646  1.00 93.24  ? 282 TYR   A CD1   1 
ATOM   2219  C  CD2   . TYR   A 1  282 ? 2.939   96.654  -68.723  1.00 75.27  ? 282 TYR   A CD2   1 
ATOM   2220  C  CE1   . TYR   A 1  282 ? 1.480   99.010  -68.864  1.00 90.30  ? 282 TYR   A CE1   1 
ATOM   2221  C  CE2   . TYR   A 1  282 ? 2.426   97.084  -69.940  1.00 77.13  ? 282 TYR   A CE2   1 
ATOM   2222  C  CZ    . TYR   A 1  282 ? 1.697   98.263  -70.004  1.00 82.32  ? 282 TYR   A CZ    1 
ATOM   2223  O  OH    . TYR   A 1  282 ? 1.183   98.698  -71.205  1.00 89.76  ? 282 TYR   A OH    1 
ATOM   2224  N  N     . HIS   A 1  283 ? 0.703   94.861  -66.954  1.00 78.57  ? 283 HIS   A N     1 
ATOM   2225  C  CA    . HIS   A 1  283 ? 0.282   93.900  -67.958  1.00 65.11  ? 283 HIS   A CA    1 
ATOM   2226  C  C     . HIS   A 1  283 ? 0.116   94.628  -69.282  1.00 69.32  ? 283 HIS   A C     1 
ATOM   2227  O  O     . HIS   A 1  283 ? -0.506  95.696  -69.324  1.00 74.64  ? 283 HIS   A O     1 
ATOM   2228  C  CB    . HIS   A 1  283 ? -1.033  93.236  -67.555  1.00 62.02  ? 283 HIS   A CB    1 
ATOM   2229  C  CG    . HIS   A 1  283 ? -1.347  92.001  -68.342  1.00 69.29  ? 283 HIS   A CG    1 
ATOM   2230  N  ND1   . HIS   A 1  283 ? -0.793  90.770  -68.049  1.00 59.45  ? 283 HIS   A ND1   1 
ATOM   2231  C  CD2   . HIS   A 1  283 ? -2.147  91.810  -69.419  1.00 62.06  ? 283 HIS   A CD2   1 
ATOM   2232  C  CE1   . HIS   A 1  283 ? -1.243  89.874  -68.911  1.00 66.80  ? 283 HIS   A CE1   1 
ATOM   2233  N  NE2   . HIS   A 1  283 ? -2.065  90.478  -69.752  1.00 64.56  ? 283 HIS   A NE2   1 
ATOM   2234  N  N     . GLU   A 1  284 ? 0.674   94.065  -70.359  1.00 63.92  ? 284 GLU   A N     1 
ATOM   2235  C  CA    . GLU   A 1  284 ? 0.401   94.608  -71.690  1.00 62.36  ? 284 GLU   A CA    1 
ATOM   2236  C  C     . GLU   A 1  284 ? -1.071  94.375  -72.029  1.00 63.22  ? 284 GLU   A C     1 
ATOM   2237  O  O     . GLU   A 1  284 ? -1.532  93.228  -72.090  1.00 51.67  ? 284 GLU   A O     1 
ATOM   2238  C  CB    . GLU   A 1  284 ? 1.314   93.981  -72.743  1.00 34.11  ? 284 GLU   A CB    1 
ATOM   2239  N  N     . GLN   A 1  285 ? -1.816  95.465  -72.220  1.00 61.07  ? 285 GLN   A N     1 
ATOM   2240  C  CA    . GLN   A 1  285 ? -3.264  95.361  -72.335  1.00 55.88  ? 285 GLN   A CA    1 
ATOM   2241  C  C     . GLN   A 1  285 ? -3.674  94.536  -73.557  1.00 52.21  ? 285 GLN   A C     1 
ATOM   2242  O  O     . GLN   A 1  285 ? -2.992  94.508  -74.586  1.00 53.77  ? 285 GLN   A O     1 
ATOM   2243  C  CB    . GLN   A 1  285 ? -3.893  96.750  -72.392  1.00 55.86  ? 285 GLN   A CB    1 
ATOM   2244  C  CG    . GLN   A 1  285 ? -5.377  96.746  -72.079  1.00 57.83  ? 285 GLN   A CG    1 
ATOM   2245  C  CD    . GLN   A 1  285 ? -5.701  96.926  -70.581  1.00 62.77  ? 285 GLN   A CD    1 
ATOM   2246  O  OE1   . GLN   A 1  285 ? -6.744  97.493  -70.227  1.00 50.05  ? 285 GLN   A OE1   1 
ATOM   2247  N  NE2   . GLN   A 1  285 ? -4.820  96.427  -69.706  1.00 63.16  ? 285 GLN   A NE2   1 
ATOM   2248  N  N     . LEU   A 1  286 ? -4.804  93.851  -73.431  1.00 50.42  ? 286 LEU   A N     1 
ATOM   2249  C  CA    . LEU   A 1  286 ? -5.290  92.976  -74.483  1.00 44.60  ? 286 LEU   A CA    1 
ATOM   2250  C  C     . LEU   A 1  286 ? -6.247  93.720  -75.408  1.00 43.07  ? 286 LEU   A C     1 
ATOM   2251  O  O     . LEU   A 1  286 ? -7.068  94.523  -74.960  1.00 40.76  ? 286 LEU   A O     1 
ATOM   2252  C  CB    . LEU   A 1  286 ? -5.986  91.751  -73.887  1.00 41.72  ? 286 LEU   A CB    1 
ATOM   2253  C  CG    . LEU   A 1  286 ? -5.120  90.610  -73.367  1.00 40.58  ? 286 LEU   A CG    1 
ATOM   2254  C  CD1   . LEU   A 1  286 ? -3.862  90.459  -74.203  1.00 47.46  ? 286 LEU   A CD1   1 
ATOM   2255  C  CD2   . LEU   A 1  286 ? -4.776  90.828  -71.929  1.00 44.46  ? 286 LEU   A CD2   1 
ATOM   2256  N  N     . SER   A 1  287 ? -6.147  93.424  -76.702  1.00 41.89  ? 287 SER   A N     1 
ATOM   2257  C  CA    . SER   A 1  287 ? -6.963  94.049  -77.731  1.00 37.71  ? 287 SER   A CA    1 
ATOM   2258  C  C     . SER   A 1  287 ? -8.353  93.410  -77.790  1.00 45.69  ? 287 SER   A C     1 
ATOM   2259  O  O     . SER   A 1  287 ? -8.656  92.439  -77.086  1.00 48.45  ? 287 SER   A O     1 
ATOM   2260  C  CB    . SER   A 1  287 ? -6.271  93.939  -79.085  1.00 26.80  ? 287 SER   A CB    1 
ATOM   2261  O  OG    . SER   A 1  287 ? -6.115  92.579  -79.458  1.00 34.26  ? 287 SER   A OG    1 
ATOM   2262  N  N     . VAL   A 1  288 ? -9.216  93.991  -78.633  1.00 29.22  ? 288 VAL   A N     1 
ATOM   2263  C  CA    . VAL   A 1  288 ? -10.513 93.395  -78.921  1.00 33.14  ? 288 VAL   A CA    1 
ATOM   2264  C  C     . VAL   A 1  288 ? -10.338 92.050  -79.617  1.00 39.05  ? 288 VAL   A C     1 
ATOM   2265  O  O     . VAL   A 1  288 ? -11.130 91.124  -79.410  1.00 39.48  ? 288 VAL   A O     1 
ATOM   2266  C  CB    . VAL   A 1  288 ? -11.360 94.381  -79.756  1.00 35.40  ? 288 VAL   A CB    1 
ATOM   2267  C  CG1   . VAL   A 1  288 ? -12.544 93.680  -80.419  1.00 29.12  ? 288 VAL   A CG1   1 
ATOM   2268  C  CG2   . VAL   A 1  288 ? -11.835 95.519  -78.869  1.00 39.55  ? 288 VAL   A CG2   1 
ATOM   2269  N  N     . ALA   A 1  289 ? -9.304  91.918  -80.447  1.00 36.22  ? 289 ALA   A N     1 
ATOM   2270  C  CA    . ALA   A 1  289 ? -9.004  90.629  -81.056  1.00 38.94  ? 289 ALA   A CA    1 
ATOM   2271  C  C     . ALA   A 1  289 ? -8.638  89.604  -79.991  1.00 44.51  ? 289 ALA   A C     1 
ATOM   2272  O  O     . ALA   A 1  289 ? -9.173  88.488  -79.965  1.00 45.31  ? 289 ALA   A O     1 
ATOM   2273  C  CB    . ALA   A 1  289 ? -7.860  90.773  -82.066  1.00 23.37  ? 289 ALA   A CB    1 
ATOM   2274  N  N     . GLU   A 1  290 ? -7.725  89.976  -79.094  1.00 38.71  ? 290 GLU   A N     1 
ATOM   2275  C  CA    . GLU   A 1  290 ? -7.198  89.026  -78.127  1.00 43.50  ? 290 GLU   A CA    1 
ATOM   2276  C  C     . GLU   A 1  290 ? -8.277  88.558  -77.143  1.00 35.68  ? 290 GLU   A C     1 
ATOM   2277  O  O     . GLU   A 1  290 ? -8.417  87.356  -76.900  1.00 40.05  ? 290 GLU   A O     1 
ATOM   2278  C  CB    . GLU   A 1  290 ? -5.995  89.655  -77.422  1.00 40.27  ? 290 GLU   A CB    1 
ATOM   2279  C  CG    . GLU   A 1  290 ? -4.796  89.828  -78.371  1.00 34.44  ? 290 GLU   A CG    1 
ATOM   2280  C  CD    . GLU   A 1  290 ? -3.643  90.676  -77.780  1.00 50.42  ? 290 GLU   A CD    1 
ATOM   2281  O  OE1   . GLU   A 1  290 ? -3.904  91.792  -77.273  1.00 45.45  ? 290 GLU   A OE1   1 
ATOM   2282  O  OE2   . GLU   A 1  290 ? -2.469  90.227  -77.830  1.00 48.84  ? 290 GLU   A OE2   1 
ATOM   2283  N  N     . ILE   A 1  291 ? -9.069  89.480  -76.592  1.00 37.05  ? 291 ILE   A N     1 
ATOM   2284  C  CA    . ILE   A 1  291 ? -10.126 89.091  -75.655  1.00 36.51  ? 291 ILE   A CA    1 
ATOM   2285  C  C     . ILE   A 1  291 ? -11.204 88.276  -76.356  1.00 40.41  ? 291 ILE   A C     1 
ATOM   2286  O  O     . ILE   A 1  291 ? -11.772 87.349  -75.771  1.00 37.59  ? 291 ILE   A O     1 
ATOM   2287  C  CB    . ILE   A 1  291 ? -10.745 90.320  -74.964  1.00 32.02  ? 291 ILE   A CB    1 
ATOM   2288  C  CG1   . ILE   A 1  291 ? -11.523 91.174  -75.978  1.00 36.07  ? 291 ILE   A CG1   1 
ATOM   2289  C  CG2   . ILE   A 1  291 ? -9.694  91.113  -74.239  1.00 32.41  ? 291 ILE   A CG2   1 
ATOM   2290  C  CD1   . ILE   A 1  291 ? -12.376 92.269  -75.358  1.00 31.50  ? 291 ILE   A CD1   1 
ATOM   2291  N  N     . THR   A 1  292 ? -11.524 88.614  -77.610  1.00 42.37  ? 292 THR   A N     1 
ATOM   2292  C  CA    . THR   A 1  292 ? -12.587 87.884  -78.296  1.00 38.42  ? 292 THR   A CA    1 
ATOM   2293  C  C     . THR   A 1  292 ? -12.132 86.481  -78.641  1.00 42.78  ? 292 THR   A C     1 
ATOM   2294  O  O     . THR   A 1  292 ? -12.872 85.511  -78.450  1.00 42.47  ? 292 THR   A O     1 
ATOM   2295  C  CB    . THR   A 1  292 ? -13.032 88.626  -79.552  1.00 30.29  ? 292 THR   A CB    1 
ATOM   2296  O  OG1   . THR   A 1  292 ? -13.468 89.939  -79.180  1.00 39.05  ? 292 THR   A OG1   1 
ATOM   2297  C  CG2   . THR   A 1  292 ? -14.185 87.902  -80.222  1.00 19.59  ? 292 THR   A CG2   1 
ATOM   2298  N  N     . ASN   A 1  293 ? -10.909 86.347  -79.141  1.00 46.15  ? 293 ASN   A N     1 
ATOM   2299  C  CA    . ASN   A 1  293 ? -10.380 85.012  -79.358  1.00 48.11  ? 293 ASN   A CA    1 
ATOM   2300  C  C     . ASN   A 1  293 ? -10.401 84.213  -78.059  1.00 44.15  ? 293 ASN   A C     1 
ATOM   2301  O  O     . ASN   A 1  293 ? -10.858 83.062  -78.027  1.00 39.84  ? 293 ASN   A O     1 
ATOM   2302  C  CB    . ASN   A 1  293 ? -8.969  85.087  -79.937  1.00 35.59  ? 293 ASN   A CB    1 
ATOM   2303  C  CG    . ASN   A 1  293 ? -8.577  83.813  -80.623  1.00 43.76  ? 293 ASN   A CG    1 
ATOM   2304  O  OD1   . ASN   A 1  293 ? -9.390  83.207  -81.347  1.00 42.22  ? 293 ASN   A OD1   1 
ATOM   2305  N  ND2   . ASN   A 1  293 ? -7.338  83.365  -80.383  1.00 39.84  ? 293 ASN   A ND2   1 
ATOM   2306  N  N     . ALA   A 1  294 ? -9.945  84.827  -76.965  1.00 35.13  ? 294 ALA   A N     1 
ATOM   2307  C  CA    . ALA   A 1  294 ? -9.873  84.118  -75.700  1.00 33.64  ? 294 ALA   A CA    1 
ATOM   2308  C  C     . ALA   A 1  294 ? -11.220 83.529  -75.308  1.00 42.66  ? 294 ALA   A C     1 
ATOM   2309  O  O     . ALA   A 1  294 ? -11.268 82.613  -74.476  1.00 35.12  ? 294 ALA   A O     1 
ATOM   2310  C  CB    . ALA   A 1  294 ? -9.366  85.061  -74.628  1.00 29.54  ? 294 ALA   A CB    1 
ATOM   2311  N  N     . CYS   A 1  295 ? -12.304 84.026  -75.919  1.00 39.44  ? 295 CYS   A N     1 
ATOM   2312  C  CA    . CYS   A 1  295 ? -13.655 83.532  -75.706  1.00 37.42  ? 295 CYS   A CA    1 
ATOM   2313  C  C     . CYS   A 1  295 ? -13.854 82.106  -76.184  1.00 33.09  ? 295 CYS   A C     1 
ATOM   2314  O  O     . CYS   A 1  295 ? -14.784 81.437  -75.723  1.00 40.23  ? 295 CYS   A O     1 
ATOM   2315  C  CB    . CYS   A 1  295 ? -14.661 84.439  -76.416  1.00 40.76  ? 295 CYS   A CB    1 
ATOM   2316  S  SG    . CYS   A 1  295 ? -15.126 85.877  -75.445  1.00 44.38  ? 295 CYS   A SG    1 
ATOM   2317  N  N     . PHE   A 1  296 ? -13.031 81.633  -77.111  1.00 39.18  ? 296 PHE   A N     1 
ATOM   2318  C  CA    . PHE   A 1  296 ? -13.120 80.267  -77.605  1.00 35.51  ? 296 PHE   A CA    1 
ATOM   2319  C  C     . PHE   A 1  296 ? -12.028 79.376  -77.029  1.00 34.24  ? 296 PHE   A C     1 
ATOM   2320  O  O     . PHE   A 1  296 ? -11.699 78.352  -77.626  1.00 34.58  ? 296 PHE   A O     1 
ATOM   2321  C  CB    . PHE   A 1  296 ? -13.099 80.276  -79.135  1.00 39.31  ? 296 PHE   A CB    1 
ATOM   2322  C  CG    . PHE   A 1  296 ? -14.233 81.076  -79.721  1.00 44.94  ? 296 PHE   A CG    1 
ATOM   2323  C  CD1   . PHE   A 1  296 ? -14.152 82.460  -79.801  1.00 37.36  ? 296 PHE   A CD1   1 
ATOM   2324  C  CD2   . PHE   A 1  296 ? -15.410 80.453  -80.115  1.00 38.71  ? 296 PHE   A CD2   1 
ATOM   2325  C  CE1   . PHE   A 1  296 ? -15.200 83.195  -80.294  1.00 34.77  ? 296 PHE   A CE1   1 
ATOM   2326  C  CE2   . PHE   A 1  296 ? -16.468 81.194  -80.608  1.00 38.84  ? 296 PHE   A CE2   1 
ATOM   2327  C  CZ    . PHE   A 1  296 ? -16.360 82.564  -80.710  1.00 33.84  ? 296 PHE   A CZ    1 
ATOM   2328  N  N     . GLU   A 1  297 ? -11.479 79.746  -75.863  1.00 34.90  ? 297 GLU   A N     1 
ATOM   2329  C  CA    . GLU   A 1  297 ? -10.523 78.932  -75.125  1.00 30.90  ? 297 GLU   A CA    1 
ATOM   2330  C  C     . GLU   A 1  297 ? -11.210 78.259  -73.941  1.00 38.73  ? 297 GLU   A C     1 
ATOM   2331  O  O     . GLU   A 1  297 ? -11.728 78.958  -73.052  1.00 33.33  ? 297 GLU   A O     1 
ATOM   2332  C  CB    . GLU   A 1  297 ? -9.372  79.791  -74.632  1.00 34.50  ? 297 GLU   A CB    1 
ATOM   2333  C  CG    . GLU   A 1  297 ? -8.486  80.292  -75.722  1.00 46.43  ? 297 GLU   A CG    1 
ATOM   2334  C  CD    . GLU   A 1  297 ? -7.682  79.186  -76.389  1.00 50.38  ? 297 GLU   A CD    1 
ATOM   2335  O  OE1   . GLU   A 1  297 ? -7.604  78.068  -75.830  1.00 50.69  ? 297 GLU   A OE1   1 
ATOM   2336  O  OE2   . GLU   A 1  297 ? -7.113  79.452  -77.472  1.00 48.69  ? 297 GLU   A OE2   1 
ATOM   2337  N  N     . PRO   A 1  298 ? -11.225 76.928  -73.868  1.00 37.65  ? 298 PRO   A N     1 
ATOM   2338  C  CA    . PRO   A 1  298 ? -11.874 76.260  -72.726  1.00 27.54  ? 298 PRO   A CA    1 
ATOM   2339  C  C     . PRO   A 1  298 ? -11.469 76.802  -71.356  1.00 33.34  ? 298 PRO   A C     1 
ATOM   2340  O  O     . PRO   A 1  298 ? -12.313 76.855  -70.445  1.00 39.69  ? 298 PRO   A O     1 
ATOM   2341  C  CB    . PRO   A 1  298 ? -11.433 74.808  -72.910  1.00 32.24  ? 298 PRO   A CB    1 
ATOM   2342  C  CG    . PRO   A 1  298 ? -11.246 74.674  -74.365  1.00 37.29  ? 298 PRO   A CG    1 
ATOM   2343  C  CD    . PRO   A 1  298 ? -10.658 75.966  -74.822  1.00 29.95  ? 298 PRO   A CD    1 
ATOM   2344  N  N     . ALA   A 1  299 ? -10.204 77.191  -71.177  1.00 25.09  ? 299 ALA   A N     1 
ATOM   2345  C  CA    . ALA   A 1  299 ? -9.675  77.673  -69.897  1.00 23.17  ? 299 ALA   A CA    1 
ATOM   2346  C  C     . ALA   A 1  299 ? -10.280 78.996  -69.446  1.00 26.83  ? 299 ALA   A C     1 
ATOM   2347  O  O     . ALA   A 1  299 ? -9.925  79.511  -68.375  1.00 30.04  ? 299 ALA   A O     1 
ATOM   2348  C  CB    . ALA   A 1  299 ? -8.155  77.820  -69.987  1.00 24.31  ? 299 ALA   A CB    1 
ATOM   2349  N  N     . ASN   A 1  300 ? -11.178 79.578  -70.218  1.00 26.11  ? 300 ASN   A N     1 
ATOM   2350  C  CA    . ASN   A 1  300 ? -11.866 80.772  -69.779  1.00 27.23  ? 300 ASN   A CA    1 
ATOM   2351  C  C     . ASN   A 1  300 ? -13.351 80.538  -69.606  1.00 27.47  ? 300 ASN   A C     1 
ATOM   2352  O  O     . ASN   A 1  300 ? -14.065 81.454  -69.196  1.00 29.79  ? 300 ASN   A O     1 
ATOM   2353  C  CB    . ASN   A 1  300 ? -11.602 81.914  -70.767  1.00 22.92  ? 300 ASN   A CB    1 
ATOM   2354  C  CG    . ASN   A 1  300 ? -10.134 82.089  -71.026  1.00 30.60  ? 300 ASN   A CG    1 
ATOM   2355  O  OD1   . ASN   A 1  300 ? -9.665  81.998  -72.165  1.00 36.89  ? 300 ASN   A OD1   1 
ATOM   2356  N  ND2   . ASN   A 1  300 ? -9.380  82.288  -69.955  1.00 26.52  ? 300 ASN   A ND2   1 
ATOM   2357  N  N     . GLN   A 1  301 ? -13.830 79.344  -69.907  1.00 23.56  ? 301 GLN   A N     1 
ATOM   2358  C  CA    . GLN   A 1  301 ? -15.233 79.024  -69.780  1.00 31.00  ? 301 GLN   A CA    1 
ATOM   2359  C  C     . GLN   A 1  301 ? -15.625 78.824  -68.309  1.00 24.60  ? 301 GLN   A C     1 
ATOM   2360  O  O     . GLN   A 1  301 ? -14.798 78.481  -67.464  1.00 26.61  ? 301 GLN   A O     1 
ATOM   2361  C  CB    . GLN   A 1  301 ? -15.531 77.793  -70.639  1.00 27.91  ? 301 GLN   A CB    1 
ATOM   2362  C  CG    . GLN   A 1  301 ? -15.007 77.990  -72.054  1.00 22.32  ? 301 GLN   A CG    1 
ATOM   2363  C  CD    . GLN   A 1  301 ? -15.233 76.814  -73.003  1.00 28.41  ? 301 GLN   A CD    1 
ATOM   2364  O  OE1   . GLN   A 1  301 ? -15.264 76.999  -74.214  1.00 37.76  ? 301 GLN   A OE1   1 
ATOM   2365  N  NE2   . GLN   A 1  301 ? -15.372 75.615  -72.469  1.00 31.65  ? 301 GLN   A NE2   1 
ATOM   2366  N  N     . MET   A 1  302 ? -16.899 79.089  -67.998  1.00 29.32  ? 302 MET   A N     1 
ATOM   2367  C  CA    . MET   A 1  302 ? -17.411 78.841  -66.648  1.00 29.26  ? 302 MET   A CA    1 
ATOM   2368  C  C     . MET   A 1  302 ? -17.671 77.367  -66.415  1.00 29.27  ? 302 MET   A C     1 
ATOM   2369  O  O     . MET   A 1  302 ? -18.073 76.981  -65.320  1.00 39.02  ? 302 MET   A O     1 
ATOM   2370  C  CB    . MET   A 1  302 ? -18.678 79.663  -66.389  1.00 27.21  ? 302 MET   A CB    1 
ATOM   2371  C  CG    . MET   A 1  302 ? -18.476 81.128  -66.725  1.00 36.20  ? 302 MET   A CG    1 
ATOM   2372  S  SD    . MET   A 1  302 ? -17.001 81.755  -65.862  1.00 52.03  ? 302 MET   A SD    1 
ATOM   2373  C  CE    . MET   A 1  302 ? -17.788 81.856  -64.283  1.00 35.49  ? 302 MET   A CE    1 
ATOM   2374  N  N     . VAL   A 1  303 ? -17.382 76.549  -67.412  1.00 23.29  ? 303 VAL   A N     1 
ATOM   2375  C  CA    . VAL   A 1  303 ? -17.548 75.115  -67.404  1.00 26.10  ? 303 VAL   A CA    1 
ATOM   2376  C  C     . VAL   A 1  303 ? -16.487 74.582  -68.356  1.00 35.27  ? 303 VAL   A C     1 
ATOM   2377  O  O     . VAL   A 1  303 ? -16.462 74.955  -69.536  1.00 37.10  ? 303 VAL   A O     1 
ATOM   2378  C  CB    . VAL   A 1  303 ? -18.963 74.726  -67.867  1.00 34.12  ? 303 VAL   A CB    1 
ATOM   2379  C  CG1   . VAL   A 1  303 ? -19.149 73.238  -67.810  1.00 31.44  ? 303 VAL   A CG1   1 
ATOM   2380  C  CG2   . VAL   A 1  303 ? -20.013 75.480  -67.057  1.00 29.79  ? 303 VAL   A CG2   1 
ATOM   2381  N  N     . LYS   A 1  304 ? -15.588 73.735  -67.868  1.00 35.51  ? 304 LYS   A N     1 
ATOM   2382  C  CA    . LYS   A 1  304 ? -14.643 73.113  -68.780  1.00 30.84  ? 304 LYS   A CA    1 
ATOM   2383  C  C     . LYS   A 1  304 ? -15.385 72.150  -69.696  1.00 32.22  ? 304 LYS   A C     1 
ATOM   2384  O  O     . LYS   A 1  304 ? -16.199 71.345  -69.237  1.00 43.50  ? 304 LYS   A O     1 
ATOM   2385  C  CB    . LYS   A 1  304 ? -13.550 72.390  -68.010  1.00 29.16  ? 304 LYS   A CB    1 
ATOM   2386  C  CG    . LYS   A 1  304 ? -12.645 73.323  -67.252  1.00 30.78  ? 304 LYS   A CG    1 
ATOM   2387  C  CD    . LYS   A 1  304 ? -11.431 72.579  -66.716  1.00 32.89  ? 304 LYS   A CD    1 
ATOM   2388  C  CE    . LYS   A 1  304 ? -10.588 73.465  -65.829  1.00 35.69  ? 304 LYS   A CE    1 
ATOM   2389  N  NZ    . LYS   A 1  304 ? -9.294  72.784  -65.506  1.00 53.52  ? 304 LYS   A NZ    1 
ATOM   2390  N  N     . CYS   A 1  305 ? -15.115 72.249  -70.992  1.00 32.83  ? 305 CYS   A N     1 
ATOM   2391  C  CA    . CYS   A 1  305 ? -15.769 71.437  -72.011  1.00 34.88  ? 305 CYS   A CA    1 
ATOM   2392  C  C     . CYS   A 1  305 ? -15.288 71.940  -73.362  1.00 30.64  ? 305 CYS   A C     1 
ATOM   2393  O  O     . CYS   A 1  305 ? -14.793 73.064  -73.449  1.00 28.96  ? 305 CYS   A O     1 
ATOM   2394  C  CB    . CYS   A 1  305 ? -17.296 71.520  -71.905  1.00 33.68  ? 305 CYS   A CB    1 
ATOM   2395  S  SG    . CYS   A 1  305 ? -18.023 73.165  -72.306  1.00 34.50  ? 305 CYS   A SG    1 
ATOM   2396  N  N     . ASP   A 1  306 ? -15.437 71.144  -74.421  1.00 31.04  ? 306 ASP   A N     1 
ATOM   2397  C  CA    . ASP   A 1  306 ? -14.825 71.460  -75.710  1.00 35.18  ? 306 ASP   A CA    1 
ATOM   2398  C  C     . ASP   A 1  306 ? -15.887 71.787  -76.759  1.00 29.13  ? 306 ASP   A C     1 
ATOM   2399  O  O     . ASP   A 1  306 ? -16.388 70.888  -77.453  1.00 29.07  ? 306 ASP   A O     1 
ATOM   2400  C  CB    . ASP   A 1  306 ? -13.934 70.300  -76.171  1.00 25.96  ? 306 ASP   A CB    1 
ATOM   2401  C  CG    . ASP   A 1  306 ? -13.037 70.672  -77.350  1.00 33.30  ? 306 ASP   A CG    1 
ATOM   2402  O  OD1   . ASP   A 1  306 ? -13.362 71.608  -78.119  1.00 32.28  ? 306 ASP   A OD1   1 
ATOM   2403  O  OD2   . ASP   A 1  306 ? -11.994 70.017  -77.513  1.00 31.59  ? 306 ASP   A OD2   1 
ATOM   2404  N  N     . PRO   A 1  307 ? -16.233 73.063  -76.941  1.00 27.44  ? 307 PRO   A N     1 
ATOM   2405  C  CA    . PRO   A 1  307 ? -17.251 73.430  -77.954  1.00 33.45  ? 307 PRO   A CA    1 
ATOM   2406  C  C     . PRO   A 1  307 ? -16.878 73.094  -79.403  1.00 30.84  ? 307 PRO   A C     1 
ATOM   2407  O  O     . PRO   A 1  307 ? -17.741 73.205  -80.279  1.00 37.60  ? 307 PRO   A O     1 
ATOM   2408  C  CB    . PRO   A 1  307 ? -17.413 74.948  -77.772  1.00 28.03  ? 307 PRO   A CB    1 
ATOM   2409  C  CG    . PRO   A 1  307 ? -16.804 75.271  -76.456  1.00 37.08  ? 307 PRO   A CG    1 
ATOM   2410  C  CD    . PRO   A 1  307 ? -15.733 74.231  -76.202  1.00 34.57  ? 307 PRO   A CD    1 
ATOM   2411  N  N     . ARG   A 1  308 ? -15.645 72.683  -79.696  1.00 35.67  ? 308 ARG   A N     1 
ATOM   2412  C  CA    . ARG   A 1  308 ? -15.362 72.187  -81.041  1.00 37.41  ? 308 ARG   A CA    1 
ATOM   2413  C  C     . ARG   A 1  308 ? -16.175 70.941  -81.345  1.00 39.36  ? 308 ARG   A C     1 
ATOM   2414  O  O     . ARG   A 1  308 ? -16.572 70.726  -82.494  1.00 46.26  ? 308 ARG   A O     1 
ATOM   2415  C  CB    . ARG   A 1  308 ? -13.872 71.888  -81.212  1.00 32.26  ? 308 ARG   A CB    1 
ATOM   2416  C  CG    . ARG   A 1  308 ? -12.952 73.089  -81.021  1.00 31.12  ? 308 ARG   A CG    1 
ATOM   2417  C  CD    . ARG   A 1  308 ? -11.497 72.642  -81.009  1.00 30.54  ? 308 ARG   A CD    1 
ATOM   2418  N  NE    . ARG   A 1  308 ? -11.241 71.705  -79.926  1.00 29.91  ? 308 ARG   A NE    1 
ATOM   2419  C  CZ    . ARG   A 1  308 ? -10.104 71.048  -79.755  1.00 32.04  ? 308 ARG   A CZ    1 
ATOM   2420  N  NH1   . ARG   A 1  308 ? -9.101  71.158  -80.617  1.00 29.38  ? 308 ARG   A NH1   1 
ATOM   2421  N  NH2   . ARG   A 1  308 ? -9.974  70.248  -78.702  1.00 28.88  ? 308 ARG   A NH2   1 
ATOM   2422  N  N     . HIS   A 1  309 ? -16.438 70.118  -80.331  1.00 36.21  ? 309 HIS   A N     1 
ATOM   2423  C  CA    . HIS   A 1  309 ? -17.141 68.849  -80.493  1.00 29.54  ? 309 HIS   A CA    1 
ATOM   2424  C  C     . HIS   A 1  309 ? -18.569 69.026  -79.999  1.00 34.05  ? 309 HIS   A C     1 
ATOM   2425  O  O     . HIS   A 1  309 ? -18.947 68.613  -78.900  1.00 46.60  ? 309 HIS   A O     1 
ATOM   2426  C  CB    . HIS   A 1  309 ? -16.402 67.750  -79.753  1.00 36.52  ? 309 HIS   A CB    1 
ATOM   2427  C  CG    . HIS   A 1  309 ? -15.049 67.498  -80.317  1.00 37.90  ? 309 HIS   A CG    1 
ATOM   2428  N  ND1   . HIS   A 1  309 ? -13.934 68.196  -79.905  1.00 36.30  ? 309 HIS   A ND1   1 
ATOM   2429  C  CD2   . HIS   A 1  309 ? -14.644 66.686  -81.320  1.00 34.91  ? 309 HIS   A CD2   1 
ATOM   2430  C  CE1   . HIS   A 1  309 ? -12.890 67.802  -80.609  1.00 37.44  ? 309 HIS   A CE1   1 
ATOM   2431  N  NE2   . HIS   A 1  309 ? -13.293 66.884  -81.472  1.00 45.42  ? 309 HIS   A NE2   1 
ATOM   2432  N  N     . GLY   A 1  310 ? -19.358 69.641  -80.849  1.00 43.86  ? 310 GLY   A N     1 
ATOM   2433  C  CA    . GLY   A 1  310 ? -20.695 70.109  -80.555  1.00 44.96  ? 310 GLY   A CA    1 
ATOM   2434  C  C     . GLY   A 1  310 ? -21.015 71.248  -81.491  1.00 44.54  ? 310 GLY   A C     1 
ATOM   2435  O  O     . GLY   A 1  310 ? -20.139 71.858  -82.098  1.00 47.05  ? 310 GLY   A O     1 
ATOM   2436  N  N     . LYS   A 1  311 ? -22.305 71.509  -81.638  1.00 44.27  ? 311 LYS   A N     1 
ATOM   2437  C  CA    . LYS   A 1  311 ? -22.759 72.604  -82.471  1.00 42.11  ? 311 LYS   A CA    1 
ATOM   2438  C  C     . LYS   A 1  311 ? -23.147 73.781  -81.591  1.00 40.97  ? 311 LYS   A C     1 
ATOM   2439  O  O     . LYS   A 1  311 ? -23.199 73.682  -80.364  1.00 44.33  ? 311 LYS   A O     1 
ATOM   2440  C  CB    . LYS   A 1  311 ? -23.935 72.174  -83.352  1.00 49.35  ? 311 LYS   A CB    1 
ATOM   2441  C  CG    . LYS   A 1  311 ? -23.796 70.807  -84.030  1.00 52.67  ? 311 LYS   A CG    1 
ATOM   2442  C  CD    . LYS   A 1  311 ? -22.609 70.704  -84.990  1.00 65.44  ? 311 LYS   A CD    1 
ATOM   2443  C  CE    . LYS   A 1  311 ? -21.300 70.228  -84.298  1.00 77.27  ? 311 LYS   A CE    1 
ATOM   2444  N  NZ    . LYS   A 1  311 ? -21.112 68.733  -84.115  1.00 79.69  ? 311 LYS   A NZ    1 
ATOM   2445  N  N     . TYR   A 1  312 ? -23.397 74.913  -82.240  1.00 43.62  ? 312 TYR   A N     1 
ATOM   2446  C  CA    . TYR   A 1  312 ? -23.901 76.123  -81.607  1.00 35.89  ? 312 TYR   A CA    1 
ATOM   2447  C  C     . TYR   A 1  312 ? -25.341 76.356  -82.047  1.00 40.48  ? 312 TYR   A C     1 
ATOM   2448  O  O     . TYR   A 1  312 ? -25.744 75.967  -83.148  1.00 40.72  ? 312 TYR   A O     1 
ATOM   2449  C  CB    . TYR   A 1  312 ? -23.067 77.351  -81.991  1.00 36.37  ? 312 TYR   A CB    1 
ATOM   2450  C  CG    . TYR   A 1  312 ? -21.741 77.490  -81.315  1.00 35.80  ? 312 TYR   A CG    1 
ATOM   2451  C  CD1   . TYR   A 1  312 ? -20.595 76.897  -81.839  1.00 36.36  ? 312 TYR   A CD1   1 
ATOM   2452  C  CD2   . TYR   A 1  312 ? -21.620 78.253  -80.154  1.00 42.90  ? 312 TYR   A CD2   1 
ATOM   2453  C  CE1   . TYR   A 1  312 ? -19.362 77.032  -81.203  1.00 29.38  ? 312 TYR   A CE1   1 
ATOM   2454  C  CE2   . TYR   A 1  312 ? -20.394 78.400  -79.515  1.00 39.28  ? 312 TYR   A CE2   1 
ATOM   2455  C  CZ    . TYR   A 1  312 ? -19.276 77.787  -80.044  1.00 38.83  ? 312 TYR   A CZ    1 
ATOM   2456  O  OH    . TYR   A 1  312 ? -18.079 77.944  -79.385  1.00 55.59  ? 312 TYR   A OH    1 
ATOM   2457  N  N     . MET   A 1  313 ? -26.107 77.006  -81.178  1.00 36.26  ? 313 MET   A N     1 
ATOM   2458  C  CA    . MET   A 1  313 ? -27.462 77.445  -81.481  1.00 38.05  ? 313 MET   A CA    1 
ATOM   2459  C  C     . MET   A 1  313 ? -27.631 78.938  -81.303  1.00 35.46  ? 313 MET   A C     1 
ATOM   2460  O  O     . MET   A 1  313 ? -28.673 79.475  -81.675  1.00 51.47  ? 313 MET   A O     1 
ATOM   2461  C  CB    . MET   A 1  313 ? -28.494 76.744  -80.578  1.00 34.48  ? 313 MET   A CB    1 
ATOM   2462  C  CG    . MET   A 1  313 ? -28.654 75.263  -80.823  1.00 43.22  ? 313 MET   A CG    1 
ATOM   2463  S  SD    . MET   A 1  313 ? -29.525 74.449  -79.455  1.00 39.88  ? 313 MET   A SD    1 
ATOM   2464  C  CE    . MET   A 1  313 ? -28.156 74.291  -78.309  1.00 47.27  ? 313 MET   A CE    1 
ATOM   2465  N  N     . ALA   A 1  314 ? -26.655 79.611  -80.714  1.00 37.21  ? 314 ALA   A N     1 
ATOM   2466  C  CA    . ALA   A 1  314 ? -26.776 81.025  -80.417  1.00 39.96  ? 314 ALA   A CA    1 
ATOM   2467  C  C     . ALA   A 1  314 ? -25.482 81.544  -79.804  1.00 39.75  ? 314 ALA   A C     1 
ATOM   2468  O  O     . ALA   A 1  314 ? -24.745 80.798  -79.157  1.00 41.67  ? 314 ALA   A O     1 
ATOM   2469  C  CB    . ALA   A 1  314 ? -27.962 81.266  -79.484  1.00 38.02  ? 314 ALA   A CB    1 
ATOM   2470  N  N     . CYS   A 1  315 ? -25.188 82.818  -79.994  1.00 36.17  ? 315 CYS   A N     1 
ATOM   2471  C  CA    A CYS   A 1  315 ? -23.969 83.388  -79.446  0.57 34.63  ? 315 CYS   A CA    1 
ATOM   2472  C  CA    B CYS   A 1  315 ? -23.978 83.388  -79.434  0.43 34.70  ? 315 CYS   A CA    1 
ATOM   2473  C  C     . CYS   A 1  315 ? -24.214 84.863  -79.183  1.00 36.24  ? 315 CYS   A C     1 
ATOM   2474  O  O     . CYS   A 1  315 ? -24.785 85.554  -80.022  1.00 41.63  ? 315 CYS   A O     1 
ATOM   2475  C  CB    A CYS   A 1  315 ? -22.787 83.192  -80.404  0.57 40.04  ? 315 CYS   A CB    1 
ATOM   2476  C  CB    B CYS   A 1  315 ? -22.779 83.189  -80.362  0.43 39.99  ? 315 CYS   A CB    1 
ATOM   2477  S  SG    A CYS   A 1  315 ? -21.181 82.884  -79.614  0.57 36.70  ? 315 CYS   A SG    1 
ATOM   2478  S  SG    B CYS   A 1  315 ? -22.350 81.464  -80.620  0.43 37.61  ? 315 CYS   A SG    1 
ATOM   2479  N  N     . CYS   A 1  316 ? -23.786 85.323  -78.020  1.00 38.64  ? 316 CYS   A N     1 
ATOM   2480  C  CA    A CYS   A 1  316 ? -23.933 86.702  -77.585  0.67 33.24  ? 316 CYS   A CA    1 
ATOM   2481  C  CA    B CYS   A 1  316 ? -23.929 86.708  -77.617  0.33 33.43  ? 316 CYS   A CA    1 
ATOM   2482  C  C     . CYS   A 1  316 ? -22.583 87.196  -77.108  1.00 38.60  ? 316 CYS   A C     1 
ATOM   2483  O  O     . CYS   A 1  316 ? -21.935 86.523  -76.302  1.00 42.59  ? 316 CYS   A O     1 
ATOM   2484  C  CB    A CYS   A 1  316 ? -24.932 86.812  -76.442  0.67 35.75  ? 316 CYS   A CB    1 
ATOM   2485  C  CB    B CYS   A 1  316 ? -25.006 86.851  -76.541  0.33 35.79  ? 316 CYS   A CB    1 
ATOM   2486  S  SG    A CYS   A 1  316 ? -26.512 87.425  -76.904  0.67 41.45  ? 316 CYS   A SG    1 
ATOM   2487  S  SG    B CYS   A 1  316 ? -25.215 88.520  -75.925  0.33 38.38  ? 316 CYS   A SG    1 
ATOM   2488  N  N     . LEU   A 1  317 ? -22.157 88.354  -77.590  1.00 44.37  ? 317 LEU   A N     1 
ATOM   2489  C  CA    . LEU   A 1  317 ? -20.896 88.953  -77.165  1.00 38.00  ? 317 LEU   A CA    1 
ATOM   2490  C  C     . LEU   A 1  317 ? -21.208 90.218  -76.377  1.00 36.21  ? 317 LEU   A C     1 
ATOM   2491  O  O     . LEU   A 1  317 ? -21.885 91.123  -76.884  1.00 35.55  ? 317 LEU   A O     1 
ATOM   2492  C  CB    . LEU   A 1  317 ? -19.994 89.236  -78.369  1.00 31.39  ? 317 LEU   A CB    1 
ATOM   2493  C  CG    . LEU   A 1  317 ? -19.328 87.965  -78.901  1.00 37.51  ? 317 LEU   A CG    1 
ATOM   2494  C  CD1   . LEU   A 1  317 ? -18.958 88.099  -80.369  1.00 43.15  ? 317 LEU   A CD1   1 
ATOM   2495  C  CD2   . LEU   A 1  317 ? -18.083 87.633  -78.075  1.00 30.28  ? 317 LEU   A CD2   1 
ATOM   2496  N  N     . LEU   A 1  318 ? -20.734 90.272  -75.134  1.00 28.82  ? 318 LEU   A N     1 
ATOM   2497  C  CA    . LEU   A 1  318 ? -21.067 91.360  -74.221  1.00 33.56  ? 318 LEU   A CA    1 
ATOM   2498  C  C     . LEU   A 1  318 ? -19.774 92.057  -73.845  1.00 33.49  ? 318 LEU   A C     1 
ATOM   2499  O  O     . LEU   A 1  318 ? -18.992 91.528  -73.048  1.00 33.51  ? 318 LEU   A O     1 
ATOM   2500  C  CB    . LEU   A 1  318 ? -21.803 90.846  -72.980  1.00 33.11  ? 318 LEU   A CB    1 
ATOM   2501  C  CG    . LEU   A 1  318 ? -23.130 90.135  -73.269  1.00 33.02  ? 318 LEU   A CG    1 
ATOM   2502  C  CD1   . LEU   A 1  318 ? -23.824 89.717  -71.983  1.00 25.67  ? 318 LEU   A CD1   1 
ATOM   2503  C  CD2   . LEU   A 1  318 ? -24.011 91.032  -74.111  1.00 29.40  ? 318 LEU   A CD2   1 
ATOM   2504  N  N     . TYR   A 1  319 ? -19.553 93.237  -74.413  1.00 33.47  ? 319 TYR   A N     1 
ATOM   2505  C  CA    . TYR   A 1  319 ? -18.307 93.962  -74.220  1.00 30.96  ? 319 TYR   A CA    1 
ATOM   2506  C  C     . TYR   A 1  319 ? -18.482 95.067  -73.203  1.00 32.82  ? 319 TYR   A C     1 
ATOM   2507  O  O     . TYR   A 1  319 ? -19.547 95.680  -73.089  1.00 32.52  ? 319 TYR   A O     1 
ATOM   2508  C  CB    . TYR   A 1  319 ? -17.807 94.566  -75.529  1.00 38.49  ? 319 TYR   A CB    1 
ATOM   2509  C  CG    . TYR   A 1  319 ? -17.251 93.560  -76.510  1.00 36.88  ? 319 TYR   A CG    1 
ATOM   2510  C  CD1   . TYR   A 1  319 ? -15.958 93.078  -76.384  1.00 31.11  ? 319 TYR   A CD1   1 
ATOM   2511  C  CD2   . TYR   A 1  319 ? -18.031 93.097  -77.570  1.00 33.08  ? 319 TYR   A CD2   1 
ATOM   2512  C  CE1   . TYR   A 1  319 ? -15.465 92.162  -77.295  1.00 41.79  ? 319 TYR   A CE1   1 
ATOM   2513  C  CE2   . TYR   A 1  319 ? -17.544 92.191  -78.480  1.00 30.79  ? 319 TYR   A CE2   1 
ATOM   2514  C  CZ    . TYR   A 1  319 ? -16.268 91.729  -78.346  1.00 29.63  ? 319 TYR   A CZ    1 
ATOM   2515  O  OH    . TYR   A 1  319 ? -15.797 90.824  -79.261  1.00 36.39  ? 319 TYR   A OH    1 
ATOM   2516  N  N     . ARG   A 1  320 ? -17.411 95.320  -72.463  1.00 39.18  ? 320 ARG   A N     1 
ATOM   2517  C  CA    . ARG   A 1  320 ? -17.383 96.386  -71.468  1.00 38.53  ? 320 ARG   A CA    1 
ATOM   2518  C  C     . ARG   A 1  320 ? -16.085 97.147  -71.647  1.00 38.60  ? 320 ARG   A C     1 
ATOM   2519  O  O     . ARG   A 1  320 ? -15.001 96.603  -71.407  1.00 34.13  ? 320 ARG   A O     1 
ATOM   2520  C  CB    . ARG   A 1  320 ? -17.498 95.844  -70.045  1.00 37.02  ? 320 ARG   A CB    1 
ATOM   2521  C  CG    . ARG   A 1  320 ? -18.887 95.391  -69.656  1.00 36.04  ? 320 ARG   A CG    1 
ATOM   2522  C  CD    . ARG   A 1  320 ? -18.923 94.967  -68.196  1.00 37.75  ? 320 ARG   A CD    1 
ATOM   2523  N  NE    . ARG   A 1  320 ? -19.716 95.866  -67.371  1.00 35.34  ? 320 ARG   A NE    1 
ATOM   2524  C  CZ    . ARG   A 1  320 ? -20.414 95.485  -66.309  1.00 41.44  ? 320 ARG   A CZ    1 
ATOM   2525  N  NH1   . ARG   A 1  320 ? -20.440 94.223  -65.914  1.00 39.11  ? 320 ARG   A NH1   1 
ATOM   2526  N  NH2   . ARG   A 1  320 ? -21.119 96.389  -65.637  1.00 41.25  ? 320 ARG   A NH2   1 
ATOM   2527  N  N     . GLY   A 1  321 ? -16.203 98.408  -72.067  1.00 44.51  ? 321 GLY   A N     1 
ATOM   2528  C  CA    . GLY   A 1  321 ? -15.076 99.307  -72.158  1.00 43.43  ? 321 GLY   A CA    1 
ATOM   2529  C  C     . GLY   A 1  321 ? -14.832 99.751  -73.592  1.00 46.02  ? 321 GLY   A C     1 
ATOM   2530  O  O     . GLY   A 1  321 ? -15.770 100.003 -74.356  1.00 41.09  ? 321 GLY   A O     1 
ATOM   2531  N  N     . ASP   A 1  322 ? -13.556 99.819  -73.954  1.00 39.08  ? 322 ASP   A N     1 
ATOM   2532  C  CA    . ASP   A 1  322 ? -13.117 100.520 -75.153  1.00 44.24  ? 322 ASP   A CA    1 
ATOM   2533  C  C     . ASP   A 1  322 ? -13.253 99.577  -76.344  1.00 39.48  ? 322 ASP   A C     1 
ATOM   2534  O  O     . ASP   A 1  322 ? -12.307 98.904  -76.757  1.00 41.03  ? 322 ASP   A O     1 
ATOM   2535  C  CB    . ASP   A 1  322 ? -11.689 101.018 -74.953  1.00 46.56  ? 322 ASP   A CB    1 
ATOM   2536  C  CG    . ASP   A 1  322 ? -11.152 101.743 -76.145  1.00 46.58  ? 322 ASP   A CG    1 
ATOM   2537  O  OD1   . ASP   A 1  322 ? -11.891 102.571 -76.712  1.00 57.59  ? 322 ASP   A OD1   1 
ATOM   2538  O  OD2   . ASP   A 1  322 ? -9.984  101.492 -76.505  1.00 47.54  ? 322 ASP   A OD2   1 
ATOM   2539  N  N     . VAL   A 1  323 ? -14.467 99.523  -76.893  1.00 38.41  ? 323 VAL   A N     1 
ATOM   2540  C  CA    . VAL   A 1  323 ? -14.787 98.669  -78.031  1.00 32.22  ? 323 VAL   A CA    1 
ATOM   2541  C  C     . VAL   A 1  323 ? -15.676 99.437  -79.007  1.00 44.48  ? 323 VAL   A C     1 
ATOM   2542  O  O     . VAL   A 1  323 ? -16.584 100.171 -78.594  1.00 39.69  ? 323 VAL   A O     1 
ATOM   2543  C  CB    . VAL   A 1  323 ? -15.484 97.371  -77.573  1.00 41.70  ? 323 VAL   A CB    1 
ATOM   2544  C  CG1   . VAL   A 1  323 ? -15.650 96.379  -78.739  1.00 28.99  ? 323 VAL   A CG1   1 
ATOM   2545  C  CG2   . VAL   A 1  323 ? -14.728 96.750  -76.408  1.00 35.10  ? 323 VAL   A CG2   1 
ATOM   2546  N  N     . VAL   A 1  324 ? -15.395 99.279  -80.303  1.00 46.61  ? 324 VAL   A N     1 
ATOM   2547  C  CA    . VAL   A 1  324 ? -16.286 99.726  -81.376  1.00 41.03  ? 324 VAL   A CA    1 
ATOM   2548  C  C     . VAL   A 1  324 ? -16.457 98.582  -82.367  1.00 41.84  ? 324 VAL   A C     1 
ATOM   2549  O  O     . VAL   A 1  324 ? -15.597 97.688  -82.468  1.00 40.28  ? 324 VAL   A O     1 
ATOM   2550  C  CB    . VAL   A 1  324 ? -15.758 101.004 -82.080  1.00 40.86  ? 324 VAL   A CB    1 
ATOM   2551  C  CG1   . VAL   A 1  324 ? -15.894 102.221 -81.164  1.00 40.08  ? 324 VAL   A CG1   1 
ATOM   2552  C  CG2   . VAL   A 1  324 ? -14.305 100.833 -82.592  1.00 32.01  ? 324 VAL   A CG2   1 
ATOM   2553  N  N     . PRO   A 1  325 ? -17.556 98.591  -83.136  1.00 41.17  ? 325 PRO   A N     1 
ATOM   2554  C  CA    . PRO   A 1  325 ? -17.867 97.416  -83.975  1.00 40.00  ? 325 PRO   A CA    1 
ATOM   2555  C  C     . PRO   A 1  325 ? -16.821 97.081  -85.029  1.00 47.48  ? 325 PRO   A C     1 
ATOM   2556  O  O     . PRO   A 1  325 ? -16.613 95.897  -85.313  1.00 51.62  ? 325 PRO   A O     1 
ATOM   2557  C  CB    . PRO   A 1  325 ? -19.214 97.789  -84.599  1.00 32.16  ? 325 PRO   A CB    1 
ATOM   2558  C  CG    . PRO   A 1  325 ? -19.839 98.722  -83.583  1.00 33.17  ? 325 PRO   A CG    1 
ATOM   2559  C  CD    . PRO   A 1  325 ? -18.681 99.542  -83.081  1.00 31.89  ? 325 PRO   A CD    1 
ATOM   2560  N  N     . LYS   A 1  326 ? -16.163 98.066  -85.641  1.00 49.13  ? 326 LYS   A N     1 
ATOM   2561  C  CA    . LYS   A 1  326 ? -15.159 97.727  -86.646  1.00 49.10  ? 326 LYS   A CA    1 
ATOM   2562  C  C     . LYS   A 1  326 ? -14.115 96.764  -86.078  1.00 50.10  ? 326 LYS   A C     1 
ATOM   2563  O  O     . LYS   A 1  326 ? -13.619 95.875  -86.783  1.00 46.42  ? 326 LYS   A O     1 
ATOM   2564  C  CB    . LYS   A 1  326 ? -14.502 99.002  -87.175  1.00 35.89  ? 326 LYS   A CB    1 
ATOM   2565  C  CG    . LYS   A 1  326 ? -15.328 100.240 -86.852  1.00 61.09  ? 326 LYS   A CG    1 
ATOM   2566  C  CD    . LYS   A 1  326 ? -14.452 101.419 -86.423  1.00 64.09  ? 326 LYS   A CD    1 
ATOM   2567  C  CE    . LYS   A 1  326 ? -15.282 102.503 -85.752  1.00 55.80  ? 326 LYS   A CE    1 
ATOM   2568  N  NZ    . LYS   A 1  326 ? -14.423 103.559 -85.135  1.00 59.68  ? 326 LYS   A NZ    1 
ATOM   2569  N  N     . ASP   A 1  327 ? -13.774 96.911  -84.801  1.00 42.59  ? 327 ASP   A N     1 
ATOM   2570  C  CA    . ASP   A 1  327 ? -12.850 95.956  -84.209  1.00 37.31  ? 327 ASP   A CA    1 
ATOM   2571  C  C     . ASP   A 1  327 ? -13.534 94.619  -83.937  1.00 41.28  ? 327 ASP   A C     1 
ATOM   2572  O  O     . ASP   A 1  327 ? -12.956 93.563  -84.207  1.00 40.56  ? 327 ASP   A O     1 
ATOM   2573  C  CB    . ASP   A 1  327 ? -12.259 96.533  -82.936  1.00 46.86  ? 327 ASP   A CB    1 
ATOM   2574  C  CG    . ASP   A 1  327 ? -11.634 97.885  -83.155  1.00 52.91  ? 327 ASP   A CG    1 
ATOM   2575  O  OD1   . ASP   A 1  327 ? -11.095 98.094  -84.259  1.00 59.76  ? 327 ASP   A OD1   1 
ATOM   2576  O  OD2   . ASP   A 1  327 ? -11.696 98.736  -82.233  1.00 53.03  ? 327 ASP   A OD2   1 
ATOM   2577  N  N     . VAL   A 1  328 ? -14.776 94.638  -83.438  1.00 42.79  ? 328 VAL   A N     1 
ATOM   2578  C  CA    . VAL   A 1  328 ? -15.488 93.387  -83.158  1.00 42.62  ? 328 VAL   A CA    1 
ATOM   2579  C  C     . VAL   A 1  328 ? -15.620 92.544  -84.424  1.00 42.41  ? 328 VAL   A C     1 
ATOM   2580  O  O     . VAL   A 1  328 ? -15.208 91.380  -84.465  1.00 43.72  ? 328 VAL   A O     1 
ATOM   2581  C  CB    . VAL   A 1  328 ? -16.865 93.664  -82.533  1.00 36.17  ? 328 VAL   A CB    1 
ATOM   2582  C  CG1   . VAL   A 1  328 ? -17.615 92.337  -82.304  1.00 35.30  ? 328 VAL   A CG1   1 
ATOM   2583  C  CG2   . VAL   A 1  328 ? -16.707 94.421  -81.247  1.00 33.97  ? 328 VAL   A CG2   1 
ATOM   2584  N  N     . ASN   A 1  329 ? -16.224 93.111  -85.468  1.00 46.19  ? 329 ASN   A N     1 
ATOM   2585  C  CA    . ASN   A 1  329 ? -16.388 92.374  -86.713  1.00 40.17  ? 329 ASN   A CA    1 
ATOM   2586  C  C     . ASN   A 1  329 ? -15.041 91.970  -87.288  1.00 38.57  ? 329 ASN   A C     1 
ATOM   2587  O  O     . ASN   A 1  329 ? -14.870 90.846  -87.758  1.00 38.74  ? 329 ASN   A O     1 
ATOM   2588  C  CB    . ASN   A 1  329 ? -17.177 93.223  -87.701  1.00 41.97  ? 329 ASN   A CB    1 
ATOM   2589  C  CG    . ASN   A 1  329 ? -18.538 93.618  -87.150  1.00 53.13  ? 329 ASN   A CG    1 
ATOM   2590  O  OD1   . ASN   A 1  329 ? -19.183 92.829  -86.463  1.00 66.45  ? 329 ASN   A OD1   1 
ATOM   2591  N  ND2   . ASN   A 1  329 ? -18.974 94.839  -87.433  1.00 50.36  ? 329 ASN   A ND2   1 
ATOM   2592  N  N     . ALA   A 1  330 ? -14.058 92.856  -87.228  1.00 37.44  ? 330 ALA   A N     1 
ATOM   2593  C  CA    . ALA   A 1  330 ? -12.733 92.476  -87.695  1.00 39.48  ? 330 ALA   A CA    1 
ATOM   2594  C  C     . ALA   A 1  330 ? -12.185 91.284  -86.905  1.00 47.75  ? 330 ALA   A C     1 
ATOM   2595  O  O     . ALA   A 1  330 ? -11.584 90.366  -87.482  1.00 48.24  ? 330 ALA   A O     1 
ATOM   2596  C  CB    . ALA   A 1  330 ? -11.796 93.681  -87.607  1.00 34.77  ? 330 ALA   A CB    1 
ATOM   2597  N  N     . ALA   A 1  331 ? -12.386 91.279  -85.583  1.00 34.47  ? 331 ALA   A N     1 
ATOM   2598  C  CA    . ALA   A 1  331 ? -11.939 90.157  -84.761  1.00 40.38  ? 331 ALA   A CA    1 
ATOM   2599  C  C     . ALA   A 1  331 ? -12.644 88.863  -85.149  1.00 46.77  ? 331 ALA   A C     1 
ATOM   2600  O  O     . ALA   A 1  331 ? -12.010 87.804  -85.230  1.00 47.73  ? 331 ALA   A O     1 
ATOM   2601  C  CB    . ALA   A 1  331 ? -12.176 90.465  -83.282  1.00 38.78  ? 331 ALA   A CB    1 
ATOM   2602  N  N     . ILE   A 1  332 ? -13.960 88.928  -85.377  1.00 40.25  ? 332 ILE   A N     1 
ATOM   2603  C  CA    . ILE   A 1  332 ? -14.736 87.740  -85.710  1.00 38.10  ? 332 ILE   A CA    1 
ATOM   2604  C  C     . ILE   A 1  332 ? -14.294 87.166  -87.048  1.00 45.90  ? 332 ILE   A C     1 
ATOM   2605  O  O     . ILE   A 1  332 ? -14.167 85.945  -87.209  1.00 45.17  ? 332 ILE   A O     1 
ATOM   2606  C  CB    . ILE   A 1  332 ? -16.233 88.087  -85.710  1.00 43.67  ? 332 ILE   A CB    1 
ATOM   2607  C  CG1   . ILE   A 1  332 ? -16.727 88.326  -84.285  1.00 30.86  ? 332 ILE   A CG1   1 
ATOM   2608  C  CG2   . ILE   A 1  332 ? -17.043 87.024  -86.440  1.00 34.25  ? 332 ILE   A CG2   1 
ATOM   2609  C  CD1   . ILE   A 1  332 ? -18.026 89.093  -84.275  1.00 41.24  ? 332 ILE   A CD1   1 
ATOM   2610  N  N     . ALA   A 1  333 ? -14.062 88.038  -88.032  1.00 46.05  ? 333 ALA   A N     1 
ATOM   2611  C  CA    . ALA   A 1  333 ? -13.464 87.611  -89.290  1.00 49.14  ? 333 ALA   A CA    1 
ATOM   2612  C  C     . ALA   A 1  333 ? -12.259 86.706  -89.046  1.00 41.01  ? 333 ALA   A C     1 
ATOM   2613  O  O     . ALA   A 1  333 ? -12.239 85.548  -89.467  1.00 55.05  ? 333 ALA   A O     1 
ATOM   2614  C  CB    . ALA   A 1  333 ? -13.065 88.834  -90.119  1.00 51.99  ? 333 ALA   A CB    1 
ATOM   2615  N  N     . THR   A 1  334 ? -11.251 87.216  -88.346  1.00 41.51  ? 334 THR   A N     1 
ATOM   2616  C  CA    . THR   A 1  334 ? -10.041 86.438  -88.111  1.00 51.88  ? 334 THR   A CA    1 
ATOM   2617  C  C     . THR   A 1  334 ? -10.354 85.097  -87.450  1.00 60.33  ? 334 THR   A C     1 
ATOM   2618  O  O     . THR   A 1  334 ? -10.122 84.032  -88.040  1.00 54.62  ? 334 THR   A O     1 
ATOM   2619  C  CB    . THR   A 1  334 ? -9.060  87.244  -87.262  1.00 52.64  ? 334 THR   A CB    1 
ATOM   2620  O  OG1   . THR   A 1  334 ? -8.758  88.465  -87.940  1.00 57.46  ? 334 THR   A OG1   1 
ATOM   2621  C  CG2   . THR   A 1  334 ? -7.767  86.456  -87.037  1.00 54.16  ? 334 THR   A CG2   1 
ATOM   2622  N  N     . ILE   A 1  335 ? -10.873 85.126  -86.212  1.00 60.67  ? 335 ILE   A N     1 
ATOM   2623  C  CA    . ILE   A 1  335 ? -11.087 83.878  -85.475  1.00 57.21  ? 335 ILE   A CA    1 
ATOM   2624  C  C     . ILE   A 1  335 ? -11.994 82.938  -86.256  1.00 56.73  ? 335 ILE   A C     1 
ATOM   2625  O  O     . ILE   A 1  335 ? -11.838 81.712  -86.174  1.00 51.46  ? 335 ILE   A O     1 
ATOM   2626  C  CB    . ILE   A 1  335 ? -11.666 84.122  -84.064  1.00 42.97  ? 335 ILE   A CB    1 
ATOM   2627  C  CG1   . ILE   A 1  335 ? -13.179 83.975  -84.103  1.00 46.73  ? 335 ILE   A CG1   1 
ATOM   2628  C  CG2   . ILE   A 1  335 ? -11.274 85.477  -83.499  1.00 43.69  ? 335 ILE   A CG2   1 
ATOM   2629  C  CD1   . ILE   A 1  335 ? -13.654 82.574  -83.801  1.00 51.05  ? 335 ILE   A CD1   1 
ATOM   2630  N  N     . LYS   A 1  336 ? -12.956 83.484  -87.016  1.00 51.02  ? 336 LYS   A N     1 
ATOM   2631  C  CA    . LYS   A 1  336 ? -13.896 82.627  -87.733  1.00 59.15  ? 336 LYS   A CA    1 
ATOM   2632  C  C     . LYS   A 1  336 ? -13.178 81.628  -88.634  1.00 62.72  ? 336 LYS   A C     1 
ATOM   2633  O  O     . LYS   A 1  336 ? -13.649 80.497  -88.803  1.00 57.23  ? 336 LYS   A O     1 
ATOM   2634  C  CB    . LYS   A 1  336 ? -14.876 83.462  -88.558  1.00 58.81  ? 336 LYS   A CB    1 
ATOM   2635  C  CG    . LYS   A 1  336 ? -15.939 82.605  -89.261  1.00 68.15  ? 336 LYS   A CG    1 
ATOM   2636  C  CD    . LYS   A 1  336 ? -16.705 81.731  -88.257  1.00 59.51  ? 336 LYS   A CD    1 
ATOM   2637  C  CE    . LYS   A 1  336 ? -16.705 80.244  -88.637  1.00 67.51  ? 336 LYS   A CE    1 
ATOM   2638  N  NZ    . LYS   A 1  336 ? -17.747 79.847  -89.628  1.00 65.82  ? 336 LYS   A NZ    1 
ATOM   2639  N  N     . THR   A 1  337 ? -12.034 82.018  -89.207  1.00 62.78  ? 337 THR   A N     1 
ATOM   2640  C  CA    . THR   A 1  337 ? -11.279 81.104  -90.055  1.00 62.28  ? 337 THR   A CA    1 
ATOM   2641  C  C     . THR   A 1  337 ? -10.375 80.164  -89.263  1.00 57.55  ? 337 THR   A C     1 
ATOM   2642  O  O     . THR   A 1  337 ? -10.043 79.086  -89.768  1.00 61.87  ? 337 THR   A O     1 
ATOM   2643  C  CB    . THR   A 1  337 ? -10.428 81.881  -91.068  1.00 57.42  ? 337 THR   A CB    1 
ATOM   2644  O  OG1   . THR   A 1  337 ? -9.253  82.383  -90.415  1.00 56.70  ? 337 THR   A OG1   1 
ATOM   2645  C  CG2   . THR   A 1  337 ? -11.230 83.045  -91.699  1.00 44.35  ? 337 THR   A CG2   1 
ATOM   2646  N  N     . LYS   A 1  338 ? -9.964  80.538  -88.050  1.00 50.46  ? 338 LYS   A N     1 
ATOM   2647  C  CA    . LYS   A 1  338 ? -9.056  79.703  -87.267  1.00 52.10  ? 338 LYS   A CA    1 
ATOM   2648  C  C     . LYS   A 1  338 ? -9.775  78.634  -86.441  1.00 62.13  ? 338 LYS   A C     1 
ATOM   2649  O  O     . LYS   A 1  338 ? -9.319  77.488  -86.390  1.00 53.77  ? 338 LYS   A O     1 
ATOM   2650  C  CB    . LYS   A 1  338 ? -8.214  80.570  -86.334  1.00 46.27  ? 338 LYS   A CB    1 
ATOM   2651  C  CG    . LYS   A 1  338 ? -7.050  81.274  -87.010  1.00 63.39  ? 338 LYS   A CG    1 
ATOM   2652  C  CD    . LYS   A 1  338 ? -7.521  82.377  -87.957  1.00 65.86  ? 338 LYS   A CD    1 
ATOM   2653  C  CE    . LYS   A 1  338 ? -6.337  82.975  -88.694  1.00 70.22  ? 338 LYS   A CE    1 
ATOM   2654  N  NZ    . LYS   A 1  338 ? -5.460  81.899  -89.263  1.00 76.80  ? 338 LYS   A NZ    1 
ATOM   2655  N  N     . ARG   A 1  339 ? -10.881 78.983  -85.791  1.00 56.24  ? 339 ARG   A N     1 
ATOM   2656  C  CA    . ARG   A 1  339 ? -11.556 78.109  -84.847  1.00 48.34  ? 339 ARG   A CA    1 
ATOM   2657  C  C     . ARG   A 1  339 ? -12.609 77.243  -85.536  1.00 56.97  ? 339 ARG   A C     1 
ATOM   2658  O  O     . ARG   A 1  339 ? -13.020 77.498  -86.670  1.00 64.84  ? 339 ARG   A O     1 
ATOM   2659  C  CB    . ARG   A 1  339 ? -12.228 78.933  -83.753  1.00 53.49  ? 339 ARG   A CB    1 
ATOM   2660  C  CG    . ARG   A 1  339 ? -11.319 79.894  -83.035  1.00 44.78  ? 339 ARG   A CG    1 
ATOM   2661  C  CD    . ARG   A 1  339 ? -10.401 79.140  -82.143  1.00 49.92  ? 339 ARG   A CD    1 
ATOM   2662  N  NE    . ARG   A 1  339 ? -9.967  79.970  -81.032  1.00 46.97  ? 339 ARG   A NE    1 
ATOM   2663  C  CZ    . ARG   A 1  339 ? -9.227  79.529  -80.024  1.00 55.66  ? 339 ARG   A CZ    1 
ATOM   2664  N  NH1   . ARG   A 1  339 ? -8.834  78.259  -79.954  1.00 43.06  ? 339 ARG   A NH1   1 
ATOM   2665  N  NH2   . ARG   A 1  339 ? -8.875  80.381  -79.058  1.00 49.21  ? 339 ARG   A NH2   1 
ATOM   2666  N  N     . SER   A 1  340 ? -13.084 76.229  -84.805  1.00 61.65  ? 340 SER   A N     1 
ATOM   2667  C  CA    . SER   A 1  340 ? -14.165 75.349  -85.259  1.00 59.52  ? 340 SER   A CA    1 
ATOM   2668  C  C     . SER   A 1  340 ? -15.466 75.820  -84.624  1.00 49.80  ? 340 SER   A C     1 
ATOM   2669  O  O     . SER   A 1  340 ? -15.782 75.437  -83.496  1.00 51.69  ? 340 SER   A O     1 
ATOM   2670  C  CB    . SER   A 1  340 ? -13.876 73.900  -84.887  1.00 49.89  ? 340 SER   A CB    1 
ATOM   2671  O  OG    . SER   A 1  340 ? -12.632 73.485  -85.412  1.00 53.96  ? 340 SER   A OG    1 
ATOM   2672  N  N     . ILE   A 1  341 ? -16.226 76.640  -85.354  1.00 49.55  ? 341 ILE   A N     1 
ATOM   2673  C  CA    . ILE   A 1  341 ? -17.470 77.217  -84.841  1.00 45.86  ? 341 ILE   A CA    1 
ATOM   2674  C  C     . ILE   A 1  341 ? -18.627 76.835  -85.747  1.00 50.76  ? 341 ILE   A C     1 
ATOM   2675  O  O     . ILE   A 1  341 ? -19.100 77.657  -86.547  1.00 56.89  ? 341 ILE   A O     1 
ATOM   2676  C  CB    . ILE   A 1  341 ? -17.384 78.751  -84.723  1.00 47.05  ? 341 ILE   A CB    1 
ATOM   2677  C  CG1   . ILE   A 1  341 ? -16.270 79.161  -83.779  1.00 39.65  ? 341 ILE   A CG1   1 
ATOM   2678  C  CG2   . ILE   A 1  341 ? -18.710 79.338  -84.238  1.00 42.33  ? 341 ILE   A CG2   1 
ATOM   2679  C  CD1   . ILE   A 1  341 ? -16.024 80.616  -83.828  1.00 45.30  ? 341 ILE   A CD1   1 
ATOM   2680  N  N     . GLN   A 1  342 ? -19.093 75.594  -85.631  1.00 50.33  ? 342 GLN   A N     1 
ATOM   2681  C  CA    . GLN   A 1  342 ? -20.231 75.119  -86.409  1.00 45.55  ? 342 GLN   A CA    1 
ATOM   2682  C  C     . GLN   A 1  342 ? -21.516 75.318  -85.616  1.00 45.07  ? 342 GLN   A C     1 
ATOM   2683  O  O     . GLN   A 1  342 ? -21.639 74.835  -84.481  1.00 41.62  ? 342 GLN   A O     1 
ATOM   2684  C  CB    . GLN   A 1  342 ? -20.066 73.649  -86.791  1.00 48.64  ? 342 GLN   A CB    1 
ATOM   2685  C  CG    . GLN   A 1  342 ? -21.154 73.171  -87.743  1.00 63.42  ? 342 GLN   A CG    1 
ATOM   2686  C  CD    . GLN   A 1  342 ? -20.907 71.772  -88.259  1.00 76.17  ? 342 GLN   A CD    1 
ATOM   2687  O  OE1   . GLN   A 1  342 ? -19.765 71.388  -88.517  1.00 84.68  ? 342 GLN   A OE1   1 
ATOM   2688  N  NE2   . GLN   A 1  342 ? -21.978 70.998  -88.412  1.00 75.79  ? 342 GLN   A NE2   1 
ATOM   2689  N  N     . PHE   A 1  343 ? -22.459 76.044  -86.210  1.00 46.00  ? 343 PHE   A N     1 
ATOM   2690  C  CA    . PHE   A 1  343 ? -23.815 76.148  -85.700  1.00 42.64  ? 343 PHE   A CA    1 
ATOM   2691  C  C     . PHE   A 1  343 ? -24.637 74.994  -86.255  1.00 49.54  ? 343 PHE   A C     1 
ATOM   2692  O  O     . PHE   A 1  343 ? -24.189 74.249  -87.128  1.00 46.14  ? 343 PHE   A O     1 
ATOM   2693  C  CB    . PHE   A 1  343 ? -24.455 77.486  -86.086  1.00 43.79  ? 343 PHE   A CB    1 
ATOM   2694  C  CG    . PHE   A 1  343 ? -23.971 78.669  -85.283  1.00 42.41  ? 343 PHE   A CG    1 
ATOM   2695  C  CD1   . PHE   A 1  343 ? -22.639 79.073  -85.333  1.00 37.26  ? 343 PHE   A CD1   1 
ATOM   2696  C  CD2   . PHE   A 1  343 ? -24.864 79.408  -84.511  1.00 36.44  ? 343 PHE   A CD2   1 
ATOM   2697  C  CE1   . PHE   A 1  343 ? -22.202 80.169  -84.590  1.00 35.47  ? 343 PHE   A CE1   1 
ATOM   2698  C  CE2   . PHE   A 1  343 ? -24.433 80.495  -83.779  1.00 38.01  ? 343 PHE   A CE2   1 
ATOM   2699  C  CZ    . PHE   A 1  343 ? -23.100 80.876  -83.823  1.00 38.10  ? 343 PHE   A CZ    1 
ATOM   2700  N  N     . VAL   A 1  344 ? -25.854 74.841  -85.721  1.00 55.06  ? 344 VAL   A N     1 
ATOM   2701  C  CA    . VAL   A 1  344 ? -26.798 73.842  -86.208  1.00 51.00  ? 344 VAL   A CA    1 
ATOM   2702  C  C     . VAL   A 1  344 ? -27.549 74.418  -87.397  1.00 57.46  ? 344 VAL   A C     1 
ATOM   2703  O  O     . VAL   A 1  344 ? -27.698 75.637  -87.527  1.00 54.37  ? 344 VAL   A O     1 
ATOM   2704  C  CB    . VAL   A 1  344 ? -27.757 73.412  -85.084  1.00 49.55  ? 344 VAL   A CB    1 
ATOM   2705  C  CG1   . VAL   A 1  344 ? -26.958 73.028  -83.879  1.00 59.71  ? 344 VAL   A CG1   1 
ATOM   2706  C  CG2   . VAL   A 1  344 ? -28.717 74.544  -84.720  1.00 57.08  ? 344 VAL   A CG2   1 
ATOM   2707  N  N     . ASP   A 1  345 ? -28.035 73.531  -88.273  1.00 57.25  ? 345 ASP   A N     1 
ATOM   2708  C  CA    . ASP   A 1  345 ? -28.574 73.977  -89.557  1.00 55.48  ? 345 ASP   A CA    1 
ATOM   2709  C  C     . ASP   A 1  345 ? -29.745 74.932  -89.376  1.00 58.03  ? 345 ASP   A C     1 
ATOM   2710  O  O     . ASP   A 1  345 ? -29.843 75.942  -90.076  1.00 67.94  ? 345 ASP   A O     1 
ATOM   2711  C  CB    . ASP   A 1  345 ? -28.992 72.778  -90.400  1.00 52.52  ? 345 ASP   A CB    1 
ATOM   2712  C  CG    . ASP   A 1  345 ? -27.841 71.841  -90.685  1.00 49.07  ? 345 ASP   A CG    1 
ATOM   2713  O  OD1   . ASP   A 1  345 ? -26.686 72.283  -90.570  1.00 43.21  ? 345 ASP   A OD1   1 
ATOM   2714  O  OD2   . ASP   A 1  345 ? -28.091 70.664  -91.031  1.00 65.21  ? 345 ASP   A OD2   1 
ATOM   2715  N  N     . TRP   A 1  346 ? -30.642 74.632  -88.447  1.00 58.25  ? 346 TRP   A N     1 
ATOM   2716  C  CA    . TRP   A 1  346 ? -31.809 75.480  -88.237  1.00 59.57  ? 346 TRP   A CA    1 
ATOM   2717  C  C     . TRP   A 1  346 ? -31.481 76.810  -87.562  1.00 67.33  ? 346 TRP   A C     1 
ATOM   2718  O  O     . TRP   A 1  346 ? -32.387 77.473  -87.051  1.00 66.28  ? 346 TRP   A O     1 
ATOM   2719  C  CB    . TRP   A 1  346 ? -32.855 74.731  -87.406  1.00 57.50  ? 346 TRP   A CB    1 
ATOM   2720  C  CG    . TRP   A 1  346 ? -32.301 74.039  -86.205  1.00 65.48  ? 346 TRP   A CG    1 
ATOM   2721  C  CD1   . TRP   A 1  346 ? -31.601 72.864  -86.182  1.00 65.50  ? 346 TRP   A CD1   1 
ATOM   2722  C  CD2   . TRP   A 1  346 ? -32.404 74.472  -84.841  1.00 71.17  ? 346 TRP   A CD2   1 
ATOM   2723  N  NE1   . TRP   A 1  346 ? -31.259 72.542  -84.888  1.00 63.38  ? 346 TRP   A NE1   1 
ATOM   2724  C  CE2   . TRP   A 1  346 ? -31.743 73.512  -84.046  1.00 73.98  ? 346 TRP   A CE2   1 
ATOM   2725  C  CE3   . TRP   A 1  346 ? -32.986 75.583  -84.214  1.00 68.52  ? 346 TRP   A CE3   1 
ATOM   2726  C  CZ2   . TRP   A 1  346 ? -31.649 73.629  -82.653  1.00 72.71  ? 346 TRP   A CZ2   1 
ATOM   2727  C  CZ3   . TRP   A 1  346 ? -32.895 75.694  -82.827  1.00 71.52  ? 346 TRP   A CZ3   1 
ATOM   2728  C  CH2   . TRP   A 1  346 ? -32.229 74.727  -82.066  1.00 67.34  ? 346 TRP   A CH2   1 
ATOM   2729  N  N     . CYS   A 1  347 ? -30.200 77.209  -87.543  1.00 65.22  ? 347 CYS   A N     1 
ATOM   2730  C  CA    . CYS   A 1  347 ? -29.773 78.463  -86.905  1.00 64.00  ? 347 CYS   A CA    1 
ATOM   2731  C  C     . CYS   A 1  347 ? -28.710 79.119  -87.774  1.00 57.97  ? 347 CYS   A C     1 
ATOM   2732  O  O     . CYS   A 1  347 ? -27.877 78.424  -88.375  1.00 56.31  ? 347 CYS   A O     1 
ATOM   2733  C  CB    . CYS   A 1  347 ? -29.215 78.257  -85.484  1.00 55.08  ? 347 CYS   A CB    1 
ATOM   2734  S  SG    . CYS   A 1  347 ? -30.477 78.024  -84.206  1.00 60.59  ? 347 CYS   A SG    1 
ATOM   2735  N  N     . PRO   A 1  348 ? -28.726 80.439  -87.884  1.00 53.04  ? 348 PRO   A N     1 
ATOM   2736  C  CA    . PRO   A 1  348 ? -27.707 81.104  -88.695  1.00 52.11  ? 348 PRO   A CA    1 
ATOM   2737  C  C     . PRO   A 1  348 ? -26.428 81.253  -87.901  1.00 52.63  ? 348 PRO   A C     1 
ATOM   2738  O  O     . PRO   A 1  348 ? -26.452 81.444  -86.682  1.00 49.21  ? 348 PRO   A O     1 
ATOM   2739  C  CB    . PRO   A 1  348 ? -28.337 82.464  -89.010  1.00 51.80  ? 348 PRO   A CB    1 
ATOM   2740  C  CG    . PRO   A 1  348 ? -29.262 82.706  -87.870  1.00 45.91  ? 348 PRO   A CG    1 
ATOM   2741  C  CD    . PRO   A 1  348 ? -29.776 81.363  -87.428  1.00 49.71  ? 348 PRO   A CD    1 
ATOM   2742  N  N     . THR   A 1  349 ? -25.305 81.122  -88.599  1.00 49.89  ? 349 THR   A N     1 
ATOM   2743  C  CA    . THR   A 1  349 ? -24.020 81.429  -87.993  1.00 44.59  ? 349 THR   A CA    1 
ATOM   2744  C  C     . THR   A 1  349 ? -23.921 82.936  -87.822  1.00 48.06  ? 349 THR   A C     1 
ATOM   2745  O  O     . THR   A 1  349 ? -23.744 83.662  -88.803  1.00 49.15  ? 349 THR   A O     1 
ATOM   2746  C  CB    . THR   A 1  349 ? -22.878 80.913  -88.857  1.00 43.27  ? 349 THR   A CB    1 
ATOM   2747  O  OG1   . THR   A 1  349 ? -23.010 79.500  -89.054  1.00 50.16  ? 349 THR   A OG1   1 
ATOM   2748  C  CG2   . THR   A 1  349 ? -21.540 81.210  -88.183  1.00 45.32  ? 349 THR   A CG2   1 
ATOM   2749  N  N     . GLY   A 1  350 ? -24.025 83.413  -86.587  1.00 47.89  ? 350 GLY   A N     1 
ATOM   2750  C  CA    . GLY   A 1  350 ? -23.878 84.838  -86.335  1.00 51.38  ? 350 GLY   A CA    1 
ATOM   2751  C  C     . GLY   A 1  350 ? -23.760 85.135  -84.856  1.00 40.76  ? 350 GLY   A C     1 
ATOM   2752  O  O     . GLY   A 1  350 ? -23.948 84.263  -84.003  1.00 46.37  ? 350 GLY   A O     1 
ATOM   2753  N  N     . PHE   A 1  351 ? -23.464 86.397  -84.563  1.00 36.59  ? 351 PHE   A N     1 
ATOM   2754  C  CA    . PHE   A 1  351 ? -23.223 86.858  -83.204  1.00 41.61  ? 351 PHE   A CA    1 
ATOM   2755  C  C     . PHE   A 1  351 ? -24.048 88.101  -82.935  1.00 36.15  ? 351 PHE   A C     1 
ATOM   2756  O  O     . PHE   A 1  351 ? -23.949 89.083  -83.671  1.00 41.88  ? 351 PHE   A O     1 
ATOM   2757  C  CB    . PHE   A 1  351 ? -21.739 87.184  -82.972  1.00 36.66  ? 351 PHE   A CB    1 
ATOM   2758  C  CG    . PHE   A 1  351 ? -20.814 86.012  -83.164  1.00 47.15  ? 351 PHE   A CG    1 
ATOM   2759  C  CD1   . PHE   A 1  351 ? -20.370 85.662  -84.421  1.00 51.02  ? 351 PHE   A CD1   1 
ATOM   2760  C  CD2   . PHE   A 1  351 ? -20.380 85.265  -82.079  1.00 47.99  ? 351 PHE   A CD2   1 
ATOM   2761  C  CE1   . PHE   A 1  351 ? -19.523 84.586  -84.595  1.00 46.33  ? 351 PHE   A CE1   1 
ATOM   2762  C  CE2   . PHE   A 1  351 ? -19.534 84.193  -82.254  1.00 44.69  ? 351 PHE   A CE2   1 
ATOM   2763  C  CZ    . PHE   A 1  351 ? -19.109 83.856  -83.515  1.00 39.69  ? 351 PHE   A CZ    1 
ATOM   2764  N  N     . LYS   A 1  352 ? -24.827 88.089  -81.868  1.00 33.07  ? 352 LYS   A N     1 
ATOM   2765  C  CA    . LYS   A 1  352 ? -25.356 89.345  -81.377  1.00 32.45  ? 352 LYS   A CA    1 
ATOM   2766  C  C     . LYS   A 1  352 ? -24.296 89.982  -80.499  1.00 37.92  ? 352 LYS   A C     1 
ATOM   2767  O  O     . LYS   A 1  352 ? -23.597 89.295  -79.750  1.00 36.93  ? 352 LYS   A O     1 
ATOM   2768  C  CB    . LYS   A 1  352 ? -26.656 89.129  -80.621  1.00 33.66  ? 352 LYS   A CB    1 
ATOM   2769  C  CG    . LYS   A 1  352 ? -27.656 88.341  -81.427  1.00 33.12  ? 352 LYS   A CG    1 
ATOM   2770  C  CD    . LYS   A 1  352 ? -28.969 89.060  -81.506  1.00 43.62  ? 352 LYS   A CD    1 
ATOM   2771  C  CE    . LYS   A 1  352 ? -30.047 88.151  -82.072  1.00 46.24  ? 352 LYS   A CE    1 
ATOM   2772  N  NZ    . LYS   A 1  352 ? -30.281 86.967  -81.180  1.00 52.71  ? 352 LYS   A NZ    1 
ATOM   2773  N  N     . VAL   A 1  353 ? -24.140 91.294  -80.631  1.00 39.39  ? 353 VAL   A N     1 
ATOM   2774  C  CA    . VAL   A 1  353 ? -23.044 92.010  -79.996  1.00 35.71  ? 353 VAL   A CA    1 
ATOM   2775  C  C     . VAL   A 1  353 ? -23.599 93.180  -79.193  1.00 37.87  ? 353 VAL   A C     1 
ATOM   2776  O  O     . VAL   A 1  353 ? -24.466 93.919  -79.675  1.00 38.33  ? 353 VAL   A O     1 
ATOM   2777  C  CB    . VAL   A 1  353 ? -22.012 92.488  -81.035  1.00 33.75  ? 353 VAL   A CB    1 
ATOM   2778  C  CG1   . VAL   A 1  353 ? -20.877 93.243  -80.348  1.00 35.24  ? 353 VAL   A CG1   1 
ATOM   2779  C  CG2   . VAL   A 1  353 ? -21.469 91.295  -81.786  1.00 41.04  ? 353 VAL   A CG2   1 
ATOM   2780  N  N     . GLY   A 1  354 ? -23.107 93.329  -77.962  1.00 37.87  ? 354 GLY   A N     1 
ATOM   2781  C  CA    . GLY   A 1  354 ? -23.452 94.425  -77.078  1.00 23.88  ? 354 GLY   A CA    1 
ATOM   2782  C  C     . GLY   A 1  354 ? -22.209 95.038  -76.476  1.00 30.43  ? 354 GLY   A C     1 
ATOM   2783  O  O     . GLY   A 1  354 ? -21.324 94.324  -75.995  1.00 32.61  ? 354 GLY   A O     1 
ATOM   2784  N  N     . ILE   A 1  355 ? -22.116 96.363  -76.520  1.00 42.91  ? 355 ILE   A N     1 
ATOM   2785  C  CA    . ILE   A 1  355 ? -20.965 97.106  -76.023  1.00 40.70  ? 355 ILE   A CA    1 
ATOM   2786  C  C     . ILE   A 1  355 ? -21.451 98.124  -75.014  1.00 36.64  ? 355 ILE   A C     1 
ATOM   2787  O  O     . ILE   A 1  355 ? -22.268 98.989  -75.347  1.00 42.89  ? 355 ILE   A O     1 
ATOM   2788  C  CB    . ILE   A 1  355 ? -20.207 97.825  -77.150  1.00 44.08  ? 355 ILE   A CB    1 
ATOM   2789  C  CG1   . ILE   A 1  355 ? -19.709 96.822  -78.201  1.00 39.12  ? 355 ILE   A CG1   1 
ATOM   2790  C  CG2   . ILE   A 1  355 ? -19.077 98.668  -76.546  1.00 29.36  ? 355 ILE   A CG2   1 
ATOM   2791  C  CD1   . ILE   A 1  355 ? -19.050 97.467  -79.432  1.00 34.73  ? 355 ILE   A CD1   1 
ATOM   2792  N  N     . ASN   A 1  356 ? -20.925 98.048  -73.801  1.00 44.18  ? 356 ASN   A N     1 
ATOM   2793  C  CA    . ASN   A 1  356 ? -21.042 99.107  -72.806  1.00 45.71  ? 356 ASN   A CA    1 
ATOM   2794  C  C     . ASN   A 1  356 ? -19.679 99.780  -72.695  1.00 45.87  ? 356 ASN   A C     1 
ATOM   2795  O  O     . ASN   A 1  356 ? -18.676 99.102  -72.442  1.00 40.67  ? 356 ASN   A O     1 
ATOM   2796  C  CB    . ASN   A 1  356 ? -21.476 98.545  -71.454  1.00 44.16  ? 356 ASN   A CB    1 
ATOM   2797  C  CG    . ASN   A 1  356 ? -22.629 99.306  -70.845  1.00 58.48  ? 356 ASN   A CG    1 
ATOM   2798  O  OD1   . ASN   A 1  356 ? -22.508 100.491 -70.500  1.00 50.96  ? 356 ASN   A OD1   1 
ATOM   2799  N  ND2   . ASN   A 1  356 ? -23.759 98.621  -70.686  1.00 62.19  ? 356 ASN   A ND2   1 
ATOM   2800  N  N     . TYR   A 1  357 ? -19.639 101.101 -72.898  1.00 48.33  ? 357 TYR   A N     1 
ATOM   2801  C  CA    . TYR   A 1  357 ? -18.353 101.794 -72.951  1.00 50.24  ? 357 TYR   A CA    1 
ATOM   2802  C  C     . TYR   A 1  357 ? -17.657 101.836 -71.601  1.00 49.11  ? 357 TYR   A C     1 
ATOM   2803  O  O     . TYR   A 1  357 ? -16.427 101.958 -71.566  1.00 51.80  ? 357 TYR   A O     1 
ATOM   2804  C  CB    . TYR   A 1  357 ? -18.514 103.227 -73.473  1.00 48.17  ? 357 TYR   A CB    1 
ATOM   2805  C  CG    . TYR   A 1  357 ? -19.013 103.335 -74.896  1.00 56.96  ? 357 TYR   A CG    1 
ATOM   2806  C  CD1   . TYR   A 1  357 ? -18.410 102.618 -75.922  1.00 53.04  ? 357 TYR   A CD1   1 
ATOM   2807  C  CD2   . TYR   A 1  357 ? -20.096 104.156 -75.216  1.00 53.63  ? 357 TYR   A CD2   1 
ATOM   2808  C  CE1   . TYR   A 1  357 ? -18.874 102.710 -77.229  1.00 55.31  ? 357 TYR   A CE1   1 
ATOM   2809  C  CE2   . TYR   A 1  357 ? -20.565 104.250 -76.514  1.00 55.52  ? 357 TYR   A CE2   1 
ATOM   2810  C  CZ    . TYR   A 1  357 ? -19.953 103.525 -77.516  1.00 55.93  ? 357 TYR   A CZ    1 
ATOM   2811  O  OH    . TYR   A 1  357 ? -20.412 103.619 -78.808  1.00 54.75  ? 357 TYR   A OH    1 
ATOM   2812  N  N     . GLN   A 1  358 ? -18.401 101.742 -70.502  1.00 46.49  ? 358 GLN   A N     1 
ATOM   2813  C  CA    . GLN   A 1  358 ? -17.808 101.816 -69.157  1.00 56.58  ? 358 GLN   A CA    1 
ATOM   2814  C  C     . GLN   A 1  358 ? -17.025 100.540 -68.847  1.00 50.82  ? 358 GLN   A C     1 
ATOM   2815  O  O     . GLN   A 1  358 ? -17.621 99.453  -68.792  1.00 47.21  ? 358 GLN   A O     1 
ATOM   2816  C  CB    . GLN   A 1  358 ? -18.911 102.052 -68.122  1.00 52.46  ? 358 GLN   A CB    1 
ATOM   2817  C  CG    . GLN   A 1  358 ? -18.445 102.595 -66.774  1.00 72.40  ? 358 GLN   A CG    1 
ATOM   2818  C  CD    . GLN   A 1  358 ? -19.617 103.098 -65.897  1.00 94.45  ? 358 GLN   A CD    1 
ATOM   2819  O  OE1   . GLN   A 1  358 ? -20.143 102.369 -65.039  1.00 75.34  ? 358 GLN   A OE1   1 
ATOM   2820  N  NE2   . GLN   A 1  358 ? -20.022 104.352 -66.116  1.00 93.16  ? 358 GLN   A NE2   1 
ATOM   2821  N  N     . PRO   A 1  359 ? -15.709 100.610 -68.660  1.00 48.73  ? 359 PRO   A N     1 
ATOM   2822  C  CA    . PRO   A 1  359 ? -14.914 99.382  -68.445  1.00 43.04  ? 359 PRO   A CA    1 
ATOM   2823  C  C     . PRO   A 1  359 ? -15.328 98.675  -67.168  1.00 43.26  ? 359 PRO   A C     1 
ATOM   2824  O  O     . PRO   A 1  359 ? -16.008 99.269  -66.315  1.00 53.31  ? 359 PRO   A O     1 
ATOM   2825  C  CB    . PRO   A 1  359 ? -13.465 99.897  -68.360  1.00 44.07  ? 359 PRO   A CB    1 
ATOM   2826  C  CG    . PRO   A 1  359 ? -13.567 101.378 -68.161  1.00 40.27  ? 359 PRO   A CG    1 
ATOM   2827  C  CD    . PRO   A 1  359 ? -14.873 101.821 -68.739  1.00 49.86  ? 359 PRO   A CD    1 
ATOM   2828  N  N     . PRO   A 1  360 ? -14.948 97.406  -66.996  1.00 47.30  ? 360 PRO   A N     1 
ATOM   2829  C  CA    . PRO   A 1  360 ? -15.388 96.668  -65.801  1.00 41.05  ? 360 PRO   A CA    1 
ATOM   2830  C  C     . PRO   A 1  360 ? -14.967 97.387  -64.529  1.00 41.75  ? 360 PRO   A C     1 
ATOM   2831  O  O     . PRO   A 1  360 ? -13.834 97.851  -64.408  1.00 45.53  ? 360 PRO   A O     1 
ATOM   2832  C  CB    . PRO   A 1  360 ? -14.694 95.305  -65.941  1.00 35.43  ? 360 PRO   A CB    1 
ATOM   2833  C  CG    . PRO   A 1  360 ? -14.367 95.189  -67.412  1.00 42.41  ? 360 PRO   A CG    1 
ATOM   2834  C  CD    . PRO   A 1  360 ? -14.066 96.593  -67.858  1.00 42.84  ? 360 PRO   A CD    1 
ATOM   2835  N  N     . THR   A 1  361 ? -15.904 97.493  -63.587  1.00 41.21  ? 361 THR   A N     1 
ATOM   2836  C  CA    . THR   A 1  361 ? -15.627 98.034  -62.267  1.00 34.29  ? 361 THR   A CA    1 
ATOM   2837  C  C     . THR   A 1  361 ? -14.861 97.013  -61.436  1.00 54.20  ? 361 THR   A C     1 
ATOM   2838  O  O     . THR   A 1  361 ? -15.263 95.847  -61.338  1.00 52.09  ? 361 THR   A O     1 
ATOM   2839  C  CB    . THR   A 1  361 ? -16.928 98.394  -61.556  1.00 50.58  ? 361 THR   A CB    1 
ATOM   2840  O  OG1   . THR   A 1  361 ? -17.599 99.453  -62.262  1.00 48.66  ? 361 THR   A OG1   1 
ATOM   2841  C  CG2   . THR   A 1  361 ? -16.636 98.796  -60.105  1.00 47.71  ? 361 THR   A CG2   1 
ATOM   2842  N  N     . VAL   A 1  362 ? -13.772 97.446  -60.824  1.00 52.55  ? 362 VAL   A N     1 
ATOM   2843  C  CA    . VAL   A 1  362 ? -12.979 96.564  -59.979  1.00 56.86  ? 362 VAL   A CA    1 
ATOM   2844  C  C     . VAL   A 1  362 ? -13.371 96.817  -58.532  1.00 58.92  ? 362 VAL   A C     1 
ATOM   2845  O  O     . VAL   A 1  362 ? -13.583 97.969  -58.125  1.00 57.08  ? 362 VAL   A O     1 
ATOM   2846  C  CB    . VAL   A 1  362 ? -11.470 96.785  -60.201  1.00 56.00  ? 362 VAL   A CB    1 
ATOM   2847  C  CG1   . VAL   A 1  362 ? -10.921 97.804  -59.213  1.00 50.80  ? 362 VAL   A CG1   1 
ATOM   2848  C  CG2   . VAL   A 1  362 ? -10.717 95.474  -60.113  1.00 56.34  ? 362 VAL   A CG2   1 
ATOM   2849  N  N     . VAL   A 1  363 ? -13.493 95.742  -57.759  1.00 55.58  ? 363 VAL   A N     1 
ATOM   2850  C  CA    . VAL   A 1  363 ? -13.697 95.856  -56.317  1.00 54.83  ? 363 VAL   A CA    1 
ATOM   2851  C  C     . VAL   A 1  363 ? -12.370 96.257  -55.694  1.00 53.78  ? 363 VAL   A C     1 
ATOM   2852  O  O     . VAL   A 1  363 ? -11.433 95.446  -55.678  1.00 53.64  ? 363 VAL   A O     1 
ATOM   2853  C  CB    . VAL   A 1  363 ? -14.215 94.545  -55.707  1.00 58.65  ? 363 VAL   A CB    1 
ATOM   2854  C  CG1   . VAL   A 1  363 ? -13.902 94.495  -54.220  1.00 53.94  ? 363 VAL   A CG1   1 
ATOM   2855  C  CG2   . VAL   A 1  363 ? -15.710 94.415  -55.938  1.00 58.32  ? 363 VAL   A CG2   1 
ATOM   2856  N  N     . PRO   A 1  364 ? -12.233 97.483  -55.194  1.00 62.12  ? 364 PRO   A N     1 
ATOM   2857  C  CA    . PRO   A 1  364 ? -10.942 97.909  -54.644  1.00 57.77  ? 364 PRO   A CA    1 
ATOM   2858  C  C     . PRO   A 1  364 ? -10.457 96.910  -53.609  1.00 59.74  ? 364 PRO   A C     1 
ATOM   2859  O  O     . PRO   A 1  364 ? -11.191 96.536  -52.692  1.00 48.11  ? 364 PRO   A O     1 
ATOM   2860  C  CB    . PRO   A 1  364 ? -11.256 99.276  -54.027  1.00 49.35  ? 364 PRO   A CB    1 
ATOM   2861  C  CG    . PRO   A 1  364 ? -12.388 99.792  -54.857  1.00 48.65  ? 364 PRO   A CG    1 
ATOM   2862  C  CD    . PRO   A 1  364 ? -13.231 98.569  -55.158  1.00 55.16  ? 364 PRO   A CD    1 
ATOM   2863  N  N     . GLY   A 1  365 ? -9.217  96.444  -53.789  1.00 60.82  ? 365 GLY   A N     1 
ATOM   2864  C  CA    . GLY   A 1  365 ? -8.607  95.463  -52.914  1.00 57.13  ? 365 GLY   A CA    1 
ATOM   2865  C  C     . GLY   A 1  365 ? -8.706  94.024  -53.391  1.00 67.50  ? 365 GLY   A C     1 
ATOM   2866  O  O     . GLY   A 1  365 ? -7.952  93.171  -52.906  1.00 77.63  ? 365 GLY   A O     1 
ATOM   2867  N  N     . GLY   A 1  366 ? -9.611  93.729  -54.316  1.00 63.40  ? 366 GLY   A N     1 
ATOM   2868  C  CA    . GLY   A 1  366 ? -9.753  92.380  -54.804  1.00 54.99  ? 366 GLY   A CA    1 
ATOM   2869  C  C     . GLY   A 1  366 ? -8.541  91.949  -55.603  1.00 45.31  ? 366 GLY   A C     1 
ATOM   2870  O  O     . GLY   A 1  366 ? -7.502  92.608  -55.651  1.00 45.64  ? 366 GLY   A O     1 
ATOM   2871  N  N     . ASP   A 1  367 ? -8.702  90.807  -56.262  1.00 48.27  ? 367 ASP   A N     1 
ATOM   2872  C  CA    . ASP   A 1  367 ? -7.618  90.176  -57.006  1.00 46.32  ? 367 ASP   A CA    1 
ATOM   2873  C  C     . ASP   A 1  367 ? -7.562  90.608  -58.464  1.00 47.52  ? 367 ASP   A C     1 
ATOM   2874  O  O     . ASP   A 1  367 ? -6.513  90.455  -59.096  1.00 45.30  ? 367 ASP   A O     1 
ATOM   2875  C  CB    . ASP   A 1  367 ? -7.764  88.652  -56.948  1.00 42.89  ? 367 ASP   A CB    1 
ATOM   2876  C  CG    . ASP   A 1  367 ? -7.988  88.139  -55.538  1.00 51.18  ? 367 ASP   A CG    1 
ATOM   2877  O  OD1   . ASP   A 1  367 ? -7.009  88.147  -54.766  1.00 51.85  ? 367 ASP   A OD1   1 
ATOM   2878  O  OD2   . ASP   A 1  367 ? -9.137  87.751  -55.203  1.00 44.88  ? 367 ASP   A OD2   1 
ATOM   2879  N  N     . LEU   A 1  368 ? -8.662  91.132  -59.006  1.00 46.29  ? 368 LEU   A N     1 
ATOM   2880  C  CA    . LEU   A 1  368 ? -8.745  91.475  -60.415  1.00 46.57  ? 368 LEU   A CA    1 
ATOM   2881  C  C     . LEU   A 1  368 ? -8.079  92.810  -60.695  1.00 43.48  ? 368 LEU   A C     1 
ATOM   2882  O  O     . LEU   A 1  368 ? -8.264  93.780  -59.960  1.00 40.75  ? 368 LEU   A O     1 
ATOM   2883  C  CB    . LEU   A 1  368 ? -10.205 91.543  -60.867  1.00 44.24  ? 368 LEU   A CB    1 
ATOM   2884  C  CG    . LEU   A 1  368 ? -10.867 90.201  -61.133  1.00 52.24  ? 368 LEU   A CG    1 
ATOM   2885  C  CD1   . LEU   A 1  368 ? -11.882 90.335  -62.250  1.00 51.17  ? 368 LEU   A CD1   1 
ATOM   2886  C  CD2   . LEU   A 1  368 ? -9.809  89.154  -61.466  1.00 51.15  ? 368 LEU   A CD2   1 
ATOM   2887  N  N     . ALA   A 1  369 ? -7.323  92.863  -61.780  1.00 37.79  ? 369 ALA   A N     1 
ATOM   2888  C  CA    . ALA   A 1  369 ? -6.785  94.125  -62.261  1.00 48.79  ? 369 ALA   A CA    1 
ATOM   2889  C  C     . ALA   A 1  369 ? -7.804  94.834  -63.160  1.00 39.26  ? 369 ALA   A C     1 
ATOM   2890  O  O     . ALA   A 1  369 ? -8.566  94.193  -63.885  1.00 54.82  ? 369 ALA   A O     1 
ATOM   2891  C  CB    . ALA   A 1  369 ? -5.466  93.887  -63.003  1.00 39.75  ? 369 ALA   A CB    1 
ATOM   2892  N  N     . LYS   A 1  370 ? -7.832  96.160  -63.086  1.00 45.44  ? 370 LYS   A N     1 
ATOM   2893  C  CA    . LYS   A 1  370 ? -8.617  96.946  -64.028  1.00 47.78  ? 370 LYS   A CA    1 
ATOM   2894  C  C     . LYS   A 1  370 ? -8.051  96.799  -65.439  1.00 47.41  ? 370 LYS   A C     1 
ATOM   2895  O  O     . LYS   A 1  370 ? -6.833  96.772  -65.637  1.00 44.26  ? 370 LYS   A O     1 
ATOM   2896  C  CB    . LYS   A 1  370 ? -8.619  98.417  -63.617  1.00 52.71  ? 370 LYS   A CB    1 
ATOM   2897  C  CG    . LYS   A 1  370 ? -8.530  99.358  -64.808  1.00 59.35  ? 370 LYS   A CG    1 
ATOM   2898  C  CD    . LYS   A 1  370 ? -7.503  100.480 -64.602  1.00 77.01  ? 370 LYS   A CD    1 
ATOM   2899  C  CE    . LYS   A 1  370 ? -7.171  101.213 -65.919  1.00 75.21  ? 370 LYS   A CE    1 
ATOM   2900  N  NZ    . LYS   A 1  370 ? -6.427  102.496 -65.699  1.00 72.12  ? 370 LYS   A NZ    1 
ATOM   2901  N  N     . VAL   A 1  371 ? -8.943  96.697  -66.420  1.00 38.98  ? 371 VAL   A N     1 
ATOM   2902  C  CA    . VAL   A 1  371 ? -8.581  96.488  -67.815  1.00 39.41  ? 371 VAL   A CA    1 
ATOM   2903  C  C     . VAL   A 1  371 ? -9.392  97.467  -68.649  1.00 45.76  ? 371 VAL   A C     1 
ATOM   2904  O  O     . VAL   A 1  371 ? -10.508 97.846  -68.276  1.00 49.88  ? 371 VAL   A O     1 
ATOM   2905  C  CB    . VAL   A 1  371 ? -8.836  95.034  -68.296  1.00 42.73  ? 371 VAL   A CB    1 
ATOM   2906  C  CG1   . VAL   A 1  371 ? -8.248  94.008  -67.339  1.00 30.92  ? 371 VAL   A CG1   1 
ATOM   2907  C  CG2   . VAL   A 1  371 ? -10.313 94.791  -68.494  1.00 34.45  ? 371 VAL   A CG2   1 
ATOM   2908  N  N     . GLN   A 1  372 ? -8.837  97.872  -69.795  1.00 45.65  ? 372 GLN   A N     1 
ATOM   2909  C  CA    A GLN   A 1  372 ? -9.485  98.875  -70.632  0.62 49.64  ? 372 GLN   A CA    1 
ATOM   2910  C  CA    B GLN   A 1  372 ? -9.516  98.885  -70.594  0.38 49.60  ? 372 GLN   A CA    1 
ATOM   2911  C  C     . GLN   A 1  372 ? -10.657 98.319  -71.435  1.00 45.20  ? 372 GLN   A C     1 
ATOM   2912  O  O     . GLN   A 1  372 ? -11.439 99.097  -71.988  1.00 44.11  ? 372 GLN   A O     1 
ATOM   2913  C  CB    A GLN   A 1  372 ? -8.461  99.519  -71.575  0.62 52.75  ? 372 GLN   A CB    1 
ATOM   2914  C  CB    B GLN   A 1  372 ? -8.505  99.638  -71.474  0.38 52.67  ? 372 GLN   A CB    1 
ATOM   2915  C  CG    A GLN   A 1  372 ? -7.302  100.236 -70.877  0.62 51.66  ? 372 GLN   A CG    1 
ATOM   2916  C  CG    B GLN   A 1  372 ? -7.680  98.784  -72.419  0.38 52.94  ? 372 GLN   A CG    1 
ATOM   2917  C  CD    A GLN   A 1  372 ? -7.742  101.414 -70.023  0.62 50.59  ? 372 GLN   A CD    1 
ATOM   2918  C  CD    B GLN   A 1  372 ? -6.351  99.435  -72.794  0.38 52.36  ? 372 GLN   A CD    1 
ATOM   2919  O  OE1   A GLN   A 1  372 ? -8.895  101.842 -70.066  0.62 46.88  ? 372 GLN   A OE1   1 
ATOM   2920  O  OE1   B GLN   A 1  372 ? -5.749  99.100  -73.819  0.38 52.44  ? 372 GLN   A OE1   1 
ATOM   2921  N  NE2   A GLN   A 1  372 ? -6.813  101.946 -69.240  0.62 55.67  ? 372 GLN   A NE2   1 
ATOM   2922  N  NE2   B GLN   A 1  372 ? -5.879  100.345 -71.950  0.38 51.73  ? 372 GLN   A NE2   1 
ATOM   2923  N  N     . ARG   A 1  373 ? -10.807 97.003  -71.513  1.00 45.47  ? 373 ARG   A N     1 
ATOM   2924  C  CA    . ARG   A 1  373 ? -11.947 96.415  -72.201  1.00 42.65  ? 373 ARG   A CA    1 
ATOM   2925  C  C     . ARG   A 1  373 ? -12.057 94.961  -71.758  1.00 37.01  ? 373 ARG   A C     1 
ATOM   2926  O  O     . ARG   A 1  373 ? -11.058 94.331  -71.408  1.00 34.97  ? 373 ARG   A O     1 
ATOM   2927  C  CB    . ARG   A 1  373 ? -11.820 96.538  -73.736  1.00 38.33  ? 373 ARG   A CB    1 
ATOM   2928  C  CG    . ARG   A 1  373 ? -10.557 95.902  -74.336  1.00 33.68  ? 373 ARG   A CG    1 
ATOM   2929  C  CD    . ARG   A 1  373 ? -10.174 96.472  -75.718  1.00 45.76  ? 373 ARG   A CD    1 
ATOM   2930  N  NE    . ARG   A 1  373 ? -9.714  97.859  -75.650  1.00 48.98  ? 373 ARG   A NE    1 
ATOM   2931  C  CZ    . ARG   A 1  373 ? -8.470  98.230  -75.363  1.00 48.41  ? 373 ARG   A CZ    1 
ATOM   2932  N  NH1   . ARG   A 1  373 ? -7.512  97.342  -75.150  1.00 44.07  ? 373 ARG   A NH1   1 
ATOM   2933  N  NH2   . ARG   A 1  373 ? -8.184  99.527  -75.270  1.00 44.20  ? 373 ARG   A NH2   1 
ATOM   2934  N  N     . ALA   A 1  374 ? -13.284 94.439  -71.775  1.00 41.75  ? 374 ALA   A N     1 
ATOM   2935  C  CA    . ALA   A 1  374 ? -13.569 93.109  -71.259  1.00 37.37  ? 374 ALA   A CA    1 
ATOM   2936  C  C     . ALA   A 1  374 ? -14.753 92.543  -72.018  1.00 34.34  ? 374 ALA   A C     1 
ATOM   2937  O  O     . ALA   A 1  374 ? -15.530 93.290  -72.622  1.00 31.80  ? 374 ALA   A O     1 
ATOM   2938  C  CB    . ALA   A 1  374 ? -13.859 93.141  -69.758  1.00 29.74  ? 374 ALA   A CB    1 
ATOM   2939  N  N     . VAL   A 1  375 ? -14.897 91.214  -71.980  1.00 27.50  ? 375 VAL   A N     1 
ATOM   2940  C  CA    . VAL   A 1  375 ? -15.949 90.577  -72.766  1.00 25.25  ? 375 VAL   A CA    1 
ATOM   2941  C  C     . VAL   A 1  375 ? -16.460 89.316  -72.073  1.00 29.19  ? 375 VAL   A C     1 
ATOM   2942  O  O     . VAL   A 1  375 ? -15.687 88.475  -71.597  1.00 28.47  ? 375 VAL   A O     1 
ATOM   2943  C  CB    . VAL   A 1  375 ? -15.460 90.276  -74.199  1.00 28.75  ? 375 VAL   A CB    1 
ATOM   2944  C  CG1   . VAL   A 1  375 ? -14.392 89.189  -74.200  1.00 26.16  ? 375 VAL   A CG1   1 
ATOM   2945  C  CG2   . VAL   A 1  375 ? -16.637 89.916  -75.101  1.00 34.21  ? 375 VAL   A CG2   1 
ATOM   2946  N  N     . CYS   A 1  376 ? -17.778 89.177  -72.025  1.00 28.86  ? 376 CYS   A N     1 
ATOM   2947  C  CA    . CYS   A 1  376 ? -18.399 87.926  -71.631  1.00 31.26  ? 376 CYS   A CA    1 
ATOM   2948  C  C     . CYS   A 1  376 ? -19.192 87.405  -72.822  1.00 34.87  ? 376 CYS   A C     1 
ATOM   2949  O  O     . CYS   A 1  376 ? -20.043 88.117  -73.366  1.00 36.81  ? 376 CYS   A O     1 
ATOM   2950  C  CB    . CYS   A 1  376 ? -19.288 88.090  -70.393  1.00 29.75  ? 376 CYS   A CB    1 
ATOM   2951  S  SG    . CYS   A 1  376 ? -20.001 86.489  -69.862  1.00 29.57  ? 376 CYS   A SG    1 
ATOM   2952  N  N     . MET   A 1  377 ? -18.887 86.182  -73.244  1.00 31.34  ? 377 MET   A N     1 
ATOM   2953  C  CA    . MET   A 1  377 ? -19.624 85.511  -74.301  1.00 33.57  ? 377 MET   A CA    1 
ATOM   2954  C  C     . MET   A 1  377 ? -20.638 84.568  -73.667  1.00 34.73  ? 377 MET   A C     1 
ATOM   2955  O  O     . MET   A 1  377 ? -20.306 83.822  -72.738  1.00 37.71  ? 377 MET   A O     1 
ATOM   2956  C  CB    . MET   A 1  377 ? -18.686 84.738  -75.235  1.00 24.87  ? 377 MET   A CB    1 
ATOM   2957  C  CG    . MET   A 1  377 ? -19.418 84.113  -76.440  1.00 31.48  ? 377 MET   A CG    1 
ATOM   2958  S  SD    . MET   A 1  377 ? -18.332 83.251  -77.622  1.00 37.28  ? 377 MET   A SD    1 
ATOM   2959  C  CE    . MET   A 1  377 ? -17.595 84.686  -78.363  1.00 39.63  ? 377 MET   A CE    1 
ATOM   2960  N  N     . LEU   A 1  378 ? -21.875 84.631  -74.146  1.00 30.68  ? 378 LEU   A N     1 
ATOM   2961  C  CA    . LEU   A 1  378 ? -22.940 83.710  -73.763  1.00 34.33  ? 378 LEU   A CA    1 
ATOM   2962  C  C     . LEU   A 1  378 ? -23.313 82.950  -75.026  1.00 31.05  ? 378 LEU   A C     1 
ATOM   2963  O  O     . LEU   A 1  378 ? -24.054 83.460  -75.867  1.00 41.25  ? 378 LEU   A O     1 
ATOM   2964  C  CB    . LEU   A 1  378 ? -24.148 84.448  -73.172  1.00 37.94  ? 378 LEU   A CB    1 
ATOM   2965  C  CG    . LEU   A 1  378 ? -23.888 85.409  -71.997  1.00 35.46  ? 378 LEU   A CG    1 
ATOM   2966  C  CD1   . LEU   A 1  378 ? -25.191 85.919  -71.464  1.00 34.99  ? 378 LEU   A CD1   1 
ATOM   2967  C  CD2   . LEU   A 1  378 ? -23.068 84.772  -70.880  1.00 22.41  ? 378 LEU   A CD2   1 
ATOM   2968  N  N     . SER   A 1  379 ? -22.772 81.762  -75.183  1.00 22.91  ? 379 SER   A N     1 
ATOM   2969  C  CA    . SER   A 1  379 ? -23.074 80.906  -76.314  1.00 31.04  ? 379 SER   A CA    1 
ATOM   2970  C  C     . SER   A 1  379 ? -23.839 79.682  -75.833  1.00 35.43  ? 379 SER   A C     1 
ATOM   2971  O  O     . SER   A 1  379 ? -23.587 79.171  -74.738  1.00 34.63  ? 379 SER   A O     1 
ATOM   2972  C  CB    . SER   A 1  379 ? -21.797 80.458  -77.018  1.00 31.09  ? 379 SER   A CB    1 
ATOM   2973  O  OG    . SER   A 1  379 ? -21.173 79.437  -76.276  1.00 31.79  ? 379 SER   A OG    1 
ATOM   2974  N  N     . ASN   A 1  380 ? -24.775 79.211  -76.647  1.00 33.49  ? 380 ASN   A N     1 
ATOM   2975  C  CA    . ASN   A 1  380 ? -25.521 77.993  -76.340  1.00 29.26  ? 380 ASN   A CA    1 
ATOM   2976  C  C     . ASN   A 1  380 ? -24.948 76.859  -77.183  1.00 34.85  ? 380 ASN   A C     1 
ATOM   2977  O  O     . ASN   A 1  380 ? -25.377 76.632  -78.315  1.00 35.95  ? 380 ASN   A O     1 
ATOM   2978  C  CB    . ASN   A 1  380 ? -27.002 78.191  -76.609  1.00 29.84  ? 380 ASN   A CB    1 
ATOM   2979  C  CG    . ASN   A 1  380 ? -27.838 77.115  -75.988  1.00 33.99  ? 380 ASN   A CG    1 
ATOM   2980  O  OD1   . ASN   A 1  380 ? -27.398 75.973  -75.873  1.00 31.40  ? 380 ASN   A OD1   1 
ATOM   2981  N  ND2   . ASN   A 1  380 ? -29.051 77.465  -75.573  1.00 35.22  ? 380 ASN   A ND2   1 
ATOM   2982  N  N     . THR   A 1  381 ? -23.964 76.142  -76.636  1.00 35.14  ? 381 THR   A N     1 
ATOM   2983  C  CA    . THR   A 1  381 ? -23.378 74.994  -77.318  1.00 35.49  ? 381 THR   A CA    1 
ATOM   2984  C  C     . THR   A 1  381 ? -23.771 73.686  -76.644  1.00 37.37  ? 381 THR   A C     1 
ATOM   2985  O  O     . THR   A 1  381 ? -23.856 73.604  -75.419  1.00 38.37  ? 381 THR   A O     1 
ATOM   2986  C  CB    . THR   A 1  381 ? -21.852 75.063  -77.380  1.00 36.98  ? 381 THR   A CB    1 
ATOM   2987  O  OG1   . THR   A 1  381 ? -21.334 73.754  -77.706  1.00 35.55  ? 381 THR   A OG1   1 
ATOM   2988  C  CG2   . THR   A 1  381 ? -21.263 75.584  -76.060  1.00 21.47  ? 381 THR   A CG2   1 
ATOM   2989  N  N     . THR   A 1  382 ? -23.998 72.663  -77.464  1.00 41.27  ? 382 THR   A N     1 
ATOM   2990  C  CA    . THR   A 1  382 ? -24.255 71.334  -76.941  1.00 30.81  ? 382 THR   A CA    1 
ATOM   2991  C  C     . THR   A 1  382 ? -23.083 70.805  -76.125  1.00 31.43  ? 382 THR   A C     1 
ATOM   2992  O  O     . THR   A 1  382 ? -23.266 69.874  -75.340  1.00 33.27  ? 382 THR   A O     1 
ATOM   2993  C  CB    . THR   A 1  382 ? -24.584 70.371  -78.098  1.00 39.30  ? 382 THR   A CB    1 
ATOM   2994  O  OG1   . THR   A 1  382 ? -23.564 70.437  -79.106  1.00 40.36  ? 382 THR   A OG1   1 
ATOM   2995  C  CG2   . THR   A 1  382 ? -25.958 70.689  -78.725  1.00 28.79  ? 382 THR   A CG2   1 
ATOM   2996  N  N     . ALA   A 1  383 ? -21.887 71.385  -76.261  1.00 31.89  ? 383 ALA   A N     1 
ATOM   2997  C  CA    . ALA   A 1  383 ? -20.745 70.875  -75.498  1.00 34.46  ? 383 ALA   A CA    1 
ATOM   2998  C  C     . ALA   A 1  383 ? -20.941 70.956  -73.974  1.00 36.13  ? 383 ALA   A C     1 
ATOM   2999  O  O     . ALA   A 1  383 ? -20.280 70.208  -73.231  1.00 25.62  ? 383 ALA   A O     1 
ATOM   3000  C  CB    . ALA   A 1  383 ? -19.467 71.618  -75.901  1.00 30.21  ? 383 ALA   A CB    1 
ATOM   3001  N  N     . ILE   A 1  384 ? -21.823 71.840  -73.485  1.00 30.17  ? 384 ILE   A N     1 
ATOM   3002  C  CA    . ILE   A 1  384 ? -22.014 71.944  -72.043  1.00 31.02  ? 384 ILE   A CA    1 
ATOM   3003  C  C     . ILE   A 1  384 ? -22.643 70.672  -71.481  1.00 32.48  ? 384 ILE   A C     1 
ATOM   3004  O  O     . ILE   A 1  384 ? -22.535 70.413  -70.276  1.00 27.26  ? 384 ILE   A O     1 
ATOM   3005  C  CB    . ILE   A 1  384 ? -22.852 73.183  -71.665  1.00 26.98  ? 384 ILE   A CB    1 
ATOM   3006  C  CG1   . ILE   A 1  384 ? -22.443 73.677  -70.278  1.00 23.09  ? 384 ILE   A CG1   1 
ATOM   3007  C  CG2   . ILE   A 1  384 ? -24.350 72.868  -71.734  1.00 24.76  ? 384 ILE   A CG2   1 
ATOM   3008  C  CD1   . ILE   A 1  384 ? -23.158 74.901  -69.769  1.00 21.41  ? 384 ILE   A CD1   1 
ATOM   3009  N  N     . ALA   A 1  385 ? -23.270 69.853  -72.329  1.00 29.41  ? 385 ALA   A N     1 
ATOM   3010  C  CA    . ALA   A 1  385 ? -23.782 68.568  -71.868  1.00 33.67  ? 385 ALA   A CA    1 
ATOM   3011  C  C     . ALA   A 1  385 ? -22.693 67.735  -71.208  1.00 34.09  ? 385 ALA   A C     1 
ATOM   3012  O  O     . ALA   A 1  385 ? -22.988 66.870  -70.373  1.00 33.06  ? 385 ALA   A O     1 
ATOM   3013  C  CB    . ALA   A 1  385 ? -24.403 67.788  -73.035  1.00 26.36  ? 385 ALA   A CB    1 
ATOM   3014  N  N     . GLU   A 1  386 ? -21.431 67.964  -71.596  1.00 32.29  ? 386 GLU   A N     1 
ATOM   3015  C  CA    . GLU   A 1  386 ? -20.327 67.260  -70.961  1.00 27.05  ? 386 GLU   A CA    1 
ATOM   3016  C  C     . GLU   A 1  386 ? -20.492 67.306  -69.465  1.00 32.09  ? 386 GLU   A C     1 
ATOM   3017  O  O     . GLU   A 1  386 ? -20.310 66.299  -68.771  1.00 29.99  ? 386 GLU   A O     1 
ATOM   3018  C  CB    . GLU   A 1  386 ? -18.994 67.892  -71.365  1.00 30.26  ? 386 GLU   A CB    1 
ATOM   3019  C  CG    . GLU   A 1  386 ? -18.429 67.384  -72.709  1.00 33.11  ? 386 GLU   A CG    1 
ATOM   3020  C  CD    . GLU   A 1  386 ? -17.075 67.990  -73.031  1.00 39.39  ? 386 GLU   A CD    1 
ATOM   3021  O  OE1   . GLU   A 1  386 ? -16.171 67.944  -72.154  1.00 38.29  ? 386 GLU   A OE1   1 
ATOM   3022  O  OE2   . GLU   A 1  386 ? -16.929 68.542  -74.150  1.00 39.26  ? 386 GLU   A OE2   1 
ATOM   3023  N  N     . ALA   A 1  387 ? -20.875 68.471  -68.944  1.00 26.93  ? 387 ALA   A N     1 
ATOM   3024  C  CA    . ALA   A 1  387 ? -21.024 68.603  -67.514  1.00 24.60  ? 387 ALA   A CA    1 
ATOM   3025  C  C     . ALA   A 1  387 ? -22.101 67.660  -67.010  1.00 33.22  ? 387 ALA   A C     1 
ATOM   3026  O  O     . ALA   A 1  387 ? -21.923 67.019  -65.966  1.00 37.66  ? 387 ALA   A O     1 
ATOM   3027  C  CB    . ALA   A 1  387 ? -21.327 70.052  -67.139  1.00 23.13  ? 387 ALA   A CB    1 
ATOM   3028  N  N     . TRP   A 1  388 ? -23.211 67.527  -67.753  1.00 29.39  ? 388 TRP   A N     1 
ATOM   3029  C  CA    . TRP   A 1  388 ? -24.261 66.588  -67.341  1.00 28.07  ? 388 TRP   A CA    1 
ATOM   3030  C  C     . TRP   A 1  388 ? -23.789 65.135  -67.385  1.00 27.71  ? 388 TRP   A C     1 
ATOM   3031  O  O     . TRP   A 1  388 ? -24.207 64.336  -66.542  1.00 39.17  ? 388 TRP   A O     1 
ATOM   3032  C  CB    . TRP   A 1  388 ? -25.516 66.732  -68.204  1.00 30.98  ? 388 TRP   A CB    1 
ATOM   3033  C  CG    . TRP   A 1  388 ? -26.189 68.072  -68.167  1.00 33.39  ? 388 TRP   A CG    1 
ATOM   3034  C  CD1   . TRP   A 1  388 ? -26.585 68.822  -69.249  1.00 27.33  ? 388 TRP   A CD1   1 
ATOM   3035  C  CD2   . TRP   A 1  388 ? -26.562 68.819  -67.007  1.00 24.48  ? 388 TRP   A CD2   1 
ATOM   3036  N  NE1   . TRP   A 1  388 ? -27.176 69.985  -68.827  1.00 25.62  ? 388 TRP   A NE1   1 
ATOM   3037  C  CE2   . TRP   A 1  388 ? -27.173 70.013  -67.458  1.00 32.39  ? 388 TRP   A CE2   1 
ATOM   3038  C  CE3   . TRP   A 1  388 ? -26.449 68.597  -65.638  1.00 26.96  ? 388 TRP   A CE3   1 
ATOM   3039  C  CZ2   . TRP   A 1  388 ? -27.652 70.982  -66.584  1.00 35.81  ? 388 TRP   A CZ2   1 
ATOM   3040  C  CZ3   . TRP   A 1  388 ? -26.925 69.552  -64.771  1.00 34.78  ? 388 TRP   A CZ3   1 
ATOM   3041  C  CH2   . TRP   A 1  388 ? -27.522 70.734  -65.245  1.00 38.62  ? 388 TRP   A CH2   1 
ATOM   3042  N  N     . ALA   A 1  389 ? -22.926 64.771  -68.340  1.00 26.33  ? 389 ALA   A N     1 
ATOM   3043  C  CA    . ALA   A 1  389 ? -22.410 63.403  -68.400  1.00 26.07  ? 389 ALA   A CA    1 
ATOM   3044  C  C     . ALA   A 1  389 ? -21.532 63.066  -67.192  1.00 29.96  ? 389 ALA   A C     1 
ATOM   3045  O  O     . ALA   A 1  389 ? -21.615 61.957  -66.650  1.00 31.34  ? 389 ALA   A O     1 
ATOM   3046  C  CB    . ALA   A 1  389 ? -21.630 63.180  -69.695  1.00 21.51  ? 389 ALA   A CB    1 
ATOM   3047  N  N     . ARG   A 1  390 ? -20.675 63.994  -66.755  1.00 30.92  ? 390 ARG   A N     1 
ATOM   3048  C  CA    . ARG   A 1  390 ? -19.868 63.741  -65.563  1.00 29.93  ? 390 ARG   A CA    1 
ATOM   3049  C  C     . ARG   A 1  390 ? -20.755 63.588  -64.335  1.00 25.91  ? 390 ARG   A C     1 
ATOM   3050  O  O     . ARG   A 1  390 ? -20.614 62.639  -63.562  1.00 26.75  ? 390 ARG   A O     1 
ATOM   3051  C  CB    . ARG   A 1  390 ? -18.852 64.869  -65.340  1.00 30.38  ? 390 ARG   A CB    1 
ATOM   3052  C  CG    . ARG   A 1  390 ? -18.386 65.570  -66.600  1.00 34.48  ? 390 ARG   A CG    1 
ATOM   3053  C  CD    . ARG   A 1  390 ? -17.028 66.223  -66.430  1.00 31.88  ? 390 ARG   A CD    1 
ATOM   3054  N  NE    . ARG   A 1  390 ? -16.964 67.047  -65.233  1.00 36.24  ? 390 ARG   A NE    1 
ATOM   3055  C  CZ    . ARG   A 1  390 ? -17.163 68.356  -65.215  1.00 36.07  ? 390 ARG   A CZ    1 
ATOM   3056  N  NH1   . ARG   A 1  390 ? -17.427 69.038  -66.326  1.00 38.49  ? 390 ARG   A NH1   1 
ATOM   3057  N  NH2   . ARG   A 1  390 ? -17.085 68.996  -64.060  1.00 26.80  ? 390 ARG   A NH2   1 
ATOM   3058  N  N     . LEU   A 1  391 ? -21.673 64.524  -64.138  1.00 24.67  ? 391 LEU   A N     1 
ATOM   3059  C  CA    . LEU   A 1  391 ? -22.521 64.483  -62.958  1.00 26.32  ? 391 LEU   A CA    1 
ATOM   3060  C  C     . LEU   A 1  391 ? -23.407 63.256  -62.989  1.00 32.36  ? 391 LEU   A C     1 
ATOM   3061  O  O     . LEU   A 1  391 ? -23.585 62.591  -61.967  1.00 30.91  ? 391 LEU   A O     1 
ATOM   3062  C  CB    . LEU   A 1  391 ? -23.345 65.768  -62.871  1.00 33.52  ? 391 LEU   A CB    1 
ATOM   3063  C  CG    . LEU   A 1  391 ? -24.148 66.077  -61.612  1.00 39.93  ? 391 LEU   A CG    1 
ATOM   3064  C  CD1   . LEU   A 1  391 ? -23.244 66.244  -60.370  1.00 38.90  ? 391 LEU   A CD1   1 
ATOM   3065  C  CD2   . LEU   A 1  391 ? -24.996 67.341  -61.840  1.00 40.43  ? 391 LEU   A CD2   1 
ATOM   3066  N  N     . ASP   A 1  392 ? -23.904 62.886  -64.175  1.00 31.91  ? 392 ASP   A N     1 
ATOM   3067  C  CA    . ASP   A 1  392 ? -24.728 61.680  -64.277  1.00 36.50  ? 392 ASP   A CA    1 
ATOM   3068  C  C     . ASP   A 1  392 ? -23.924 60.407  -63.977  1.00 32.91  ? 392 ASP   A C     1 
ATOM   3069  O  O     . ASP   A 1  392 ? -24.451 59.459  -63.381  1.00 31.17  ? 392 ASP   A O     1 
ATOM   3070  C  CB    . ASP   A 1  392 ? -25.391 61.611  -65.661  1.00 29.64  ? 392 ASP   A CB    1 
ATOM   3071  C  CG    . ASP   A 1  392 ? -26.575 62.561  -65.789  1.00 35.09  ? 392 ASP   A CG    1 
ATOM   3072  O  OD1   . ASP   A 1  392 ? -27.003 63.131  -64.759  1.00 43.93  ? 392 ASP   A OD1   1 
ATOM   3073  O  OD2   . ASP   A 1  392 ? -27.081 62.751  -66.916  1.00 35.14  ? 392 ASP   A OD2   1 
ATOM   3074  N  N     . HIS   A 1  393 ? -22.655 60.353  -64.382  1.00 27.53  ? 393 HIS   A N     1 
ATOM   3075  C  CA    . HIS   A 1  393 ? -21.825 59.202  -64.034  1.00 29.49  ? 393 HIS   A CA    1 
ATOM   3076  C  C     . HIS   A 1  393 ? -21.644 59.081  -62.512  1.00 36.09  ? 393 HIS   A C     1 
ATOM   3077  O  O     . HIS   A 1  393 ? -21.830 58.004  -61.950  1.00 36.34  ? 393 HIS   A O     1 
ATOM   3078  C  CB    . HIS   A 1  393 ? -20.484 59.320  -64.754  1.00 31.23  ? 393 HIS   A CB    1 
ATOM   3079  C  CG    . HIS   A 1  393 ? -19.541 58.176  -64.532  1.00 32.22  ? 393 HIS   A CG    1 
ATOM   3080  N  ND1   . HIS   A 1  393 ? -19.768 56.910  -65.027  1.00 40.10  ? 393 HIS   A ND1   1 
ATOM   3081  C  CD2   . HIS   A 1  393 ? -18.327 58.128  -63.926  1.00 33.21  ? 393 HIS   A CD2   1 
ATOM   3082  C  CE1   . HIS   A 1  393 ? -18.751 56.125  -64.709  1.00 36.98  ? 393 HIS   A CE1   1 
ATOM   3083  N  NE2   . HIS   A 1  393 ? -17.864 56.840  -64.040  1.00 39.39  ? 393 HIS   A NE2   1 
ATOM   3084  N  N     . LYS   A 1  394 ? -21.293 60.176  -61.821  1.00 26.02  ? 394 LYS   A N     1 
ATOM   3085  C  CA    . LYS   A 1  394 ? -21.112 60.086  -60.374  1.00 27.49  ? 394 LYS   A CA    1 
ATOM   3086  C  C     . LYS   A 1  394 ? -22.370 59.577  -59.696  1.00 35.31  ? 394 LYS   A C     1 
ATOM   3087  O  O     . LYS   A 1  394 ? -22.309 58.711  -58.810  1.00 32.27  ? 394 LYS   A O     1 
ATOM   3088  C  CB    . LYS   A 1  394 ? -20.710 61.444  -59.791  1.00 27.95  ? 394 LYS   A CB    1 
ATOM   3089  C  CG    . LYS   A 1  394 ? -19.329 61.876  -60.261  1.00 28.77  ? 394 LYS   A CG    1 
ATOM   3090  C  CD    . LYS   A 1  394 ? -18.784 63.033  -59.473  1.00 31.31  ? 394 LYS   A CD    1 
ATOM   3091  C  CE    . LYS   A 1  394 ? -17.361 63.309  -59.937  1.00 38.52  ? 394 LYS   A CE    1 
ATOM   3092  N  NZ    . LYS   A 1  394 ? -16.721 62.016  -60.335  1.00 48.79  ? 394 LYS   A NZ    1 
ATOM   3093  N  N     . PHE   A 1  395 ? -23.524 60.109  -60.102  1.00 33.84  ? 395 PHE   A N     1 
ATOM   3094  C  CA    . PHE   A 1  395 ? -24.800 59.625  -59.592  1.00 28.14  ? 395 PHE   A CA    1 
ATOM   3095  C  C     . PHE   A 1  395 ? -24.950 58.114  -59.834  1.00 35.84  ? 395 PHE   A C     1 
ATOM   3096  O  O     . PHE   A 1  395 ? -25.301 57.358  -58.917  1.00 33.32  ? 395 PHE   A O     1 
ATOM   3097  C  CB    . PHE   A 1  395 ? -25.914 60.447  -60.250  1.00 21.61  ? 395 PHE   A CB    1 
ATOM   3098  C  CG    . PHE   A 1  395 ? -27.321 60.057  -59.853  1.00 27.47  ? 395 PHE   A CG    1 
ATOM   3099  C  CD1   . PHE   A 1  395 ? -27.910 58.899  -60.359  1.00 28.19  ? 395 PHE   A CD1   1 
ATOM   3100  C  CD2   . PHE   A 1  395 ? -28.082 60.895  -59.036  1.00 26.02  ? 395 PHE   A CD2   1 
ATOM   3101  C  CE1   . PHE   A 1  395 ? -29.213 58.563  -60.021  1.00 26.16  ? 395 PHE   A CE1   1 
ATOM   3102  C  CE2   . PHE   A 1  395 ? -29.373 60.567  -58.684  1.00 23.23  ? 395 PHE   A CE2   1 
ATOM   3103  C  CZ    . PHE   A 1  395 ? -29.943 59.399  -59.176  1.00 23.75  ? 395 PHE   A CZ    1 
ATOM   3104  N  N     . ASP   A 1  396 ? -24.659 57.646  -61.056  1.00 28.49  ? 396 ASP   A N     1 
ATOM   3105  C  CA    . ASP   A 1  396 ? -24.859 56.228  -61.365  1.00 32.36  ? 396 ASP   A CA    1 
ATOM   3106  C  C     . ASP   A 1  396 ? -24.004 55.340  -60.461  1.00 35.50  ? 396 ASP   A C     1 
ATOM   3107  O  O     . ASP   A 1  396 ? -24.456 54.275  -60.014  1.00 35.96  ? 396 ASP   A O     1 
ATOM   3108  C  CB    . ASP   A 1  396 ? -24.547 55.925  -62.848  1.00 29.66  ? 396 ASP   A CB    1 
ATOM   3109  C  CG    . ASP   A 1  396 ? -25.523 56.603  -63.848  1.00 36.72  ? 396 ASP   A CG    1 
ATOM   3110  O  OD1   . ASP   A 1  396 ? -26.611 57.084  -63.458  1.00 34.03  ? 396 ASP   A OD1   1 
ATOM   3111  O  OD2   . ASP   A 1  396 ? -25.184 56.661  -65.053  1.00 37.07  ? 396 ASP   A OD2   1 
ATOM   3112  N  N     . LEU   A 1  397 ? -22.761 55.764  -60.183  1.00 35.04  ? 397 LEU   A N     1 
ATOM   3113  C  CA    . LEU   A 1  397 ? -21.846 54.967  -59.367  1.00 32.45  ? 397 LEU   A CA    1 
ATOM   3114  C  C     . LEU   A 1  397 ? -22.395 54.782  -57.958  1.00 36.51  ? 397 LEU   A C     1 
ATOM   3115  O  O     . LEU   A 1  397 ? -22.400 53.667  -57.431  1.00 39.04  ? 397 LEU   A O     1 
ATOM   3116  C  CB    . LEU   A 1  397 ? -20.458 55.622  -59.328  1.00 29.81  ? 397 LEU   A CB    1 
ATOM   3117  C  CG    . LEU   A 1  397 ? -19.559 55.449  -60.567  1.00 30.71  ? 397 LEU   A CG    1 
ATOM   3118  C  CD1   . LEU   A 1  397 ? -18.422 56.447  -60.590  1.00 22.30  ? 397 LEU   A CD1   1 
ATOM   3119  C  CD2   . LEU   A 1  397 ? -19.014 54.027  -60.644  1.00 26.81  ? 397 LEU   A CD2   1 
ATOM   3120  N  N     . MET   A 1  398 ? -22.886 55.868  -57.346  1.00 31.77  ? 398 MET   A N     1 
ATOM   3121  C  CA    . MET   A 1  398 ? -23.448 55.797  -56.002  1.00 30.29  ? 398 MET   A CA    1 
ATOM   3122  C  C     . MET   A 1  398 ? -24.796 55.081  -55.997  1.00 31.41  ? 398 MET   A C     1 
ATOM   3123  O  O     . MET   A 1  398 ? -24.976 54.087  -55.290  1.00 28.22  ? 398 MET   A O     1 
ATOM   3124  C  CB    . MET   A 1  398 ? -23.582 57.202  -55.404  1.00 25.84  ? 398 MET   A CB    1 
ATOM   3125  C  CG    . MET   A 1  398 ? -22.289 57.780  -54.876  1.00 30.02  ? 398 MET   A CG    1 
ATOM   3126  S  SD    . MET   A 1  398 ? -22.522 59.267  -53.882  1.00 31.02  ? 398 MET   A SD    1 
ATOM   3127  C  CE    . MET   A 1  398 ? -23.213 60.360  -55.118  1.00 32.19  ? 398 MET   A CE    1 
ATOM   3128  N  N     . TYR   A 1  399 ? -25.753 55.567  -56.794  1.00 35.54  ? 399 TYR   A N     1 
ATOM   3129  C  CA    . TYR   A 1  399 ? -27.118 55.039  -56.750  1.00 31.20  ? 399 TYR   A CA    1 
ATOM   3130  C  C     . TYR   A 1  399 ? -27.183 53.543  -57.059  1.00 24.65  ? 399 TYR   A C     1 
ATOM   3131  O  O     . TYR   A 1  399 ? -28.105 52.868  -56.609  1.00 26.27  ? 399 TYR   A O     1 
ATOM   3132  C  CB    . TYR   A 1  399 ? -28.032 55.808  -57.724  1.00 30.67  ? 399 TYR   A CB    1 
ATOM   3133  C  CG    . TYR   A 1  399 ? -29.493 55.444  -57.557  1.00 34.46  ? 399 TYR   A CG    1 
ATOM   3134  C  CD1   . TYR   A 1  399 ? -30.245 56.007  -56.535  1.00 34.79  ? 399 TYR   A CD1   1 
ATOM   3135  C  CD2   . TYR   A 1  399 ? -30.112 54.506  -58.396  1.00 32.32  ? 399 TYR   A CD2   1 
ATOM   3136  C  CE1   . TYR   A 1  399 ? -31.574 55.665  -56.345  1.00 39.43  ? 399 TYR   A CE1   1 
ATOM   3137  C  CE2   . TYR   A 1  399 ? -31.439 54.157  -58.213  1.00 32.73  ? 399 TYR   A CE2   1 
ATOM   3138  C  CZ    . TYR   A 1  399 ? -32.167 54.744  -57.185  1.00 40.38  ? 399 TYR   A CZ    1 
ATOM   3139  O  OH    . TYR   A 1  399 ? -33.493 54.420  -56.975  1.00 44.21  ? 399 TYR   A OH    1 
ATOM   3140  N  N     . ALA   A 1  400 ? -26.245 53.009  -57.830  1.00 23.72  ? 400 ALA   A N     1 
ATOM   3141  C  CA    . ALA   A 1  400 ? -26.307 51.583  -58.126  1.00 29.18  ? 400 ALA   A CA    1 
ATOM   3142  C  C     . ALA   A 1  400 ? -26.112 50.748  -56.877  1.00 31.10  ? 400 ALA   A C     1 
ATOM   3143  O  O     . ALA   A 1  400 ? -26.408 49.552  -56.888  1.00 39.74  ? 400 ALA   A O     1 
ATOM   3144  C  CB    . ALA   A 1  400 ? -25.259 51.190  -59.182  1.00 17.25  ? 400 ALA   A CB    1 
ATOM   3145  N  N     . LYS   A 1  401 ? -25.597 51.345  -55.818  1.00 26.29  ? 401 LYS   A N     1 
ATOM   3146  C  CA    . LYS   A 1  401 ? -25.459 50.688  -54.533  1.00 28.71  ? 401 LYS   A CA    1 
ATOM   3147  C  C     . LYS   A 1  401 ? -26.368 51.300  -53.481  1.00 30.57  ? 401 LYS   A C     1 
ATOM   3148  O  O     . LYS   A 1  401 ? -26.303 50.922  -52.311  1.00 33.19  ? 401 LYS   A O     1 
ATOM   3149  C  CB    . LYS   A 1  401 ? -24.000 50.754  -54.089  1.00 37.45  ? 401 LYS   A CB    1 
ATOM   3150  C  CG    . LYS   A 1  401 ? -23.048 50.317  -55.187  1.00 34.68  ? 401 LYS   A CG    1 
ATOM   3151  C  CD    . LYS   A 1  401 ? -22.380 49.022  -54.841  1.00 26.16  ? 401 LYS   A CD    1 
ATOM   3152  C  CE    . LYS   A 1  401 ? -21.379 48.661  -55.927  1.00 33.73  ? 401 LYS   A CE    1 
ATOM   3153  N  NZ    . LYS   A 1  401 ? -22.036 48.680  -57.265  1.00 34.08  ? 401 LYS   A NZ    1 
ATOM   3154  N  N     . ARG   A 1  402 ? -27.216 52.238  -53.870  1.00 32.04  ? 402 ARG   A N     1 
ATOM   3155  C  CA    . ARG   A 1  402 ? -28.111 52.903  -52.952  1.00 31.82  ? 402 ARG   A CA    1 
ATOM   3156  C  C     . ARG   A 1  402 ? -27.343 53.622  -51.862  1.00 34.86  ? 402 ARG   A C     1 
ATOM   3157  O  O     . ARG   A 1  402 ? -27.904 53.949  -50.805  1.00 36.76  ? 402 ARG   A O     1 
ATOM   3158  C  CB    . ARG   A 1  402 ? -29.113 51.907  -52.360  1.00 32.62  ? 402 ARG   A CB    1 
ATOM   3159  C  CG    . ARG   A 1  402 ? -30.039 51.293  -53.411  1.00 36.02  ? 402 ARG   A CG    1 
ATOM   3160  C  CD    . ARG   A 1  402 ? -30.723 52.381  -54.221  1.00 44.07  ? 402 ARG   A CD    1 
ATOM   3161  N  NE    . ARG   A 1  402 ? -31.755 51.859  -55.105  1.00 39.16  ? 402 ARG   A NE    1 
ATOM   3162  C  CZ    . ARG   A 1  402 ? -31.530 51.339  -56.301  1.00 36.97  ? 402 ARG   A CZ    1 
ATOM   3163  N  NH1   . ARG   A 1  402 ? -30.311 51.252  -56.798  1.00 34.46  ? 402 ARG   A NH1   1 
ATOM   3164  N  NH2   . ARG   A 1  402 ? -32.557 50.878  -57.009  1.00 41.06  ? 402 ARG   A NH2   1 
ATOM   3165  N  N     . ALA   A 1  403 ? -26.073 53.898  -52.131  1.00 28.05  ? 403 ALA   A N     1 
ATOM   3166  C  CA    . ALA   A 1  403 ? -25.231 54.580  -51.168  1.00 28.97  ? 403 ALA   A CA    1 
ATOM   3167  C  C     . ALA   A 1  403 ? -25.914 55.856  -50.737  1.00 25.30  ? 403 ALA   A C     1 
ATOM   3168  O  O     . ALA   A 1  403 ? -26.325 56.646  -51.581  1.00 28.52  ? 403 ALA   A O     1 
ATOM   3169  C  CB    . ALA   A 1  403 ? -23.861 54.878  -51.784  1.00 27.88  ? 403 ALA   A CB    1 
ATOM   3170  N  N     . PHE   A 1  404 ? -26.072 56.027  -49.416  1.00 26.56  ? 404 PHE   A N     1 
ATOM   3171  C  CA    . PHE   A 1  404 ? -26.654 57.228  -48.812  1.00 27.41  ? 404 PHE   A CA    1 
ATOM   3172  C  C     . PHE   A 1  404 ? -28.144 57.433  -49.067  1.00 27.82  ? 404 PHE   A C     1 
ATOM   3173  O  O     . PHE   A 1  404 ? -28.712 58.379  -48.505  1.00 25.35  ? 404 PHE   A O     1 
ATOM   3174  C  CB    . PHE   A 1  404 ? -25.956 58.494  -49.304  1.00 23.39  ? 404 PHE   A CB    1 
ATOM   3175  C  CG    . PHE   A 1  404 ? -24.526 58.546  -48.960  1.00 29.93  ? 404 PHE   A CG    1 
ATOM   3176  C  CD1   . PHE   A 1  404 ? -24.123 59.010  -47.715  1.00 20.79  ? 404 PHE   A CD1   1 
ATOM   3177  C  CD2   . PHE   A 1  404 ? -23.565 58.131  -49.890  1.00 28.56  ? 404 PHE   A CD2   1 
ATOM   3178  C  CE1   . PHE   A 1  404 ? -22.790 59.064  -47.410  1.00 30.32  ? 404 PHE   A CE1   1 
ATOM   3179  C  CE2   . PHE   A 1  404 ? -22.233 58.170  -49.590  1.00 26.00  ? 404 PHE   A CE2   1 
ATOM   3180  C  CZ    . PHE   A 1  404 ? -21.830 58.642  -48.356  1.00 28.64  ? 404 PHE   A CZ    1 
ATOM   3181  N  N     . VAL   A 1  405 ? -28.769 56.603  -49.922  1.00 23.08  ? 405 VAL   A N     1 
ATOM   3182  C  CA    . VAL   A 1  405 ? -30.167 56.830  -50.310  1.00 22.45  ? 405 VAL   A CA    1 
ATOM   3183  C  C     . VAL   A 1  405 ? -31.084 56.874  -49.091  1.00 31.87  ? 405 VAL   A C     1 
ATOM   3184  O  O     . VAL   A 1  405 ? -32.087 57.610  -49.080  1.00 30.21  ? 405 VAL   A O     1 
ATOM   3185  C  CB    . VAL   A 1  405 ? -30.662 55.755  -51.294  1.00 33.33  ? 405 VAL   A CB    1 
ATOM   3186  C  CG1   . VAL   A 1  405 ? -32.160 55.848  -51.387  1.00 27.99  ? 405 VAL   A CG1   1 
ATOM   3187  C  CG2   . VAL   A 1  405 ? -30.011 55.887  -52.697  1.00 30.80  ? 405 VAL   A CG2   1 
ATOM   3188  N  N     . HIS   A 1  406 ? -30.765 56.093  -48.046  1.00 28.51  ? 406 HIS   A N     1 
ATOM   3189  C  CA    . HIS   A 1  406 ? -31.656 56.010  -46.897  1.00 22.14  ? 406 HIS   A CA    1 
ATOM   3190  C  C     . HIS   A 1  406 ? -31.832 57.365  -46.249  1.00 28.69  ? 406 HIS   A C     1 
ATOM   3191  O  O     . HIS   A 1  406 ? -32.830 57.576  -45.555  1.00 34.55  ? 406 HIS   A O     1 
ATOM   3192  C  CB    . HIS   A 1  406 ? -31.133 54.997  -45.875  1.00 23.24  ? 406 HIS   A CB    1 
ATOM   3193  C  CG    . HIS   A 1  406 ? -29.892 55.448  -45.180  1.00 28.67  ? 406 HIS   A CG    1 
ATOM   3194  N  ND1   . HIS   A 1  406 ? -28.644 55.384  -45.770  1.00 23.99  ? 406 HIS   A ND1   1 
ATOM   3195  C  CD2   . HIS   A 1  406 ? -29.712 56.019  -43.969  1.00 22.41  ? 406 HIS   A CD2   1 
ATOM   3196  C  CE1   . HIS   A 1  406 ? -27.744 55.870  -44.941  1.00 24.93  ? 406 HIS   A CE1   1 
ATOM   3197  N  NE2   . HIS   A 1  406 ? -28.364 56.263  -43.839  1.00 36.59  ? 406 HIS   A NE2   1 
ATOM   3198  N  N     . TRP   A 1  407 ? -30.891 58.288  -46.473  1.00 27.16  ? 407 TRP   A N     1 
ATOM   3199  C  CA    . TRP   A 1  407 ? -31.011 59.630  -45.914  1.00 29.49  ? 407 TRP   A CA    1 
ATOM   3200  C  C     . TRP   A 1  407 ? -32.122 60.405  -46.593  1.00 31.70  ? 407 TRP   A C     1 
ATOM   3201  O  O     . TRP   A 1  407 ? -32.689 61.331  -46.006  1.00 30.00  ? 407 TRP   A O     1 
ATOM   3202  C  CB    . TRP   A 1  407 ? -29.695 60.398  -46.066  1.00 22.58  ? 407 TRP   A CB    1 
ATOM   3203  C  CG    . TRP   A 1  407 ? -28.632 60.036  -45.115  1.00 25.04  ? 407 TRP   A CG    1 
ATOM   3204  C  CD1   . TRP   A 1  407 ? -27.450 59.447  -45.410  1.00 21.07  ? 407 TRP   A CD1   1 
ATOM   3205  C  CD2   . TRP   A 1  407 ? -28.631 60.248  -43.689  1.00 30.28  ? 407 TRP   A CD2   1 
ATOM   3206  N  NE1   . TRP   A 1  407 ? -26.698 59.288  -44.266  1.00 22.14  ? 407 TRP   A NE1   1 
ATOM   3207  C  CE2   . TRP   A 1  407 ? -27.405 59.761  -43.195  1.00 24.69  ? 407 TRP   A CE2   1 
ATOM   3208  C  CE3   . TRP   A 1  407 ? -29.549 60.797  -42.785  1.00 29.25  ? 407 TRP   A CE3   1 
ATOM   3209  C  CZ2   . TRP   A 1  407 ? -27.068 59.803  -41.827  1.00 31.29  ? 407 TRP   A CZ2   1 
ATOM   3210  C  CZ3   . TRP   A 1  407 ? -29.210 60.834  -41.414  1.00 30.31  ? 407 TRP   A CZ3   1 
ATOM   3211  C  CH2   . TRP   A 1  407 ? -27.977 60.343  -40.959  1.00 23.39  ? 407 TRP   A CH2   1 
ATOM   3212  N  N     . TYR   A 1  408 ? -32.404 60.067  -47.848  1.00 34.34  ? 408 TYR   A N     1 
ATOM   3213  C  CA    . TYR   A 1  408 ? -33.430 60.764  -48.613  1.00 38.48  ? 408 TYR   A CA    1 
ATOM   3214  C  C     . TYR   A 1  408 ? -34.801 60.174  -48.312  1.00 36.26  ? 408 TYR   A C     1 
ATOM   3215  O  O     . TYR   A 1  408 ? -35.737 60.902  -47.959  1.00 31.85  ? 408 TYR   A O     1 
ATOM   3216  C  CB    . TYR   A 1  408 ? -33.073 60.688  -50.108  1.00 36.40  ? 408 TYR   A CB    1 
ATOM   3217  C  CG    . TYR   A 1  408 ? -31.826 61.495  -50.449  1.00 41.61  ? 408 TYR   A CG    1 
ATOM   3218  C  CD1   . TYR   A 1  408 ? -30.546 61.012  -50.157  1.00 38.35  ? 408 TYR   A CD1   1 
ATOM   3219  C  CD2   . TYR   A 1  408 ? -31.929 62.756  -51.030  1.00 34.59  ? 408 TYR   A CD2   1 
ATOM   3220  C  CE1   . TYR   A 1  408 ? -29.404 61.766  -50.447  1.00 30.12  ? 408 TYR   A CE1   1 
ATOM   3221  C  CE2   . TYR   A 1  408 ? -30.818 63.507  -51.308  1.00 35.18  ? 408 TYR   A CE2   1 
ATOM   3222  C  CZ    . TYR   A 1  408 ? -29.552 63.011  -51.024  1.00 36.04  ? 408 TYR   A CZ    1 
ATOM   3223  O  OH    . TYR   A 1  408 ? -28.448 63.782  -51.318  1.00 33.24  ? 408 TYR   A OH    1 
ATOM   3224  N  N     . VAL   A 1  409 ? -34.907 58.842  -48.410  1.00 34.52  ? 409 VAL   A N     1 
ATOM   3225  C  CA    . VAL   A 1  409 ? -36.101 58.107  -48.002  1.00 34.50  ? 409 VAL   A CA    1 
ATOM   3226  C  C     . VAL   A 1  409 ? -36.500 58.462  -46.572  1.00 39.45  ? 409 VAL   A C     1 
ATOM   3227  O  O     . VAL   A 1  409 ? -37.678 58.702  -46.277  1.00 44.58  ? 409 VAL   A O     1 
ATOM   3228  C  CB    . VAL   A 1  409 ? -35.854 56.598  -48.154  1.00 38.55  ? 409 VAL   A CB    1 
ATOM   3229  C  CG1   . VAL   A 1  409 ? -37.060 55.822  -47.707  1.00 29.45  ? 409 VAL   A CG1   1 
ATOM   3230  C  CG2   . VAL   A 1  409 ? -35.461 56.262  -49.590  1.00 26.92  ? 409 VAL   A CG2   1 
ATOM   3231  N  N     . GLY   A 1  410 ? -35.528 58.513  -45.663  1.00 29.88  ? 410 GLY   A N     1 
ATOM   3232  C  CA    . GLY   A 1  410 ? -35.834 58.836  -44.285  1.00 28.48  ? 410 GLY   A CA    1 
ATOM   3233  C  C     . GLY   A 1  410 ? -36.570 60.148  -44.109  1.00 39.55  ? 410 GLY   A C     1 
ATOM   3234  O  O     . GLY   A 1  410 ? -37.178 60.371  -43.056  1.00 41.82  ? 410 GLY   A O     1 
ATOM   3235  N  N     . GLU   A 1  411 ? -36.532 61.020  -45.115  1.00 39.47  ? 411 GLU   A N     1 
ATOM   3236  C  CA    . GLU   A 1  411 ? -37.144 62.338  -45.051  1.00 44.66  ? 411 GLU   A CA    1 
ATOM   3237  C  C     . GLU   A 1  411 ? -38.506 62.397  -45.748  1.00 46.56  ? 411 GLU   A C     1 
ATOM   3238  O  O     . GLU   A 1  411 ? -39.124 63.465  -45.794  1.00 42.25  ? 411 GLU   A O     1 
ATOM   3239  C  CB    . GLU   A 1  411 ? -36.190 63.377  -45.655  1.00 47.13  ? 411 GLU   A CB    1 
ATOM   3240  C  CG    . GLU   A 1  411 ? -34.947 63.652  -44.833  1.00 33.15  ? 411 GLU   A CG    1 
ATOM   3241  C  CD    . GLU   A 1  411 ? -35.266 64.481  -43.625  1.00 46.66  ? 411 GLU   A CD    1 
ATOM   3242  O  OE1   . GLU   A 1  411 ? -36.467 64.786  -43.455  1.00 48.34  ? 411 GLU   A OE1   1 
ATOM   3243  O  OE2   . GLU   A 1  411 ? -34.335 64.830  -42.859  1.00 42.83  ? 411 GLU   A OE2   1 
ATOM   3244  N  N     . GLY   A 1  412 ? -38.991 61.278  -46.279  1.00 40.10  ? 412 GLY   A N     1 
ATOM   3245  C  CA    . GLY   A 1  412 ? -40.283 61.222  -46.922  1.00 46.20  ? 412 GLY   A CA    1 
ATOM   3246  C  C     . GLY   A 1  412 ? -40.217 61.054  -48.420  1.00 48.11  ? 412 GLY   A C     1 
ATOM   3247  O  O     . GLY   A 1  412 ? -41.266 60.884  -49.055  1.00 51.49  ? 412 GLY   A O     1 
ATOM   3248  N  N     . MET   A 1  413 ? -39.024 61.093  -49.001  1.00 41.36  ? 413 MET   A N     1 
ATOM   3249  C  CA    . MET   A 1  413 ? -38.861 60.953  -50.437  1.00 36.96  ? 413 MET   A CA    1 
ATOM   3250  C  C     . MET   A 1  413 ? -38.812 59.478  -50.803  1.00 40.32  ? 413 MET   A C     1 
ATOM   3251  O  O     . MET   A 1  413 ? -38.236 58.659  -50.083  1.00 44.73  ? 413 MET   A O     1 
ATOM   3252  C  CB    . MET   A 1  413 ? -37.581 61.660  -50.884  1.00 36.21  ? 413 MET   A CB    1 
ATOM   3253  C  CG    . MET   A 1  413 ? -37.582 62.183  -52.304  1.00 42.93  ? 413 MET   A CG    1 
ATOM   3254  S  SD    . MET   A 1  413 ? -36.032 62.984  -52.817  1.00 50.00  ? 413 MET   A SD    1 
ATOM   3255  C  CE    . MET   A 1  413 ? -35.084 61.558  -53.358  1.00 31.59  ? 413 MET   A CE    1 
ATOM   3256  N  N     . GLU   A 1  414 ? -39.424 59.133  -51.916  1.00 43.60  ? 414 GLU   A N     1 
ATOM   3257  C  CA    . GLU   A 1  414 ? -39.477 57.744  -52.330  1.00 41.11  ? 414 GLU   A CA    1 
ATOM   3258  C  C     . GLU   A 1  414 ? -38.298 57.426  -53.230  1.00 41.69  ? 414 GLU   A C     1 
ATOM   3259  O  O     . GLU   A 1  414 ? -37.879 58.250  -54.037  1.00 42.38  ? 414 GLU   A O     1 
ATOM   3260  C  CB    . GLU   A 1  414 ? -40.784 57.444  -53.065  1.00 36.37  ? 414 GLU   A CB    1 
ATOM   3261  C  CG    . GLU   A 1  414 ? -42.003 58.061  -52.429  1.00 50.86  ? 414 GLU   A CG    1 
ATOM   3262  C  CD    . GLU   A 1  414 ? -43.271 57.646  -53.148  1.00 66.46  ? 414 GLU   A CD    1 
ATOM   3263  O  OE1   . GLU   A 1  414 ? -43.654 56.458  -53.025  1.00 65.97  ? 414 GLU   A OE1   1 
ATOM   3264  O  OE2   . GLU   A 1  414 ? -43.860 58.496  -53.857  1.00 53.26  ? 414 GLU   A OE2   1 
ATOM   3265  N  N     . GLU   A 1  415 ? -37.789 56.205  -53.112  1.00 44.33  ? 415 GLU   A N     1 
ATOM   3266  C  CA    . GLU   A 1  415 ? -36.637 55.826  -53.909  1.00 46.78  ? 415 GLU   A CA    1 
ATOM   3267  C  C     . GLU   A 1  415 ? -36.839 56.161  -55.384  1.00 53.83  ? 415 GLU   A C     1 
ATOM   3268  O  O     . GLU   A 1  415 ? -35.886 56.542  -56.074  1.00 53.64  ? 415 GLU   A O     1 
ATOM   3269  C  CB    . GLU   A 1  415 ? -36.355 54.336  -53.713  1.00 43.51  ? 415 GLU   A CB    1 
ATOM   3270  C  CG    . GLU   A 1  415 ? -35.116 53.828  -54.414  1.00 51.90  ? 415 GLU   A CG    1 
ATOM   3271  C  CD    . GLU   A 1  415 ? -34.510 52.624  -53.713  1.00 56.41  ? 415 GLU   A CD    1 
ATOM   3272  O  OE1   . GLU   A 1  415 ? -34.324 52.697  -52.474  1.00 62.99  ? 415 GLU   A OE1   1 
ATOM   3273  O  OE2   . GLU   A 1  415 ? -34.233 51.604  -54.395  1.00 57.33  ? 415 GLU   A OE2   1 
ATOM   3274  N  N     . GLY   A 1  416 ? -38.076 56.064  -55.879  1.00 52.52  ? 416 GLY   A N     1 
ATOM   3275  C  CA    . GLY   A 1  416 ? -38.301 56.137  -57.314  1.00 38.85  ? 416 GLY   A CA    1 
ATOM   3276  C  C     . GLY   A 1  416 ? -38.122 57.525  -57.879  1.00 44.68  ? 416 GLY   A C     1 
ATOM   3277  O  O     . GLY   A 1  416 ? -37.789 57.680  -59.056  1.00 42.21  ? 416 GLY   A O     1 
ATOM   3278  N  N     . GLU   A 1  417 ? -38.356 58.549  -57.060  1.00 41.79  ? 417 GLU   A N     1 
ATOM   3279  C  CA    . GLU   A 1  417 ? -38.011 59.899  -57.459  1.00 33.24  ? 417 GLU   A CA    1 
ATOM   3280  C  C     . GLU   A 1  417 ? -36.552 59.996  -57.902  1.00 45.86  ? 417 GLU   A C     1 
ATOM   3281  O  O     . GLU   A 1  417 ? -36.234 60.780  -58.804  1.00 45.76  ? 417 GLU   A O     1 
ATOM   3282  C  CB    . GLU   A 1  417 ? -38.303 60.862  -56.311  1.00 29.88  ? 417 GLU   A CB    1 
ATOM   3283  C  CG    . GLU   A 1  417 ? -37.761 62.253  -56.550  1.00 37.34  ? 417 GLU   A CG    1 
ATOM   3284  C  CD    . GLU   A 1  417 ? -38.380 63.275  -55.628  1.00 44.01  ? 417 GLU   A CD    1 
ATOM   3285  O  OE1   . GLU   A 1  417 ? -39.241 62.883  -54.799  1.00 41.91  ? 417 GLU   A OE1   1 
ATOM   3286  O  OE2   . GLU   A 1  417 ? -38.019 64.470  -55.744  1.00 44.45  ? 417 GLU   A OE2   1 
ATOM   3287  N  N     . PHE   A 1  418 ? -35.650 59.219  -57.285  1.00 46.03  ? 418 PHE   A N     1 
ATOM   3288  C  CA    . PHE   A 1  418 ? -34.265 59.167  -57.763  1.00 44.48  ? 418 PHE   A CA    1 
ATOM   3289  C  C     . PHE   A 1  418 ? -34.215 58.701  -59.208  1.00 36.41  ? 418 PHE   A C     1 
ATOM   3290  O  O     . PHE   A 1  418 ? -33.513 59.275  -60.043  1.00 36.33  ? 418 PHE   A O     1 
ATOM   3291  C  CB    . PHE   A 1  418 ? -33.411 58.223  -56.902  1.00 36.81  ? 418 PHE   A CB    1 
ATOM   3292  C  CG    . PHE   A 1  418 ? -32.711 58.886  -55.737  1.00 42.11  ? 418 PHE   A CG    1 
ATOM   3293  C  CD1   . PHE   A 1  418 ? -31.448 59.438  -55.889  1.00 38.05  ? 418 PHE   A CD1   1 
ATOM   3294  C  CD2   . PHE   A 1  418 ? -33.295 58.919  -54.479  1.00 43.11  ? 418 PHE   A CD2   1 
ATOM   3295  C  CE1   . PHE   A 1  418 ? -30.801 60.032  -54.815  1.00 31.19  ? 418 PHE   A CE1   1 
ATOM   3296  C  CE2   . PHE   A 1  418 ? -32.642 59.502  -53.405  1.00 37.74  ? 418 PHE   A CE2   1 
ATOM   3297  C  CZ    . PHE   A 1  418 ? -31.396 60.066  -53.574  1.00 31.55  ? 418 PHE   A CZ    1 
ATOM   3298  N  N     . SER   A 1  419 ? -34.943 57.645  -59.519  1.00 37.48  ? 419 SER   A N     1 
ATOM   3299  C  CA    . SER   A 1  419 ? -34.847 57.091  -60.857  1.00 35.74  ? 419 SER   A CA    1 
ATOM   3300  C  C     . SER   A 1  419 ? -35.546 57.985  -61.873  1.00 43.78  ? 419 SER   A C     1 
ATOM   3301  O  O     . SER   A 1  419 ? -35.082 58.108  -63.016  1.00 48.93  ? 419 SER   A O     1 
ATOM   3302  C  CB    . SER   A 1  419 ? -35.412 55.675  -60.857  1.00 39.77  ? 419 SER   A CB    1 
ATOM   3303  O  OG    . SER   A 1  419 ? -36.482 55.591  -59.924  1.00 50.78  ? 419 SER   A OG    1 
ATOM   3304  N  N     . GLU   A 1  420 ? -36.635 58.649  -61.473  1.00 44.92  ? 420 GLU   A N     1 
ATOM   3305  C  CA    A GLU   A 1  420 ? -37.314 59.568  -62.383  0.56 40.66  ? 420 GLU   A CA    1 
ATOM   3306  C  CA    B GLU   A 1  420 ? -37.309 59.565  -62.390  0.44 40.65  ? 420 GLU   A CA    1 
ATOM   3307  C  C     . GLU   A 1  420 ? -36.434 60.773  -62.707  1.00 41.93  ? 420 GLU   A C     1 
ATOM   3308  O  O     . GLU   A 1  420 ? -36.353 61.196  -63.865  1.00 45.61  ? 420 GLU   A O     1 
ATOM   3309  C  CB    A GLU   A 1  420 ? -38.650 60.007  -61.783  0.56 35.40  ? 420 GLU   A CB    1 
ATOM   3310  C  CB    B GLU   A 1  420 ? -38.661 59.994  -61.817  0.44 35.53  ? 420 GLU   A CB    1 
ATOM   3311  C  CG    A GLU   A 1  420 ? -38.863 61.500  -61.791  0.56 41.01  ? 420 GLU   A CG    1 
ATOM   3312  C  CG    B GLU   A 1  420 ? -39.801 59.095  -62.260  0.44 34.59  ? 420 GLU   A CG    1 
ATOM   3313  C  CD    A GLU   A 1  420 ? -40.244 61.880  -61.317  0.56 40.46  ? 420 GLU   A CD    1 
ATOM   3314  C  CD    B GLU   A 1  420 ? -40.604 58.548  -61.098  0.44 37.83  ? 420 GLU   A CD    1 
ATOM   3315  O  OE1   A GLU   A 1  420 ? -40.988 60.955  -60.938  0.56 39.91  ? 420 GLU   A OE1   1 
ATOM   3316  O  OE1   B GLU   A 1  420 ? -41.409 59.306  -60.527  0.44 38.82  ? 420 GLU   A OE1   1 
ATOM   3317  O  OE2   A GLU   A 1  420 ? -40.581 63.088  -61.330  0.56 34.76  ? 420 GLU   A OE2   1 
ATOM   3318  O  OE2   B GLU   A 1  420 ? -40.426 57.362  -60.750  0.44 38.68  ? 420 GLU   A OE2   1 
ATOM   3319  N  N     . ALA   A 1  421 ? -35.754 61.332  -61.702  1.00 44.41  ? 421 ALA   A N     1 
ATOM   3320  C  CA    . ALA   A 1  421 ? -34.806 62.410  -61.966  1.00 37.81  ? 421 ALA   A CA    1 
ATOM   3321  C  C     . ALA   A 1  421 ? -33.683 61.942  -62.892  1.00 42.99  ? 421 ALA   A C     1 
ATOM   3322  O  O     . ALA   A 1  421 ? -33.361 62.608  -63.881  1.00 41.40  ? 421 ALA   A O     1 
ATOM   3323  C  CB    . ALA   A 1  421 ? -34.237 62.948  -60.659  1.00 40.06  ? 421 ALA   A CB    1 
ATOM   3324  N  N     . ARG   A 1  422 ? -33.072 60.791  -62.603  1.00 40.66  ? 422 ARG   A N     1 
ATOM   3325  C  CA    . ARG   A 1  422 ? -31.943 60.378  -63.438  1.00 39.30  ? 422 ARG   A CA    1 
ATOM   3326  C  C     . ARG   A 1  422 ? -32.386 60.106  -64.872  1.00 43.00  ? 422 ARG   A C     1 
ATOM   3327  O  O     . ARG   A 1  422 ? -31.602 60.298  -65.813  1.00 37.41  ? 422 ARG   A O     1 
ATOM   3328  C  CB    . ARG   A 1  422 ? -31.249 59.143  -62.846  1.00 30.10  ? 422 ARG   A CB    1 
ATOM   3329  C  CG    . ARG   A 1  422 ? -30.157 58.525  -63.728  1.00 17.34  ? 422 ARG   A CG    1 
ATOM   3330  C  CD    . ARG   A 1  422 ? -28.973 59.451  -63.849  1.00 30.66  ? 422 ARG   A CD    1 
ATOM   3331  N  NE    . ARG   A 1  422 ? -27.862 58.854  -64.583  1.00 37.59  ? 422 ARG   A NE    1 
ATOM   3332  C  CZ    . ARG   A 1  422 ? -27.688 58.942  -65.898  1.00 38.75  ? 422 ARG   A CZ    1 
ATOM   3333  N  NH1   . ARG   A 1  422 ? -28.570 59.547  -66.676  1.00 33.12  ? 422 ARG   A NH1   1 
ATOM   3334  N  NH2   . ARG   A 1  422 ? -26.597 58.417  -66.445  1.00 36.29  ? 422 ARG   A NH2   1 
ATOM   3335  N  N     . GLU   A 1  423 ? -33.633 59.653  -65.057  1.00 49.50  ? 423 GLU   A N     1 
ATOM   3336  C  CA    . GLU   A 1  423 ? -34.132 59.397  -66.404  1.00 46.98  ? 423 GLU   A CA    1 
ATOM   3337  C  C     . GLU   A 1  423 ? -34.360 60.700  -67.158  1.00 44.11  ? 423 GLU   A C     1 
ATOM   3338  O  O     . GLU   A 1  423 ? -34.031 60.802  -68.346  1.00 44.89  ? 423 GLU   A O     1 
ATOM   3339  C  CB    . GLU   A 1  423 ? -35.411 58.563  -66.359  1.00 46.06  ? 423 GLU   A CB    1 
ATOM   3340  C  CG    . GLU   A 1  423 ? -35.760 57.959  -67.729  1.00 55.72  ? 423 GLU   A CG    1 
ATOM   3341  C  CD    . GLU   A 1  423 ? -34.583 57.213  -68.373  1.00 63.61  ? 423 GLU   A CD    1 
ATOM   3342  O  OE1   . GLU   A 1  423 ? -33.914 56.424  -67.660  1.00 62.67  ? 423 GLU   A OE1   1 
ATOM   3343  O  OE2   . GLU   A 1  423 ? -34.322 57.419  -69.586  1.00 53.73  ? 423 GLU   A OE2   1 
ATOM   3344  N  N     . ASP   A 1  424 ? -34.910 61.708  -66.482  1.00 34.45  ? 424 ASP   A N     1 
ATOM   3345  C  CA    . ASP   A 1  424 ? -34.963 63.049  -67.049  1.00 35.76  ? 424 ASP   A CA    1 
ATOM   3346  C  C     . ASP   A 1  424 ? -33.588 63.477  -67.580  1.00 45.60  ? 424 ASP   A C     1 
ATOM   3347  O  O     . ASP   A 1  424 ? -33.461 63.947  -68.720  1.00 42.22  ? 424 ASP   A O     1 
ATOM   3348  C  CB    . ASP   A 1  424 ? -35.480 64.011  -65.980  1.00 37.46  ? 424 ASP   A CB    1 
ATOM   3349  C  CG    . ASP   A 1  424 ? -36.042 65.270  -66.557  1.00 44.07  ? 424 ASP   A CG    1 
ATOM   3350  O  OD1   . ASP   A 1  424 ? -36.171 65.311  -67.792  1.00 40.60  ? 424 ASP   A OD1   1 
ATOM   3351  O  OD2   . ASP   A 1  424 ? -36.360 66.212  -65.781  1.00 48.22  ? 424 ASP   A OD2   1 
ATOM   3352  N  N     . MET   A 1  425 ? -32.537 63.304  -66.767  1.00 40.33  ? 425 MET   A N     1 
ATOM   3353  C  CA    . MET   A 1  425 ? -31.197 63.685  -67.202  1.00 35.50  ? 425 MET   A CA    1 
ATOM   3354  C  C     . MET   A 1  425 ? -30.730 62.803  -68.343  1.00 33.07  ? 425 MET   A C     1 
ATOM   3355  O  O     . MET   A 1  425 ? -30.013 63.258  -69.240  1.00 36.73  ? 425 MET   A O     1 
ATOM   3356  C  CB    . MET   A 1  425 ? -30.204 63.607  -66.038  1.00 31.26  ? 425 MET   A CB    1 
ATOM   3357  C  CG    . MET   A 1  425 ? -30.529 64.497  -64.853  1.00 35.30  ? 425 MET   A CG    1 
ATOM   3358  S  SD    . MET   A 1  425 ? -30.415 66.266  -65.166  1.00 37.58  ? 425 MET   A SD    1 
ATOM   3359  C  CE    . MET   A 1  425 ? -28.810 66.292  -65.984  1.00 39.85  ? 425 MET   A CE    1 
ATOM   3360  N  N     . ALA   A 1  426 ? -31.096 61.530  -68.316  1.00 41.07  ? 426 ALA   A N     1 
ATOM   3361  C  CA    . ALA   A 1  426 ? -30.765 60.660  -69.441  1.00 45.01  ? 426 ALA   A CA    1 
ATOM   3362  C  C     . ALA   A 1  426 ? -31.350 61.215  -70.736  1.00 41.80  ? 426 ALA   A C     1 
ATOM   3363  O  O     . ALA   A 1  426 ? -30.667 61.293  -71.759  1.00 43.69  ? 426 ALA   A O     1 
ATOM   3364  C  CB    . ALA   A 1  426 ? -31.277 59.243  -69.171  1.00 31.52  ? 426 ALA   A CB    1 
ATOM   3365  N  N     . ALA   A 1  427 ? -32.624 61.605  -70.698  1.00 44.28  ? 427 ALA   A N     1 
ATOM   3366  C  CA    . ALA   A 1  427 ? -33.272 62.198  -71.856  1.00 47.12  ? 427 ALA   A CA    1 
ATOM   3367  C  C     . ALA   A 1  427 ? -32.636 63.539  -72.234  1.00 42.57  ? 427 ALA   A C     1 
ATOM   3368  O  O     . ALA   A 1  427 ? -32.485 63.850  -73.420  1.00 32.80  ? 427 ALA   A O     1 
ATOM   3369  C  CB    . ALA   A 1  427 ? -34.760 62.360  -71.566  1.00 38.17  ? 427 ALA   A CB    1 
ATOM   3370  N  N     . LEU   A 1  428 ? -32.276 64.352  -71.244  1.00 37.54  ? 428 LEU   A N     1 
ATOM   3371  C  CA    . LEU   A 1  428 ? -31.590 65.605  -71.539  1.00 35.19  ? 428 LEU   A CA    1 
ATOM   3372  C  C     . LEU   A 1  428 ? -30.273 65.354  -72.262  1.00 39.37  ? 428 LEU   A C     1 
ATOM   3373  O  O     . LEU   A 1  428 ? -29.928 66.065  -73.214  1.00 42.15  ? 428 LEU   A O     1 
ATOM   3374  C  CB    . LEU   A 1  428 ? -31.364 66.391  -70.252  1.00 33.40  ? 428 LEU   A CB    1 
ATOM   3375  C  CG    . LEU   A 1  428 ? -30.914 67.844  -70.363  1.00 39.39  ? 428 LEU   A CG    1 
ATOM   3376  C  CD1   . LEU   A 1  428 ? -31.945 68.726  -71.103  1.00 32.19  ? 428 LEU   A CD1   1 
ATOM   3377  C  CD2   . LEU   A 1  428 ? -30.656 68.353  -68.952  1.00 31.93  ? 428 LEU   A CD2   1 
ATOM   3378  N  N     . GLU   A 1  429 ? -29.524 64.344  -71.838  1.00 40.43  ? 429 GLU   A N     1 
ATOM   3379  C  CA    . GLU   A 1  429 ? -28.302 64.022  -72.561  1.00 40.20  ? 429 GLU   A CA    1 
ATOM   3380  C  C     . GLU   A 1  429 ? -28.598 63.591  -73.994  1.00 46.99  ? 429 GLU   A C     1 
ATOM   3381  O  O     . GLU   A 1  429 ? -27.771 63.815  -74.889  1.00 46.46  ? 429 GLU   A O     1 
ATOM   3382  C  CB    . GLU   A 1  429 ? -27.511 62.943  -71.815  1.00 26.79  ? 429 GLU   A CB    1 
ATOM   3383  C  CG    . GLU   A 1  429 ? -26.894 63.458  -70.523  1.00 34.46  ? 429 GLU   A CG    1 
ATOM   3384  C  CD    . GLU   A 1  429 ? -25.752 62.597  -69.993  1.00 38.04  ? 429 GLU   A CD    1 
ATOM   3385  O  OE1   . GLU   A 1  429 ? -24.718 62.455  -70.669  1.00 31.92  ? 429 GLU   A OE1   1 
ATOM   3386  O  OE2   . GLU   A 1  429 ? -25.879 62.062  -68.880  1.00 43.74  ? 429 GLU   A OE2   1 
ATOM   3387  N  N     . LYS   A 1  430 ? -29.764 62.976  -74.237  1.00 40.98  ? 430 LYS   A N     1 
ATOM   3388  C  CA    . LYS   A 1  430 ? -30.110 62.572  -75.599  1.00 46.49  ? 430 LYS   A CA    1 
ATOM   3389  C  C     . LYS   A 1  430 ? -30.440 63.794  -76.455  1.00 46.62  ? 430 LYS   A C     1 
ATOM   3390  O  O     . LYS   A 1  430 ? -29.951 63.926  -77.583  1.00 45.10  ? 430 LYS   A O     1 
ATOM   3391  C  CB    . LYS   A 1  430 ? -31.283 61.576  -75.589  1.00 48.06  ? 430 LYS   A CB    1 
ATOM   3392  C  CG    . LYS   A 1  430 ? -30.952 60.158  -75.101  1.00 56.11  ? 430 LYS   A CG    1 
ATOM   3393  C  CD    . LYS   A 1  430 ? -32.229 59.352  -74.755  1.00 59.78  ? 430 LYS   A CD    1 
ATOM   3394  C  CE    . LYS   A 1  430 ? -32.171 58.716  -73.340  1.00 57.93  ? 430 LYS   A CE    1 
ATOM   3395  N  NZ    . LYS   A 1  430 ? -33.522 58.599  -72.669  1.00 41.83  ? 430 LYS   A NZ    1 
ATOM   3396  N  N     . ASP   A 1  431 ? -31.269 64.700  -75.928  1.00 39.59  ? 431 ASP   A N     1 
ATOM   3397  C  CA    . ASP   A 1  431 ? -31.525 65.964  -76.603  1.00 42.87  ? 431 ASP   A CA    1 
ATOM   3398  C  C     . ASP   A 1  431 ? -30.217 66.591  -77.085  1.00 47.02  ? 431 ASP   A C     1 
ATOM   3399  O  O     . ASP   A 1  431 ? -30.012 66.794  -78.289  1.00 42.80  ? 431 ASP   A O     1 
ATOM   3400  C  CB    . ASP   A 1  431 ? -32.275 66.916  -75.666  1.00 33.88  ? 431 ASP   A CB    1 
ATOM   3401  C  CG    . ASP   A 1  431 ? -33.572 66.328  -75.139  1.00 42.69  ? 431 ASP   A CG    1 
ATOM   3402  O  OD1   . ASP   A 1  431 ? -34.162 65.487  -75.842  1.00 43.32  ? 431 ASP   A OD1   1 
ATOM   3403  O  OD2   . ASP   A 1  431 ? -34.010 66.720  -74.022  1.00 48.65  ? 431 ASP   A OD2   1 
ATOM   3404  N  N     . TYR   A 1  432 ? -29.300 66.880  -76.154  1.00 40.09  ? 432 TYR   A N     1 
ATOM   3405  C  CA    . TYR   A 1  432 ? -28.061 67.528  -76.557  1.00 43.67  ? 432 TYR   A CA    1 
ATOM   3406  C  C     . TYR   A 1  432 ? -27.390 66.761  -77.692  1.00 45.06  ? 432 TYR   A C     1 
ATOM   3407  O  O     . TYR   A 1  432 ? -26.951 67.364  -78.676  1.00 45.27  ? 432 TYR   A O     1 
ATOM   3408  C  CB    . TYR   A 1  432 ? -27.115 67.692  -75.367  1.00 41.26  ? 432 TYR   A CB    1 
ATOM   3409  C  CG    . TYR   A 1  432 ? -27.420 68.878  -74.477  1.00 36.19  ? 432 TYR   A CG    1 
ATOM   3410  C  CD1   . TYR   A 1  432 ? -26.982 70.159  -74.807  1.00 35.00  ? 432 TYR   A CD1   1 
ATOM   3411  C  CD2   . TYR   A 1  432 ? -28.114 68.712  -73.290  1.00 36.62  ? 432 TYR   A CD2   1 
ATOM   3412  C  CE1   . TYR   A 1  432 ? -27.250 71.250  -73.987  1.00 28.82  ? 432 TYR   A CE1   1 
ATOM   3413  C  CE2   . TYR   A 1  432 ? -28.383 69.788  -72.454  1.00 37.25  ? 432 TYR   A CE2   1 
ATOM   3414  C  CZ    . TYR   A 1  432 ? -27.955 71.054  -72.809  1.00 39.10  ? 432 TYR   A CZ    1 
ATOM   3415  O  OH    . TYR   A 1  432 ? -28.235 72.112  -71.968  1.00 43.28  ? 432 TYR   A OH    1 
ATOM   3416  N  N     . GLU   A 1  433 ? -27.347 65.430  -77.603  1.00 47.20  ? 433 GLU   A N     1 
ATOM   3417  C  CA    . GLU   A 1  433 ? -26.713 64.646  -78.662  1.00 38.93  ? 433 GLU   A CA    1 
ATOM   3418  C  C     . GLU   A 1  433 ? -27.431 64.828  -79.996  1.00 49.31  ? 433 GLU   A C     1 
ATOM   3419  O  O     . GLU   A 1  433 ? -26.799 65.137  -81.013  1.00 50.91  ? 433 GLU   A O     1 
ATOM   3420  C  CB    . GLU   A 1  433 ? -26.673 63.176  -78.280  1.00 39.87  ? 433 GLU   A CB    1 
ATOM   3421  C  CG    . GLU   A 1  433 ? -26.088 62.295  -79.347  1.00 52.48  ? 433 GLU   A CG    1 
ATOM   3422  C  CD    . GLU   A 1  433 ? -24.819 61.610  -78.902  1.00 65.66  ? 433 GLU   A CD    1 
ATOM   3423  O  OE1   . GLU   A 1  433 ? -24.072 62.226  -78.115  1.00 72.39  ? 433 GLU   A OE1   1 
ATOM   3424  O  OE2   . GLU   A 1  433 ? -24.566 60.463  -79.335  1.00 77.78  ? 433 GLU   A OE2   1 
ATOM   3425  N  N     . GLU   A 1  434 ? -28.755 64.632  -80.015  1.00 48.50  ? 434 GLU   A N     1 
ATOM   3426  C  CA    . GLU   A 1  434 ? -29.513 64.780  -81.258  1.00 50.76  ? 434 GLU   A CA    1 
ATOM   3427  C  C     . GLU   A 1  434 ? -29.142 66.072  -81.973  1.00 47.32  ? 434 GLU   A C     1 
ATOM   3428  O  O     . GLU   A 1  434 ? -28.771 66.065  -83.153  1.00 52.61  ? 434 GLU   A O     1 
ATOM   3429  C  CB    . GLU   A 1  434 ? -31.018 64.750  -80.976  1.00 56.20  ? 434 GLU   A CB    1 
ATOM   3430  C  CG    . GLU   A 1  434 ? -31.572 63.395  -80.553  1.00 61.75  ? 434 GLU   A CG    1 
ATOM   3431  C  CD    . GLU   A 1  434 ? -33.085 63.422  -80.401  1.00 84.39  ? 434 GLU   A CD    1 
ATOM   3432  O  OE1   . GLU   A 1  434 ? -33.778 63.752  -81.396  1.00 92.40  ? 434 GLU   A OE1   1 
ATOM   3433  O  OE2   . GLU   A 1  434 ? -33.580 63.132  -79.287  1.00 80.56  ? 434 GLU   A OE2   1 
ATOM   3434  N  N     . VAL   A 1  435 ? -29.211 67.191  -81.253  1.00 45.23  ? 435 VAL   A N     1 
ATOM   3435  C  CA    . VAL   A 1  435 ? -28.917 68.490  -81.837  1.00 41.89  ? 435 VAL   A CA    1 
ATOM   3436  C  C     . VAL   A 1  435 ? -27.465 68.593  -82.311  1.00 38.56  ? 435 VAL   A C     1 
ATOM   3437  O  O     . VAL   A 1  435 ? -27.176 69.353  -83.242  1.00 54.78  ? 435 VAL   A O     1 
ATOM   3438  C  CB    . VAL   A 1  435 ? -29.279 69.600  -80.825  1.00 42.06  ? 435 VAL   A CB    1 
ATOM   3439  C  CG1   . VAL   A 1  435 ? -29.013 70.977  -81.410  1.00 46.23  ? 435 VAL   A CG1   1 
ATOM   3440  C  CG2   . VAL   A 1  435 ? -30.722 69.489  -80.426  1.00 29.76  ? 435 VAL   A CG2   1 
ATOM   3441  N  N     . GLY   A 1  436 ? -26.534 67.840  -81.710  1.00 41.46  ? 436 GLY   A N     1 
ATOM   3442  C  CA    . GLY   A 1  436 ? -25.110 68.000  -82.019  1.00 46.49  ? 436 GLY   A CA    1 
ATOM   3443  C  C     . GLY   A 1  436 ? -24.424 66.905  -82.825  1.00 58.90  ? 436 GLY   A C     1 
ATOM   3444  O  O     . GLY   A 1  436 ? -23.190 66.842  -82.867  1.00 57.58  ? 436 GLY   A O     1 
ATOM   3445  N  N     . VAL   A 1  437 ? -25.222 66.071  -83.505  1.00 72.20  ? 437 VAL   A N     1 
ATOM   3446  C  CA    . VAL   A 1  437 ? -24.756 64.828  -84.134  1.00 77.36  ? 437 VAL   A CA    1 
ATOM   3447  C  C     . VAL   A 1  437 ? -23.853 65.077  -85.340  1.00 93.31  ? 437 VAL   A C     1 
ATOM   3448  O  O     . VAL   A 1  437 ? -23.050 64.207  -85.707  1.00 88.77  ? 437 VAL   A O     1 
ATOM   3449  C  CB    . VAL   A 1  437 ? -25.966 63.969  -84.554  1.00 76.34  ? 437 VAL   A CB    1 
ATOM   3450  C  CG1   . VAL   A 1  437 ? -26.999 64.820  -85.311  1.00 62.10  ? 437 VAL   A CG1   1 
ATOM   3451  C  CG2   . VAL   A 1  437 ? -25.509 62.801  -85.423  1.00 80.86  ? 437 VAL   A CG2   1 
ATOM   3452  N  N     . ASP   A 1  438 ? -24.007 66.231  -85.999  1.00 97.69  ? 438 ASP   A N     1 
ATOM   3453  C  CA    . ASP   A 1  438 ? -23.389 66.553  -87.286  1.00 96.71  ? 438 ASP   A CA    1 
ATOM   3454  C  C     . ASP   A 1  438 ? -22.046 65.854  -87.503  1.00 105.24 ? 438 ASP   A C     1 
ATOM   3455  O  O     . ASP   A 1  438 ? -22.019 64.701  -87.950  1.00 106.62 ? 438 ASP   A O     1 
ATOM   3456  C  CB    . ASP   A 1  438 ? -23.235 68.078  -87.417  1.00 104.20 ? 438 ASP   A CB    1 
ATOM   3457  C  CG    . ASP   A 1  438 ? -24.583 68.821  -87.380  1.00 98.95  ? 438 ASP   A CG    1 
ATOM   3458  O  OD1   . ASP   A 1  438 ? -25.476 68.490  -88.194  1.00 105.67 ? 438 ASP   A OD1   1 
ATOM   3459  O  OD2   . ASP   A 1  438 ? -24.747 69.733  -86.534  1.00 74.17  ? 438 ASP   A OD2   1 
ATOM   3460  N  N     . SER   A 1  439 ? -20.936 66.532  -87.190  1.00 103.22 ? 439 SER   A N     1 
ATOM   3461  C  CA    . SER   A 1  439 ? -19.589 65.990  -87.423  1.00 99.60  ? 439 SER   A CA    1 
ATOM   3462  C  C     . SER   A 1  439 ? -19.293 64.780  -86.531  1.00 100.74 ? 439 SER   A C     1 
ATOM   3463  O  O     . SER   A 1  439 ? -18.375 63.998  -86.801  1.00 93.54  ? 439 SER   A O     1 
ATOM   3464  C  CB    . SER   A 1  439 ? -18.521 67.076  -87.204  1.00 93.91  ? 439 SER   A CB    1 
ATOM   3465  O  OG    . SER   A 1  439 ? -17.204 66.559  -87.372  1.00 82.43  ? 439 SER   A OG    1 
ATOM   3466  N  N     . MET   B 1  1   ? -20.987 50.906  2.201    1.00 71.10  ? 1   MET   C N     1 
ATOM   3467  C  CA    . MET   B 1  1   ? -21.613 49.594  2.275    1.00 55.42  ? 1   MET   C CA    1 
ATOM   3468  C  C     . MET   B 1  1   ? -20.564 48.488  2.149    1.00 57.22  ? 1   MET   C C     1 
ATOM   3469  O  O     . MET   B 1  1   ? -19.467 48.610  2.690    1.00 70.58  ? 1   MET   C O     1 
ATOM   3470  C  CB    . MET   B 1  1   ? -22.694 49.442  1.190    1.00 60.10  ? 1   MET   C CB    1 
ATOM   3471  C  CG    . MET   B 1  1   ? -22.816 50.613  0.211    1.00 67.91  ? 1   MET   C CG    1 
ATOM   3472  S  SD    . MET   B 1  1   ? -24.144 51.775  0.607    1.00 80.06  ? 1   MET   C SD    1 
ATOM   3473  C  CE    . MET   B 1  1   ? -23.579 52.440  2.176    1.00 62.82  ? 1   MET   C CE    1 
ATOM   3474  N  N     . ARG   B 1  2   ? -20.919 47.395  1.467    1.00 61.41  ? 2   ARG   C N     1 
ATOM   3475  C  CA    . ARG   B 1  2   ? -20.040 46.264  1.158    1.00 55.88  ? 2   ARG   C CA    1 
ATOM   3476  C  C     . ARG   B 1  2   ? -19.808 45.314  2.327    1.00 46.32  ? 2   ARG   C C     1 
ATOM   3477  O  O     . ARG   B 1  2   ? -18.892 44.499  2.244    1.00 47.97  ? 2   ARG   C O     1 
ATOM   3478  C  CB    . ARG   B 1  2   ? -18.665 46.725  0.664    1.00 58.77  ? 2   ARG   C CB    1 
ATOM   3479  C  CG    . ARG   B 1  2   ? -18.697 47.626  -0.565   1.00 74.20  ? 2   ARG   C CG    1 
ATOM   3480  C  CD    . ARG   B 1  2   ? -17.532 48.616  -0.508   1.00 79.80  ? 2   ARG   C CD    1 
ATOM   3481  N  NE    . ARG   B 1  2   ? -17.323 49.106  0.853    1.00 71.35  ? 2   ARG   C NE    1 
ATOM   3482  C  CZ    . ARG   B 1  2   ? -17.861 50.213  1.353    1.00 67.44  ? 2   ARG   C CZ    1 
ATOM   3483  N  NH1   . ARG   B 1  2   ? -18.644 50.996  0.621    1.00 50.65  ? 2   ARG   C NH1   1 
ATOM   3484  N  NH2   . ARG   B 1  2   ? -17.615 50.535  2.626    1.00 58.85  ? 2   ARG   C NH2   1 
ATOM   3485  N  N     . GLU   B 1  3   ? -20.588 45.376  3.401    1.00 35.94  ? 3   GLU   C N     1 
ATOM   3486  C  CA    . GLU   B 1  3   ? -20.284 44.548  4.564    1.00 48.42  ? 3   GLU   C CA    1 
ATOM   3487  C  C     . GLU   B 1  3   ? -20.339 43.045  4.247    1.00 43.47  ? 3   GLU   C C     1 
ATOM   3488  O  O     . GLU   B 1  3   ? -21.059 42.592  3.349    1.00 38.67  ? 3   GLU   C O     1 
ATOM   3489  C  CB    . GLU   B 1  3   ? -21.240 44.861  5.721    1.00 42.37  ? 3   GLU   C CB    1 
ATOM   3490  C  CG    . GLU   B 1  3   ? -21.054 46.224  6.340    1.00 36.75  ? 3   GLU   C CG    1 
ATOM   3491  C  CD    . GLU   B 1  3   ? -22.008 47.248  5.756    1.00 42.54  ? 3   GLU   C CD    1 
ATOM   3492  O  OE1   . GLU   B 1  3   ? -22.620 46.975  4.694    1.00 39.31  ? 3   GLU   C OE1   1 
ATOM   3493  O  OE2   . GLU   B 1  3   ? -22.158 48.319  6.376    1.00 46.21  ? 3   GLU   C OE2   1 
ATOM   3494  N  N     . CYS   B 1  4   ? -19.550 42.279  5.013    1.00 37.34  ? 4   CYS   C N     1 
ATOM   3495  C  CA    A CYS   B 1  4   ? -19.499 40.826  4.943    0.44 37.22  ? 4   CYS   C CA    1 
ATOM   3496  C  CA    B CYS   B 1  4   ? -19.502 40.820  4.944    0.56 37.25  ? 4   CYS   C CA    1 
ATOM   3497  C  C     . CYS   B 1  4   ? -19.635 40.274  6.355    1.00 30.74  ? 4   CYS   C C     1 
ATOM   3498  O  O     . CYS   B 1  4   ? -18.934 40.722  7.261    1.00 33.31  ? 4   CYS   C O     1 
ATOM   3499  C  CB    A CYS   B 1  4   ? -18.183 40.368  4.307    0.44 36.56  ? 4   CYS   C CB    1 
ATOM   3500  C  CB    B CYS   B 1  4   ? -18.192 40.308  4.324    0.56 36.53  ? 4   CYS   C CB    1 
ATOM   3501  S  SG    A CYS   B 1  4   ? -18.037 38.613  4.071    0.44 39.57  ? 4   CYS   C SG    1 
ATOM   3502  S  SG    B CYS   B 1  4   ? -17.990 40.605  2.558    0.56 36.61  ? 4   CYS   C SG    1 
ATOM   3503  N  N     . ILE   B 1  5   ? -20.536 39.317  6.547    1.00 28.82  ? 5   ILE   C N     1 
ATOM   3504  C  CA    . ILE   B 1  5   ? -20.774 38.717  7.854    1.00 27.63  ? 5   ILE   C CA    1 
ATOM   3505  C  C     . ILE   B 1  5   ? -20.219 37.301  7.845    1.00 29.62  ? 5   ILE   C C     1 
ATOM   3506  O  O     . ILE   B 1  5   ? -20.621 36.462  7.018    1.00 31.00  ? 5   ILE   C O     1 
ATOM   3507  C  CB    . ILE   B 1  5   ? -22.264 38.696  8.223    1.00 30.53  ? 5   ILE   C CB    1 
ATOM   3508  C  CG1   . ILE   B 1  5   ? -22.794 40.101  8.469    1.00 31.12  ? 5   ILE   C CG1   1 
ATOM   3509  C  CG2   . ILE   B 1  5   ? -22.482 37.805  9.472    1.00 30.98  ? 5   ILE   C CG2   1 
ATOM   3510  C  CD1   . ILE   B 1  5   ? -24.305 40.133  8.675    1.00 30.45  ? 5   ILE   C CD1   1 
ATOM   3511  N  N     . SER   B 1  6   ? -19.313 37.028  8.773    1.00 28.30  ? 6   SER   C N     1 
ATOM   3512  C  CA    . SER   B 1  6   ? -18.740 35.699  8.901    1.00 26.98  ? 6   SER   C CA    1 
ATOM   3513  C  C     . SER   B 1  6   ? -19.559 34.919  9.905    1.00 33.31  ? 6   SER   C C     1 
ATOM   3514  O  O     . SER   B 1  6   ? -20.073 35.486  10.876   1.00 32.94  ? 6   SER   C O     1 
ATOM   3515  C  CB    . SER   B 1  6   ? -17.280 35.756  9.334    1.00 27.24  ? 6   SER   C CB    1 
ATOM   3516  O  OG    . SER   B 1  6   ? -16.494 36.331  8.305    1.00 26.57  ? 6   SER   C OG    1 
ATOM   3517  N  N     . ILE   B 1  7   ? -19.716 33.627  9.640    1.00 27.08  ? 7   ILE   C N     1 
ATOM   3518  C  CA    . ILE   B 1  7   ? -20.450 32.730  10.509   1.00 24.85  ? 7   ILE   C CA    1 
ATOM   3519  C  C     . ILE   B 1  7   ? -19.558 31.523  10.718   1.00 26.69  ? 7   ILE   C C     1 
ATOM   3520  O  O     . ILE   B 1  7   ? -19.180 30.857  9.750    1.00 32.35  ? 7   ILE   C O     1 
ATOM   3521  C  CB    . ILE   B 1  7   ? -21.810 32.333  9.907    1.00 25.39  ? 7   ILE   C CB    1 
ATOM   3522  C  CG1   . ILE   B 1  7   ? -22.550 33.573  9.399    1.00 25.49  ? 7   ILE   C CG1   1 
ATOM   3523  C  CG2   . ILE   B 1  7   ? -22.682 31.570  10.926   1.00 21.16  ? 7   ILE   C CG2   1 
ATOM   3524  C  CD1   . ILE   B 1  7   ? -24.002 33.306  9.037    1.00 25.54  ? 7   ILE   C CD1   1 
ATOM   3525  N  N     . HIS   B 1  8   ? -19.186 31.267  11.963   1.00 29.02  ? 8   HIS   C N     1 
ATOM   3526  C  CA    . HIS   B 1  8   ? -18.280 30.178  12.309   1.00 24.03  ? 8   HIS   C CA    1 
ATOM   3527  C  C     . HIS   B 1  8   ? -19.066 29.124  13.077   1.00 29.12  ? 8   HIS   C C     1 
ATOM   3528  O  O     . HIS   B 1  8   ? -19.643 29.424  14.123   1.00 30.26  ? 8   HIS   C O     1 
ATOM   3529  C  CB    . HIS   B 1  8   ? -17.102 30.708  13.121   1.00 23.61  ? 8   HIS   C CB    1 
ATOM   3530  C  CG    . HIS   B 1  8   ? -16.413 31.873  12.480   1.00 26.14  ? 8   HIS   C CG    1 
ATOM   3531  N  ND1   . HIS   B 1  8   ? -15.390 31.727  11.564   1.00 26.28  ? 8   HIS   C ND1   1 
ATOM   3532  C  CD2   . HIS   B 1  8   ? -16.616 33.204  12.603   1.00 26.52  ? 8   HIS   C CD2   1 
ATOM   3533  C  CE1   . HIS   B 1  8   ? -14.972 32.915  11.176   1.00 22.87  ? 8   HIS   C CE1   1 
ATOM   3534  N  NE2   . HIS   B 1  8   ? -15.706 33.830  11.784   1.00 31.68  ? 8   HIS   C NE2   1 
ATOM   3535  N  N     . VAL   B 1  9   ? -19.069 27.893  12.568   1.00 23.96  ? 9   VAL   C N     1 
ATOM   3536  C  CA    . VAL   B 1  9   ? -20.019 26.862  12.962   1.00 22.78  ? 9   VAL   C CA    1 
ATOM   3537  C  C     . VAL   B 1  9   ? -19.251 25.603  13.360   1.00 30.14  ? 9   VAL   C C     1 
ATOM   3538  O  O     . VAL   B 1  9   ? -18.480 25.061  12.554   1.00 34.14  ? 9   VAL   C O     1 
ATOM   3539  C  CB    . VAL   B 1  9   ? -20.991 26.546  11.814   1.00 23.07  ? 9   VAL   C CB    1 
ATOM   3540  C  CG1   . VAL   B 1  9   ? -21.815 25.308  12.138   1.00 28.19  ? 9   VAL   C CG1   1 
ATOM   3541  C  CG2   . VAL   B 1  9   ? -21.855 27.731  11.506   1.00 25.81  ? 9   VAL   C CG2   1 
ATOM   3542  N  N     . GLY   B 1  10  ? -19.496 25.107  14.574   1.00 25.87  ? 10  GLY   C N     1 
ATOM   3543  C  CA    . GLY   B 1  10  ? -18.784 23.944  15.065   1.00 25.00  ? 10  GLY   C CA    1 
ATOM   3544  C  C     . GLY   B 1  10  ? -17.354 24.248  15.506   1.00 30.16  ? 10  GLY   C C     1 
ATOM   3545  O  O     . GLY   B 1  10  ? -16.829 25.363  15.355   1.00 29.44  ? 10  GLY   C O     1 
ATOM   3546  N  N     . GLN   B 1  11  ? -16.694 23.212  16.043   1.00 21.09  ? 11  GLN   C N     1 
ATOM   3547  C  CA    . GLN   B 1  11  ? -15.337 23.400  16.559   1.00 25.14  ? 11  GLN   C CA    1 
ATOM   3548  C  C     . GLN   B 1  11  ? -14.402 23.985  15.494   1.00 28.32  ? 11  GLN   C C     1 
ATOM   3549  O  O     . GLN   B 1  11  ? -13.769 25.026  15.710   1.00 26.72  ? 11  GLN   C O     1 
ATOM   3550  C  CB    . GLN   B 1  11  ? -14.779 22.083  17.099   1.00 19.50  ? 11  GLN   C CB    1 
ATOM   3551  C  CG    . GLN   B 1  11  ? -13.347 22.262  17.576   1.00 32.99  ? 11  GLN   C CG    1 
ATOM   3552  C  CD    . GLN   B 1  11  ? -12.752 21.021  18.170   1.00 34.21  ? 11  GLN   C CD    1 
ATOM   3553  O  OE1   . GLN   B 1  11  ? -13.240 20.508  19.179   1.00 34.37  ? 11  GLN   C OE1   1 
ATOM   3554  N  NE2   . GLN   B 1  11  ? -11.680 20.526  17.553   1.00 26.96  ? 11  GLN   C NE2   1 
ATOM   3555  N  N     . ALA   B 1  12  ? -14.299 23.313  14.336   1.00 25.27  ? 12  ALA   C N     1 
ATOM   3556  C  CA    . ALA   B 1  12  ? -13.396 23.753  13.279   1.00 19.60  ? 12  ALA   C CA    1 
ATOM   3557  C  C     . ALA   B 1  12  ? -13.729 25.161  12.834   1.00 24.94  ? 12  ALA   C C     1 
ATOM   3558  O  O     . ALA   B 1  12  ? -12.854 26.034  12.784   1.00 28.05  ? 12  ALA   C O     1 
ATOM   3559  C  CB    . ALA   B 1  12  ? -13.449 22.791  12.086   1.00 17.37  ? 12  ALA   C CB    1 
ATOM   3560  N  N     . GLY   B 1  13  ? -14.992 25.401  12.487   1.00 26.22  ? 13  GLY   C N     1 
ATOM   3561  C  CA    . GLY   B 1  13  ? -15.383 26.741  12.091   1.00 22.39  ? 13  GLY   C CA    1 
ATOM   3562  C  C     . GLY   B 1  13  ? -15.065 27.760  13.160   1.00 25.04  ? 13  GLY   C C     1 
ATOM   3563  O  O     . GLY   B 1  13  ? -14.585 28.860  12.862   1.00 26.43  ? 13  GLY   C O     1 
ATOM   3564  N  N     . VAL   B 1  14  ? -15.293 27.397  14.423   1.00 23.50  ? 14  VAL   C N     1 
ATOM   3565  C  CA    . VAL   B 1  14  ? -15.011 28.333  15.501   1.00 28.41  ? 14  VAL   C CA    1 
ATOM   3566  C  C     . VAL   B 1  14  ? -13.516 28.524  15.675   1.00 28.87  ? 14  VAL   C C     1 
ATOM   3567  O  O     . VAL   B 1  14  ? -13.055 29.643  15.924   1.00 31.63  ? 14  VAL   C O     1 
ATOM   3568  C  CB    . VAL   B 1  14  ? -15.658 27.888  16.818   1.00 23.60  ? 14  VAL   C CB    1 
ATOM   3569  C  CG1   . VAL   B 1  14  ? -14.926 28.523  17.941   1.00 20.12  ? 14  VAL   C CG1   1 
ATOM   3570  C  CG2   . VAL   B 1  14  ? -17.110 28.334  16.852   1.00 25.40  ? 14  VAL   C CG2   1 
ATOM   3571  N  N     . GLN   B 1  15  ? -12.734 27.446  15.567   1.00 27.58  ? 15  GLN   C N     1 
ATOM   3572  C  CA    . GLN   B 1  15  ? -11.300 27.572  15.838   1.00 31.24  ? 15  GLN   C CA    1 
ATOM   3573  C  C     . GLN   B 1  15  ? -10.553 28.200  14.659   1.00 34.68  ? 15  GLN   C C     1 
ATOM   3574  O  O     . GLN   B 1  15  ? -9.674  29.052  14.851   1.00 33.86  ? 15  GLN   C O     1 
ATOM   3575  C  CB    . GLN   B 1  15  ? -10.715 26.215  16.211   1.00 24.69  ? 15  GLN   C CB    1 
ATOM   3576  C  CG    . GLN   B 1  15  ? -11.264 25.707  17.523   1.00 26.38  ? 15  GLN   C CG    1 
ATOM   3577  C  CD    . GLN   B 1  15  ? -10.463 24.564  18.115   1.00 32.37  ? 15  GLN   C CD    1 
ATOM   3578  O  OE1   . GLN   B 1  15  ? -9.696  23.917  17.417   1.00 35.90  ? 15  GLN   C OE1   1 
ATOM   3579  N  NE2   . GLN   B 1  15  ? -10.631 24.318  19.414   1.00 41.01  ? 15  GLN   C NE2   1 
ATOM   3580  N  N     . ILE   B 1  16  ? -10.902 27.832  13.429   1.00 30.01  ? 16  ILE   C N     1 
ATOM   3581  C  CA    . ILE   B 1  16  ? -10.435 28.620  12.291   1.00 34.92  ? 16  ILE   C CA    1 
ATOM   3582  C  C     . ILE   B 1  16  ? -10.855 30.083  12.477   1.00 32.24  ? 16  ILE   C C     1 
ATOM   3583  O  O     . ILE   B 1  16  ? -10.043 31.006  12.337   1.00 28.41  ? 16  ILE   C O     1 
ATOM   3584  C  CB    . ILE   B 1  16  ? -10.951 27.997  10.972   1.00 30.14  ? 16  ILE   C CB    1 
ATOM   3585  C  CG1   . ILE   B 1  16  ? -10.334 26.609  10.769   1.00 25.55  ? 16  ILE   C CG1   1 
ATOM   3586  C  CG2   . ILE   B 1  16  ? -10.617 28.827  9.773    1.00 25.91  ? 16  ILE   C CG2   1 
ATOM   3587  C  CD1   . ILE   B 1  16  ? -10.842 25.906  9.530    1.00 26.23  ? 16  ILE   C CD1   1 
ATOM   3588  N  N     . GLY   B 1  17  ? -12.117 30.303  12.875   1.00 34.92  ? 17  GLY   C N     1 
ATOM   3589  C  CA    . GLY   B 1  17  ? -12.583 31.655  13.178   1.00 28.01  ? 17  GLY   C CA    1 
ATOM   3590  C  C     . GLY   B 1  17  ? -11.656 32.436  14.091   1.00 33.59  ? 17  GLY   C C     1 
ATOM   3591  O  O     . GLY   B 1  17  ? -11.378 33.614  13.847   1.00 36.57  ? 17  GLY   C O     1 
ATOM   3592  N  N     . ASN   B 1  18  ? -11.160 31.800  15.157   1.00 28.46  ? 18  ASN   C N     1 
ATOM   3593  C  CA    . ASN   B 1  18  ? -10.265 32.503  16.071   1.00 30.99  ? 18  ASN   C CA    1 
ATOM   3594  C  C     . ASN   B 1  18  ? -8.985  32.943  15.368   1.00 33.08  ? 18  ASN   C C     1 
ATOM   3595  O  O     . ASN   B 1  18  ? -8.533  34.080  15.531   1.00 34.82  ? 18  ASN   C O     1 
ATOM   3596  C  CB    . ASN   B 1  18  ? -9.913  31.620  17.268   1.00 37.89  ? 18  ASN   C CB    1 
ATOM   3597  C  CG    . ASN   B 1  18  ? -11.103 31.276  18.115   1.00 30.12  ? 18  ASN   C CG    1 
ATOM   3598  O  OD1   . ASN   B 1  18  ? -11.976 32.101  18.352   1.00 35.46  ? 18  ASN   C OD1   1 
ATOM   3599  N  ND2   . ASN   B 1  18  ? -11.148 30.042  18.575   1.00 32.67  ? 18  ASN   C ND2   1 
ATOM   3600  N  N     . ALA   B 1  19  ? -8.367  32.031  14.615   1.00 30.85  ? 19  ALA   C N     1 
ATOM   3601  C  CA    . ALA   B 1  19  ? -7.167  32.357  13.860   1.00 30.38  ? 19  ALA   C CA    1 
ATOM   3602  C  C     . ALA   B 1  19  ? -7.401  33.533  12.911   1.00 37.62  ? 19  ALA   C C     1 
ATOM   3603  O  O     . ALA   B 1  19  ? -6.620  34.494  12.889   1.00 31.49  ? 19  ALA   C O     1 
ATOM   3604  C  CB    . ALA   B 1  19  ? -6.707  31.122  13.091   1.00 30.33  ? 19  ALA   C CB    1 
ATOM   3605  N  N     . CYS   B 1  20  ? -8.475  33.471  12.113   1.00 34.15  ? 20  CYS   C N     1 
ATOM   3606  C  CA    . CYS   B 1  20  ? -8.753  34.532  11.149   1.00 31.32  ? 20  CYS   C CA    1 
ATOM   3607  C  C     . CYS   B 1  20  ? -8.912  35.882  11.832   1.00 37.05  ? 20  CYS   C C     1 
ATOM   3608  O  O     . CYS   B 1  20  ? -8.359  36.891  11.376   1.00 38.00  ? 20  CYS   C O     1 
ATOM   3609  C  CB    . CYS   B 1  20  ? -10.007 34.196  10.348   1.00 34.87  ? 20  CYS   C CB    1 
ATOM   3610  S  SG    . CYS   B 1  20  ? -9.774  32.869  9.176    1.00 46.82  ? 20  CYS   C SG    1 
ATOM   3611  N  N     . TRP   B 1  21  ? -9.676  35.932  12.925   1.00 32.45  ? 21  TRP   C N     1 
ATOM   3612  C  CA    . TRP   B 1  21  ? -9.963  37.245  13.487   1.00 34.83  ? 21  TRP   C CA    1 
ATOM   3613  C  C     . TRP   B 1  21  ? -8.749  37.811  14.195   1.00 33.08  ? 21  TRP   C C     1 
ATOM   3614  O  O     . TRP   B 1  21  ? -8.503  39.018  14.110   1.00 35.30  ? 21  TRP   C O     1 
ATOM   3615  C  CB    . TRP   B 1  21  ? -11.206 37.195  14.388   1.00 29.84  ? 21  TRP   C CB    1 
ATOM   3616  C  CG    . TRP   B 1  21  ? -12.444 37.116  13.527   1.00 31.35  ? 21  TRP   C CG    1 
ATOM   3617  C  CD1   . TRP   B 1  21  ? -13.174 36.003  13.233   1.00 28.80  ? 21  TRP   C CD1   1 
ATOM   3618  C  CD2   . TRP   B 1  21  ? -13.032 38.190  12.774   1.00 34.28  ? 21  TRP   C CD2   1 
ATOM   3619  N  NE1   . TRP   B 1  21  ? -14.199 36.316  12.379   1.00 32.92  ? 21  TRP   C NE1   1 
ATOM   3620  C  CE2   . TRP   B 1  21  ? -14.132 37.653  12.073   1.00 32.90  ? 21  TRP   C CE2   1 
ATOM   3621  C  CE3   . TRP   B 1  21  ? -12.748 39.555  12.643   1.00 27.40  ? 21  TRP   C CE3   1 
ATOM   3622  C  CZ2   . TRP   B 1  21  ? -14.953 38.434  11.257   1.00 25.97  ? 21  TRP   C CZ2   1 
ATOM   3623  C  CZ3   . TRP   B 1  21  ? -13.563 40.327  11.817   1.00 34.89  ? 21  TRP   C CZ3   1 
ATOM   3624  C  CH2   . TRP   B 1  21  ? -14.647 39.760  11.132   1.00 28.76  ? 21  TRP   C CH2   1 
ATOM   3625  N  N     . GLU   B 1  22  ? -7.944  36.963  14.837   1.00 29.01  ? 22  GLU   C N     1 
ATOM   3626  C  CA    . GLU   B 1  22  ? -6.676  37.442  15.375   1.00 31.63  ? 22  GLU   C CA    1 
ATOM   3627  C  C     . GLU   B 1  22  ? -5.781  37.970  14.260   1.00 35.78  ? 22  GLU   C C     1 
ATOM   3628  O  O     . GLU   B 1  22  ? -5.182  39.043  14.382   1.00 34.10  ? 22  GLU   C O     1 
ATOM   3629  C  CB    . GLU   B 1  22  ? -5.963  36.335  16.137   1.00 31.80  ? 22  GLU   C CB    1 
ATOM   3630  C  CG    . GLU   B 1  22  ? -4.546  36.736  16.498   1.00 40.20  ? 22  GLU   C CG    1 
ATOM   3631  C  CD    . GLU   B 1  22  ? -3.842  35.698  17.339   1.00 48.88  ? 22  GLU   C CD    1 
ATOM   3632  O  OE1   . GLU   B 1  22  ? -3.953  34.489  17.027   1.00 54.20  ? 22  GLU   C OE1   1 
ATOM   3633  O  OE2   . GLU   B 1  22  ? -3.181  36.097  18.319   1.00 50.52  ? 22  GLU   C OE2   1 
ATOM   3634  N  N     . LEU   B 1  23  ? -5.684  37.225  13.158   1.00 33.78  ? 23  LEU   C N     1 
ATOM   3635  C  CA    . LEU   B 1  23  ? -4.889  37.680  12.028   1.00 37.51  ? 23  LEU   C CA    1 
ATOM   3636  C  C     . LEU   B 1  23  ? -5.426  39.003  11.481   1.00 43.95  ? 23  LEU   C C     1 
ATOM   3637  O  O     . LEU   B 1  23  ? -4.647  39.903  11.121   1.00 33.11  ? 23  LEU   C O     1 
ATOM   3638  C  CB    . LEU   B 1  23  ? -4.855  36.594  10.946   1.00 28.26  ? 23  LEU   C CB    1 
ATOM   3639  C  CG    . LEU   B 1  23  ? -3.816  36.895  9.876    1.00 36.66  ? 23  LEU   C CG    1 
ATOM   3640  C  CD1   . LEU   B 1  23  ? -2.438  37.011  10.530   1.00 41.44  ? 23  LEU   C CD1   1 
ATOM   3641  C  CD2   . LEU   B 1  23  ? -3.831  35.863  8.757    1.00 36.23  ? 23  LEU   C CD2   1 
ATOM   3642  N  N     . TYR   B 1  24  ? -6.758  39.148  11.428   1.00 38.47  ? 24  TYR   C N     1 
ATOM   3643  C  CA    . TYR   B 1  24  ? -7.352  40.412  10.998   1.00 31.38  ? 24  TYR   C CA    1 
ATOM   3644  C  C     . TYR   B 1  24  ? -6.938  41.561  11.915   1.00 33.50  ? 24  TYR   C C     1 
ATOM   3645  O  O     . TYR   B 1  24  ? -6.496  42.617  11.447   1.00 35.47  ? 24  TYR   C O     1 
ATOM   3646  C  CB    . TYR   B 1  24  ? -8.868  40.288  10.972   1.00 34.46  ? 24  TYR   C CB    1 
ATOM   3647  C  CG    . TYR   B 1  24  ? -9.428  39.375  9.915    1.00 39.24  ? 24  TYR   C CG    1 
ATOM   3648  C  CD1   . TYR   B 1  24  ? -8.669  38.996  8.812    1.00 31.03  ? 24  TYR   C CD1   1 
ATOM   3649  C  CD2   . TYR   B 1  24  ? -10.730 38.886  10.018   1.00 37.45  ? 24  TYR   C CD2   1 
ATOM   3650  C  CE1   . TYR   B 1  24  ? -9.192  38.154  7.843    1.00 28.49  ? 24  TYR   C CE1   1 
ATOM   3651  C  CE2   . TYR   B 1  24  ? -11.264 38.059  9.048    1.00 37.07  ? 24  TYR   C CE2   1 
ATOM   3652  C  CZ    . TYR   B 1  24  ? -10.489 37.702  7.961    1.00 35.81  ? 24  TYR   C CZ    1 
ATOM   3653  O  OH    . TYR   B 1  24  ? -11.013 36.878  7.002    1.00 34.87  ? 24  TYR   C OH    1 
ATOM   3654  N  N     . CYS   B 1  25  ? -7.104  41.388  13.229   1.00 35.51  ? 25  CYS   C N     1 
ATOM   3655  C  CA    . CYS   B 1  25  ? -6.779  42.469  14.164   1.00 39.90  ? 25  CYS   C CA    1 
ATOM   3656  C  C     . CYS   B 1  25  ? -5.324  42.894  14.026   1.00 38.02  ? 25  CYS   C C     1 
ATOM   3657  O  O     . CYS   B 1  25  ? -5.011  44.090  14.092   1.00 36.98  ? 25  CYS   C O     1 
ATOM   3658  C  CB    . CYS   B 1  25  ? -7.087  42.052  15.609   1.00 31.43  ? 25  CYS   C CB    1 
ATOM   3659  S  SG    . CYS   B 1  25  ? -8.858  41.915  16.009   1.00 33.26  ? 25  CYS   C SG    1 
ATOM   3660  N  N     . LEU   B 1  26  ? -4.424  41.924  13.810   1.00 38.58  ? 26  LEU   C N     1 
ATOM   3661  C  CA    . LEU   B 1  26  ? -3.008  42.220  13.620   1.00 36.18  ? 26  LEU   C CA    1 
ATOM   3662  C  C     . LEU   B 1  26  ? -2.766  42.938  12.301   1.00 34.62  ? 26  LEU   C C     1 
ATOM   3663  O  O     . LEU   B 1  26  ? -1.961  43.873  12.233   1.00 42.90  ? 26  LEU   C O     1 
ATOM   3664  C  CB    . LEU   B 1  26  ? -2.187  40.927  13.691   1.00 45.19  ? 26  LEU   C CB    1 
ATOM   3665  C  CG    . LEU   B 1  26  ? -1.998  40.267  15.074   1.00 48.45  ? 26  LEU   C CG    1 
ATOM   3666  C  CD1   . LEU   B 1  26  ? -1.628  38.778  14.951   1.00 43.73  ? 26  LEU   C CD1   1 
ATOM   3667  C  CD2   . LEU   B 1  26  ? -0.929  40.988  15.865   1.00 39.26  ? 26  LEU   C CD2   1 
ATOM   3668  N  N     . GLU   B 1  27  ? -3.455  42.525  11.241   1.00 38.20  ? 27  GLU   C N     1 
ATOM   3669  C  CA    . GLU   B 1  27  ? -3.315  43.218  9.965    1.00 33.03  ? 27  GLU   C CA    1 
ATOM   3670  C  C     . GLU   B 1  27  ? -3.848  44.643  10.024   1.00 35.16  ? 27  GLU   C C     1 
ATOM   3671  O  O     . GLU   B 1  27  ? -3.343  45.524  9.319    1.00 32.44  ? 27  GLU   C O     1 
ATOM   3672  C  CB    . GLU   B 1  27  ? -4.034  42.445  8.865    1.00 33.65  ? 27  GLU   C CB    1 
ATOM   3673  C  CG    . GLU   B 1  27  ? -3.304  41.206  8.412    1.00 27.68  ? 27  GLU   C CG    1 
ATOM   3674  C  CD    . GLU   B 1  27  ? -3.988  40.525  7.260    1.00 30.26  ? 27  GLU   C CD    1 
ATOM   3675  O  OE1   . GLU   B 1  27  ? -4.986  41.046  6.722    1.00 33.19  ? 27  GLU   C OE1   1 
ATOM   3676  O  OE2   . GLU   B 1  27  ? -3.527  39.446  6.889    1.00 37.92  ? 27  GLU   C OE2   1 
ATOM   3677  N  N     . HIS   B 1  28  ? -4.851  44.902  10.850   1.00 36.63  ? 28  HIS   C N     1 
ATOM   3678  C  CA    . HIS   B 1  28  ? -5.514  46.198  10.818   1.00 40.26  ? 28  HIS   C CA    1 
ATOM   3679  C  C     . HIS   B 1  28  ? -5.120  47.136  11.962   1.00 44.97  ? 28  HIS   C C     1 
ATOM   3680  O  O     . HIS   B 1  28  ? -5.669  48.241  12.053   1.00 42.63  ? 28  HIS   C O     1 
ATOM   3681  C  CB    . HIS   B 1  28  ? -7.032  45.995  10.803   1.00 40.12  ? 28  HIS   C CB    1 
ATOM   3682  C  CG    . HIS   B 1  28  ? -7.572  45.492  9.491    1.00 36.16  ? 28  HIS   C CG    1 
ATOM   3683  N  ND1   . HIS   B 1  28  ? -7.412  46.178  8.306    1.00 30.47  ? 28  HIS   C ND1   1 
ATOM   3684  C  CD2   . HIS   B 1  28  ? -8.292  44.385  9.189    1.00 27.88  ? 28  HIS   C CD2   1 
ATOM   3685  C  CE1   . HIS   B 1  28  ? -8.011  45.520  7.332    1.00 37.23  ? 28  HIS   C CE1   1 
ATOM   3686  N  NE2   . HIS   B 1  28  ? -8.547  44.425  7.840    1.00 41.81  ? 28  HIS   C NE2   1 
ATOM   3687  N  N     . GLY   B 1  29  ? -4.183  46.755  12.825   1.00 29.60  ? 29  GLY   C N     1 
ATOM   3688  C  CA    . GLY   B 1  29  ? -3.879  47.662  13.911   1.00 26.26  ? 29  GLY   C CA    1 
ATOM   3689  C  C     . GLY   B 1  29  ? -4.924  47.708  15.008   1.00 40.45  ? 29  GLY   C C     1 
ATOM   3690  O  O     . GLY   B 1  29  ? -5.009  48.707  15.722   1.00 39.14  ? 29  GLY   C O     1 
ATOM   3691  N  N     . ILE   B 1  30  ? -5.719  46.645  15.166   1.00 35.41  ? 30  ILE   C N     1 
ATOM   3692  C  CA    . ILE   B 1  30  ? -6.778  46.573  16.163   1.00 34.84  ? 30  ILE   C CA    1 
ATOM   3693  C  C     . ILE   B 1  30  ? -6.265  45.795  17.370   1.00 43.10  ? 30  ILE   C C     1 
ATOM   3694  O  O     . ILE   B 1  30  ? -5.750  44.674  17.230   1.00 42.81  ? 30  ILE   C O     1 
ATOM   3695  C  CB    . ILE   B 1  30  ? -8.043  45.916  15.577   1.00 42.44  ? 30  ILE   C CB    1 
ATOM   3696  C  CG1   . ILE   B 1  30  ? -8.622  46.774  14.445   1.00 39.21  ? 30  ILE   C CG1   1 
ATOM   3697  C  CG2   . ILE   B 1  30  ? -9.074  45.692  16.651   1.00 34.16  ? 30  ILE   C CG2   1 
ATOM   3698  C  CD1   . ILE   B 1  30  ? -9.474  45.991  13.491   1.00 24.27  ? 30  ILE   C CD1   1 
ATOM   3699  N  N     . GLN   B 1  31  ? -6.400  46.384  18.558   1.00 40.67  ? 31  GLN   C N     1 
ATOM   3700  C  CA    . GLN   B 1  31  ? -5.933  45.712  19.756   1.00 41.49  ? 31  GLN   C CA    1 
ATOM   3701  C  C     . GLN   B 1  31  ? -6.962  44.711  20.253   1.00 43.41  ? 31  GLN   C C     1 
ATOM   3702  O  O     . GLN   B 1  31  ? -8.134  44.761  19.876   1.00 55.47  ? 31  GLN   C O     1 
ATOM   3703  C  CB    . GLN   B 1  31  ? -5.616  46.722  20.845   1.00 48.41  ? 31  GLN   C CB    1 
ATOM   3704  C  CG    . GLN   B 1  31  ? -4.300  47.460  20.612   1.00 44.16  ? 31  GLN   C CG    1 
ATOM   3705  C  CD    . GLN   B 1  31  ? -4.413  48.930  20.953   1.00 64.15  ? 31  GLN   C CD    1 
ATOM   3706  O  OE1   . GLN   B 1  31  ? -5.393  49.364  21.588   1.00 64.54  ? 31  GLN   C OE1   1 
ATOM   3707  N  NE2   . GLN   B 1  31  ? -3.424  49.717  20.521   1.00 62.34  ? 31  GLN   C NE2   1 
ATOM   3708  N  N     . PRO   B 1  32  ? -6.533  43.763  21.081   1.00 38.27  ? 32  PRO   C N     1 
ATOM   3709  C  CA    . PRO   B 1  32  ? -7.464  42.741  21.593   1.00 42.50  ? 32  PRO   C CA    1 
ATOM   3710  C  C     . PRO   B 1  32  ? -8.691  43.285  22.333   1.00 47.12  ? 32  PRO   C C     1 
ATOM   3711  O  O     . PRO   B 1  32  ? -9.602  42.501  22.627   1.00 50.52  ? 32  PRO   C O     1 
ATOM   3712  C  CB    . PRO   B 1  32  ? -6.576  41.912  22.526   1.00 37.31  ? 32  PRO   C CB    1 
ATOM   3713  C  CG    . PRO   B 1  32  ? -5.206  42.033  21.889   1.00 37.97  ? 32  PRO   C CG    1 
ATOM   3714  C  CD    . PRO   B 1  32  ? -5.124  43.432  21.348   1.00 33.26  ? 32  PRO   C CD    1 
ATOM   3715  N  N     . ASP   B 1  33  ? -8.757  44.576  22.655   1.00 47.09  ? 33  ASP   C N     1 
ATOM   3716  C  CA    . ASP   B 1  33  ? -9.945  45.119  23.300   1.00 51.89  ? 33  ASP   C CA    1 
ATOM   3717  C  C     . ASP   B 1  33  ? -10.860 45.840  22.318   1.00 54.44  ? 33  ASP   C C     1 
ATOM   3718  O  O     . ASP   B 1  33  ? -11.942 46.296  22.717   1.00 50.29  ? 33  ASP   C O     1 
ATOM   3719  C  CB    . ASP   B 1  33  ? -9.556  46.061  24.441   1.00 42.78  ? 33  ASP   C CB    1 
ATOM   3720  C  CG    . ASP   B 1  33  ? -9.031  47.390  23.943   1.00 54.44  ? 33  ASP   C CG    1 
ATOM   3721  O  OD1   . ASP   B 1  33  ? -8.230  47.392  22.986   1.00 57.29  ? 33  ASP   C OD1   1 
ATOM   3722  O  OD2   . ASP   B 1  33  ? -9.431  48.436  24.504   1.00 65.59  ? 33  ASP   C OD2   1 
ATOM   3723  N  N     . GLY   B 1  34  ? -10.450 45.946  21.051   1.00 46.55  ? 34  GLY   C N     1 
ATOM   3724  C  CA    . GLY   B 1  34  ? -11.250 46.526  19.989   1.00 40.62  ? 34  GLY   C CA    1 
ATOM   3725  C  C     . GLY   B 1  34  ? -10.771 47.876  19.518   1.00 50.65  ? 34  GLY   C C     1 
ATOM   3726  O  O     . GLY   B 1  34  ? -11.280 48.371  18.497   1.00 51.87  ? 34  GLY   C O     1 
ATOM   3727  N  N     . GLN   B 1  35  ? -9.814  48.492  20.222   1.00 52.65  ? 35  GLN   C N     1 
ATOM   3728  C  CA    . GLN   B 1  35  ? -9.398  49.855  19.907   1.00 46.83  ? 35  GLN   C CA    1 
ATOM   3729  C  C     . GLN   B 1  35  ? -8.402  49.841  18.755   1.00 45.91  ? 35  GLN   C C     1 
ATOM   3730  O  O     . GLN   B 1  35  ? -7.471  49.032  18.725   1.00 49.42  ? 35  GLN   C O     1 
ATOM   3731  C  CB    . GLN   B 1  35  ? -8.772  50.557  21.124   1.00 38.02  ? 35  GLN   C CB    1 
ATOM   3732  C  CG    . GLN   B 1  35  ? -9.693  50.857  22.293   1.00 35.62  ? 35  GLN   C CG    1 
ATOM   3733  C  CD    . GLN   B 1  35  ? -10.782 51.881  21.977   1.00 44.20  ? 35  GLN   C CD    1 
ATOM   3734  O  OE1   . GLN   B 1  35  ? -11.979 51.606  22.152   1.00 41.71  ? 35  GLN   C OE1   1 
ATOM   3735  N  NE2   . GLN   B 1  35  ? -10.376 53.074  21.527   1.00 32.69  ? 35  GLN   C NE2   1 
ATOM   3736  N  N     . MET   B 1  36  ? -8.612  50.758  17.807   1.00 45.01  ? 36  MET   C N     1 
ATOM   3737  C  CA    . MET   B 1  36  ? -7.780  50.940  16.621   1.00 39.74  ? 36  MET   C CA    1 
ATOM   3738  C  C     . MET   B 1  36  ? -7.305  52.389  16.611   1.00 46.56  ? 36  MET   C C     1 
ATOM   3739  O  O     . MET   B 1  36  ? -7.899  53.239  15.930   1.00 42.25  ? 36  MET   C O     1 
ATOM   3740  C  CB    . MET   B 1  36  ? -8.571  50.604  15.359   1.00 47.67  ? 36  MET   C CB    1 
ATOM   3741  C  CG    . MET   B 1  36  ? -7.827  50.718  14.027   1.00 44.44  ? 36  MET   C CG    1 
ATOM   3742  S  SD    . MET   B 1  36  ? -8.994  50.122  12.781   1.00 47.02  ? 36  MET   C SD    1 
ATOM   3743  C  CE    . MET   B 1  36  ? -7.958  50.123  11.328   1.00 37.70  ? 36  MET   C CE    1 
ATOM   3744  N  N     . PRO   B 1  37  ? -6.238  52.712  17.355   1.00 46.70  ? 37  PRO   C N     1 
ATOM   3745  C  CA    . PRO   B 1  37  ? -5.828  54.121  17.461   1.00 46.93  ? 37  PRO   C CA    1 
ATOM   3746  C  C     . PRO   B 1  37  ? -5.749  54.834  16.120   1.00 51.08  ? 37  PRO   C C     1 
ATOM   3747  O  O     . PRO   B 1  37  ? -6.098  56.021  16.035   1.00 47.53  ? 37  PRO   C O     1 
ATOM   3748  C  CB    . PRO   B 1  37  ? -4.460  54.027  18.145   1.00 35.14  ? 37  PRO   C CB    1 
ATOM   3749  C  CG    . PRO   B 1  37  ? -4.042  52.604  18.001   1.00 41.68  ? 37  PRO   C CG    1 
ATOM   3750  C  CD    . PRO   B 1  37  ? -5.280  51.814  18.021   1.00 46.77  ? 37  PRO   C CD    1 
ATOM   3751  N  N     . SER   B 1  38  ? -5.317  54.125  15.069   1.00 45.96  ? 38  SER   C N     1 
ATOM   3752  C  CA    . SER   B 1  38  ? -5.255  54.679  13.716   1.00 46.86  ? 38  SER   C CA    1 
ATOM   3753  C  C     . SER   B 1  38  ? -6.609  55.142  13.188   1.00 51.19  ? 38  SER   C C     1 
ATOM   3754  O  O     . SER   B 1  38  ? -6.644  55.966  12.270   1.00 61.65  ? 38  SER   C O     1 
ATOM   3755  C  CB    . SER   B 1  38  ? -4.676  53.648  12.748   1.00 44.35  ? 38  SER   C CB    1 
ATOM   3756  O  OG    . SER   B 1  38  ? -5.105  52.327  13.080   1.00 55.18  ? 38  SER   C OG    1 
ATOM   3757  N  N     . ASP   B 1  39  ? -7.719  54.638  13.720   1.00 47.33  ? 39  ASP   C N     1 
ATOM   3758  C  CA    . ASP   B 1  39  ? -9.027  55.054  13.230   1.00 44.99  ? 39  ASP   C CA    1 
ATOM   3759  C  C     . ASP   B 1  39  ? -9.442  56.359  13.906   1.00 44.08  ? 39  ASP   C C     1 
ATOM   3760  O  O     . ASP   B 1  39  ? -9.515  56.434  15.134   1.00 56.58  ? 39  ASP   C O     1 
ATOM   3761  C  CB    . ASP   B 1  39  ? -10.074 53.967  13.461   1.00 33.02  ? 39  ASP   C CB    1 
ATOM   3762  C  CG    . ASP   B 1  39  ? -11.341 54.233  12.698   1.00 41.49  ? 39  ASP   C CG    1 
ATOM   3763  O  OD1   . ASP   B 1  39  ? -11.313 55.153  11.866   1.00 43.19  ? 39  ASP   C OD1   1 
ATOM   3764  O  OD2   . ASP   B 1  39  ? -12.374 53.562  12.915   1.00 45.72  ? 39  ASP   C OD2   1 
ATOM   3765  N  N     . LYS   B 1  40  ? -9.695  57.388  13.101   1.00 45.86  ? 40  LYS   C N     1 
ATOM   3766  C  CA    . LYS   B 1  40  ? -10.306 58.629  13.558   1.00 45.61  ? 40  LYS   C CA    1 
ATOM   3767  C  C     . LYS   B 1  40  ? -11.826 58.631  13.413   1.00 48.14  ? 40  LYS   C C     1 
ATOM   3768  O  O     . LYS   B 1  40  ? -12.502 59.333  14.168   1.00 59.52  ? 40  LYS   C O     1 
ATOM   3769  C  CB    . LYS   B 1  40  ? -9.701  59.802  12.794   1.00 43.34  ? 40  LYS   C CB    1 
ATOM   3770  C  CG    . LYS   B 1  40  ? -8.196  59.680  12.694   1.00 45.98  ? 40  LYS   C CG    1 
ATOM   3771  C  CD    . LYS   B 1  40  ? -7.596  59.641  14.089   1.00 45.17  ? 40  LYS   C CD    1 
ATOM   3772  C  CE    . LYS   B 1  40  ? -6.314  58.844  14.136   1.00 48.98  ? 40  LYS   C CE    1 
ATOM   3773  N  NZ    . LYS   B 1  40  ? -5.434  59.131  12.971   1.00 57.22  ? 40  LYS   C NZ    1 
ATOM   3774  N  N     . THR   B 1  41  ? -12.383 57.887  12.447   1.00 49.92  ? 41  THR   C N     1 
ATOM   3775  C  CA    . THR   B 1  41  ? -13.800 57.525  12.470   1.00 53.70  ? 41  THR   C CA    1 
ATOM   3776  C  C     . THR   B 1  41  ? -14.133 56.899  13.813   1.00 49.73  ? 41  THR   C C     1 
ATOM   3777  O  O     . THR   B 1  41  ? -13.847 55.715  14.015   1.00 46.59  ? 41  THR   C O     1 
ATOM   3778  C  CB    . THR   B 1  41  ? -14.166 56.499  11.379   1.00 53.74  ? 41  THR   C CB    1 
ATOM   3779  O  OG1   . THR   B 1  41  ? -13.806 55.142  11.792   1.00 27.80  ? 41  THR   C OG1   1 
ATOM   3780  C  CG2   . THR   B 1  41  ? -13.530 56.875  10.057   1.00 50.29  ? 41  THR   C CG2   1 
ATOM   3781  N  N     . ILE   B 1  42  ? -14.729 57.654  14.730   1.00 52.75  ? 42  ILE   C N     1 
ATOM   3782  C  CA    . ILE   B 1  42  ? -15.198 57.103  15.998   1.00 53.38  ? 42  ILE   C CA    1 
ATOM   3783  C  C     . ILE   B 1  42  ? -16.687 56.827  15.885   1.00 51.77  ? 42  ILE   C C     1 
ATOM   3784  O  O     . ILE   B 1  42  ? -17.457 57.691  15.440   1.00 51.33  ? 42  ILE   C O     1 
ATOM   3785  C  CB    . ILE   B 1  42  ? -14.908 58.047  17.171   1.00 49.11  ? 42  ILE   C CB    1 
ATOM   3786  C  CG1   . ILE   B 1  42  ? -13.447 58.501  17.127   1.00 46.90  ? 42  ILE   C CG1   1 
ATOM   3787  C  CG2   . ILE   B 1  42  ? -15.232 57.332  18.466   1.00 40.92  ? 42  ILE   C CG2   1 
ATOM   3788  C  CD1   . ILE   B 1  42  ? -13.127 59.550  18.149   1.00 51.97  ? 42  ILE   C CD1   1 
ATOM   3789  N  N     . GLY   B 1  43  ? -17.094 55.623  16.293   1.00 46.62  ? 43  GLY   C N     1 
ATOM   3790  C  CA    . GLY   B 1  43  ? -18.470 55.196  16.182   1.00 54.54  ? 43  GLY   C CA    1 
ATOM   3791  C  C     . GLY   B 1  43  ? -18.856 54.586  14.849   1.00 56.87  ? 43  GLY   C C     1 
ATOM   3792  O  O     . GLY   B 1  43  ? -19.937 53.984  14.748   1.00 63.56  ? 43  GLY   C O     1 
ATOM   3793  N  N     . GLY   B 1  44  ? -18.023 54.720  13.830   1.00 43.63  ? 44  GLY   C N     1 
ATOM   3794  C  CA    . GLY   B 1  44  ? -18.319 54.126  12.546   1.00 51.38  ? 44  GLY   C CA    1 
ATOM   3795  C  C     . GLY   B 1  44  ? -17.452 54.745  11.468   1.00 53.01  ? 44  GLY   C C     1 
ATOM   3796  O  O     . GLY   B 1  44  ? -16.522 55.502  11.745   1.00 55.10  ? 44  GLY   C O     1 
ATOM   3797  N  N     . GLY   B 1  45  ? -17.785 54.405  10.234   1.00 46.68  ? 45  GLY   C N     1 
ATOM   3798  C  CA    . GLY   B 1  45  ? -17.085 54.947  9.091    1.00 52.01  ? 45  GLY   C CA    1 
ATOM   3799  C  C     . GLY   B 1  45  ? -17.405 54.120  7.864    1.00 44.25  ? 45  GLY   C C     1 
ATOM   3800  O  O     . GLY   B 1  45  ? -18.219 53.197  7.912    1.00 44.21  ? 45  GLY   C O     1 
ATOM   3801  N  N     . ASP   B 1  46  ? -16.731 54.465  6.767    1.00 45.78  ? 46  ASP   C N     1 
ATOM   3802  C  CA    . ASP   B 1  46  ? -16.863 53.723  5.520    1.00 53.16  ? 46  ASP   C CA    1 
ATOM   3803  C  C     . ASP   B 1  46  ? -15.512 53.227  4.996    1.00 57.19  ? 46  ASP   C C     1 
ATOM   3804  O  O     . ASP   B 1  46  ? -15.333 53.044  3.786    1.00 50.35  ? 46  ASP   C O     1 
ATOM   3805  C  CB    . ASP   B 1  46  ? -17.574 54.572  4.471    1.00 52.03  ? 46  ASP   C CB    1 
ATOM   3806  C  CG    . ASP   B 1  46  ? -18.574 53.773  3.694    1.00 67.77  ? 46  ASP   C CG    1 
ATOM   3807  O  OD1   . ASP   B 1  46  ? -18.923 52.675  4.182    1.00 73.70  ? 46  ASP   C OD1   1 
ATOM   3808  O  OD2   . ASP   B 1  46  ? -19.002 54.221  2.606    1.00 80.64  ? 46  ASP   C OD2   1 
ATOM   3809  N  N     . ASP   B 1  47  ? -14.558 52.989  5.896    1.00 48.03  ? 47  ASP   C N     1 
ATOM   3810  C  CA    . ASP   B 1  47  ? -13.250 52.500  5.491    1.00 45.19  ? 47  ASP   C CA    1 
ATOM   3811  C  C     . ASP   B 1  47  ? -13.329 51.056  5.025    1.00 45.20  ? 47  ASP   C C     1 
ATOM   3812  O  O     . ASP   B 1  47  ? -14.293 50.331  5.291    1.00 46.75  ? 47  ASP   C O     1 
ATOM   3813  C  CB    . ASP   B 1  47  ? -12.245 52.596  6.633    1.00 44.55  ? 47  ASP   C CB    1 
ATOM   3814  C  CG    . ASP   B 1  47  ? -11.940 54.011  7.002    1.00 45.34  ? 47  ASP   C CG    1 
ATOM   3815  O  OD1   . ASP   B 1  47  ? -11.690 54.792  6.071    1.00 45.28  ? 47  ASP   C OD1   1 
ATOM   3816  O  OD2   . ASP   B 1  47  ? -11.964 54.343  8.215    1.00 59.57  ? 47  ASP   C OD2   1 
ATOM   3817  N  N     . SER   B 1  48  ? -12.281 50.638  4.322    1.00 47.90  ? 48  SER   C N     1 
ATOM   3818  C  CA    . SER   B 1  48  ? -12.241 49.276  3.816    1.00 40.17  ? 48  SER   C CA    1 
ATOM   3819  C  C     . SER   B 1  48  ? -12.440 48.265  4.931    1.00 38.81  ? 48  SER   C C     1 
ATOM   3820  O  O     . SER   B 1  48  ? -13.203 47.305  4.772    1.00 41.17  ? 48  SER   C O     1 
ATOM   3821  C  CB    . SER   B 1  48  ? -10.931 49.036  3.080    1.00 42.11  ? 48  SER   C CB    1 
ATOM   3822  O  OG    . SER   B 1  48  ? -11.112 49.388  1.719    1.00 56.25  ? 48  SER   C OG    1 
ATOM   3823  N  N     . PHE   B 1  49  ? -11.784 48.467  6.080    1.00 35.60  ? 49  PHE   C N     1 
ATOM   3824  C  CA    . PHE   B 1  49  ? -11.936 47.492  7.157    1.00 36.94  ? 49  PHE   C CA    1 
ATOM   3825  C  C     . PHE   B 1  49  ? -13.347 47.485  7.742    1.00 30.04  ? 49  PHE   C C     1 
ATOM   3826  O  O     . PHE   B 1  49  ? -13.723 46.506  8.384    1.00 34.35  ? 49  PHE   C O     1 
ATOM   3827  C  CB    . PHE   B 1  49  ? -10.897 47.719  8.269    1.00 42.70  ? 49  PHE   C CB    1 
ATOM   3828  C  CG    . PHE   B 1  49  ? -10.900 49.111  8.843    1.00 42.64  ? 49  PHE   C CG    1 
ATOM   3829  C  CD1   . PHE   B 1  49  ? -11.892 49.510  9.731    1.00 33.30  ? 49  PHE   C CD1   1 
ATOM   3830  C  CD2   . PHE   B 1  49  ? -9.904  50.021  8.489    1.00 34.99  ? 49  PHE   C CD2   1 
ATOM   3831  C  CE1   . PHE   B 1  49  ? -11.892 50.797  10.239   1.00 44.97  ? 49  PHE   C CE1   1 
ATOM   3832  C  CE2   . PHE   B 1  49  ? -9.900  51.305  8.996    1.00 34.80  ? 49  PHE   C CE2   1 
ATOM   3833  C  CZ    . PHE   B 1  49  ? -10.886 51.701  9.871    1.00 35.99  ? 49  PHE   C CZ    1 
ATOM   3834  N  N     . ASN   B 1  50  ? -14.153 48.518  7.507    1.00 31.00  ? 50  ASN   C N     1 
ATOM   3835  C  CA    . ASN   B 1  50  ? -15.531 48.472  7.984    1.00 34.98  ? 50  ASN   C CA    1 
ATOM   3836  C  C     . ASN   B 1  50  ? -16.342 47.386  7.302    1.00 35.27  ? 50  ASN   C C     1 
ATOM   3837  O  O     . ASN   B 1  50  ? -17.446 47.084  7.763    1.00 36.59  ? 50  ASN   C O     1 
ATOM   3838  C  CB    . ASN   B 1  50  ? -16.222 49.825  7.800    1.00 34.97  ? 50  ASN   C CB    1 
ATOM   3839  C  CG    . ASN   B 1  50  ? -15.581 50.925  8.653    1.00 49.25  ? 50  ASN   C CG    1 
ATOM   3840  O  OD1   . ASN   B 1  50  ? -15.179 51.975  8.146    1.00 49.79  ? 50  ASN   C OD1   1 
ATOM   3841  N  ND2   . ASN   B 1  50  ? -15.459 50.671  9.949    1.00 41.61  ? 50  ASN   C ND2   1 
ATOM   3842  N  N     . THR   B 1  51  ? -15.827 46.774  6.237    1.00 29.89  ? 51  THR   C N     1 
ATOM   3843  C  CA    . THR   B 1  51  ? -16.546 45.635  5.676    1.00 41.39  ? 51  THR   C CA    1 
ATOM   3844  C  C     . THR   B 1  51  ? -16.554 44.445  6.637    1.00 41.73  ? 51  THR   C C     1 
ATOM   3845  O  O     . THR   B 1  51  ? -17.470 43.608  6.567    1.00 40.31  ? 51  THR   C O     1 
ATOM   3846  C  CB    . THR   B 1  51  ? -15.952 45.218  4.313    1.00 37.00  ? 51  THR   C CB    1 
ATOM   3847  O  OG1   . THR   B 1  51  ? -14.735 44.495  4.518    1.00 42.33  ? 51  THR   C OG1   1 
ATOM   3848  C  CG2   . THR   B 1  51  ? -15.664 46.429  3.427    1.00 26.55  ? 51  THR   C CG2   1 
ATOM   3849  N  N     . PHE   B 1  52  ? -15.573 44.361  7.552    1.00 33.64  ? 52  PHE   C N     1 
ATOM   3850  C  CA    . PHE   B 1  52  ? -15.479 43.227  8.470    1.00 35.60  ? 52  PHE   C CA    1 
ATOM   3851  C  C     . PHE   B 1  52  ? -15.612 43.571  9.954    1.00 35.43  ? 52  PHE   C C     1 
ATOM   3852  O  O     . PHE   B 1  52  ? -15.801 42.647  10.752   1.00 36.78  ? 52  PHE   C O     1 
ATOM   3853  C  CB    . PHE   B 1  52  ? -14.153 42.478  8.257    1.00 34.92  ? 52  PHE   C CB    1 
ATOM   3854  C  CG    . PHE   B 1  52  ? -14.204 41.458  7.158    1.00 31.53  ? 52  PHE   C CG    1 
ATOM   3855  C  CD1   . PHE   B 1  52  ? -14.465 41.837  5.857    1.00 34.19  ? 52  PHE   C CD1   1 
ATOM   3856  C  CD2   . PHE   B 1  52  ? -13.983 40.115  7.431    1.00 35.50  ? 52  PHE   C CD2   1 
ATOM   3857  C  CE1   . PHE   B 1  52  ? -14.506 40.886  4.835    1.00 42.80  ? 52  PHE   C CE1   1 
ATOM   3858  C  CE2   . PHE   B 1  52  ? -14.021 39.154  6.421    1.00 37.54  ? 52  PHE   C CE2   1 
ATOM   3859  C  CZ    . PHE   B 1  52  ? -14.277 39.536  5.120    1.00 39.89  ? 52  PHE   C CZ    1 
ATOM   3860  N  N     . PHE   B 1  53  ? -15.515 44.853  10.342   1.00 30.70  ? 53  PHE   C N     1 
ATOM   3861  C  CA    . PHE   B 1  53  ? -15.583 45.323  11.729   1.00 36.36  ? 53  PHE   C CA    1 
ATOM   3862  C  C     . PHE   B 1  53  ? -16.598 46.458  11.847   1.00 42.85  ? 53  PHE   C C     1 
ATOM   3863  O  O     . PHE   B 1  53  ? -16.509 47.446  11.105   1.00 38.78  ? 53  PHE   C O     1 
ATOM   3864  C  CB    . PHE   B 1  53  ? -14.227 45.856  12.233   1.00 32.88  ? 53  PHE   C CB    1 
ATOM   3865  C  CG    . PHE   B 1  53  ? -13.157 44.829  12.305   1.00 33.26  ? 53  PHE   C CG    1 
ATOM   3866  C  CD1   . PHE   B 1  53  ? -13.052 44.002  13.410   1.00 32.35  ? 53  PHE   C CD1   1 
ATOM   3867  C  CD2   . PHE   B 1  53  ? -12.235 44.707  11.285   1.00 32.66  ? 53  PHE   C CD2   1 
ATOM   3868  C  CE1   . PHE   B 1  53  ? -12.059 43.047  13.482   1.00 36.07  ? 53  PHE   C CE1   1 
ATOM   3869  C  CE2   . PHE   B 1  53  ? -11.234 43.747  11.337   1.00 31.32  ? 53  PHE   C CE2   1 
ATOM   3870  C  CZ    . PHE   B 1  53  ? -11.147 42.910  12.437   1.00 32.50  ? 53  PHE   C CZ    1 
ATOM   3871  N  N     . SER   B 1  54  ? -17.546 46.336  12.779   1.00 30.96  ? 54  SER   C N     1 
ATOM   3872  C  CA    . SER   B 1  54  ? -18.379 47.483  13.113   1.00 39.29  ? 54  SER   C CA    1 
ATOM   3873  C  C     . SER   B 1  54  ? -17.716 48.250  14.249   1.00 41.28  ? 54  SER   C C     1 
ATOM   3874  O  O     . SER   B 1  54  ? -16.932 47.696  15.021   1.00 45.06  ? 54  SER   C O     1 
ATOM   3875  C  CB    . SER   B 1  54  ? -19.809 47.077  13.492   1.00 34.83  ? 54  SER   C CB    1 
ATOM   3876  O  OG    . SER   B 1  54  ? -19.852 46.203  14.600   1.00 37.83  ? 54  SER   C OG    1 
ATOM   3877  N  N     . GLU   B 1  55  ? -17.995 49.544  14.313   1.00 46.67  ? 55  GLU   C N     1 
ATOM   3878  C  CA    . GLU   B 1  55  ? -17.404 50.425  15.311   1.00 51.04  ? 55  GLU   C CA    1 
ATOM   3879  C  C     . GLU   B 1  55  ? -18.452 50.774  16.357   1.00 48.10  ? 55  GLU   C C     1 
ATOM   3880  O  O     . GLU   B 1  55  ? -19.619 51.014  16.019   1.00 53.24  ? 55  GLU   C O     1 
ATOM   3881  C  CB    . GLU   B 1  55  ? -16.843 51.691  14.652   1.00 44.62  ? 55  GLU   C CB    1 
ATOM   3882  C  CG    . GLU   B 1  55  ? -15.708 51.375  13.721   1.00 38.33  ? 55  GLU   C CG    1 
ATOM   3883  C  CD    . GLU   B 1  55  ? -15.217 52.575  12.931   1.00 47.14  ? 55  GLU   C CD    1 
ATOM   3884  O  OE1   . GLU   B 1  55  ? -14.781 53.569  13.533   1.00 44.13  ? 55  GLU   C OE1   1 
ATOM   3885  O  OE2   . GLU   B 1  55  ? -15.253 52.522  11.685   1.00 54.37  ? 55  GLU   C OE2   1 
ATOM   3886  N  N     . THR   B 1  56  ? -18.050 50.745  17.631   1.00 48.30  ? 56  THR   C N     1 
ATOM   3887  C  CA    . THR   B 1  56  ? -18.900 51.212  18.722   1.00 47.71  ? 56  THR   C CA    1 
ATOM   3888  C  C     . THR   B 1  56  ? -18.521 52.648  19.052   1.00 43.99  ? 56  THR   C C     1 
ATOM   3889  O  O     . THR   B 1  56  ? -17.393 53.083  18.797   1.00 39.36  ? 56  THR   C O     1 
ATOM   3890  C  CB    . THR   B 1  56  ? -18.786 50.346  19.996   1.00 45.01  ? 56  THR   C CB    1 
ATOM   3891  O  OG1   . THR   B 1  56  ? -17.723 50.831  20.827   1.00 43.82  ? 56  THR   C OG1   1 
ATOM   3892  C  CG2   . THR   B 1  56  ? -18.534 48.883  19.676   1.00 39.33  ? 56  THR   C CG2   1 
ATOM   3893  N  N     . GLY   B 1  57  ? -19.491 53.385  19.607   1.00 52.00  ? 57  GLY   C N     1 
ATOM   3894  C  CA    . GLY   B 1  57  ? -19.261 54.778  19.968   1.00 47.64  ? 57  GLY   C CA    1 
ATOM   3895  C  C     . GLY   B 1  57  ? -18.065 54.983  20.880   1.00 47.64  ? 57  GLY   C C     1 
ATOM   3896  O  O     . GLY   B 1  57  ? -17.371 56.004  20.779   1.00 48.16  ? 57  GLY   C O     1 
ATOM   3897  N  N     . ALA   B 1  58  ? -17.794 54.020  21.768   1.00 35.59  ? 58  ALA   C N     1 
ATOM   3898  C  CA    . ALA   B 1  58  ? -16.618 54.070  22.628   1.00 37.96  ? 58  ALA   C CA    1 
ATOM   3899  C  C     . ALA   B 1  58  ? -15.332 53.692  21.901   1.00 42.19  ? 58  ALA   C C     1 
ATOM   3900  O  O     . ALA   B 1  58  ? -14.292 53.529  22.558   1.00 40.72  ? 58  ALA   C O     1 
ATOM   3901  C  CB    . ALA   B 1  58  ? -16.806 53.160  23.849   1.00 40.52  ? 58  ALA   C CB    1 
ATOM   3902  N  N     . GLY   B 1  59  ? -15.386 53.518  20.580   1.00 43.49  ? 59  GLY   C N     1 
ATOM   3903  C  CA    . GLY   B 1  59  ? -14.199 53.232  19.791   1.00 51.55  ? 59  GLY   C CA    1 
ATOM   3904  C  C     . GLY   B 1  59  ? -13.796 51.777  19.677   1.00 47.04  ? 59  GLY   C C     1 
ATOM   3905  O  O     . GLY   B 1  59  ? -12.640 51.495  19.324   1.00 42.04  ? 59  GLY   C O     1 
ATOM   3906  N  N     . LYS   B 1  60  ? -14.694 50.839  19.963   1.00 40.68  ? 60  LYS   C N     1 
ATOM   3907  C  CA    . LYS   B 1  60  ? -14.375 49.431  19.776   1.00 50.35  ? 60  LYS   C CA    1 
ATOM   3908  C  C     . LYS   B 1  60  ? -14.665 49.029  18.335   1.00 43.46  ? 60  LYS   C C     1 
ATOM   3909  O  O     . LYS   B 1  60  ? -15.712 49.378  17.779   1.00 44.62  ? 60  LYS   C O     1 
ATOM   3910  C  CB    . LYS   B 1  60  ? -15.152 48.531  20.739   1.00 46.12  ? 60  LYS   C CB    1 
ATOM   3911  C  CG    . LYS   B 1  60  ? -14.747 47.067  20.618   1.00 43.21  ? 60  LYS   C CG    1 
ATOM   3912  C  CD    . LYS   B 1  60  ? -15.633 46.133  21.431   1.00 49.72  ? 60  LYS   C CD    1 
ATOM   3913  C  CE    . LYS   B 1  60  ? -15.450 46.267  22.937   1.00 40.69  ? 60  LYS   C CE    1 
ATOM   3914  N  NZ    . LYS   B 1  60  ? -16.485 45.439  23.662   1.00 51.18  ? 60  LYS   C NZ    1 
ATOM   3915  N  N     . HIS   B 1  61  ? -13.726 48.306  17.740   1.00 43.88  ? 61  HIS   C N     1 
ATOM   3916  C  CA    . HIS   B 1  61  ? -13.913 47.673  16.440   1.00 40.60  ? 61  HIS   C CA    1 
ATOM   3917  C  C     . HIS   B 1  61  ? -14.280 46.209  16.669   1.00 42.25  ? 61  HIS   C C     1 
ATOM   3918  O  O     . HIS   B 1  61  ? -13.474 45.422  17.186   1.00 45.97  ? 61  HIS   C O     1 
ATOM   3919  C  CB    . HIS   B 1  61  ? -12.654 47.837  15.598   1.00 31.75  ? 61  HIS   C CB    1 
ATOM   3920  C  CG    . HIS   B 1  61  ? -12.353 49.266  15.291   1.00 44.11  ? 61  HIS   C CG    1 
ATOM   3921  N  ND1   . HIS   B 1  61  ? -12.079 50.191  16.277   1.00 38.11  ? 61  HIS   C ND1   1 
ATOM   3922  C  CD2   . HIS   B 1  61  ? -12.320 49.942  14.120   1.00 41.73  ? 61  HIS   C CD2   1 
ATOM   3923  C  CE1   . HIS   B 1  61  ? -11.871 51.372  15.723   1.00 29.51  ? 61  HIS   C CE1   1 
ATOM   3924  N  NE2   . HIS   B 1  61  ? -12.005 51.248  14.417   1.00 40.09  ? 61  HIS   C NE2   1 
ATOM   3925  N  N     . VAL   B 1  62  ? -15.503 45.862  16.304   1.00 31.90  ? 62  VAL   C N     1 
ATOM   3926  C  CA    . VAL   B 1  62  ? -16.149 44.602  16.653   1.00 38.43  ? 62  VAL   C CA    1 
ATOM   3927  C  C     . VAL   B 1  62  ? -16.344 43.794  15.370   1.00 35.53  ? 62  VAL   C C     1 
ATOM   3928  O  O     . VAL   B 1  62  ? -16.999 44.275  14.439   1.00 32.06  ? 62  VAL   C O     1 
ATOM   3929  C  CB    . VAL   B 1  62  ? -17.492 44.853  17.361   1.00 39.21  ? 62  VAL   C CB    1 
ATOM   3930  C  CG1   . VAL   B 1  62  ? -18.085 43.547  17.908   1.00 40.19  ? 62  VAL   C CG1   1 
ATOM   3931  C  CG2   . VAL   B 1  62  ? -17.323 45.909  18.472   1.00 35.50  ? 62  VAL   C CG2   1 
ATOM   3932  N  N     . PRO   B 1  63  ? -15.773 42.595  15.260   1.00 33.90  ? 63  PRO   C N     1 
ATOM   3933  C  CA    . PRO   B 1  63  ? -16.000 41.769  14.069   1.00 34.59  ? 63  PRO   C CA    1 
ATOM   3934  C  C     . PRO   B 1  63  ? -17.483 41.579  13.762   1.00 33.11  ? 63  PRO   C C     1 
ATOM   3935  O  O     . PRO   B 1  63  ? -18.321 41.432  14.663   1.00 32.52  ? 63  PRO   C O     1 
ATOM   3936  C  CB    . PRO   B 1  63  ? -15.328 40.436  14.438   1.00 35.33  ? 63  PRO   C CB    1 
ATOM   3937  C  CG    . PRO   B 1  63  ? -14.206 40.824  15.318   1.00 35.06  ? 63  PRO   C CG    1 
ATOM   3938  C  CD    . PRO   B 1  63  ? -14.715 42.031  16.119   1.00 39.58  ? 63  PRO   C CD    1 
ATOM   3939  N  N     . ARG   B 1  64  ? -17.803 41.577  12.467   1.00 23.77  ? 64  ARG   C N     1 
ATOM   3940  C  CA    . ARG   B 1  64  ? -19.165 41.292  12.010   1.00 27.39  ? 64  ARG   C CA    1 
ATOM   3941  C  C     . ARG   B 1  64  ? -19.345 39.785  11.850   1.00 28.25  ? 64  ARG   C C     1 
ATOM   3942  O  O     . ARG   B 1  64  ? -19.518 39.261  10.754   1.00 35.37  ? 64  ARG   C O     1 
ATOM   3943  C  CB    . ARG   B 1  64  ? -19.462 42.010  10.701   1.00 22.64  ? 64  ARG   C CB    1 
ATOM   3944  C  CG    . ARG   B 1  64  ? -19.192 43.499  10.688   1.00 29.87  ? 64  ARG   C CG    1 
ATOM   3945  C  CD    . ARG   B 1  64  ? -19.721 44.072  9.414    1.00 32.71  ? 64  ARG   C CD    1 
ATOM   3946  N  NE    . ARG   B 1  64  ? -19.377 45.474  9.230    1.00 35.02  ? 64  ARG   C NE    1 
ATOM   3947  C  CZ    . ARG   B 1  64  ? -20.151 46.491  9.589    1.00 38.94  ? 64  ARG   C CZ    1 
ATOM   3948  N  NH1   . ARG   B 1  64  ? -21.298 46.301  10.226   1.00 28.74  ? 64  ARG   C NH1   1 
ATOM   3949  N  NH2   . ARG   B 1  64  ? -19.772 47.729  9.289    1.00 43.27  ? 64  ARG   C NH2   1 
ATOM   3950  N  N     . ALA   B 1  65  ? -19.284 39.079  12.970   1.00 21.30  ? 65  ALA   C N     1 
ATOM   3951  C  CA    . ALA   B 1  65  ? -19.330 37.630  12.908   1.00 25.61  ? 65  ALA   C CA    1 
ATOM   3952  C  C     . ALA   B 1  65  ? -20.211 37.077  14.019   1.00 29.27  ? 65  ALA   C C     1 
ATOM   3953  O  O     . ALA   B 1  65  ? -20.449 37.724  15.042   1.00 28.22  ? 65  ALA   C O     1 
ATOM   3954  C  CB    . ALA   B 1  65  ? -17.929 37.021  13.003   1.00 31.99  ? 65  ALA   C CB    1 
ATOM   3955  N  N     . VAL   B 1  66  ? -20.700 35.866  13.792   1.00 30.59  ? 66  VAL   C N     1 
ATOM   3956  C  CA    . VAL   B 1  66  ? -21.341 35.063  14.820   1.00 31.95  ? 66  VAL   C CA    1 
ATOM   3957  C  C     . VAL   B 1  66  ? -20.550 33.776  14.965   1.00 30.99  ? 66  VAL   C C     1 
ATOM   3958  O  O     . VAL   B 1  66  ? -19.973 33.279  13.995   1.00 35.10  ? 66  VAL   C O     1 
ATOM   3959  C  CB    . VAL   B 1  66  ? -22.811 34.756  14.478   1.00 28.99  ? 66  VAL   C CB    1 
ATOM   3960  C  CG1   . VAL   B 1  66  ? -23.359 33.766  15.470   1.00 35.36  ? 66  VAL   C CG1   1 
ATOM   3961  C  CG2   . VAL   B 1  66  ? -23.622 36.020  14.488   1.00 25.75  ? 66  VAL   C CG2   1 
ATOM   3962  N  N     . PHE   B 1  67  ? -20.521 33.238  16.179   1.00 36.45  ? 67  PHE   C N     1 
ATOM   3963  C  CA    . PHE   B 1  67  ? -19.932 31.933  16.461   1.00 30.94  ? 67  PHE   C CA    1 
ATOM   3964  C  C     . PHE   B 1  67  ? -21.006 31.013  17.008   1.00 32.20  ? 67  PHE   C C     1 
ATOM   3965  O  O     . PHE   B 1  67  ? -21.682 31.365  17.975   1.00 43.69  ? 67  PHE   C O     1 
ATOM   3966  C  CB    . PHE   B 1  67  ? -18.808 32.036  17.472   1.00 30.06  ? 67  PHE   C CB    1 
ATOM   3967  C  CG    . PHE   B 1  67  ? -17.574 32.671  16.937   1.00 33.60  ? 67  PHE   C CG    1 
ATOM   3968  C  CD1   . PHE   B 1  67  ? -17.570 34.000  16.552   1.00 37.67  ? 67  PHE   C CD1   1 
ATOM   3969  C  CD2   . PHE   B 1  67  ? -16.407 31.958  16.853   1.00 31.28  ? 67  PHE   C CD2   1 
ATOM   3970  C  CE1   . PHE   B 1  67  ? -16.416 34.599  16.078   1.00 34.01  ? 67  PHE   C CE1   1 
ATOM   3971  C  CE2   . PHE   B 1  67  ? -15.256 32.559  16.379   1.00 37.51  ? 67  PHE   C CE2   1 
ATOM   3972  C  CZ    . PHE   B 1  67  ? -15.266 33.877  15.991   1.00 30.92  ? 67  PHE   C CZ    1 
ATOM   3973  N  N     . VAL   B 1  68  ? -21.138 29.828  16.420   1.00 31.95  ? 68  VAL   C N     1 
ATOM   3974  C  CA    A VAL   B 1  68  ? -22.172 28.866  16.785   0.90 30.47  ? 68  VAL   C CA    1 
ATOM   3975  C  CA    B VAL   B 1  68  ? -22.168 28.874  16.802   0.10 30.09  ? 68  VAL   C CA    1 
ATOM   3976  C  C     . VAL   B 1  68  ? -21.521 27.515  17.015   1.00 32.59  ? 68  VAL   C C     1 
ATOM   3977  O  O     . VAL   B 1  68  ? -20.732 27.052  16.184   1.00 34.88  ? 68  VAL   C O     1 
ATOM   3978  C  CB    A VAL   B 1  68  ? -23.257 28.725  15.703   0.90 28.97  ? 68  VAL   C CB    1 
ATOM   3979  C  CB    B VAL   B 1  68  ? -23.285 28.782  15.745   0.10 29.35  ? 68  VAL   C CB    1 
ATOM   3980  C  CG1   A VAL   B 1  68  ? -24.562 28.315  16.342   0.90 30.32  ? 68  VAL   C CG1   1 
ATOM   3981  C  CG1   B VAL   B 1  68  ? -22.733 28.242  14.442   0.10 29.73  ? 68  VAL   C CG1   1 
ATOM   3982  C  CG2   A VAL   B 1  68  ? -23.411 30.003  14.901   0.90 30.65  ? 68  VAL   C CG2   1 
ATOM   3983  C  CG2   B VAL   B 1  68  ? -24.423 27.912  16.253   0.10 30.62  ? 68  VAL   C CG2   1 
ATOM   3984  N  N     . ASP   B 1  69  ? -21.855 26.882  18.130   1.00 36.50  ? 69  ASP   C N     1 
ATOM   3985  C  CA    . ASP   B 1  69  ? -21.481 25.502  18.377   1.00 33.45  ? 69  ASP   C CA    1 
ATOM   3986  C  C     . ASP   B 1  69  ? -22.592 24.892  19.207   1.00 32.50  ? 69  ASP   C C     1 
ATOM   3987  O  O     . ASP   B 1  69  ? -23.239 25.582  20.003   1.00 36.70  ? 69  ASP   C O     1 
ATOM   3988  C  CB    . ASP   B 1  69  ? -20.134 25.373  19.086   1.00 30.15  ? 69  ASP   C CB    1 
ATOM   3989  C  CG    . ASP   B 1  69  ? -19.493 24.048  18.816   1.00 28.68  ? 69  ASP   C CG    1 
ATOM   3990  O  OD1   . ASP   B 1  69  ? -20.131 23.269  18.094   1.00 31.12  ? 69  ASP   C OD1   1 
ATOM   3991  O  OD2   . ASP   B 1  69  ? -18.390 23.761  19.329   1.00 37.01  ? 69  ASP   C OD2   1 
ATOM   3992  N  N     . LEU   B 1  70  ? -22.842 23.615  18.993   1.00 26.17  ? 70  LEU   C N     1 
ATOM   3993  C  CA    . LEU   B 1  70  ? -23.939 23.002  19.724   1.00 33.62  ? 70  LEU   C CA    1 
ATOM   3994  C  C     . LEU   B 1  70  ? -23.525 22.543  21.117   1.00 36.09  ? 70  LEU   C C     1 
ATOM   3995  O  O     . LEU   B 1  70  ? -24.331 21.927  21.821   1.00 41.78  ? 70  LEU   C O     1 
ATOM   3996  C  CB    . LEU   B 1  70  ? -24.512 21.847  18.910   1.00 31.59  ? 70  LEU   C CB    1 
ATOM   3997  C  CG    . LEU   B 1  70  ? -25.180 22.305  17.618   1.00 33.97  ? 70  LEU   C CG    1 
ATOM   3998  C  CD1   . LEU   B 1  70  ? -26.000 21.206  16.994   1.00 28.56  ? 70  LEU   C CD1   1 
ATOM   3999  C  CD2   . LEU   B 1  70  ? -26.060 23.483  17.931   1.00 31.65  ? 70  LEU   C CD2   1 
ATOM   4000  N  N     . GLU   B 1  71  ? -22.290 22.821  21.521   1.00 34.24  ? 71  GLU   C N     1 
ATOM   4001  C  CA    . GLU   B 1  71  ? -21.797 22.584  22.868   1.00 37.32  ? 71  GLU   C CA    1 
ATOM   4002  C  C     . GLU   B 1  71  ? -20.859 23.727  23.211   1.00 35.82  ? 71  GLU   C C     1 
ATOM   4003  O  O     . GLU   B 1  71  ? -20.246 24.316  22.316   1.00 40.61  ? 71  GLU   C O     1 
ATOM   4004  C  CB    . GLU   B 1  71  ? -21.079 21.228  23.017   1.00 37.87  ? 71  GLU   C CB    1 
ATOM   4005  C  CG    . GLU   B 1  71  ? -19.853 21.023  22.143   1.00 27.07  ? 71  GLU   C CG    1 
ATOM   4006  C  CD    . GLU   B 1  71  ? -18.528 21.182  22.907   1.00 37.38  ? 71  GLU   C CD    1 
ATOM   4007  O  OE1   . GLU   B 1  71  ? -18.557 21.401  24.136   1.00 40.91  ? 71  GLU   C OE1   1 
ATOM   4008  O  OE2   . GLU   B 1  71  ? -17.447 21.080  22.282   1.00 44.45  ? 71  GLU   C OE2   1 
ATOM   4009  N  N     . PRO   B 1  72  ? -20.722 24.058  24.499   1.00 47.62  ? 72  PRO   C N     1 
ATOM   4010  C  CA    . PRO   B 1  72  ? -20.118 25.340  24.877   1.00 34.22  ? 72  PRO   C CA    1 
ATOM   4011  C  C     . PRO   B 1  72  ? -18.605 25.355  24.972   1.00 35.46  ? 72  PRO   C C     1 
ATOM   4012  O  O     . PRO   B 1  72  ? -18.006 26.438  24.954   1.00 38.90  ? 72  PRO   C O     1 
ATOM   4013  C  CB    . PRO   B 1  72  ? -20.740 25.598  26.255   1.00 39.18  ? 72  PRO   C CB    1 
ATOM   4014  C  CG    . PRO   B 1  72  ? -20.881 24.263  26.812   1.00 27.56  ? 72  PRO   C CG    1 
ATOM   4015  C  CD    . PRO   B 1  72  ? -21.310 23.383  25.668   1.00 43.84  ? 72  PRO   C CD    1 
ATOM   4016  N  N     . THR   B 1  73  ? -17.954 24.197  25.089   1.00 34.23  ? 73  THR   C N     1 
ATOM   4017  C  CA    . THR   B 1  73  ? -16.557 24.231  25.521   1.00 33.12  ? 73  THR   C CA    1 
ATOM   4018  C  C     . THR   B 1  73  ? -15.679 25.016  24.555   1.00 35.60  ? 73  THR   C C     1 
ATOM   4019  O  O     . THR   B 1  73  ? -14.833 25.805  24.999   1.00 44.73  ? 73  THR   C O     1 
ATOM   4020  C  CB    . THR   B 1  73  ? -16.007 22.824  25.725   1.00 35.68  ? 73  THR   C CB    1 
ATOM   4021  O  OG1   . THR   B 1  73  ? -16.206 22.055  24.543   1.00 38.44  ? 73  THR   C OG1   1 
ATOM   4022  C  CG2   . THR   B 1  73  ? -16.696 22.159  26.924   1.00 27.70  ? 73  THR   C CG2   1 
ATOM   4023  N  N     . VAL   B 1  74  ? -15.864 24.834  23.234   1.00 38.02  ? 74  VAL   C N     1 
ATOM   4024  C  CA    . VAL   B 1  74  ? -14.954 25.484  22.286   1.00 38.73  ? 74  VAL   C CA    1 
ATOM   4025  C  C     . VAL   B 1  74  ? -15.185 26.985  22.265   1.00 34.06  ? 74  VAL   C C     1 
ATOM   4026  O  O     . VAL   B 1  74  ? -14.231 27.769  22.249   1.00 36.10  ? 74  VAL   C O     1 
ATOM   4027  C  CB    . VAL   B 1  74  ? -15.056 24.879  20.872   1.00 32.40  ? 74  VAL   C CB    1 
ATOM   4028  C  CG1   . VAL   B 1  74  ? -14.196 25.654  19.925   1.00 19.46  ? 74  VAL   C CG1   1 
ATOM   4029  C  CG2   . VAL   B 1  74  ? -14.549 23.486  20.871   1.00 31.52  ? 74  VAL   C CG2   1 
ATOM   4030  N  N     . ILE   B 1  75  ? -16.447 27.421  22.295   1.00 41.77  ? 75  ILE   C N     1 
ATOM   4031  C  CA    . ILE   B 1  75  ? -16.697 28.861  22.306   1.00 34.04  ? 75  ILE   C CA    1 
ATOM   4032  C  C     . ILE   B 1  75  ? -16.353 29.465  23.676   1.00 40.03  ? 75  ILE   C C     1 
ATOM   4033  O  O     . ILE   B 1  75  ? -15.810 30.573  23.743   1.00 38.02  ? 75  ILE   C O     1 
ATOM   4034  C  CB    . ILE   B 1  75  ? -18.139 29.155  21.843   1.00 27.78  ? 75  ILE   C CB    1 
ATOM   4035  C  CG1   . ILE   B 1  75  ? -18.164 29.222  20.307   1.00 32.92  ? 75  ILE   C CG1   1 
ATOM   4036  C  CG2   . ILE   B 1  75  ? -18.684 30.450  22.447   1.00 32.86  ? 75  ILE   C CG2   1 
ATOM   4037  C  CD1   . ILE   B 1  75  ? -19.499 28.812  19.628   1.00 29.04  ? 75  ILE   C CD1   1 
ATOM   4038  N  N     . ASP   B 1  76  ? -16.606 28.737  24.786   1.00 33.81  ? 76  ASP   C N     1 
ATOM   4039  C  CA    . ASP   B 1  76  ? -16.173 29.230  26.100   1.00 37.13  ? 76  ASP   C CA    1 
ATOM   4040  C  C     . ASP   B 1  76  ? -14.703 29.636  26.083   1.00 39.30  ? 76  ASP   C C     1 
ATOM   4041  O  O     . ASP   B 1  76  ? -14.300 30.568  26.796   1.00 41.36  ? 76  ASP   C O     1 
ATOM   4042  C  CB    . ASP   B 1  76  ? -16.382 28.188  27.222   1.00 30.81  ? 76  ASP   C CB    1 
ATOM   4043  C  CG    . ASP   B 1  76  ? -17.852 27.992  27.618   1.00 35.76  ? 76  ASP   C CG    1 
ATOM   4044  O  OD1   . ASP   B 1  76  ? -18.645 28.955  27.611   1.00 31.95  ? 76  ASP   C OD1   1 
ATOM   4045  O  OD2   . ASP   B 1  76  ? -18.229 26.850  27.948   1.00 41.96  ? 76  ASP   C OD2   1 
ATOM   4046  N  N     . GLU   B 1  77  ? -13.883 28.946  25.286   1.00 37.30  ? 77  GLU   C N     1 
ATOM   4047  C  CA    . GLU   B 1  77  ? -12.478 29.325  25.193   1.00 42.09  ? 77  GLU   C CA    1 
ATOM   4048  C  C     . GLU   B 1  77  ? -12.320 30.744  24.648   1.00 42.56  ? 77  GLU   C C     1 
ATOM   4049  O  O     . GLU   B 1  77  ? -11.389 31.455  25.043   1.00 47.46  ? 77  GLU   C O     1 
ATOM   4050  C  CB    . GLU   B 1  77  ? -11.719 28.314  24.326   1.00 39.02  ? 77  GLU   C CB    1 
ATOM   4051  C  CG    . GLU   B 1  77  ? -11.356 27.003  24.998   1.00 31.57  ? 77  GLU   C CG    1 
ATOM   4052  C  CD    . GLU   B 1  77  ? -10.134 27.153  25.866   1.00 56.29  ? 77  GLU   C CD    1 
ATOM   4053  O  OE1   . GLU   B 1  77  ? -9.039  27.350  25.293   1.00 63.70  ? 77  GLU   C OE1   1 
ATOM   4054  O  OE2   . GLU   B 1  77  ? -10.264 27.110  27.116   1.00 53.26  ? 77  GLU   C OE2   1 
ATOM   4055  N  N     . VAL   B 1  78  ? -13.217 31.170  23.754   1.00 39.12  ? 78  VAL   C N     1 
ATOM   4056  C  CA    . VAL   B 1  78  ? -13.194 32.530  23.217   1.00 37.50  ? 78  VAL   C CA    1 
ATOM   4057  C  C     . VAL   B 1  78  ? -13.710 33.521  24.249   1.00 43.05  ? 78  VAL   C C     1 
ATOM   4058  O  O     . VAL   B 1  78  ? -13.104 34.570  24.483   1.00 46.44  ? 78  VAL   C O     1 
ATOM   4059  C  CB    . VAL   B 1  78  ? -14.032 32.626  21.924   1.00 41.27  ? 78  VAL   C CB    1 
ATOM   4060  C  CG1   . VAL   B 1  78  ? -13.961 34.040  21.372   1.00 38.72  ? 78  VAL   C CG1   1 
ATOM   4061  C  CG2   . VAL   B 1  78  ? -13.659 31.529  20.868   1.00 25.27  ? 78  VAL   C CG2   1 
ATOM   4062  N  N     . ARG   B 1  79  ? -14.864 33.209  24.851   1.00 47.25  ? 79  ARG   C N     1 
ATOM   4063  C  CA    . ARG   B 1  79  ? -15.436 34.009  25.933   1.00 41.38  ? 79  ARG   C CA    1 
ATOM   4064  C  C     . ARG   B 1  79  ? -14.412 34.389  26.999   1.00 45.68  ? 79  ARG   C C     1 
ATOM   4065  O  O     . ARG   B 1  79  ? -14.489 35.486  27.567   1.00 45.41  ? 79  ARG   C O     1 
ATOM   4066  C  CB    . ARG   B 1  79  ? -16.595 33.240  26.564   1.00 36.90  ? 79  ARG   C CB    1 
ATOM   4067  C  CG    . ARG   B 1  79  ? -17.826 33.155  25.655   1.00 38.62  ? 79  ARG   C CG    1 
ATOM   4068  C  CD    . ARG   B 1  79  ? -18.914 32.227  26.199   1.00 32.20  ? 79  ARG   C CD    1 
ATOM   4069  N  NE    . ARG   B 1  79  ? -20.139 32.298  25.406   1.00 38.88  ? 79  ARG   C NE    1 
ATOM   4070  C  CZ    . ARG   B 1  79  ? -20.981 31.286  25.235   1.00 38.41  ? 79  ARG   C CZ    1 
ATOM   4071  N  NH1   . ARG   B 1  79  ? -20.765 30.104  25.793   1.00 35.62  ? 79  ARG   C NH1   1 
ATOM   4072  N  NH2   . ARG   B 1  79  ? -22.062 31.458  24.472   1.00 30.34  ? 79  ARG   C NH2   1 
ATOM   4073  N  N     . THR   B 1  80  ? -13.447 33.502  27.286   1.00 49.06  ? 80  THR   C N     1 
ATOM   4074  C  CA    . THR   B 1  80  ? -12.381 33.774  28.246   1.00 43.70  ? 80  THR   C CA    1 
ATOM   4075  C  C     . THR   B 1  80  ? -11.020 34.055  27.609   1.00 47.39  ? 80  THR   C C     1 
ATOM   4076  O  O     . THR   B 1  80  ? -10.089 34.423  28.333   1.00 52.80  ? 80  THR   C O     1 
ATOM   4077  C  CB    . THR   B 1  80  ? -12.228 32.596  29.228   1.00 41.34  ? 80  THR   C CB    1 
ATOM   4078  O  OG1   . THR   B 1  80  ? -11.619 31.489  28.560   1.00 48.35  ? 80  THR   C OG1   1 
ATOM   4079  C  CG2   . THR   B 1  80  ? -13.579 32.151  29.776   1.00 42.67  ? 80  THR   C CG2   1 
ATOM   4080  N  N     . GLY   B 1  81  ? -10.870 33.894  26.288   1.00 49.21  ? 81  GLY   C N     1 
ATOM   4081  C  CA    . GLY   B 1  81  ? -9.581  34.030  25.630   1.00 48.25  ? 81  GLY   C CA    1 
ATOM   4082  C  C     . GLY   B 1  81  ? -9.143  35.474  25.449   1.00 48.07  ? 81  GLY   C C     1 
ATOM   4083  O  O     . GLY   B 1  81  ? -9.827  36.419  25.839   1.00 47.61  ? 81  GLY   C O     1 
ATOM   4084  N  N     . THR   B 1  82  ? -7.969  35.637  24.822   1.00 42.24  ? 82  THR   C N     1 
ATOM   4085  C  CA    . THR   B 1  82  ? -7.363  36.963  24.666   1.00 36.61  ? 82  THR   C CA    1 
ATOM   4086  C  C     . THR   B 1  82  ? -8.230  37.946  23.885   1.00 43.06  ? 82  THR   C C     1 
ATOM   4087  O  O     . THR   B 1  82  ? -7.964  39.154  23.915   1.00 45.67  ? 82  THR   C O     1 
ATOM   4088  C  CB    . THR   B 1  82  ? -6.016  36.859  23.963   1.00 43.34  ? 82  THR   C CB    1 
ATOM   4089  O  OG1   . THR   B 1  82  ? -5.222  35.855  24.602   1.00 50.25  ? 82  THR   C OG1   1 
ATOM   4090  C  CG2   . THR   B 1  82  ? -5.282  38.218  24.022   1.00 44.26  ? 82  THR   C CG2   1 
ATOM   4091  N  N     . TYR   B 1  83  ? -9.239  37.472  23.165   1.00 41.15  ? 83  TYR   C N     1 
ATOM   4092  C  CA    . TYR   B 1  83  ? -10.107 38.366  22.414   1.00 48.36  ? 83  TYR   C CA    1 
ATOM   4093  C  C     . TYR   B 1  83  ? -11.500 38.437  23.032   1.00 54.08  ? 83  TYR   C C     1 
ATOM   4094  O  O     . TYR   B 1  83  ? -12.454 38.865  22.374   1.00 50.90  ? 83  TYR   C O     1 
ATOM   4095  C  CB    . TYR   B 1  83  ? -10.127 37.941  20.941   1.00 47.76  ? 83  TYR   C CB    1 
ATOM   4096  C  CG    . TYR   B 1  83  ? -8.788  38.244  20.291   1.00 41.95  ? 83  TYR   C CG    1 
ATOM   4097  C  CD1   . TYR   B 1  83  ? -7.746  37.320  20.327   1.00 42.50  ? 83  TYR   C CD1   1 
ATOM   4098  C  CD2   . TYR   B 1  83  ? -8.544  39.488  19.713   1.00 43.21  ? 83  TYR   C CD2   1 
ATOM   4099  C  CE1   . TYR   B 1  83  ? -6.500  37.613  19.767   1.00 39.01  ? 83  TYR   C CE1   1 
ATOM   4100  C  CE2   . TYR   B 1  83  ? -7.308  39.793  19.154   1.00 42.80  ? 83  TYR   C CE2   1 
ATOM   4101  C  CZ    . TYR   B 1  83  ? -6.289  38.853  19.188   1.00 44.92  ? 83  TYR   C CZ    1 
ATOM   4102  O  OH    . TYR   B 1  83  ? -5.062  39.167  18.631   1.00 53.00  ? 83  TYR   C OH    1 
ATOM   4103  N  N     . ARG   B 1  84  ? -11.607 38.072  24.317   1.00 55.72  ? 84  ARG   C N     1 
ATOM   4104  C  CA    . ARG   B 1  84  ? -12.887 38.031  25.015   1.00 47.65  ? 84  ARG   C CA    1 
ATOM   4105  C  C     . ARG   B 1  84  ? -13.587 39.384  25.001   1.00 47.03  ? 84  ARG   C C     1 
ATOM   4106  O  O     . ARG   B 1  84  ? -14.821 39.443  25.089   1.00 56.32  ? 84  ARG   C O     1 
ATOM   4107  C  CB    . ARG   B 1  84  ? -12.677 37.538  26.457   1.00 49.04  ? 84  ARG   C CB    1 
ATOM   4108  C  CG    . ARG   B 1  84  ? -12.477 38.631  27.507   1.00 53.09  ? 84  ARG   C CG    1 
ATOM   4109  C  CD    . ARG   B 1  84  ? -11.924 38.091  28.831   1.00 54.72  ? 84  ARG   C CD    1 
ATOM   4110  N  NE    . ARG   B 1  84  ? -10.481 38.289  28.924   1.00 63.65  ? 84  ARG   C NE    1 
ATOM   4111  C  CZ    . ARG   B 1  84  ? -9.900  39.333  29.505   1.00 79.90  ? 84  ARG   C CZ    1 
ATOM   4112  N  NH1   . ARG   B 1  84  ? -10.612 40.267  30.119   1.00 76.33  ? 84  ARG   C NH1   1 
ATOM   4113  N  NH2   . ARG   B 1  84  ? -8.569  39.446  29.466   1.00 74.05  ? 84  ARG   C NH2   1 
ATOM   4114  N  N     . GLN   B 1  85  ? -12.830 40.475  24.893   1.00 44.02  ? 85  GLN   C N     1 
ATOM   4115  C  CA    . GLN   B 1  85  ? -13.440 41.801  24.822   1.00 51.99  ? 85  GLN   C CA    1 
ATOM   4116  C  C     . GLN   B 1  85  ? -13.873 42.155  23.413   1.00 46.26  ? 85  GLN   C C     1 
ATOM   4117  O  O     . GLN   B 1  85  ? -14.697 43.060  23.237   1.00 49.34  ? 85  GLN   C O     1 
ATOM   4118  C  CB    . GLN   B 1  85  ? -12.477 42.882  25.334   1.00 54.03  ? 85  GLN   C CB    1 
ATOM   4119  C  CG    . GLN   B 1  85  ? -12.110 42.766  26.818   1.00 58.85  ? 85  GLN   C CG    1 
ATOM   4120  C  CD    . GLN   B 1  85  ? -10.842 43.538  27.158   1.00 68.40  ? 85  GLN   C CD    1 
ATOM   4121  O  OE1   . GLN   B 1  85  ? -10.908 44.650  27.681   1.00 65.43  ? 85  GLN   C OE1   1 
ATOM   4122  N  NE2   . GLN   B 1  85  ? -9.679  42.953  26.855   1.00 60.81  ? 85  GLN   C NE2   1 
ATOM   4123  N  N     . LEU   B 1  86  ? -13.344 41.449  22.416   1.00 48.20  ? 86  LEU   C N     1 
ATOM   4124  C  CA    . LEU   B 1  86  ? -13.601 41.785  21.023   1.00 39.62  ? 86  LEU   C CA    1 
ATOM   4125  C  C     . LEU   B 1  86  ? -15.032 41.479  20.617   1.00 44.73  ? 86  LEU   C C     1 
ATOM   4126  O  O     . LEU   B 1  86  ? -15.558 42.122  19.702   1.00 45.93  ? 86  LEU   C O     1 
ATOM   4127  C  CB    . LEU   B 1  86  ? -12.627 41.017  20.136   1.00 47.89  ? 86  LEU   C CB    1 
ATOM   4128  C  CG    . LEU   B 1  86  ? -12.415 41.457  18.693   1.00 47.58  ? 86  LEU   C CG    1 
ATOM   4129  C  CD1   . LEU   B 1  86  ? -11.972 42.915  18.681   1.00 46.24  ? 86  LEU   C CD1   1 
ATOM   4130  C  CD2   . LEU   B 1  86  ? -11.386 40.550  17.992   1.00 35.87  ? 86  LEU   C CD2   1 
ATOM   4131  N  N     . PHE   B 1  87  ? -15.682 40.518  21.277   1.00 41.32  ? 87  PHE   C N     1 
ATOM   4132  C  CA    . PHE   B 1  87  ? -16.964 39.995  20.817   1.00 44.05  ? 87  PHE   C CA    1 
ATOM   4133  C  C     . PHE   B 1  87  ? -18.071 40.295  21.818   1.00 47.64  ? 87  PHE   C C     1 
ATOM   4134  O  O     . PHE   B 1  87  ? -17.924 40.018  23.014   1.00 53.67  ? 87  PHE   C O     1 
ATOM   4135  C  CB    . PHE   B 1  87  ? -16.888 38.478  20.590   1.00 47.10  ? 87  PHE   C CB    1 
ATOM   4136  C  CG    . PHE   B 1  87  ? -15.850 38.053  19.588   1.00 42.73  ? 87  PHE   C CG    1 
ATOM   4137  C  CD1   . PHE   B 1  87  ? -16.088 38.173  18.231   1.00 36.61  ? 87  PHE   C CD1   1 
ATOM   4138  C  CD2   . PHE   B 1  87  ? -14.644 37.510  20.006   1.00 43.73  ? 87  PHE   C CD2   1 
ATOM   4139  C  CE1   . PHE   B 1  87  ? -15.126 37.767  17.298   1.00 42.82  ? 87  PHE   C CE1   1 
ATOM   4140  C  CE2   . PHE   B 1  87  ? -13.683 37.110  19.081   1.00 41.96  ? 87  PHE   C CE2   1 
ATOM   4141  C  CZ    . PHE   B 1  87  ? -13.930 37.235  17.724   1.00 39.19  ? 87  PHE   C CZ    1 
ATOM   4142  N  N     . HIS   B 1  88  ? -19.189 40.825  21.325   1.00 48.09  ? 88  HIS   C N     1 
ATOM   4143  C  CA    . HIS   B 1  88  ? -20.350 41.017  22.178   1.00 40.04  ? 88  HIS   C CA    1 
ATOM   4144  C  C     . HIS   B 1  88  ? -20.873 39.653  22.621   1.00 44.05  ? 88  HIS   C C     1 
ATOM   4145  O  O     . HIS   B 1  88  ? -20.947 38.728  21.814   1.00 47.47  ? 88  HIS   C O     1 
ATOM   4146  C  CB    . HIS   B 1  88  ? -21.450 41.792  21.445   1.00 43.25  ? 88  HIS   C CB    1 
ATOM   4147  C  CG    . HIS   B 1  88  ? -22.619 42.164  22.315   1.00 52.79  ? 88  HIS   C CG    1 
ATOM   4148  N  ND1   . HIS   B 1  88  ? -23.488 41.231  22.843   1.00 56.05  ? 88  HIS   C ND1   1 
ATOM   4149  C  CD2   . HIS   B 1  88  ? -23.063 43.370  22.744   1.00 47.39  ? 88  HIS   C CD2   1 
ATOM   4150  C  CE1   . HIS   B 1  88  ? -24.410 41.845  23.565   1.00 53.40  ? 88  HIS   C CE1   1 
ATOM   4151  N  NE2   . HIS   B 1  88  ? -24.172 43.143  23.525   1.00 51.11  ? 88  HIS   C NE2   1 
ATOM   4152  N  N     . PRO   B 1  89  ? -21.233 39.496  23.890   1.00 49.07  ? 89  PRO   C N     1 
ATOM   4153  C  CA    . PRO   B 1  89  ? -21.677 38.169  24.356   1.00 52.65  ? 89  PRO   C CA    1 
ATOM   4154  C  C     . PRO   B 1  89  ? -22.656 37.489  23.421   1.00 47.46  ? 89  PRO   C C     1 
ATOM   4155  O  O     . PRO   B 1  89  ? -22.554 36.272  23.196   1.00 34.90  ? 89  PRO   C O     1 
ATOM   4156  C  CB    . PRO   B 1  89  ? -22.304 38.489  25.721   1.00 44.05  ? 89  PRO   C CB    1 
ATOM   4157  C  CG    . PRO   B 1  89  ? -21.464 39.614  26.214   1.00 43.56  ? 89  PRO   C CG    1 
ATOM   4158  C  CD    . PRO   B 1  89  ? -21.177 40.474  24.987   1.00 40.39  ? 89  PRO   C CD    1 
ATOM   4159  N  N     . GLU   B 1  90  ? -23.596 38.262  22.858   1.00 51.86  ? 90  GLU   C N     1 
ATOM   4160  C  CA    . GLU   B 1  90  ? -24.641 37.760  21.971   1.00 43.23  ? 90  GLU   C CA    1 
ATOM   4161  C  C     . GLU   B 1  90  ? -24.105 37.226  20.656   1.00 46.65  ? 90  GLU   C C     1 
ATOM   4162  O  O     . GLU   B 1  90  ? -24.861 36.569  19.925   1.00 43.76  ? 90  GLU   C O     1 
ATOM   4163  C  CB    . GLU   B 1  90  ? -25.654 38.862  21.673   1.00 48.86  ? 90  GLU   C CB    1 
ATOM   4164  C  CG    . GLU   B 1  90  ? -26.349 39.418  22.903   1.00 57.88  ? 90  GLU   C CG    1 
ATOM   4165  C  CD    . GLU   B 1  90  ? -27.725 39.943  22.581   1.00 54.26  ? 90  GLU   C CD    1 
ATOM   4166  O  OE1   . GLU   B 1  90  ? -28.002 40.168  21.382   1.00 61.45  ? 90  GLU   C OE1   1 
ATOM   4167  O  OE2   . GLU   B 1  90  ? -28.534 40.113  23.516   1.00 64.94  ? 90  GLU   C OE2   1 
ATOM   4168  N  N     . GLN   B 1  91  ? -22.844 37.523  20.318   1.00 40.21  ? 91  GLN   C N     1 
ATOM   4169  C  CA    . GLN   B 1  91  ? -22.222 36.951  19.126   1.00 47.57  ? 91  GLN   C CA    1 
ATOM   4170  C  C     . GLN   B 1  91  ? -21.653 35.557  19.362   1.00 44.65  ? 91  GLN   C C     1 
ATOM   4171  O  O     . GLN   B 1  91  ? -21.188 34.939  18.400   1.00 39.19  ? 91  GLN   C O     1 
ATOM   4172  C  CB    . GLN   B 1  91  ? -21.094 37.848  18.610   1.00 36.48  ? 91  GLN   C CB    1 
ATOM   4173  C  CG    . GLN   B 1  91  ? -21.547 39.124  17.995   1.00 39.15  ? 91  GLN   C CG    1 
ATOM   4174  C  CD    . GLN   B 1  91  ? -20.402 40.094  17.763   1.00 39.94  ? 91  GLN   C CD    1 
ATOM   4175  O  OE1   . GLN   B 1  91  ? -20.240 41.065  18.506   1.00 42.62  ? 91  GLN   C OE1   1 
ATOM   4176  N  NE2   . GLN   B 1  91  ? -19.611 39.841  16.731   1.00 22.96  ? 91  GLN   C NE2   1 
ATOM   4177  N  N     . LEU   B 1  92  ? -21.661 35.064  20.608   1.00 38.83  ? 92  LEU   C N     1 
ATOM   4178  C  CA    . LEU   B 1  92  ? -21.086 33.767  20.956   1.00 36.19  ? 92  LEU   C CA    1 
ATOM   4179  C  C     . LEU   B 1  92  ? -22.225 32.869  21.444   1.00 36.92  ? 92  LEU   C C     1 
ATOM   4180  O  O     . LEU   B 1  92  ? -22.691 33.006  22.576   1.00 45.18  ? 92  LEU   C O     1 
ATOM   4181  C  CB    . LEU   B 1  92  ? -19.970 33.940  21.986   1.00 39.24  ? 92  LEU   C CB    1 
ATOM   4182  C  CG    . LEU   B 1  92  ? -18.870 34.955  21.627   1.00 36.72  ? 92  LEU   C CG    1 
ATOM   4183  C  CD1   . LEU   B 1  92  ? -17.800 34.949  22.672   1.00 30.53  ? 92  LEU   C CD1   1 
ATOM   4184  C  CD2   . LEU   B 1  92  ? -18.238 34.682  20.266   1.00 35.85  ? 92  LEU   C CD2   1 
ATOM   4185  N  N     . ILE   B 1  93  ? -22.668 31.947  20.586   1.00 38.43  ? 93  ILE   C N     1 
ATOM   4186  C  CA    . ILE   B 1  93  ? -23.930 31.220  20.740   1.00 33.53  ? 93  ILE   C CA    1 
ATOM   4187  C  C     . ILE   B 1  93  ? -23.615 29.740  20.903   1.00 36.07  ? 93  ILE   C C     1 
ATOM   4188  O  O     . ILE   B 1  93  ? -23.158 29.095  19.951   1.00 34.10  ? 93  ILE   C O     1 
ATOM   4189  C  CB    . ILE   B 1  93  ? -24.854 31.425  19.534   1.00 32.32  ? 93  ILE   C CB    1 
ATOM   4190  C  CG1   . ILE   B 1  93  ? -25.132 32.892  19.282   1.00 42.15  ? 93  ILE   C CG1   1 
ATOM   4191  C  CG2   . ILE   B 1  93  ? -26.174 30.628  19.659   1.00 25.00  ? 93  ILE   C CG2   1 
ATOM   4192  C  CD1   . ILE   B 1  93  ? -26.261 33.081  18.274   1.00 39.07  ? 93  ILE   C CD1   1 
ATOM   4193  N  N     . THR   B 1  94  ? -23.917 29.176  22.074   1.00 40.11  ? 94  THR   C N     1 
ATOM   4194  C  CA    . THR   B 1  94  ? -23.633 27.773  22.352   1.00 41.81  ? 94  THR   C CA    1 
ATOM   4195  C  C     . THR   B 1  94  ? -24.874 27.072  22.886   1.00 36.74  ? 94  THR   C C     1 
ATOM   4196  O  O     . THR   B 1  94  ? -25.689 27.674  23.577   1.00 38.94  ? 94  THR   C O     1 
ATOM   4197  C  CB    . THR   B 1  94  ? -22.484 27.628  23.367   1.00 44.48  ? 94  THR   C CB    1 
ATOM   4198  O  OG1   . THR   B 1  94  ? -22.874 28.217  24.613   1.00 43.46  ? 94  THR   C OG1   1 
ATOM   4199  C  CG2   . THR   B 1  94  ? -21.185 28.316  22.852   1.00 37.35  ? 94  THR   C CG2   1 
ATOM   4200  N  N     . GLY   B 1  95  ? -25.029 25.799  22.528   1.00 31.21  ? 95  GLY   C N     1 
ATOM   4201  C  CA    . GLY   B 1  95  ? -25.982 24.923  23.172   1.00 29.09  ? 95  GLY   C CA    1 
ATOM   4202  C  C     . GLY   B 1  95  ? -25.318 24.120  24.286   1.00 49.42  ? 95  GLY   C C     1 
ATOM   4203  O  O     . GLY   B 1  95  ? -24.206 24.416  24.733   1.00 48.22  ? 95  GLY   C O     1 
ATOM   4204  N  N     . LYS   B 1  96  ? -26.019 23.072  24.731   1.00 41.30  ? 96  LYS   C N     1 
ATOM   4205  C  CA    . LYS   B 1  96  ? -25.530 22.214  25.811   1.00 47.73  ? 96  LYS   C CA    1 
ATOM   4206  C  C     . LYS   B 1  96  ? -25.025 20.855  25.345   1.00 50.32  ? 96  LYS   C C     1 
ATOM   4207  O  O     . LYS   B 1  96  ? -24.013 20.366  25.853   1.00 60.83  ? 96  LYS   C O     1 
ATOM   4208  C  CB    . LYS   B 1  96  ? -26.625 22.007  26.863   1.00 49.16  ? 96  LYS   C CB    1 
ATOM   4209  C  CG    . LYS   B 1  96  ? -26.684 23.107  27.922   1.00 59.47  ? 96  LYS   C CG    1 
ATOM   4210  C  CD    . LYS   B 1  96  ? -27.740 22.833  29.002   1.00 60.13  ? 96  LYS   C CD    1 
ATOM   4211  C  CE    . LYS   B 1  96  ? -27.809 23.974  30.026   1.00 71.70  ? 96  LYS   C CE    1 
ATOM   4212  N  NZ    . LYS   B 1  96  ? -26.494 24.243  30.705   1.00 71.40  ? 96  LYS   C NZ    1 
ATOM   4213  N  N     . GLU   B 1  97  ? -25.691 20.245  24.378   1.00 38.58  ? 97  GLU   C N     1 
ATOM   4214  C  CA    . GLU   B 1  97  ? -25.386 18.908  23.900   1.00 42.90  ? 97  GLU   C CA    1 
ATOM   4215  C  C     . GLU   B 1  97  ? -25.064 19.002  22.417   1.00 41.27  ? 97  GLU   C C     1 
ATOM   4216  O  O     . GLU   B 1  97  ? -25.801 19.648  21.668   1.00 38.79  ? 97  GLU   C O     1 
ATOM   4217  C  CB    . GLU   B 1  97  ? -26.587 17.993  24.161   1.00 45.97  ? 97  GLU   C CB    1 
ATOM   4218  C  CG    . GLU   B 1  97  ? -26.592 16.643  23.492   1.00 43.62  ? 97  GLU   C CG    1 
ATOM   4219  C  CD    . GLU   B 1  97  ? -27.777 15.798  23.955   1.00 57.18  ? 97  GLU   C CD    1 
ATOM   4220  O  OE1   . GLU   B 1  97  ? -28.928 16.288  23.899   1.00 61.58  ? 97  GLU   C OE1   1 
ATOM   4221  O  OE2   . GLU   B 1  97  ? -27.556 14.652  24.396   1.00 62.87  ? 97  GLU   C OE2   1 
ATOM   4222  N  N     . ASP   B 1  98  ? -23.975 18.366  21.988   1.00 36.11  ? 98  ASP   C N     1 
ATOM   4223  C  CA    . ASP   B 1  98  ? -23.511 18.570  20.623   1.00 32.07  ? 98  ASP   C CA    1 
ATOM   4224  C  C     . ASP   B 1  98  ? -24.139 17.522  19.711   1.00 35.42  ? 98  ASP   C C     1 
ATOM   4225  O  O     . ASP   B 1  98  ? -25.113 16.854  20.066   1.00 37.06  ? 98  ASP   C O     1 
ATOM   4226  C  CB    . ASP   B 1  98  ? -21.971 18.591  20.554   1.00 26.27  ? 98  ASP   C CB    1 
ATOM   4227  C  CG    . ASP   B 1  98  ? -21.324 17.200  20.627   1.00 25.27  ? 98  ASP   C CG    1 
ATOM   4228  O  OD1   . ASP   B 1  98  ? -21.874 16.210  20.097   1.00 32.81  ? 98  ASP   C OD1   1 
ATOM   4229  O  OD2   . ASP   B 1  98  ? -20.203 17.112  21.178   1.00 26.76  ? 98  ASP   C OD2   1 
ATOM   4230  N  N     . ALA   B 1  99  ? -23.585 17.363  18.521   1.00 32.81  ? 99  ALA   C N     1 
ATOM   4231  C  CA    . ALA   B 1  99  ? -24.238 16.559  17.518   1.00 27.07  ? 99  ALA   C CA    1 
ATOM   4232  C  C     . ALA   B 1  99  ? -23.689 15.153  17.446   1.00 29.13  ? 99  ALA   C C     1 
ATOM   4233  O  O     . ALA   B 1  99  ? -24.263 14.320  16.732   1.00 33.48  ? 99  ALA   C O     1 
ATOM   4234  C  CB    . ALA   B 1  99  ? -24.134 17.243  16.152   1.00 24.33  ? 99  ALA   C CB    1 
ATOM   4235  N  N     . ALA   B 1  100 ? -22.607 14.856  18.153   1.00 19.57  ? 100 ALA   C N     1 
ATOM   4236  C  CA    . ALA   B 1  100 ? -22.089 13.483  18.173   1.00 30.54  ? 100 ALA   C CA    1 
ATOM   4237  C  C     . ALA   B 1  100 ? -21.754 12.978  16.757   1.00 34.07  ? 100 ALA   C C     1 
ATOM   4238  O  O     . ALA   B 1  100 ? -22.138 11.871  16.353   1.00 24.61  ? 100 ALA   C O     1 
ATOM   4239  C  CB    . ALA   B 1  100 ? -23.090 12.547  18.861   1.00 20.14  ? 100 ALA   C CB    1 
ATOM   4240  N  N     . ASN   B 1  101 ? -21.047 13.815  15.986   1.00 32.91  ? 101 ASN   C N     1 
ATOM   4241  C  CA    . ASN   B 1  101 ? -20.617 13.472  14.615   1.00 25.37  ? 101 ASN   C CA    1 
ATOM   4242  C  C     . ASN   B 1  101 ? -21.739 12.862  13.799   1.00 24.47  ? 101 ASN   C C     1 
ATOM   4243  O  O     . ASN   B 1  101 ? -21.507 11.987  12.958   1.00 34.68  ? 101 ASN   C O     1 
ATOM   4244  C  CB    . ASN   B 1  101 ? -19.416 12.534  14.624   1.00 22.12  ? 101 ASN   C CB    1 
ATOM   4245  C  CG    . ASN   B 1  101 ? -18.297 13.040  15.514   1.00 31.02  ? 101 ASN   C CG    1 
ATOM   4246  O  OD1   . ASN   B 1  101 ? -17.740 12.290  16.326   1.00 31.24  ? 101 ASN   C OD1   1 
ATOM   4247  N  ND2   . ASN   B 1  101 ? -17.961 14.323  15.367   1.00 28.25  ? 101 ASN   C ND2   1 
ATOM   4248  N  N     . ASN   B 1  102 ? -22.964 13.319  14.034   1.00 24.75  ? 102 ASN   C N     1 
ATOM   4249  C  CA    . ASN   B 1  102 ? -24.143 12.812  13.339   1.00 30.36  ? 102 ASN   C CA    1 
ATOM   4250  C  C     . ASN   B 1  102 ? -24.784 13.980  12.606   1.00 28.81  ? 102 ASN   C C     1 
ATOM   4251  O  O     . ASN   B 1  102 ? -25.385 14.858  13.238   1.00 28.71  ? 102 ASN   C O     1 
ATOM   4252  C  CB    . ASN   B 1  102 ? -25.130 12.159  14.325   1.00 31.79  ? 102 ASN   C CB    1 
ATOM   4253  C  CG    . ASN   B 1  102 ? -26.348 11.517  13.632   1.00 31.71  ? 102 ASN   C CG    1 
ATOM   4254  O  OD1   . ASN   B 1  102 ? -26.691 11.869  12.499   1.00 34.99  ? 102 ASN   C OD1   1 
ATOM   4255  N  ND2   . ASN   B 1  102 ? -27.000 10.571  14.321   1.00 27.79  ? 102 ASN   C ND2   1 
ATOM   4256  N  N     . TYR   B 1  103 ? -24.655 13.993  11.275   1.00 30.56  ? 103 TYR   C N     1 
ATOM   4257  C  CA    . TYR   B 1  103 ? -25.335 15.013  10.479   1.00 30.36  ? 103 TYR   C CA    1 
ATOM   4258  C  C     . TYR   B 1  103 ? -26.783 15.158  10.923   1.00 35.34  ? 103 TYR   C C     1 
ATOM   4259  O  O     . TYR   B 1  103 ? -27.290 16.278  11.073   1.00 27.64  ? 103 TYR   C O     1 
ATOM   4260  C  CB    . TYR   B 1  103 ? -25.266 14.653  8.996    1.00 27.39  ? 103 TYR   C CB    1 
ATOM   4261  C  CG    . TYR   B 1  103 ? -26.052 15.573  8.092    1.00 35.19  ? 103 TYR   C CG    1 
ATOM   4262  C  CD1   . TYR   B 1  103 ? -27.445 15.433  7.950    1.00 36.56  ? 103 TYR   C CD1   1 
ATOM   4263  C  CD2   . TYR   B 1  103 ? -25.413 16.570  7.356    1.00 32.66  ? 103 TYR   C CD2   1 
ATOM   4264  C  CE1   . TYR   B 1  103 ? -28.175 16.269  7.118    1.00 28.92  ? 103 TYR   C CE1   1 
ATOM   4265  C  CE2   . TYR   B 1  103 ? -26.138 17.416  6.519    1.00 34.33  ? 103 TYR   C CE2   1 
ATOM   4266  C  CZ    . TYR   B 1  103 ? -27.516 17.260  6.407    1.00 28.16  ? 103 TYR   C CZ    1 
ATOM   4267  O  OH    . TYR   B 1  103 ? -28.220 18.080  5.580    1.00 27.19  ? 103 TYR   C OH    1 
ATOM   4268  N  N     . ALA   B 1  104 ? -27.452 14.022  11.158   1.00 34.57  ? 104 ALA   C N     1 
ATOM   4269  C  CA    . ALA   B 1  104 ? -28.851 14.041  11.555   1.00 30.30  ? 104 ALA   C CA    1 
ATOM   4270  C  C     . ALA   B 1  104 ? -29.059 14.953  12.752   1.00 36.29  ? 104 ALA   C C     1 
ATOM   4271  O  O     . ALA   B 1  104 ? -29.923 15.838  12.733   1.00 33.43  ? 104 ALA   C O     1 
ATOM   4272  C  CB    . ALA   B 1  104 ? -29.329 12.625  11.855   1.00 28.21  ? 104 ALA   C CB    1 
ATOM   4273  N  N     . ARG   B 1  105 ? -28.261 14.771  13.806   1.00 38.67  ? 105 ARG   C N     1 
ATOM   4274  C  CA    . ARG   B 1  105 ? -28.442 15.630  14.974   1.00 35.45  ? 105 ARG   C CA    1 
ATOM   4275  C  C     . ARG   B 1  105 ? -28.199 17.091  14.614   1.00 33.45  ? 105 ARG   C C     1 
ATOM   4276  O  O     . ARG   B 1  105 ? -28.991 17.962  14.986   1.00 36.66  ? 105 ARG   C O     1 
ATOM   4277  C  CB    . ARG   B 1  105 ? -27.550 15.162  16.129   1.00 30.51  ? 105 ARG   C CB    1 
ATOM   4278  C  CG    . ARG   B 1  105 ? -27.971 13.771  16.630   1.00 36.43  ? 105 ARG   C CG    1 
ATOM   4279  C  CD    . ARG   B 1  105 ? -27.012 13.125  17.631   1.00 27.36  ? 105 ARG   C CD    1 
ATOM   4280  N  NE    . ARG   B 1  105 ? -26.901 13.877  18.869   1.00 32.73  ? 105 ARG   C NE    1 
ATOM   4281  C  CZ    . ARG   B 1  105 ? -27.746 13.778  19.887   1.00 40.67  ? 105 ARG   C CZ    1 
ATOM   4282  N  NH1   . ARG   B 1  105 ? -28.770 12.934  19.859   1.00 25.92  ? 105 ARG   C NH1   1 
ATOM   4283  N  NH2   . ARG   B 1  105 ? -27.564 14.556  20.956   1.00 38.90  ? 105 ARG   C NH2   1 
ATOM   4284  N  N     . GLY   B 1  106 ? -27.144 17.372  13.837   1.00 37.67  ? 106 GLY   C N     1 
ATOM   4285  C  CA    . GLY   B 1  106 ? -26.845 18.754  13.478   1.00 29.24  ? 106 GLY   C CA    1 
ATOM   4286  C  C     . GLY   B 1  106 ? -27.974 19.426  12.707   1.00 30.19  ? 106 GLY   C C     1 
ATOM   4287  O  O     . GLY   B 1  106 ? -28.367 20.551  13.020   1.00 31.96  ? 106 GLY   C O     1 
ATOM   4288  N  N     . HIS   B 1  107 ? -28.508 18.752  11.684   1.00 26.49  ? 107 HIS   C N     1 
ATOM   4289  C  CA    . HIS   B 1  107 ? -29.567 19.360  10.881   1.00 30.45  ? 107 HIS   C CA    1 
ATOM   4290  C  C     . HIS   B 1  107 ? -30.927 19.367  11.586   1.00 38.79  ? 107 HIS   C C     1 
ATOM   4291  O  O     . HIS   B 1  107 ? -31.698 20.320  11.416   1.00 40.24  ? 107 HIS   C O     1 
ATOM   4292  C  CB    . HIS   B 1  107 ? -29.694 18.647  9.540    1.00 30.82  ? 107 HIS   C CB    1 
ATOM   4293  C  CG    . HIS   B 1  107 ? -30.512 19.399  8.523    1.00 37.95  ? 107 HIS   C CG    1 
ATOM   4294  N  ND1   . HIS   B 1  107 ? -31.883 19.267  8.416    1.00 38.98  ? 107 HIS   C ND1   1 
ATOM   4295  C  CD2   . HIS   B 1  107 ? -30.145 20.268  7.550    1.00 32.13  ? 107 HIS   C CD2   1 
ATOM   4296  C  CE1   . HIS   B 1  107 ? -32.325 20.022  7.427    1.00 38.85  ? 107 HIS   C CE1   1 
ATOM   4297  N  NE2   . HIS   B 1  107 ? -31.290 20.642  6.886    1.00 49.43  ? 107 HIS   C NE2   1 
ATOM   4298  N  N     . TYR   B 1  108 ? -31.255 18.320  12.360   1.00 41.96  ? 108 TYR   C N     1 
ATOM   4299  C  CA    . TYR   B 1  108 ? -32.608 18.149  12.903   1.00 38.77  ? 108 TYR   C CA    1 
ATOM   4300  C  C     . TYR   B 1  108 ? -32.652 18.153  14.429   1.00 44.05  ? 108 TYR   C C     1 
ATOM   4301  O  O     . TYR   B 1  108 ? -32.948 19.180  15.049   1.00 43.47  ? 108 TYR   C O     1 
ATOM   4302  C  CB    . TYR   B 1  108 ? -33.234 16.845  12.392   1.00 38.56  ? 108 TYR   C CB    1 
ATOM   4303  C  CG    . TYR   B 1  108 ? -33.202 16.675  10.880   1.00 46.41  ? 108 TYR   C CG    1 
ATOM   4304  C  CD1   . TYR   B 1  108 ? -32.096 16.103  10.242   1.00 43.06  ? 108 TYR   C CD1   1 
ATOM   4305  C  CD2   . TYR   B 1  108 ? -34.274 17.085  10.087   1.00 43.80  ? 108 TYR   C CD2   1 
ATOM   4306  C  CE1   . TYR   B 1  108 ? -32.063 15.950  8.863    1.00 36.97  ? 108 TYR   C CE1   1 
ATOM   4307  C  CE2   . TYR   B 1  108 ? -34.248 16.931  8.710    1.00 46.56  ? 108 TYR   C CE2   1 
ATOM   4308  C  CZ    . TYR   B 1  108 ? -33.138 16.373  8.103    1.00 42.12  ? 108 TYR   C CZ    1 
ATOM   4309  O  OH    . TYR   B 1  108 ? -33.112 16.222  6.737    1.00 42.34  ? 108 TYR   C OH    1 
ATOM   4310  N  N     . THR   B 1  109 ? -32.338 17.006  15.037   1.00 43.46  ? 109 THR   C N     1 
ATOM   4311  C  CA    . THR   B 1  109 ? -32.659 16.768  16.442   1.00 37.40  ? 109 THR   C CA    1 
ATOM   4312  C  C     . THR   B 1  109 ? -32.187 17.885  17.354   1.00 36.95  ? 109 THR   C C     1 
ATOM   4313  O  O     . THR   B 1  109 ? -32.959 18.398  18.168   1.00 43.38  ? 109 THR   C O     1 
ATOM   4314  C  CB    . THR   B 1  109 ? -32.063 15.441  16.887   1.00 37.81  ? 109 THR   C CB    1 
ATOM   4315  O  OG1   . THR   B 1  109 ? -32.477 14.421  15.970   1.00 31.74  ? 109 THR   C OG1   1 
ATOM   4316  C  CG2   . THR   B 1  109 ? -32.571 15.101  18.274   1.00 38.74  ? 109 THR   C CG2   1 
ATOM   4317  N  N     . ILE   B 1  110 ? -30.916 18.256  17.269   1.00 33.49  ? 110 ILE   C N     1 
ATOM   4318  C  CA    . ILE   B 1  110 ? -30.361 19.263  18.160   1.00 35.25  ? 110 ILE   C CA    1 
ATOM   4319  C  C     . ILE   B 1  110 ? -30.383 20.646  17.529   1.00 48.44  ? 110 ILE   C C     1 
ATOM   4320  O  O     . ILE   B 1  110 ? -30.663 21.636  18.215   1.00 46.67  ? 110 ILE   C O     1 
ATOM   4321  C  CB    . ILE   B 1  110 ? -28.931 18.891  18.603   1.00 42.36  ? 110 ILE   C CB    1 
ATOM   4322  C  CG1   . ILE   B 1  110 ? -28.913 17.507  19.250   1.00 36.49  ? 110 ILE   C CG1   1 
ATOM   4323  C  CG2   . ILE   B 1  110 ? -28.370 19.966  19.552   1.00 27.71  ? 110 ILE   C CG2   1 
ATOM   4324  C  CD1   . ILE   B 1  110 ? -29.603 17.459  20.554   1.00 41.50  ? 110 ILE   C CD1   1 
ATOM   4325  N  N     . GLY   B 1  111 ? -30.068 20.734  16.230   1.00 40.34  ? 111 GLY   C N     1 
ATOM   4326  C  CA    . GLY   B 1  111 ? -29.961 22.043  15.594   1.00 34.02  ? 111 GLY   C CA    1 
ATOM   4327  C  C     . GLY   B 1  111 ? -31.257 22.834  15.621   1.00 33.89  ? 111 GLY   C C     1 
ATOM   4328  O  O     . GLY   B 1  111 ? -31.248 24.046  15.838   1.00 42.76  ? 111 GLY   C O     1 
ATOM   4329  N  N     . LYS   B 1  112 ? -32.386 22.159  15.392   1.00 40.56  ? 112 LYS   C N     1 
ATOM   4330  C  CA    . LYS   B 1  112 ? -33.691 22.808  15.428   1.00 33.79  ? 112 LYS   C CA    1 
ATOM   4331  C  C     . LYS   B 1  112 ? -33.859 23.668  16.665   1.00 40.93  ? 112 LYS   C C     1 
ATOM   4332  O  O     . LYS   B 1  112 ? -34.521 24.708  16.611   1.00 49.53  ? 112 LYS   C O     1 
ATOM   4333  C  CB    . LYS   B 1  112 ? -34.801 21.751  15.397   1.00 45.49  ? 112 LYS   C CB    1 
ATOM   4334  C  CG    . LYS   B 1  112 ? -34.745 20.788  16.614   1.00 48.53  ? 112 LYS   C CG    1 
ATOM   4335  C  CD    . LYS   B 1  112 ? -36.048 20.015  16.846   1.00 41.46  ? 112 LYS   C CD    1 
ATOM   4336  C  CE    . LYS   B 1  112 ? -36.536 19.351  15.565   1.00 44.19  ? 112 LYS   C CE    1 
ATOM   4337  N  NZ    . LYS   B 1  112 ? -37.850 18.639  15.773   1.00 59.61  ? 112 LYS   C NZ    1 
ATOM   4338  N  N     . GLU   B 1  113 ? -33.276 23.259  17.791   1.00 34.56  ? 113 GLU   C N     1 
ATOM   4339  C  CA    . GLU   B 1  113 ? -33.575 23.954  19.037   1.00 36.10  ? 113 GLU   C CA    1 
ATOM   4340  C  C     . GLU   B 1  113 ? -32.912 25.314  19.113   1.00 34.39  ? 113 GLU   C C     1 
ATOM   4341  O  O     . GLU   B 1  113 ? -33.344 26.149  19.912   1.00 45.83  ? 113 GLU   C O     1 
ATOM   4342  C  CB    . GLU   B 1  113 ? -33.159 23.112  20.259   1.00 37.58  ? 113 GLU   C CB    1 
ATOM   4343  C  CG    . GLU   B 1  113 ? -33.966 21.826  20.481   1.00 36.90  ? 113 GLU   C CG    1 
ATOM   4344  C  CD    . GLU   B 1  113 ? -35.477 22.078  20.653   1.00 56.86  ? 113 GLU   C CD    1 
ATOM   4345  O  OE1   . GLU   B 1  113 ? -35.852 23.117  21.248   1.00 68.08  ? 113 GLU   C OE1   1 
ATOM   4346  O  OE2   . GLU   B 1  113 ? -36.290 21.242  20.190   1.00 59.09  ? 113 GLU   C OE2   1 
ATOM   4347  N  N     . ILE   B 1  114 ? -31.874 25.563  18.317   1.00 33.43  ? 114 ILE   C N     1 
ATOM   4348  C  CA    . ILE   B 1  114 ? -31.112 26.798  18.428   1.00 28.69  ? 114 ILE   C CA    1 
ATOM   4349  C  C     . ILE   B 1  114 ? -31.082 27.604  17.134   1.00 30.79  ? 114 ILE   C C     1 
ATOM   4350  O  O     . ILE   B 1  114 ? -30.575 28.723  17.141   1.00 30.64  ? 114 ILE   C O     1 
ATOM   4351  C  CB    . ILE   B 1  114 ? -29.678 26.528  18.928   1.00 33.42  ? 114 ILE   C CB    1 
ATOM   4352  C  CG1   . ILE   B 1  114 ? -29.068 27.817  19.495   1.00 31.76  ? 114 ILE   C CG1   1 
ATOM   4353  C  CG2   . ILE   B 1  114 ? -28.807 25.887  17.819   1.00 21.93  ? 114 ILE   C CG2   1 
ATOM   4354  C  CD1   . ILE   B 1  114 ? -27.802 27.597  20.293   1.00 23.82  ? 114 ILE   C CD1   1 
ATOM   4355  N  N     . ILE   B 1  115 ? -31.644 27.094  16.033   1.00 31.82  ? 115 ILE   C N     1 
ATOM   4356  C  CA    . ILE   B 1  115 ? -31.520 27.786  14.742   1.00 39.84  ? 115 ILE   C CA    1 
ATOM   4357  C  C     . ILE   B 1  115 ? -32.215 29.151  14.772   1.00 36.01  ? 115 ILE   C C     1 
ATOM   4358  O  O     . ILE   B 1  115 ? -31.637 30.167  14.356   1.00 36.76  ? 115 ILE   C O     1 
ATOM   4359  C  CB    . ILE   B 1  115 ? -32.044 26.902  13.593   1.00 42.47  ? 115 ILE   C CB    1 
ATOM   4360  C  CG1   . ILE   B 1  115 ? -32.091 27.696  12.280   1.00 34.71  ? 115 ILE   C CG1   1 
ATOM   4361  C  CG2   . ILE   B 1  115 ? -33.406 26.257  13.944   1.00 29.48  ? 115 ILE   C CG2   1 
ATOM   4362  C  CD1   . ILE   B 1  115 ? -30.754 28.127  11.781   1.00 34.43  ? 115 ILE   C CD1   1 
ATOM   4363  N  N     . ASP   B 1  116 ? -33.458 29.208  15.266   1.00 38.49  ? 116 ASP   C N     1 
ATOM   4364  C  CA    . ASP   B 1  116 ? -34.132 30.509  15.361   1.00 36.47  ? 116 ASP   C CA    1 
ATOM   4365  C  C     . ASP   B 1  116 ? -33.292 31.503  16.156   1.00 27.24  ? 116 ASP   C C     1 
ATOM   4366  O  O     . ASP   B 1  116 ? -33.080 32.637  15.717   1.00 33.62  ? 116 ASP   C O     1 
ATOM   4367  C  CB    . ASP   B 1  116 ? -35.534 30.370  15.963   1.00 20.45  ? 116 ASP   C CB    1 
ATOM   4368  C  CG    . ASP   B 1  116 ? -36.440 29.477  15.132   1.00 27.44  ? 116 ASP   C CG    1 
ATOM   4369  O  OD1   . ASP   B 1  116 ? -36.527 29.655  13.902   1.00 36.01  ? 116 ASP   C OD1   1 
ATOM   4370  O  OD2   . ASP   B 1  116 ? -37.045 28.557  15.700   1.00 43.63  ? 116 ASP   C OD2   1 
ATOM   4371  N  N     . LEU   B 1  117 ? -32.769 31.086  17.308   1.00 24.17  ? 117 LEU   C N     1 
ATOM   4372  C  CA    . LEU   B 1  117 ? -31.860 31.961  18.048   1.00 31.46  ? 117 LEU   C CA    1 
ATOM   4373  C  C     . LEU   B 1  117 ? -30.756 32.491  17.134   1.00 36.30  ? 117 LEU   C C     1 
ATOM   4374  O  O     . LEU   B 1  117 ? -30.521 33.702  17.048   1.00 36.02  ? 117 LEU   C O     1 
ATOM   4375  C  CB    . LEU   B 1  117 ? -31.260 31.210  19.241   1.00 29.37  ? 117 LEU   C CB    1 
ATOM   4376  C  CG    . LEU   B 1  117 ? -30.404 31.911  20.301   1.00 33.51  ? 117 LEU   C CG    1 
ATOM   4377  C  CD1   . LEU   B 1  117 ? -30.322 33.420  20.076   1.00 45.11  ? 117 LEU   C CD1   1 
ATOM   4378  C  CD2   . LEU   B 1  117 ? -30.983 31.645  21.671   1.00 37.20  ? 117 LEU   C CD2   1 
ATOM   4379  N  N     . VAL   B 1  118 ? -30.098 31.592  16.407   1.00 32.89  ? 118 VAL   C N     1 
ATOM   4380  C  CA    . VAL   B 1  118 ? -28.931 31.969  15.620   1.00 31.75  ? 118 VAL   C CA    1 
ATOM   4381  C  C     . VAL   B 1  118 ? -29.320 32.916  14.495   1.00 39.66  ? 118 VAL   C C     1 
ATOM   4382  O  O     . VAL   B 1  118 ? -28.695 33.971  14.306   1.00 34.62  ? 118 VAL   C O     1 
ATOM   4383  C  CB    . VAL   B 1  118 ? -28.235 30.713  15.081   1.00 33.93  ? 118 VAL   C CB    1 
ATOM   4384  C  CG1   . VAL   B 1  118 ? -27.143 31.115  14.115   1.00 28.60  ? 118 VAL   C CG1   1 
ATOM   4385  C  CG2   . VAL   B 1  118 ? -27.705 29.865  16.257   1.00 27.08  ? 118 VAL   C CG2   1 
ATOM   4386  N  N     . LEU   B 1  119 ? -30.341 32.543  13.710   1.00 38.95  ? 119 LEU   C N     1 
ATOM   4387  C  CA    . LEU   B 1  119 ? -30.804 33.433  12.649   1.00 36.57  ? 119 LEU   C CA    1 
ATOM   4388  C  C     . LEU   B 1  119 ? -31.195 34.786  13.211   1.00 38.88  ? 119 LEU   C C     1 
ATOM   4389  O  O     . LEU   B 1  119 ? -31.020 35.808  12.532   1.00 40.11  ? 119 LEU   C O     1 
ATOM   4390  C  CB    . LEU   B 1  119 ? -31.992 32.827  11.896   1.00 35.17  ? 119 LEU   C CB    1 
ATOM   4391  C  CG    . LEU   B 1  119 ? -31.705 31.766  10.851   1.00 31.57  ? 119 LEU   C CG    1 
ATOM   4392  C  CD1   . LEU   B 1  119 ? -33.031 31.186  10.414   1.00 41.87  ? 119 LEU   C CD1   1 
ATOM   4393  C  CD2   . LEU   B 1  119 ? -31.006 32.378  9.676    1.00 28.54  ? 119 LEU   C CD2   1 
ATOM   4394  N  N     . ASP   B 1  120 ? -31.720 34.816  14.445   1.00 38.23  ? 120 ASP   C N     1 
ATOM   4395  C  CA    A ASP   B 1  120 ? -32.042 36.087  15.087   0.41 36.91  ? 120 ASP   C CA    1 
ATOM   4396  C  CA    B ASP   B 1  120 ? -32.049 36.097  15.061   0.59 36.95  ? 120 ASP   C CA    1 
ATOM   4397  C  C     . ASP   B 1  120 ? -30.796 36.946  15.262   1.00 36.04  ? 120 ASP   C C     1 
ATOM   4398  O  O     . ASP   B 1  120 ? -30.775 38.120  14.885   1.00 39.14  ? 120 ASP   C O     1 
ATOM   4399  C  CB    A ASP   B 1  120 ? -32.717 35.838  16.435   0.41 34.64  ? 120 ASP   C CB    1 
ATOM   4400  C  CB    B ASP   B 1  120 ? -32.802 35.887  16.378   0.59 34.58  ? 120 ASP   C CB    1 
ATOM   4401  C  CG    A ASP   B 1  120 ? -32.935 37.115  17.220   0.41 35.31  ? 120 ASP   C CG    1 
ATOM   4402  C  CG    B ASP   B 1  120 ? -34.318 35.728  16.183   0.59 38.78  ? 120 ASP   C CG    1 
ATOM   4403  O  OD1   A ASP   B 1  120 ? -33.635 38.003  16.697   0.41 34.54  ? 120 ASP   C OD1   1 
ATOM   4404  O  OD1   B ASP   B 1  120 ? -34.861 36.216  15.161   0.59 37.56  ? 120 ASP   C OD1   1 
ATOM   4405  O  OD2   A ASP   B 1  120 ? -32.409 37.233  18.353   0.41 35.17  ? 120 ASP   C OD2   1 
ATOM   4406  O  OD2   B ASP   B 1  120 ? -34.970 35.115  17.067   0.59 37.55  ? 120 ASP   C OD2   1 
ATOM   4407  N  N     . ARG   B 1  121 ? -29.734 36.370  15.841   1.00 34.52  ? 121 ARG   C N     1 
ATOM   4408  C  CA    . ARG   B 1  121 ? -28.498 37.138  16.017   1.00 39.01  ? 121 ARG   C CA    1 
ATOM   4409  C  C     . ARG   B 1  121 ? -27.902 37.556  14.673   1.00 41.11  ? 121 ARG   C C     1 
ATOM   4410  O  O     . ARG   B 1  121 ? -27.443 38.696  14.522   1.00 40.67  ? 121 ARG   C O     1 
ATOM   4411  C  CB    . ARG   B 1  121 ? -27.463 36.349  16.817   1.00 34.39  ? 121 ARG   C CB    1 
ATOM   4412  C  CG    . ARG   B 1  121 ? -27.925 35.883  18.189   1.00 43.49  ? 121 ARG   C CG    1 
ATOM   4413  C  CD    . ARG   B 1  121 ? -27.781 36.948  19.276   1.00 42.79  ? 121 ARG   C CD    1 
ATOM   4414  N  NE    . ARG   B 1  121 ? -28.747 36.675  20.329   1.00 46.44  ? 121 ARG   C NE    1 
ATOM   4415  C  CZ    . ARG   B 1  121 ? -28.558 35.808  21.313   1.00 52.57  ? 121 ARG   C CZ    1 
ATOM   4416  N  NH1   . ARG   B 1  121 ? -27.383 35.217  21.497   1.00 39.07  ? 121 ARG   C NH1   1 
ATOM   4417  N  NH2   . ARG   B 1  121 ? -29.578 35.516  22.124   1.00 47.45  ? 121 ARG   C NH2   1 
ATOM   4418  N  N     . ILE   B 1  122 ? -27.879 36.649  13.687   1.00 33.71  ? 122 ILE   C N     1 
ATOM   4419  C  CA    . ILE   B 1  122 ? -27.423 37.041  12.352   1.00 34.77  ? 122 ILE   C CA    1 
ATOM   4420  C  C     . ILE   B 1  122 ? -28.226 38.244  11.858   1.00 38.20  ? 122 ILE   C C     1 
ATOM   4421  O  O     . ILE   B 1  122 ? -27.683 39.175  11.249   1.00 37.10  ? 122 ILE   C O     1 
ATOM   4422  C  CB    . ILE   B 1  122 ? -27.522 35.856  11.370   1.00 34.38  ? 122 ILE   C CB    1 
ATOM   4423  C  CG1   . ILE   B 1  122 ? -26.552 34.720  11.737   1.00 27.96  ? 122 ILE   C CG1   1 
ATOM   4424  C  CG2   . ILE   B 1  122 ? -27.315 36.327  9.934    1.00 30.64  ? 122 ILE   C CG2   1 
ATOM   4425  C  CD1   . ILE   B 1  122 ? -26.934 33.348  11.104   1.00 22.16  ? 122 ILE   C CD1   1 
ATOM   4426  N  N     . ARG   B 1  123 ? -29.530 38.253  12.144   1.00 40.65  ? 123 ARG   C N     1 
ATOM   4427  C  CA    . ARG   B 1  123 ? -30.383 39.360  11.733   1.00 37.87  ? 123 ARG   C CA    1 
ATOM   4428  C  C     . ARG   B 1  123 ? -29.988 40.658  12.427   1.00 36.07  ? 123 ARG   C C     1 
ATOM   4429  O  O     . ARG   B 1  123 ? -29.956 41.723  11.796   1.00 39.13  ? 123 ARG   C O     1 
ATOM   4430  C  CB    . ARG   B 1  123 ? -31.845 39.005  12.008   1.00 38.32  ? 123 ARG   C CB    1 
ATOM   4431  C  CG    . ARG   B 1  123 ? -32.809 40.152  11.808   1.00 41.59  ? 123 ARG   C CG    1 
ATOM   4432  C  CD    . ARG   B 1  123 ? -32.620 40.776  10.443   1.00 43.83  ? 123 ARG   C CD    1 
ATOM   4433  N  NE    . ARG   B 1  123 ? -33.116 39.920  9.371    1.00 43.40  ? 123 ARG   C NE    1 
ATOM   4434  C  CZ    . ARG   B 1  123 ? -33.023 40.224  8.081    1.00 50.47  ? 123 ARG   C CZ    1 
ATOM   4435  N  NH1   . ARG   B 1  123 ? -32.433 41.343  7.672    1.00 47.23  ? 123 ARG   C NH1   1 
ATOM   4436  N  NH2   . ARG   B 1  123 ? -33.534 39.388  7.179    1.00 43.20  ? 123 ARG   C NH2   1 
ATOM   4437  N  N     . LYS   B 1  124 ? -29.671 40.593  13.722   1.00 38.85  ? 124 LYS   C N     1 
ATOM   4438  C  CA    . LYS   B 1  124 ? -29.197 41.781  14.430   1.00 33.55  ? 124 LYS   C CA    1 
ATOM   4439  C  C     . LYS   B 1  124 ? -27.965 42.369  13.750   1.00 40.81  ? 124 LYS   C C     1 
ATOM   4440  O  O     . LYS   B 1  124 ? -27.860 43.586  13.583   1.00 44.42  ? 124 LYS   C O     1 
ATOM   4441  C  CB    . LYS   B 1  124 ? -28.892 41.430  15.886   1.00 37.27  ? 124 LYS   C CB    1 
ATOM   4442  C  CG    . LYS   B 1  124 ? -27.821 42.335  16.526   1.00 60.34  ? 124 LYS   C CG    1 
ATOM   4443  C  CD    . LYS   B 1  124 ? -27.260 41.769  17.847   1.00 57.63  ? 124 LYS   C CD    1 
ATOM   4444  C  CE    . LYS   B 1  124 ? -26.143 42.639  18.415   1.00 48.80  ? 124 LYS   C CE    1 
ATOM   4445  N  NZ    . LYS   B 1  124 ? -25.277 41.876  19.356   1.00 55.21  ? 124 LYS   C NZ    1 
ATOM   4446  N  N     . LEU   B 1  125 ? -27.032 41.511  13.331   1.00 45.44  ? 125 LEU   C N     1 
ATOM   4447  C  CA    . LEU   B 1  125 ? -25.836 41.971  12.639   1.00 36.73  ? 125 LEU   C CA    1 
ATOM   4448  C  C     . LEU   B 1  125 ? -26.170 42.611  11.297   1.00 37.32  ? 125 LEU   C C     1 
ATOM   4449  O  O     . LEU   B 1  125 ? -25.572 43.628  10.921   1.00 40.01  ? 125 LEU   C O     1 
ATOM   4450  C  CB    . LEU   B 1  125 ? -24.878 40.799  12.441   1.00 30.03  ? 125 LEU   C CB    1 
ATOM   4451  C  CG    . LEU   B 1  125 ? -24.184 40.267  13.687   1.00 33.41  ? 125 LEU   C CG    1 
ATOM   4452  C  CD1   . LEU   B 1  125 ? -23.118 39.258  13.326   1.00 33.29  ? 125 LEU   C CD1   1 
ATOM   4453  C  CD2   . LEU   B 1  125 ? -23.573 41.405  14.452   1.00 35.30  ? 125 LEU   C CD2   1 
ATOM   4454  N  N     . ALA   B 1  126 ? -27.091 42.013  10.541   1.00 32.51  ? 126 ALA   C N     1 
ATOM   4455  C  CA    . ALA   B 1  126 ? -27.402 42.543  9.217    1.00 39.02  ? 126 ALA   C CA    1 
ATOM   4456  C  C     . ALA   B 1  126 ? -28.000 43.942  9.297    1.00 45.72  ? 126 ALA   C C     1 
ATOM   4457  O  O     . ALA   B 1  126 ? -27.749 44.783  8.419    1.00 41.55  ? 126 ALA   C O     1 
ATOM   4458  C  CB    . ALA   B 1  126 ? -28.353 41.600  8.476    1.00 34.18  ? 126 ALA   C CB    1 
ATOM   4459  N  N     . ASP   B 1  127 ? -28.791 44.214  10.338   1.00 46.20  ? 127 ASP   C N     1 
ATOM   4460  C  CA    . ASP   B 1  127 ? -29.427 45.521  10.463   1.00 37.58  ? 127 ASP   C CA    1 
ATOM   4461  C  C     . ASP   B 1  127 ? -28.425 46.625  10.777   1.00 41.46  ? 127 ASP   C C     1 
ATOM   4462  O  O     . ASP   B 1  127 ? -28.768 47.804  10.650   1.00 49.87  ? 127 ASP   C O     1 
ATOM   4463  C  CB    . ASP   B 1  127 ? -30.521 45.471  11.531   1.00 39.44  ? 127 ASP   C CB    1 
ATOM   4464  C  CG    . ASP   B 1  127 ? -31.717 44.615  11.120   1.00 44.12  ? 127 ASP   C CG    1 
ATOM   4465  O  OD1   . ASP   B 1  127 ? -31.918 44.357  9.910    1.00 41.08  ? 127 ASP   C OD1   1 
ATOM   4466  O  OD2   . ASP   B 1  127 ? -32.465 44.199  12.022   1.00 41.47  ? 127 ASP   C OD2   1 
ATOM   4467  N  N     . GLN   B 1  128 ? -27.207 46.280  11.201   1.00 43.81  ? 128 GLN   C N     1 
ATOM   4468  C  CA    . GLN   B 1  128 ? -26.143 47.272  11.313   1.00 48.46  ? 128 GLN   C CA    1 
ATOM   4469  C  C     . GLN   B 1  128 ? -25.457 47.546  9.982    1.00 47.03  ? 128 GLN   C C     1 
ATOM   4470  O  O     . GLN   B 1  128 ? -24.603 48.433  9.914    1.00 47.16  ? 128 GLN   C O     1 
ATOM   4471  C  CB    . GLN   B 1  128 ? -25.095 46.829  12.321   1.00 37.24  ? 128 GLN   C CB    1 
ATOM   4472  C  CG    . GLN   B 1  128 ? -25.603 46.771  13.734   1.00 58.70  ? 128 GLN   C CG    1 
ATOM   4473  C  CD    . GLN   B 1  128 ? -24.564 46.203  14.697   1.00 69.49  ? 128 GLN   C CD    1 
ATOM   4474  O  OE1   . GLN   B 1  128 ? -23.424 46.686  14.766   1.00 71.12  ? 128 GLN   C OE1   1 
ATOM   4475  N  NE2   . GLN   B 1  128 ? -24.953 45.164  15.441   1.00 57.35  ? 128 GLN   C NE2   1 
ATOM   4476  N  N     . CYS   B 1  129 ? -25.806 46.812  8.931    1.00 45.46  ? 129 CYS   C N     1 
ATOM   4477  C  CA    . CYS   B 1  129 ? -25.183 46.987  7.626    1.00 50.75  ? 129 CYS   C CA    1 
ATOM   4478  C  C     . CYS   B 1  129 ? -26.011 47.939  6.782    1.00 42.53  ? 129 CYS   C C     1 
ATOM   4479  O  O     . CYS   B 1  129 ? -27.238 47.833  6.735    1.00 42.85  ? 129 CYS   C O     1 
ATOM   4480  C  CB    . CYS   B 1  129 ? -25.044 45.648  6.888    1.00 45.46  ? 129 CYS   C CB    1 
ATOM   4481  S  SG    . CYS   B 1  129 ? -23.975 44.432  7.681    1.00 39.72  ? 129 CYS   C SG    1 
ATOM   4482  N  N     . THR   B 1  130 ? -25.327 48.861  6.111    1.00 44.09  ? 130 THR   C N     1 
ATOM   4483  C  CA    . THR   B 1  130 ? -25.957 49.715  5.114    1.00 44.73  ? 130 THR   C CA    1 
ATOM   4484  C  C     . THR   B 1  130 ? -25.954 49.099  3.722    1.00 45.41  ? 130 THR   C C     1 
ATOM   4485  O  O     . THR   B 1  130 ? -26.737 49.523  2.865    1.00 44.90  ? 130 THR   C O     1 
ATOM   4486  C  CB    . THR   B 1  130 ? -25.246 51.058  5.066    1.00 40.24  ? 130 THR   C CB    1 
ATOM   4487  O  OG1   . THR   B 1  130 ? -23.892 50.840  4.679    1.00 47.20  ? 130 THR   C OG1   1 
ATOM   4488  C  CG2   . THR   B 1  130 ? -25.277 51.733  6.453    1.00 50.03  ? 130 THR   C CG2   1 
ATOM   4489  N  N     . GLY   B 1  131 ? -25.105 48.110  3.474    1.00 39.43  ? 131 GLY   C N     1 
ATOM   4490  C  CA    . GLY   B 1  131 ? -25.069 47.494  2.166    1.00 38.56  ? 131 GLY   C CA    1 
ATOM   4491  C  C     . GLY   B 1  131 ? -24.575 46.068  2.215    1.00 44.92  ? 131 GLY   C C     1 
ATOM   4492  O  O     . GLY   B 1  131 ? -23.599 45.724  1.534    1.00 43.65  ? 131 GLY   C O     1 
ATOM   4493  N  N     . LEU   B 1  132 ? -25.237 45.234  3.020    1.00 37.02  ? 132 LEU   C N     1 
ATOM   4494  C  CA    . LEU   B 1  132 ? -24.818 43.850  3.184    1.00 36.16  ? 132 LEU   C CA    1 
ATOM   4495  C  C     . LEU   B 1  132 ? -24.567 43.209  1.835    1.00 37.21  ? 132 LEU   C C     1 
ATOM   4496  O  O     . LEU   B 1  132 ? -25.440 43.206  0.967    1.00 40.38  ? 132 LEU   C O     1 
ATOM   4497  C  CB    . LEU   B 1  132 ? -25.873 43.055  3.941    1.00 35.21  ? 132 LEU   C CB    1 
ATOM   4498  C  CG    . LEU   B 1  132 ? -25.390 41.663  4.345    1.00 32.56  ? 132 LEU   C CG    1 
ATOM   4499  C  CD1   . LEU   B 1  132 ? -24.044 41.757  5.075    1.00 28.25  ? 132 LEU   C CD1   1 
ATOM   4500  C  CD2   . LEU   B 1  132 ? -26.437 40.955  5.183    1.00 28.71  ? 132 LEU   C CD2   1 
ATOM   4501  N  N     . GLN   B 1  133 ? -23.364 42.669  1.661    1.00 39.62  ? 133 GLN   C N     1 
ATOM   4502  C  CA    . GLN   B 1  133 ? -22.987 42.010  0.419    1.00 38.41  ? 133 GLN   C CA    1 
ATOM   4503  C  C     . GLN   B 1  133 ? -23.161 40.504  0.479    1.00 39.13  ? 133 GLN   C C     1 
ATOM   4504  O  O     . GLN   B 1  133 ? -23.630 39.916  -0.493   1.00 40.77  ? 133 GLN   C O     1 
ATOM   4505  C  CB    . GLN   B 1  133 ? -21.537 42.344  0.058    1.00 39.50  ? 133 GLN   C CB    1 
ATOM   4506  C  CG    . GLN   B 1  133 ? -21.250 42.209  -1.426   1.00 57.78  ? 133 GLN   C CG    1 
ATOM   4507  C  CD    . GLN   B 1  133 ? -19.883 42.748  -1.812   1.00 57.29  ? 133 GLN   C CD    1 
ATOM   4508  O  OE1   . GLN   B 1  133 ? -19.103 43.168  -0.953   1.00 62.82  ? 133 GLN   C OE1   1 
ATOM   4509  N  NE2   . GLN   B 1  133 ? -19.591 42.748  -3.108   1.00 58.08  ? 133 GLN   C NE2   1 
ATOM   4510  N  N     . GLY   B 1  134 ? -22.801 39.866  1.591    1.00 41.90  ? 134 GLY   C N     1 
ATOM   4511  C  CA    . GLY   B 1  134 ? -22.994 38.435  1.712    1.00 38.86  ? 134 GLY   C CA    1 
ATOM   4512  C  C     . GLY   B 1  134 ? -22.369 37.879  2.977    1.00 35.57  ? 134 GLY   C C     1 
ATOM   4513  O  O     . GLY   B 1  134 ? -21.889 38.621  3.835    1.00 35.96  ? 134 GLY   C O     1 
ATOM   4514  N  N     . PHE   B 1  135 ? -22.366 36.541  3.050    1.00 31.03  ? 135 PHE   C N     1 
ATOM   4515  C  CA    . PHE   B 1  135 ? -21.932 35.764  4.203    1.00 28.83  ? 135 PHE   C CA    1 
ATOM   4516  C  C     . PHE   B 1  135 ? -20.702 34.918  3.879    1.00 35.26  ? 135 PHE   C C     1 
ATOM   4517  O  O     . PHE   B 1  135 ? -20.531 34.466  2.736    1.00 28.98  ? 135 PHE   C O     1 
ATOM   4518  C  CB    . PHE   B 1  135 ? -23.063 34.840  4.659    1.00 28.30  ? 135 PHE   C CB    1 
ATOM   4519  C  CG    . PHE   B 1  135 ? -24.300 35.568  5.049    1.00 29.15  ? 135 PHE   C CG    1 
ATOM   4520  C  CD1   . PHE   B 1  135 ? -24.428 36.101  6.323    1.00 26.27  ? 135 PHE   C CD1   1 
ATOM   4521  C  CD2   . PHE   B 1  135 ? -25.329 35.748  4.138    1.00 33.86  ? 135 PHE   C CD2   1 
ATOM   4522  C  CE1   . PHE   B 1  135 ? -25.561 36.769  6.694    1.00 27.91  ? 135 PHE   C CE1   1 
ATOM   4523  C  CE2   . PHE   B 1  135 ? -26.470 36.432  4.497    1.00 32.34  ? 135 PHE   C CE2   1 
ATOM   4524  C  CZ    . PHE   B 1  135 ? -26.592 36.948  5.770    1.00 31.26  ? 135 PHE   C CZ    1 
ATOM   4525  N  N     . LEU   B 1  136 ? -19.853 34.696  4.898    1.00 27.75  ? 136 LEU   C N     1 
ATOM   4526  C  CA    . LEU   B 1  136 ? -18.787 33.690  4.857    1.00 23.54  ? 136 LEU   C CA    1 
ATOM   4527  C  C     . LEU   B 1  136 ? -19.044 32.669  5.963    1.00 27.83  ? 136 LEU   C C     1 
ATOM   4528  O  O     . LEU   B 1  136 ? -19.077 33.026  7.144    1.00 36.80  ? 136 LEU   C O     1 
ATOM   4529  C  CB    . LEU   B 1  136 ? -17.390 34.308  5.025    1.00 29.24  ? 136 LEU   C CB    1 
ATOM   4530  C  CG    . LEU   B 1  136 ? -16.965 35.540  4.205    1.00 31.50  ? 136 LEU   C CG    1 
ATOM   4531  C  CD1   . LEU   B 1  136 ? -15.442 35.771  4.231    1.00 24.56  ? 136 LEU   C CD1   1 
ATOM   4532  C  CD2   . LEU   B 1  136 ? -17.472 35.441  2.790    1.00 25.10  ? 136 LEU   C CD2   1 
ATOM   4533  N  N     . VAL   B 1  137 ? -19.226 31.408  5.588    1.00 22.27  ? 137 VAL   C N     1 
ATOM   4534  C  CA    . VAL   B 1  137 ? -19.596 30.349  6.511    1.00 23.06  ? 137 VAL   C CA    1 
ATOM   4535  C  C     . VAL   B 1  137 ? -18.429 29.372  6.593    1.00 30.66  ? 137 VAL   C C     1 
ATOM   4536  O  O     . VAL   B 1  137 ? -18.089 28.721  5.600    1.00 28.47  ? 137 VAL   C O     1 
ATOM   4537  C  CB    . VAL   B 1  137 ? -20.883 29.650  6.071    1.00 29.49  ? 137 VAL   C CB    1 
ATOM   4538  C  CG1   . VAL   B 1  137 ? -21.286 28.543  7.084    1.00 23.79  ? 137 VAL   C CG1   1 
ATOM   4539  C  CG2   . VAL   B 1  137 ? -21.983 30.684  5.934    1.00 30.99  ? 137 VAL   C CG2   1 
ATOM   4540  N  N     . PHE   B 1  138 ? -17.813 29.287  7.775    1.00 26.22  ? 138 PHE   C N     1 
ATOM   4541  C  CA    . PHE   B 1  138 ? -16.654 28.446  8.060    1.00 24.44  ? 138 PHE   C CA    1 
ATOM   4542  C  C     . PHE   B 1  138 ? -17.111 27.213  8.832    1.00 29.28  ? 138 PHE   C C     1 
ATOM   4543  O  O     . PHE   B 1  138 ? -17.827 27.326  9.835    1.00 29.25  ? 138 PHE   C O     1 
ATOM   4544  C  CB    . PHE   B 1  138 ? -15.614 29.186  8.904    1.00 18.70  ? 138 PHE   C CB    1 
ATOM   4545  C  CG    . PHE   B 1  138 ? -15.064 30.425  8.274    1.00 24.66  ? 138 PHE   C CG    1 
ATOM   4546  C  CD1   . PHE   B 1  138 ? -15.870 31.537  8.059    1.00 25.89  ? 138 PHE   C CD1   1 
ATOM   4547  C  CD2   . PHE   B 1  138 ? -13.719 30.500  7.939    1.00 23.00  ? 138 PHE   C CD2   1 
ATOM   4548  C  CE1   . PHE   B 1  138 ? -15.351 32.682  7.481    1.00 21.03  ? 138 PHE   C CE1   1 
ATOM   4549  C  CE2   . PHE   B 1  138 ? -13.195 31.643  7.372    1.00 22.58  ? 138 PHE   C CE2   1 
ATOM   4550  C  CZ    . PHE   B 1  138 ? -14.015 32.729  7.142    1.00 23.05  ? 138 PHE   C CZ    1 
ATOM   4551  N  N     . HIS   B 1  139 ? -16.694 26.038  8.389    1.00 24.94  ? 139 HIS   C N     1 
ATOM   4552  C  CA    . HIS   B 1  139 ? -17.248 24.869  9.047    1.00 26.29  ? 139 HIS   C CA    1 
ATOM   4553  C  C     . HIS   B 1  139 ? -16.529 23.649  8.517    1.00 21.63  ? 139 HIS   C C     1 
ATOM   4554  O  O     . HIS   B 1  139 ? -15.927 23.686  7.441    1.00 26.43  ? 139 HIS   C O     1 
ATOM   4555  C  CB    . HIS   B 1  139 ? -18.768 24.757  8.818    1.00 21.86  ? 139 HIS   C CB    1 
ATOM   4556  C  CG    . HIS   B 1  139 ? -19.139 24.474  7.395    1.00 22.94  ? 139 HIS   C CG    1 
ATOM   4557  N  ND1   . HIS   B 1  139 ? -19.355 23.196  6.920    1.00 25.56  ? 139 HIS   C ND1   1 
ATOM   4558  C  CD2   . HIS   B 1  139 ? -19.291 25.301  6.332    1.00 23.33  ? 139 HIS   C CD2   1 
ATOM   4559  C  CE1   . HIS   B 1  139 ? -19.642 23.251  5.632    1.00 23.10  ? 139 HIS   C CE1   1 
ATOM   4560  N  NE2   . HIS   B 1  139 ? -19.608 24.516  5.250    1.00 22.32  ? 139 HIS   C NE2   1 
ATOM   4561  N  N     . SER   B 1  140 ? -16.602 22.575  9.291    1.00 19.22  ? 140 SER   C N     1 
ATOM   4562  C  CA    . SER   B 1  140 ? -16.043 21.289  8.914    1.00 22.68  ? 140 SER   C CA    1 
ATOM   4563  C  C     . SER   B 1  140 ? -17.081 20.498  8.121    1.00 26.41  ? 140 SER   C C     1 
ATOM   4564  O  O     . SER   B 1  140 ? -18.285 20.609  8.378    1.00 26.61  ? 140 SER   C O     1 
ATOM   4565  C  CB    . SER   B 1  140 ? -15.615 20.494  10.157   1.00 22.11  ? 140 SER   C CB    1 
ATOM   4566  O  OG    . SER   B 1  140 ? -16.753 20.037  10.916   1.00 21.17  ? 140 SER   C OG    1 
ATOM   4567  N  N     . PHE   B 1  141 ? -16.606 19.724  7.136    1.00 22.57  ? 141 PHE   C N     1 
ATOM   4568  C  CA    . PHE   B 1  141 ? -17.445 18.703  6.513    1.00 25.77  ? 141 PHE   C CA    1 
ATOM   4569  C  C     . PHE   B 1  141 ? -17.837 17.624  7.507    1.00 31.22  ? 141 PHE   C C     1 
ATOM   4570  O  O     . PHE   B 1  141 ? -18.918 17.040  7.385    1.00 38.04  ? 141 PHE   C O     1 
ATOM   4571  C  CB    . PHE   B 1  141 ? -16.716 18.026  5.340    1.00 23.48  ? 141 PHE   C CB    1 
ATOM   4572  C  CG    . PHE   B 1  141 ? -16.869 18.729  4.004    1.00 32.91  ? 141 PHE   C CG    1 
ATOM   4573  C  CD1   . PHE   B 1  141 ? -17.658 19.875  3.864    1.00 24.80  ? 141 PHE   C CD1   1 
ATOM   4574  C  CD2   . PHE   B 1  141 ? -16.221 18.220  2.865    1.00 34.44  ? 141 PHE   C CD2   1 
ATOM   4575  C  CE1   . PHE   B 1  141 ? -17.775 20.502  2.631    1.00 22.82  ? 141 PHE   C CE1   1 
ATOM   4576  C  CE2   . PHE   B 1  141 ? -16.345 18.851  1.615    1.00 27.43  ? 141 PHE   C CE2   1 
ATOM   4577  C  CZ    . PHE   B 1  141 ? -17.119 19.990  1.500    1.00 20.77  ? 141 PHE   C CZ    1 
ATOM   4578  N  N     . GLY   B 1  142 ? -16.970 17.333  8.489    1.00 29.96  ? 142 GLY   C N     1 
ATOM   4579  C  CA    . GLY   B 1  142 ? -16.993 16.054  9.190    1.00 23.13  ? 142 GLY   C CA    1 
ATOM   4580  C  C     . GLY   B 1  142 ? -17.783 15.985  10.479   1.00 30.44  ? 142 GLY   C C     1 
ATOM   4581  O  O     . GLY   B 1  142 ? -18.358 14.944  10.806   1.00 28.56  ? 142 GLY   C O     1 
ATOM   4582  N  N     . GLY   B 1  143 ? -17.804 17.082  11.236   1.00 37.05  ? 143 GLY   C N     1 
ATOM   4583  C  CA    . GLY   B 1  143 ? -18.540 17.112  12.482   1.00 24.64  ? 143 GLY   C CA    1 
ATOM   4584  C  C     . GLY   B 1  143 ? -20.027 16.997  12.243   1.00 29.77  ? 143 GLY   C C     1 
ATOM   4585  O  O     . GLY   B 1  143 ? -20.520 17.080  11.109   1.00 28.94  ? 143 GLY   C O     1 
ATOM   4586  N  N     . GLY   B 1  144 ? -20.746 16.743  13.344   1.00 26.48  ? 144 GLY   C N     1 
ATOM   4587  C  CA    . GLY   B 1  144 ? -22.195 16.737  13.291   1.00 18.79  ? 144 GLY   C CA    1 
ATOM   4588  C  C     . GLY   B 1  144 ? -22.758 18.128  13.109   1.00 27.07  ? 144 GLY   C C     1 
ATOM   4589  O  O     . GLY   B 1  144 ? -23.775 18.311  12.427   1.00 32.52  ? 144 GLY   C O     1 
ATOM   4590  N  N     . THR   B 1  145 ? -22.088 19.130  13.674   1.00 17.27  ? 145 THR   C N     1 
ATOM   4591  C  CA    . THR   B 1  145 ? -22.548 20.506  13.563   1.00 21.92  ? 145 THR   C CA    1 
ATOM   4592  C  C     . THR   B 1  145 ? -22.067 21.148  12.263   1.00 26.65  ? 145 THR   C C     1 
ATOM   4593  O  O     . THR   B 1  145 ? -22.872 21.713  11.508   1.00 29.46  ? 145 THR   C O     1 
ATOM   4594  C  CB    . THR   B 1  145 ? -22.067 21.308  14.769   1.00 22.27  ? 145 THR   C CB    1 
ATOM   4595  O  OG1   . THR   B 1  145 ? -22.700 20.818  15.954   1.00 26.17  ? 145 THR   C OG1   1 
ATOM   4596  C  CG2   . THR   B 1  145 ? -22.359 22.775  14.584   1.00 29.45  ? 145 THR   C CG2   1 
ATOM   4597  N  N     . GLY   B 1  146 ? -20.757 21.058  11.990   1.00 25.35  ? 146 GLY   C N     1 
ATOM   4598  C  CA    . GLY   B 1  146 ? -20.212 21.588  10.742   1.00 20.05  ? 146 GLY   C CA    1 
ATOM   4599  C  C     . GLY   B 1  146 ? -20.971 21.119  9.525    1.00 25.44  ? 146 GLY   C C     1 
ATOM   4600  O  O     . GLY   B 1  146 ? -21.173 21.880  8.574    1.00 28.07  ? 146 GLY   C O     1 
ATOM   4601  N  N     . SER   B 1  147 ? -21.444 19.873  9.554    1.00 24.36  ? 147 SER   C N     1 
ATOM   4602  C  CA    . SER   B 1  147 ? -22.195 19.328  8.430    1.00 28.19  ? 147 SER   C CA    1 
ATOM   4603  C  C     . SER   B 1  147 ? -23.681 19.700  8.497    1.00 25.30  ? 147 SER   C C     1 
ATOM   4604  O  O     . SER   B 1  147 ? -24.189 20.457  7.661    1.00 29.17  ? 147 SER   C O     1 
ATOM   4605  C  CB    . SER   B 1  147 ? -22.004 17.812  8.384    1.00 30.68  ? 147 SER   C CB    1 
ATOM   4606  O  OG    . SER   B 1  147 ? -22.473 17.197  9.578    1.00 28.94  ? 147 SER   C OG    1 
ATOM   4607  N  N     . GLY   B 1  148 ? -24.398 19.150  9.473    1.00 27.31  ? 148 GLY   C N     1 
ATOM   4608  C  CA    . GLY   B 1  148 ? -25.851 19.266  9.494    1.00 24.78  ? 148 GLY   C CA    1 
ATOM   4609  C  C     . GLY   B 1  148 ? -26.371 20.609  9.957    1.00 27.77  ? 148 GLY   C C     1 
ATOM   4610  O  O     . GLY   B 1  148 ? -27.378 21.092  9.438    1.00 28.52  ? 148 GLY   C O     1 
ATOM   4611  N  N     . PHE   B 1  149 ? -25.686 21.263  10.897   1.00 24.61  ? 149 PHE   C N     1 
ATOM   4612  C  CA    . PHE   B 1  149 ? -26.218 22.550  11.313   1.00 25.95  ? 149 PHE   C CA    1 
ATOM   4613  C  C     . PHE   B 1  149 ? -25.890 23.642  10.304   1.00 27.43  ? 149 PHE   C C     1 
ATOM   4614  O  O     . PHE   B 1  149 ? -26.724 24.523  10.060   1.00 28.09  ? 149 PHE   C O     1 
ATOM   4615  C  CB    . PHE   B 1  149 ? -25.725 22.930  12.716   1.00 26.84  ? 149 PHE   C CB    1 
ATOM   4616  C  CG    . PHE   B 1  149 ? -26.315 24.214  13.210   1.00 31.19  ? 149 PHE   C CG    1 
ATOM   4617  C  CD1   . PHE   B 1  149 ? -27.636 24.257  13.662   1.00 29.62  ? 149 PHE   C CD1   1 
ATOM   4618  C  CD2   . PHE   B 1  149 ? -25.586 25.399  13.159   1.00 26.46  ? 149 PHE   C CD2   1 
ATOM   4619  C  CE1   . PHE   B 1  149 ? -28.215 25.471  14.101   1.00 24.11  ? 149 PHE   C CE1   1 
ATOM   4620  C  CE2   . PHE   B 1  149 ? -26.158 26.603  13.589   1.00 37.85  ? 149 PHE   C CE2   1 
ATOM   4621  C  CZ    . PHE   B 1  149 ? -27.483 26.630  14.065   1.00 31.09  ? 149 PHE   C CZ    1 
ATOM   4622  N  N     . THR   B 1  150 ? -24.681 23.608  9.721    1.00 33.92  ? 150 THR   C N     1 
ATOM   4623  C  CA    . THR   B 1  150 ? -24.332 24.507  8.616    1.00 22.95  ? 150 THR   C CA    1 
ATOM   4624  C  C     . THR   B 1  150 ? -25.356 24.433  7.485    1.00 24.80  ? 150 THR   C C     1 
ATOM   4625  O  O     . THR   B 1  150 ? -25.823 25.464  6.990    1.00 24.87  ? 150 THR   C O     1 
ATOM   4626  C  CB    . THR   B 1  150 ? -22.937 24.170  8.056    1.00 26.67  ? 150 THR   C CB    1 
ATOM   4627  O  OG1   . THR   B 1  150 ? -21.915 24.431  9.024    1.00 22.30  ? 150 THR   C OG1   1 
ATOM   4628  C  CG2   . THR   B 1  150 ? -22.647 24.968  6.783    1.00 22.26  ? 150 THR   C CG2   1 
ATOM   4629  N  N     . SER   B 1  151 ? -25.703 23.219  7.038    1.00 24.76  ? 151 SER   C N     1 
ATOM   4630  C  CA    A SER   B 1  151 ? -26.587 23.111  5.882    0.60 26.45  ? 151 SER   C CA    1 
ATOM   4631  C  CA    B SER   B 1  151 ? -26.590 23.092  5.886    0.40 26.58  ? 151 SER   C CA    1 
ATOM   4632  C  C     . SER   B 1  151 ? -27.980 23.607  6.218    1.00 29.62  ? 151 SER   C C     1 
ATOM   4633  O  O     . SER   B 1  151 ? -28.605 24.309  5.410    1.00 27.85  ? 151 SER   C O     1 
ATOM   4634  C  CB    A SER   B 1  151 ? -26.647 21.672  5.379    0.60 30.73  ? 151 SER   C CB    1 
ATOM   4635  C  CB    B SER   B 1  151 ? -26.653 21.633  5.422    0.40 30.69  ? 151 SER   C CB    1 
ATOM   4636  O  OG    A SER   B 1  151 ? -27.317 20.858  6.321    0.60 34.35  ? 151 SER   C OG    1 
ATOM   4637  O  OG    B SER   B 1  151 ? -25.463 20.922  5.743    0.40 31.74  ? 151 SER   C OG    1 
ATOM   4638  N  N     . LEU   B 1  152 ? -28.483 23.249  7.399    1.00 34.30  ? 152 LEU   C N     1 
ATOM   4639  C  CA    . LEU   B 1  152 ? -29.744 23.803  7.870    1.00 29.04  ? 152 LEU   C CA    1 
ATOM   4640  C  C     . LEU   B 1  152 ? -29.684 25.323  7.865    1.00 27.99  ? 152 LEU   C C     1 
ATOM   4641  O  O     . LEU   B 1  152 ? -30.593 25.987  7.357    1.00 30.86  ? 152 LEU   C O     1 
ATOM   4642  C  CB    . LEU   B 1  152 ? -30.077 23.275  9.277    1.00 31.09  ? 152 LEU   C CB    1 
ATOM   4643  C  CG    . LEU   B 1  152 ? -31.307 23.980  9.880    1.00 37.08  ? 152 LEU   C CG    1 
ATOM   4644  C  CD1   . LEU   B 1  152 ? -32.611 23.475  9.217    1.00 23.79  ? 152 LEU   C CD1   1 
ATOM   4645  C  CD2   . LEU   B 1  152 ? -31.353 23.945  11.424   1.00 29.34  ? 152 LEU   C CD2   1 
ATOM   4646  N  N     . LEU   B 1  153 ? -28.599 25.888  8.414    1.00 27.21  ? 153 LEU   C N     1 
ATOM   4647  C  CA    . LEU   B 1  153 ? -28.438 27.343  8.442    1.00 27.13  ? 153 LEU   C CA    1 
ATOM   4648  C  C     . LEU   B 1  153 ? -28.332 27.937  7.037    1.00 24.83  ? 153 LEU   C C     1 
ATOM   4649  O  O     . LEU   B 1  153 ? -28.781 29.064  6.806    1.00 28.02  ? 153 LEU   C O     1 
ATOM   4650  C  CB    . LEU   B 1  153 ? -27.207 27.719  9.277    1.00 28.94  ? 153 LEU   C CB    1 
ATOM   4651  C  CG    . LEU   B 1  153 ? -26.842 29.207  9.448    1.00 31.02  ? 153 LEU   C CG    1 
ATOM   4652  C  CD1   . LEU   B 1  153 ? -27.831 30.000  10.347   1.00 21.42  ? 153 LEU   C CD1   1 
ATOM   4653  C  CD2   . LEU   B 1  153 ? -25.424 29.340  9.946    1.00 25.22  ? 153 LEU   C CD2   1 
ATOM   4654  N  N     . MET   B 1  154 ? -27.742 27.207  6.093    1.00 24.29  ? 154 MET   C N     1 
ATOM   4655  C  CA    . MET   B 1  154 ? -27.653 27.707  4.725    1.00 30.87  ? 154 MET   C CA    1 
ATOM   4656  C  C     . MET   B 1  154 ? -29.032 27.779  4.090    1.00 32.02  ? 154 MET   C C     1 
ATOM   4657  O  O     . MET   B 1  154 ? -29.399 28.798  3.494    1.00 34.73  ? 154 MET   C O     1 
ATOM   4658  C  CB    . MET   B 1  154 ? -26.718 26.829  3.873    1.00 25.68  ? 154 MET   C CB    1 
ATOM   4659  C  CG    . MET   B 1  154 ? -25.226 26.941  4.227    1.00 28.16  ? 154 MET   C CG    1 
ATOM   4660  S  SD    . MET   B 1  154 ? -24.469 28.534  3.849    1.00 32.34  ? 154 MET   C SD    1 
ATOM   4661  C  CE    . MET   B 1  154 ? -23.825 28.152  2.220    1.00 30.91  ? 154 MET   C CE    1 
ATOM   4662  N  N     . GLU   B 1  155 ? -29.814 26.705  4.202    1.00 33.70  ? 155 GLU   C N     1 
ATOM   4663  C  CA    . GLU   B 1  155 ? -31.181 26.752  3.693    1.00 31.96  ? 155 GLU   C CA    1 
ATOM   4664  C  C     . GLU   B 1  155 ? -31.928 27.957  4.259    1.00 32.00  ? 155 GLU   C C     1 
ATOM   4665  O  O     . GLU   B 1  155 ? -32.619 28.675  3.526    1.00 34.45  ? 155 GLU   C O     1 
ATOM   4666  C  CB    . GLU   B 1  155 ? -31.906 25.450  4.020    1.00 31.87  ? 155 GLU   C CB    1 
ATOM   4667  C  CG    . GLU   B 1  155 ? -31.382 24.268  3.234    1.00 35.21  ? 155 GLU   C CG    1 
ATOM   4668  C  CD    . GLU   B 1  155 ? -31.710 22.930  3.875    1.00 42.60  ? 155 GLU   C CD    1 
ATOM   4669  O  OE1   . GLU   B 1  155 ? -32.011 22.888  5.087    1.00 38.87  ? 155 GLU   C OE1   1 
ATOM   4670  O  OE2   . GLU   B 1  155 ? -31.660 21.907  3.166    1.00 46.84  ? 155 GLU   C OE2   1 
ATOM   4671  N  N     . ARG   B 1  156 ? -31.745 28.236  5.546    1.00 29.16  ? 156 ARG   C N     1 
ATOM   4672  C  CA    . ARG   B 1  156 ? -32.496 29.311  6.185    1.00 28.40  ? 156 ARG   C CA    1 
ATOM   4673  C  C     . ARG   B 1  156 ? -32.009 30.676  5.726    1.00 29.62  ? 156 ARG   C C     1 
ATOM   4674  O  O     . ARG   B 1  156 ? -32.810 31.590  5.522    1.00 32.24  ? 156 ARG   C O     1 
ATOM   4675  C  CB    . ARG   B 1  156 ? -32.403 29.174  7.705    1.00 34.71  ? 156 ARG   C CB    1 
ATOM   4676  C  CG    . ARG   B 1  156 ? -33.003 27.860  8.224    1.00 36.50  ? 156 ARG   C CG    1 
ATOM   4677  C  CD    . ARG   B 1  156 ? -34.512 27.860  8.021    1.00 27.38  ? 156 ARG   C CD    1 
ATOM   4678  N  NE    . ARG   B 1  156 ? -35.089 28.955  8.785    1.00 36.90  ? 156 ARG   C NE    1 
ATOM   4679  C  CZ    . ARG   B 1  156 ? -35.561 28.828  10.016   1.00 34.68  ? 156 ARG   C CZ    1 
ATOM   4680  N  NH1   . ARG   B 1  156 ? -35.675 27.637  10.587   1.00 33.50  ? 156 ARG   C NH1   1 
ATOM   4681  N  NH2   . ARG   B 1  156 ? -35.899 29.923  10.697   1.00 26.99  ? 156 ARG   C NH2   1 
ATOM   4682  N  N     . LEU   B 1  157 ? -30.704 30.839  5.543    1.00 33.72  ? 157 LEU   C N     1 
ATOM   4683  C  CA    . LEU   B 1  157 ? -30.217 32.096  4.982    1.00 31.81  ? 157 LEU   C CA    1 
ATOM   4684  C  C     . LEU   B 1  157 ? -30.758 32.317  3.567    1.00 28.38  ? 157 LEU   C C     1 
ATOM   4685  O  O     . LEU   B 1  157 ? -31.122 33.438  3.206    1.00 30.14  ? 157 LEU   C O     1 
ATOM   4686  C  CB    . LEU   B 1  157 ? -28.693 32.116  5.013    1.00 27.82  ? 157 LEU   C CB    1 
ATOM   4687  C  CG    . LEU   B 1  157 ? -28.170 31.981  6.439    1.00 27.93  ? 157 LEU   C CG    1 
ATOM   4688  C  CD1   . LEU   B 1  157 ? -26.643 32.204  6.531    1.00 27.17  ? 157 LEU   C CD1   1 
ATOM   4689  C  CD2   . LEU   B 1  157 ? -28.899 32.966  7.303    1.00 25.94  ? 157 LEU   C CD2   1 
ATOM   4690  N  N     . SER   B 1  158 ? -30.863 31.255  2.764    1.00 29.69  ? 158 SER   C N     1 
ATOM   4691  C  CA    . SER   B 1  158 ? -31.459 31.411  1.440    1.00 32.48  ? 158 SER   C CA    1 
ATOM   4692  C  C     . SER   B 1  158 ? -32.863 31.981  1.536    1.00 35.01  ? 158 SER   C C     1 
ATOM   4693  O  O     . SER   B 1  158 ? -33.261 32.793  0.694    1.00 34.81  ? 158 SER   C O     1 
ATOM   4694  C  CB    . SER   B 1  158 ? -31.488 30.084  0.697    1.00 27.75  ? 158 SER   C CB    1 
ATOM   4695  O  OG    . SER   B 1  158 ? -30.237 29.813  0.125    1.00 28.18  ? 158 SER   C OG    1 
ATOM   4696  N  N     . VAL   B 1  159 ? -33.625 31.583  2.566    1.00 36.98  ? 159 VAL   C N     1 
ATOM   4697  C  CA    . VAL   B 1  159 ? -34.985 32.090  2.725    1.00 30.99  ? 159 VAL   C CA    1 
ATOM   4698  C  C     . VAL   B 1  159 ? -34.963 33.531  3.222    1.00 33.55  ? 159 VAL   C C     1 
ATOM   4699  O  O     . VAL   B 1  159 ? -35.557 34.421  2.602    1.00 41.92  ? 159 VAL   C O     1 
ATOM   4700  C  CB    . VAL   B 1  159 ? -35.801 31.168  3.648    1.00 33.67  ? 159 VAL   C CB    1 
ATOM   4701  C  CG1   . VAL   B 1  159 ? -37.186 31.754  3.928    1.00 27.20  ? 159 VAL   C CG1   1 
ATOM   4702  C  CG2   . VAL   B 1  159 ? -35.957 29.825  3.006    1.00 31.89  ? 159 VAL   C CG2   1 
ATOM   4703  N  N     . ASP   B 1  160 ? -34.240 33.795  4.316    1.00 34.14  ? 160 ASP   C N     1 
ATOM   4704  C  CA    . ASP   B 1  160 ? -34.219 35.136  4.919    1.00 30.80  ? 160 ASP   C CA    1 
ATOM   4705  C  C     . ASP   B 1  160 ? -33.559 36.187  4.039    1.00 31.25  ? 160 ASP   C C     1 
ATOM   4706  O  O     . ASP   B 1  160 ? -33.872 37.373  4.168    1.00 40.53  ? 160 ASP   C O     1 
ATOM   4707  C  CB    . ASP   B 1  160 ? -33.460 35.130  6.245    1.00 35.21  ? 160 ASP   C CB    1 
ATOM   4708  C  CG    . ASP   B 1  160 ? -34.286 34.611  7.406    1.00 45.21  ? 160 ASP   C CG    1 
ATOM   4709  O  OD1   . ASP   B 1  160 ? -34.833 33.484  7.278    1.00 30.60  ? 160 ASP   C OD1   1 
ATOM   4710  O  OD2   . ASP   B 1  160 ? -34.339 35.333  8.445    1.00 39.48  ? 160 ASP   C OD2   1 
ATOM   4711  N  N     . TYR   B 1  161 ? -32.572 35.803  3.228    1.00 29.35  ? 161 TYR   C N     1 
ATOM   4712  C  CA    . TYR   B 1  161 ? -31.757 36.777  2.517    1.00 29.11  ? 161 TYR   C CA    1 
ATOM   4713  C  C     . TYR   B 1  161 ? -31.728 36.499  1.021    1.00 41.24  ? 161 TYR   C C     1 
ATOM   4714  O  O     . TYR   B 1  161 ? -31.010 37.188  0.286    1.00 46.30  ? 161 TYR   C O     1 
ATOM   4715  C  CB    . TYR   B 1  161 ? -30.327 36.823  3.073    1.00 26.63  ? 161 TYR   C CB    1 
ATOM   4716  C  CG    . TYR   B 1  161 ? -30.264 37.233  4.508    1.00 34.00  ? 161 TYR   C CG    1 
ATOM   4717  C  CD1   . TYR   B 1  161 ? -30.182 38.566  4.856    1.00 29.94  ? 161 TYR   C CD1   1 
ATOM   4718  C  CD2   . TYR   B 1  161 ? -30.311 36.282  5.538    1.00 33.49  ? 161 TYR   C CD2   1 
ATOM   4719  C  CE1   . TYR   B 1  161 ? -30.135 38.953  6.182    1.00 26.81  ? 161 TYR   C CE1   1 
ATOM   4720  C  CE2   . TYR   B 1  161 ? -30.255 36.663  6.861    1.00 21.68  ? 161 TYR   C CE2   1 
ATOM   4721  C  CZ    . TYR   B 1  161 ? -30.168 38.003  7.174    1.00 29.27  ? 161 TYR   C CZ    1 
ATOM   4722  O  OH    . TYR   B 1  161 ? -30.120 38.422  8.494    1.00 40.36  ? 161 TYR   C OH    1 
ATOM   4723  N  N     . GLY   B 1  162 ? -32.506 35.534  0.548    1.00 41.33  ? 162 GLY   C N     1 
ATOM   4724  C  CA    . GLY   B 1  162 ? -32.604 35.353  -0.884   1.00 44.65  ? 162 GLY   C CA    1 
ATOM   4725  C  C     . GLY   B 1  162 ? -31.244 35.100  -1.491   1.00 49.59  ? 162 GLY   C C     1 
ATOM   4726  O  O     . GLY   B 1  162 ? -30.407 34.375  -0.938   1.00 49.20  ? 162 GLY   C O     1 
ATOM   4727  N  N     . LYS   B 1  163 ? -31.004 35.740  -2.633   1.00 55.83  ? 163 LYS   C N     1 
ATOM   4728  C  CA    . LYS   B 1  163 ? -29.796 35.499  -3.406   1.00 51.96  ? 163 LYS   C CA    1 
ATOM   4729  C  C     . LYS   B 1  163 ? -28.544 36.130  -2.795   1.00 47.79  ? 163 LYS   C C     1 
ATOM   4730  O  O     . LYS   B 1  163 ? -27.446 35.840  -3.284   1.00 44.94  ? 163 LYS   C O     1 
ATOM   4731  C  CB    . LYS   B 1  163 ? -30.012 35.994  -4.842   1.00 50.56  ? 163 LYS   C CB    1 
ATOM   4732  C  CG    . LYS   B 1  163 ? -30.905 35.057  -5.646   1.00 59.92  ? 163 LYS   C CG    1 
ATOM   4733  C  CD    . LYS   B 1  163 ? -30.490 33.604  -5.372   1.00 58.40  ? 163 LYS   C CD    1 
ATOM   4734  C  CE    . LYS   B 1  163 ? -31.314 32.605  -6.161   1.00 50.64  ? 163 LYS   C CE    1 
ATOM   4735  N  NZ    . LYS   B 1  163 ? -30.595 31.302  -6.268   1.00 53.84  ? 163 LYS   C NZ    1 
ATOM   4736  N  N     . LYS   B 1  164 ? -28.679 36.975  -1.759   1.00 40.52  ? 164 LYS   C N     1 
ATOM   4737  C  CA    . LYS   B 1  164 ? -27.533 37.506  -1.015   1.00 33.47  ? 164 LYS   C CA    1 
ATOM   4738  C  C     . LYS   B 1  164 ? -26.447 36.440  -0.948   1.00 31.56  ? 164 LYS   C C     1 
ATOM   4739  O  O     . LYS   B 1  164 ? -26.727 35.286  -0.614   1.00 37.22  ? 164 LYS   C O     1 
ATOM   4740  C  CB    . LYS   B 1  164 ? -27.961 37.943  0.390    1.00 36.31  ? 164 LYS   C CB    1 
ATOM   4741  C  CG    . LYS   B 1  164 ? -26.939 38.719  1.190    1.00 36.31  ? 164 LYS   C CG    1 
ATOM   4742  C  CD    . LYS   B 1  164 ? -26.959 40.191  0.807    1.00 45.96  ? 164 LYS   C CD    1 
ATOM   4743  C  CE    . LYS   B 1  164 ? -28.272 40.838  1.208    1.00 38.05  ? 164 LYS   C CE    1 
ATOM   4744  N  NZ    . LYS   B 1  164 ? -28.324 42.266  0.800    1.00 41.52  ? 164 LYS   C NZ    1 
ATOM   4745  N  N     . SER   B 1  165 ? -25.218 36.794  -1.283   1.00 32.88  ? 165 SER   C N     1 
ATOM   4746  C  CA    . SER   B 1  165 ? -24.235 35.779  -1.627   1.00 31.09  ? 165 SER   C CA    1 
ATOM   4747  C  C     . SER   B 1  165 ? -23.670 35.106  -0.378   1.00 31.10  ? 165 SER   C C     1 
ATOM   4748  O  O     . SER   B 1  165 ? -23.490 35.739  0.664    1.00 30.55  ? 165 SER   C O     1 
ATOM   4749  C  CB    . SER   B 1  165 ? -23.113 36.392  -2.468   1.00 36.22  ? 165 SER   C CB    1 
ATOM   4750  O  OG    . SER   B 1  165 ? -21.900 36.454  -1.745   1.00 42.81  ? 165 SER   C OG    1 
ATOM   4751  N  N     . LYS   B 1  166 ? -23.413 33.804  -0.488   1.00 28.55  ? 166 LYS   C N     1 
ATOM   4752  C  CA    . LYS   B 1  166 ? -22.890 33.001  0.607    1.00 23.73  ? 166 LYS   C CA    1 
ATOM   4753  C  C     . LYS   B 1  166 ? -21.679 32.241  0.093    1.00 29.02  ? 166 LYS   C C     1 
ATOM   4754  O  O     . LYS   B 1  166 ? -21.808 31.415  -0.816   1.00 31.66  ? 166 LYS   C O     1 
ATOM   4755  C  CB    . LYS   B 1  166 ? -23.948 32.037  1.131    1.00 22.41  ? 166 LYS   C CB    1 
ATOM   4756  C  CG    . LYS   B 1  166 ? -25.313 32.677  1.280    1.00 30.74  ? 166 LYS   C CG    1 
ATOM   4757  C  CD    . LYS   B 1  166 ? -26.174 31.943  2.314    1.00 34.60  ? 166 LYS   C CD    1 
ATOM   4758  C  CE    . LYS   B 1  166 ? -26.945 30.774  1.687    1.00 32.83  ? 166 LYS   C CE    1 
ATOM   4759  N  NZ    . LYS   B 1  166 ? -27.928 31.259  0.668    1.00 36.76  ? 166 LYS   C NZ    1 
ATOM   4760  N  N     . LEU   B 1  167 ? -20.509 32.543  0.654    1.00 24.00  ? 167 LEU   C N     1 
ATOM   4761  C  CA    . LEU   B 1  167 ? -19.258 31.860  0.359    1.00 21.95  ? 167 LEU   C CA    1 
ATOM   4762  C  C     . LEU   B 1  167 ? -18.887 30.971  1.541    1.00 29.08  ? 167 LEU   C C     1 
ATOM   4763  O  O     . LEU   B 1  167 ? -19.114 31.343  2.692    1.00 28.38  ? 167 LEU   C O     1 
ATOM   4764  C  CB    . LEU   B 1  167 ? -18.142 32.874  0.076    1.00 19.39  ? 167 LEU   C CB    1 
ATOM   4765  C  CG    . LEU   B 1  167 ? -18.232 33.321  -1.395   1.00 26.61  ? 167 LEU   C CG    1 
ATOM   4766  C  CD1   . LEU   B 1  167 ? -19.454 34.169  -1.659   1.00 31.63  ? 167 LEU   C CD1   1 
ATOM   4767  C  CD2   . LEU   B 1  167 ? -16.995 33.992  -1.910   1.00 20.92  ? 167 LEU   C CD2   1 
ATOM   4768  N  N     . GLU   B 1  168 ? -18.320 29.799  1.266    1.00 23.00  ? 168 GLU   C N     1 
ATOM   4769  C  CA    . GLU   B 1  168 ? -17.928 28.874  2.313    1.00 22.93  ? 168 GLU   C CA    1 
ATOM   4770  C  C     . GLU   B 1  168 ? -16.430 28.633  2.326    1.00 35.01  ? 168 GLU   C C     1 
ATOM   4771  O  O     . GLU   B 1  168 ? -15.774 28.576  1.269    1.00 28.71  ? 168 GLU   C O     1 
ATOM   4772  C  CB    . GLU   B 1  168 ? -18.554 27.493  2.164    1.00 27.00  ? 168 GLU   C CB    1 
ATOM   4773  C  CG    . GLU   B 1  168 ? -19.974 27.442  1.864    1.00 20.08  ? 168 GLU   C CG    1 
ATOM   4774  C  CD    . GLU   B 1  168 ? -20.384 26.030  1.655    1.00 30.06  ? 168 GLU   C CD    1 
ATOM   4775  O  OE1   . GLU   B 1  168 ? -20.236 25.217  2.604    1.00 23.69  ? 168 GLU   C OE1   1 
ATOM   4776  O  OE2   . GLU   B 1  168 ? -20.810 25.725  0.521    1.00 37.78  ? 168 GLU   C OE2   1 
ATOM   4777  N  N     . PHE   B 1  169 ? -15.917 28.430  3.550    1.00 26.47  ? 169 PHE   C N     1 
ATOM   4778  C  CA    . PHE   B 1  169 ? -14.635 27.785  3.796    1.00 22.02  ? 169 PHE   C CA    1 
ATOM   4779  C  C     . PHE   B 1  169 ? -14.937 26.472  4.509    1.00 28.49  ? 169 PHE   C C     1 
ATOM   4780  O  O     . PHE   B 1  169 ? -15.367 26.472  5.672    1.00 27.47  ? 169 PHE   C O     1 
ATOM   4781  C  CB    . PHE   B 1  169 ? -13.727 28.681  4.625    1.00 21.63  ? 169 PHE   C CB    1 
ATOM   4782  C  CG    . PHE   B 1  169 ? -13.282 29.897  3.904    1.00 27.79  ? 169 PHE   C CG    1 
ATOM   4783  C  CD1   . PHE   B 1  169 ? -14.057 31.051  3.919    1.00 28.58  ? 169 PHE   C CD1   1 
ATOM   4784  C  CD2   . PHE   B 1  169 ? -12.101 29.899  3.194    1.00 26.62  ? 169 PHE   C CD2   1 
ATOM   4785  C  CE1   . PHE   B 1  169 ? -13.654 32.171  3.239    1.00 28.81  ? 169 PHE   C CE1   1 
ATOM   4786  C  CE2   . PHE   B 1  169 ? -11.699 31.031  2.503    1.00 27.88  ? 169 PHE   C CE2   1 
ATOM   4787  C  CZ    . PHE   B 1  169 ? -12.469 32.162  2.534    1.00 26.60  ? 169 PHE   C CZ    1 
ATOM   4788  N  N     . SER   B 1  170 ? -14.721 25.356  3.817    1.00 24.16  ? 170 SER   C N     1 
ATOM   4789  C  CA    . SER   B 1  170 ? -15.140 24.043  4.291    1.00 16.51  ? 170 SER   C CA    1 
ATOM   4790  C  C     . SER   B 1  170 ? -13.936 23.142  4.499    1.00 25.16  ? 170 SER   C C     1 
ATOM   4791  O  O     . SER   B 1  170 ? -13.119 22.954  3.586    1.00 23.31  ? 170 SER   C O     1 
ATOM   4792  C  CB    . SER   B 1  170 ? -16.102 23.377  3.312    1.00 23.31  ? 170 SER   C CB    1 
ATOM   4793  O  OG    . SER   B 1  170 ? -17.230 24.188  3.083    1.00 38.13  ? 170 SER   C OG    1 
ATOM   4794  N  N     . ILE   B 1  171 ? -13.869 22.540  5.682    1.00 24.64  ? 171 ILE   C N     1 
ATOM   4795  C  CA    . ILE   B 1  171 ? -12.757 21.688  6.069    1.00 23.30  ? 171 ILE   C CA    1 
ATOM   4796  C  C     . ILE   B 1  171 ? -13.090 20.249  5.692    1.00 25.19  ? 171 ILE   C C     1 
ATOM   4797  O  O     . ILE   B 1  171 ? -13.997 19.638  6.249    1.00 26.64  ? 171 ILE   C O     1 
ATOM   4798  C  CB    . ILE   B 1  171 ? -12.466 21.827  7.561    1.00 23.92  ? 171 ILE   C CB    1 
ATOM   4799  C  CG1   . ILE   B 1  171 ? -12.219 23.294  7.858    1.00 25.90  ? 171 ILE   C CG1   1 
ATOM   4800  C  CG2   . ILE   B 1  171 ? -11.261 21.036  7.904    1.00 21.05  ? 171 ILE   C CG2   1 
ATOM   4801  C  CD1   . ILE   B 1  171 ? -10.887 23.730  7.353    1.00 28.09  ? 171 ILE   C CD1   1 
ATOM   4802  N  N     . TYR   B 1  172 ? -12.363 19.716  4.741    1.00 27.06  ? 172 TYR   C N     1 
ATOM   4803  C  CA    . TYR   B 1  172 ? -12.459 18.400  4.143    1.00 26.50  ? 172 TYR   C CA    1 
ATOM   4804  C  C     . TYR   B 1  172 ? -11.674 17.410  4.999    1.00 26.41  ? 172 TYR   C C     1 
ATOM   4805  O  O     . TYR   B 1  172 ? -10.580 17.723  5.466    1.00 27.61  ? 172 TYR   C O     1 
ATOM   4806  C  CB    . TYR   B 1  172 ? -11.917 18.464  2.708    1.00 23.96  ? 172 TYR   C CB    1 
ATOM   4807  C  CG    . TYR   B 1  172 ? -11.883 17.211  1.863    1.00 23.06  ? 172 TYR   C CG    1 
ATOM   4808  C  CD1   . TYR   B 1  172 ? -10.851 16.294  1.997    1.00 23.76  ? 172 TYR   C CD1   1 
ATOM   4809  C  CD2   . TYR   B 1  172 ? -12.822 16.992  0.858    1.00 25.79  ? 172 TYR   C CD2   1 
ATOM   4810  C  CE1   . TYR   B 1  172 ? -10.774 15.176  1.191    1.00 24.26  ? 172 TYR   C CE1   1 
ATOM   4811  C  CE2   . TYR   B 1  172 ? -12.749 15.849  0.034    1.00 26.51  ? 172 TYR   C CE2   1 
ATOM   4812  C  CZ    . TYR   B 1  172 ? -11.713 14.947  0.223    1.00 26.86  ? 172 TYR   C CZ    1 
ATOM   4813  O  OH    . TYR   B 1  172 ? -11.587 13.810  -0.542   1.00 26.29  ? 172 TYR   C OH    1 
ATOM   4814  N  N     . PRO   B 1  173 ? -12.222 16.237  5.282    1.00 33.08  ? 173 PRO   C N     1 
ATOM   4815  C  CA    . PRO   B 1  173 ? -11.626 15.378  6.319    1.00 25.85  ? 173 PRO   C CA    1 
ATOM   4816  C  C     . PRO   B 1  173 ? -10.426 14.585  5.829    1.00 28.11  ? 173 PRO   C C     1 
ATOM   4817  O  O     . PRO   B 1  173 ? -10.371 14.139  4.684    1.00 41.07  ? 173 PRO   C O     1 
ATOM   4818  C  CB    . PRO   B 1  173 ? -12.778 14.452  6.718    1.00 21.27  ? 173 PRO   C CB    1 
ATOM   4819  C  CG    . PRO   B 1  173 ? -13.747 14.510  5.572    1.00 28.78  ? 173 PRO   C CG    1 
ATOM   4820  C  CD    . PRO   B 1  173 ? -13.575 15.822  4.882    1.00 30.94  ? 173 PRO   C CD    1 
ATOM   4821  N  N     . ALA   B 1  174 ? -9.467  14.430  6.741    1.00 35.28  ? 174 ALA   C N     1 
ATOM   4822  C  CA    . ALA   B 1  174 ? -8.199  13.718  6.607    1.00 33.73  ? 174 ALA   C CA    1 
ATOM   4823  C  C     . ALA   B 1  174 ? -8.055  12.721  7.752    1.00 35.27  ? 174 ALA   C C     1 
ATOM   4824  O  O     . ALA   B 1  174 ? -8.300  13.075  8.921    1.00 39.13  ? 174 ALA   C O     1 
ATOM   4825  C  CB    . ALA   B 1  174 ? -7.023  14.689  6.636    1.00 25.47  ? 174 ALA   C CB    1 
ATOM   4826  N  N     . PRO   B 1  175 ? -7.628  11.489  7.482    1.00 41.54  ? 175 PRO   C N     1 
ATOM   4827  C  CA    . PRO   B 1  175 ? -7.568  10.476  8.550    1.00 37.11  ? 175 PRO   C CA    1 
ATOM   4828  C  C     . PRO   B 1  175 ? -6.519  10.762  9.615    1.00 36.73  ? 175 PRO   C C     1 
ATOM   4829  O  O     . PRO   B 1  175 ? -6.558  10.125  10.674   1.00 35.90  ? 175 PRO   C O     1 
ATOM   4830  C  CB    . PRO   B 1  175 ? -7.247  9.199   7.786    1.00 28.48  ? 175 PRO   C CB    1 
ATOM   4831  C  CG    . PRO   B 1  175 ? -6.379  9.697   6.651    1.00 39.17  ? 175 PRO   C CG    1 
ATOM   4832  C  CD    . PRO   B 1  175 ? -6.952  11.039  6.254    1.00 39.38  ? 175 PRO   C CD    1 
ATOM   4833  N  N     . GLN   B 1  176 ? -5.612  11.720  9.383    1.00 46.04  ? 176 GLN   C N     1 
ATOM   4834  C  CA    . GLN   B 1  176 ? -4.571  12.066  10.349   1.00 38.16  ? 176 GLN   C CA    1 
ATOM   4835  C  C     . GLN   B 1  176 ? -5.098  12.857  11.542   1.00 40.12  ? 176 GLN   C C     1 
ATOM   4836  O  O     . GLN   B 1  176 ? -4.410  12.924  12.571   1.00 43.77  ? 176 GLN   C O     1 
ATOM   4837  C  CB    . GLN   B 1  176 ? -3.455  12.875  9.674    1.00 30.27  ? 176 GLN   C CB    1 
ATOM   4838  C  CG    . GLN   B 1  176 ? -2.702  12.154  8.576    1.00 38.38  ? 176 GLN   C CG    1 
ATOM   4839  C  CD    . GLN   B 1  176 ? -3.310  12.324  7.189    1.00 40.18  ? 176 GLN   C CD    1 
ATOM   4840  O  OE1   . GLN   B 1  176 ? -4.494  12.643  7.030    1.00 36.82  ? 176 GLN   C OE1   1 
ATOM   4841  N  NE2   . GLN   B 1  176 ? -2.492  12.099  6.170    1.00 45.43  ? 176 GLN   C NE2   1 
ATOM   4842  N  N     . VAL   B 1  177 ? -6.271  13.488  11.431   1.00 40.35  ? 177 VAL   C N     1 
ATOM   4843  C  CA    . VAL   B 1  177 ? -6.795  14.279  12.546   1.00 36.97  ? 177 VAL   C CA    1 
ATOM   4844  C  C     . VAL   B 1  177 ? -8.302  14.104  12.670   1.00 30.68  ? 177 VAL   C C     1 
ATOM   4845  O  O     . VAL   B 1  177 ? -8.979  14.924  13.289   1.00 44.22  ? 177 VAL   C O     1 
ATOM   4846  C  CB    . VAL   B 1  177 ? -6.423  15.773  12.408   1.00 35.96  ? 177 VAL   C CB    1 
ATOM   4847  C  CG1   . VAL   B 1  177 ? -4.920  15.943  12.287   1.00 45.32  ? 177 VAL   C CG1   1 
ATOM   4848  C  CG2   . VAL   B 1  177 ? -7.113  16.412  11.207   1.00 41.18  ? 177 VAL   C CG2   1 
ATOM   4849  N  N     . SER   B 1  178 ? -8.842  13.036  12.113   1.00 37.97  ? 178 SER   C N     1 
ATOM   4850  C  CA    . SER   B 1  178 ? -10.288 12.874  12.101   1.00 45.20  ? 178 SER   C CA    1 
ATOM   4851  C  C     . SER   B 1  178 ? -10.778 12.100  13.324   1.00 41.23  ? 178 SER   C C     1 
ATOM   4852  O  O     . SER   B 1  178 ? -10.082 11.241  13.879   1.00 38.69  ? 178 SER   C O     1 
ATOM   4853  C  CB    . SER   B 1  178 ? -10.739 12.160  10.831   1.00 38.72  ? 178 SER   C CB    1 
ATOM   4854  O  OG    . SER   B 1  178 ? -10.566 10.774  11.025   1.00 48.41  ? 178 SER   C OG    1 
ATOM   4855  N  N     . THR   B 1  179 ? -12.015 12.391  13.715   1.00 42.41  ? 179 THR   C N     1 
ATOM   4856  C  CA    . THR   B 1  179 ? -12.568 11.900  14.965   1.00 40.12  ? 179 THR   C CA    1 
ATOM   4857  C  C     . THR   B 1  179 ? -13.846 11.098  14.795   1.00 43.43  ? 179 THR   C C     1 
ATOM   4858  O  O     . THR   B 1  179 ? -14.454 10.720  15.800   1.00 52.04  ? 179 THR   C O     1 
ATOM   4859  C  CB    . THR   B 1  179 ? -12.837 13.067  15.926   1.00 39.67  ? 179 THR   C CB    1 
ATOM   4860  O  OG1   . THR   B 1  179 ? -13.439 14.172  15.221   1.00 41.54  ? 179 THR   C OG1   1 
ATOM   4861  C  CG2   . THR   B 1  179 ? -11.540 13.516  16.573   1.00 42.64  ? 179 THR   C CG2   1 
ATOM   4862  N  N     . ALA   B 1  180 ? -14.283 10.832  13.570   1.00 41.50  ? 180 ALA   C N     1 
ATOM   4863  C  CA    . ALA   B 1  180 ? -15.486 10.040  13.392   1.00 34.00  ? 180 ALA   C CA    1 
ATOM   4864  C  C     . ALA   B 1  180 ? -15.340 9.238   12.118   1.00 37.96  ? 180 ALA   C C     1 
ATOM   4865  O  O     . ALA   B 1  180 ? -14.900 9.766   11.093   1.00 32.08  ? 180 ALA   C O     1 
ATOM   4866  C  CB    . ALA   B 1  180 ? -16.754 10.896  13.333   1.00 24.14  ? 180 ALA   C CB    1 
ATOM   4867  N  N     . VAL   B 1  181 ? -15.703 7.955   12.210   1.00 36.25  ? 181 VAL   C N     1 
ATOM   4868  C  CA    . VAL   B 1  181 ? -15.681 7.066   11.064   1.00 28.99  ? 181 VAL   C CA    1 
ATOM   4869  C  C     . VAL   B 1  181 ? -16.660 7.520   10.001   1.00 31.44  ? 181 VAL   C C     1 
ATOM   4870  O  O     . VAL   B 1  181 ? -16.466 7.240   8.807    1.00 35.27  ? 181 VAL   C O     1 
ATOM   4871  C  CB    . VAL   B 1  181 ? -15.997 5.634   11.509   1.00 32.34  ? 181 VAL   C CB    1 
ATOM   4872  C  CG1   . VAL   B 1  181 ? -15.902 4.706   10.306   1.00 31.33  ? 181 VAL   C CG1   1 
ATOM   4873  C  CG2   . VAL   B 1  181 ? -15.070 5.215   12.631   1.00 34.20  ? 181 VAL   C CG2   1 
ATOM   4874  N  N     . VAL   B 1  182 ? -17.739 8.198   10.417   1.00 30.51  ? 182 VAL   C N     1 
ATOM   4875  C  CA    . VAL   B 1  182 ? -18.841 8.561   9.529    1.00 34.21  ? 182 VAL   C CA    1 
ATOM   4876  C  C     . VAL   B 1  182 ? -18.604 9.874   8.777    1.00 36.69  ? 182 VAL   C C     1 
ATOM   4877  O  O     . VAL   B 1  182 ? -19.453 10.266  7.961    1.00 37.02  ? 182 VAL   C O     1 
ATOM   4878  C  CB    . VAL   B 1  182 ? -20.185 8.668   10.297   1.00 34.84  ? 182 VAL   C CB    1 
ATOM   4879  C  CG1   . VAL   B 1  182 ? -20.725 7.294   10.638   1.00 28.26  ? 182 VAL   C CG1   1 
ATOM   4880  C  CG2   . VAL   B 1  182 ? -20.045 9.545   11.553   1.00 26.10  ? 182 VAL   C CG2   1 
ATOM   4881  N  N     . GLU   B 1  183 ? -17.485 10.576  9.035    1.00 37.79  ? 183 GLU   C N     1 
ATOM   4882  C  CA    . GLU   B 1  183 ? -17.132 11.819  8.356    1.00 32.13  ? 183 GLU   C CA    1 
ATOM   4883  C  C     . GLU   B 1  183 ? -17.519 11.729  6.863    1.00 32.76  ? 183 GLU   C C     1 
ATOM   4884  O  O     . GLU   B 1  183 ? -18.129 12.671  6.336    1.00 32.12  ? 183 GLU   C O     1 
ATOM   4885  C  CB    . GLU   B 1  183 ? -15.634 12.145  8.617    1.00 32.64  ? 183 GLU   C CB    1 
ATOM   4886  C  CG    . GLU   B 1  183 ? -15.390 13.579  9.248    1.00 41.14  ? 183 GLU   C CG    1 
ATOM   4887  C  CD    . GLU   B 1  183 ? -14.226 13.736  10.290   1.00 44.52  ? 183 GLU   C CD    1 
ATOM   4888  O  OE1   . GLU   B 1  183 ? -14.054 12.855  11.167   1.00 52.17  ? 183 GLU   C OE1   1 
ATOM   4889  O  OE2   . GLU   B 1  183 ? -13.507 14.786  10.272   1.00 35.59  ? 183 GLU   C OE2   1 
ATOM   4890  N  N     . PRO   B 1  184 ? -17.278 10.609  6.165    1.00 29.84  ? 184 PRO   C N     1 
ATOM   4891  C  CA    . PRO   B 1  184 ? -17.760 10.498  4.762    1.00 31.28  ? 184 PRO   C CA    1 
ATOM   4892  C  C     . PRO   B 1  184 ? -19.277 10.605  4.564    1.00 29.19  ? 184 PRO   C C     1 
ATOM   4893  O  O     . PRO   B 1  184 ? -19.706 11.092  3.516    1.00 34.62  ? 184 PRO   C O     1 
ATOM   4894  C  CB    . PRO   B 1  184 ? -17.257 9.115   4.324    1.00 25.74  ? 184 PRO   C CB    1 
ATOM   4895  C  CG    . PRO   B 1  184 ? -16.087 8.876   5.155    1.00 25.92  ? 184 PRO   C CG    1 
ATOM   4896  C  CD    . PRO   B 1  184 ? -16.397 9.489   6.515    1.00 23.69  ? 184 PRO   C CD    1 
ATOM   4897  N  N     . TYR   B 1  185 ? -20.106 10.130  5.492    1.00 27.21  ? 185 TYR   C N     1 
ATOM   4898  C  CA    . TYR   B 1  185 ? -21.544 10.352  5.365    1.00 29.88  ? 185 TYR   C CA    1 
ATOM   4899  C  C     . TYR   B 1  185 ? -21.887 11.821  5.578    1.00 29.55  ? 185 TYR   C C     1 
ATOM   4900  O  O     . TYR   B 1  185 ? -22.684 12.406  4.830    1.00 26.55  ? 185 TYR   C O     1 
ATOM   4901  C  CB    . TYR   B 1  185 ? -22.322 9.483   6.364    1.00 30.43  ? 185 TYR   C CB    1 
ATOM   4902  C  CG    . TYR   B 1  185 ? -22.388 8.004   6.054    1.00 39.75  ? 185 TYR   C CG    1 
ATOM   4903  C  CD1   . TYR   B 1  185 ? -22.105 7.514   4.774    1.00 34.80  ? 185 TYR   C CD1   1 
ATOM   4904  C  CD2   . TYR   B 1  185 ? -22.746 7.088   7.043    1.00 38.65  ? 185 TYR   C CD2   1 
ATOM   4905  C  CE1   . TYR   B 1  185 ? -22.180 6.149   4.497    1.00 37.31  ? 185 TYR   C CE1   1 
ATOM   4906  C  CE2   . TYR   B 1  185 ? -22.823 5.731   6.778    1.00 30.87  ? 185 TYR   C CE2   1 
ATOM   4907  C  CZ    . TYR   B 1  185 ? -22.540 5.264   5.506    1.00 38.99  ? 185 TYR   C CZ    1 
ATOM   4908  O  OH    . TYR   B 1  185 ? -22.620 3.914   5.237    1.00 35.91  ? 185 TYR   C OH    1 
ATOM   4909  N  N     . ASN   B 1  186 ? -21.322 12.434  6.616    1.00 30.61  ? 186 ASN   C N     1 
ATOM   4910  C  CA    . ASN   B 1  186 ? -21.634 13.840  6.858    1.00 33.89  ? 186 ASN   C CA    1 
ATOM   4911  C  C     . ASN   B 1  186 ? -21.172 14.706  5.691    1.00 30.55  ? 186 ASN   C C     1 
ATOM   4912  O  O     . ASN   B 1  186 ? -21.901 15.593  5.240    1.00 31.50  ? 186 ASN   C O     1 
ATOM   4913  C  CB    . ASN   B 1  186 ? -21.009 14.299  8.176    1.00 33.37  ? 186 ASN   C CB    1 
ATOM   4914  C  CG    . ASN   B 1  186 ? -21.496 13.474  9.369    1.00 33.60  ? 186 ASN   C CG    1 
ATOM   4915  O  OD1   . ASN   B 1  186 ? -22.596 12.906  9.348    1.00 29.27  ? 186 ASN   C OD1   1 
ATOM   4916  N  ND2   . ASN   B 1  186 ? -20.671 13.402  10.412   1.00 28.49  ? 186 ASN   C ND2   1 
ATOM   4917  N  N     . SER   B 1  187 ? -19.979 14.426  5.160    1.00 34.95  ? 187 SER   C N     1 
ATOM   4918  C  CA    . SER   B 1  187 ? -19.434 15.210  4.055    1.00 27.76  ? 187 SER   C CA    1 
ATOM   4919  C  C     . SER   B 1  187 ? -20.383 15.252  2.863    1.00 28.42  ? 187 SER   C C     1 
ATOM   4920  O  O     . SER   B 1  187 ? -20.631 16.325  2.307    1.00 23.95  ? 187 SER   C O     1 
ATOM   4921  C  CB    . SER   B 1  187 ? -18.092 14.638  3.627    1.00 23.54  ? 187 SER   C CB    1 
ATOM   4922  O  OG    . SER   B 1  187 ? -17.079 15.016  4.513    1.00 27.36  ? 187 SER   C OG    1 
ATOM   4923  N  N     . ILE   B 1  188 ? -20.885 14.085  2.423    1.00 29.03  ? 188 ILE   C N     1 
ATOM   4924  C  CA    . ILE   B 1  188 ? -21.704 14.043  1.215    1.00 26.26  ? 188 ILE   C CA    1 
ATOM   4925  C  C     . ILE   B 1  188 ? -23.100 14.576  1.492    1.00 30.10  ? 188 ILE   C C     1 
ATOM   4926  O  O     . ILE   B 1  188 ? -23.686 15.274  0.656    1.00 28.98  ? 188 ILE   C O     1 
ATOM   4927  C  CB    . ILE   B 1  188 ? -21.744 12.626  0.612    1.00 34.05  ? 188 ILE   C CB    1 
ATOM   4928  C  CG1   . ILE   B 1  188 ? -20.616 12.437  -0.415   1.00 28.77  ? 188 ILE   C CG1   1 
ATOM   4929  C  CG2   . ILE   B 1  188 ? -23.087 12.359  -0.070   1.00 26.57  ? 188 ILE   C CG2   1 
ATOM   4930  C  CD1   . ILE   B 1  188 ? -19.407 11.794  0.157    1.00 30.98  ? 188 ILE   C CD1   1 
ATOM   4931  N  N     . LEU   B 1  189 ? -23.656 14.280  2.667    1.00 27.36  ? 189 LEU   C N     1 
ATOM   4932  C  CA    . LEU   B 1  189 ? -24.956 14.847  3.000    1.00 27.68  ? 189 LEU   C CA    1 
ATOM   4933  C  C     . LEU   B 1  189 ? -24.916 16.376  2.951    1.00 28.14  ? 189 LEU   C C     1 
ATOM   4934  O  O     . LEU   B 1  189 ? -25.738 17.004  2.279    1.00 32.92  ? 189 LEU   C O     1 
ATOM   4935  C  CB    . LEU   B 1  189 ? -25.423 14.349  4.368    1.00 24.76  ? 189 LEU   C CB    1 
ATOM   4936  C  CG    . LEU   B 1  189 ? -25.919 12.909  4.490    1.00 22.44  ? 189 LEU   C CG    1 
ATOM   4937  C  CD1   . LEU   B 1  189 ? -26.077 12.565  5.955    1.00 28.05  ? 189 LEU   C CD1   1 
ATOM   4938  C  CD2   . LEU   B 1  189 ? -27.215 12.674  3.770    1.00 18.72  ? 189 LEU   C CD2   1 
ATOM   4939  N  N     . THR   B 1  190 ? -23.958 16.996  3.639    1.00 25.94  ? 190 THR   C N     1 
ATOM   4940  C  CA    . THR   B 1  190 ? -23.925 18.463  3.693    1.00 33.44  ? 190 THR   C CA    1 
ATOM   4941  C  C     . THR   B 1  190 ? -23.630 19.066  2.330    1.00 26.04  ? 190 THR   C C     1 
ATOM   4942  O  O     . THR   B 1  190 ? -24.188 20.108  1.968    1.00 32.02  ? 190 THR   C O     1 
ATOM   4943  C  CB    . THR   B 1  190 ? -22.871 18.948  4.695    1.00 41.70  ? 190 THR   C CB    1 
ATOM   4944  O  OG1   . THR   B 1  190 ? -23.054 20.353  4.938    1.00 33.12  ? 190 THR   C OG1   1 
ATOM   4945  C  CG2   . THR   B 1  190 ? -21.451 18.710  4.134    1.00 25.61  ? 190 THR   C CG2   1 
ATOM   4946  N  N     . THR   B 1  191 ? -22.745 18.426  1.570    1.00 32.20  ? 191 THR   C N     1 
ATOM   4947  C  CA    . THR   B 1  191 ? -22.411 18.892  0.233    1.00 29.17  ? 191 THR   C CA    1 
ATOM   4948  C  C     . THR   B 1  191 ? -23.626 18.854  -0.677   1.00 25.71  ? 191 THR   C C     1 
ATOM   4949  O  O     . THR   B 1  191 ? -23.906 19.823  -1.386   1.00 35.11  ? 191 THR   C O     1 
ATOM   4950  C  CB    . THR   B 1  191 ? -21.265 18.049  -0.329   1.00 27.55  ? 191 THR   C CB    1 
ATOM   4951  O  OG1   . THR   B 1  191 ? -20.040 18.428  0.329    1.00 27.68  ? 191 THR   C OG1   1 
ATOM   4952  C  CG2   . THR   B 1  191 ? -21.138 18.254  -1.832   1.00 19.54  ? 191 THR   C CG2   1 
ATOM   4953  N  N     . HIS   B 1  192 ? -24.365 17.741  -0.664   1.00 28.22  ? 192 HIS   C N     1 
ATOM   4954  C  CA    . HIS   B 1  192 ? -25.641 17.676  -1.377   1.00 30.87  ? 192 HIS   C CA    1 
ATOM   4955  C  C     . HIS   B 1  192 ? -26.580 18.780  -0.922   1.00 34.46  ? 192 HIS   C C     1 
ATOM   4956  O  O     . HIS   B 1  192 ? -27.102 19.555  -1.732   1.00 34.75  ? 192 HIS   C O     1 
ATOM   4957  C  CB    . HIS   B 1  192 ? -26.311 16.328  -1.147   1.00 27.42  ? 192 HIS   C CB    1 
ATOM   4958  C  CG    . HIS   B 1  192 ? -27.749 16.294  -1.560   1.00 33.01  ? 192 HIS   C CG    1 
ATOM   4959  N  ND1   . HIS   B 1  192 ? -28.202 16.869  -2.731   1.00 37.39  ? 192 HIS   C ND1   1 
ATOM   4960  C  CD2   . HIS   B 1  192 ? -28.833 15.722  -0.979   1.00 29.42  ? 192 HIS   C CD2   1 
ATOM   4961  C  CE1   . HIS   B 1  192 ? -29.504 16.661  -2.844   1.00 33.40  ? 192 HIS   C CE1   1 
ATOM   4962  N  NE2   . HIS   B 1  192 ? -29.909 15.959  -1.798   1.00 27.41  ? 192 HIS   C NE2   1 
ATOM   4963  N  N     . THR   B 1  193 ? -26.805 18.866  0.383    1.00 33.19  ? 193 THR   C N     1 
ATOM   4964  C  CA    . THR   B 1  193 ? -27.847 19.751  0.875    1.00 31.86  ? 193 THR   C CA    1 
ATOM   4965  C  C     . THR   B 1  193 ? -27.491 21.215  0.717    1.00 31.04  ? 193 THR   C C     1 
ATOM   4966  O  O     . THR   B 1  193 ? -28.399 22.045  0.660    1.00 34.87  ? 193 THR   C O     1 
ATOM   4967  C  CB    . THR   B 1  193 ? -28.164 19.431  2.331    1.00 25.66  ? 193 THR   C CB    1 
ATOM   4968  O  OG1   . THR   B 1  193 ? -28.844 18.168  2.390    1.00 31.39  ? 193 THR   C OG1   1 
ATOM   4969  C  CG2   . THR   B 1  193 ? -29.058 20.495  2.913    1.00 37.58  ? 193 THR   C CG2   1 
ATOM   4970  N  N     . THR   B 1  194 ? -26.207 21.549  0.596    1.00 27.06  ? 194 THR   C N     1 
ATOM   4971  C  CA    A THR   B 1  194 ? -25.767 22.931  0.494    0.78 27.84  ? 194 THR   C CA    1 
ATOM   4972  C  CA    B THR   B 1  194 ? -25.813 22.947  0.485    0.22 27.96  ? 194 THR   C CA    1 
ATOM   4973  C  C     . THR   B 1  194 ? -25.487 23.374  -0.940   1.00 24.67  ? 194 THR   C C     1 
ATOM   4974  O  O     . THR   B 1  194 ? -25.270 24.565  -1.178   1.00 28.68  ? 194 THR   C O     1 
ATOM   4975  C  CB    A THR   B 1  194 ? -24.517 23.126  1.365    0.78 25.04  ? 194 THR   C CB    1 
ATOM   4976  C  CB    B THR   B 1  194 ? -24.606 23.239  1.386    0.22 25.24  ? 194 THR   C CB    1 
ATOM   4977  O  OG1   A THR   B 1  194 ? -24.867 22.880  2.729    0.78 27.53  ? 194 THR   C OG1   1 
ATOM   4978  O  OG1   B THR   B 1  194 ? -23.482 22.468  0.949    0.22 26.04  ? 194 THR   C OG1   1 
ATOM   4979  C  CG2   A THR   B 1  194 ? -23.978 24.525  1.253    0.78 22.57  ? 194 THR   C CG2   1 
ATOM   4980  C  CG2   B THR   B 1  194 ? -24.926 22.891  2.830    0.22 27.65  ? 194 THR   C CG2   1 
ATOM   4981  N  N     . LEU   B 1  195 ? -25.481 22.452  -1.897   1.00 28.42  ? 195 LEU   C N     1 
ATOM   4982  C  CA    . LEU   B 1  195 ? -24.985 22.786  -3.228   1.00 27.90  ? 195 LEU   C CA    1 
ATOM   4983  C  C     . LEU   B 1  195 ? -25.740 23.961  -3.838   1.00 34.70  ? 195 LEU   C C     1 
ATOM   4984  O  O     . LEU   B 1  195 ? -25.121 24.871  -4.399   1.00 34.42  ? 195 LEU   C O     1 
ATOM   4985  C  CB    . LEU   B 1  195 ? -25.066 21.560  -4.126   1.00 27.70  ? 195 LEU   C CB    1 
ATOM   4986  C  CG    . LEU   B 1  195 ? -24.141 21.516  -5.324   1.00 19.56  ? 195 LEU   C CG    1 
ATOM   4987  C  CD1   . LEU   B 1  195 ? -22.825 22.199  -4.988   1.00 19.70  ? 195 LEU   C CD1   1 
ATOM   4988  C  CD2   . LEU   B 1  195 ? -23.923 20.052  -5.619   1.00 26.79  ? 195 LEU   C CD2   1 
ATOM   4989  N  N     . GLU   B 1  196 ? -27.073 23.981  -3.719   1.00 32.56  ? 196 GLU   C N     1 
ATOM   4990  C  CA    . GLU   B 1  196 ? -27.828 25.047  -4.374   1.00 35.28  ? 196 GLU   C CA    1 
ATOM   4991  C  C     . GLU   B 1  196 ? -27.922 26.325  -3.549   1.00 32.18  ? 196 GLU   C C     1 
ATOM   4992  O  O     . GLU   B 1  196 ? -28.486 27.306  -4.033   1.00 38.18  ? 196 GLU   C O     1 
ATOM   4993  C  CB    . GLU   B 1  196 ? -29.240 24.554  -4.765   1.00 29.80  ? 196 GLU   C CB    1 
ATOM   4994  C  CG    . GLU   B 1  196 ? -30.065 23.954  -3.643   1.00 50.05  ? 196 GLU   C CG    1 
ATOM   4995  C  CD    . GLU   B 1  196 ? -31.491 23.605  -4.080   1.00 61.71  ? 196 GLU   C CD    1 
ATOM   4996  O  OE1   . GLU   B 1  196 ? -31.721 23.380  -5.295   1.00 56.74  ? 196 GLU   C OE1   1 
ATOM   4997  O  OE2   . GLU   B 1  196 ? -32.383 23.562  -3.202   1.00 69.21  ? 196 GLU   C OE2   1 
ATOM   4998  N  N     . HIS   B 1  197 ? -27.361 26.362  -2.347   1.00 25.81  ? 197 HIS   C N     1 
ATOM   4999  C  CA    . HIS   B 1  197 ? -27.443 27.533  -1.486   1.00 27.38  ? 197 HIS   C CA    1 
ATOM   5000  C  C     . HIS   B 1  197 ? -26.118 28.268  -1.343   1.00 32.78  ? 197 HIS   C C     1 
ATOM   5001  O  O     . HIS   B 1  197 ? -26.045 29.266  -0.621   1.00 32.35  ? 197 HIS   C O     1 
ATOM   5002  C  CB    . HIS   B 1  197 ? -27.957 27.123  -0.099   1.00 24.59  ? 197 HIS   C CB    1 
ATOM   5003  C  CG    . HIS   B 1  197 ? -29.333 26.544  -0.127   1.00 31.95  ? 197 HIS   C CG    1 
ATOM   5004  N  ND1   . HIS   B 1  197 ? -30.464 27.322  -0.249   1.00 29.50  ? 197 HIS   C ND1   1 
ATOM   5005  C  CD2   . HIS   B 1  197 ? -29.761 25.257  -0.098   1.00 34.89  ? 197 HIS   C CD2   1 
ATOM   5006  C  CE1   . HIS   B 1  197 ? -31.530 26.541  -0.276   1.00 31.43  ? 197 HIS   C CE1   1 
ATOM   5007  N  NE2   . HIS   B 1  197 ? -31.131 25.284  -0.185   1.00 34.88  ? 197 HIS   C NE2   1 
ATOM   5008  N  N     . SER   B 1  198 ? -25.071 27.811  -2.003   1.00 30.33  ? 198 SER   C N     1 
ATOM   5009  C  CA    . SER   B 1  198 ? -23.751 28.384  -1.844   1.00 28.33  ? 198 SER   C CA    1 
ATOM   5010  C  C     . SER   B 1  198 ? -23.271 28.850  -3.202   1.00 24.62  ? 198 SER   C C     1 
ATOM   5011  O  O     . SER   B 1  198 ? -23.402 28.114  -4.177   1.00 27.22  ? 198 SER   C O     1 
ATOM   5012  C  CB    . SER   B 1  198 ? -22.787 27.356  -1.258   1.00 29.00  ? 198 SER   C CB    1 
ATOM   5013  O  OG    . SER   B 1  198 ? -21.484 27.898  -1.169   1.00 31.35  ? 198 SER   C OG    1 
ATOM   5014  N  N     . ASP   B 1  199 ? -22.711 30.062  -3.262   1.00 22.29  ? 199 ASP   C N     1 
ATOM   5015  C  CA    . ASP   B 1  199 ? -22.257 30.632  -4.526   1.00 25.75  ? 199 ASP   C CA    1 
ATOM   5016  C  C     . ASP   B 1  199 ? -20.799 30.298  -4.858   1.00 24.62  ? 199 ASP   C C     1 
ATOM   5017  O  O     . ASP   B 1  199 ? -20.380 30.465  -6.009   1.00 29.30  ? 199 ASP   C O     1 
ATOM   5018  C  CB    . ASP   B 1  199 ? -22.434 32.163  -4.503   1.00 32.07  ? 199 ASP   C CB    1 
ATOM   5019  C  CG    . ASP   B 1  199 ? -23.848 32.594  -4.113   1.00 32.56  ? 199 ASP   C CG    1 
ATOM   5020  O  OD1   . ASP   B 1  199 ? -24.808 32.256  -4.828   1.00 37.84  ? 199 ASP   C OD1   1 
ATOM   5021  O  OD2   . ASP   B 1  199 ? -24.008 33.254  -3.064   1.00 35.41  ? 199 ASP   C OD2   1 
ATOM   5022  N  N     . CYS   B 1  200 ? -20.017 29.858  -3.874   1.00 24.84  ? 200 CYS   C N     1 
ATOM   5023  C  CA    . CYS   B 1  200 ? -18.576 29.673  -3.985   1.00 23.74  ? 200 CYS   C CA    1 
ATOM   5024  C  C     . CYS   B 1  200 ? -18.099 29.029  -2.694   1.00 28.30  ? 200 CYS   C C     1 
ATOM   5025  O  O     . CYS   B 1  200 ? -18.481 29.475  -1.610   1.00 28.47  ? 200 CYS   C O     1 
ATOM   5026  C  CB    . CYS   B 1  200 ? -17.861 31.005  -4.207   1.00 30.09  ? 200 CYS   C CB    1 
ATOM   5027  S  SG    . CYS   B 1  200 ? -16.096 30.861  -4.639   1.00 34.79  ? 200 CYS   C SG    1 
ATOM   5028  N  N     . ALA   B 1  201 ? -17.302 27.967  -2.779   1.00 27.93  ? 201 ALA   C N     1 
ATOM   5029  C  CA    . ALA   B 1  201 ? -16.864 27.253  -1.584   1.00 26.57  ? 201 ALA   C CA    1 
ATOM   5030  C  C     . ALA   B 1  201 ? -15.412 26.839  -1.758   1.00 23.94  ? 201 ALA   C C     1 
ATOM   5031  O  O     . ALA   B 1  201 ? -15.080 26.132  -2.711   1.00 31.61  ? 201 ALA   C O     1 
ATOM   5032  C  CB    . ALA   B 1  201 ? -17.754 26.037  -1.301   1.00 22.11  ? 201 ALA   C CB    1 
ATOM   5033  N  N     . PHE   B 1  202 ? -14.553 27.285  -0.836   1.00 21.53  ? 202 PHE   C N     1 
ATOM   5034  C  CA    . PHE   B 1  202 ? -13.141 26.924  -0.816   1.00 20.96  ? 202 PHE   C CA    1 
ATOM   5035  C  C     . PHE   B 1  202 ? -12.952 25.740  0.130    1.00 22.89  ? 202 PHE   C C     1 
ATOM   5036  O  O     . PHE   B 1  202 ? -13.036 25.891  1.356    1.00 23.46  ? 202 PHE   C O     1 
ATOM   5037  C  CB    . PHE   B 1  202 ? -12.293 28.118  -0.374   1.00 19.19  ? 202 PHE   C CB    1 
ATOM   5038  C  CG    . PHE   B 1  202 ? -12.500 29.335  -1.208   1.00 25.36  ? 202 PHE   C CG    1 
ATOM   5039  C  CD1   . PHE   B 1  202 ? -13.565 30.172  -0.970   1.00 23.66  ? 202 PHE   C CD1   1 
ATOM   5040  C  CD2   . PHE   B 1  202 ? -11.658 29.622  -2.254   1.00 25.79  ? 202 PHE   C CD2   1 
ATOM   5041  C  CE1   . PHE   B 1  202 ? -13.769 31.245  -1.738   1.00 19.35  ? 202 PHE   C CE1   1 
ATOM   5042  C  CE2   . PHE   B 1  202 ? -11.870 30.712  -3.041   1.00 23.42  ? 202 PHE   C CE2   1 
ATOM   5043  C  CZ    . PHE   B 1  202 ? -12.917 31.529  -2.769   1.00 29.70  ? 202 PHE   C CZ    1 
ATOM   5044  N  N     . MET   B 1  203 ? -12.690 24.569  -0.430   1.00 25.51  ? 203 MET   C N     1 
ATOM   5045  C  CA    . MET   B 1  203 ? -12.385 23.401  0.388    1.00 25.33  ? 203 MET   C CA    1 
ATOM   5046  C  C     . MET   B 1  203 ? -10.941 23.452  0.864    1.00 23.27  ? 203 MET   C C     1 
ATOM   5047  O  O     . MET   B 1  203 ? -10.053 23.901  0.140    1.00 37.52  ? 203 MET   C O     1 
ATOM   5048  C  CB    . MET   B 1  203 ? -12.639 22.116  -0.395   1.00 19.96  ? 203 MET   C CB    1 
ATOM   5049  C  CG    . MET   B 1  203 ? -14.119 21.823  -0.577   1.00 22.40  ? 203 MET   C CG    1 
ATOM   5050  S  SD    . MET   B 1  203 ? -14.426 20.227  -1.334   1.00 31.02  ? 203 MET   C SD    1 
ATOM   5051  C  CE    . MET   B 1  203 ? -13.677 20.507  -2.952   1.00 28.70  ? 203 MET   C CE    1 
ATOM   5052  N  N     . VAL   B 1  204 ? -10.717 23.016  2.096    1.00 24.38  ? 204 VAL   C N     1 
ATOM   5053  C  CA    . VAL   B 1  204 ? -9.383  22.880  2.672    1.00 22.31  ? 204 VAL   C CA    1 
ATOM   5054  C  C     . VAL   B 1  204 ? -9.259  21.423  3.082    1.00 26.84  ? 204 VAL   C C     1 
ATOM   5055  O  O     . VAL   B 1  204 ? -9.962  20.971  3.994    1.00 23.28  ? 204 VAL   C O     1 
ATOM   5056  C  CB    . VAL   B 1  204 ? -9.152  23.815  3.867    1.00 28.15  ? 204 VAL   C CB    1 
ATOM   5057  C  CG1   . VAL   B 1  204 ? -7.697  23.831  4.227    1.00 30.54  ? 204 VAL   C CG1   1 
ATOM   5058  C  CG2   . VAL   B 1  204 ? -9.631  25.245  3.568    1.00 18.93  ? 204 VAL   C CG2   1 
ATOM   5059  N  N     . ASP   B 1  205 ? -8.440  20.667  2.342    1.00 32.41  ? 205 ASP   C N     1 
ATOM   5060  C  CA    . ASP   B 1  205 ? -8.140  19.263  2.635    1.00 28.74  ? 205 ASP   C CA    1 
ATOM   5061  C  C     . ASP   B 1  205 ? -7.234  19.205  3.860    1.00 27.80  ? 205 ASP   C C     1 
ATOM   5062  O  O     . ASP   B 1  205 ? -6.095  19.677  3.821    1.00 26.69  ? 205 ASP   C O     1 
ATOM   5063  C  CB    . ASP   B 1  205 ? -7.468  18.605  1.428    1.00 25.20  ? 205 ASP   C CB    1 
ATOM   5064  C  CG    . ASP   B 1  205 ? -7.276  17.114  1.601    1.00 29.15  ? 205 ASP   C CG    1 
ATOM   5065  O  OD1   . ASP   B 1  205 ? -7.380  16.623  2.743    1.00 30.58  ? 205 ASP   C OD1   1 
ATOM   5066  O  OD2   . ASP   B 1  205 ? -7.006  16.425  0.597    1.00 28.31  ? 205 ASP   C OD2   1 
ATOM   5067  N  N     . ASN   B 1  206 ? -7.733  18.660  4.966    1.00 27.79  ? 206 ASN   C N     1 
ATOM   5068  C  CA    . ASN   B 1  206 ? -6.912  18.700  6.167    1.00 32.45  ? 206 ASN   C CA    1 
ATOM   5069  C  C     . ASN   B 1  206 ? -5.585  17.987  5.943    1.00 36.72  ? 206 ASN   C C     1 
ATOM   5070  O  O     . ASN   B 1  206 ? -4.555  18.400  6.488    1.00 34.31  ? 206 ASN   C O     1 
ATOM   5071  C  CB    . ASN   B 1  206 ? -7.662  18.114  7.355    1.00 28.01  ? 206 ASN   C CB    1 
ATOM   5072  C  CG    . ASN   B 1  206 ? -8.035  19.181  8.383    1.00 30.00  ? 206 ASN   C CG    1 
ATOM   5073  O  OD1   . ASN   B 1  206 ? -7.550  20.296  8.318    1.00 27.50  ? 206 ASN   C OD1   1 
ATOM   5074  N  ND2   . ASN   B 1  206 ? -8.881  18.830  9.343    1.00 26.97  ? 206 ASN   C ND2   1 
ATOM   5075  N  N     . GLU   B 1  207 ? -5.577  16.952  5.105    1.00 30.02  ? 207 GLU   C N     1 
ATOM   5076  C  CA    . GLU   B 1  207 ? -4.331  16.261  4.842    1.00 29.25  ? 207 GLU   C CA    1 
ATOM   5077  C  C     . GLU   B 1  207 ? -3.406  17.126  3.999    1.00 32.57  ? 207 GLU   C C     1 
ATOM   5078  O  O     . GLU   B 1  207 ? -2.191  17.099  4.195    1.00 28.71  ? 207 GLU   C O     1 
ATOM   5079  C  CB    . GLU   B 1  207 ? -4.615  14.920  4.174    1.00 30.82  ? 207 GLU   C CB    1 
ATOM   5080  C  CG    . GLU   B 1  207 ? -3.379  14.112  3.883    1.00 32.37  ? 207 GLU   C CG    1 
ATOM   5081  C  CD    . GLU   B 1  207 ? -3.676  12.936  3.009    1.00 32.90  ? 207 GLU   C CD    1 
ATOM   5082  O  OE1   . GLU   B 1  207 ? -4.487  12.105  3.419    1.00 36.89  ? 207 GLU   C OE1   1 
ATOM   5083  O  OE2   . GLU   B 1  207 ? -3.120  12.850  1.897    1.00 43.69  ? 207 GLU   C OE2   1 
ATOM   5084  N  N     . ALA   B 1  208 ? -3.962  17.922  3.084    1.00 31.54  ? 208 ALA   C N     1 
ATOM   5085  C  CA    . ALA   B 1  208 ? -3.145  18.877  2.345    1.00 29.94  ? 208 ALA   C CA    1 
ATOM   5086  C  C     . ALA   B 1  208 ? -2.414  19.818  3.292    1.00 36.02  ? 208 ALA   C C     1 
ATOM   5087  O  O     . ALA   B 1  208 ? -1.217  20.100  3.112    1.00 29.26  ? 208 ALA   C O     1 
ATOM   5088  C  CB    . ALA   B 1  208 ? -4.017  19.674  1.374    1.00 28.39  ? 208 ALA   C CB    1 
ATOM   5089  N  N     . ILE   B 1  209 ? -3.140  20.346  4.288    1.00 33.96  ? 209 ILE   C N     1 
ATOM   5090  C  CA    . ILE   B 1  209 ? -2.555  21.284  5.241    1.00 33.28  ? 209 ILE   C CA    1 
ATOM   5091  C  C     . ILE   B 1  209 ? -1.613  20.550  6.186    1.00 29.35  ? 209 ILE   C C     1 
ATOM   5092  O  O     . ILE   B 1  209 ? -0.567  21.071  6.577    1.00 33.95  ? 209 ILE   C O     1 
ATOM   5093  C  CB    . ILE   B 1  209 ? -3.665  22.033  6.005    1.00 31.38  ? 209 ILE   C CB    1 
ATOM   5094  C  CG1   . ILE   B 1  209 ? -4.422  22.907  5.050    1.00 29.13  ? 209 ILE   C CG1   1 
ATOM   5095  C  CG2   . ILE   B 1  209 ? -3.080  22.967  7.015    1.00 36.38  ? 209 ILE   C CG2   1 
ATOM   5096  C  CD1   . ILE   B 1  209 ? -3.518  23.834  4.354    1.00 33.52  ? 209 ILE   C CD1   1 
ATOM   5097  N  N     . TYR   B 1  210 ? -1.959  19.323  6.553    1.00 31.98  ? 210 TYR   C N     1 
ATOM   5098  C  CA    . TYR   B 1  210 ? -1.040  18.508  7.330    1.00 33.13  ? 210 TYR   C CA    1 
ATOM   5099  C  C     . TYR   B 1  210 ? 0.317   18.382  6.636    1.00 37.18  ? 210 TYR   C C     1 
ATOM   5100  O  O     . TYR   B 1  210 ? 1.365   18.585  7.258    1.00 39.41  ? 210 TYR   C O     1 
ATOM   5101  C  CB    . TYR   B 1  210 ? -1.663  17.146  7.574    1.00 28.19  ? 210 TYR   C CB    1 
ATOM   5102  C  CG    . TYR   B 1  210 ? -1.189  16.501  8.838    1.00 39.89  ? 210 TYR   C CG    1 
ATOM   5103  C  CD1   . TYR   B 1  210 ? -1.618  16.961  10.082   1.00 48.29  ? 210 TYR   C CD1   1 
ATOM   5104  C  CD2   . TYR   B 1  210 ? -0.323  15.421  8.797    1.00 37.98  ? 210 TYR   C CD2   1 
ATOM   5105  C  CE1   . TYR   B 1  210 ? -1.183  16.358  11.258   1.00 50.96  ? 210 TYR   C CE1   1 
ATOM   5106  C  CE2   . TYR   B 1  210 ? 0.115   14.816  9.949    1.00 44.79  ? 210 TYR   C CE2   1 
ATOM   5107  C  CZ    . TYR   B 1  210 ? -0.313  15.278  11.180   1.00 53.93  ? 210 TYR   C CZ    1 
ATOM   5108  O  OH    . TYR   B 1  210 ? 0.136   14.651  12.323   1.00 51.38  ? 210 TYR   C OH    1 
ATOM   5109  N  N     . ASP   B 1  211 ? 0.318   18.069  5.337    1.00 30.71  ? 211 ASP   C N     1 
ATOM   5110  C  CA    . ASP   B 1  211 ? 1.576   17.783  4.651    1.00 35.25  ? 211 ASP   C CA    1 
ATOM   5111  C  C     . ASP   B 1  211 ? 2.393   19.047  4.448    1.00 43.84  ? 211 ASP   C C     1 
ATOM   5112  O  O     . ASP   B 1  211 ? 3.612   19.042  4.655    1.00 40.56  ? 211 ASP   C O     1 
ATOM   5113  C  CB    . ASP   B 1  211 ? 1.322   17.108  3.308    1.00 26.83  ? 211 ASP   C CB    1 
ATOM   5114  C  CG    . ASP   B 1  211 ? 0.815   15.704  3.451    1.00 40.18  ? 211 ASP   C CG    1 
ATOM   5115  O  OD1   . ASP   B 1  211 ? 1.163   15.029  4.443    1.00 45.02  ? 211 ASP   C OD1   1 
ATOM   5116  O  OD2   . ASP   B 1  211 ? 0.059   15.268  2.563    1.00 48.64  ? 211 ASP   C OD2   1 
ATOM   5117  N  N     . ILE   B 1  212 ? 1.741   20.138  4.034    1.00 41.37  ? 212 ILE   C N     1 
ATOM   5118  C  CA    . ILE   B 1  212 ? 2.429   21.418  3.917    1.00 32.45  ? 212 ILE   C CA    1 
ATOM   5119  C  C     . ILE   B 1  212 ? 3.100   21.803  5.235    1.00 39.85  ? 212 ILE   C C     1 
ATOM   5120  O  O     . ILE   B 1  212 ? 4.209   22.355  5.240    1.00 40.03  ? 212 ILE   C O     1 
ATOM   5121  C  CB    . ILE   B 1  212 ? 1.450   22.499  3.433    1.00 31.47  ? 212 ILE   C CB    1 
ATOM   5122  C  CG1   . ILE   B 1  212 ? 1.110   22.263  1.949    1.00 37.32  ? 212 ILE   C CG1   1 
ATOM   5123  C  CG2   . ILE   B 1  212 ? 2.050   23.867  3.661    1.00 27.72  ? 212 ILE   C CG2   1 
ATOM   5124  C  CD1   . ILE   B 1  212 ? -0.081  23.042  1.435    1.00 32.24  ? 212 ILE   C CD1   1 
ATOM   5125  N  N     . CYS   B 1  213 ? 2.462   21.492  6.375    1.00 31.77  ? 213 CYS   C N     1 
ATOM   5126  C  CA    . CYS   B 1  213 ? 3.049   21.853  7.660    1.00 33.92  ? 213 CYS   C CA    1 
ATOM   5127  C  C     . CYS   B 1  213 ? 4.228   20.945  8.031    1.00 39.60  ? 213 CYS   C C     1 
ATOM   5128  O  O     . CYS   B 1  213 ? 5.225   21.411  8.591    1.00 40.11  ? 213 CYS   C O     1 
ATOM   5129  C  CB    . CYS   B 1  213 ? 1.972   21.841  8.745    1.00 44.52  ? 213 CYS   C CB    1 
ATOM   5130  S  SG    . CYS   B 1  213 ? 0.962   23.373  8.797    1.00 43.64  ? 213 CYS   C SG    1 
ATOM   5131  N  N     . ARG   B 1  214 ? 4.142   19.652  7.736    1.00 41.12  ? 214 ARG   C N     1 
ATOM   5132  C  CA    . ARG   B 1  214 ? 5.294   18.782  7.953    1.00 48.32  ? 214 ARG   C CA    1 
ATOM   5133  C  C     . ARG   B 1  214 ? 6.455   19.166  7.043    1.00 47.84  ? 214 ARG   C C     1 
ATOM   5134  O  O     . ARG   B 1  214 ? 7.585   19.351  7.514    1.00 47.83  ? 214 ARG   C O     1 
ATOM   5135  C  CB    . ARG   B 1  214 ? 4.911   17.314  7.736    1.00 38.96  ? 214 ARG   C CB    1 
ATOM   5136  C  CG    . ARG   B 1  214 ? 4.075   16.762  8.852    1.00 39.84  ? 214 ARG   C CG    1 
ATOM   5137  C  CD    . ARG   B 1  214 ? 4.053   15.253  8.873    1.00 40.37  ? 214 ARG   C CD    1 
ATOM   5138  N  NE    . ARG   B 1  214 ? 2.971   14.736  8.050    1.00 52.74  ? 214 ARG   C NE    1 
ATOM   5139  C  CZ    . ARG   B 1  214 ? 2.841   13.468  7.690    1.00 59.67  ? 214 ARG   C CZ    1 
ATOM   5140  N  NH1   . ARG   B 1  214 ? 3.688   12.536  8.114    1.00 57.24  ? 214 ARG   C NH1   1 
ATOM   5141  N  NH2   . ARG   B 1  214 ? 1.844   13.129  6.874    1.00 47.43  ? 214 ARG   C NH2   1 
ATOM   5142  N  N     . ARG   B 1  215 ? 6.181   19.325  5.738    1.00 45.82  ? 215 ARG   C N     1 
ATOM   5143  C  CA    . ARG   B 1  215 ? 7.221   19.429  4.716    1.00 33.21  ? 215 ARG   C CA    1 
ATOM   5144  C  C     . ARG   B 1  215 ? 7.826   20.808  4.609    1.00 38.49  ? 215 ARG   C C     1 
ATOM   5145  O  O     . ARG   B 1  215 ? 8.963   20.922  4.140    1.00 45.95  ? 215 ARG   C O     1 
ATOM   5146  C  CB    . ARG   B 1  215 ? 6.680   19.057  3.339    1.00 37.40  ? 215 ARG   C CB    1 
ATOM   5147  C  CG    . ARG   B 1  215 ? 6.362   17.582  3.141    1.00 55.04  ? 215 ARG   C CG    1 
ATOM   5148  C  CD    . ARG   B 1  215 ? 5.771   17.315  1.745    1.00 66.80  ? 215 ARG   C CD    1 
ATOM   5149  N  NE    . ARG   B 1  215 ? 5.455   15.902  1.556    1.00 72.51  ? 215 ARG   C NE    1 
ATOM   5150  C  CZ    . ARG   B 1  215 ? 4.658   15.197  2.350    1.00 58.06  ? 215 ARG   C CZ    1 
ATOM   5151  N  NH1   . ARG   B 1  215 ? 4.110   15.728  3.433    1.00 48.68  ? 215 ARG   C NH1   1 
ATOM   5152  N  NH2   . ARG   B 1  215 ? 4.412   13.925  2.054    1.00 66.56  ? 215 ARG   C NH2   1 
ATOM   5153  N  N     . ASN   B 1  216 ? 7.086   21.853  4.981    1.00 41.44  ? 216 ASN   C N     1 
ATOM   5154  C  CA    . ASN   B 1  216 ? 7.486   23.246  4.772    1.00 36.13  ? 216 ASN   C CA    1 
ATOM   5155  C  C     . ASN   B 1  216 ? 7.873   23.957  6.053    1.00 48.78  ? 216 ASN   C C     1 
ATOM   5156  O  O     . ASN   B 1  216 ? 8.772   24.803  6.041    1.00 50.20  ? 216 ASN   C O     1 
ATOM   5157  C  CB    . ASN   B 1  216 ? 6.345   24.043  4.132    1.00 42.31  ? 216 ASN   C CB    1 
ATOM   5158  C  CG    . ASN   B 1  216 ? 6.272   23.882  2.643    1.00 35.60  ? 216 ASN   C CG    1 
ATOM   5159  O  OD1   . ASN   B 1  216 ? 5.750   22.896  2.134    1.00 32.17  ? 216 ASN   C OD1   1 
ATOM   5160  N  ND2   . ASN   B 1  216 ? 6.746   24.884  1.931    1.00 39.30  ? 216 ASN   C ND2   1 
ATOM   5161  N  N     . LEU   B 1  217 ? 7.165   23.666  7.140    1.00 46.80  ? 217 LEU   C N     1 
ATOM   5162  C  CA    . LEU   B 1  217 ? 7.422   24.231  8.452    1.00 44.57  ? 217 LEU   C CA    1 
ATOM   5163  C  C     . LEU   B 1  217 ? 8.288   23.331  9.327    1.00 45.59  ? 217 LEU   C C     1 
ATOM   5164  O  O     . LEU   B 1  217 ? 8.535   23.670  10.487   1.00 44.29  ? 217 LEU   C O     1 
ATOM   5165  C  CB    . LEU   B 1  217 ? 6.092   24.502  9.157    1.00 36.89  ? 217 LEU   C CB    1 
ATOM   5166  C  CG    . LEU   B 1  217 ? 5.195   25.425  8.361    1.00 43.33  ? 217 LEU   C CG    1 
ATOM   5167  C  CD1   . LEU   B 1  217 ? 4.004   25.797  9.197    1.00 43.73  ? 217 LEU   C CD1   1 
ATOM   5168  C  CD2   . LEU   B 1  217 ? 5.980   26.659  7.928    1.00 42.30  ? 217 LEU   C CD2   1 
ATOM   5169  N  N     . ASP   B 1  218 ? 8.745   22.195  8.809    1.00 45.73  ? 218 ASP   C N     1 
ATOM   5170  C  CA    . ASP   B 1  218 ? 9.504   21.223  9.599    1.00 53.21  ? 218 ASP   C CA    1 
ATOM   5171  C  C     . ASP   B 1  218 ? 8.812   20.976  10.938   1.00 48.25  ? 218 ASP   C C     1 
ATOM   5172  O  O     . ASP   B 1  218 ? 9.425   21.046  12.005   1.00 54.62  ? 218 ASP   C O     1 
ATOM   5173  C  CB    . ASP   B 1  218 ? 10.962  21.674  9.800    1.00 48.90  ? 218 ASP   C CB    1 
ATOM   5174  C  CG    . ASP   B 1  218 ? 11.663  22.064  8.479    1.00 68.52  ? 218 ASP   C CG    1 
ATOM   5175  O  OD1   . ASP   B 1  218 ? 11.819  21.186  7.600    1.00 83.98  ? 218 ASP   C OD1   1 
ATOM   5176  O  OD2   . ASP   B 1  218 ? 12.053  23.251  8.311    1.00 60.68  ? 218 ASP   C OD2   1 
ATOM   5177  N  N     . ILE   B 1  219 ? 7.509   20.695  10.878   1.00 45.07  ? 219 ILE   C N     1 
ATOM   5178  C  CA    . ILE   B 1  219 ? 6.707   20.393  12.065   1.00 46.90  ? 219 ILE   C CA    1 
ATOM   5179  C  C     . ILE   B 1  219 ? 6.427   18.899  12.073   1.00 49.22  ? 219 ILE   C C     1 
ATOM   5180  O  O     . ILE   B 1  219 ? 5.748   18.381  11.178   1.00 50.35  ? 219 ILE   C O     1 
ATOM   5181  C  CB    . ILE   B 1  219 ? 5.401   21.203  12.100   1.00 47.12  ? 219 ILE   C CB    1 
ATOM   5182  C  CG1   . ILE   B 1  219 ? 5.713   22.696  11.983   1.00 45.56  ? 219 ILE   C CG1   1 
ATOM   5183  C  CG2   . ILE   B 1  219 ? 4.596   20.901  13.371   1.00 39.02  ? 219 ILE   C CG2   1 
ATOM   5184  C  CD1   . ILE   B 1  219 ? 4.543   23.597  12.254   1.00 44.38  ? 219 ILE   C CD1   1 
ATOM   5185  N  N     . GLU   B 1  220 ? 6.963   18.205  13.078   1.00 59.69  ? 220 GLU   C N     1 
ATOM   5186  C  CA    . GLU   B 1  220 ? 6.861   16.749  13.118   1.00 59.63  ? 220 GLU   C CA    1 
ATOM   5187  C  C     . GLU   B 1  220 ? 5.407   16.304  13.036   1.00 52.26  ? 220 GLU   C C     1 
ATOM   5188  O  O     . GLU   B 1  220 ? 5.011   15.577  12.118   1.00 58.15  ? 220 GLU   C O     1 
ATOM   5189  C  CB    . GLU   B 1  220 ? 7.520   16.210  14.396   1.00 62.62  ? 220 GLU   C CB    1 
ATOM   5190  C  CG    . GLU   B 1  220 ? 9.007   16.525  14.530   1.00 81.35  ? 220 GLU   C CG    1 
ATOM   5191  C  CD    . GLU   B 1  220 ? 9.499   16.484  15.976   1.00 93.20  ? 220 GLU   C CD    1 
ATOM   5192  O  OE1   . GLU   B 1  220 ? 8.809   15.857  16.822   1.00 67.93  ? 220 GLU   C OE1   1 
ATOM   5193  O  OE2   . GLU   B 1  220 ? 10.573  17.087  16.255   1.00 80.66  ? 220 GLU   C OE2   1 
ATOM   5194  N  N     . ARG   B 1  221 ? 4.596   16.743  13.995   1.00 49.29  ? 221 ARG   C N     1 
ATOM   5195  C  CA    . ARG   B 1  221 ? 3.225   16.272  14.158   1.00 53.52  ? 221 ARG   C CA    1 
ATOM   5196  C  C     . ARG   B 1  221 ? 2.343   17.496  14.400   1.00 58.17  ? 221 ARG   C C     1 
ATOM   5197  O  O     . ARG   B 1  221 ? 2.069   17.877  15.546   1.00 57.54  ? 221 ARG   C O     1 
ATOM   5198  C  CB    . ARG   B 1  221 ? 3.138   15.246  15.290   1.00 47.96  ? 221 ARG   C CB    1 
ATOM   5199  C  CG    . ARG   B 1  221 ? 1.759   14.794  15.664   1.00 55.80  ? 221 ARG   C CG    1 
ATOM   5200  C  CD    . ARG   B 1  221 ? 1.264   13.689  14.768   1.00 57.76  ? 221 ARG   C CD    1 
ATOM   5201  N  NE    . ARG   B 1  221 ? -0.122  13.321  15.057   1.00 61.90  ? 221 ARG   C NE    1 
ATOM   5202  C  CZ    . ARG   B 1  221 ? -1.155  14.158  15.013   1.00 64.41  ? 221 ARG   C CZ    1 
ATOM   5203  N  NH1   . ARG   B 1  221 ? -0.986  15.459  14.794   1.00 61.05  ? 221 ARG   C NH1   1 
ATOM   5204  N  NH2   . ARG   B 1  221 ? -2.388  13.680  15.187   1.00 49.87  ? 221 ARG   C NH2   1 
ATOM   5205  N  N     . PRO   B 1  222 ? 1.883   18.140  13.322   1.00 53.46  ? 222 PRO   C N     1 
ATOM   5206  C  CA    . PRO   B 1  222 ? 1.150   19.407  13.440   1.00 42.47  ? 222 PRO   C CA    1 
ATOM   5207  C  C     . PRO   B 1  222 ? -0.139  19.308  14.243   1.00 40.63  ? 222 PRO   C C     1 
ATOM   5208  O  O     . PRO   B 1  222 ? -0.775  18.257  14.365   1.00 41.91  ? 222 PRO   C O     1 
ATOM   5209  C  CB    . PRO   B 1  222 ? 0.839   19.762  11.983   1.00 47.80  ? 222 PRO   C CB    1 
ATOM   5210  C  CG    . PRO   B 1  222 ? 1.829   19.016  11.183   1.00 43.35  ? 222 PRO   C CG    1 
ATOM   5211  C  CD    . PRO   B 1  222 ? 2.093   17.752  11.918   1.00 39.88  ? 222 PRO   C CD    1 
ATOM   5212  N  N     . THR   B 1  223 ? -0.537  20.456  14.769   1.00 45.24  ? 223 THR   C N     1 
ATOM   5213  C  CA    . THR   B 1  223 ? -1.754  20.612  15.552   1.00 43.87  ? 223 THR   C CA    1 
ATOM   5214  C  C     . THR   B 1  223 ? -2.773  21.424  14.768   1.00 44.95  ? 223 THR   C C     1 
ATOM   5215  O  O     . THR   B 1  223 ? -2.477  22.014  13.721   1.00 46.47  ? 223 THR   C O     1 
ATOM   5216  C  CB    . THR   B 1  223 ? -1.483  21.316  16.890   1.00 35.19  ? 223 THR   C CB    1 
ATOM   5217  O  OG1   . THR   B 1  223 ? -1.162  22.690  16.650   1.00 43.72  ? 223 THR   C OG1   1 
ATOM   5218  C  CG2   . THR   B 1  223 ? -0.350  20.663  17.640   1.00 40.96  ? 223 THR   C CG2   1 
ATOM   5219  N  N     . TYR   B 1  224 ? -3.994  21.464  15.301   1.00 37.87  ? 224 TYR   C N     1 
ATOM   5220  C  CA    . TYR   B 1  224 ? -4.973  22.381  14.736   1.00 36.07  ? 224 TYR   C CA    1 
ATOM   5221  C  C     . TYR   B 1  224 ? -4.456  23.816  14.743   1.00 28.38  ? 224 TYR   C C     1 
ATOM   5222  O  O     . TYR   B 1  224 ? -4.886  24.636  13.929   1.00 31.90  ? 224 TYR   C O     1 
ATOM   5223  C  CB    . TYR   B 1  224 ? -6.284  22.288  15.510   1.00 24.88  ? 224 TYR   C CB    1 
ATOM   5224  C  CG    . TYR   B 1  224 ? -7.061  21.028  15.319   1.00 22.56  ? 224 TYR   C CG    1 
ATOM   5225  C  CD1   . TYR   B 1  224 ? -7.136  20.402  14.070   1.00 22.08  ? 224 TYR   C CD1   1 
ATOM   5226  C  CD2   . TYR   B 1  224 ? -7.757  20.458  16.399   1.00 23.80  ? 224 TYR   C CD2   1 
ATOM   5227  C  CE1   . TYR   B 1  224 ? -7.893  19.239  13.910   1.00 25.16  ? 224 TYR   C CE1   1 
ATOM   5228  C  CE2   . TYR   B 1  224 ? -8.507  19.312  16.258   1.00 22.86  ? 224 TYR   C CE2   1 
ATOM   5229  C  CZ    . TYR   B 1  224 ? -8.579  18.700  15.019   1.00 27.87  ? 224 TYR   C CZ    1 
ATOM   5230  O  OH    . TYR   B 1  224 ? -9.329  17.551  14.909   1.00 29.03  ? 224 TYR   C OH    1 
ATOM   5231  N  N     . THR   B 1  225 ? -3.547  24.146  15.656   1.00 34.36  ? 225 THR   C N     1 
ATOM   5232  C  CA    . THR   B 1  225 ? -3.027  25.509  15.677   1.00 41.39  ? 225 THR   C CA    1 
ATOM   5233  C  C     . THR   B 1  225 ? -2.036  25.734  14.537   1.00 39.04  ? 225 THR   C C     1 
ATOM   5234  O  O     . THR   B 1  225 ? -2.040  26.799  13.911   1.00 41.24  ? 225 THR   C O     1 
ATOM   5235  C  CB    . THR   B 1  225 ? -2.391  25.821  17.036   1.00 42.00  ? 225 THR   C CB    1 
ATOM   5236  O  OG1   . THR   B 1  225 ? -3.374  25.680  18.069   1.00 39.65  ? 225 THR   C OG1   1 
ATOM   5237  C  CG2   . THR   B 1  225 ? -1.847  27.253  17.054   1.00 44.96  ? 225 THR   C CG2   1 
ATOM   5238  N  N     . ASN   B 1  226 ? -1.196  24.749  14.229   1.00 24.77  ? 226 ASN   C N     1 
ATOM   5239  C  CA    . ASN   B 1  226 ? -0.411  24.854  13.004   1.00 39.10  ? 226 ASN   C CA    1 
ATOM   5240  C  C     . ASN   B 1  226 ? -1.336  25.048  11.800   1.00 42.16  ? 226 ASN   C C     1 
ATOM   5241  O  O     . ASN   B 1  226 ? -1.201  26.019  11.034   1.00 33.96  ? 226 ASN   C O     1 
ATOM   5242  C  CB    . ASN   B 1  226 ? 0.462   23.604  12.817   1.00 42.79  ? 226 ASN   C CB    1 
ATOM   5243  C  CG    . ASN   B 1  226 ? 1.289   23.258  14.049   1.00 42.96  ? 226 ASN   C CG    1 
ATOM   5244  O  OD1   . ASN   B 1  226 ? 1.004   22.288  14.742   1.00 49.20  ? 226 ASN   C OD1   1 
ATOM   5245  N  ND2   . ASN   B 1  226 ? 2.330   24.028  14.306   1.00 48.22  ? 226 ASN   C ND2   1 
ATOM   5246  N  N     . LEU   B 1  227 ? -2.314  24.144  11.654   1.00 35.26  ? 227 LEU   C N     1 
ATOM   5247  C  CA    . LEU   B 1  227 ? -3.221  24.154  10.512   1.00 27.49  ? 227 LEU   C CA    1 
ATOM   5248  C  C     . LEU   B 1  227 ? -4.006  25.454  10.431   1.00 33.91  ? 227 LEU   C C     1 
ATOM   5249  O  O     . LEU   B 1  227 ? -4.103  26.068  9.366    1.00 41.99  ? 227 LEU   C O     1 
ATOM   5250  C  CB    . LEU   B 1  227 ? -4.167  22.959  10.604   1.00 31.19  ? 227 LEU   C CB    1 
ATOM   5251  C  CG    . LEU   B 1  227 ? -3.619  21.585  10.162   1.00 38.63  ? 227 LEU   C CG    1 
ATOM   5252  C  CD1   . LEU   B 1  227 ? -2.305  21.307  10.795   1.00 31.99  ? 227 LEU   C CD1   1 
ATOM   5253  C  CD2   . LEU   B 1  227 ? -4.594  20.447  10.466   1.00 33.68  ? 227 LEU   C CD2   1 
ATOM   5254  N  N     . ASN   B 1  228 ? -4.563  25.907  11.547   1.00 33.74  ? 228 ASN   C N     1 
ATOM   5255  C  CA    . ASN   B 1  228 ? -5.494  27.019  11.457   1.00 29.36  ? 228 ASN   C CA    1 
ATOM   5256  C  C     . ASN   B 1  228 ? -4.780  28.317  11.152   1.00 30.58  ? 228 ASN   C C     1 
ATOM   5257  O  O     . ASN   B 1  228 ? -5.347  29.191  10.491   1.00 32.95  ? 228 ASN   C O     1 
ATOM   5258  C  CB    . ASN   B 1  228 ? -6.324  27.104  12.742   1.00 37.23  ? 228 ASN   C CB    1 
ATOM   5259  C  CG    . ASN   B 1  228 ? -7.281  25.920  12.887   1.00 33.38  ? 228 ASN   C CG    1 
ATOM   5260  O  OD1   . ASN   B 1  228 ? -7.490  25.161  11.924   1.00 40.18  ? 228 ASN   C OD1   1 
ATOM   5261  N  ND2   . ASN   B 1  228 ? -7.880  25.769  14.059   1.00 25.41  ? 228 ASN   C ND2   1 
ATOM   5262  N  N     . ARG   B 1  229 ? -3.526  28.452  11.584   1.00 41.47  ? 229 ARG   C N     1 
ATOM   5263  C  CA    . ARG   B 1  229 ? -2.736  29.606  11.158   1.00 39.10  ? 229 ARG   C CA    1 
ATOM   5264  C  C     . ARG   B 1  229 ? -2.443  29.552  9.666    1.00 37.98  ? 229 ARG   C C     1 
ATOM   5265  O  O     . ARG   B 1  229 ? -2.609  30.552  8.961    1.00 40.25  ? 229 ARG   C O     1 
ATOM   5266  C  CB    . ARG   B 1  229 ? -1.452  29.696  11.975   1.00 36.72  ? 229 ARG   C CB    1 
ATOM   5267  C  CG    . ARG   B 1  229 ? -1.721  30.349  13.330   1.00 49.46  ? 229 ARG   C CG    1 
ATOM   5268  C  CD    . ARG   B 1  229 ? -0.679  30.016  14.368   1.00 55.99  ? 229 ARG   C CD    1 
ATOM   5269  N  NE    . ARG   B 1  229 ? -1.024  30.644  15.634   1.00 59.44  ? 229 ARG   C NE    1 
ATOM   5270  C  CZ    . ARG   B 1  229 ? -0.277  30.605  16.726   1.00 52.01  ? 229 ARG   C CZ    1 
ATOM   5271  N  NH1   . ARG   B 1  229 ? 0.870   29.941  16.759   1.00 58.15  ? 229 ARG   C NH1   1 
ATOM   5272  N  NH2   . ARG   B 1  229 ? -0.691  31.249  17.811   1.00 61.72  ? 229 ARG   C NH2   1 
ATOM   5273  N  N     . LEU   B 1  230 ? -2.053  28.391  9.147    1.00 28.70  ? 230 LEU   C N     1 
ATOM   5274  C  CA    . LEU   B 1  230 ? -1.888  28.316  7.702    1.00 39.36  ? 230 LEU   C CA    1 
ATOM   5275  C  C     . LEU   B 1  230 ? -3.197  28.665  6.999    1.00 37.47  ? 230 LEU   C C     1 
ATOM   5276  O  O     . LEU   B 1  230 ? -3.207  29.456  6.050    1.00 36.06  ? 230 LEU   C O     1 
ATOM   5277  C  CB    . LEU   B 1  230 ? -1.379  26.929  7.300    1.00 42.24  ? 230 LEU   C CB    1 
ATOM   5278  C  CG    . LEU   B 1  230 ? -0.895  26.699  5.875    1.00 35.61  ? 230 LEU   C CG    1 
ATOM   5279  C  CD1   . LEU   B 1  230 ? -0.040  27.851  5.414    1.00 40.65  ? 230 LEU   C CD1   1 
ATOM   5280  C  CD2   . LEU   B 1  230 ? -0.104  25.415  5.869    1.00 37.27  ? 230 LEU   C CD2   1 
ATOM   5281  N  N     . ILE   B 1  231 ? -4.320  28.118  7.487    1.00 36.27  ? 231 ILE   C N     1 
ATOM   5282  C  CA    . ILE   B 1  231 ? -5.625  28.413  6.901    1.00 30.62  ? 231 ILE   C CA    1 
ATOM   5283  C  C     . ILE   B 1  231 ? -5.949  29.896  7.028    1.00 36.89  ? 231 ILE   C C     1 
ATOM   5284  O  O     . ILE   B 1  231 ? -6.522  30.506  6.113    1.00 32.19  ? 231 ILE   C O     1 
ATOM   5285  C  CB    . ILE   B 1  231 ? -6.713  27.565  7.573    1.00 31.02  ? 231 ILE   C CB    1 
ATOM   5286  C  CG1   . ILE   B 1  231 ? -6.419  26.066  7.470    1.00 31.53  ? 231 ILE   C CG1   1 
ATOM   5287  C  CG2   . ILE   B 1  231 ? -8.063  27.909  6.987    1.00 30.17  ? 231 ILE   C CG2   1 
ATOM   5288  C  CD1   . ILE   B 1  231 ? -7.604  25.250  7.948    1.00 25.17  ? 231 ILE   C CD1   1 
ATOM   5289  N  N     . SER   B 1  232 ? -5.620  30.490  8.182    1.00 31.98  ? 232 SER   C N     1 
ATOM   5290  C  CA    . SER   B 1  232 ? -5.818  31.925  8.381    1.00 35.50  ? 232 SER   C CA    1 
ATOM   5291  C  C     . SER   B 1  232 ? -5.200  32.749  7.259    1.00 34.98  ? 232 SER   C C     1 
ATOM   5292  O  O     . SER   B 1  232 ? -5.781  33.740  6.811    1.00 38.08  ? 232 SER   C O     1 
ATOM   5293  C  CB    . SER   B 1  232 ? -5.207  32.352  9.710    1.00 48.45  ? 232 SER   C CB    1 
ATOM   5294  O  OG    . SER   B 1  232 ? -3.882  32.844  9.490    1.00 57.54  ? 232 SER   C OG    1 
ATOM   5295  N  N     . GLN   B 1  233 ? -4.005  32.367  6.810    1.00 38.90  ? 233 GLN   C N     1 
ATOM   5296  C  CA    . GLN   B 1  233 ? -3.341  33.100  5.739    1.00 33.26  ? 233 GLN   C CA    1 
ATOM   5297  C  C     . GLN   B 1  233 ? -4.152  33.037  4.454    1.00 32.16  ? 233 GLN   C C     1 
ATOM   5298  O  O     . GLN   B 1  233 ? -4.498  34.073  3.881    1.00 30.87  ? 233 GLN   C O     1 
ATOM   5299  C  CB    . GLN   B 1  233 ? -1.928  32.551  5.535    1.00 36.49  ? 233 GLN   C CB    1 
ATOM   5300  C  CG    . GLN   B 1  233 ? -1.112  32.574  6.812    1.00 33.87  ? 233 GLN   C CG    1 
ATOM   5301  C  CD    . GLN   B 1  233 ? -0.793  33.965  7.200    1.00 32.20  ? 233 GLN   C CD    1 
ATOM   5302  O  OE1   . GLN   B 1  233 ? -0.963  34.878  6.400    1.00 32.08  ? 233 GLN   C OE1   1 
ATOM   5303  N  NE2   . GLN   B 1  233 ? -0.328  34.156  8.419    1.00 35.45  ? 233 GLN   C NE2   1 
ATOM   5304  N  N     . ILE   B 1  234 ? -4.472  31.825  3.980    1.00 36.77  ? 234 ILE   C N     1 
ATOM   5305  C  CA    . ILE   B 1  234 ? -5.271  31.707  2.756    1.00 33.05  ? 234 ILE   C CA    1 
ATOM   5306  C  C     . ILE   B 1  234 ? -6.538  32.543  2.870    1.00 31.16  ? 234 ILE   C C     1 
ATOM   5307  O  O     . ILE   B 1  234 ? -6.876  33.324  1.974    1.00 34.32  ? 234 ILE   C O     1 
ATOM   5308  C  CB    . ILE   B 1  234 ? -5.599  30.233  2.448    1.00 33.13  ? 234 ILE   C CB    1 
ATOM   5309  C  CG1   . ILE   B 1  234 ? -4.331  29.445  2.155    1.00 36.74  ? 234 ILE   C CG1   1 
ATOM   5310  C  CG2   . ILE   B 1  234 ? -6.472  30.129  1.240    1.00 32.74  ? 234 ILE   C CG2   1 
ATOM   5311  C  CD1   . ILE   B 1  234 ? -3.622  28.973  3.388    1.00 34.99  ? 234 ILE   C CD1   1 
ATOM   5312  N  N     . VAL   B 1  235 ? -7.252  32.411  3.987    1.00 32.31  ? 235 VAL   C N     1 
ATOM   5313  C  CA    . VAL   B 1  235 ? -8.483  33.176  4.158    1.00 32.53  ? 235 VAL   C CA    1 
ATOM   5314  C  C     . VAL   B 1  235 ? -8.195  34.674  4.115    1.00 31.81  ? 235 VAL   C C     1 
ATOM   5315  O  O     . VAL   B 1  235 ? -8.899  35.444  3.454    1.00 38.94  ? 235 VAL   C O     1 
ATOM   5316  C  CB    . VAL   B 1  235 ? -9.194  32.767  5.460    1.00 31.75  ? 235 VAL   C CB    1 
ATOM   5317  C  CG1   . VAL   B 1  235 ? -10.345 33.739  5.773    1.00 30.47  ? 235 VAL   C CG1   1 
ATOM   5318  C  CG2   . VAL   B 1  235 ? -9.692  31.363  5.342    1.00 21.43  ? 235 VAL   C CG2   1 
ATOM   5319  N  N     . SER   B 1  236 ? -7.171  35.118  4.835    1.00 31.28  ? 236 SER   C N     1 
ATOM   5320  C  CA    . SER   B 1  236 ? -6.840  36.541  4.805    1.00 38.88  ? 236 SER   C CA    1 
ATOM   5321  C  C     . SER   B 1  236 ? -6.524  37.018  3.378    1.00 37.24  ? 236 SER   C C     1 
ATOM   5322  O  O     . SER   B 1  236 ? -6.912  38.125  2.987    1.00 36.76  ? 236 SER   C O     1 
ATOM   5323  C  CB    . SER   B 1  236 ? -5.669  36.821  5.750    1.00 31.56  ? 236 SER   C CB    1 
ATOM   5324  O  OG    . SER   B 1  236 ? -5.049  38.045  5.401    1.00 36.05  ? 236 SER   C OG    1 
ATOM   5325  N  N     . SER   B 1  237 ? -5.817  36.201  2.586    1.00 34.54  ? 237 SER   C N     1 
ATOM   5326  C  CA    . SER   B 1  237 ? -5.569  36.561  1.193    1.00 35.53  ? 237 SER   C CA    1 
ATOM   5327  C  C     . SER   B 1  237 ? -6.873  36.683  0.424    1.00 39.23  ? 237 SER   C C     1 
ATOM   5328  O  O     . SER   B 1  237 ? -7.112  37.695  -0.242   1.00 41.88  ? 237 SER   C O     1 
ATOM   5329  C  CB    . SER   B 1  237 ? -4.668  35.534  0.524    1.00 31.31  ? 237 SER   C CB    1 
ATOM   5330  O  OG    . SER   B 1  237 ? -3.920  34.864  1.504    1.00 33.48  ? 237 SER   C OG    1 
ATOM   5331  N  N     . ILE   B 1  238 ? -7.738  35.660  0.506    1.00 33.78  ? 238 ILE   C N     1 
ATOM   5332  C  CA    . ILE   B 1  238 ? -9.038  35.749  -0.161   1.00 37.47  ? 238 ILE   C CA    1 
ATOM   5333  C  C     . ILE   B 1  238 ? -9.731  37.057  0.194    1.00 39.49  ? 238 ILE   C C     1 
ATOM   5334  O  O     . ILE   B 1  238 ? -10.198 37.792  -0.685   1.00 47.11  ? 238 ILE   C O     1 
ATOM   5335  C  CB    . ILE   B 1  238 ? -9.931  34.546  0.188    1.00 42.43  ? 238 ILE   C CB    1 
ATOM   5336  C  CG1   . ILE   B 1  238 ? -9.668  33.358  -0.745   1.00 33.81  ? 238 ILE   C CG1   1 
ATOM   5337  C  CG2   . ILE   B 1  238 ? -11.405 34.967  0.097    1.00 41.16  ? 238 ILE   C CG2   1 
ATOM   5338  C  CD1   . ILE   B 1  238 ? -8.677  32.356  -0.214   1.00 38.92  ? 238 ILE   C CD1   1 
ATOM   5339  N  N     . THR   B 1  239 ? -9.802  37.374  1.490    1.00 41.73  ? 239 THR   C N     1 
ATOM   5340  C  CA    . THR   B 1  239 ? -10.611 38.495  1.967    1.00 42.68  ? 239 THR   C CA    1 
ATOM   5341  C  C     . THR   B 1  239 ? -9.880  39.824  2.028    1.00 36.07  ? 239 THR   C C     1 
ATOM   5342  O  O     . THR   B 1  239 ? -10.527 40.842  2.258    1.00 39.03  ? 239 THR   C O     1 
ATOM   5343  C  CB    . THR   B 1  239 ? -11.153 38.205  3.355    1.00 41.30  ? 239 THR   C CB    1 
ATOM   5344  O  OG1   . THR   B 1  239 ? -10.051 37.898  4.214    1.00 45.97  ? 239 THR   C OG1   1 
ATOM   5345  C  CG2   . THR   B 1  239 ? -12.127 37.028  3.301    1.00 34.99  ? 239 THR   C CG2   1 
ATOM   5346  N  N     . ALA   B 1  240 ? -8.564  39.849  1.834    1.00 42.47  ? 240 ALA   C N     1 
ATOM   5347  C  CA    . ALA   B 1  240 ? -7.827  41.103  1.976    1.00 44.98  ? 240 ALA   C CA    1 
ATOM   5348  C  C     . ALA   B 1  240 ? -8.303  42.171  0.991    1.00 43.61  ? 240 ALA   C C     1 
ATOM   5349  O  O     . ALA   B 1  240 ? -8.189  43.369  1.275    1.00 44.44  ? 240 ALA   C O     1 
ATOM   5350  C  CB    . ALA   B 1  240 ? -6.331  40.845  1.800    1.00 37.39  ? 240 ALA   C CB    1 
ATOM   5351  N  N     . SER   B 1  241 ? -8.828  41.760  -0.169   1.00 43.76  ? 241 SER   C N     1 
ATOM   5352  C  CA    . SER   B 1  241 ? -9.284  42.718  -1.176   1.00 45.92  ? 241 SER   C CA    1 
ATOM   5353  C  C     . SER   B 1  241 ? -10.470 43.542  -0.676   1.00 49.74  ? 241 SER   C C     1 
ATOM   5354  O  O     . SER   B 1  241 ? -10.647 44.693  -1.096   1.00 44.78  ? 241 SER   C O     1 
ATOM   5355  C  CB    . SER   B 1  241 ? -9.654  41.977  -2.463   1.00 56.04  ? 241 SER   C CB    1 
ATOM   5356  O  OG    . SER   B 1  241 ? -8.915  40.763  -2.600   1.00 55.83  ? 241 SER   C OG    1 
ATOM   5357  N  N     . LEU   B 1  242 ? -11.287 42.974  0.222    1.00 36.73  ? 242 LEU   C N     1 
ATOM   5358  C  CA    . LEU   B 1  242 ? -12.419 43.675  0.814    1.00 35.17  ? 242 LEU   C CA    1 
ATOM   5359  C  C     . LEU   B 1  242 ? -12.042 44.480  2.042    1.00 47.89  ? 242 LEU   C C     1 
ATOM   5360  O  O     . LEU   B 1  242 ? -12.719 45.468  2.361    1.00 44.22  ? 242 LEU   C O     1 
ATOM   5361  C  CB    . LEU   B 1  242 ? -13.508 42.698  1.241    1.00 39.42  ? 242 LEU   C CB    1 
ATOM   5362  C  CG    . LEU   B 1  242 ? -13.949 41.618  0.283    1.00 30.55  ? 242 LEU   C CG    1 
ATOM   5363  C  CD1   . LEU   B 1  242 ? -12.818 40.662  0.027    1.00 42.74  ? 242 LEU   C CD1   1 
ATOM   5364  C  CD2   . LEU   B 1  242 ? -15.094 40.926  0.946    1.00 44.22  ? 242 LEU   C CD2   1 
ATOM   5365  N  N     . ARG   B 1  243 ? -10.997 44.057  2.755    1.00 48.73  ? 243 ARG   C N     1 
ATOM   5366  C  CA    . ARG   B 1  243 ? -10.569 44.737  3.963    1.00 43.62  ? 243 ARG   C CA    1 
ATOM   5367  C  C     . ARG   B 1  243 ? -9.585  45.869  3.687    1.00 44.39  ? 243 ARG   C C     1 
ATOM   5368  O  O     . ARG   B 1  243 ? -9.499  46.807  4.486    1.00 46.54  ? 243 ARG   C O     1 
ATOM   5369  C  CB    . ARG   B 1  243 ? -9.973  43.712  4.933    1.00 44.04  ? 243 ARG   C CB    1 
ATOM   5370  C  CG    . ARG   B 1  243 ? -10.981 42.626  5.336    1.00 39.08  ? 243 ARG   C CG    1 
ATOM   5371  C  CD    . ARG   B 1  243 ? -10.363 41.580  6.255    1.00 35.94  ? 243 ARG   C CD    1 
ATOM   5372  N  NE    . ARG   B 1  243 ? -9.381  40.756  5.558    1.00 35.69  ? 243 ARG   C NE    1 
ATOM   5373  C  CZ    . ARG   B 1  243 ? -8.070  40.824  5.743    1.00 36.07  ? 243 ARG   C CZ    1 
ATOM   5374  N  NH1   . ARG   B 1  243 ? -7.528  41.666  6.618    1.00 28.06  ? 243 ARG   C NH1   1 
ATOM   5375  N  NH2   . ARG   B 1  243 ? -7.281  40.026  5.035    1.00 38.29  ? 243 ARG   C NH2   1 
ATOM   5376  N  N     . PHE   B 1  244 ? -8.865  45.818  2.573    1.00 46.39  ? 244 PHE   C N     1 
ATOM   5377  C  CA    . PHE   B 1  244 ? -7.989  46.902  2.163    1.00 47.33  ? 244 PHE   C CA    1 
ATOM   5378  C  C     . PHE   B 1  244 ? -8.411  47.415  0.795    1.00 53.26  ? 244 PHE   C C     1 
ATOM   5379  O  O     . PHE   B 1  244 ? -9.155  46.759  0.061    1.00 64.13  ? 244 PHE   C O     1 
ATOM   5380  C  CB    . PHE   B 1  244 ? -6.531  46.446  2.122    1.00 38.14  ? 244 PHE   C CB    1 
ATOM   5381  C  CG    . PHE   B 1  244 ? -6.031  45.956  3.428    1.00 45.18  ? 244 PHE   C CG    1 
ATOM   5382  C  CD1   . PHE   B 1  244 ? -5.625  46.857  4.408    1.00 39.20  ? 244 PHE   C CD1   1 
ATOM   5383  C  CD2   . PHE   B 1  244 ? -5.973  44.595  3.695    1.00 41.94  ? 244 PHE   C CD2   1 
ATOM   5384  C  CE1   . PHE   B 1  244 ? -5.157  46.413  5.627    1.00 29.98  ? 244 PHE   C CE1   1 
ATOM   5385  C  CE2   . PHE   B 1  244 ? -5.503  44.140  4.919    1.00 40.84  ? 244 PHE   C CE2   1 
ATOM   5386  C  CZ    . PHE   B 1  244 ? -5.100  45.056  5.892    1.00 32.48  ? 244 PHE   C CZ    1 
ATOM   5387  N  N     . ASP   B 1  245 ? -7.936  48.602  0.455    1.00 44.30  ? 245 ASP   C N     1 
ATOM   5388  C  CA    . ASP   B 1  245 ? -8.146  49.158  -0.872   1.00 63.92  ? 245 ASP   C CA    1 
ATOM   5389  C  C     . ASP   B 1  245 ? -6.794  49.513  -1.479   1.00 63.88  ? 245 ASP   C C     1 
ATOM   5390  O  O     . ASP   B 1  245 ? -6.031  50.295  -0.904   1.00 57.08  ? 245 ASP   C O     1 
ATOM   5391  C  CB    . ASP   B 1  245 ? -9.075  50.374  -0.815   1.00 65.58  ? 245 ASP   C CB    1 
ATOM   5392  C  CG    . ASP   B 1  245 ? -10.496 50.038  -1.247   1.00 74.14  ? 245 ASP   C CG    1 
ATOM   5393  O  OD1   . ASP   B 1  245 ? -10.648 49.281  -2.242   1.00 60.60  ? 245 ASP   C OD1   1 
ATOM   5394  O  OD2   . ASP   B 1  245 ? -11.451 50.530  -0.590   1.00 72.60  ? 245 ASP   C OD2   1 
ATOM   5395  N  N     . GLY   B 1  246 ? -6.492  48.918  -2.622   1.00 64.21  ? 246 GLY   C N     1 
ATOM   5396  C  CA    . GLY   B 1  246 ? -5.309  49.294  -3.363   1.00 65.83  ? 246 GLY   C CA    1 
ATOM   5397  C  C     . GLY   B 1  246 ? -5.657  49.753  -4.764   1.00 60.52  ? 246 GLY   C C     1 
ATOM   5398  O  O     . GLY   B 1  246 ? -6.749  49.460  -5.264   1.00 58.41  ? 246 GLY   C O     1 
ATOM   5399  N  N     . ALA   B 1  247 ? -4.736  50.468  -5.417   1.00 63.72  ? 247 ALA   C N     1 
ATOM   5400  C  CA    . ALA   B 1  247 ? -4.985  50.879  -6.798   1.00 66.23  ? 247 ALA   C CA    1 
ATOM   5401  C  C     . ALA   B 1  247 ? -4.997  49.671  -7.741   1.00 61.25  ? 247 ALA   C C     1 
ATOM   5402  O  O     . ALA   B 1  247 ? -5.849  49.584  -8.637   1.00 55.14  ? 247 ALA   C O     1 
ATOM   5403  C  CB    . ALA   B 1  247 ? -3.947  51.919  -7.228   1.00 49.54  ? 247 ALA   C CB    1 
ATOM   5404  N  N     . LEU   B 1  248 ? -4.077  48.720  -7.539   1.00 46.55  ? 248 LEU   C N     1 
ATOM   5405  C  CA    . LEU   B 1  248 ? -4.061  47.459  -8.273   1.00 59.13  ? 248 LEU   C CA    1 
ATOM   5406  C  C     . LEU   B 1  248 ? -4.906  46.374  -7.604   1.00 48.51  ? 248 LEU   C C     1 
ATOM   5407  O  O     . LEU   B 1  248 ? -4.859  45.210  -8.024   1.00 49.30  ? 248 LEU   C O     1 
ATOM   5408  C  CB    . LEU   B 1  248 ? -2.614  46.989  -8.452   1.00 51.21  ? 248 LEU   C CB    1 
ATOM   5409  C  CG    . LEU   B 1  248 ? -1.876  48.048  -9.272   1.00 53.31  ? 248 LEU   C CG    1 
ATOM   5410  C  CD1   . LEU   B 1  248 ? -0.466  47.624  -9.571   1.00 48.80  ? 248 LEU   C CD1   1 
ATOM   5411  C  CD2   . LEU   B 1  248 ? -2.662  48.358  -10.576  1.00 49.31  ? 248 LEU   C CD2   1 
ATOM   5412  N  N     . ASN   B 1  249 ? -5.699  46.753  -6.608   1.00 51.37  ? 249 ASN   C N     1 
ATOM   5413  C  CA    . ASN   B 1  249 ? -6.484  45.837  -5.789   1.00 55.94  ? 249 ASN   C CA    1 
ATOM   5414  C  C     . ASN   B 1  249 ? -7.766  45.444  -6.530   1.00 51.67  ? 249 ASN   C C     1 
ATOM   5415  O  O     . ASN   B 1  249 ? -8.444  46.302  -7.104   1.00 58.27  ? 249 ASN   C O     1 
ATOM   5416  C  CB    . ASN   B 1  249 ? -6.758  46.552  -4.459   1.00 54.11  ? 249 ASN   C CB    1 
ATOM   5417  C  CG    . ASN   B 1  249 ? -7.605  45.764  -3.487   1.00 57.42  ? 249 ASN   C CG    1 
ATOM   5418  O  OD1   . ASN   B 1  249 ? -7.493  44.542  -3.366   1.00 59.89  ? 249 ASN   C OD1   1 
ATOM   5419  N  ND2   . ASN   B 1  249 ? -8.442  46.489  -2.744   1.00 52.54  ? 249 ASN   C ND2   1 
ATOM   5420  N  N     . VAL   B 1  250 ? -8.088  44.151  -6.544   1.00 45.94  ? 250 VAL   C N     1 
ATOM   5421  C  CA    . VAL   B 1  250 ? -9.226  43.625  -7.298   1.00 50.00  ? 250 VAL   C CA    1 
ATOM   5422  C  C     . VAL   B 1  250 ? -10.205 42.949  -6.341   1.00 51.06  ? 250 VAL   C C     1 
ATOM   5423  O  O     . VAL   B 1  250 ? -9.826  42.026  -5.607   1.00 64.10  ? 250 VAL   C O     1 
ATOM   5424  C  CB    . VAL   B 1  250 ? -8.776  42.645  -8.395   1.00 58.30  ? 250 VAL   C CB    1 
ATOM   5425  C  CG1   . VAL   B 1  250 ? -9.994  42.139  -9.192   1.00 55.22  ? 250 VAL   C CG1   1 
ATOM   5426  C  CG2   . VAL   B 1  250 ? -7.727  43.301  -9.311   1.00 38.95  ? 250 VAL   C CG2   1 
ATOM   5427  N  N     . ASP   B 1  251 ? -11.467 43.392  -6.368   1.00 56.99  ? 251 ASP   C N     1 
ATOM   5428  C  CA    . ASP   B 1  251 ? -12.498 42.858  -5.469   1.00 70.97  ? 251 ASP   C CA    1 
ATOM   5429  C  C     . ASP   B 1  251 ? -12.654 41.346  -5.642   1.00 54.84  ? 251 ASP   C C     1 
ATOM   5430  O  O     . ASP   B 1  251 ? -12.672 40.837  -6.770   1.00 52.89  ? 251 ASP   C O     1 
ATOM   5431  C  CB    . ASP   B 1  251 ? -13.849 43.563  -5.730   1.00 69.23  ? 251 ASP   C CB    1 
ATOM   5432  C  CG    . ASP   B 1  251 ? -14.413 44.281  -4.484   1.00 76.65  ? 251 ASP   C CG    1 
ATOM   5433  O  OD1   . ASP   B 1  251 ? -13.615 44.848  -3.695   1.00 62.73  ? 251 ASP   C OD1   1 
ATOM   5434  O  OD2   . ASP   B 1  251 ? -15.661 44.299  -4.308   1.00 75.74  ? 251 ASP   C OD2   1 
ATOM   5435  N  N     . LEU   B 1  252 ? -12.783 40.624  -4.512   1.00 47.07  ? 252 LEU   C N     1 
ATOM   5436  C  CA    . LEU   B 1  252 ? -12.966 39.174  -4.579   1.00 46.23  ? 252 LEU   C CA    1 
ATOM   5437  C  C     . LEU   B 1  252 ? -14.203 38.776  -5.379   1.00 43.58  ? 252 LEU   C C     1 
ATOM   5438  O  O     . LEU   B 1  252 ? -14.239 37.670  -5.929   1.00 36.68  ? 252 LEU   C O     1 
ATOM   5439  C  CB    . LEU   B 1  252 ? -13.054 38.552  -3.190   1.00 44.87  ? 252 LEU   C CB    1 
ATOM   5440  C  CG    . LEU   B 1  252 ? -13.536 37.070  -3.200   1.00 52.24  ? 252 LEU   C CG    1 
ATOM   5441  C  CD1   . LEU   B 1  252 ? -12.778 36.128  -4.173   1.00 47.50  ? 252 LEU   C CD1   1 
ATOM   5442  C  CD2   . LEU   B 1  252 ? -13.513 36.466  -1.807   1.00 37.94  ? 252 LEU   C CD2   1 
ATOM   5443  N  N     . THR   B 1  253 ? -15.221 39.647  -5.448   1.00 50.18  ? 253 THR   C N     1 
ATOM   5444  C  CA    . THR   B 1  253 ? -16.364 39.400  -6.326   1.00 40.33  ? 253 THR   C CA    1 
ATOM   5445  C  C     . THR   B 1  253 ? -15.909 39.217  -7.760   1.00 38.44  ? 253 THR   C C     1 
ATOM   5446  O  O     . THR   B 1  253 ? -16.162 38.181  -8.381   1.00 39.70  ? 253 THR   C O     1 
ATOM   5447  C  CB    . THR   B 1  253 ? -17.373 40.550  -6.270   1.00 52.34  ? 253 THR   C CB    1 
ATOM   5448  O  OG1   . THR   B 1  253 ? -18.069 40.552  -5.015   1.00 28.77  ? 253 THR   C OG1   1 
ATOM   5449  C  CG2   . THR   B 1  253 ? -18.390 40.401  -7.451   1.00 45.61  ? 253 THR   C CG2   1 
ATOM   5450  N  N     . GLU   B 1  254 ? -15.264 40.248  -8.309   1.00 45.35  ? 254 GLU   C N     1 
ATOM   5451  C  CA    . GLU   B 1  254 ? -14.637 40.187  -9.625   1.00 49.17  ? 254 GLU   C CA    1 
ATOM   5452  C  C     . GLU   B 1  254 ? -13.934 38.859  -9.890   1.00 51.90  ? 254 GLU   C C     1 
ATOM   5453  O  O     . GLU   B 1  254 ? -14.150 38.228  -10.934  1.00 43.18  ? 254 GLU   C O     1 
ATOM   5454  C  CB    . GLU   B 1  254 ? -13.640 41.341  -9.765   1.00 53.01  ? 254 GLU   C CB    1 
ATOM   5455  C  CG    . GLU   B 1  254 ? -14.276 42.669  -10.115  1.00 59.59  ? 254 GLU   C CG    1 
ATOM   5456  C  CD    . GLU   B 1  254 ? -13.250 43.772  -10.226  1.00 68.49  ? 254 GLU   C CD    1 
ATOM   5457  O  OE1   . GLU   B 1  254 ? -12.492 43.966  -9.240   1.00 62.75  ? 254 GLU   C OE1   1 
ATOM   5458  O  OE2   . GLU   B 1  254 ? -13.197 44.425  -11.298  1.00 57.08  ? 254 GLU   C OE2   1 
ATOM   5459  N  N     . PHE   B 1  255 ? -13.056 38.433  -8.965   1.00 47.75  ? 255 PHE   C N     1 
ATOM   5460  C  CA    . PHE   B 1  255 ? -12.468 37.102  -9.090   1.00 39.20  ? 255 PHE   C CA    1 
ATOM   5461  C  C     . PHE   B 1  255 ? -13.550 36.026  -9.128   1.00 36.59  ? 255 PHE   C C     1 
ATOM   5462  O  O     . PHE   B 1  255 ? -13.377 35.018  -9.819   1.00 37.05  ? 255 PHE   C O     1 
ATOM   5463  C  CB    . PHE   B 1  255 ? -11.471 36.826  -7.950   1.00 50.22  ? 255 PHE   C CB    1 
ATOM   5464  C  CG    . PHE   B 1  255 ? -10.171 37.614  -8.053   1.00 45.88  ? 255 PHE   C CG    1 
ATOM   5465  C  CD1   . PHE   B 1  255 ? -9.146  37.192  -8.896   1.00 49.99  ? 255 PHE   C CD1   1 
ATOM   5466  C  CD2   . PHE   B 1  255 ? -9.975  38.763  -7.303   1.00 38.71  ? 255 PHE   C CD2   1 
ATOM   5467  C  CE1   . PHE   B 1  255 ? -7.942  37.908  -9.006   1.00 38.27  ? 255 PHE   C CE1   1 
ATOM   5468  C  CE2   . PHE   B 1  255 ? -8.784  39.479  -7.404   1.00 54.54  ? 255 PHE   C CE2   1 
ATOM   5469  C  CZ    . PHE   B 1  255 ? -7.761  39.044  -8.263   1.00 42.39  ? 255 PHE   C CZ    1 
ATOM   5470  N  N     . GLN   B 1  256 ? -14.685 36.231  -8.429   1.00 31.18  ? 256 GLN   C N     1 
ATOM   5471  C  CA    . GLN   B 1  256 ? -15.739 35.211  -8.400   1.00 34.98  ? 256 GLN   C CA    1 
ATOM   5472  C  C     . GLN   B 1  256 ? -16.404 35.029  -9.770   1.00 33.92  ? 256 GLN   C C     1 
ATOM   5473  O  O     . GLN   B 1  256 ? -16.660 33.895  -10.202  1.00 24.28  ? 256 GLN   C O     1 
ATOM   5474  C  CB    . GLN   B 1  256 ? -16.787 35.554  -7.346   1.00 27.38  ? 256 GLN   C CB    1 
ATOM   5475  C  CG    . GLN   B 1  256 ? -17.859 34.461  -7.171   1.00 33.04  ? 256 GLN   C CG    1 
ATOM   5476  C  CD    . GLN   B 1  256 ? -18.845 34.707  -5.985   1.00 46.09  ? 256 GLN   C CD    1 
ATOM   5477  O  OE1   . GLN   B 1  256 ? -18.476 35.307  -4.962   1.00 38.28  ? 256 GLN   C OE1   1 
ATOM   5478  N  NE2   . GLN   B 1  256 ? -20.100 34.240  -6.136   1.00 30.25  ? 256 GLN   C NE2   1 
ATOM   5479  N  N     . THR   B 1  257 ? -16.713 36.128  -10.460  1.00 27.91  ? 257 THR   C N     1 
ATOM   5480  C  CA    . THR   B 1  257 ? -17.234 36.010  -11.811  1.00 29.07  ? 257 THR   C CA    1 
ATOM   5481  C  C     . THR   B 1  257 ? -16.347 35.110  -12.653  1.00 29.58  ? 257 THR   C C     1 
ATOM   5482  O  O     . THR   B 1  257 ? -16.830 34.227  -13.371  1.00 27.70  ? 257 THR   C O     1 
ATOM   5483  C  CB    . THR   B 1  257 ? -17.344 37.386  -12.440  1.00 33.70  ? 257 THR   C CB    1 
ATOM   5484  O  OG1   . THR   B 1  257 ? -18.246 38.176  -11.650  1.00 45.87  ? 257 THR   C OG1   1 
ATOM   5485  C  CG2   . THR   B 1  257 ? -17.838 37.265  -13.889  1.00 22.06  ? 257 THR   C CG2   1 
ATOM   5486  N  N     . ASN   B 1  258 ? -15.034 35.314  -12.564  1.00 28.17  ? 258 ASN   C N     1 
ATOM   5487  C  CA    . ASN   B 1  258 ? -14.112 34.496  -13.333  1.00 30.60  ? 258 ASN   C CA    1 
ATOM   5488  C  C     . ASN   B 1  258 ? -14.011 33.067  -12.821  1.00 25.00  ? 258 ASN   C C     1 
ATOM   5489  O  O     . ASN   B 1  258 ? -13.696 32.175  -13.608  1.00 27.93  ? 258 ASN   C O     1 
ATOM   5490  C  CB    . ASN   B 1  258 ? -12.736 35.156  -13.349  1.00 36.23  ? 258 ASN   C CB    1 
ATOM   5491  C  CG    . ASN   B 1  258 ? -12.516 36.007  -14.594  1.00 32.83  ? 258 ASN   C CG    1 
ATOM   5492  O  OD1   . ASN   B 1  258 ? -13.457 36.567  -15.165  1.00 33.96  ? 258 ASN   C OD1   1 
ATOM   5493  N  ND2   . ASN   B 1  258 ? -11.284 36.074  -15.038  1.00 27.77  ? 258 ASN   C ND2   1 
ATOM   5494  N  N     . LEU   B 1  259 ? -14.302 32.826  -11.542  1.00 29.20  ? 259 LEU   C N     1 
ATOM   5495  C  CA    . LEU   B 1  259 ? -14.096 31.522  -10.914  1.00 28.38  ? 259 LEU   C CA    1 
ATOM   5496  C  C     . LEU   B 1  259 ? -15.261 30.557  -11.091  1.00 26.54  ? 259 LEU   C C     1 
ATOM   5497  O  O     . LEU   B 1  259 ? -15.067 29.345  -10.950  1.00 30.56  ? 259 LEU   C O     1 
ATOM   5498  C  CB    . LEU   B 1  259 ? -13.817 31.703  -9.416   1.00 27.61  ? 259 LEU   C CB    1 
ATOM   5499  C  CG    . LEU   B 1  259 ? -12.415 32.228  -9.090   1.00 24.35  ? 259 LEU   C CG    1 
ATOM   5500  C  CD1   . LEU   B 1  259 ? -12.262 32.674  -7.646   1.00 19.81  ? 259 LEU   C CD1   1 
ATOM   5501  C  CD2   . LEU   B 1  259 ? -11.399 31.161  -9.451   1.00 25.23  ? 259 LEU   C CD2   1 
ATOM   5502  N  N     . VAL   B 1  260 ? -16.452 31.044  -11.415  1.00 23.64  ? 260 VAL   C N     1 
ATOM   5503  C  CA    . VAL   B 1  260 ? -17.643 30.191  -11.383  1.00 28.16  ? 260 VAL   C CA    1 
ATOM   5504  C  C     . VAL   B 1  260 ? -18.321 30.183  -12.747  1.00 23.30  ? 260 VAL   C C     1 
ATOM   5505  O  O     . VAL   B 1  260 ? -19.127 31.084  -13.026  1.00 28.58  ? 260 VAL   C O     1 
ATOM   5506  C  CB    . VAL   B 1  260 ? -18.626 30.662  -10.292  1.00 27.00  ? 260 VAL   C CB    1 
ATOM   5507  C  CG1   . VAL   B 1  260 ? -19.877 29.826  -10.331  1.00 19.01  ? 260 VAL   C CG1   1 
ATOM   5508  C  CG2   . VAL   B 1  260 ? -17.960 30.596  -8.925   1.00 15.94  ? 260 VAL   C CG2   1 
ATOM   5509  N  N     . PRO   B 1  261 ? -18.008 29.222  -13.642  1.00 23.65  ? 261 PRO   C N     1 
ATOM   5510  C  CA    . PRO   B 1  261 ? -18.601 29.243  -14.994  1.00 22.42  ? 261 PRO   C CA    1 
ATOM   5511  C  C     . PRO   B 1  261 ? -20.041 28.754  -15.020  1.00 26.67  ? 261 PRO   C C     1 
ATOM   5512  O  O     . PRO   B 1  261 ? -20.825 29.151  -15.886  1.00 33.06  ? 261 PRO   C O     1 
ATOM   5513  C  CB    . PRO   B 1  261 ? -17.689 28.303  -15.792  1.00 16.98  ? 261 PRO   C CB    1 
ATOM   5514  C  CG    . PRO   B 1  261 ? -17.164 27.363  -14.785  1.00 16.53  ? 261 PRO   C CG    1 
ATOM   5515  C  CD    . PRO   B 1  261 ? -16.969 28.186  -13.526  1.00 22.17  ? 261 PRO   C CD    1 
ATOM   5516  N  N     . TYR   B 1  262 ? -20.384 27.868  -14.093  1.00 25.09  ? 262 TYR   C N     1 
ATOM   5517  C  CA    . TYR   B 1  262 ? -21.723 27.324  -13.917  1.00 23.66  ? 262 TYR   C CA    1 
ATOM   5518  C  C     . TYR   B 1  262 ? -22.058 27.296  -12.430  1.00 25.75  ? 262 TYR   C C     1 
ATOM   5519  O  O     . TYR   B 1  262 ? -21.159 27.144  -11.590  1.00 27.37  ? 262 TYR   C O     1 
ATOM   5520  C  CB    . TYR   B 1  262 ? -21.812 25.921  -14.521  1.00 21.18  ? 262 TYR   C CB    1 
ATOM   5521  C  CG    . TYR   B 1  262 ? -21.393 25.874  -15.973  1.00 27.39  ? 262 TYR   C CG    1 
ATOM   5522  C  CD1   . TYR   B 1  262 ? -22.307 26.087  -16.989  1.00 21.46  ? 262 TYR   C CD1   1 
ATOM   5523  C  CD2   . TYR   B 1  262 ? -20.071 25.628  -16.327  1.00 29.69  ? 262 TYR   C CD2   1 
ATOM   5524  C  CE1   . TYR   B 1  262 ? -21.908 26.048  -18.316  1.00 22.94  ? 262 TYR   C CE1   1 
ATOM   5525  C  CE2   . TYR   B 1  262 ? -19.669 25.583  -17.649  1.00 22.33  ? 262 TYR   C CE2   1 
ATOM   5526  C  CZ    . TYR   B 1  262 ? -20.594 25.791  -18.631  1.00 23.61  ? 262 TYR   C CZ    1 
ATOM   5527  O  OH    . TYR   B 1  262 ? -20.192 25.765  -19.932  1.00 26.50  ? 262 TYR   C OH    1 
ATOM   5528  N  N     . PRO   B 1  263 ? -23.325 27.465  -12.067  1.00 20.55  ? 263 PRO   C N     1 
ATOM   5529  C  CA    . PRO   B 1  263 ? -23.643 27.517  -10.627  1.00 18.46  ? 263 PRO   C CA    1 
ATOM   5530  C  C     . PRO   B 1  263 ? -23.052 26.355  -9.823   1.00 19.44  ? 263 PRO   C C     1 
ATOM   5531  O  O     . PRO   B 1  263 ? -22.520 26.600  -8.736   1.00 22.25  ? 263 PRO   C O     1 
ATOM   5532  C  CB    . PRO   B 1  263 ? -25.193 27.540  -10.609  1.00 14.22  ? 263 PRO   C CB    1 
ATOM   5533  C  CG    . PRO   B 1  263 ? -25.551 28.212  -11.872  1.00 16.57  ? 263 PRO   C CG    1 
ATOM   5534  C  CD    . PRO   B 1  263 ? -24.523 27.677  -12.895  1.00 17.44  ? 263 PRO   C CD    1 
ATOM   5535  N  N     . ARG   B 1  264 ? -23.096 25.105  -10.322  1.00 22.50  ? 264 ARG   C N     1 
ATOM   5536  C  CA    . ARG   B 1  264 ? -22.597 23.982  -9.529   1.00 20.46  ? 264 ARG   C CA    1 
ATOM   5537  C  C     . ARG   B 1  264 ? -21.064 23.879  -9.503   1.00 30.27  ? 264 ARG   C C     1 
ATOM   5538  O  O     . ARG   B 1  264 ? -20.515 23.307  -8.543   1.00 24.67  ? 264 ARG   C O     1 
ATOM   5539  C  CB    . ARG   B 1  264 ? -23.210 22.676  -10.027  1.00 14.93  ? 264 ARG   C CB    1 
ATOM   5540  C  CG    . ARG   B 1  264 ? -24.702 22.556  -9.738   1.00 14.53  ? 264 ARG   C CG    1 
ATOM   5541  C  CD    . ARG   B 1  264 ? -25.364 21.434  -10.557  1.00 10.53  ? 264 ARG   C CD    1 
ATOM   5542  N  NE    . ARG   B 1  264 ? -24.740 20.122  -10.340  1.00 20.52  ? 264 ARG   C NE    1 
ATOM   5543  C  CZ    . ARG   B 1  264 ? -25.126 19.240  -9.416   1.00 27.36  ? 264 ARG   C CZ    1 
ATOM   5544  N  NH1   . ARG   B 1  264 ? -26.086 19.525  -8.546   1.00 24.72  ? 264 ARG   C NH1   1 
ATOM   5545  N  NH2   . ARG   B 1  264 ? -24.548 18.036  -9.373   1.00 21.36  ? 264 ARG   C NH2   1 
ATOM   5546  N  N     . ILE   B 1  265 ? -20.370 24.424  -10.516  1.00 25.23  ? 265 ILE   C N     1 
ATOM   5547  C  CA    . ILE   B 1  265 ? -18.912 24.384  -10.616  1.00 22.97  ? 265 ILE   C CA    1 
ATOM   5548  C  C     . ILE   B 1  265 ? -18.320 25.591  -9.881   1.00 22.39  ? 265 ILE   C C     1 
ATOM   5549  O  O     . ILE   B 1  265 ? -17.763 26.502  -10.505  1.00 21.77  ? 265 ILE   C O     1 
ATOM   5550  C  CB    . ILE   B 1  265 ? -18.459 24.360  -12.097  1.00 25.38  ? 265 ILE   C CB    1 
ATOM   5551  C  CG1   . ILE   B 1  265 ? -19.120 23.203  -12.869  1.00 21.50  ? 265 ILE   C CG1   1 
ATOM   5552  C  CG2   . ILE   B 1  265 ? -16.919 24.312  -12.221  1.00 22.84  ? 265 ILE   C CG2   1 
ATOM   5553  C  CD1   . ILE   B 1  265 ? -18.825 21.831  -12.276  1.00 24.73  ? 265 ILE   C CD1   1 
ATOM   5554  N  N     . HIS   B 1  266 ? -18.408 25.604  -8.556   1.00 16.74  ? 266 HIS   C N     1 
ATOM   5555  C  CA    . HIS   B 1  266 ? -18.096 26.789  -7.769   1.00 18.64  ? 266 HIS   C CA    1 
ATOM   5556  C  C     . HIS   B 1  266 ? -17.154 26.456  -6.615   1.00 21.36  ? 266 HIS   C C     1 
ATOM   5557  O  O     . HIS   B 1  266 ? -17.290 26.981  -5.502   1.00 24.46  ? 266 HIS   C O     1 
ATOM   5558  C  CB    . HIS   B 1  266 ? -19.377 27.451  -7.261   1.00 19.51  ? 266 HIS   C CB    1 
ATOM   5559  C  CG    . HIS   B 1  266 ? -20.141 26.636  -6.244   1.00 27.74  ? 266 HIS   C CG    1 
ATOM   5560  N  ND1   . HIS   B 1  266 ? -19.558 26.094  -5.113   1.00 27.69  ? 266 HIS   C ND1   1 
ATOM   5561  C  CD2   . HIS   B 1  266 ? -21.455 26.311  -6.174   1.00 20.20  ? 266 HIS   C CD2   1 
ATOM   5562  C  CE1   . HIS   B 1  266 ? -20.481 25.468  -4.401   1.00 29.08  ? 266 HIS   C CE1   1 
ATOM   5563  N  NE2   . HIS   B 1  266 ? -21.637 25.575  -5.031   1.00 17.90  ? 266 HIS   C NE2   1 
ATOM   5564  N  N     . PHE   B 1  267 ? -16.184 25.578  -6.869   1.00 17.86  ? 267 PHE   C N     1 
ATOM   5565  C  CA    . PHE   B 1  267 ? -15.251 25.059  -5.869   1.00 21.56  ? 267 PHE   C CA    1 
ATOM   5566  C  C     . PHE   B 1  267 ? -13.811 25.328  -6.312   1.00 20.43  ? 267 PHE   C C     1 
ATOM   5567  O  O     . PHE   B 1  267 ? -13.172 24.443  -6.897   1.00 19.93  ? 267 PHE   C O     1 
ATOM   5568  C  CB    . PHE   B 1  267 ? -15.441 23.553  -5.686   1.00 13.81  ? 267 PHE   C CB    1 
ATOM   5569  C  CG    . PHE   B 1  267 ? -16.753 23.168  -5.126   1.00 19.20  ? 267 PHE   C CG    1 
ATOM   5570  C  CD1   . PHE   B 1  267 ? -16.937 23.068  -3.747   1.00 22.40  ? 267 PHE   C CD1   1 
ATOM   5571  C  CD2   . PHE   B 1  267 ? -17.812 22.868  -5.962   1.00 21.74  ? 267 PHE   C CD2   1 
ATOM   5572  C  CE1   . PHE   B 1  267 ? -18.157 22.674  -3.206   1.00 14.58  ? 267 PHE   C CE1   1 
ATOM   5573  C  CE2   . PHE   B 1  267 ? -19.038 22.498  -5.431   1.00 24.62  ? 267 PHE   C CE2   1 
ATOM   5574  C  CZ    . PHE   B 1  267 ? -19.208 22.396  -4.044   1.00 17.86  ? 267 PHE   C CZ    1 
ATOM   5575  N  N     . PRO   B 1  268 ? -13.268 26.519  -6.057   1.00 17.67  ? 268 PRO   C N     1 
ATOM   5576  C  CA    . PRO   B 1  268 ? -11.912 26.822  -6.532   1.00 20.11  ? 268 PRO   C CA    1 
ATOM   5577  C  C     . PRO   B 1  268 ? -10.872 26.157  -5.650   1.00 22.64  ? 268 PRO   C C     1 
ATOM   5578  O  O     . PRO   B 1  268 ? -11.031 26.085  -4.434   1.00 32.90  ? 268 PRO   C O     1 
ATOM   5579  C  CB    . PRO   B 1  268 ? -11.819 28.354  -6.425   1.00 21.22  ? 268 PRO   C CB    1 
ATOM   5580  C  CG    . PRO   B 1  268 ? -13.176 28.828  -6.002   1.00 20.88  ? 268 PRO   C CG    1 
ATOM   5581  C  CD    . PRO   B 1  268 ? -13.847 27.662  -5.336   1.00 20.05  ? 268 PRO   C CD    1 
ATOM   5582  N  N     . LEU   B 1  269 ? -9.805  25.667  -6.280   1.00 21.94  ? 269 LEU   C N     1 
ATOM   5583  C  CA    . LEU   B 1  269 ? -8.659  25.123  -5.567   1.00 21.46  ? 269 LEU   C CA    1 
ATOM   5584  C  C     . LEU   B 1  269 ? -7.752  26.272  -5.156   1.00 24.59  ? 269 LEU   C C     1 
ATOM   5585  O  O     . LEU   B 1  269 ? -7.501  27.171  -5.950   1.00 32.51  ? 269 LEU   C O     1 
ATOM   5586  C  CB    . LEU   B 1  269 ? -7.908  24.145  -6.460   1.00 24.58  ? 269 LEU   C CB    1 
ATOM   5587  C  CG    . LEU   B 1  269 ? -6.602  23.563  -5.939   1.00 31.61  ? 269 LEU   C CG    1 
ATOM   5588  C  CD1   . LEU   B 1  269 ? -6.862  22.736  -4.699   1.00 30.94  ? 269 LEU   C CD1   1 
ATOM   5589  C  CD2   . LEU   B 1  269 ? -5.953  22.709  -7.031   1.00 22.91  ? 269 LEU   C CD2   1 
ATOM   5590  N  N     . ALA   B 1  270 ? -7.307  26.290  -3.907   1.00 27.80  ? 270 ALA   C N     1 
ATOM   5591  C  CA    . ALA   B 1  270 ? -6.479  27.389  -3.440   1.00 23.56  ? 270 ALA   C CA    1 
ATOM   5592  C  C     . ALA   B 1  270 ? -5.060  26.887  -3.265   1.00 27.57  ? 270 ALA   C C     1 
ATOM   5593  O  O     . ALA   B 1  270 ? -4.833  25.702  -3.019   1.00 29.97  ? 270 ALA   C O     1 
ATOM   5594  C  CB    . ALA   B 1  270 ? -6.990  27.985  -2.122   1.00 23.36  ? 270 ALA   C CB    1 
ATOM   5595  N  N     . THR   B 1  271 ? -4.108  27.796  -3.432   1.00 23.28  ? 271 THR   C N     1 
ATOM   5596  C  CA    . THR   B 1  271 ? -2.693  27.503  -3.260   1.00 27.67  ? 271 THR   C CA    1 
ATOM   5597  C  C     . THR   B 1  271 ? -2.041  28.752  -2.690   1.00 32.96  ? 271 THR   C C     1 
ATOM   5598  O  O     . THR   B 1  271 ? -2.407  29.867  -3.066   1.00 37.42  ? 271 THR   C O     1 
ATOM   5599  C  CB    . THR   B 1  271 ? -1.978  27.124  -4.567   1.00 31.60  ? 271 THR   C CB    1 
ATOM   5600  O  OG1   . THR   B 1  271 ? -2.704  26.108  -5.283   1.00 38.33  ? 271 THR   C OG1   1 
ATOM   5601  C  CG2   . THR   B 1  271 ? -0.611  26.577  -4.227   1.00 41.74  ? 271 THR   C CG2   1 
ATOM   5602  N  N     . TYR   B 1  272 ? -1.072  28.568  -1.801   1.00 26.45  ? 272 TYR   C N     1 
ATOM   5603  C  CA    . TYR   B 1  272 ? -0.508  29.692  -1.071   1.00 26.65  ? 272 TYR   C CA    1 
ATOM   5604  C  C     . TYR   B 1  272 ? 1.003   29.538  -1.016   1.00 31.20  ? 272 TYR   C C     1 
ATOM   5605  O  O     . TYR   B 1  272 ? 1.502   28.452  -0.709   1.00 41.28  ? 272 TYR   C O     1 
ATOM   5606  C  CB    . TYR   B 1  272 ? -1.085  29.789  0.352    1.00 28.34  ? 272 TYR   C CB    1 
ATOM   5607  C  CG    . TYR   B 1  272 ? -0.555  30.992  1.095    1.00 27.79  ? 272 TYR   C CG    1 
ATOM   5608  C  CD1   . TYR   B 1  272 ? -1.120  32.234  0.917    1.00 22.57  ? 272 TYR   C CD1   1 
ATOM   5609  C  CD2   . TYR   B 1  272 ? 0.538   30.882  1.946    1.00 27.86  ? 272 TYR   C CD2   1 
ATOM   5610  C  CE1   . TYR   B 1  272 ? -0.629  33.326  1.568    1.00 30.79  ? 272 TYR   C CE1   1 
ATOM   5611  C  CE2   . TYR   B 1  272 ? 1.042   31.978  2.604    1.00 24.91  ? 272 TYR   C CE2   1 
ATOM   5612  C  CZ    . TYR   B 1  272 ? 0.460   33.196  2.405    1.00 27.94  ? 272 TYR   C CZ    1 
ATOM   5613  O  OH    . TYR   B 1  272 ? 0.947   34.302  3.053    1.00 39.40  ? 272 TYR   C OH    1 
ATOM   5614  N  N     . ALA   B 1  273 ? 1.730   30.612  -1.313   1.00 28.68  ? 273 ALA   C N     1 
ATOM   5615  C  CA    . ALA   B 1  273 ? 3.172   30.607  -1.108   1.00 29.54  ? 273 ALA   C CA    1 
ATOM   5616  C  C     . ALA   B 1  273 ? 3.587   32.003  -0.700   1.00 29.32  ? 273 ALA   C C     1 
ATOM   5617  O  O     . ALA   B 1  273 ? 2.908   32.971  -1.049   1.00 38.17  ? 273 ALA   C O     1 
ATOM   5618  C  CB    . ALA   B 1  273 ? 3.942   30.174  -2.362   1.00 18.62  ? 273 ALA   C CB    1 
ATOM   5619  N  N     . PRO   B 1  274 ? 4.685   32.142  0.027    1.00 31.52  ? 274 PRO   C N     1 
ATOM   5620  C  CA    . PRO   B 1  274 ? 5.539   31.069  0.537    1.00 33.11  ? 274 PRO   C CA    1 
ATOM   5621  C  C     . PRO   B 1  274 ? 5.071   30.614  1.912    1.00 30.11  ? 274 PRO   C C     1 
ATOM   5622  O  O     . PRO   B 1  274 ? 4.682   31.429  2.756    1.00 34.14  ? 274 PRO   C O     1 
ATOM   5623  C  CB    . PRO   B 1  274 ? 6.920   31.737  0.583    1.00 27.36  ? 274 PRO   C CB    1 
ATOM   5624  C  CG    . PRO   B 1  274 ? 6.576   33.149  1.024    1.00 36.89  ? 274 PRO   C CG    1 
ATOM   5625  C  CD    . PRO   B 1  274 ? 5.239   33.469  0.344    1.00 30.59  ? 274 PRO   C CD    1 
ATOM   5626  N  N     . VAL   B 1  275 ? 5.070   29.304  2.130    1.00 31.19  ? 275 VAL   C N     1 
ATOM   5627  C  CA    . VAL   B 1  275 ? 4.961   28.711  3.455    1.00 27.97  ? 275 VAL   C CA    1 
ATOM   5628  C  C     . VAL   B 1  275 ? 6.356   28.229  3.802    1.00 27.30  ? 275 VAL   C C     1 
ATOM   5629  O  O     . VAL   B 1  275 ? 6.844   27.252  3.223    1.00 28.78  ? 275 VAL   C O     1 
ATOM   5630  C  CB    . VAL   B 1  275 ? 3.946   27.562  3.511    1.00 26.63  ? 275 VAL   C CB    1 
ATOM   5631  C  CG1   . VAL   B 1  275 ? 3.784   27.085  4.960    1.00 21.85  ? 275 VAL   C CG1   1 
ATOM   5632  C  CG2   . VAL   B 1  275 ? 2.610   27.999  2.938    1.00 28.43  ? 275 VAL   C CG2   1 
ATOM   5633  N  N     . ILE   B 1  276 ? 6.990   28.913  4.754    1.00 24.29  ? 276 ILE   C N     1 
ATOM   5634  C  CA    . ILE   B 1  276 ? 8.413   28.754  5.001    1.00 27.49  ? 276 ILE   C CA    1 
ATOM   5635  C  C     . ILE   B 1  276 ? 8.670   29.151  6.442    1.00 28.33  ? 276 ILE   C C     1 
ATOM   5636  O  O     . ILE   B 1  276 ? 8.000   30.027  6.981    1.00 36.89  ? 276 ILE   C O     1 
ATOM   5637  C  CB    . ILE   B 1  276 ? 9.229   29.613  4.003    1.00 31.79  ? 276 ILE   C CB    1 
ATOM   5638  C  CG1   . ILE   B 1  276 ? 10.546  28.937  3.633    1.00 41.12  ? 276 ILE   C CG1   1 
ATOM   5639  C  CG2   . ILE   B 1  276 ? 9.484   30.984  4.577    1.00 30.77  ? 276 ILE   C CG2   1 
ATOM   5640  C  CD1   . ILE   B 1  276 ? 11.582  29.906  3.050    1.00 46.08  ? 276 ILE   C CD1   1 
ATOM   5641  N  N     . SER   B 1  277 ? 9.640   28.501  7.073    1.00 43.92  ? 277 SER   C N     1 
ATOM   5642  C  CA    . SER   B 1  277 ? 10.014  28.841  8.448    1.00 36.91  ? 277 SER   C CA    1 
ATOM   5643  C  C     . SER   B 1  277 ? 10.893  30.089  8.504    1.00 30.41  ? 277 SER   C C     1 
ATOM   5644  O  O     . SER   B 1  277 ? 11.618  30.407  7.558    1.00 32.81  ? 277 SER   C O     1 
ATOM   5645  C  CB    . SER   B 1  277 ? 10.786  27.696  9.081    1.00 41.76  ? 277 SER   C CB    1 
ATOM   5646  O  OG    . SER   B 1  277 ? 12.064  27.622  8.460    1.00 42.69  ? 277 SER   C OG    1 
ATOM   5647  N  N     . ALA   B 1  278 ? 10.841  30.786  9.640    1.00 36.32  ? 278 ALA   C N     1 
ATOM   5648  C  CA    . ALA   B 1  278 ? 11.848  31.809  9.922    1.00 35.88  ? 278 ALA   C CA    1 
ATOM   5649  C  C     . ALA   B 1  278 ? 13.269  31.279  9.702    1.00 35.39  ? 278 ALA   C C     1 
ATOM   5650  O  O     . ALA   B 1  278 ? 14.102  31.947  9.081    1.00 34.70  ? 278 ALA   C O     1 
ATOM   5651  C  CB    . ALA   B 1  278 ? 11.676  32.318  11.350   1.00 22.64  ? 278 ALA   C CB    1 
ATOM   5652  N  N     . GLU   B 1  279 ? 13.551  30.062  10.169   1.00 31.76  ? 279 GLU   C N     1 
ATOM   5653  C  CA    . GLU   B 1  279 ? 14.886  29.487  10.008   1.00 37.46  ? 279 GLU   C CA    1 
ATOM   5654  C  C     . GLU   B 1  279 ? 15.294  29.389  8.538    1.00 44.29  ? 279 GLU   C C     1 
ATOM   5655  O  O     . GLU   B 1  279 ? 16.437  29.706  8.184    1.00 45.57  ? 279 GLU   C O     1 
ATOM   5656  C  CB    . GLU   B 1  279 ? 14.954  28.099  10.664   1.00 51.45  ? 279 GLU   C CB    1 
ATOM   5657  C  CG    . GLU   B 1  279 ? 14.967  28.062  12.187   1.00 36.28  ? 279 GLU   C CG    1 
ATOM   5658  C  CD    . GLU   B 1  279 ? 13.587  28.165  12.803   1.00 45.03  ? 279 GLU   C CD    1 
ATOM   5659  O  OE1   . GLU   B 1  279 ? 12.597  27.844  12.114   1.00 43.71  ? 279 GLU   C OE1   1 
ATOM   5660  O  OE2   . GLU   B 1  279 ? 13.495  28.568  13.987   1.00 52.59  ? 279 GLU   C OE2   1 
ATOM   5661  N  N     . LYS   B 1  280 ? 14.389  28.913  7.663    1.00 42.87  ? 280 LYS   C N     1 
ATOM   5662  C  CA    . LYS   B 1  280 ? 14.722  28.790  6.240    1.00 36.78  ? 280 LYS   C CA    1 
ATOM   5663  C  C     . LYS   B 1  280 ? 14.504  30.076  5.431    1.00 36.57  ? 280 LYS   C C     1 
ATOM   5664  O  O     . LYS   B 1  280 ? 14.946  30.133  4.280    1.00 36.28  ? 280 LYS   C O     1 
ATOM   5665  C  CB    . LYS   B 1  280 ? 13.938  27.645  5.595    1.00 34.04  ? 280 LYS   C CB    1 
ATOM   5666  C  CG    . LYS   B 1  280 ? 14.325  27.383  4.128    1.00 55.60  ? 280 LYS   C CG    1 
ATOM   5667  C  CD    . LYS   B 1  280 ? 13.441  26.312  3.425    1.00 64.27  ? 280 LYS   C CD    1 
ATOM   5668  C  CE    . LYS   B 1  280 ? 13.658  26.245  1.894    1.00 54.49  ? 280 LYS   C CE    1 
ATOM   5669  N  NZ    . LYS   B 1  280 ? 13.125  27.424  1.099    1.00 40.18  ? 280 LYS   C NZ    1 
ATOM   5670  N  N     . ALA   B 1  281 ? 13.871  31.118  5.995    1.00 36.03  ? 281 ALA   C N     1 
ATOM   5671  C  CA    . ALA   B 1  281 ? 13.701  32.395  5.288    1.00 42.47  ? 281 ALA   C CA    1 
ATOM   5672  C  C     . ALA   B 1  281 ? 14.816  33.392  5.559    1.00 39.68  ? 281 ALA   C C     1 
ATOM   5673  O  O     . ALA   B 1  281 ? 14.863  34.434  4.906    1.00 33.12  ? 281 ALA   C O     1 
ATOM   5674  C  CB    . ALA   B 1  281 ? 12.377  33.082  5.655    1.00 25.58  ? 281 ALA   C CB    1 
ATOM   5675  N  N     . TYR   B 1  282 ? 15.677  33.127  6.530    1.00 42.80  ? 282 TYR   C N     1 
ATOM   5676  C  CA    . TYR   B 1  282 ? 16.786  34.025  6.807    1.00 37.39  ? 282 TYR   C CA    1 
ATOM   5677  C  C     . TYR   B 1  282 ? 17.686  34.131  5.582    1.00 36.25  ? 282 TYR   C C     1 
ATOM   5678  O  O     . TYR   B 1  282 ? 18.148  33.114  5.051    1.00 42.98  ? 282 TYR   C O     1 
ATOM   5679  C  CB    . TYR   B 1  282 ? 17.570  33.501  8.012    1.00 46.11  ? 282 TYR   C CB    1 
ATOM   5680  C  CG    . TYR   B 1  282 ? 18.528  34.502  8.588    1.00 40.69  ? 282 TYR   C CG    1 
ATOM   5681  C  CD1   . TYR   B 1  282 ? 18.070  35.715  9.060    1.00 35.70  ? 282 TYR   C CD1   1 
ATOM   5682  C  CD2   . TYR   B 1  282 ? 19.883  34.235  8.656    1.00 41.54  ? 282 TYR   C CD2   1 
ATOM   5683  C  CE1   . TYR   B 1  282 ? 18.916  36.633  9.570    1.00 35.48  ? 282 TYR   C CE1   1 
ATOM   5684  C  CE2   . TYR   B 1  282 ? 20.747  35.154  9.185    1.00 39.36  ? 282 TYR   C CE2   1 
ATOM   5685  C  CZ    . TYR   B 1  282 ? 20.253  36.355  9.634    1.00 39.11  ? 282 TYR   C CZ    1 
ATOM   5686  O  OH    . TYR   B 1  282 ? 21.105  37.303  10.157   1.00 52.42  ? 282 TYR   C OH    1 
ATOM   5687  N  N     . HIS   B 1  283 ? 17.905  35.354  5.108    1.00 35.63  ? 283 HIS   C N     1 
ATOM   5688  C  CA    . HIS   B 1  283 ? 18.866  35.576  4.029    1.00 51.88  ? 283 HIS   C CA    1 
ATOM   5689  C  C     . HIS   B 1  283 ? 18.490  34.886  2.716    1.00 51.76  ? 283 HIS   C C     1 
ATOM   5690  O  O     . HIS   B 1  283 ? 19.269  34.915  1.760    1.00 57.98  ? 283 HIS   C O     1 
ATOM   5691  C  CB    . HIS   B 1  283 ? 20.270  35.096  4.451    1.00 57.46  ? 283 HIS   C CB    1 
ATOM   5692  C  CG    . HIS   B 1  283 ? 20.972  36.005  5.417    1.00 49.12  ? 283 HIS   C CG    1 
ATOM   5693  N  ND1   . HIS   B 1  283 ? 22.240  35.740  5.893    1.00 42.81  ? 283 HIS   C ND1   1 
ATOM   5694  C  CD2   . HIS   B 1  283 ? 20.588  37.170  5.996    1.00 41.77  ? 283 HIS   C CD2   1 
ATOM   5695  C  CE1   . HIS   B 1  283 ? 22.605  36.700  6.725    1.00 40.14  ? 283 HIS   C CE1   1 
ATOM   5696  N  NE2   . HIS   B 1  283 ? 21.623  37.582  6.800    1.00 43.64  ? 283 HIS   C NE2   1 
ATOM   5697  N  N     . GLU   B 1  284 ? 17.334  34.241  2.641    1.00 48.72  ? 284 GLU   C N     1 
ATOM   5698  C  CA    . GLU   B 1  284 ? 16.883  33.662  1.381    1.00 50.51  ? 284 GLU   C CA    1 
ATOM   5699  C  C     . GLU   B 1  284 ? 15.536  34.289  1.071    1.00 53.61  ? 284 GLU   C C     1 
ATOM   5700  O  O     . GLU   B 1  284 ? 14.505  33.659  1.306    1.00 65.97  ? 284 GLU   C O     1 
ATOM   5701  C  CB    . GLU   B 1  284 ? 16.791  32.115  1.439    1.00 53.61  ? 284 GLU   C CB    1 
ATOM   5702  C  CG    . GLU   B 1  284 ? 16.203  31.491  0.161    1.00 62.00  ? 284 GLU   C CG    1 
ATOM   5703  C  CD    . GLU   B 1  284 ? 15.813  30.012  0.302    1.00 78.95  ? 284 GLU   C CD    1 
ATOM   5704  O  OE1   . GLU   B 1  284 ? 16.723  29.164  0.460    1.00 83.23  ? 284 GLU   C OE1   1 
ATOM   5705  O  OE2   . GLU   B 1  284 ? 14.596  29.694  0.242    1.00 71.28  ? 284 GLU   C OE2   1 
ATOM   5706  N  N     . GLN   B 1  285 ? 15.545  35.523  0.553    1.00 37.90  ? 285 GLN   C N     1 
ATOM   5707  C  CA    . GLN   B 1  285 ? 14.301  36.233  0.300    1.00 47.63  ? 285 GLN   C CA    1 
ATOM   5708  C  C     . GLN   B 1  285 ? 13.692  35.798  -1.034   1.00 46.24  ? 285 GLN   C C     1 
ATOM   5709  O  O     . GLN   B 1  285 ? 14.396  35.477  -1.991   1.00 53.35  ? 285 GLN   C O     1 
ATOM   5710  C  CB    . GLN   B 1  285 ? 14.522  37.747  0.334    1.00 68.35  ? 285 GLN   C CB    1 
ATOM   5711  C  CG    . GLN   B 1  285 ? 13.355  38.527  0.995    1.00 65.07  ? 285 GLN   C CG    1 
ATOM   5712  C  CD    . GLN   B 1  285 ? 13.782  39.890  1.555    1.00 71.65  ? 285 GLN   C CD    1 
ATOM   5713  O  OE1   . GLN   B 1  285 ? 14.516  39.973  2.558    1.00 62.21  ? 285 GLN   C OE1   1 
ATOM   5714  N  NE2   . GLN   B 1  285 ? 13.321  40.963  0.910    1.00 60.06  ? 285 GLN   C NE2   1 
ATOM   5715  N  N     . LEU   B 1  286 ? 12.365  35.789  -1.085   1.00 44.39  ? 286 LEU   C N     1 
ATOM   5716  C  CA    . LEU   B 1  286 ? 11.617  34.979  -2.045   1.00 47.83  ? 286 LEU   C CA    1 
ATOM   5717  C  C     . LEU   B 1  286 ? 10.911  35.871  -3.068   1.00 40.91  ? 286 LEU   C C     1 
ATOM   5718  O  O     . LEU   B 1  286 ? 10.068  36.708  -2.717   1.00 36.91  ? 286 LEU   C O     1 
ATOM   5719  C  CB    . LEU   B 1  286 ? 10.626  34.079  -1.302   1.00 56.31  ? 286 LEU   C CB    1 
ATOM   5720  C  CG    . LEU   B 1  286 ? 11.101  33.559  0.075    1.00 53.71  ? 286 LEU   C CG    1 
ATOM   5721  C  CD1   . LEU   B 1  286 ? 10.950  34.620  1.209    1.00 39.40  ? 286 LEU   C CD1   1 
ATOM   5722  C  CD2   . LEU   B 1  286 ? 10.410  32.245  0.433    1.00 36.99  ? 286 LEU   C CD2   1 
ATOM   5723  N  N     . SER   B 1  287 ? 11.264  35.687  -4.326   1.00 37.49  ? 287 SER   C N     1 
ATOM   5724  C  CA    . SER   B 1  287 ? 10.871  36.575  -5.398   1.00 33.67  ? 287 SER   C CA    1 
ATOM   5725  C  C     . SER   B 1  287 ? 9.474   36.250  -5.916   1.00 36.25  ? 287 SER   C C     1 
ATOM   5726  O  O     . SER   B 1  287 ? 8.992   35.114  -5.827   1.00 31.21  ? 287 SER   C O     1 
ATOM   5727  C  CB    . SER   B 1  287 ? 11.836  36.436  -6.560   1.00 38.31  ? 287 SER   C CB    1 
ATOM   5728  O  OG    . SER   B 1  287 ? 11.513  35.239  -7.252   1.00 43.36  ? 287 SER   C OG    1 
ATOM   5729  N  N     . VAL   B 1  288 ? 8.857   37.262  -6.530   1.00 35.86  ? 288 VAL   C N     1 
ATOM   5730  C  CA    . VAL   B 1  288 ? 7.610   37.115  -7.272   1.00 30.11  ? 288 VAL   C CA    1 
ATOM   5731  C  C     . VAL   B 1  288 ? 7.632   35.841  -8.114   1.00 33.26  ? 288 VAL   C C     1 
ATOM   5732  O  O     . VAL   B 1  288 ? 6.630   35.122  -8.205   1.00 33.28  ? 288 VAL   C O     1 
ATOM   5733  C  CB    . VAL   B 1  288 ? 7.359   38.355  -8.145   1.00 31.24  ? 288 VAL   C CB    1 
ATOM   5734  C  CG1   . VAL   B 1  288 ? 6.332   38.047  -9.254   1.00 25.45  ? 288 VAL   C CG1   1 
ATOM   5735  C  CG2   . VAL   B 1  288 ? 6.923   39.522  -7.265   1.00 27.93  ? 288 VAL   C CG2   1 
ATOM   5736  N  N     . ALA   B 1  289 ? 8.778   35.528  -8.715   1.00 33.39  ? 289 ALA   C N     1 
ATOM   5737  C  CA    . ALA   B 1  289 ? 8.832   34.382  -9.619   1.00 27.88  ? 289 ALA   C CA    1 
ATOM   5738  C  C     . ALA   B 1  289 ? 8.787   33.064  -8.857   1.00 36.19  ? 289 ALA   C C     1 
ATOM   5739  O  O     . ALA   B 1  289 ? 8.138   32.103  -9.284   1.00 38.30  ? 289 ALA   C O     1 
ATOM   5740  C  CB    . ALA   B 1  289 ? 10.094  34.463  -10.480  1.00 24.92  ? 289 ALA   C CB    1 
ATOM   5741  N  N     . GLU   B 1  290 ? 9.463   32.996  -7.720   1.00 44.71  ? 290 GLU   C N     1 
ATOM   5742  C  CA    . GLU   B 1  290 ? 9.491   31.734  -7.001   1.00 45.59  ? 290 GLU   C CA    1 
ATOM   5743  C  C     . GLU   B 1  290 ? 8.136   31.410  -6.376   1.00 38.49  ? 290 GLU   C C     1 
ATOM   5744  O  O     . GLU   B 1  290 ? 7.729   30.235  -6.368   1.00 36.04  ? 290 GLU   C O     1 
ATOM   5745  C  CB    . GLU   B 1  290 ? 10.612  31.767  -5.965   1.00 48.30  ? 290 GLU   C CB    1 
ATOM   5746  C  CG    . GLU   B 1  290 ? 11.982  31.827  -6.628   1.00 50.97  ? 290 GLU   C CG    1 
ATOM   5747  C  CD    . GLU   B 1  290 ? 13.090  32.178  -5.659   1.00 59.77  ? 290 GLU   C CD    1 
ATOM   5748  O  OE1   . GLU   B 1  290 ? 12.812  32.862  -4.649   1.00 55.46  ? 290 GLU   C OE1   1 
ATOM   5749  O  OE2   . GLU   B 1  290 ? 14.239  31.763  -5.908   1.00 63.52  ? 290 GLU   C OE2   1 
ATOM   5750  N  N     . ILE   B 1  291 ? 7.412   32.429  -5.870   1.00 24.11  ? 291 ILE   C N     1 
ATOM   5751  C  CA    . ILE   B 1  291 ? 6.107   32.167  -5.244   1.00 31.46  ? 291 ILE   C CA    1 
ATOM   5752  C  C     . ILE   B 1  291 ? 5.047   31.859  -6.299   1.00 35.31  ? 291 ILE   C C     1 
ATOM   5753  O  O     . ILE   B 1  291 ? 4.181   30.998  -6.093   1.00 31.60  ? 291 ILE   C O     1 
ATOM   5754  C  CB    . ILE   B 1  291 ? 5.669   33.329  -4.330   1.00 33.07  ? 291 ILE   C CB    1 
ATOM   5755  C  CG1   . ILE   B 1  291 ? 5.500   34.626  -5.126   1.00 31.13  ? 291 ILE   C CG1   1 
ATOM   5756  C  CG2   . ILE   B 1  291 ? 6.659   33.495  -3.169   1.00 31.60  ? 291 ILE   C CG2   1 
ATOM   5757  C  CD1   . ILE   B 1  291 ? 4.920   35.747  -4.350   1.00 23.49  ? 291 ILE   C CD1   1 
ATOM   5758  N  N     . THR   B 1  292 ? 5.111   32.532  -7.453   1.00 32.03  ? 292 THR   C N     1 
ATOM   5759  C  CA    . THR   B 1  292 ? 4.206   32.208  -8.549   1.00 31.16  ? 292 THR   C CA    1 
ATOM   5760  C  C     . THR   B 1  292 ? 4.431   30.788  -9.024   1.00 32.96  ? 292 THR   C C     1 
ATOM   5761  O  O     . THR   B 1  292 ? 3.484   30.012  -9.187   1.00 32.52  ? 292 THR   C O     1 
ATOM   5762  C  CB    . THR   B 1  292 ? 4.406   33.169  -9.722   1.00 30.85  ? 292 THR   C CB    1 
ATOM   5763  O  OG1   . THR   B 1  292 ? 4.374   34.510  -9.260   1.00 29.50  ? 292 THR   C OG1   1 
ATOM   5764  C  CG2   . THR   B 1  292 ? 3.309   32.988  -10.725  1.00 26.18  ? 292 THR   C CG2   1 
ATOM   5765  N  N     . ASN   B 1  293 ? 5.686   30.447  -9.307   1.00 38.32  ? 293 ASN   C N     1 
ATOM   5766  C  CA    . ASN   B 1  293 ? 5.995   29.077  -9.696   1.00 40.74  ? 293 ASN   C CA    1 
ATOM   5767  C  C     . ASN   B 1  293 ? 5.574   28.104  -8.596   1.00 36.73  ? 293 ASN   C C     1 
ATOM   5768  O  O     . ASN   B 1  293 ? 5.115   26.990  -8.874   1.00 33.83  ? 293 ASN   C O     1 
ATOM   5769  C  CB    . ASN   B 1  293 ? 7.491   28.986  -10.036  1.00 43.29  ? 293 ASN   C CB    1 
ATOM   5770  C  CG    . ASN   B 1  293 ? 7.923   27.593  -10.492  1.00 68.64  ? 293 ASN   C CG    1 
ATOM   5771  O  OD1   . ASN   B 1  293 ? 7.103   26.673  -10.650  1.00 67.24  ? 293 ASN   C OD1   1 
ATOM   5772  N  ND2   . ASN   B 1  293 ? 9.227   27.433  -10.707  1.00 72.12  ? 293 ASN   C ND2   1 
ATOM   5773  N  N     . ALA   B 1  294 ? 5.679   28.534  -7.340   1.00 38.32  ? 294 ALA   C N     1 
ATOM   5774  C  CA    . ALA   B 1  294 ? 5.219   27.717  -6.234   1.00 37.13  ? 294 ALA   C CA    1 
ATOM   5775  C  C     . ALA   B 1  294 ? 3.744   27.342  -6.378   1.00 41.73  ? 294 ALA   C C     1 
ATOM   5776  O  O     . ALA   B 1  294 ? 3.346   26.239  -5.981   1.00 33.09  ? 294 ALA   C O     1 
ATOM   5777  C  CB    . ALA   B 1  294 ? 5.466   28.466  -4.927   1.00 30.68  ? 294 ALA   C CB    1 
ATOM   5778  N  N     . CYS   B 1  295 ? 2.918   28.238  -6.944   1.00 39.55  ? 295 CYS   C N     1 
ATOM   5779  C  CA    . CYS   B 1  295 ? 1.475   27.979  -7.004   1.00 38.93  ? 295 CYS   C CA    1 
ATOM   5780  C  C     . CYS   B 1  295 ? 1.110   26.841  -7.932   1.00 35.80  ? 295 CYS   C C     1 
ATOM   5781  O  O     . CYS   B 1  295 ? -0.041  26.397  -7.894   1.00 35.17  ? 295 CYS   C O     1 
ATOM   5782  C  CB    . CYS   B 1  295 ? 0.695   29.208  -7.448   1.00 27.14  ? 295 CYS   C CB    1 
ATOM   5783  S  SG    . CYS   B 1  295 ? 0.827   30.581  -6.336   1.00 36.85  ? 295 CYS   C SG    1 
ATOM   5784  N  N     . PHE   B 1  296 ? 2.055   26.348  -8.732   1.00 33.71  ? 296 PHE   C N     1 
ATOM   5785  C  CA    . PHE   B 1  296 ? 1.783   25.303  -9.703   1.00 33.98  ? 296 PHE   C CA    1 
ATOM   5786  C  C     . PHE   B 1  296 ? 2.411   23.959  -9.351   1.00 43.72  ? 296 PHE   C C     1 
ATOM   5787  O  O     . PHE   B 1  296 ? 2.334   23.020  -10.152  1.00 47.95  ? 296 PHE   C O     1 
ATOM   5788  C  CB    . PHE   B 1  296 ? 2.216   25.785  -11.078  1.00 40.20  ? 296 PHE   C CB    1 
ATOM   5789  C  CG    . PHE   B 1  296 ? 1.290   26.825  -11.639  1.00 44.43  ? 296 PHE   C CG    1 
ATOM   5790  C  CD1   . PHE   B 1  296 ? 0.078   26.449  -12.221  1.00 38.43  ? 296 PHE   C CD1   1 
ATOM   5791  C  CD2   . PHE   B 1  296 ? 1.583   28.164  -11.524  1.00 31.38  ? 296 PHE   C CD2   1 
ATOM   5792  C  CE1   . PHE   B 1  296 ? -0.793  27.383  -12.705  1.00 29.81  ? 296 PHE   C CE1   1 
ATOM   5793  C  CE2   . PHE   B 1  296 ? 0.707   29.104  -12.006  1.00 36.70  ? 296 PHE   C CE2   1 
ATOM   5794  C  CZ    . PHE   B 1  296 ? -0.480  28.713  -12.606  1.00 38.17  ? 296 PHE   C CZ    1 
ATOM   5795  N  N     . GLU   B 1  297 ? 2.992   23.824  -8.160   1.00 45.13  ? 297 GLU   C N     1 
ATOM   5796  C  CA    . GLU   B 1  297 ? 3.426   22.518  -7.676   1.00 49.98  ? 297 GLU   C CA    1 
ATOM   5797  C  C     . GLU   B 1  297 ? 2.247   21.871  -6.958   1.00 48.02  ? 297 GLU   C C     1 
ATOM   5798  O  O     . GLU   B 1  297 ? 1.826   22.378  -5.911   1.00 48.74  ? 297 GLU   C O     1 
ATOM   5799  C  CB    . GLU   B 1  297 ? 4.616   22.654  -6.729   1.00 46.54  ? 297 GLU   C CB    1 
ATOM   5800  C  CG    . GLU   B 1  297 ? 5.547   23.824  -7.022   1.00 45.76  ? 297 GLU   C CG    1 
ATOM   5801  C  CD    . GLU   B 1  297 ? 6.694   23.470  -7.965   1.00 56.12  ? 297 GLU   C CD    1 
ATOM   5802  O  OE1   . GLU   B 1  297 ? 6.694   22.345  -8.532   1.00 56.26  ? 297 GLU   C OE1   1 
ATOM   5803  O  OE2   . GLU   B 1  297 ? 7.598   24.327  -8.128   1.00 45.21  ? 297 GLU   C OE2   1 
ATOM   5804  N  N     . PRO   B 1  298 ? 1.695   20.774  -7.452   1.00 48.49  ? 298 PRO   C N     1 
ATOM   5805  C  CA    . PRO   B 1  298 ? 0.503   20.207  -6.803   1.00 41.23  ? 298 PRO   C CA    1 
ATOM   5806  C  C     . PRO   B 1  298 ? 0.651   19.971  -5.300   1.00 47.30  ? 298 PRO   C C     1 
ATOM   5807  O  O     . PRO   B 1  298 ? -0.334  19.670  -4.625   1.00 49.99  ? 298 PRO   C O     1 
ATOM   5808  C  CB    . PRO   B 1  298 ? 0.291   18.890  -7.561   1.00 44.87  ? 298 PRO   C CB    1 
ATOM   5809  C  CG    . PRO   B 1  298 ? 0.886   19.148  -8.935   1.00 37.68  ? 298 PRO   C CG    1 
ATOM   5810  C  CD    . PRO   B 1  298 ? 2.096   20.017  -8.650   1.00 44.94  ? 298 PRO   C CD    1 
ATOM   5811  N  N     . ALA   B 1  299 ? 1.847   20.122  -4.744   1.00 46.89  ? 299 ALA   C N     1 
ATOM   5812  C  CA    . ALA   B 1  299 ? 2.024   19.876  -3.323   1.00 35.25  ? 299 ALA   C CA    1 
ATOM   5813  C  C     . ALA   B 1  299 ? 1.867   21.124  -2.476   1.00 41.81  ? 299 ALA   C C     1 
ATOM   5814  O  O     . ALA   B 1  299 ? 1.996   21.039  -1.251   1.00 46.05  ? 299 ALA   C O     1 
ATOM   5815  C  CB    . ALA   B 1  299 ? 3.397   19.249  -3.058   1.00 32.24  ? 299 ALA   C CB    1 
ATOM   5816  N  N     . ASN   B 1  300 ? 1.637   22.284  -3.078   1.00 37.73  ? 300 ASN   C N     1 
ATOM   5817  C  CA    . ASN   B 1  300 ? 1.345   23.480  -2.305   1.00 31.96  ? 300 ASN   C CA    1 
ATOM   5818  C  C     . ASN   B 1  300 ? -0.149  23.758  -2.190   1.00 34.21  ? 300 ASN   C C     1 
ATOM   5819  O  O     . ASN   B 1  300 ? -0.523  24.811  -1.669   1.00 38.07  ? 300 ASN   C O     1 
ATOM   5820  C  CB    . ASN   B 1  300 ? 2.034   24.693  -2.907   1.00 30.75  ? 300 ASN   C CB    1 
ATOM   5821  C  CG    . ASN   B 1  300 ? 3.506   24.711  -2.643   1.00 43.92  ? 300 ASN   C CG    1 
ATOM   5822  O  OD1   . ASN   B 1  300 ? 3.937   25.026  -1.541   1.00 51.72  ? 300 ASN   C OD1   1 
ATOM   5823  N  ND2   . ASN   B 1  300 ? 4.300   24.408  -3.661   1.00 42.82  ? 300 ASN   C ND2   1 
ATOM   5824  N  N     . GLN   B 1  301 ? -1.003  22.843  -2.659   1.00 33.81  ? 301 GLN   C N     1 
ATOM   5825  C  CA    . GLN   B 1  301 ? -2.437  23.073  -2.774   1.00 28.43  ? 301 GLN   C CA    1 
ATOM   5826  C  C     . GLN   B 1  301 ? -3.167  22.828  -1.456   1.00 37.56  ? 301 GLN   C C     1 
ATOM   5827  O  O     . GLN   B 1  301 ? -2.668  22.167  -0.543   1.00 44.69  ? 301 GLN   C O     1 
ATOM   5828  C  CB    . GLN   B 1  301 ? -3.036  22.174  -3.843   1.00 34.49  ? 301 GLN   C CB    1 
ATOM   5829  C  CG    . GLN   B 1  301 ? -2.045  21.772  -4.891   1.00 40.28  ? 301 GLN   C CG    1 
ATOM   5830  C  CD    . GLN   B 1  301 ? -2.549  21.984  -6.287   1.00 44.57  ? 301 GLN   C CD    1 
ATOM   5831  O  OE1   . GLN   B 1  301 ? -2.650  21.033  -7.076   1.00 42.24  ? 301 GLN   C OE1   1 
ATOM   5832  N  NE2   . GLN   B 1  301 ? -2.852  23.243  -6.621   1.00 46.19  ? 301 GLN   C NE2   1 
ATOM   5833  N  N     . MET   B 1  302 ? -4.375  23.380  -1.369   1.00 32.21  ? 302 MET   C N     1 
ATOM   5834  C  CA    . MET   B 1  302 ? -5.220  23.154  -0.209   1.00 28.63  ? 302 MET   C CA    1 
ATOM   5835  C  C     . MET   B 1  302 ? -5.997  21.862  -0.312   1.00 30.35  ? 302 MET   C C     1 
ATOM   5836  O  O     . MET   B 1  302 ? -6.456  21.361  0.715    1.00 31.09  ? 302 MET   C O     1 
ATOM   5837  C  CB    . MET   B 1  302 ? -6.206  24.309  -0.002   1.00 30.54  ? 302 MET   C CB    1 
ATOM   5838  C  CG    . MET   B 1  302 ? -5.539  25.565  0.498    1.00 42.97  ? 302 MET   C CG    1 
ATOM   5839  S  SD    . MET   B 1  302 ? -4.146  25.076  1.534    1.00 63.05  ? 302 MET   C SD    1 
ATOM   5840  C  CE    . MET   B 1  302 ? -3.156  26.561  1.614    1.00 35.33  ? 302 MET   C CE    1 
ATOM   5841  N  N     . VAL   B 1  303 ? -6.159  21.310  -1.510   1.00 29.91  ? 303 VAL   C N     1 
ATOM   5842  C  CA    . VAL   B 1  303 ? -6.836  20.024  -1.682   1.00 28.98  ? 303 VAL   C CA    1 
ATOM   5843  C  C     . VAL   B 1  303 ? -5.921  19.112  -2.479   1.00 30.56  ? 303 VAL   C C     1 
ATOM   5844  O  O     . VAL   B 1  303 ? -5.376  19.521  -3.508   1.00 27.94  ? 303 VAL   C O     1 
ATOM   5845  C  CB    . VAL   B 1  303 ? -8.187  20.165  -2.405   1.00 21.87  ? 303 VAL   C CB    1 
ATOM   5846  C  CG1   . VAL   B 1  303 ? -8.830  18.807  -2.610   1.00 20.25  ? 303 VAL   C CG1   1 
ATOM   5847  C  CG2   . VAL   B 1  303 ? -9.085  21.133  -1.669   1.00 28.68  ? 303 VAL   C CG2   1 
ATOM   5848  N  N     . LYS   B 1  304 ? -5.767  17.881  -2.028   1.00 34.20  ? 304 LYS   C N     1 
ATOM   5849  C  CA    . LYS   B 1  304 ? -4.915  16.966  -2.761   1.00 28.03  ? 304 LYS   C CA    1 
ATOM   5850  C  C     . LYS   B 1  304 ? -5.618  16.505  -4.025   1.00 31.58  ? 304 LYS   C C     1 
ATOM   5851  O  O     . LYS   B 1  304 ? -6.656  15.840  -3.964   1.00 38.85  ? 304 LYS   C O     1 
ATOM   5852  C  CB    . LYS   B 1  304 ? -4.520  15.790  -1.882   1.00 24.13  ? 304 LYS   C CB    1 
ATOM   5853  C  CG    . LYS   B 1  304 ? -3.477  16.179  -0.838   1.00 27.01  ? 304 LYS   C CG    1 
ATOM   5854  C  CD    . LYS   B 1  304 ? -2.869  14.935  -0.222   1.00 38.24  ? 304 LYS   C CD    1 
ATOM   5855  C  CE    . LYS   B 1  304 ? -1.477  15.184  0.320    1.00 46.83  ? 304 LYS   C CE    1 
ATOM   5856  N  NZ    . LYS   B 1  304 ? -0.915  13.906  0.822    1.00 39.53  ? 304 LYS   C NZ    1 
ATOM   5857  N  N     . CYS   B 1  305 ? -5.036  16.854  -5.166   1.00 24.19  ? 305 CYS   C N     1 
ATOM   5858  C  CA    . CYS   B 1  305 ? -5.511  16.478  -6.486   1.00 29.22  ? 305 CYS   C CA    1 
ATOM   5859  C  C     . CYS   B 1  305 ? -4.385  16.848  -7.436   1.00 31.98  ? 305 CYS   C C     1 
ATOM   5860  O  O     . CYS   B 1  305 ? -3.449  17.541  -7.040   1.00 31.42  ? 305 CYS   C O     1 
ATOM   5861  C  CB    . CYS   B 1  305 ? -6.795  17.226  -6.830   1.00 37.73  ? 305 CYS   C CB    1 
ATOM   5862  S  SG    . CYS   B 1  305 ? -6.534  19.011  -6.750   1.00 25.03  ? 305 CYS   C SG    1 
ATOM   5863  N  N     . ASP   B 1  306 ? -4.486  16.418  -8.702   1.00 25.09  ? 306 ASP   C N     1 
ATOM   5864  C  CA    . ASP   B 1  306 ? -3.440  16.715  -9.684   1.00 32.41  ? 306 ASP   C CA    1 
ATOM   5865  C  C     . ASP   B 1  306 ? -3.918  17.604  -10.830  1.00 36.08  ? 306 ASP   C C     1 
ATOM   5866  O  O     . ASP   B 1  306 ? -4.374  17.109  -11.881  1.00 29.59  ? 306 ASP   C O     1 
ATOM   5867  C  CB    . ASP   B 1  306 ? -2.826  15.441  -10.250  1.00 36.10  ? 306 ASP   C CB    1 
ATOM   5868  C  CG    . ASP   B 1  306 ? -1.459  15.702  -10.867  1.00 46.37  ? 306 ASP   C CG    1 
ATOM   5869  O  OD1   . ASP   B 1  306 ? -1.047  16.896  -10.943  1.00 34.15  ? 306 ASP   C OD1   1 
ATOM   5870  O  OD2   . ASP   B 1  306 ? -0.799  14.716  -11.267  1.00 59.31  ? 306 ASP   C OD2   1 
ATOM   5871  N  N     . PRO   B 1  307 ? -3.761  18.923  -10.699  1.00 30.16  ? 307 PRO   C N     1 
ATOM   5872  C  CA    . PRO   B 1  307 ? -4.209  19.827  -11.773  1.00 34.25  ? 307 PRO   C CA    1 
ATOM   5873  C  C     . PRO   B 1  307 ? -3.421  19.688  -13.078  1.00 37.16  ? 307 PRO   C C     1 
ATOM   5874  O  O     . PRO   B 1  307 ? -3.956  20.045  -14.140  1.00 34.08  ? 307 PRO   C O     1 
ATOM   5875  C  CB    . PRO   B 1  307 ? -4.036  21.225  -11.164  1.00 24.74  ? 307 PRO   C CB    1 
ATOM   5876  C  CG    . PRO   B 1  307 ? -3.771  21.008  -9.692   1.00 30.98  ? 307 PRO   C CG    1 
ATOM   5877  C  CD    . PRO   B 1  307 ? -3.176  19.642  -9.557   1.00 34.42  ? 307 PRO   C CD    1 
ATOM   5878  N  N     . ARG   B 1  308 ? -2.182  19.184  -13.042  1.00 35.33  ? 308 ARG   C N     1 
ATOM   5879  C  CA    . ARG   B 1  308 ? -1.441  19.004  -14.289  1.00 37.26  ? 308 ARG   C CA    1 
ATOM   5880  C  C     . ARG   B 1  308 ? -2.139  17.995  -15.180  1.00 41.53  ? 308 ARG   C C     1 
ATOM   5881  O  O     . ARG   B 1  308 ? -1.948  18.028  -16.402  1.00 45.81  ? 308 ARG   C O     1 
ATOM   5882  C  CB    . ARG   B 1  308 ? 0.022   18.580  -14.033  1.00 34.14  ? 308 ARG   C CB    1 
ATOM   5883  C  CG    . ARG   B 1  308 ? 0.715   19.326  -12.854  1.00 46.61  ? 308 ARG   C CG    1 
ATOM   5884  C  CD    . ARG   B 1  308 ? 2.044   18.707  -12.387  1.00 48.41  ? 308 ARG   C CD    1 
ATOM   5885  N  NE    . ARG   B 1  308 ? 1.949   17.282  -12.067  1.00 65.25  ? 308 ARG   C NE    1 
ATOM   5886  C  CZ    . ARG   B 1  308 ? 2.083   16.293  -12.953  1.00 64.36  ? 308 ARG   C CZ    1 
ATOM   5887  N  NH1   . ARG   B 1  308 ? 2.284   16.539  -14.247  1.00 44.12  ? 308 ARG   C NH1   1 
ATOM   5888  N  NH2   . ARG   B 1  308 ? 2.009   15.025  -12.532  1.00 39.44  ? 308 ARG   C NH2   1 
ATOM   5889  N  N     . HIS   B 1  309 ? -2.974  17.128  -14.596  1.00 36.35  ? 309 HIS   C N     1 
ATOM   5890  C  CA    . HIS   B 1  309 ? -3.766  16.144  -15.330  1.00 35.66  ? 309 HIS   C CA    1 
ATOM   5891  C  C     . HIS   B 1  309 ? -5.235  16.542  -15.395  1.00 37.84  ? 309 HIS   C C     1 
ATOM   5892  O  O     . HIS   B 1  309 ? -6.109  15.680  -15.582  1.00 31.85  ? 309 HIS   C O     1 
ATOM   5893  C  CB    . HIS   B 1  309 ? -3.625  14.745  -14.706  1.00 38.18  ? 309 HIS   C CB    1 
ATOM   5894  C  CG    . HIS   B 1  309 ? -2.246  14.162  -14.832  1.00 51.94  ? 309 HIS   C CG    1 
ATOM   5895  N  ND1   . HIS   B 1  309 ? -1.564  13.621  -13.759  1.00 57.38  ? 309 HIS   C ND1   1 
ATOM   5896  C  CD2   . HIS   B 1  309 ? -1.418  14.049  -15.901  1.00 40.77  ? 309 HIS   C CD2   1 
ATOM   5897  C  CE1   . HIS   B 1  309 ? -0.374  13.207  -14.162  1.00 52.86  ? 309 HIS   C CE1   1 
ATOM   5898  N  NE2   . HIS   B 1  309 ? -0.263  13.451  -15.457  1.00 49.12  ? 309 HIS   C NE2   1 
ATOM   5899  N  N     . GLY   B 1  310 ? -5.522  17.828  -15.197  1.00 34.72  ? 310 GLY   C N     1 
ATOM   5900  C  CA    . GLY   B 1  310 ? -6.870  18.335  -15.334  1.00 29.52  ? 310 GLY   C CA    1 
ATOM   5901  C  C     . GLY   B 1  310 ? -6.895  19.430  -16.373  1.00 44.38  ? 310 GLY   C C     1 
ATOM   5902  O  O     . GLY   B 1  310 ? -5.907  19.639  -17.092  1.00 47.08  ? 310 GLY   C O     1 
ATOM   5903  N  N     . LYS   B 1  311 ? -8.007  20.134  -16.480  1.00 32.53  ? 311 LYS   C N     1 
ATOM   5904  C  CA    . LYS   B 1  311 ? -8.080  21.289  -17.351  1.00 34.14  ? 311 LYS   C CA    1 
ATOM   5905  C  C     . LYS   B 1  311 ? -8.519  22.465  -16.501  1.00 33.12  ? 311 LYS   C C     1 
ATOM   5906  O  O     . LYS   B 1  311 ? -9.313  22.291  -15.578  1.00 34.19  ? 311 LYS   C O     1 
ATOM   5907  C  CB    . LYS   B 1  311 ? -9.051  21.055  -18.532  1.00 38.76  ? 311 LYS   C CB    1 
ATOM   5908  C  CG    . LYS   B 1  311 ? -8.423  20.384  -19.789  1.00 30.44  ? 311 LYS   C CG    1 
ATOM   5909  C  CD    . LYS   B 1  311 ? -9.515  19.874  -20.733  1.00 34.47  ? 311 LYS   C CD    1 
ATOM   5910  C  CE    . LYS   B 1  311 ? -9.009  19.655  -22.126  1.00 37.10  ? 311 LYS   C CE    1 
ATOM   5911  N  NZ    . LYS   B 1  311 ? -9.946  18.858  -22.951  1.00 46.55  ? 311 LYS   C NZ    1 
ATOM   5912  N  N     . TYR   B 1  312 ? -7.990  23.652  -16.819  1.00 34.02  ? 312 TYR   C N     1 
ATOM   5913  C  CA    . TYR   B 1  312 ? -8.256  24.886  -16.086  1.00 22.63  ? 312 TYR   C CA    1 
ATOM   5914  C  C     . TYR   B 1  312 ? -9.420  25.659  -16.695  1.00 29.40  ? 312 TYR   C C     1 
ATOM   5915  O  O     . TYR   B 1  312 ? -9.472  25.879  -17.910  1.00 29.50  ? 312 TYR   C O     1 
ATOM   5916  C  CB    . TYR   B 1  312 ? -7.027  25.784  -16.101  1.00 24.12  ? 312 TYR   C CB    1 
ATOM   5917  C  CG    . TYR   B 1  312 ? -5.944  25.404  -15.138  1.00 26.66  ? 312 TYR   C CG    1 
ATOM   5918  C  CD1   . TYR   B 1  312 ? -6.045  25.723  -13.792  1.00 27.07  ? 312 TYR   C CD1   1 
ATOM   5919  C  CD2   . TYR   B 1  312 ? -4.797  24.761  -15.576  1.00 27.17  ? 312 TYR   C CD2   1 
ATOM   5920  C  CE1   . TYR   B 1  312 ? -5.037  25.399  -12.913  1.00 32.01  ? 312 TYR   C CE1   1 
ATOM   5921  C  CE2   . TYR   B 1  312 ? -3.792  24.430  -14.702  1.00 31.92  ? 312 TYR   C CE2   1 
ATOM   5922  C  CZ    . TYR   B 1  312 ? -3.909  24.749  -13.375  1.00 29.13  ? 312 TYR   C CZ    1 
ATOM   5923  O  OH    . TYR   B 1  312 ? -2.901  24.415  -12.507  1.00 36.50  ? 312 TYR   C OH    1 
ATOM   5924  N  N     . MET   B 1  313 ? -10.322 26.125  -15.850  1.00 25.12  ? 313 MET   C N     1 
ATOM   5925  C  CA    . MET   B 1  313 ? -11.351 27.034  -16.304  1.00 23.77  ? 313 MET   C CA    1 
ATOM   5926  C  C     . MET   B 1  313 ? -11.095 28.462  -15.862  1.00 27.73  ? 313 MET   C C     1 
ATOM   5927  O  O     . MET   B 1  313 ? -11.832 29.374  -16.257  1.00 25.28  ? 313 MET   C O     1 
ATOM   5928  C  CB    . MET   B 1  313 ? -12.702 26.549  -15.812  1.00 28.58  ? 313 MET   C CB    1 
ATOM   5929  C  CG    . MET   B 1  313 ? -13.022 25.222  -16.401  1.00 24.54  ? 313 MET   C CG    1 
ATOM   5930  S  SD    . MET   B 1  313 ? -13.996 24.369  -15.226  1.00 33.78  ? 313 MET   C SD    1 
ATOM   5931  C  CE    . MET   B 1  313 ? -15.122 23.696  -16.375  1.00 31.34  ? 313 MET   C CE    1 
ATOM   5932  N  N     . ALA   B 1  314 ? -10.060 28.678  -15.068  1.00 27.85  ? 314 ALA   C N     1 
ATOM   5933  C  CA    . ALA   B 1  314 ? -9.780  29.990  -14.521  1.00 26.24  ? 314 ALA   C CA    1 
ATOM   5934  C  C     . ALA   B 1  314 ? -8.525  29.864  -13.687  1.00 32.56  ? 314 ALA   C C     1 
ATOM   5935  O  O     . ALA   B 1  314 ? -8.238  28.799  -13.124  1.00 29.70  ? 314 ALA   C O     1 
ATOM   5936  C  CB    . ALA   B 1  314 ? -10.940 30.513  -13.675  1.00 20.73  ? 314 ALA   C CB    1 
ATOM   5937  N  N     . CYS   B 1  315 ? -7.767  30.945  -13.619  1.00 26.91  ? 315 CYS   C N     1 
ATOM   5938  C  CA    . CYS   B 1  315 ? -6.577  30.971  -12.794  1.00 30.07  ? 315 CYS   C CA    1 
ATOM   5939  C  C     . CYS   B 1  315 ? -6.438  32.393  -12.274  1.00 28.69  ? 315 CYS   C C     1 
ATOM   5940  O  O     . CYS   B 1  315 ? -6.161  33.319  -13.042  1.00 28.13  ? 315 CYS   C O     1 
ATOM   5941  C  CB    . CYS   B 1  315 ? -5.371  30.528  -13.603  1.00 36.99  ? 315 CYS   C CB    1 
ATOM   5942  S  SG    . CYS   B 1  315 ? -4.054  30.016  -12.597  1.00 48.82  ? 315 CYS   C SG    1 
ATOM   5943  N  N     . CYS   B 1  316 ? -6.685  32.575  -10.991  1.00 20.06  ? 316 CYS   C N     1 
ATOM   5944  C  CA    . CYS   B 1  316 ? -6.671  33.895  -10.376  1.00 31.24  ? 316 CYS   C CA    1 
ATOM   5945  C  C     . CYS   B 1  316 ? -5.519  33.965  -9.392   1.00 33.13  ? 316 CYS   C C     1 
ATOM   5946  O  O     . CYS   B 1  316 ? -5.329  33.052  -8.576   1.00 36.03  ? 316 CYS   C O     1 
ATOM   5947  C  CB    . CYS   B 1  316 ? -8.003  34.207  -9.676   1.00 30.07  ? 316 CYS   C CB    1 
ATOM   5948  S  SG    . CYS   B 1  316 ? -9.425  34.167  -10.819  1.00 32.64  ? 316 CYS   C SG    1 
ATOM   5949  N  N     . LEU   B 1  317 ? -4.739  35.027  -9.488   1.00 29.95  ? 317 LEU   C N     1 
ATOM   5950  C  CA    . LEU   B 1  317 ? -3.561  35.196  -8.654   1.00 28.98  ? 317 LEU   C CA    1 
ATOM   5951  C  C     . LEU   B 1  317 ? -3.761  36.438  -7.794   1.00 28.21  ? 317 LEU   C C     1 
ATOM   5952  O  O     . LEU   B 1  317 ? -3.915  37.551  -8.313   1.00 33.77  ? 317 LEU   C O     1 
ATOM   5953  C  CB    . LEU   B 1  317 ? -2.296  35.274  -9.523   1.00 28.20  ? 317 LEU   C CB    1 
ATOM   5954  C  CG    . LEU   B 1  317 ? -1.841  33.953  -10.167  1.00 26.39  ? 317 LEU   C CG    1 
ATOM   5955  C  CD1   . LEU   B 1  317 ? -1.111  34.174  -11.479  1.00 25.65  ? 317 LEU   C CD1   1 
ATOM   5956  C  CD2   . LEU   B 1  317 ? -0.917  33.212  -9.218   1.00 40.23  ? 317 LEU   C CD2   1 
ATOM   5957  N  N     . LEU   B 1  318 ? -3.771  36.256  -6.497   1.00 28.48  ? 318 LEU   C N     1 
ATOM   5958  C  CA    . LEU   B 1  318 ? -3.940  37.376  -5.571   1.00 29.91  ? 318 LEU   C CA    1 
ATOM   5959  C  C     . LEU   B 1  318 ? -2.594  37.593  -4.887   1.00 31.86  ? 318 LEU   C C     1 
ATOM   5960  O  O     . LEU   B 1  318 ? -2.201  36.805  -4.025   1.00 37.38  ? 318 LEU   C O     1 
ATOM   5961  C  CB    . LEU   B 1  318 ? -5.057  37.091  -4.571   1.00 15.70  ? 318 LEU   C CB    1 
ATOM   5962  C  CG    . LEU   B 1  318 ? -6.487  37.001  -5.095   1.00 32.19  ? 318 LEU   C CG    1 
ATOM   5963  C  CD1   . LEU   B 1  318 ? -6.629  36.054  -6.324   1.00 34.94  ? 318 LEU   C CD1   1 
ATOM   5964  C  CD2   . LEU   B 1  318 ? -7.367  36.528  -3.953   1.00 33.12  ? 318 LEU   C CD2   1 
ATOM   5965  N  N     . TYR   B 1  319 ? -1.881  38.643  -5.286   1.00 27.47  ? 319 TYR   C N     1 
ATOM   5966  C  CA    . TYR   B 1  319 ? -0.558  38.942  -4.757   1.00 24.66  ? 319 TYR   C CA    1 
ATOM   5967  C  C     . TYR   B 1  319 ? -0.651  39.906  -3.598   1.00 30.76  ? 319 TYR   C C     1 
ATOM   5968  O  O     . TYR   B 1  319 ? -1.501  40.804  -3.575   1.00 20.75  ? 319 TYR   C O     1 
ATOM   5969  C  CB    . TYR   B 1  319 ? 0.356   39.567  -5.813   1.00 25.40  ? 319 TYR   C CB    1 
ATOM   5970  C  CG    . TYR   B 1  319 ? 0.789   38.627  -6.901   1.00 26.72  ? 319 TYR   C CG    1 
ATOM   5971  C  CD1   . TYR   B 1  319 ? 1.938   37.854  -6.760   1.00 27.59  ? 319 TYR   C CD1   1 
ATOM   5972  C  CD2   . TYR   B 1  319 ? 0.060   38.514  -8.073   1.00 24.31  ? 319 TYR   C CD2   1 
ATOM   5973  C  CE1   . TYR   B 1  319 ? 2.346   36.978  -7.764   1.00 27.71  ? 319 TYR   C CE1   1 
ATOM   5974  C  CE2   . TYR   B 1  319 ? 0.457   37.652  -9.086   1.00 31.14  ? 319 TYR   C CE2   1 
ATOM   5975  C  CZ    . TYR   B 1  319 ? 1.602   36.884  -8.923   1.00 33.66  ? 319 TYR   C CZ    1 
ATOM   5976  O  OH    . TYR   B 1  319 ? 1.994   36.027  -9.918   1.00 29.45  ? 319 TYR   C OH    1 
ATOM   5977  N  N     . ARG   B 1  320 ? 0.289   39.754  -2.663   1.00 36.95  ? 320 ARG   C N     1 
ATOM   5978  C  CA    . ARG   B 1  320 ? 0.289   40.557  -1.452   1.00 33.75  ? 320 ARG   C CA    1 
ATOM   5979  C  C     . ARG   B 1  320 ? 1.673   41.112  -1.135   1.00 27.53  ? 320 ARG   C C     1 
ATOM   5980  O  O     . ARG   B 1  320 ? 2.675   40.395  -1.215   1.00 35.17  ? 320 ARG   C O     1 
ATOM   5981  C  CB    . ARG   B 1  320 ? -0.224  39.728  -0.288   1.00 26.02  ? 320 ARG   C CB    1 
ATOM   5982  C  CG    . ARG   B 1  320 ? -0.773  40.600  0.789    1.00 31.14  ? 320 ARG   C CG    1 
ATOM   5983  C  CD    . ARG   B 1  320 ? -1.674  39.845  1.689    1.00 35.94  ? 320 ARG   C CD    1 
ATOM   5984  N  NE    . ARG   B 1  320 ? -2.245  40.755  2.663    1.00 35.74  ? 320 ARG   C NE    1 
ATOM   5985  C  CZ    . ARG   B 1  320 ? -3.146  40.385  3.552    1.00 41.43  ? 320 ARG   C CZ    1 
ATOM   5986  N  NH1   . ARG   B 1  320 ? -3.627  39.152  3.569    1.00 45.04  ? 320 ARG   C NH1   1 
ATOM   5987  N  NH2   . ARG   B 1  320 ? -3.568  41.267  4.450    1.00 49.31  ? 320 ARG   C NH2   1 
ATOM   5988  N  N     . GLY   B 1  321 ? 1.716   42.394  -0.772   1.00 31.01  ? 321 GLY   C N     1 
ATOM   5989  C  CA    . GLY   B 1  321 ? 2.942   43.078  -0.391   1.00 35.55  ? 321 GLY   C CA    1 
ATOM   5990  C  C     . GLY   B 1  321 ? 3.786   43.661  -1.521   1.00 46.25  ? 321 GLY   C C     1 
ATOM   5991  O  O     . GLY   B 1  321 ? 3.253   44.216  -2.490   1.00 35.98  ? 321 GLY   C O     1 
ATOM   5992  N  N     . ASP   B 1  322 ? 5.117   43.531  -1.398   1.00 44.63  ? 322 ASP   C N     1 
ATOM   5993  C  CA    . ASP   B 1  322 ? 6.071   44.122  -2.336   1.00 43.47  ? 322 ASP   C CA    1 
ATOM   5994  C  C     . ASP   B 1  322 ? 6.056   43.393  -3.677   1.00 35.97  ? 322 ASP   C C     1 
ATOM   5995  O  O     . ASP   B 1  322 ? 6.866   42.491  -3.906   1.00 39.52  ? 322 ASP   C O     1 
ATOM   5996  C  CB    . ASP   B 1  322 ? 7.480   44.116  -1.716   1.00 40.51  ? 322 ASP   C CB    1 
ATOM   5997  C  CG    . ASP   B 1  322 ? 8.578   44.561  -2.686   1.00 39.93  ? 322 ASP   C CG    1 
ATOM   5998  O  OD1   . ASP   B 1  322 ? 8.316   45.301  -3.662   1.00 55.53  ? 322 ASP   C OD1   1 
ATOM   5999  O  OD2   . ASP   B 1  322 ? 9.732   44.157  -2.465   1.00 47.08  ? 322 ASP   C OD2   1 
ATOM   6000  N  N     . VAL   B 1  323 ? 5.143   43.785  -4.566   1.00 33.54  ? 323 VAL   C N     1 
ATOM   6001  C  CA    . VAL   B 1  323 ? 4.938   43.128  -5.853   1.00 34.86  ? 323 VAL   C CA    1 
ATOM   6002  C  C     . VAL   B 1  323 ? 4.720   44.197  -6.920   1.00 41.72  ? 323 VAL   C C     1 
ATOM   6003  O  O     . VAL   B 1  323 ? 3.751   44.961  -6.850   1.00 40.64  ? 323 VAL   C O     1 
ATOM   6004  C  CB    . VAL   B 1  323 ? 3.735   42.167  -5.822   1.00 31.35  ? 323 VAL   C CB    1 
ATOM   6005  C  CG1   . VAL   B 1  323 ? 3.614   41.410  -7.139   1.00 35.56  ? 323 VAL   C CG1   1 
ATOM   6006  C  CG2   . VAL   B 1  323 ? 3.864   41.178  -4.682   1.00 35.36  ? 323 VAL   C CG2   1 
ATOM   6007  N  N     . VAL   B 1  324 ? 5.596   44.244  -7.920   1.00 40.22  ? 324 VAL   C N     1 
ATOM   6008  C  CA    . VAL   B 1  324 ? 5.406   45.208  -9.006   1.00 44.36  ? 324 VAL   C CA    1 
ATOM   6009  C  C     . VAL   B 1  324 ? 4.893   44.509  -10.259  1.00 37.38  ? 324 VAL   C C     1 
ATOM   6010  O  O     . VAL   B 1  324 ? 5.369   43.414  -10.613  1.00 34.56  ? 324 VAL   C O     1 
ATOM   6011  C  CB    . VAL   B 1  324 ? 6.696   45.973  -9.324   1.00 42.80  ? 324 VAL   C CB    1 
ATOM   6012  C  CG1   . VAL   B 1  324 ? 7.214   46.678  -8.076   1.00 46.14  ? 324 VAL   C CG1   1 
ATOM   6013  C  CG2   . VAL   B 1  324 ? 7.725   45.012  -9.904   1.00 38.05  ? 324 VAL   C CG2   1 
ATOM   6014  N  N     . PRO   B 1  325 ? 3.950   45.129  -10.966  1.00 29.01  ? 325 PRO   C N     1 
ATOM   6015  C  CA    . PRO   B 1  325 ? 3.353   44.470  -12.136  1.00 29.44  ? 325 PRO   C CA    1 
ATOM   6016  C  C     . PRO   B 1  325 ? 4.356   43.834  -13.080  1.00 36.87  ? 325 PRO   C C     1 
ATOM   6017  O  O     . PRO   B 1  325 ? 4.229   42.638  -13.407  1.00 29.77  ? 325 PRO   C O     1 
ATOM   6018  C  CB    . PRO   B 1  325 ? 2.571   45.610  -12.781  1.00 25.94  ? 325 PRO   C CB    1 
ATOM   6019  C  CG    . PRO   B 1  325 ? 2.046   46.358  -11.580  1.00 30.75  ? 325 PRO   C CG    1 
ATOM   6020  C  CD    . PRO   B 1  325 ? 3.196   46.331  -10.568  1.00 27.65  ? 325 PRO   C CD    1 
ATOM   6021  N  N     . LYS   B 1  326 ? 5.366   44.592  -13.509  1.00 33.92  ? 326 LYS   C N     1 
ATOM   6022  C  CA    . LYS   B 1  326 ? 6.393   44.054  -14.391  1.00 35.01  ? 326 LYS   C CA    1 
ATOM   6023  C  C     . LYS   B 1  326 ? 6.840   42.651  -13.957  1.00 42.14  ? 326 LYS   C C     1 
ATOM   6024  O  O     . LYS   B 1  326 ? 6.938   41.736  -14.788  1.00 46.23  ? 326 LYS   C O     1 
ATOM   6025  C  CB    . LYS   B 1  326 ? 7.573   45.011  -14.436  1.00 33.21  ? 326 LYS   C CB    1 
ATOM   6026  C  CG    . LYS   B 1  326 ? 8.239   45.124  -15.768  1.00 50.31  ? 326 LYS   C CG    1 
ATOM   6027  C  CD    . LYS   B 1  326 ? 9.597   45.783  -15.601  1.00 64.21  ? 326 LYS   C CD    1 
ATOM   6028  C  CE    . LYS   B 1  326 ? 10.326  45.182  -14.405  1.00 57.46  ? 326 LYS   C CE    1 
ATOM   6029  N  NZ    . LYS   B 1  326 ? 11.621  45.873  -14.125  1.00 75.14  ? 326 LYS   C NZ    1 
ATOM   6030  N  N     . ASP   B 1  327 ? 7.074   42.444  -12.657  1.00 41.72  ? 327 ASP   C N     1 
ATOM   6031  C  CA    . ASP   B 1  327 ? 7.554   41.136  -12.213  1.00 39.34  ? 327 ASP   C CA    1 
ATOM   6032  C  C     . ASP   B 1  327 ? 6.500   40.046  -12.400  1.00 37.22  ? 327 ASP   C C     1 
ATOM   6033  O  O     . ASP   B 1  327 ? 6.826   38.941  -12.852  1.00 34.62  ? 327 ASP   C O     1 
ATOM   6034  C  CB    . ASP   B 1  327 ? 8.009   41.216  -10.764  1.00 43.16  ? 327 ASP   C CB    1 
ATOM   6035  C  CG    . ASP   B 1  327 ? 9.186   42.151  -10.584  1.00 47.91  ? 327 ASP   C CG    1 
ATOM   6036  O  OD1   . ASP   B 1  327 ? 9.885   42.435  -11.590  1.00 48.17  ? 327 ASP   C OD1   1 
ATOM   6037  O  OD2   . ASP   B 1  327 ? 9.406   42.603  -9.440   1.00 57.04  ? 327 ASP   C OD2   1 
ATOM   6038  N  N     . VAL   B 1  328 ? 5.237   40.333  -12.063  1.00 36.36  ? 328 VAL   C N     1 
ATOM   6039  C  CA    . VAL   B 1  328 ? 4.160   39.368  -12.288  1.00 28.56  ? 328 VAL   C CA    1 
ATOM   6040  C  C     . VAL   B 1  328 ? 4.049   39.022  -13.770  1.00 30.28  ? 328 VAL   C C     1 
ATOM   6041  O  O     . VAL   B 1  328 ? 3.861   37.856  -14.136  1.00 26.05  ? 328 VAL   C O     1 
ATOM   6042  C  CB    . VAL   B 1  328 ? 2.824   39.902  -11.732  1.00 31.83  ? 328 VAL   C CB    1 
ATOM   6043  C  CG1   . VAL   B 1  328 ? 1.671   38.967  -12.123  1.00 27.61  ? 328 VAL   C CG1   1 
ATOM   6044  C  CG2   . VAL   B 1  328 ? 2.891   40.061  -10.222  1.00 25.40  ? 328 VAL   C CG2   1 
ATOM   6045  N  N     . ASN   B 1  329 ? 4.175   40.016  -14.650  1.00 28.75  ? 329 ASN   C N     1 
ATOM   6046  C  CA    . ASN   B 1  329 ? 4.158   39.706  -16.075  1.00 31.33  ? 329 ASN   C CA    1 
ATOM   6047  C  C     . ASN   B 1  329 ? 5.201   38.642  -16.409  1.00 28.50  ? 329 ASN   C C     1 
ATOM   6048  O  O     . ASN   B 1  329 ? 4.875   37.595  -16.981  1.00 33.20  ? 329 ASN   C O     1 
ATOM   6049  C  CB    . ASN   B 1  329 ? 4.373   40.971  -16.908  1.00 26.38  ? 329 ASN   C CB    1 
ATOM   6050  C  CG    . ASN   B 1  329 ? 3.104   41.785  -17.081  1.00 28.91  ? 329 ASN   C CG    1 
ATOM   6051  O  OD1   . ASN   B 1  329 ? 2.497   42.208  -16.109  1.00 30.48  ? 329 ASN   C OD1   1 
ATOM   6052  N  ND2   . ASN   B 1  329 ? 2.703   42.019  -18.332  1.00 33.81  ? 329 ASN   C ND2   1 
ATOM   6053  N  N     . ALA   B 1  330 ? 6.453   38.866  -16.008  1.00 29.27  ? 330 ALA   C N     1 
ATOM   6054  C  CA    . ALA   B 1  330 ? 7.518   37.926  -16.376  1.00 35.57  ? 330 ALA   C CA    1 
ATOM   6055  C  C     . ALA   B 1  330 ? 7.254   36.527  -15.836  1.00 28.95  ? 330 ALA   C C     1 
ATOM   6056  O  O     . ALA   B 1  330 ? 7.437   35.537  -16.551  1.00 42.50  ? 330 ALA   C O     1 
ATOM   6057  C  CB    . ALA   B 1  330 ? 8.877   38.431  -15.889  1.00 26.40  ? 330 ALA   C CB    1 
ATOM   6058  N  N     . ALA   B 1  331 ? 6.806   36.425  -14.587  1.00 29.21  ? 331 ALA   C N     1 
ATOM   6059  C  CA    . ALA   B 1  331 ? 6.621   35.117  -13.976  1.00 29.71  ? 331 ALA   C CA    1 
ATOM   6060  C  C     . ALA   B 1  331 ? 5.516   34.338  -14.666  1.00 34.12  ? 331 ALA   C C     1 
ATOM   6061  O  O     . ALA   B 1  331 ? 5.603   33.106  -14.766  1.00 31.72  ? 331 ALA   C O     1 
ATOM   6062  C  CB    . ALA   B 1  331 ? 6.335   35.257  -12.471  1.00 24.39  ? 331 ALA   C CB    1 
ATOM   6063  N  N     . ILE   B 1  332 ? 4.482   35.029  -15.167  1.00 35.39  ? 332 ILE   C N     1 
ATOM   6064  C  CA    . ILE   B 1  332 ? 3.391   34.303  -15.815  1.00 37.89  ? 332 ILE   C CA    1 
ATOM   6065  C  C     . ILE   B 1  332 ? 3.829   33.783  -17.181  1.00 40.09  ? 332 ILE   C C     1 
ATOM   6066  O  O     . ILE   B 1  332 ? 3.443   32.679  -17.591  1.00 43.41  ? 332 ILE   C O     1 
ATOM   6067  C  CB    . ILE   B 1  332 ? 2.126   35.175  -15.903  1.00 28.66  ? 332 ILE   C CB    1 
ATOM   6068  C  CG1   . ILE   B 1  332 ? 1.650   35.530  -14.503  1.00 28.67  ? 332 ILE   C CG1   1 
ATOM   6069  C  CG2   . ILE   B 1  332 ? 1.003   34.422  -16.627  1.00 30.91  ? 332 ILE   C CG2   1 
ATOM   6070  C  CD1   . ILE   B 1  332 ? 0.454   36.437  -14.487  1.00 28.42  ? 332 ILE   C CD1   1 
ATOM   6071  N  N     . ALA   B 1  333 ? 4.655   34.552  -17.897  1.00 30.68  ? 333 ALA   C N     1 
ATOM   6072  C  CA    . ALA   B 1  333 ? 5.128   34.109  -19.206  1.00 35.61  ? 333 ALA   C CA    1 
ATOM   6073  C  C     . ALA   B 1  333 ? 5.953   32.840  -19.075  1.00 37.06  ? 333 ALA   C C     1 
ATOM   6074  O  O     . ALA   B 1  333 ? 5.744   31.867  -19.809  1.00 42.62  ? 333 ALA   C O     1 
ATOM   6075  C  CB    . ALA   B 1  333 ? 5.947   35.215  -19.870  1.00 26.74  ? 333 ALA   C CB    1 
ATOM   6076  N  N     . THR   B 1  334 ? 6.901   32.842  -18.139  1.00 37.57  ? 334 THR   C N     1 
ATOM   6077  C  CA    . THR   B 1  334 ? 7.657   31.641  -17.812  1.00 42.62  ? 334 THR   C CA    1 
ATOM   6078  C  C     . THR   B 1  334 ? 6.732   30.444  -17.607  1.00 47.15  ? 334 THR   C C     1 
ATOM   6079  O  O     . THR   B 1  334 ? 6.856   29.415  -18.283  1.00 46.51  ? 334 THR   C O     1 
ATOM   6080  C  CB    . THR   B 1  334 ? 8.489   31.895  -16.557  1.00 46.87  ? 334 THR   C CB    1 
ATOM   6081  O  OG1   . THR   B 1  334 ? 9.624   32.700  -16.899  1.00 51.10  ? 334 THR   C OG1   1 
ATOM   6082  C  CG2   . THR   B 1  334 ? 8.952   30.572  -15.943  1.00 44.10  ? 334 THR   C CG2   1 
ATOM   6083  N  N     . ILE   B 1  335 ? 5.805   30.566  -16.653  1.00 43.79  ? 335 ILE   C N     1 
ATOM   6084  C  CA    . ILE   B 1  335 ? 4.833   29.509  -16.393  1.00 38.69  ? 335 ILE   C CA    1 
ATOM   6085  C  C     . ILE   B 1  335 ? 4.151   29.085  -17.685  1.00 48.91  ? 335 ILE   C C     1 
ATOM   6086  O  O     . ILE   B 1  335 ? 3.972   27.890  -17.954  1.00 51.38  ? 335 ILE   C O     1 
ATOM   6087  C  CB    . ILE   B 1  335 ? 3.818   29.991  -15.338  1.00 47.55  ? 335 ILE   C CB    1 
ATOM   6088  C  CG1   . ILE   B 1  335 ? 4.264   29.578  -13.947  1.00 44.94  ? 335 ILE   C CG1   1 
ATOM   6089  C  CG2   . ILE   B 1  335 ? 2.441   29.404  -15.573  1.00 40.14  ? 335 ILE   C CG2   1 
ATOM   6090  C  CD1   . ILE   B 1  335 ? 3.833   28.165  -13.635  1.00 48.30  ? 335 ILE   C CD1   1 
ATOM   6091  N  N     . LYS   B 1  336 ? 3.793   30.062  -18.520  1.00 53.02  ? 336 LYS   C N     1 
ATOM   6092  C  CA    . LYS   B 1  336 ? 2.935   29.794  -19.669  1.00 52.55  ? 336 LYS   C CA    1 
ATOM   6093  C  C     . LYS   B 1  336 ? 3.617   28.892  -20.685  1.00 54.18  ? 336 LYS   C C     1 
ATOM   6094  O  O     . LYS   B 1  336 ? 2.962   28.050  -21.309  1.00 60.38  ? 336 LYS   C O     1 
ATOM   6095  C  CB    . LYS   B 1  336 ? 2.512   31.108  -20.321  1.00 48.56  ? 336 LYS   C CB    1 
ATOM   6096  C  CG    . LYS   B 1  336 ? 1.107   31.601  -19.937  1.00 50.59  ? 336 LYS   C CG    1 
ATOM   6097  C  CD    . LYS   B 1  336 ? 0.683   32.739  -20.881  1.00 44.42  ? 336 LYS   C CD    1 
ATOM   6098  C  CE    . LYS   B 1  336 ? -0.787  33.077  -20.774  1.00 42.66  ? 336 LYS   C CE    1 
ATOM   6099  N  NZ    . LYS   B 1  336 ? -1.151  34.006  -21.870  1.00 44.54  ? 336 LYS   C NZ    1 
ATOM   6100  N  N     . THR   B 1  337 ? 4.923   29.057  -20.885  1.00 53.44  ? 337 THR   C N     1 
ATOM   6101  C  CA    . THR   B 1  337 ? 5.632   28.190  -21.819  1.00 56.43  ? 337 THR   C CA    1 
ATOM   6102  C  C     . THR   B 1  337 ? 6.091   26.896  -21.142  1.00 62.61  ? 337 THR   C C     1 
ATOM   6103  O  O     . THR   B 1  337 ? 5.698   25.795  -21.545  1.00 69.66  ? 337 THR   C O     1 
ATOM   6104  C  CB    . THR   B 1  337 ? 6.825   28.934  -22.421  1.00 55.85  ? 337 THR   C CB    1 
ATOM   6105  O  OG1   . THR   B 1  337 ? 7.583   29.535  -21.362  1.00 51.08  ? 337 THR   C OG1   1 
ATOM   6106  C  CG2   . THR   B 1  337 ? 6.345   30.008  -23.395  1.00 55.76  ? 337 THR   C CG2   1 
ATOM   6107  N  N     . LYS   B 1  338 ? 6.906   27.018  -20.101  1.00 44.77  ? 338 LYS   C N     1 
ATOM   6108  C  CA    . LYS   B 1  338 ? 7.492   25.843  -19.473  1.00 56.84  ? 338 LYS   C CA    1 
ATOM   6109  C  C     . LYS   B 1  338 ? 6.554   25.130  -18.494  1.00 59.96  ? 338 LYS   C C     1 
ATOM   6110  O  O     . LYS   B 1  338 ? 7.023   24.457  -17.568  1.00 58.99  ? 338 LYS   C O     1 
ATOM   6111  C  CB    . LYS   B 1  338 ? 8.796   26.257  -18.777  1.00 57.61  ? 338 LYS   C CB    1 
ATOM   6112  C  CG    . LYS   B 1  338 ? 9.577   27.283  -19.604  1.00 60.31  ? 338 LYS   C CG    1 
ATOM   6113  C  CD    . LYS   B 1  338 ? 11.078  27.181  -19.400  1.00 47.07  ? 338 LYS   C CD    1 
ATOM   6114  C  CE    . LYS   B 1  338 ? 11.485  27.672  -18.020  1.00 52.00  ? 338 LYS   C CE    1 
ATOM   6115  N  NZ    . LYS   B 1  338 ? 12.959  27.552  -17.809  1.00 55.30  ? 338 LYS   C NZ    1 
ATOM   6116  N  N     . ARG   B 1  339 ? 5.237   25.237  -18.678  1.00 59.29  ? 339 ARG   C N     1 
ATOM   6117  C  CA    . ARG   B 1  339 ? 4.346   24.437  -17.847  1.00 56.61  ? 339 ARG   C CA    1 
ATOM   6118  C  C     . ARG   B 1  339 ? 3.102   24.008  -18.609  1.00 69.07  ? 339 ARG   C C     1 
ATOM   6119  O  O     . ARG   B 1  339 ? 2.658   24.671  -19.556  1.00 64.02  ? 339 ARG   C O     1 
ATOM   6120  C  CB    . ARG   B 1  339 ? 3.944   25.163  -16.566  1.00 60.63  ? 339 ARG   C CB    1 
ATOM   6121  C  CG    . ARG   B 1  339 ? 4.913   24.869  -15.440  1.00 64.49  ? 339 ARG   C CG    1 
ATOM   6122  C  CD    . ARG   B 1  339 ? 4.304   25.133  -14.083  1.00 63.60  ? 339 ARG   C CD    1 
ATOM   6123  N  NE    . ARG   B 1  339 ? 5.312   25.106  -13.025  1.00 68.87  ? 339 ARG   C NE    1 
ATOM   6124  C  CZ    . ARG   B 1  339 ? 5.594   24.039  -12.290  1.00 64.64  ? 339 ARG   C CZ    1 
ATOM   6125  N  NH1   . ARG   B 1  339 ? 4.968   22.889  -12.477  1.00 58.70  ? 339 ARG   C NH1   1 
ATOM   6126  N  NH2   . ARG   B 1  339 ? 6.526   24.131  -11.341  1.00 69.74  ? 339 ARG   C NH2   1 
ATOM   6127  N  N     . SER   B 1  340 ? 2.548   22.872  -18.163  1.00 77.38  ? 340 SER   C N     1 
ATOM   6128  C  CA    . SER   B 1  340 ? 1.386   22.233  -18.786  1.00 77.46  ? 340 SER   C CA    1 
ATOM   6129  C  C     . SER   B 1  340 ? 0.119   22.833  -18.184  1.00 68.70  ? 340 SER   C C     1 
ATOM   6130  O  O     . SER   B 1  340 ? -0.561  22.235  -17.347  1.00 65.45  ? 340 SER   C O     1 
ATOM   6131  C  CB    . SER   B 1  340 ? 1.440   20.714  -18.608  1.00 78.04  ? 340 SER   C CB    1 
ATOM   6132  O  OG    . SER   B 1  340 ? 1.600   20.328  -17.243  1.00 63.19  ? 340 SER   C OG    1 
ATOM   6133  N  N     . ILE   B 1  341 ? -0.206  24.044  -18.635  1.00 68.38  ? 341 ILE   C N     1 
ATOM   6134  C  CA    . ILE   B 1  341 ? -1.406  24.724  -18.169  1.00 57.71  ? 341 ILE   C CA    1 
ATOM   6135  C  C     . ILE   B 1  341 ? -2.453  24.684  -19.274  1.00 58.09  ? 341 ILE   C C     1 
ATOM   6136  O  O     . ILE   B 1  341 ? -2.781  25.721  -19.864  1.00 62.97  ? 341 ILE   C O     1 
ATOM   6137  C  CB    . ILE   B 1  341 ? -1.097  26.173  -17.742  1.00 56.58  ? 341 ILE   C CB    1 
ATOM   6138  C  CG1   . ILE   B 1  341 ? 0.070   26.207  -16.774  1.00 53.58  ? 341 ILE   C CG1   1 
ATOM   6139  C  CG2   . ILE   B 1  341 ? -2.287  26.844  -17.048  1.00 40.73  ? 341 ILE   C CG2   1 
ATOM   6140  C  CD1   . ILE   B 1  341 ? 0.152   27.536  -16.078  1.00 57.13  ? 341 ILE   C CD1   1 
ATOM   6141  N  N     . GLN   B 1  342 ? -2.993  23.498  -19.564  1.00 43.08  ? 342 GLN   C N     1 
ATOM   6142  C  CA    . GLN   B 1  342 ? -4.070  23.403  -20.545  1.00 54.46  ? 342 GLN   C CA    1 
ATOM   6143  C  C     . GLN   B 1  342 ? -5.342  24.053  -19.999  1.00 45.17  ? 342 GLN   C C     1 
ATOM   6144  O  O     . GLN   B 1  342 ? -5.807  23.683  -18.914  1.00 45.28  ? 342 GLN   C O     1 
ATOM   6145  C  CB    . GLN   B 1  342 ? -4.328  21.943  -20.911  1.00 54.88  ? 342 GLN   C CB    1 
ATOM   6146  C  CG    . GLN   B 1  342 ? -4.576  21.742  -22.402  1.00 66.55  ? 342 GLN   C CG    1 
ATOM   6147  C  CD    . GLN   B 1  342 ? -5.644  20.699  -22.699  1.00 69.06  ? 342 GLN   C CD    1 
ATOM   6148  O  OE1   . GLN   B 1  342 ? -6.646  20.998  -23.359  1.00 70.75  ? 342 GLN   C OE1   1 
ATOM   6149  N  NE2   . GLN   B 1  342 ? -5.434  19.470  -22.223  1.00 57.78  ? 342 GLN   C NE2   1 
ATOM   6150  N  N     . PHE   B 1  343 ? -5.899  25.028  -20.737  1.00 38.79  ? 343 PHE   C N     1 
ATOM   6151  C  CA    . PHE   B 1  343 ? -7.211  25.594  -20.430  1.00 27.16  ? 343 PHE   C CA    1 
ATOM   6152  C  C     . PHE   B 1  343 ? -8.280  24.928  -21.292  1.00 33.43  ? 343 PHE   C C     1 
ATOM   6153  O  O     . PHE   B 1  343 ? -8.027  24.524  -22.429  1.00 39.50  ? 343 PHE   C O     1 
ATOM   6154  C  CB    . PHE   B 1  343 ? -7.254  27.117  -20.639  1.00 27.76  ? 343 PHE   C CB    1 
ATOM   6155  C  CG    . PHE   B 1  343 ? -6.691  27.935  -19.481  1.00 33.04  ? 343 PHE   C CG    1 
ATOM   6156  C  CD1   . PHE   B 1  343 ? -5.316  28.054  -19.282  1.00 36.78  ? 343 PHE   C CD1   1 
ATOM   6157  C  CD2   . PHE   B 1  343 ? -7.535  28.604  -18.609  1.00 32.29  ? 343 PHE   C CD2   1 
ATOM   6158  C  CE1   . PHE   B 1  343 ? -4.797  28.816  -18.226  1.00 27.59  ? 343 PHE   C CE1   1 
ATOM   6159  C  CE2   . PHE   B 1  343 ? -7.017  29.361  -17.550  1.00 33.52  ? 343 PHE   C CE2   1 
ATOM   6160  C  CZ    . PHE   B 1  343 ? -5.644  29.461  -17.365  1.00 24.63  ? 343 PHE   C CZ    1 
ATOM   6161  N  N     . VAL   B 1  344 ? -9.478  24.766  -20.722  1.00 33.26  ? 344 VAL   C N     1 
ATOM   6162  C  CA    . VAL   B 1  344 ? -10.577 24.301  -21.549  1.00 29.27  ? 344 VAL   C CA    1 
ATOM   6163  C  C     . VAL   B 1  344 ? -10.726 25.272  -22.713  1.00 29.30  ? 344 VAL   C C     1 
ATOM   6164  O  O     . VAL   B 1  344 ? -10.309 26.436  -22.639  1.00 28.91  ? 344 VAL   C O     1 
ATOM   6165  C  CB    . VAL   B 1  344 ? -11.885 24.168  -20.747  1.00 34.38  ? 344 VAL   C CB    1 
ATOM   6166  C  CG1   . VAL   B 1  344 ? -11.736 23.093  -19.678  1.00 32.61  ? 344 VAL   C CG1   1 
ATOM   6167  C  CG2   . VAL   B 1  344 ? -12.322 25.507  -20.117  1.00 28.52  ? 344 VAL   C CG2   1 
ATOM   6168  N  N     . ASP   B 1  345 ? -11.299 24.777  -23.820  1.00 38.84  ? 345 ASP   C N     1 
ATOM   6169  C  CA    . ASP   B 1  345 ? -11.345 25.579  -25.048  1.00 35.20  ? 345 ASP   C CA    1 
ATOM   6170  C  C     . ASP   B 1  345 ? -12.438 26.631  -25.013  1.00 37.75  ? 345 ASP   C C     1 
ATOM   6171  O  O     . ASP   B 1  345 ? -12.397 27.576  -25.804  1.00 43.77  ? 345 ASP   C O     1 
ATOM   6172  C  CB    . ASP   B 1  345 ? -11.524 24.708  -26.305  1.00 32.15  ? 345 ASP   C CB    1 
ATOM   6173  C  CG    . ASP   B 1  345 ? -12.854 23.953  -26.334  1.00 39.29  ? 345 ASP   C CG    1 
ATOM   6174  O  OD1   . ASP   B 1  345 ? -13.885 24.500  -25.892  1.00 45.09  ? 345 ASP   C OD1   1 
ATOM   6175  O  OD2   . ASP   B 1  345 ? -12.884 22.809  -26.822  1.00 37.51  ? 345 ASP   C OD2   1 
ATOM   6176  N  N     . TRP   B 1  346 ? -13.406 26.502  -24.114  1.00 38.79  ? 346 TRP   C N     1 
ATOM   6177  C  CA    . TRP   B 1  346 ? -14.400 27.547  -23.966  1.00 31.04  ? 346 TRP   C CA    1 
ATOM   6178  C  C     . TRP   B 1  346 ? -13.956 28.645  -23.003  1.00 39.06  ? 346 TRP   C C     1 
ATOM   6179  O  O     . TRP   B 1  346 ? -14.728 29.585  -22.743  1.00 35.24  ? 346 TRP   C O     1 
ATOM   6180  C  CB    . TRP   B 1  346 ? -15.732 26.941  -23.525  1.00 27.73  ? 346 TRP   C CB    1 
ATOM   6181  C  CG    . TRP   B 1  346 ? -15.667 26.066  -22.314  1.00 34.17  ? 346 TRP   C CG    1 
ATOM   6182  C  CD1   . TRP   B 1  346 ? -15.585 24.701  -22.289  1.00 28.19  ? 346 TRP   C CD1   1 
ATOM   6183  C  CD2   . TRP   B 1  346 ? -15.728 26.495  -20.936  1.00 28.75  ? 346 TRP   C CD2   1 
ATOM   6184  N  NE1   . TRP   B 1  346 ? -15.577 24.260  -20.980  1.00 38.23  ? 346 TRP   C NE1   1 
ATOM   6185  C  CE2   . TRP   B 1  346 ? -15.658 25.345  -20.139  1.00 33.67  ? 346 TRP   C CE2   1 
ATOM   6186  C  CE3   . TRP   B 1  346 ? -15.832 27.741  -20.311  1.00 26.28  ? 346 TRP   C CE3   1 
ATOM   6187  C  CZ2   . TRP   B 1  346 ? -15.692 25.407  -18.758  1.00 29.70  ? 346 TRP   C CZ2   1 
ATOM   6188  C  CZ3   . TRP   B 1  346 ? -15.861 27.800  -18.939  1.00 26.03  ? 346 TRP   C CZ3   1 
ATOM   6189  C  CH2   . TRP   B 1  346 ? -15.792 26.646  -18.178  1.00 28.08  ? 346 TRP   C CH2   1 
ATOM   6190  N  N     . CYS   B 1  347 ? -12.724 28.584  -22.493  1.00 28.14  ? 347 CYS   C N     1 
ATOM   6191  C  CA    . CYS   B 1  347 ? -12.206 29.638  -21.629  1.00 36.34  ? 347 CYS   C CA    1 
ATOM   6192  C  C     . CYS   B 1  347 ? -10.957 30.262  -22.235  1.00 42.91  ? 347 CYS   C C     1 
ATOM   6193  O  O     . CYS   B 1  347 ? -9.847  30.075  -21.723  1.00 52.73  ? 347 CYS   C O     1 
ATOM   6194  C  CB    . CYS   B 1  347 ? -11.903 29.130  -20.222  1.00 34.41  ? 347 CYS   C CB    1 
ATOM   6195  S  SG    . CYS   B 1  347 ? -11.320 30.452  -19.184  1.00 42.71  ? 347 CYS   C SG    1 
ATOM   6196  N  N     . PRO   B 1  348 ? -11.099 31.050  -23.292  1.00 51.85  ? 348 PRO   C N     1 
ATOM   6197  C  CA    . PRO   B 1  348 ? -9.967  31.874  -23.712  1.00 69.22  ? 348 PRO   C CA    1 
ATOM   6198  C  C     . PRO   B 1  348 ? -9.614  32.810  -22.567  1.00 65.75  ? 348 PRO   C C     1 
ATOM   6199  O  O     . PRO   B 1  348 ? -10.430 33.074  -21.677  1.00 65.00  ? 348 PRO   C O     1 
ATOM   6200  C  CB    . PRO   B 1  348 ? -10.508 32.633  -24.928  1.00 70.25  ? 348 PRO   C CB    1 
ATOM   6201  C  CG    . PRO   B 1  348 ? -11.964 32.820  -24.595  1.00 56.77  ? 348 PRO   C CG    1 
ATOM   6202  C  CD    . PRO   B 1  348 ? -12.367 31.536  -23.868  1.00 59.91  ? 348 PRO   C CD    1 
ATOM   6203  N  N     . THR   B 1  349 ? -8.385  33.309  -22.585  1.00 63.92  ? 349 THR   C N     1 
ATOM   6204  C  CA    . THR   B 1  349 ? -7.851  34.058  -21.432  1.00 74.45  ? 349 THR   C CA    1 
ATOM   6205  C  C     . THR   B 1  349 ? -7.797  33.053  -20.283  1.00 55.60  ? 349 THR   C C     1 
ATOM   6206  O  O     . THR   B 1  349 ? -7.232  31.960  -20.460  1.00 61.81  ? 349 THR   C O     1 
ATOM   6207  C  CB    . THR   B 1  349 ? -8.654  35.337  -21.150  1.00 68.91  ? 349 THR   C CB    1 
ATOM   6208  O  OG1   . THR   B 1  349 ? -9.896  35.016  -20.491  1.00 54.10  ? 349 THR   C OG1   1 
ATOM   6209  C  CG2   . THR   B 1  349 ? -8.910  36.102  -22.450  1.00 57.25  ? 349 THR   C CG2   1 
ATOM   6210  N  N     . GLY   B 1  350 ? -8.357  33.351  -19.120  1.00 38.31  ? 350 GLY   C N     1 
ATOM   6211  C  CA    . GLY   B 1  350 ? -8.267  32.458  -17.981  1.00 55.90  ? 350 GLY   C CA    1 
ATOM   6212  C  C     . GLY   B 1  350 ? -7.330  32.910  -16.870  1.00 39.42  ? 350 GLY   C C     1 
ATOM   6213  O  O     . GLY   B 1  350 ? -7.500  32.469  -15.722  1.00 39.81  ? 350 GLY   C O     1 
ATOM   6214  N  N     . PHE   B 1  351 ? -6.359  33.772  -17.167  1.00 33.07  ? 351 PHE   C N     1 
ATOM   6215  C  CA    . PHE   B 1  351 ? -5.525  34.375  -16.135  1.00 34.81  ? 351 PHE   C CA    1 
ATOM   6216  C  C     . PHE   B 1  351 ? -6.088  35.718  -15.679  1.00 32.50  ? 351 PHE   C C     1 
ATOM   6217  O  O     . PHE   B 1  351 ? -6.412  36.581  -16.499  1.00 43.68  ? 351 PHE   C O     1 
ATOM   6218  C  CB    . PHE   B 1  351 ? -4.100  34.551  -16.631  1.00 28.51  ? 351 PHE   C CB    1 
ATOM   6219  C  CG    . PHE   B 1  351 ? -3.230  33.355  -16.393  1.00 38.31  ? 351 PHE   C CG    1 
ATOM   6220  C  CD1   . PHE   B 1  351 ? -2.870  32.992  -15.104  1.00 43.55  ? 351 PHE   C CD1   1 
ATOM   6221  C  CD2   . PHE   B 1  351 ? -2.755  32.601  -17.453  1.00 32.69  ? 351 PHE   C CD2   1 
ATOM   6222  C  CE1   . PHE   B 1  351 ? -2.048  31.890  -14.875  1.00 43.62  ? 351 PHE   C CE1   1 
ATOM   6223  C  CE2   . PHE   B 1  351 ? -1.953  31.511  -17.237  1.00 38.22  ? 351 PHE   C CE2   1 
ATOM   6224  C  CZ    . PHE   B 1  351 ? -1.592  31.154  -15.937  1.00 40.53  ? 351 PHE   C CZ    1 
ATOM   6225  N  N     . LYS   B 1  352 ? -6.216  35.876  -14.368  1.00 25.90  ? 352 LYS   C N     1 
ATOM   6226  C  CA    . LYS   B 1  352 ? -6.683  37.095  -13.749  1.00 26.99  ? 352 LYS   C CA    1 
ATOM   6227  C  C     . LYS   B 1  352 ? -5.833  37.343  -12.512  1.00 26.92  ? 352 LYS   C C     1 
ATOM   6228  O  O     . LYS   B 1  352 ? -5.421  36.410  -11.825  1.00 36.84  ? 352 LYS   C O     1 
ATOM   6229  C  CB    . LYS   B 1  352 ? -8.178  37.021  -13.392  1.00 26.69  ? 352 LYS   C CB    1 
ATOM   6230  C  CG    . LYS   B 1  352 ? -8.695  38.305  -12.742  1.00 29.22  ? 352 LYS   C CG    1 
ATOM   6231  C  CD    . LYS   B 1  352 ? -10.173 38.255  -12.391  1.00 36.32  ? 352 LYS   C CD    1 
ATOM   6232  C  CE    . LYS   B 1  352 ? -10.709 39.657  -12.018  1.00 44.18  ? 352 LYS   C CE    1 
ATOM   6233  N  NZ    . LYS   B 1  352 ? -11.158 40.507  -13.183  1.00 28.38  ? 352 LYS   C NZ    1 
ATOM   6234  N  N     . VAL   B 1  353 ? -5.626  38.611  -12.203  1.00 31.50  ? 353 VAL   C N     1 
ATOM   6235  C  CA    . VAL   B 1  353 ? -4.458  39.045  -11.448  1.00 33.88  ? 353 VAL   C CA    1 
ATOM   6236  C  C     . VAL   B 1  353 ? -4.775  40.356  -10.717  1.00 30.22  ? 353 VAL   C C     1 
ATOM   6237  O  O     . VAL   B 1  353 ? -5.376  41.266  -11.290  1.00 31.81  ? 353 VAL   C O     1 
ATOM   6238  C  CB    . VAL   B 1  353 ? -3.283  39.186  -12.437  1.00 36.29  ? 353 VAL   C CB    1 
ATOM   6239  C  CG1   . VAL   B 1  353 ? -2.559  40.464  -12.226  1.00 30.25  ? 353 VAL   C CG1   1 
ATOM   6240  C  CG2   . VAL   B 1  353 ? -2.368  37.943  -12.405  1.00 28.23  ? 353 VAL   C CG2   1 
ATOM   6241  N  N     . GLY   B 1  354 ? -4.404  40.447  -9.441   1.00 29.98  ? 354 GLY   C N     1 
ATOM   6242  C  CA    . GLY   B 1  354 ? -4.538  41.687  -8.700   1.00 24.43  ? 354 GLY   C CA    1 
ATOM   6243  C  C     . GLY   B 1  354 ? -3.479  41.712  -7.620   1.00 34.80  ? 354 GLY   C C     1 
ATOM   6244  O  O     . GLY   B 1  354 ? -2.852  40.696  -7.316   1.00 32.93  ? 354 GLY   C O     1 
ATOM   6245  N  N     . ILE   B 1  355 ? -3.264  42.891  -7.052   1.00 38.23  ? 355 ILE   C N     1 
ATOM   6246  C  CA    . ILE   B 1  355 ? -2.283  43.080  -5.992   1.00 27.70  ? 355 ILE   C CA    1 
ATOM   6247  C  C     . ILE   B 1  355 ? -2.941  43.803  -4.837   1.00 28.23  ? 355 ILE   C C     1 
ATOM   6248  O  O     . ILE   B 1  355 ? -3.715  44.745  -5.031   1.00 34.02  ? 355 ILE   C O     1 
ATOM   6249  C  CB    . ILE   B 1  355 ? -1.059  43.904  -6.437   1.00 30.85  ? 355 ILE   C CB    1 
ATOM   6250  C  CG1   . ILE   B 1  355 ? -0.289  43.236  -7.553   1.00 25.71  ? 355 ILE   C CG1   1 
ATOM   6251  C  CG2   . ILE   B 1  355 ? -0.128  44.107  -5.258   1.00 33.46  ? 355 ILE   C CG2   1 
ATOM   6252  C  CD1   . ILE   B 1  355 ? 1.017   43.912  -7.786   1.00 30.51  ? 355 ILE   C CD1   1 
ATOM   6253  N  N     . ASN   B 1  356 ? -2.583  43.410  -3.638   1.00 29.64  ? 356 ASN   C N     1 
ATOM   6254  C  CA    . ASN   B 1  356 ? -2.926  44.172  -2.453   1.00 29.86  ? 356 ASN   C CA    1 
ATOM   6255  C  C     . ASN   B 1  356 ? -1.624  44.519  -1.749   1.00 36.89  ? 356 ASN   C C     1 
ATOM   6256  O  O     . ASN   B 1  356 ? -0.929  43.632  -1.240   1.00 39.45  ? 356 ASN   C O     1 
ATOM   6257  C  CB    . ASN   B 1  356 ? -3.879  43.394  -1.559   1.00 33.01  ? 356 ASN   C CB    1 
ATOM   6258  C  CG    . ASN   B 1  356 ? -4.581  44.291  -0.588   1.00 52.88  ? 356 ASN   C CG    1 
ATOM   6259  O  OD1   . ASN   B 1  356 ? -5.532  45.011  -0.952   1.00 54.23  ? 356 ASN   C OD1   1 
ATOM   6260  N  ND2   . ASN   B 1  356 ? -4.097  44.301  0.654    1.00 45.75  ? 356 ASN   C ND2   1 
ATOM   6261  N  N     . TYR   B 1  357 ? -1.270  45.802  -1.754   1.00 36.08  ? 357 TYR   C N     1 
ATOM   6262  C  CA    . TYR   B 1  357 ? 0.050   46.187  -1.272   1.00 41.36  ? 357 TYR   C CA    1 
ATOM   6263  C  C     . TYR   B 1  357 ? 0.244   45.910  0.215    1.00 43.95  ? 357 TYR   C C     1 
ATOM   6264  O  O     . TYR   B 1  357 ? 1.394   45.896  0.677    1.00 48.64  ? 357 TYR   C O     1 
ATOM   6265  C  CB    . TYR   B 1  357 ? 0.306   47.660  -1.626   1.00 34.61  ? 357 TYR   C CB    1 
ATOM   6266  C  CG    . TYR   B 1  357 ? 0.472   47.808  -3.124   1.00 51.16  ? 357 TYR   C CG    1 
ATOM   6267  C  CD1   . TYR   B 1  357 ? 1.520   47.164  -3.779   1.00 51.23  ? 357 TYR   C CD1   1 
ATOM   6268  C  CD2   . TYR   B 1  357 ? -0.442  48.529  -3.900   1.00 61.75  ? 357 TYR   C CD2   1 
ATOM   6269  C  CE1   . TYR   B 1  357 ? 1.675   47.244  -5.144   1.00 50.93  ? 357 TYR   C CE1   1 
ATOM   6270  C  CE2   . TYR   B 1  357 ? -0.285  48.629  -5.293   1.00 49.81  ? 357 TYR   C CE2   1 
ATOM   6271  C  CZ    . TYR   B 1  357 ? 0.778   47.976  -5.904   1.00 55.19  ? 357 TYR   C CZ    1 
ATOM   6272  O  OH    . TYR   B 1  357 ? 0.977   48.038  -7.275   1.00 52.10  ? 357 TYR   C OH    1 
ATOM   6273  N  N     . GLN   B 1  358 ? -0.823  45.635  0.953    1.00 38.29  ? 358 GLN   C N     1 
ATOM   6274  C  CA    . GLN   B 1  358 ? -0.715  45.408  2.386    1.00 41.95  ? 358 GLN   C CA    1 
ATOM   6275  C  C     . GLN   B 1  358 ? 0.161   44.194  2.687    1.00 41.81  ? 358 GLN   C C     1 
ATOM   6276  O  O     . GLN   B 1  358 ? -0.197  43.068  2.306    1.00 40.35  ? 358 GLN   C O     1 
ATOM   6277  C  CB    . GLN   B 1  358 ? -2.089  45.213  2.992    1.00 43.55  ? 358 GLN   C CB    1 
ATOM   6278  C  CG    . GLN   B 1  358 ? -2.232  45.941  4.268    1.00 50.35  ? 358 GLN   C CG    1 
ATOM   6279  C  CD    . GLN   B 1  358 ? -1.981  47.401  4.068    1.00 57.90  ? 358 GLN   C CD    1 
ATOM   6280  O  OE1   . GLN   B 1  358 ? -2.025  47.885  2.934    1.00 56.03  ? 358 GLN   C OE1   1 
ATOM   6281  N  NE2   . GLN   B 1  358 ? -1.700  48.125  5.162    1.00 60.99  ? 358 GLN   C NE2   1 
ATOM   6282  N  N     . PRO   B 1  359 ? 1.266   44.354  3.394    1.00 43.54  ? 359 PRO   C N     1 
ATOM   6283  C  CA    . PRO   B 1  359 ? 2.254   43.289  3.453    1.00 41.97  ? 359 PRO   C CA    1 
ATOM   6284  C  C     . PRO   B 1  359 ? 1.722   42.110  4.245    1.00 39.96  ? 359 PRO   C C     1 
ATOM   6285  O  O     . PRO   B 1  359 ? 0.844   42.270  5.105    1.00 45.30  ? 359 PRO   C O     1 
ATOM   6286  C  CB    . PRO   B 1  359 ? 3.453   43.943  4.153    1.00 37.67  ? 359 PRO   C CB    1 
ATOM   6287  C  CG    . PRO   B 1  359 ? 2.964   45.306  4.641    1.00 48.46  ? 359 PRO   C CG    1 
ATOM   6288  C  CD    . PRO   B 1  359 ? 1.486   45.352  4.457    1.00 48.97  ? 359 PRO   C CD    1 
ATOM   6289  N  N     . PRO   B 1  360 ? 2.233   40.914  3.985    1.00 40.11  ? 360 PRO   C N     1 
ATOM   6290  C  CA    . PRO   B 1  360 ? 1.809   39.748  4.775    1.00 32.39  ? 360 PRO   C CA    1 
ATOM   6291  C  C     . PRO   B 1  360 ? 2.064   39.933  6.271    1.00 32.85  ? 360 PRO   C C     1 
ATOM   6292  O  O     . PRO   B 1  360 ? 2.986   40.624  6.703    1.00 37.39  ? 360 PRO   C O     1 
ATOM   6293  C  CB    . PRO   B 1  360 ? 2.651   38.600  4.194    1.00 33.24  ? 360 PRO   C CB    1 
ATOM   6294  C  CG    . PRO   B 1  360 ? 2.966   39.023  2.808    1.00 34.97  ? 360 PRO   C CG    1 
ATOM   6295  C  CD    . PRO   B 1  360 ? 3.107   40.545  2.858    1.00 31.74  ? 360 PRO   C CD    1 
ATOM   6296  N  N     . THR   B 1  361 ? 1.236   39.283  7.065    1.00 34.85  ? 361 THR   C N     1 
ATOM   6297  C  CA    . THR   B 1  361 ? 1.299   39.386  8.509    1.00 33.39  ? 361 THR   C CA    1 
ATOM   6298  C  C     . THR   B 1  361 ? 1.410   37.991  9.099    1.00 31.93  ? 361 THR   C C     1 
ATOM   6299  O  O     . THR   B 1  361 ? 0.864   37.027  8.551    1.00 34.00  ? 361 THR   C O     1 
ATOM   6300  C  CB    . THR   B 1  361 ? 0.035   40.084  9.042    1.00 34.87  ? 361 THR   C CB    1 
ATOM   6301  O  OG1   . THR   B 1  361 ? 0.114   41.483  8.786    1.00 37.12  ? 361 THR   C OG1   1 
ATOM   6302  C  CG2   . THR   B 1  361 ? -0.147  39.845  10.510   1.00 35.56  ? 361 THR   C CG2   1 
ATOM   6303  N  N     . VAL   B 1  362 ? 2.081   37.876  10.234   1.00 25.87  ? 362 VAL   C N     1 
ATOM   6304  C  CA    . VAL   B 1  362 ? 2.120   36.599  10.926   1.00 35.56  ? 362 VAL   C CA    1 
ATOM   6305  C  C     . VAL   B 1  362 ? 1.876   36.802  12.410   1.00 43.58  ? 362 VAL   C C     1 
ATOM   6306  O  O     . VAL   B 1  362 ? 2.371   37.757  13.018   1.00 42.36  ? 362 VAL   C O     1 
ATOM   6307  C  CB    . VAL   B 1  362 ? 3.445   35.855  10.703   1.00 34.52  ? 362 VAL   C CB    1 
ATOM   6308  C  CG1   . VAL   B 1  362 ? 3.542   35.358  9.231    1.00 28.60  ? 362 VAL   C CG1   1 
ATOM   6309  C  CG2   . VAL   B 1  362 ? 4.603   36.747  11.096   1.00 37.39  ? 362 VAL   C CG2   1 
ATOM   6310  N  N     . VAL   B 1  363 ? 1.092   35.901  12.983   1.00 40.80  ? 363 VAL   C N     1 
ATOM   6311  C  CA    A VAL   B 1  363 ? 0.871   35.847  14.417   1.00 43.52  ? 363 VAL   C CA    1 
ATOM   6312  C  CA    B VAL   B 1  363 ? 0.866   35.871  14.423   0.00 43.61  ? 363 VAL   C CA    1 
ATOM   6313  C  C     . VAL   B 1  363 ? 2.223   35.755  15.105   1.00 42.77  ? 363 VAL   C C     1 
ATOM   6314  O  O     . VAL   B 1  363 ? 2.941   34.770  14.892   1.00 35.27  ? 363 VAL   C O     1 
ATOM   6315  C  CB    A VAL   B 1  363 ? -0.011  34.648  14.786   1.00 47.02  ? 363 VAL   C CB    1 
ATOM   6316  C  CB    B VAL   B 1  363 ? -0.064  34.716  14.824   0.00 46.89  ? 363 VAL   C CB    1 
ATOM   6317  C  CG1   A VAL   B 1  363 ? 0.058   34.394  16.305   1.00 50.43  ? 363 VAL   C CG1   1 
ATOM   6318  C  CG1   B VAL   B 1  363 ? -0.276  34.705  16.330   0.00 48.95  ? 363 VAL   C CG1   1 
ATOM   6319  C  CG2   A VAL   B 1  363 ? -1.437  34.875  14.311   1.00 41.16  ? 363 VAL   C CG2   1 
ATOM   6320  C  CG2   B VAL   B 1  363 ? -1.394  34.828  14.092   0.00 42.28  ? 363 VAL   C CG2   1 
ATOM   6321  N  N     . PRO   B 1  364 ? 2.609   36.735  15.925   1.00 54.93  ? 364 PRO   C N     1 
ATOM   6322  C  CA    . PRO   B 1  364 ? 3.904   36.650  16.612   1.00 57.74  ? 364 PRO   C CA    1 
ATOM   6323  C  C     . PRO   B 1  364 ? 3.995   35.363  17.423   1.00 56.61  ? 364 PRO   C C     1 
ATOM   6324  O  O     . PRO   B 1  364 ? 3.027   34.933  18.057   1.00 40.54  ? 364 PRO   C O     1 
ATOM   6325  C  CB    . PRO   B 1  364 ? 3.914   37.894  17.510   1.00 55.03  ? 364 PRO   C CB    1 
ATOM   6326  C  CG    . PRO   B 1  364 ? 2.912   38.828  16.887   1.00 52.88  ? 364 PRO   C CG    1 
ATOM   6327  C  CD    . PRO   B 1  364 ? 1.849   37.929  16.335   1.00 56.71  ? 364 PRO   C CD    1 
ATOM   6328  N  N     . GLY   B 1  365 ? 5.174   34.742  17.383   1.00 56.20  ? 365 GLY   C N     1 
ATOM   6329  C  CA    . GLY   B 1  365 ? 5.344   33.410  17.927   1.00 57.86  ? 365 GLY   C CA    1 
ATOM   6330  C  C     . GLY   B 1  365 ? 4.592   32.340  17.154   1.00 62.30  ? 365 GLY   C C     1 
ATOM   6331  O  O     . GLY   B 1  365 ? 3.892   31.507  17.746   1.00 59.53  ? 365 GLY   C O     1 
ATOM   6332  N  N     . GLY   B 1  366 ? 4.728   32.355  15.825   1.00 52.85  ? 366 GLY   C N     1 
ATOM   6333  C  CA    . GLY   B 1  366 ? 4.177   31.331  14.972   1.00 39.63  ? 366 GLY   C CA    1 
ATOM   6334  C  C     . GLY   B 1  366 ? 5.263   30.515  14.296   1.00 41.71  ? 366 GLY   C C     1 
ATOM   6335  O  O     . GLY   B 1  366 ? 6.432   30.541  14.683   1.00 51.30  ? 366 GLY   C O     1 
ATOM   6336  N  N     . ASP   B 1  367 ? 4.849   29.766  13.272   1.00 42.24  ? 367 ASP   C N     1 
ATOM   6337  C  CA    . ASP   B 1  367 ? 5.776   29.025  12.434   1.00 45.20  ? 367 ASP   C CA    1 
ATOM   6338  C  C     . ASP   B 1  367 ? 5.995   29.644  11.060   1.00 49.84  ? 367 ASP   C C     1 
ATOM   6339  O  O     . ASP   B 1  367 ? 7.041   29.393  10.451   1.00 52.60  ? 367 ASP   C O     1 
ATOM   6340  C  CB    . ASP   B 1  367 ? 5.298   27.581  12.255   1.00 51.36  ? 367 ASP   C CB    1 
ATOM   6341  C  CG    . ASP   B 1  367 ? 5.035   26.890  13.581   1.00 60.65  ? 367 ASP   C CG    1 
ATOM   6342  O  OD1   . ASP   B 1  367 ? 6.016   26.577  14.304   1.00 52.21  ? 367 ASP   C OD1   1 
ATOM   6343  O  OD2   . ASP   B 1  367 ? 3.839   26.689  13.900   1.00 57.64  ? 367 ASP   C OD2   1 
ATOM   6344  N  N     . LEU   B 1  368 ? 5.059   30.443  10.561   1.00 39.41  ? 368 LEU   C N     1 
ATOM   6345  C  CA    . LEU   B 1  368 ? 5.270   31.077  9.272    1.00 42.01  ? 368 LEU   C CA    1 
ATOM   6346  C  C     . LEU   B 1  368 ? 6.299   32.185  9.403    1.00 35.41  ? 368 LEU   C C     1 
ATOM   6347  O  O     . LEU   B 1  368 ? 6.160   33.074  10.243   1.00 33.33  ? 368 LEU   C O     1 
ATOM   6348  C  CB    . LEU   B 1  368 ? 3.964   31.642  8.727    1.00 41.70  ? 368 LEU   C CB    1 
ATOM   6349  C  CG    . LEU   B 1  368 ? 3.068   30.649  8.003    1.00 49.18  ? 368 LEU   C CG    1 
ATOM   6350  C  CD1   . LEU   B 1  368 ? 3.277   29.264  8.567    1.00 45.08  ? 368 LEU   C CD1   1 
ATOM   6351  C  CD2   . LEU   B 1  368 ? 1.610   31.081  8.147    1.00 50.87  ? 368 LEU   C CD2   1 
ATOM   6352  N  N     . ALA   B 1  369 ? 7.341   32.132  8.581    1.00 32.09  ? 369 ALA   C N     1 
ATOM   6353  C  CA    . ALA   B 1  369 ? 8.179   33.310  8.433    1.00 33.46  ? 369 ALA   C CA    1 
ATOM   6354  C  C     . ALA   B 1  369 ? 7.317   34.481  7.969    1.00 29.10  ? 369 ALA   C C     1 
ATOM   6355  O  O     . ALA   B 1  369 ? 6.329   34.305  7.259    1.00 36.66  ? 369 ALA   C O     1 
ATOM   6356  C  CB    . ALA   B 1  369 ? 9.321   33.041  7.444    1.00 24.28  ? 369 ALA   C CB    1 
ATOM   6357  N  N     . LYS   B 1  370 ? 7.670   35.675  8.416    1.00 31.30  ? 370 LYS   C N     1 
ATOM   6358  C  CA    . LYS   B 1  370 ? 7.090   36.905  7.900    1.00 29.37  ? 370 LYS   C CA    1 
ATOM   6359  C  C     . LYS   B 1  370 ? 7.874   37.302  6.659    1.00 35.37  ? 370 LYS   C C     1 
ATOM   6360  O  O     . LYS   B 1  370 ? 9.061   37.623  6.750    1.00 34.21  ? 370 LYS   C O     1 
ATOM   6361  C  CB    . LYS   B 1  370 ? 7.130   38.020  8.938    1.00 30.55  ? 370 LYS   C CB    1 
ATOM   6362  C  CG    . LYS   B 1  370 ? 6.705   39.381  8.354    1.00 43.63  ? 370 LYS   C CG    1 
ATOM   6363  C  CD    . LYS   B 1  370 ? 6.241   40.360  9.440    1.00 47.55  ? 370 LYS   C CD    1 
ATOM   6364  C  CE    . LYS   B 1  370 ? 5.669   41.667  8.852    1.00 54.00  ? 370 LYS   C CE    1 
ATOM   6365  N  NZ    . LYS   B 1  370 ? 6.697   42.629  8.341    1.00 43.28  ? 370 LYS   C NZ    1 
ATOM   6366  N  N     . VAL   B 1  371 ? 7.210   37.283  5.503    1.00 37.70  ? 371 VAL   C N     1 
ATOM   6367  C  CA    . VAL   B 1  371 ? 7.851   37.515  4.215    1.00 37.91  ? 371 VAL   C CA    1 
ATOM   6368  C  C     . VAL   B 1  371 ? 7.337   38.812  3.617    1.00 28.37  ? 371 VAL   C C     1 
ATOM   6369  O  O     . VAL   B 1  371 ? 6.321   39.362  4.041    1.00 36.80  ? 371 VAL   C O     1 
ATOM   6370  C  CB    . VAL   B 1  371 ? 7.619   36.345  3.250    1.00 35.68  ? 371 VAL   C CB    1 
ATOM   6371  C  CG1   . VAL   B 1  371 ? 8.090   35.079  3.897    1.00 30.06  ? 371 VAL   C CG1   1 
ATOM   6372  C  CG2   . VAL   B 1  371 ? 6.154   36.254  2.878    1.00 37.01  ? 371 VAL   C CG2   1 
ATOM   6373  N  N     . GLN   B 1  372 ? 8.068   39.311  2.618    1.00 40.61  ? 372 GLN   C N     1 
ATOM   6374  C  CA    . GLN   B 1  372 ? 7.745   40.612  2.024    1.00 42.13  ? 372 GLN   C CA    1 
ATOM   6375  C  C     . GLN   B 1  372 ? 6.585   40.527  1.035    1.00 41.12  ? 372 GLN   C C     1 
ATOM   6376  O  O     . GLN   B 1  372 ? 5.753   41.439  0.971    1.00 44.73  ? 372 GLN   C O     1 
ATOM   6377  C  CB    . GLN   B 1  372 ? 8.970   41.195  1.318    1.00 40.60  ? 372 GLN   C CB    1 
ATOM   6378  C  CG    . GLN   B 1  372 ? 10.019  41.756  2.256    1.00 54.87  ? 372 GLN   C CG    1 
ATOM   6379  C  CD    . GLN   B 1  372 ? 11.004  42.663  1.535    1.00 64.59  ? 372 GLN   C CD    1 
ATOM   6380  O  OE1   . GLN   B 1  372 ? 11.796  42.195  0.703    1.00 63.28  ? 372 GLN   C OE1   1 
ATOM   6381  N  NE2   . GLN   B 1  372 ? 10.948  43.978  1.836    1.00 49.40  ? 372 GLN   C NE2   1 
ATOM   6382  N  N     . ARG   B 1  373 ? 6.528   39.465  0.242    1.00 31.06  ? 373 ARG   C N     1 
ATOM   6383  C  CA    . ARG   B 1  373 ? 5.520   39.311  -0.786   1.00 33.14  ? 373 ARG   C CA    1 
ATOM   6384  C  C     . ARG   B 1  373 ? 4.931   37.916  -0.689   1.00 33.96  ? 373 ARG   C C     1 
ATOM   6385  O  O     . ARG   B 1  373 ? 5.660   36.945  -0.474   1.00 44.31  ? 373 ARG   C O     1 
ATOM   6386  C  CB    . ARG   B 1  373 ? 6.140   39.522  -2.154   1.00 36.67  ? 373 ARG   C CB    1 
ATOM   6387  C  CG    . ARG   B 1  373 ? 7.176   38.475  -2.511   1.00 26.53  ? 373 ARG   C CG    1 
ATOM   6388  C  CD    . ARG   B 1  373 ? 8.149   39.019  -3.554   1.00 32.89  ? 373 ARG   C CD    1 
ATOM   6389  N  NE    . ARG   B 1  373 ? 8.900   40.202  -3.130   1.00 34.64  ? 373 ARG   C NE    1 
ATOM   6390  C  CZ    . ARG   B 1  373 ? 10.093  40.162  -2.534   1.00 47.92  ? 373 ARG   C CZ    1 
ATOM   6391  N  NH1   . ARG   B 1  373 ? 10.682  39.009  -2.232   1.00 39.13  ? 373 ARG   C NH1   1 
ATOM   6392  N  NH2   . ARG   B 1  373 ? 10.700  41.304  -2.205   1.00 39.40  ? 373 ARG   C NH2   1 
ATOM   6393  N  N     . ALA   B 1  374 ? 3.623   37.801  -0.850   1.00 27.03  ? 374 ALA   C N     1 
ATOM   6394  C  CA    . ALA   B 1  374 ? 3.014   36.474  -0.871   1.00 31.53  ? 374 ALA   C CA    1 
ATOM   6395  C  C     . ALA   B 1  374 ? 2.009   36.415  -2.001   1.00 33.80  ? 374 ALA   C C     1 
ATOM   6396  O  O     . ALA   B 1  374 ? 1.674   37.434  -2.624   1.00 31.99  ? 374 ALA   C O     1 
ATOM   6397  C  CB    . ALA   B 1  374 ? 2.328   36.111  0.449    1.00 27.95  ? 374 ALA   C CB    1 
ATOM   6398  N  N     . VAL   B 1  375 ? 1.513   35.208  -2.253   1.00 29.17  ? 375 VAL   C N     1 
ATOM   6399  C  CA    . VAL   B 1  375 ? 0.533   35.027  -3.318   1.00 31.35  ? 375 VAL   C CA    1 
ATOM   6400  C  C     . VAL   B 1  375 ? -0.403  33.874  -2.978   1.00 32.15  ? 375 VAL   C C     1 
ATOM   6401  O  O     . VAL   B 1  375 ? 0.031   32.777  -2.609   1.00 30.12  ? 375 VAL   C O     1 
ATOM   6402  C  CB    . VAL   B 1  375 ? 1.189   34.792  -4.692   1.00 26.99  ? 375 VAL   C CB    1 
ATOM   6403  C  CG1   . VAL   B 1  375 ? 1.984   33.485  -4.689   1.00 27.71  ? 375 VAL   C CG1   1 
ATOM   6404  C  CG2   . VAL   B 1  375 ? 0.106   34.767  -5.748   1.00 28.52  ? 375 VAL   C CG2   1 
ATOM   6405  N  N     . CYS   B 1  376 ? -1.694  34.127  -3.128   1.00 26.27  ? 376 CYS   C N     1 
ATOM   6406  C  CA    . CYS   B 1  376 ? -2.695  33.090  -3.119   1.00 22.50  ? 376 CYS   C CA    1 
ATOM   6407  C  C     . CYS   B 1  376 ? -3.270  32.990  -4.523   1.00 30.00  ? 376 CYS   C C     1 
ATOM   6408  O  O     . CYS   B 1  376 ? -3.622  34.004  -5.135   1.00 36.28  ? 376 CYS   C O     1 
ATOM   6409  C  CB    . CYS   B 1  376 ? -3.799  33.378  -2.099   1.00 21.02  ? 376 CYS   C CB    1 
ATOM   6410  S  SG    . CYS   B 1  376 ? -4.993  32.029  -2.117   1.00 29.37  ? 376 CYS   C SG    1 
ATOM   6411  N  N     . MET   B 1  377 ? -3.343  31.781  -5.041   1.00 25.52  ? 377 MET   C N     1 
ATOM   6412  C  CA    . MET   B 1  377 ? -3.893  31.545  -6.357   1.00 31.35  ? 377 MET   C CA    1 
ATOM   6413  C  C     . MET   B 1  377 ? -5.182  30.756  -6.194   1.00 32.85  ? 377 MET   C C     1 
ATOM   6414  O  O     . MET   B 1  377 ? -5.229  29.782  -5.436   1.00 25.84  ? 377 MET   C O     1 
ATOM   6415  C  CB    . MET   B 1  377 ? -2.900  30.799  -7.246   1.00 24.44  ? 377 MET   C CB    1 
ATOM   6416  C  CG    . MET   B 1  377 ? -3.587  29.993  -8.300   1.00 26.43  ? 377 MET   C CG    1 
ATOM   6417  S  SD    . MET   B 1  377 ? -2.524  29.776  -9.712   1.00 39.01  ? 377 MET   C SD    1 
ATOM   6418  C  CE    . MET   B 1  377 ? -2.497  28.007  -9.844   1.00 26.56  ? 377 MET   C CE    1 
ATOM   6419  N  N     . LEU   B 1  378 ? -6.233  31.203  -6.870   1.00 32.46  ? 378 LEU   C N     1 
ATOM   6420  C  CA    . LEU   B 1  378 ? -7.509  30.506  -6.879   1.00 30.47  ? 378 LEU   C CA    1 
ATOM   6421  C  C     . LEU   B 1  378 ? -7.711  29.942  -8.282   1.00 26.16  ? 378 LEU   C C     1 
ATOM   6422  O  O     . LEU   B 1  378 ? -7.915  30.693  -9.237   1.00 32.95  ? 378 LEU   C O     1 
ATOM   6423  C  CB    . LEU   B 1  378 ? -8.641  31.444  -6.460   1.00 31.00  ? 378 LEU   C CB    1 
ATOM   6424  C  CG    . LEU   B 1  378 ? -8.487  32.034  -5.052   1.00 42.89  ? 378 LEU   C CG    1 
ATOM   6425  C  CD1   . LEU   B 1  378 ? -9.560  33.107  -4.764   1.00 40.15  ? 378 LEU   C CD1   1 
ATOM   6426  C  CD2   . LEU   B 1  378 ? -8.464  30.936  -3.949   1.00 31.59  ? 378 LEU   C CD2   1 
ATOM   6427  N  N     . SER   B 1  379 ? -7.617  28.636  -8.404   1.00 21.75  ? 379 SER   C N     1 
ATOM   6428  C  CA    . SER   B 1  379 ? -7.819  27.932  -9.657   1.00 29.48  ? 379 SER   C CA    1 
ATOM   6429  C  C     . SER   B 1  379 ? -9.168  27.252  -9.650   1.00 30.83  ? 379 SER   C C     1 
ATOM   6430  O  O     . SER   B 1  379 ? -9.636  26.782  -8.607   1.00 30.99  ? 379 SER   C O     1 
ATOM   6431  C  CB    . SER   B 1  379 ? -6.759  26.860  -9.888   1.00 22.73  ? 379 SER   C CB    1 
ATOM   6432  O  OG    . SER   B 1  379 ? -5.492  27.436  -9.867   1.00 32.75  ? 379 SER   C OG    1 
ATOM   6433  N  N     . ASN   B 1  380 ? -9.785  27.200  -10.825  1.00 22.76  ? 380 ASN   C N     1 
ATOM   6434  C  CA    . ASN   B 1  380 ? -10.920 26.326  -11.055  1.00 22.30  ? 380 ASN   C CA    1 
ATOM   6435  C  C     . ASN   B 1  380 ? -10.450 25.276  -12.052  1.00 26.79  ? 380 ASN   C C     1 
ATOM   6436  O  O     . ASN   B 1  380 ? -10.361 25.529  -13.258  1.00 27.88  ? 380 ASN   C O     1 
ATOM   6437  C  CB    . ASN   B 1  380 ? -12.127 27.087  -11.557  1.00 23.51  ? 380 ASN   C CB    1 
ATOM   6438  C  CG    . ASN   B 1  380 ? -13.348 26.191  -11.708  1.00 31.07  ? 380 ASN   C CG    1 
ATOM   6439  O  OD1   . ASN   B 1  380 ? -13.465 25.145  -11.057  1.00 34.71  ? 380 ASN   C OD1   1 
ATOM   6440  N  ND2   . ASN   B 1  380 ? -14.268 26.602  -12.560  1.00 32.44  ? 380 ASN   C ND2   1 
ATOM   6441  N  N     . THR   B 1  381 ? -10.136 24.106  -11.537  1.00 25.12  ? 381 THR   C N     1 
ATOM   6442  C  CA    . THR   B 1  381 ? -9.602  23.015  -12.323  1.00 20.49  ? 381 THR   C CA    1 
ATOM   6443  C  C     . THR   B 1  381 ? -10.517 21.829  -12.129  1.00 23.43  ? 381 THR   C C     1 
ATOM   6444  O  O     . THR   B 1  381 ? -10.981 21.585  -11.015  1.00 23.41  ? 381 THR   C O     1 
ATOM   6445  C  CB    . THR   B 1  381 ? -8.178  22.654  -11.894  1.00 25.80  ? 381 THR   C CB    1 
ATOM   6446  O  OG1   . THR   B 1  381 ? -7.925  21.282  -12.233  1.00 34.16  ? 381 THR   C OG1   1 
ATOM   6447  C  CG2   . THR   B 1  381 ? -7.990  22.840  -10.383  1.00 16.54  ? 381 THR   C CG2   1 
ATOM   6448  N  N     . THR   B 1  382 ? -10.806 21.117  -13.221  1.00 23.81  ? 382 THR   C N     1 
ATOM   6449  C  CA    . THR   B 1  382 ? -11.546 19.871  -13.109  1.00 19.76  ? 382 THR   C CA    1 
ATOM   6450  C  C     . THR   B 1  382 ? -10.880 18.935  -12.119  1.00 26.07  ? 382 THR   C C     1 
ATOM   6451  O  O     . THR   B 1  382 ? -11.533 18.015  -11.605  1.00 22.97  ? 382 THR   C O     1 
ATOM   6452  C  CB    . THR   B 1  382 ? -11.642 19.200  -14.477  1.00 22.83  ? 382 THR   C CB    1 
ATOM   6453  O  OG1   . THR   B 1  382 ? -10.333 18.857  -14.929  1.00 22.47  ? 382 THR   C OG1   1 
ATOM   6454  C  CG2   . THR   B 1  382 ? -12.277 20.142  -15.476  1.00 26.85  ? 382 THR   C CG2   1 
ATOM   6455  N  N     . ALA   B 1  383 ? -9.591  19.170  -11.840  1.00 23.10  ? 383 ALA   C N     1 
ATOM   6456  C  CA    . ALA   B 1  383 ? -8.822  18.288  -10.976  1.00 25.81  ? 383 ALA   C CA    1 
ATOM   6457  C  C     . ALA   B 1  383 ? -9.452  18.191  -9.598   1.00 33.53  ? 383 ALA   C C     1 
ATOM   6458  O  O     . ALA   B 1  383 ? -9.407  17.127  -8.961   1.00 31.28  ? 383 ALA   C O     1 
ATOM   6459  C  CB    . ALA   B 1  383 ? -7.378  18.783  -10.874  1.00 25.35  ? 383 ALA   C CB    1 
ATOM   6460  N  N     . ILE   B 1  384 ? -10.040 19.294  -9.112   1.00 24.18  ? 384 ILE   C N     1 
ATOM   6461  C  CA    . ILE   B 1  384 ? -10.589 19.258  -7.763   1.00 26.87  ? 384 ILE   C CA    1 
ATOM   6462  C  C     . ILE   B 1  384 ? -11.626 18.147  -7.606   1.00 29.60  ? 384 ILE   C C     1 
ATOM   6463  O  O     . ILE   B 1  384 ? -11.935 17.757  -6.480   1.00 26.74  ? 384 ILE   C O     1 
ATOM   6464  C  CB    . ILE   B 1  384 ? -11.187 20.619  -7.374   1.00 24.08  ? 384 ILE   C CB    1 
ATOM   6465  C  CG1   . ILE   B 1  384 ? -11.067 20.813  -5.862   1.00 19.93  ? 384 ILE   C CG1   1 
ATOM   6466  C  CG2   . ILE   B 1  384 ? -12.624 20.744  -7.891   1.00 17.53  ? 384 ILE   C CG2   1 
ATOM   6467  C  CD1   . ILE   B 1  384 ? -11.100 22.225  -5.409   1.00 18.02  ? 384 ILE   C CD1   1 
ATOM   6468  N  N     . ALA   B 1  385 ? -12.165 17.614  -8.711   1.00 23.98  ? 385 ALA   C N     1 
ATOM   6469  C  CA    . ALA   B 1  385 ? -13.139 16.541  -8.589   1.00 22.74  ? 385 ALA   C CA    1 
ATOM   6470  C  C     . ALA   B 1  385 ? -12.532 15.285  -7.995   1.00 32.85  ? 385 ALA   C C     1 
ATOM   6471  O  O     . ALA   B 1  385 ? -13.277 14.452  -7.464   1.00 36.12  ? 385 ALA   C O     1 
ATOM   6472  C  CB    . ALA   B 1  385 ? -13.770 16.208  -9.938   1.00 20.76  ? 385 ALA   C CB    1 
ATOM   6473  N  N     . GLU   B 1  386 ? -11.207 15.120  -8.069   1.00 25.63  ? 386 GLU   C N     1 
ATOM   6474  C  CA    . GLU   B 1  386 ? -10.591 13.975  -7.400   1.00 33.01  ? 386 GLU   C CA    1 
ATOM   6475  C  C     . GLU   B 1  386 ? -11.012 13.908  -5.942   1.00 30.64  ? 386 GLU   C C     1 
ATOM   6476  O  O     . GLU   B 1  386 ? -11.362 12.838  -5.435   1.00 33.66  ? 386 GLU   C O     1 
ATOM   6477  C  CB    . GLU   B 1  386 ? -9.069  14.049  -7.484   1.00 35.11  ? 386 GLU   C CB    1 
ATOM   6478  C  CG    . GLU   B 1  386 ? -8.499  13.899  -8.872   1.00 23.90  ? 386 GLU   C CG    1 
ATOM   6479  C  CD    . GLU   B 1  386 ? -7.055  14.303  -8.894   1.00 34.64  ? 386 GLU   C CD    1 
ATOM   6480  O  OE1   . GLU   B 1  386 ? -6.279  13.760  -8.072   1.00 42.52  ? 386 GLU   C OE1   1 
ATOM   6481  O  OE2   . GLU   B 1  386 ? -6.705  15.195  -9.695   1.00 39.74  ? 386 GLU   C OE2   1 
ATOM   6482  N  N     . ALA   B 1  387 ? -11.000 15.051  -5.256   1.00 27.25  ? 387 ALA   C N     1 
ATOM   6483  C  CA    . ALA   B 1  387 ? -11.430 15.082  -3.867   1.00 23.04  ? 387 ALA   C CA    1 
ATOM   6484  C  C     . ALA   B 1  387 ? -12.850 14.545  -3.710   1.00 30.92  ? 387 ALA   C C     1 
ATOM   6485  O  O     . ALA   B 1  387 ? -13.118 13.772  -2.783   1.00 36.57  ? 387 ALA   C O     1 
ATOM   6486  C  CB    . ALA   B 1  387 ? -11.320 16.494  -3.311   1.00 28.54  ? 387 ALA   C CB    1 
ATOM   6487  N  N     . TRP   B 1  388 ? -13.778 14.918  -4.600   1.00 24.94  ? 388 TRP   C N     1 
ATOM   6488  C  CA    . TRP   B 1  388 ? -15.114 14.324  -4.492   1.00 28.83  ? 388 TRP   C CA    1 
ATOM   6489  C  C     . TRP   B 1  388 ? -15.057 12.818  -4.743   1.00 31.53  ? 388 TRP   C C     1 
ATOM   6490  O  O     . TRP   B 1  388 ? -15.717 12.039  -4.048   1.00 33.64  ? 388 TRP   C O     1 
ATOM   6491  C  CB    . TRP   B 1  388 ? -16.130 14.961  -5.460   1.00 25.54  ? 388 TRP   C CB    1 
ATOM   6492  C  CG    . TRP   B 1  388 ? -16.306 16.459  -5.430   1.00 25.83  ? 388 TRP   C CG    1 
ATOM   6493  C  CD1   . TRP   B 1  388 ? -16.196 17.334  -6.503   1.00 28.25  ? 388 TRP   C CD1   1 
ATOM   6494  C  CD2   . TRP   B 1  388 ? -16.632 17.264  -4.297   1.00 25.09  ? 388 TRP   C CD2   1 
ATOM   6495  N  NE1   . TRP   B 1  388 ? -16.432 18.631  -6.087   1.00 26.90  ? 388 TRP   C NE1   1 
ATOM   6496  C  CE2   . TRP   B 1  388 ? -16.704 18.614  -4.742   1.00 23.56  ? 388 TRP   C CE2   1 
ATOM   6497  C  CE3   . TRP   B 1  388 ? -16.867 16.984  -2.952   1.00 28.13  ? 388 TRP   C CE3   1 
ATOM   6498  C  CZ2   . TRP   B 1  388 ? -16.997 19.663  -3.884   1.00 25.40  ? 388 TRP   C CZ2   1 
ATOM   6499  C  CZ3   . TRP   B 1  388 ? -17.176 18.041  -2.095   1.00 33.80  ? 388 TRP   C CZ3   1 
ATOM   6500  C  CH2   . TRP   B 1  388 ? -17.239 19.357  -2.564   1.00 29.76  ? 388 TRP   C CH2   1 
ATOM   6501  N  N     . ALA   B 1  389 ? -14.276 12.383  -5.737   1.00 33.48  ? 389 ALA   C N     1 
ATOM   6502  C  CA    . ALA   B 1  389 ? -14.203 10.953  -6.030   1.00 32.54  ? 389 ALA   C CA    1 
ATOM   6503  C  C     . ALA   B 1  389 ? -13.761 10.157  -4.801   1.00 34.10  ? 389 ALA   C C     1 
ATOM   6504  O  O     . ALA   B 1  389 ? -14.432 9.210   -4.385   1.00 37.50  ? 389 ALA   C O     1 
ATOM   6505  C  CB    . ALA   B 1  389 ? -13.265 10.699  -7.207   1.00 29.43  ? 389 ALA   C CB    1 
ATOM   6506  N  N     . ARG   B 1  390 ? -12.640 10.541  -4.195   1.00 25.04  ? 390 ARG   C N     1 
ATOM   6507  C  CA    . ARG   B 1  390 ? -12.197 9.862   -2.988   1.00 27.89  ? 390 ARG   C CA    1 
ATOM   6508  C  C     . ARG   B 1  390 ? -13.310 9.800   -1.937   1.00 40.04  ? 390 ARG   C C     1 
ATOM   6509  O  O     . ARG   B 1  390 ? -13.566 8.745   -1.342   1.00 34.44  ? 390 ARG   C O     1 
ATOM   6510  C  CB    . ARG   B 1  390 ? -10.961 10.569  -2.434   1.00 27.21  ? 390 ARG   C CB    1 
ATOM   6511  C  CG    . ARG   B 1  390 ? -9.725  10.459  -3.296   1.00 22.72  ? 390 ARG   C CG    1 
ATOM   6512  C  CD    . ARG   B 1  390 ? -8.503  10.872  -2.512   1.00 25.13  ? 390 ARG   C CD    1 
ATOM   6513  N  NE    . ARG   B 1  390 ? -8.596  12.207  -1.943   1.00 19.01  ? 390 ARG   C NE    1 
ATOM   6514  C  CZ    . ARG   B 1  390 ? -8.290  13.312  -2.615   1.00 34.05  ? 390 ARG   C CZ    1 
ATOM   6515  N  NH1   . ARG   B 1  390 ? -7.973  13.275  -3.905   1.00 27.20  ? 390 ARG   C NH1   1 
ATOM   6516  N  NH2   . ARG   B 1  390 ? -8.304  14.486  -1.982   1.00 31.81  ? 390 ARG   C NH2   1 
ATOM   6517  N  N     . LEU   B 1  391 ? -13.982 10.932  -1.691   1.00 34.46  ? 391 LEU   C N     1 
ATOM   6518  C  CA    . LEU   B 1  391 ? -14.993 10.966  -0.643   1.00 32.96  ? 391 LEU   C CA    1 
ATOM   6519  C  C     . LEU   B 1  391 ? -16.172 10.076  -1.004   1.00 39.90  ? 391 LEU   C C     1 
ATOM   6520  O  O     . LEU   B 1  391 ? -16.655 9.296   -0.176   1.00 38.03  ? 391 LEU   C O     1 
ATOM   6521  C  CB    . LEU   B 1  391 ? -15.457 12.402  -0.407   1.00 36.96  ? 391 LEU   C CB    1 
ATOM   6522  C  CG    . LEU   B 1  391 ? -15.166 12.941  0.991    1.00 31.87  ? 391 LEU   C CG    1 
ATOM   6523  C  CD1   . LEU   B 1  391 ? -15.645 14.368  1.091    1.00 44.25  ? 391 LEU   C CD1   1 
ATOM   6524  C  CD2   . LEU   B 1  391 ? -15.861 12.101  1.979    1.00 32.21  ? 391 LEU   C CD2   1 
ATOM   6525  N  N     . ASP   B 1  392 ? -16.647 10.181  -2.250   1.00 41.40  ? 392 ASP   C N     1 
ATOM   6526  C  CA    . ASP   B 1  392 ? -17.748 9.347   -2.699   1.00 29.79  ? 392 ASP   C CA    1 
ATOM   6527  C  C     . ASP   B 1  392 ? -17.391 7.868   -2.598   1.00 37.89  ? 392 ASP   C C     1 
ATOM   6528  O  O     . ASP   B 1  392 ? -18.258 7.037   -2.295   1.00 36.33  ? 392 ASP   C O     1 
ATOM   6529  C  CB    . ASP   B 1  392 ? -18.139 9.745   -4.124   1.00 28.90  ? 392 ASP   C CB    1 
ATOM   6530  C  CG    . ASP   B 1  392 ? -18.887 11.092  -4.181   1.00 36.60  ? 392 ASP   C CG    1 
ATOM   6531  O  OD1   . ASP   B 1  392 ? -19.556 11.466  -3.190   1.00 40.66  ? 392 ASP   C OD1   1 
ATOM   6532  O  OD2   . ASP   B 1  392 ? -18.814 11.792  -5.218   1.00 38.12  ? 392 ASP   C OD2   1 
ATOM   6533  N  N     . HIS   B 1  393 ? -16.115 7.522   -2.805   1.00 36.52  ? 393 HIS   C N     1 
ATOM   6534  C  CA    . HIS   B 1  393 ? -15.721 6.118   -2.732   1.00 36.25  ? 393 HIS   C CA    1 
ATOM   6535  C  C     . HIS   B 1  393 ? -15.708 5.615   -1.291   1.00 40.29  ? 393 HIS   C C     1 
ATOM   6536  O  O     . HIS   B 1  393 ? -16.047 4.453   -1.030   1.00 39.28  ? 393 HIS   C O     1 
ATOM   6537  C  CB    . HIS   B 1  393 ? -14.354 5.894   -3.370   1.00 34.44  ? 393 HIS   C CB    1 
ATOM   6538  C  CG    . HIS   B 1  393 ? -13.886 4.481   -3.251   1.00 43.77  ? 393 HIS   C CG    1 
ATOM   6539  N  ND1   . HIS   B 1  393 ? -14.578 3.423   -3.808   1.00 40.10  ? 393 HIS   C ND1   1 
ATOM   6540  C  CD2   . HIS   B 1  393 ? -12.827 3.943   -2.597   1.00 33.64  ? 393 HIS   C CD2   1 
ATOM   6541  C  CE1   . HIS   B 1  393 ? -13.949 2.296   -3.521   1.00 36.90  ? 393 HIS   C CE1   1 
ATOM   6542  N  NE2   . HIS   B 1  393 ? -12.889 2.583   -2.783   1.00 35.76  ? 393 HIS   C NE2   1 
ATOM   6543  N  N     . LYS   B 1  394 ? -15.312 6.462   -0.340   1.00 36.92  ? 394 LYS   C N     1 
ATOM   6544  C  CA    . LYS   B 1  394 ? -15.456 6.080   1.059    1.00 36.14  ? 394 LYS   C CA    1 
ATOM   6545  C  C     . LYS   B 1  394 ? -16.926 5.928   1.421    1.00 33.81  ? 394 LYS   C C     1 
ATOM   6546  O  O     . LYS   B 1  394 ? -17.329 4.926   2.015    1.00 38.31  ? 394 LYS   C O     1 
ATOM   6547  C  CB    . LYS   B 1  394 ? -14.734 7.082   1.959    1.00 28.36  ? 394 LYS   C CB    1 
ATOM   6548  C  CG    . LYS   B 1  394 ? -13.216 6.870   1.862    1.00 30.40  ? 394 LYS   C CG    1 
ATOM   6549  C  CD    . LYS   B 1  394 ? -12.335 7.929   2.516    1.00 22.86  ? 394 LYS   C CD    1 
ATOM   6550  C  CE    . LYS   B 1  394 ? -10.855 7.545   2.341    1.00 27.21  ? 394 LYS   C CE    1 
ATOM   6551  N  NZ    . LYS   B 1  394 ? -9.884  8.500   2.985    1.00 44.67  ? 394 LYS   C NZ    1 
ATOM   6552  N  N     . PHE   B 1  395 ? -17.758 6.878   1.004    1.00 36.07  ? 395 PHE   C N     1 
ATOM   6553  C  CA    . PHE   B 1  395 ? -19.192 6.766   1.253    1.00 31.71  ? 395 PHE   C CA    1 
ATOM   6554  C  C     . PHE   B 1  395 ? -19.749 5.424   0.745    1.00 37.07  ? 395 PHE   C C     1 
ATOM   6555  O  O     . PHE   B 1  395 ? -20.502 4.741   1.451    1.00 38.64  ? 395 PHE   C O     1 
ATOM   6556  C  CB    . PHE   B 1  395 ? -19.889 7.973   0.612    1.00 25.14  ? 395 PHE   C CB    1 
ATOM   6557  C  CG    . PHE   B 1  395 ? -21.392 7.940   0.673    1.00 29.81  ? 395 PHE   C CG    1 
ATOM   6558  C  CD1   . PHE   B 1  395 ? -22.127 7.183   -0.236   1.00 28.15  ? 395 PHE   C CD1   1 
ATOM   6559  C  CD2   . PHE   B 1  395 ? -22.075 8.720   1.593    1.00 30.55  ? 395 PHE   C CD2   1 
ATOM   6560  C  CE1   . PHE   B 1  395 ? -23.509 7.170   -0.200   1.00 30.68  ? 395 PHE   C CE1   1 
ATOM   6561  C  CE2   . PHE   B 1  395 ? -23.466 8.713   1.628    1.00 32.69  ? 395 PHE   C CE2   1 
ATOM   6562  C  CZ    . PHE   B 1  395 ? -24.189 7.931   0.737    1.00 24.63  ? 395 PHE   C CZ    1 
ATOM   6563  N  N     . ASP   B 1  396 ? -19.368 5.016   -0.471   1.00 30.78  ? 396 ASP   C N     1 
ATOM   6564  C  CA    . ASP   B 1  396 ? -19.987 3.837   -1.082   1.00 29.59  ? 396 ASP   C CA    1 
ATOM   6565  C  C     . ASP   B 1  396 ? -19.606 2.541   -0.378   1.00 33.55  ? 396 ASP   C C     1 
ATOM   6566  O  O     . ASP   B 1  396 ? -20.401 1.597   -0.351   1.00 27.05  ? 396 ASP   C O     1 
ATOM   6567  C  CB    . ASP   B 1  396 ? -19.593 3.724   -2.548   1.00 22.42  ? 396 ASP   C CB    1 
ATOM   6568  C  CG    . ASP   B 1  396 ? -20.209 4.800   -3.398   1.00 29.69  ? 396 ASP   C CG    1 
ATOM   6569  O  OD1   . ASP   B 1  396 ? -21.184 5.435   -2.939   1.00 30.28  ? 396 ASP   C OD1   1 
ATOM   6570  O  OD2   . ASP   B 1  396 ? -19.704 5.008   -4.519   1.00 27.72  ? 396 ASP   C OD2   1 
ATOM   6571  N  N     . LEU   B 1  397 ? -18.375 2.446   0.125    1.00 39.08  ? 397 LEU   C N     1 
ATOM   6572  C  CA    . LEU   B 1  397 ? -17.971 1.247   0.835    1.00 23.51  ? 397 LEU   C CA    1 
ATOM   6573  C  C     . LEU   B 1  397 ? -18.885 1.013   2.019    1.00 36.91  ? 397 LEU   C C     1 
ATOM   6574  O  O     . LEU   B 1  397 ? -19.417 -0.089  2.193    1.00 35.76  ? 397 LEU   C O     1 
ATOM   6575  C  CB    . LEU   B 1  397 ? -16.523 1.370   1.293    1.00 27.85  ? 397 LEU   C CB    1 
ATOM   6576  C  CG    . LEU   B 1  397 ? -15.466 1.322   0.198    1.00 31.32  ? 397 LEU   C CG    1 
ATOM   6577  C  CD1   . LEU   B 1  397 ? -14.103 1.713   0.761    1.00 25.51  ? 397 LEU   C CD1   1 
ATOM   6578  C  CD2   . LEU   B 1  397 ? -15.436 -0.061  -0.389   1.00 21.22  ? 397 LEU   C CD2   1 
ATOM   6579  N  N     . MET   B 1  398 ? -19.104 2.059   2.836    1.00 37.32  ? 398 MET   C N     1 
ATOM   6580  C  CA    . MET   B 1  398 ? -19.946 1.906   4.021    1.00 34.01  ? 398 MET   C CA    1 
ATOM   6581  C  C     . MET   B 1  398 ? -21.408 1.723   3.652    1.00 30.17  ? 398 MET   C C     1 
ATOM   6582  O  O     . MET   B 1  398 ? -22.091 0.878   4.238    1.00 31.15  ? 398 MET   C O     1 
ATOM   6583  C  CB    . MET   B 1  398 ? -19.799 3.104   4.950    1.00 34.32  ? 398 MET   C CB    1 
ATOM   6584  C  CG    . MET   B 1  398 ? -18.515 3.143   5.733    1.00 35.73  ? 398 MET   C CG    1 
ATOM   6585  S  SD    . MET   B 1  398 ? -18.276 4.833   6.250    1.00 38.09  ? 398 MET   C SD    1 
ATOM   6586  C  CE    . MET   B 1  398 ? -17.982 4.541   7.979    1.00 42.75  ? 398 MET   C CE    1 
ATOM   6587  N  N     . TYR   B 1  399 ? -21.917 2.517   2.700    1.00 29.98  ? 399 TYR   C N     1 
ATOM   6588  C  CA    . TYR   B 1  399 ? -23.355 2.517   2.463    1.00 30.34  ? 399 TYR   C CA    1 
ATOM   6589  C  C     . TYR   B 1  399 ? -23.823 1.267   1.727    1.00 37.04  ? 399 TYR   C C     1 
ATOM   6590  O  O     . TYR   B 1  399 ? -24.998 0.897   1.847    1.00 40.35  ? 399 TYR   C O     1 
ATOM   6591  C  CB    . TYR   B 1  399 ? -23.793 3.769   1.706    1.00 31.58  ? 399 TYR   C CB    1 
ATOM   6592  C  CG    . TYR   B 1  399 ? -25.292 3.938   1.695    1.00 25.45  ? 399 TYR   C CG    1 
ATOM   6593  C  CD1   . TYR   B 1  399 ? -25.947 4.557   2.743    1.00 30.50  ? 399 TYR   C CD1   1 
ATOM   6594  C  CD2   . TYR   B 1  399 ? -26.055 3.453   0.648    1.00 29.99  ? 399 TYR   C CD2   1 
ATOM   6595  C  CE1   . TYR   B 1  399 ? -27.335 4.701   2.738    1.00 34.63  ? 399 TYR   C CE1   1 
ATOM   6596  C  CE2   . TYR   B 1  399 ? -27.442 3.596   0.632    1.00 29.66  ? 399 TYR   C CE2   1 
ATOM   6597  C  CZ    . TYR   B 1  399 ? -28.071 4.215   1.675    1.00 33.47  ? 399 TYR   C CZ    1 
ATOM   6598  O  OH    . TYR   B 1  399 ? -29.443 4.345   1.652    1.00 45.84  ? 399 TYR   C OH    1 
ATOM   6599  N  N     . ALA   B 1  400 ? -22.940 0.598   0.982    1.00 34.71  ? 400 ALA   C N     1 
ATOM   6600  C  CA    . ALA   B 1  400 ? -23.314 -0.683  0.397    1.00 36.81  ? 400 ALA   C CA    1 
ATOM   6601  C  C     . ALA   B 1  400 ? -23.720 -1.678  1.482    1.00 43.16  ? 400 ALA   C C     1 
ATOM   6602  O  O     . ALA   B 1  400 ? -24.639 -2.482  1.292    1.00 43.28  ? 400 ALA   C O     1 
ATOM   6603  C  CB    . ALA   B 1  400 ? -22.160 -1.233  -0.444   1.00 34.74  ? 400 ALA   C CB    1 
ATOM   6604  N  N     . LYS   B 1  401 ? -23.045 -1.648  2.625    1.00 37.79  ? 401 LYS   C N     1 
ATOM   6605  C  CA    . LYS   B 1  401 ? -23.406 -2.517  3.733    1.00 38.35  ? 401 LYS   C CA    1 
ATOM   6606  C  C     . LYS   B 1  401 ? -24.253 -1.810  4.774    1.00 34.39  ? 401 LYS   C C     1 
ATOM   6607  O  O     . LYS   B 1  401 ? -24.556 -2.406  5.808    1.00 38.58  ? 401 LYS   C O     1 
ATOM   6608  C  CB    . LYS   B 1  401 ? -22.146 -3.107  4.390    1.00 36.71  ? 401 LYS   C CB    1 
ATOM   6609  C  CG    . LYS   B 1  401 ? -21.536 -4.313  3.634    1.00 40.69  ? 401 LYS   C CG    1 
ATOM   6610  C  CD    . LYS   B 1  401 ? -21.719 -4.183  2.121    1.00 45.63  ? 401 LYS   C CD    1 
ATOM   6611  C  CE    . LYS   B 1  401 ? -20.765 -5.069  1.341    1.00 34.81  ? 401 LYS   C CE    1 
ATOM   6612  N  NZ    . LYS   B 1  401 ? -19.392 -4.647  1.610    1.00 44.39  ? 401 LYS   C NZ    1 
ATOM   6613  N  N     . ARG   B 1  402 ? -24.645 -0.558  4.532    1.00 33.41  ? 402 ARG   C N     1 
ATOM   6614  C  CA    . ARG   B 1  402 ? -25.462 0.222   5.469    1.00 37.19  ? 402 ARG   C CA    1 
ATOM   6615  C  C     . ARG   B 1  402 ? -24.796 0.416   6.828    1.00 37.62  ? 402 ARG   C C     1 
ATOM   6616  O  O     . ARG   B 1  402 ? -25.483 0.705   7.815    1.00 40.61  ? 402 ARG   C O     1 
ATOM   6617  C  CB    . ARG   B 1  402 ? -26.849 -0.397  5.694    1.00 26.06  ? 402 ARG   C CB    1 
ATOM   6618  C  CG    . ARG   B 1  402 ? -27.724 -0.475  4.478    1.00 26.02  ? 402 ARG   C CG    1 
ATOM   6619  C  CD    . ARG   B 1  402 ? -27.914 0.867   3.837    1.00 36.57  ? 402 ARG   C CD    1 
ATOM   6620  N  NE    . ARG   B 1  402 ? -28.882 0.794   2.749    1.00 46.00  ? 402 ARG   C NE    1 
ATOM   6621  C  CZ    . ARG   B 1  402 ? -28.588 0.461   1.496    1.00 38.72  ? 402 ARG   C CZ    1 
ATOM   6622  N  NH1   . ARG   B 1  402 ? -27.347 0.205   1.117    1.00 27.83  ? 402 ARG   C NH1   1 
ATOM   6623  N  NH2   . ARG   B 1  402 ? -29.567 0.369   0.606    1.00 37.33  ? 402 ARG   C NH2   1 
ATOM   6624  N  N     . ALA   B 1  403 ? -23.478 0.261   6.918    1.00 32.50  ? 403 ALA   C N     1 
ATOM   6625  C  CA    . ALA   B 1  403 ? -22.803 0.470   8.192    1.00 34.55  ? 403 ALA   C CA    1 
ATOM   6626  C  C     . ALA   B 1  403 ? -23.049 1.892   8.691    1.00 33.49  ? 403 ALA   C C     1 
ATOM   6627  O  O     . ALA   B 1  403 ? -22.876 2.855   7.948    1.00 38.02  ? 403 ALA   C O     1 
ATOM   6628  C  CB    . ALA   B 1  403 ? -21.302 0.209   8.045    1.00 35.80  ? 403 ALA   C CB    1 
ATOM   6629  N  N     . PHE   B 1  404 ? -23.470 2.000   9.953    1.00 29.24  ? 404 PHE   C N     1 
ATOM   6630  C  CA    . PHE   B 1  404 ? -23.698 3.230   10.721   1.00 27.82  ? 404 PHE   C CA    1 
ATOM   6631  C  C     . PHE   B 1  404 ? -24.949 3.988   10.274   1.00 32.36  ? 404 PHE   C C     1 
ATOM   6632  O  O     . PHE   B 1  404 ? -25.346 4.948   10.935   1.00 28.35  ? 404 PHE   C O     1 
ATOM   6633  C  CB    . PHE   B 1  404 ? -22.487 4.185   10.704   1.00 29.17  ? 404 PHE   C CB    1 
ATOM   6634  C  CG    . PHE   B 1  404 ? -21.170 3.557   11.153   1.00 37.49  ? 404 PHE   C CG    1 
ATOM   6635  C  CD1   . PHE   B 1  404 ? -20.748 3.636   12.476   1.00 31.28  ? 404 PHE   C CD1   1 
ATOM   6636  C  CD2   . PHE   B 1  404 ? -20.343 2.906   10.235   1.00 34.40  ? 404 PHE   C CD2   1 
ATOM   6637  C  CE1   . PHE   B 1  404 ? -19.545 3.062   12.884   1.00 33.26  ? 404 PHE   C CE1   1 
ATOM   6638  C  CE2   . PHE   B 1  404 ? -19.139 2.338   10.633   1.00 33.15  ? 404 PHE   C CE2   1 
ATOM   6639  C  CZ    . PHE   B 1  404 ? -18.734 2.424   11.954   1.00 36.47  ? 404 PHE   C CZ    1 
ATOM   6640  N  N     . VAL   B 1  405 ? -25.609 3.569   9.188    1.00 30.17  ? 405 VAL   C N     1 
ATOM   6641  C  CA    . VAL   B 1  405 ? -26.817 4.266   8.754    1.00 30.67  ? 405 VAL   C CA    1 
ATOM   6642  C  C     . VAL   B 1  405 ? -27.873 4.314   9.860    1.00 35.59  ? 405 VAL   C C     1 
ATOM   6643  O  O     . VAL   B 1  405 ? -28.717 5.223   9.882    1.00 35.18  ? 405 VAL   C O     1 
ATOM   6644  C  CB    . VAL   B 1  405 ? -27.379 3.613   7.478    1.00 31.45  ? 405 VAL   C CB    1 
ATOM   6645  C  CG1   . VAL   B 1  405 ? -28.690 4.290   7.093    1.00 29.35  ? 405 VAL   C CG1   1 
ATOM   6646  C  CG2   . VAL   B 1  405 ? -26.361 3.672   6.337    1.00 26.27  ? 405 VAL   C CG2   1 
ATOM   6647  N  N     . HIS   B 1  406 ? -27.862 3.343   10.785   1.00 35.21  ? 406 HIS   C N     1 
ATOM   6648  C  CA    . HIS   B 1  406 ? -28.896 3.304   11.822   1.00 31.27  ? 406 HIS   C CA    1 
ATOM   6649  C  C     . HIS   B 1  406 ? -28.806 4.509   12.760   1.00 32.89  ? 406 HIS   C C     1 
ATOM   6650  O  O     . HIS   B 1  406 ? -29.829 4.933   13.315   1.00 35.23  ? 406 HIS   C O     1 
ATOM   6651  C  CB    . HIS   B 1  406 ? -28.836 1.973   12.598   1.00 29.01  ? 406 HIS   C CB    1 
ATOM   6652  C  CG    . HIS   B 1  406 ? -27.665 1.839   13.525   1.00 36.26  ? 406 HIS   C CG    1 
ATOM   6653  N  ND1   . HIS   B 1  406 ? -27.782 1.973   14.893   1.00 35.57  ? 406 HIS   C ND1   1 
ATOM   6654  C  CD2   . HIS   B 1  406 ? -26.354 1.582   13.284   1.00 37.30  ? 406 HIS   C CD2   1 
ATOM   6655  C  CE1   . HIS   B 1  406 ? -26.593 1.813   15.456   1.00 33.95  ? 406 HIS   C CE1   1 
ATOM   6656  N  NE2   . HIS   B 1  406 ? -25.711 1.571   14.504   1.00 36.37  ? 406 HIS   C NE2   1 
ATOM   6657  N  N     . TRP   B 1  407 ? -27.611 5.091   12.929   1.00 34.43  ? 407 TRP   C N     1 
ATOM   6658  C  CA    . TRP   B 1  407 ? -27.491 6.310   13.724   1.00 26.24  ? 407 TRP   C CA    1 
ATOM   6659  C  C     . TRP   B 1  407 ? -28.237 7.451   13.088   1.00 27.12  ? 407 TRP   C C     1 
ATOM   6660  O  O     . TRP   B 1  407 ? -28.696 8.363   13.784   1.00 31.85  ? 407 TRP   C O     1 
ATOM   6661  C  CB    . TRP   B 1  407 ? -26.033 6.711   13.900   1.00 23.87  ? 407 TRP   C CB    1 
ATOM   6662  C  CG    . TRP   B 1  407 ? -25.297 5.771   14.780   1.00 37.05  ? 407 TRP   C CG    1 
ATOM   6663  C  CD1   . TRP   B 1  407 ? -24.349 4.878   14.399   1.00 38.96  ? 407 TRP   C CD1   1 
ATOM   6664  C  CD2   . TRP   B 1  407 ? -25.489 5.573   16.185   1.00 39.62  ? 407 TRP   C CD2   1 
ATOM   6665  N  NE1   . TRP   B 1  407 ? -23.912 4.160   15.474   1.00 38.81  ? 407 TRP   C NE1   1 
ATOM   6666  C  CE2   . TRP   B 1  407 ? -24.599 4.564   16.586   1.00 36.04  ? 407 TRP   C CE2   1 
ATOM   6667  C  CE3   . TRP   B 1  407 ? -26.326 6.151   17.141   1.00 39.39  ? 407 TRP   C CE3   1 
ATOM   6668  C  CZ2   . TRP   B 1  407 ? -24.517 4.119   17.894   1.00 34.46  ? 407 TRP   C CZ2   1 
ATOM   6669  C  CZ3   . TRP   B 1  407 ? -26.225 5.722   18.449   1.00 38.69  ? 407 TRP   C CZ3   1 
ATOM   6670  C  CH2   . TRP   B 1  407 ? -25.330 4.715   18.811   1.00 40.03  ? 407 TRP   C CH2   1 
ATOM   6671  N  N     . TYR   B 1  408 ? -28.343 7.433   11.767   1.00 31.62  ? 408 TYR   C N     1 
ATOM   6672  C  CA    . TYR   B 1  408 ? -28.998 8.526   11.074   1.00 31.36  ? 408 TYR   C CA    1 
ATOM   6673  C  C     . TYR   B 1  408 ? -30.500 8.314   11.060   1.00 31.40  ? 408 TYR   C C     1 
ATOM   6674  O  O     . TYR   B 1  408 ? -31.263 9.220   11.413   1.00 32.29  ? 408 TYR   C O     1 
ATOM   6675  C  CB    . TYR   B 1  408 ? -28.424 8.655   9.664    1.00 30.10  ? 408 TYR   C CB    1 
ATOM   6676  C  CG    . TYR   B 1  408 ? -26.978 9.083   9.678    1.00 30.45  ? 408 TYR   C CG    1 
ATOM   6677  C  CD1   . TYR   B 1  408 ? -25.966 8.163   9.917    1.00 30.06  ? 408 TYR   C CD1   1 
ATOM   6678  C  CD2   . TYR   B 1  408 ? -26.625 10.415  9.495    1.00 30.94  ? 408 TYR   C CD2   1 
ATOM   6679  C  CE1   . TYR   B 1  408 ? -24.637 8.557   9.961    1.00 34.49  ? 408 TYR   C CE1   1 
ATOM   6680  C  CE2   . TYR   B 1  408 ? -25.303 10.818  9.528    1.00 28.12  ? 408 TYR   C CE2   1 
ATOM   6681  C  CZ    . TYR   B 1  408 ? -24.314 9.888   9.754    1.00 33.61  ? 408 TYR   C CZ    1 
ATOM   6682  O  OH    . TYR   B 1  408 ? -22.998 10.277  9.785    1.00 33.77  ? 408 TYR   C OH    1 
ATOM   6683  N  N     . VAL   B 1  409 ? -30.926 7.108   10.667   1.00 30.87  ? 409 VAL   C N     1 
ATOM   6684  C  CA    . VAL   B 1  409 ? -32.346 6.760   10.636   1.00 32.29  ? 409 VAL   C CA    1 
ATOM   6685  C  C     . VAL   B 1  409 ? -32.974 6.950   12.018   1.00 36.26  ? 409 VAL   C C     1 
ATOM   6686  O  O     . VAL   B 1  409 ? -34.018 7.594   12.165   1.00 33.81  ? 409 VAL   C O     1 
ATOM   6687  C  CB    . VAL   B 1  409 ? -32.518 5.315   10.133   1.00 38.71  ? 409 VAL   C CB    1 
ATOM   6688  C  CG1   . VAL   B 1  409 ? -33.973 4.860   10.246   1.00 31.74  ? 409 VAL   C CG1   1 
ATOM   6689  C  CG2   . VAL   B 1  409 ? -31.970 5.159   8.716    1.00 24.68  ? 409 VAL   C CG2   1 
ATOM   6690  N  N     . GLY   B 1  410 ? -32.342 6.403   13.052   1.00 36.11  ? 410 GLY   C N     1 
ATOM   6691  C  CA    . GLY   B 1  410 ? -32.830 6.569   14.406   1.00 32.61  ? 410 GLY   C CA    1 
ATOM   6692  C  C     . GLY   B 1  410 ? -33.063 8.010   14.810   1.00 42.23  ? 410 GLY   C C     1 
ATOM   6693  O  O     . GLY   B 1  410 ? -33.831 8.284   15.732   1.00 46.63  ? 410 GLY   C O     1 
ATOM   6694  N  N     . GLU   B 1  411 ? -32.419 8.960   14.147   1.00 39.05  ? 411 GLU   C N     1 
ATOM   6695  C  CA    . GLU   B 1  411 ? -32.674 10.350  14.479   1.00 39.78  ? 411 GLU   C CA    1 
ATOM   6696  C  C     . GLU   B 1  411 ? -33.617 11.020  13.492   1.00 32.89  ? 411 GLU   C C     1 
ATOM   6697  O  O     . GLU   B 1  411 ? -33.746 12.242  13.525   1.00 38.42  ? 411 GLU   C O     1 
ATOM   6698  C  CB    . GLU   B 1  411 ? -31.357 11.121  14.588   1.00 37.05  ? 411 GLU   C CB    1 
ATOM   6699  C  CG    . GLU   B 1  411 ? -30.461 10.651  15.745   1.00 34.84  ? 411 GLU   C CG    1 
ATOM   6700  C  CD    . GLU   B 1  411 ? -30.700 11.405  17.055   1.00 40.24  ? 411 GLU   C CD    1 
ATOM   6701  O  OE1   . GLU   B 1  411 ? -31.687 12.158  17.161   1.00 45.14  ? 411 GLU   C OE1   1 
ATOM   6702  O  OE2   . GLU   B 1  411 ? -29.881 11.261  17.985   1.00 41.62  ? 411 GLU   C OE2   1 
ATOM   6703  N  N     . GLY   B 1  412 ? -34.279 10.253  12.623   1.00 27.24  ? 412 GLY   C N     1 
ATOM   6704  C  CA    . GLY   B 1  412 ? -35.328 10.776  11.756   1.00 37.98  ? 412 GLY   C CA    1 
ATOM   6705  C  C     . GLY   B 1  412 ? -35.075 10.702  10.254   1.00 42.09  ? 412 GLY   C C     1 
ATOM   6706  O  O     . GLY   B 1  412 ? -36.021 10.920  9.479    1.00 40.87  ? 412 GLY   C O     1 
ATOM   6707  N  N     . MET   B 1  413 ? -33.867 10.407  9.781    1.00 32.53  ? 413 MET   C N     1 
ATOM   6708  C  CA    . MET   B 1  413 ? -33.619 10.402  8.348    1.00 35.01  ? 413 MET   C CA    1 
ATOM   6709  C  C     . MET   B 1  413 ? -34.003 9.056   7.722    1.00 33.76  ? 413 MET   C C     1 
ATOM   6710  O  O     . MET   B 1  413 ? -34.009 8.012   8.379    1.00 33.04  ? 413 MET   C O     1 
ATOM   6711  C  CB    . MET   B 1  413 ? -32.146 10.721  8.060    1.00 32.43  ? 413 MET   C CB    1 
ATOM   6712  C  CG    . MET   B 1  413 ? -31.653 12.003  8.712    1.00 32.15  ? 413 MET   C CG    1 
ATOM   6713  S  SD    . MET   B 1  413 ? -29.963 12.495  8.236    1.00 30.51  ? 413 MET   C SD    1 
ATOM   6714  C  CE    . MET   B 1  413 ? -29.836 11.895  6.560    1.00 24.51  ? 413 MET   C CE    1 
ATOM   6715  N  N     . GLU   B 1  414 ? -34.299 9.099   6.424    1.00 36.20  ? 414 GLU   C N     1 
ATOM   6716  C  CA    . GLU   B 1  414 ? -34.627 7.929   5.622    1.00 34.66  ? 414 GLU   C CA    1 
ATOM   6717  C  C     . GLU   B 1  414 ? -33.444 7.552   4.732    1.00 33.81  ? 414 GLU   C C     1 
ATOM   6718  O  O     . GLU   B 1  414 ? -32.609 8.388   4.389    1.00 37.90  ? 414 GLU   C O     1 
ATOM   6719  C  CB    . GLU   B 1  414 ? -35.860 8.187   4.750    1.00 31.22  ? 414 GLU   C CB    1 
ATOM   6720  C  CG    . GLU   B 1  414 ? -37.013 8.920   5.453    1.00 37.29  ? 414 GLU   C CG    1 
ATOM   6721  C  CD    . GLU   B 1  414 ? -38.227 9.085   4.546    1.00 43.87  ? 414 GLU   C CD    1 
ATOM   6722  O  OE1   . GLU   B 1  414 ? -38.210 8.505   3.437    1.00 64.90  ? 414 GLU   C OE1   1 
ATOM   6723  O  OE2   . GLU   B 1  414 ? -39.197 9.777   4.926    1.00 42.55  ? 414 GLU   C OE2   1 
ATOM   6724  N  N     . GLU   B 1  415 ? -33.369 6.278   4.362    1.00 32.76  ? 415 GLU   C N     1 
ATOM   6725  C  CA    . GLU   B 1  415 ? -32.336 5.871   3.420    1.00 43.52  ? 415 GLU   C CA    1 
ATOM   6726  C  C     . GLU   B 1  415 ? -32.294 6.801   2.212    1.00 41.93  ? 415 GLU   C C     1 
ATOM   6727  O  O     . GLU   B 1  415 ? -31.225 7.035   1.639    1.00 42.75  ? 415 GLU   C O     1 
ATOM   6728  C  CB    . GLU   B 1  415 ? -32.565 4.418   2.963    1.00 32.68  ? 415 GLU   C CB    1 
ATOM   6729  C  CG    . GLU   B 1  415 ? -32.674 3.407   4.104    1.00 45.59  ? 415 GLU   C CG    1 
ATOM   6730  C  CD    . GLU   B 1  415 ? -31.988 2.082   3.796    1.00 52.33  ? 415 GLU   C CD    1 
ATOM   6731  O  OE1   . GLU   B 1  415 ? -32.164 1.566   2.673    1.00 50.73  ? 415 GLU   C OE1   1 
ATOM   6732  O  OE2   . GLU   B 1  415 ? -31.273 1.556   4.678    1.00 54.85  ? 415 GLU   C OE2   1 
ATOM   6733  N  N     . GLY   B 1  416 ? -33.442 7.358   1.826    1.00 41.73  ? 416 GLY   C N     1 
ATOM   6734  C  CA    . GLY   B 1  416 ? -33.556 8.048   0.556    1.00 30.36  ? 416 GLY   C CA    1 
ATOM   6735  C  C     . GLY   B 1  416 ? -32.934 9.420   0.513    1.00 38.05  ? 416 GLY   C C     1 
ATOM   6736  O  O     . GLY   B 1  416 ? -32.737 9.952   -0.585   1.00 33.82  ? 416 GLY   C O     1 
ATOM   6737  N  N     . GLU   B 1  417 ? -32.669 10.034  1.674    1.00 33.02  ? 417 GLU   C N     1 
ATOM   6738  C  CA    A GLU   B 1  417 ? -31.844 11.231  1.641    0.44 30.25  ? 417 GLU   C CA    1 
ATOM   6739  C  CA    B GLU   B 1  417 ? -31.836 11.230  1.696    0.56 30.12  ? 417 GLU   C CA    1 
ATOM   6740  C  C     . GLU   B 1  417 ? -30.380 10.879  1.402    1.00 34.10  ? 417 GLU   C C     1 
ATOM   6741  O  O     . GLU   B 1  417 ? -29.638 11.701  0.845    1.00 36.27  ? 417 GLU   C O     1 
ATOM   6742  C  CB    A GLU   B 1  417 ? -32.009 12.054  2.919    0.44 26.71  ? 417 GLU   C CB    1 
ATOM   6743  C  CB    B GLU   B 1  417 ? -31.962 11.940  3.049    0.56 26.66  ? 417 GLU   C CB    1 
ATOM   6744  C  CG    A GLU   B 1  417 ? -31.244 13.384  2.864    0.44 29.98  ? 417 GLU   C CG    1 
ATOM   6745  C  CG    B GLU   B 1  417 ? -33.380 12.324  3.450    0.56 26.64  ? 417 GLU   C CG    1 
ATOM   6746  C  CD    A GLU   B 1  417 ? -31.676 14.366  3.931    0.44 33.51  ? 417 GLU   C CD    1 
ATOM   6747  C  CD    B GLU   B 1  417 ? -33.494 12.772  4.909    0.56 31.77  ? 417 GLU   C CD    1 
ATOM   6748  O  OE1   A GLU   B 1  417 ? -32.666 14.069  4.639    0.44 33.20  ? 417 GLU   C OE1   1 
ATOM   6749  O  OE1   B GLU   B 1  417 ? -33.003 13.878  5.225    0.56 32.00  ? 417 GLU   C OE1   1 
ATOM   6750  O  OE2   A GLU   B 1  417 ? -31.029 15.432  4.066    0.44 31.26  ? 417 GLU   C OE2   1 
ATOM   6751  O  OE2   B GLU   B 1  417 ? -34.062 12.020  5.746    0.56 27.53  ? 417 GLU   C OE2   1 
ATOM   6752  N  N     . PHE   B 1  418 ? -29.957 9.660   1.778    1.00 30.52  ? 418 PHE   C N     1 
ATOM   6753  C  CA    . PHE   B 1  418 ? -28.603 9.182   1.487    1.00 29.87  ? 418 PHE   C CA    1 
ATOM   6754  C  C     . PHE   B 1  418 ? -28.403 8.968   -0.003   1.00 28.64  ? 418 PHE   C C     1 
ATOM   6755  O  O     . PHE   B 1  418 ? -27.519 9.562   -0.621   1.00 32.69  ? 418 PHE   C O     1 
ATOM   6756  C  CB    . PHE   B 1  418 ? -28.322 7.865   2.208    1.00 30.72  ? 418 PHE   C CB    1 
ATOM   6757  C  CG    . PHE   B 1  418 ? -27.785 8.018   3.581    1.00 36.97  ? 418 PHE   C CG    1 
ATOM   6758  C  CD1   . PHE   B 1  418 ? -28.641 8.191   4.661    1.00 36.18  ? 418 PHE   C CD1   1 
ATOM   6759  C  CD2   . PHE   B 1  418 ? -26.426 7.966   3.809    1.00 30.74  ? 418 PHE   C CD2   1 
ATOM   6760  C  CE1   . PHE   B 1  418 ? -28.143 8.321   5.951    1.00 30.16  ? 418 PHE   C CE1   1 
ATOM   6761  C  CE2   . PHE   B 1  418 ? -25.932 8.108   5.104    1.00 35.33  ? 418 PHE   C CE2   1 
ATOM   6762  C  CZ    . PHE   B 1  418 ? -26.802 8.283   6.170    1.00 27.80  ? 418 PHE   C CZ    1 
ATOM   6763  N  N     . SER   B 1  419 ? -29.164 8.053   -0.585   1.00 32.40  ? 419 SER   C N     1 
ATOM   6764  C  CA    . SER   B 1  419 ? -29.043 7.840   -2.017   1.00 34.29  ? 419 SER   C CA    1 
ATOM   6765  C  C     . SER   B 1  419 ? -29.227 9.155   -2.766   1.00 36.86  ? 419 SER   C C     1 
ATOM   6766  O  O     . SER   B 1  419 ? -28.534 9.420   -3.754   1.00 31.31  ? 419 SER   C O     1 
ATOM   6767  C  CB    . SER   B 1  419 ? -30.052 6.783   -2.468   1.00 26.40  ? 419 SER   C CB    1 
ATOM   6768  O  OG    . SER   B 1  419 ? -31.356 7.087   -2.004   1.00 34.73  ? 419 SER   C OG    1 
ATOM   6769  N  N     . GLU   B 1  420 ? -30.121 10.018  -2.278   1.00 32.75  ? 420 GLU   C N     1 
ATOM   6770  C  CA    . GLU   B 1  420 ? -30.291 11.318  -2.918   1.00 29.41  ? 420 GLU   C CA    1 
ATOM   6771  C  C     . GLU   B 1  420 ? -29.004 12.144  -2.855   1.00 31.60  ? 420 GLU   C C     1 
ATOM   6772  O  O     . GLU   B 1  420 ? -28.533 12.658  -3.878   1.00 30.30  ? 420 GLU   C O     1 
ATOM   6773  C  CB    . GLU   B 1  420 ? -31.462 12.060  -2.284   1.00 26.17  ? 420 GLU   C CB    1 
ATOM   6774  C  CG    . GLU   B 1  420 ? -31.786 13.370  -2.952   1.00 38.73  ? 420 GLU   C CG    1 
ATOM   6775  C  CD    . GLU   B 1  420 ? -32.851 14.149  -2.209   1.00 51.79  ? 420 GLU   C CD    1 
ATOM   6776  O  OE1   . GLU   B 1  420 ? -33.963 13.600  -2.021   1.00 49.82  ? 420 GLU   C OE1   1 
ATOM   6777  O  OE2   . GLU   B 1  420 ? -32.562 15.297  -1.803   1.00 50.51  ? 420 GLU   C OE2   1 
ATOM   6778  N  N     . ALA   B 1  421 ? -28.416 12.293  -1.666   1.00 29.11  ? 421 ALA   C N     1 
ATOM   6779  C  CA    . ALA   B 1  421 ? -27.141 13.000  -1.588   1.00 26.57  ? 421 ALA   C CA    1 
ATOM   6780  C  C     . ALA   B 1  421 ? -26.122 12.382  -2.538   1.00 31.77  ? 421 ALA   C C     1 
ATOM   6781  O  O     . ALA   B 1  421 ? -25.492 13.083  -3.335   1.00 32.51  ? 421 ALA   C O     1 
ATOM   6782  C  CB    . ALA   B 1  421 ? -26.612 12.984  -0.160   1.00 27.71  ? 421 ALA   C CB    1 
ATOM   6783  N  N     . ARG   B 1  422 ? -25.984 11.054  -2.491   1.00 27.73  ? 422 ARG   C N     1 
ATOM   6784  C  CA    . ARG   B 1  422 ? -24.984 10.362  -3.295   1.00 24.98  ? 422 ARG   C CA    1 
ATOM   6785  C  C     . ARG   B 1  422 ? -25.197 10.588  -4.797   1.00 34.92  ? 422 ARG   C C     1 
ATOM   6786  O  O     . ARG   B 1  422 ? -24.233 10.801  -5.549   1.00 33.39  ? 422 ARG   C O     1 
ATOM   6787  C  CB    . ARG   B 1  422 ? -25.016 8.876   -2.965   1.00 26.65  ? 422 ARG   C CB    1 
ATOM   6788  C  CG    . ARG   B 1  422 ? -23.981 8.061   -3.703   1.00 28.08  ? 422 ARG   C CG    1 
ATOM   6789  C  CD    . ARG   B 1  422 ? -22.601 8.462   -3.213   1.00 33.68  ? 422 ARG   C CD    1 
ATOM   6790  N  NE    . ARG   B 1  422 ? -21.543 7.795   -3.960   1.00 33.32  ? 422 ARG   C NE    1 
ATOM   6791  C  CZ    . ARG   B 1  422 ? -21.080 8.206   -5.134   1.00 32.44  ? 422 ARG   C CZ    1 
ATOM   6792  N  NH1   . ARG   B 1  422 ? -21.581 9.271   -5.745   1.00 30.55  ? 422 ARG   C NH1   1 
ATOM   6793  N  NH2   . ARG   B 1  422 ? -20.080 7.539   -5.703   1.00 30.68  ? 422 ARG   C NH2   1 
ATOM   6794  N  N     . GLU   B 1  423 ? -26.448 10.532  -5.263   1.00 26.61  ? 423 GLU   C N     1 
ATOM   6795  C  CA    . GLU   B 1  423 ? -26.696 10.792  -6.674   1.00 28.17  ? 423 GLU   C CA    1 
ATOM   6796  C  C     . GLU   B 1  423 ? -26.325 12.223  -7.042   1.00 35.57  ? 423 GLU   C C     1 
ATOM   6797  O  O     . GLU   B 1  423 ? -25.751 12.466  -8.107   1.00 30.60  ? 423 GLU   C O     1 
ATOM   6798  C  CB    . GLU   B 1  423 ? -28.151 10.505  -7.035   1.00 26.66  ? 423 GLU   C CB    1 
ATOM   6799  C  CG    . GLU   B 1  423 ? -28.266 9.283   -7.925   1.00 45.79  ? 423 GLU   C CG    1 
ATOM   6800  C  CD    . GLU   B 1  423 ? -27.204 9.281   -9.044   1.00 59.44  ? 423 GLU   C CD    1 
ATOM   6801  O  OE1   . GLU   B 1  423 ? -26.797 10.392  -9.496   1.00 44.75  ? 423 GLU   C OE1   1 
ATOM   6802  O  OE2   . GLU   B 1  423 ? -26.775 8.174   -9.470   1.00 51.57  ? 423 GLU   C OE2   1 
ATOM   6803  N  N     . ASP   B 1  424 ? -26.646 13.190  -6.184   1.00 29.36  ? 424 ASP   C N     1 
ATOM   6804  C  CA    . ASP   B 1  424 ? -26.220 14.547  -6.478   1.00 26.08  ? 424 ASP   C CA    1 
ATOM   6805  C  C     . ASP   B 1  424 ? -24.720 14.582  -6.722   1.00 34.71  ? 424 ASP   C C     1 
ATOM   6806  O  O     . ASP   B 1  424 ? -24.249 15.268  -7.645   1.00 33.62  ? 424 ASP   C O     1 
ATOM   6807  C  CB    . ASP   B 1  424 ? -26.621 15.494  -5.343   1.00 25.25  ? 424 ASP   C CB    1 
ATOM   6808  C  CG    . ASP   B 1  424 ? -26.662 16.948  -5.773   1.00 28.61  ? 424 ASP   C CG    1 
ATOM   6809  O  OD1   . ASP   B 1  424 ? -26.635 17.243  -6.989   1.00 30.85  ? 424 ASP   C OD1   1 
ATOM   6810  O  OD2   . ASP   B 1  424 ? -26.725 17.817  -4.876   1.00 39.09  ? 424 ASP   C OD2   1 
ATOM   6811  N  N     . MET   B 1  425 ? -23.954 13.801  -5.934   1.00 30.21  ? 425 MET   C N     1 
ATOM   6812  C  CA    . MET   B 1  425 ? -22.499 13.804  -6.077   1.00 27.13  ? 425 MET   C CA    1 
ATOM   6813  C  C     . MET   B 1  425 ? -22.055 13.098  -7.354   1.00 27.30  ? 425 MET   C C     1 
ATOM   6814  O  O     . MET   B 1  425 ? -21.067 13.503  -7.969   1.00 29.63  ? 425 MET   C O     1 
ATOM   6815  C  CB    . MET   B 1  425 ? -21.834 13.158  -4.859   1.00 26.08  ? 425 MET   C CB    1 
ATOM   6816  C  CG    . MET   B 1  425 ? -22.035 13.869  -3.532   1.00 21.66  ? 425 MET   C CG    1 
ATOM   6817  S  SD    . MET   B 1  425 ? -21.447 15.557  -3.417   1.00 32.56  ? 425 MET   C SD    1 
ATOM   6818  C  CE    . MET   B 1  425 ? -19.703 15.375  -3.852   1.00 21.86  ? 425 MET   C CE    1 
ATOM   6819  N  N     . ALA   B 1  426 ? -22.758 12.046  -7.773   1.00 27.57  ? 426 ALA   C N     1 
ATOM   6820  C  CA    . ALA   B 1  426 ? -22.431 11.419  -9.053   1.00 25.24  ? 426 ALA   C CA    1 
ATOM   6821  C  C     . ALA   B 1  426 ? -22.566 12.423  -10.189  1.00 29.88  ? 426 ALA   C C     1 
ATOM   6822  O  O     . ALA   B 1  426 ? -21.693 12.520  -11.063  1.00 31.67  ? 426 ALA   C O     1 
ATOM   6823  C  CB    . ALA   B 1  426 ? -23.332 10.204  -9.310   1.00 18.17  ? 426 ALA   C CB    1 
ATOM   6824  N  N     . ALA   B 1  427 ? -23.671 13.179  -10.185  1.00 26.21  ? 427 ALA   C N     1 
ATOM   6825  C  CA    . ALA   B 1  427 ? -23.892 14.220  -11.178  1.00 26.51  ? 427 ALA   C CA    1 
ATOM   6826  C  C     . ALA   B 1  427 ? -22.799 15.273  -11.109  1.00 29.20  ? 427 ALA   C C     1 
ATOM   6827  O  O     . ALA   B 1  427 ? -22.281 15.707  -12.138  1.00 29.56  ? 427 ALA   C O     1 
ATOM   6828  C  CB    . ALA   B 1  427 ? -25.270 14.853  -10.975  1.00 16.10  ? 427 ALA   C CB    1 
ATOM   6829  N  N     . LEU   B 1  428 ? -22.412 15.676  -9.904   1.00 26.09  ? 428 LEU   C N     1 
ATOM   6830  C  CA    . LEU   B 1  428 ? -21.363 16.671  -9.801   1.00 25.99  ? 428 LEU   C CA    1 
ATOM   6831  C  C     . LEU   B 1  428 ? -20.037 16.118  -10.327  1.00 29.46  ? 428 LEU   C C     1 
ATOM   6832  O  O     . LEU   B 1  428 ? -19.246 16.841  -10.951  1.00 28.30  ? 428 LEU   C O     1 
ATOM   6833  C  CB    . LEU   B 1  428 ? -21.264 17.154  -8.355   1.00 23.39  ? 428 LEU   C CB    1 
ATOM   6834  C  CG    . LEU   B 1  428 ? -20.301 18.310  -8.122   1.00 25.64  ? 428 LEU   C CG    1 
ATOM   6835  C  CD1   . LEU   B 1  428 ? -20.802 19.560  -8.810   1.00 26.05  ? 428 LEU   C CD1   1 
ATOM   6836  C  CD2   . LEU   B 1  428 ? -20.023 18.534  -6.643   1.00 19.77  ? 428 LEU   C CD2   1 
ATOM   6837  N  N     . GLU   B 1  429 ? -19.769 14.839  -10.102  1.00 29.49  ? 429 GLU   C N     1 
ATOM   6838  C  CA    . GLU   B 1  429 ? -18.570 14.275  -10.708  1.00 30.28  ? 429 GLU   C CA    1 
ATOM   6839  C  C     . GLU   B 1  429 ? -18.730 14.215  -12.212  1.00 26.85  ? 429 GLU   C C     1 
ATOM   6840  O  O     . GLU   B 1  429 ? -17.785 14.497  -12.951  1.00 34.83  ? 429 GLU   C O     1 
ATOM   6841  C  CB    . GLU   B 1  429 ? -18.258 12.886  -10.138  1.00 34.71  ? 429 GLU   C CB    1 
ATOM   6842  C  CG    . GLU   B 1  429 ? -17.725 12.901  -8.710   1.00 32.47  ? 429 GLU   C CG    1 
ATOM   6843  C  CD    . GLU   B 1  429 ? -17.252 11.539  -8.275   1.00 40.81  ? 429 GLU   C CD    1 
ATOM   6844  O  OE1   . GLU   B 1  429 ? -16.328 10.998  -8.928   1.00 40.53  ? 429 GLU   C OE1   1 
ATOM   6845  O  OE2   . GLU   B 1  429 ? -17.816 10.995  -7.300   1.00 36.65  ? 429 GLU   C OE2   1 
ATOM   6846  N  N     . LYS   B 1  430 ? -19.934 13.893  -12.685  1.00 31.92  ? 430 LYS   C N     1 
ATOM   6847  C  CA    . LYS   B 1  430 ? -20.195 13.936  -14.124  1.00 35.01  ? 430 LYS   C CA    1 
ATOM   6848  C  C     . LYS   B 1  430 ? -20.099 15.366  -14.683  1.00 38.82  ? 430 LYS   C C     1 
ATOM   6849  O  O     . LYS   B 1  430 ? -19.671 15.549  -15.833  1.00 36.28  ? 430 LYS   C O     1 
ATOM   6850  C  CB    . LYS   B 1  430 ? -21.561 13.305  -14.422  1.00 36.74  ? 430 LYS   C CB    1 
ATOM   6851  C  CG    . LYS   B 1  430 ? -22.059 13.438  -15.861  1.00 42.74  ? 430 LYS   C CG    1 
ATOM   6852  C  CD    . LYS   B 1  430 ? -21.705 12.204  -16.693  1.00 58.80  ? 430 LYS   C CD    1 
ATOM   6853  C  CE    . LYS   B 1  430 ? -21.985 12.433  -18.178  1.00 57.26  ? 430 LYS   C CE    1 
ATOM   6854  N  NZ    . LYS   B 1  430 ? -21.547 11.281  -19.026  1.00 65.23  ? 430 LYS   C NZ    1 
ATOM   6855  N  N     . ASP   B 1  431 ? -20.451 16.395  -13.889  1.00 25.52  ? 431 ASP   C N     1 
ATOM   6856  C  CA    . ASP   B 1  431 ? -20.314 17.757  -14.395  1.00 26.21  ? 431 ASP   C CA    1 
ATOM   6857  C  C     . ASP   B 1  431 ? -18.849 18.152  -14.556  1.00 30.96  ? 431 ASP   C C     1 
ATOM   6858  O  O     . ASP   B 1  431 ? -18.491 18.854  -15.515  1.00 25.73  ? 431 ASP   C O     1 
ATOM   6859  C  CB    . ASP   B 1  431 ? -21.007 18.763  -13.483  1.00 24.38  ? 431 ASP   C CB    1 
ATOM   6860  C  CG    . ASP   B 1  431 ? -22.457 18.478  -13.300  1.00 25.59  ? 431 ASP   C CG    1 
ATOM   6861  O  OD1   . ASP   B 1  431 ? -23.079 17.911  -14.217  1.00 33.28  ? 431 ASP   C OD1   1 
ATOM   6862  O  OD2   . ASP   B 1  431 ? -22.968 18.826  -12.213  1.00 36.25  ? 431 ASP   C OD2   1 
ATOM   6863  N  N     . TYR   B 1  432 ? -17.988 17.758  -13.610  1.00 25.20  ? 432 TYR   C N     1 
ATOM   6864  C  CA    . TYR   B 1  432 ? -16.594 18.144  -13.762  1.00 26.38  ? 432 TYR   C CA    1 
ATOM   6865  C  C     . TYR   B 1  432 ? -15.973 17.445  -14.959  1.00 28.44  ? 432 TYR   C C     1 
ATOM   6866  O  O     . TYR   B 1  432 ? -15.035 17.970  -15.559  1.00 34.80  ? 432 TYR   C O     1 
ATOM   6867  C  CB    . TYR   B 1  432 ? -15.826 17.875  -12.461  1.00 37.21  ? 432 TYR   C CB    1 
ATOM   6868  C  CG    . TYR   B 1  432 ? -16.000 19.014  -11.477  1.00 33.34  ? 432 TYR   C CG    1 
ATOM   6869  C  CD1   . TYR   B 1  432 ? -15.169 20.125  -11.536  1.00 26.84  ? 432 TYR   C CD1   1 
ATOM   6870  C  CD2   . TYR   B 1  432 ? -17.024 19.006  -10.535  1.00 24.96  ? 432 TYR   C CD2   1 
ATOM   6871  C  CE1   . TYR   B 1  432 ? -15.337 21.181  -10.702  1.00 29.56  ? 432 TYR   C CE1   1 
ATOM   6872  C  CE2   . TYR   B 1  432 ? -17.193 20.074  -9.682   1.00 27.80  ? 432 TYR   C CE2   1 
ATOM   6873  C  CZ    . TYR   B 1  432 ? -16.345 21.163  -9.776   1.00 28.30  ? 432 TYR   C CZ    1 
ATOM   6874  O  OH    . TYR   B 1  432 ? -16.474 22.251  -8.946   1.00 33.79  ? 432 TYR   C OH    1 
ATOM   6875  N  N     . GLU   B 1  433 ? -16.522 16.301  -15.343  1.00 29.75  ? 433 GLU   C N     1 
ATOM   6876  C  CA    . GLU   B 1  433 ? -16.137 15.632  -16.579  1.00 31.84  ? 433 GLU   C CA    1 
ATOM   6877  C  C     . GLU   B 1  433 ? -16.592 16.434  -17.795  1.00 33.84  ? 433 GLU   C C     1 
ATOM   6878  O  O     . GLU   B 1  433 ? -15.808 16.699  -18.717  1.00 34.34  ? 433 GLU   C O     1 
ATOM   6879  C  CB    . GLU   B 1  433 ? -16.760 14.232  -16.595  1.00 27.84  ? 433 GLU   C CB    1 
ATOM   6880  C  CG    . GLU   B 1  433 ? -15.852 13.094  -16.964  1.00 49.61  ? 433 GLU   C CG    1 
ATOM   6881  C  CD    . GLU   B 1  433 ? -16.545 11.738  -16.780  1.00 64.38  ? 433 GLU   C CD    1 
ATOM   6882  O  OE1   . GLU   B 1  433 ? -17.586 11.496  -17.437  1.00 58.45  ? 433 GLU   C OE1   1 
ATOM   6883  O  OE2   . GLU   B 1  433 ? -16.057 10.928  -15.955  1.00 67.94  ? 433 GLU   C OE2   1 
ATOM   6884  N  N     . GLU   B 1  434 ? -17.867 16.824  -17.811  1.00 32.91  ? 434 GLU   C N     1 
ATOM   6885  C  CA    . GLU   B 1  434 ? -18.433 17.442  -19.000  1.00 29.73  ? 434 GLU   C CA    1 
ATOM   6886  C  C     . GLU   B 1  434 ? -17.720 18.742  -19.335  1.00 32.14  ? 434 GLU   C C     1 
ATOM   6887  O  O     . GLU   B 1  434 ? -17.407 19.000  -20.502  1.00 33.46  ? 434 GLU   C O     1 
ATOM   6888  C  CB    . GLU   B 1  434 ? -19.940 17.655  -18.814  1.00 26.87  ? 434 GLU   C CB    1 
ATOM   6889  C  CG    . GLU   B 1  434 ? -20.750 16.391  -19.170  1.00 40.95  ? 434 GLU   C CG    1 
ATOM   6890  C  CD    . GLU   B 1  434 ? -22.208 16.392  -18.676  1.00 51.04  ? 434 GLU   C CD    1 
ATOM   6891  O  OE1   . GLU   B 1  434 ? -22.809 17.480  -18.481  1.00 44.61  ? 434 GLU   C OE1   1 
ATOM   6892  O  OE2   . GLU   B 1  434 ? -22.751 15.278  -18.481  1.00 51.17  ? 434 GLU   C OE2   1 
ATOM   6893  N  N     . VAL   B 1  435 ? -17.422 19.565  -18.331  1.00 28.13  ? 435 VAL   C N     1 
ATOM   6894  C  CA    . VAL   B 1  435 ? -16.805 20.846  -18.645  1.00 32.71  ? 435 VAL   C CA    1 
ATOM   6895  C  C     . VAL   B 1  435 ? -15.425 20.694  -19.283  1.00 31.25  ? 435 VAL   C C     1 
ATOM   6896  O  O     . VAL   B 1  435 ? -14.978 21.585  -20.013  1.00 32.89  ? 435 VAL   C O     1 
ATOM   6897  C  CB    . VAL   B 1  435 ? -16.756 21.705  -17.379  1.00 27.40  ? 435 VAL   C CB    1 
ATOM   6898  C  CG1   . VAL   B 1  435 ? -18.146 22.245  -17.047  1.00 29.46  ? 435 VAL   C CG1   1 
ATOM   6899  C  CG2   . VAL   B 1  435 ? -16.205 20.888  -16.209  1.00 37.11  ? 435 VAL   C CG2   1 
ATOM   6900  N  N     . GLY   B 1  436 ? -14.744 19.574  -19.049  1.00 29.47  ? 436 GLY   C N     1 
ATOM   6901  C  CA    . GLY   B 1  436 ? -13.410 19.399  -19.584  1.00 29.07  ? 436 GLY   C CA    1 
ATOM   6902  C  C     . GLY   B 1  436 ? -13.369 18.903  -21.010  1.00 41.46  ? 436 GLY   C C     1 
ATOM   6903  O  O     . GLY   B 1  436 ? -12.361 19.113  -21.696  1.00 48.27  ? 436 GLY   C O     1 
ATOM   6904  N  N     . VAL   B 1  437 ? -14.433 18.239  -21.468  1.00 33.28  ? 437 VAL   C N     1 
ATOM   6905  C  CA    . VAL   B 1  437 ? -14.480 17.765  -22.843  1.00 29.23  ? 437 VAL   C CA    1 
ATOM   6906  C  C     . VAL   B 1  437 ? -14.435 18.947  -23.798  1.00 33.57  ? 437 VAL   C C     1 
ATOM   6907  O  O     . VAL   B 1  437 ? -15.101 19.967  -23.584  1.00 36.65  ? 437 VAL   C O     1 
ATOM   6908  C  CB    . VAL   B 1  437 ? -15.750 16.929  -23.076  1.00 37.56  ? 437 VAL   C CB    1 
ATOM   6909  C  CG1   . VAL   B 1  437 ? -15.733 16.311  -24.471  1.00 34.73  ? 437 VAL   C CG1   1 
ATOM   6910  C  CG2   . VAL   B 1  437 ? -15.908 15.843  -22.010  1.00 33.13  ? 437 VAL   C CG2   1 
ATOM   6911  N  N     . ASP   B 1  438 ? -13.655 18.802  -24.870  1.00 37.55  ? 438 ASP   C N     1 
ATOM   6912  C  CA    . ASP   B 1  438 ? -13.541 19.832  -25.891  1.00 36.27  ? 438 ASP   C CA    1 
ATOM   6913  C  C     . ASP   B 1  438 ? -14.836 19.993  -26.666  1.00 45.01  ? 438 ASP   C C     1 
ATOM   6914  O  O     . ASP   B 1  438 ? -15.485 19.007  -27.024  1.00 40.79  ? 438 ASP   C O     1 
ATOM   6915  C  CB    . ASP   B 1  438 ? -12.430 19.488  -26.868  1.00 35.91  ? 438 ASP   C CB    1 
ATOM   6916  C  CG    . ASP   B 1  438 ? -11.060 19.571  -26.240  1.00 49.84  ? 438 ASP   C CG    1 
ATOM   6917  O  OD1   . ASP   B 1  438 ? -10.837 20.481  -25.415  1.00 53.37  ? 438 ASP   C OD1   1 
ATOM   6918  O  OD2   . ASP   B 1  438 ? -10.204 18.723  -26.569  1.00 67.62  ? 438 ASP   C OD2   1 
ATOM   6919  N  N     . SER   B 1  439 ? -15.182 21.244  -26.974  1.00 44.57  ? 439 SER   C N     1 
ATOM   6920  C  CA    . SER   B 1  439 ? -16.408 21.519  -27.715  1.00 46.51  ? 439 SER   C CA    1 
ATOM   6921  C  C     . SER   B 1  439 ? -16.375 20.890  -29.107  1.00 54.79  ? 439 SER   C C     1 
ATOM   6922  O  O     . SER   B 1  439 ? -15.315 20.555  -29.650  1.00 50.24  ? 439 SER   C O     1 
ATOM   6923  C  CB    . SER   B 1  439 ? -16.630 23.023  -27.826  1.00 41.48  ? 439 SER   C CB    1 
ATOM   6924  O  OG    . SER   B 1  439 ? -16.497 23.638  -26.550  1.00 45.72  ? 439 SER   C OG    1 
ATOM   6925  N  N     . VAL   B 1  440 ? -17.562 20.744  -29.697  1.00 65.51  ? 440 VAL   C N     1 
ATOM   6926  C  CA    . VAL   B 1  440 ? -17.688 20.130  -31.027  1.00 75.16  ? 440 VAL   C CA    1 
ATOM   6927  C  C     . VAL   B 1  440 ? -17.779 21.184  -32.134  1.00 74.37  ? 440 VAL   C C     1 
ATOM   6928  O  O     . VAL   B 1  440 ? -17.968 20.856  -33.312  1.00 78.58  ? 440 VAL   C O     1 
ATOM   6929  C  CB    . VAL   B 1  440 ? -18.907 19.186  -31.100  1.00 67.77  ? 440 VAL   C CB    1 
ATOM   6930  C  CG1   . VAL   B 1  440 ? -18.928 18.225  -29.901  1.00 52.16  ? 440 VAL   C CG1   1 
ATOM   6931  C  CG2   . VAL   B 1  440 ? -20.207 19.995  -31.215  1.00 56.68  ? 440 VAL   C CG2   1 
ATOM   6932  N  N     . MET   C 2  1   ? -22.172 20.689  30.043   1.00 73.37  ? 1   MET   D N     1 
ATOM   6933  C  CA    . MET   C 2  1   ? -21.342 19.505  30.262   1.00 76.68  ? 1   MET   D CA    1 
ATOM   6934  C  C     . MET   C 2  1   ? -22.160 18.213  30.236   1.00 75.38  ? 1   MET   D C     1 
ATOM   6935  O  O     . MET   C 2  1   ? -23.320 18.206  29.810   1.00 76.80  ? 1   MET   D O     1 
ATOM   6936  C  CB    . MET   C 2  1   ? -20.591 19.610  31.591   1.00 78.36  ? 1   MET   D CB    1 
ATOM   6937  C  CG    . MET   C 2  1   ? -21.490 19.673  32.800   1.00 66.06  ? 1   MET   D CG    1 
ATOM   6938  S  SD    . MET   C 2  1   ? -20.661 20.499  34.154   1.00 92.94  ? 1   MET   D SD    1 
ATOM   6939  C  CE    . MET   C 2  1   ? -21.989 20.608  35.362   1.00 89.77  ? 1   MET   D CE    1 
ATOM   6940  N  N     . ARG   C 2  2   ? -21.550 17.123  30.705   1.00 60.78  ? 2   ARG   D N     1 
ATOM   6941  C  CA    . ARG   C 2  2   ? -22.095 15.793  30.518   1.00 47.50  ? 2   ARG   D CA    1 
ATOM   6942  C  C     . ARG   C 2  2   ? -21.795 14.953  31.748   1.00 59.82  ? 2   ARG   D C     1 
ATOM   6943  O  O     . ARG   C 2  2   ? -20.683 14.986  32.282   1.00 55.96  ? 2   ARG   D O     1 
ATOM   6944  C  CB    . ARG   C 2  2   ? -21.502 15.139  29.268   1.00 44.10  ? 2   ARG   D CB    1 
ATOM   6945  C  CG    . ARG   C 2  2   ? -21.383 16.064  28.054   1.00 52.03  ? 2   ARG   D CG    1 
ATOM   6946  C  CD    . ARG   C 2  2   ? -22.740 16.396  27.422   1.00 50.76  ? 2   ARG   D CD    1 
ATOM   6947  N  NE    . ARG   C 2  2   ? -23.483 15.177  27.135   1.00 63.11  ? 2   ARG   D NE    1 
ATOM   6948  C  CZ    . ARG   C 2  2   ? -23.356 14.467  26.023   1.00 54.16  ? 2   ARG   D CZ    1 
ATOM   6949  N  NH1   . ARG   C 2  2   ? -22.564 14.867  25.043   1.00 53.13  ? 2   ARG   D NH1   1 
ATOM   6950  N  NH2   . ARG   C 2  2   ? -24.038 13.328  25.893   1.00 42.02  ? 2   ARG   D NH2   1 
ATOM   6951  N  N     . GLU   C 2  3   ? -22.794 14.205  32.201   1.00 62.90  ? 3   GLU   D N     1 
ATOM   6952  C  CA    . GLU   C 2  3   ? -22.683 13.405  33.411   1.00 53.16  ? 3   GLU   D CA    1 
ATOM   6953  C  C     . GLU   C 2  3   ? -23.001 11.957  33.091   1.00 51.50  ? 3   GLU   D C     1 
ATOM   6954  O  O     . GLU   C 2  3   ? -23.867 11.664  32.254   1.00 50.51  ? 3   GLU   D O     1 
ATOM   6955  C  CB    . GLU   C 2  3   ? -23.630 13.889  34.516   1.00 50.98  ? 3   GLU   D CB    1 
ATOM   6956  C  CG    . GLU   C 2  3   ? -23.383 15.302  34.993   1.00 53.22  ? 3   GLU   D CG    1 
ATOM   6957  C  CD    . GLU   C 2  3   ? -24.043 16.356  34.123   1.00 55.99  ? 3   GLU   D CD    1 
ATOM   6958  O  OE1   . GLU   C 2  3   ? -24.796 16.004  33.189   1.00 52.88  ? 3   GLU   D OE1   1 
ATOM   6959  O  OE2   . GLU   C 2  3   ? -23.801 17.552  34.378   1.00 65.81  ? 3   GLU   D OE2   1 
ATOM   6960  N  N     . ILE   C 2  4   ? -22.301 11.060  33.766   1.00 48.89  ? 4   ILE   D N     1 
ATOM   6961  C  CA    . ILE   C 2  4   ? -22.577 9.638   33.687   1.00 47.93  ? 4   ILE   D CA    1 
ATOM   6962  C  C     . ILE   C 2  4   ? -23.041 9.178   35.062   1.00 44.39  ? 4   ILE   D C     1 
ATOM   6963  O  O     . ILE   C 2  4   ? -22.523 9.633   36.088   1.00 46.41  ? 4   ILE   D O     1 
ATOM   6964  C  CB    . ILE   C 2  4   ? -21.346 8.856   33.186   1.00 45.09  ? 4   ILE   D CB    1 
ATOM   6965  C  CG1   . ILE   C 2  4   ? -20.839 9.495   31.875   1.00 47.04  ? 4   ILE   D CG1   1 
ATOM   6966  C  CG2   . ILE   C 2  4   ? -21.712 7.395   32.976   1.00 46.70  ? 4   ILE   D CG2   1 
ATOM   6967  C  CD1   . ILE   C 2  4   ? -19.589 8.842   31.257   1.00 43.02  ? 4   ILE   D CD1   1 
ATOM   6968  N  N     . VAL   C 2  5   ? -24.068 8.335   35.074   1.00 34.56  ? 5   VAL   D N     1 
ATOM   6969  C  CA    . VAL   C 2  5   ? -24.651 7.796   36.291   1.00 40.96  ? 5   VAL   D CA    1 
ATOM   6970  C  C     . VAL   C 2  5   ? -24.243 6.333   36.362   1.00 38.80  ? 5   VAL   D C     1 
ATOM   6971  O  O     . VAL   C 2  5   ? -24.598 5.548   35.476   1.00 37.36  ? 5   VAL   D O     1 
ATOM   6972  C  CB    . VAL   C 2  5   ? -26.181 7.959   36.306   1.00 48.81  ? 5   VAL   D CB    1 
ATOM   6973  C  CG1   . VAL   C 2  5   ? -26.826 7.128   37.425   1.00 41.88  ? 5   VAL   D CG1   1 
ATOM   6974  C  CG2   . VAL   C 2  5   ? -26.555 9.412   36.452   1.00 42.42  ? 5   VAL   D CG2   1 
ATOM   6975  N  N     . HIS   C 2  6   ? -23.492 5.972   37.407   1.00 39.68  ? 6   HIS   D N     1 
ATOM   6976  C  CA    . HIS   C 2  6   ? -22.966 4.619   37.561   1.00 42.81  ? 6   HIS   D CA    1 
ATOM   6977  C  C     . HIS   C 2  6   ? -23.898 3.744   38.396   1.00 43.56  ? 6   HIS   D C     1 
ATOM   6978  O  O     . HIS   C 2  6   ? -24.331 4.146   39.480   1.00 46.76  ? 6   HIS   D O     1 
ATOM   6979  C  CB    . HIS   C 2  6   ? -21.584 4.645   38.213   1.00 46.76  ? 6   HIS   D CB    1 
ATOM   6980  C  CG    . HIS   C 2  6   ? -21.051 3.281   38.526   1.00 52.12  ? 6   HIS   D CG    1 
ATOM   6981  N  ND1   . HIS   C 2  6   ? -20.455 2.478   37.576   1.00 52.54  ? 6   HIS   D ND1   1 
ATOM   6982  C  CD2   . HIS   C 2  6   ? -21.060 2.563   39.676   1.00 51.82  ? 6   HIS   D CD2   1 
ATOM   6983  C  CE1   . HIS   C 2  6   ? -20.114 1.328   38.129   1.00 54.27  ? 6   HIS   D CE1   1 
ATOM   6984  N  NE2   . HIS   C 2  6   ? -20.463 1.356   39.405   1.00 50.67  ? 6   HIS   D NE2   1 
ATOM   6985  N  N     . ILE   C 2  7   ? -24.158 2.531   37.913   1.00 39.18  ? 7   ILE   D N     1 
ATOM   6986  C  CA    . ILE   C 2  7   ? -25.037 1.580   38.582   1.00 45.36  ? 7   ILE   D CA    1 
ATOM   6987  C  C     . ILE   C 2  7   ? -24.325 0.236   38.602   1.00 51.30  ? 7   ILE   D C     1 
ATOM   6988  O  O     . ILE   C 2  7   ? -24.118 -0.375  37.549   1.00 49.22  ? 7   ILE   D O     1 
ATOM   6989  C  CB    . ILE   C 2  7   ? -26.406 1.461   37.899   1.00 40.60  ? 7   ILE   D CB    1 
ATOM   6990  C  CG1   . ILE   C 2  7   ? -27.205 2.755   38.079   1.00 43.75  ? 7   ILE   D CG1   1 
ATOM   6991  C  CG2   . ILE   C 2  7   ? -27.170 0.274   38.449   1.00 34.59  ? 7   ILE   D CG2   1 
ATOM   6992  C  CD1   . ILE   C 2  7   ? -28.596 2.700   37.474   1.00 40.28  ? 7   ILE   D CD1   1 
ATOM   6993  N  N     . GLN   C 2  8   ? -23.955 -0.223  39.796   1.00 50.20  ? 8   GLN   D N     1 
ATOM   6994  C  CA    . GLN   C 2  8   ? -23.266 -1.490  39.998   1.00 50.09  ? 8   GLN   D CA    1 
ATOM   6995  C  C     . GLN   C 2  8   ? -24.170 -2.428  40.788   1.00 51.87  ? 8   GLN   D C     1 
ATOM   6996  O  O     . GLN   C 2  8   ? -24.668 -2.068  41.859   1.00 55.16  ? 8   GLN   D O     1 
ATOM   6997  C  CB    . GLN   C 2  8   ? -21.948 -1.274  40.739   1.00 52.80  ? 8   GLN   D CB    1 
ATOM   6998  C  CG    . GLN   C 2  8   ? -22.131 -0.910  42.196   1.00 49.77  ? 8   GLN   D CG    1 
ATOM   6999  C  CD    . GLN   C 2  8   ? -20.906 -0.273  42.780   1.00 54.62  ? 8   GLN   D CD    1 
ATOM   7000  O  OE1   . GLN   C 2  8   ? -20.300 0.602   42.153   1.00 58.26  ? 8   GLN   D OE1   1 
ATOM   7001  N  NE2   . GLN   C 2  8   ? -20.519 -0.704  43.988   1.00 54.59  ? 8   GLN   D NE2   1 
ATOM   7002  N  N     . ALA   C 2  9   ? -24.383 -3.623  40.267   1.00 51.74  ? 9   ALA   D N     1 
ATOM   7003  C  CA    . ALA   C 2  9   ? -25.420 -4.491  40.788   1.00 47.18  ? 9   ALA   D CA    1 
ATOM   7004  C  C     . ALA   C 2  9   ? -24.854 -5.869  41.094   1.00 54.11  ? 9   ALA   D C     1 
ATOM   7005  O  O     . ALA   C 2  9   ? -24.003 -6.383  40.357   1.00 49.76  ? 9   ALA   D O     1 
ATOM   7006  C  CB    . ALA   C 2  9   ? -26.569 -4.589  39.795   1.00 45.91  ? 9   ALA   D CB    1 
ATOM   7007  N  N     . GLY   C 2  10  ? -25.331 -6.462  42.197   1.00 55.14  ? 10  GLY   D N     1 
ATOM   7008  C  CA    . GLY   C 2  10  ? -24.921 -7.794  42.590   1.00 46.70  ? 10  GLY   D CA    1 
ATOM   7009  C  C     . GLY   C 2  10  ? -23.541 -7.829  43.224   1.00 54.05  ? 10  GLY   D C     1 
ATOM   7010  O  O     . GLY   C 2  10  ? -22.856 -6.810  43.426   1.00 45.50  ? 10  GLY   D O     1 
ATOM   7011  N  N     . GLN   C 2  11  ? -23.131 -9.051  43.565   1.00 55.90  ? 11  GLN   D N     1 
ATOM   7012  C  CA    . GLN   C 2  11  ? -21.799 -9.241  44.123   1.00 57.80  ? 11  GLN   D CA    1 
ATOM   7013  C  C     . GLN   C 2  11  ? -20.744 -8.787  43.124   1.00 58.81  ? 11  GLN   D C     1 
ATOM   7014  O  O     . GLN   C 2  11  ? -20.008 -7.822  43.368   1.00 54.42  ? 11  GLN   D O     1 
ATOM   7015  C  CB    . GLN   C 2  11  ? -21.602 -10.711 44.505   1.00 59.88  ? 11  GLN   D CB    1 
ATOM   7016  C  CG    . GLN   C 2  11  ? -20.194 -11.083 44.959   1.00 56.51  ? 11  GLN   D CG    1 
ATOM   7017  C  CD    . GLN   C 2  11  ? -20.014 -12.599 45.106   1.00 67.05  ? 11  GLN   D CD    1 
ATOM   7018  O  OE1   . GLN   C 2  11  ? -20.907 -13.389 44.761   1.00 62.95  ? 11  GLN   D OE1   1 
ATOM   7019  N  NE2   . GLN   C 2  11  ? -18.852 -13.008 45.613   1.00 67.43  ? 11  GLN   D NE2   1 
ATOM   7020  N  N     . CYS   C 2  12  ? -20.698 -9.449  41.963   1.00 57.42  ? 12  CYS   D N     1 
ATOM   7021  C  CA    . CYS   C 2  12  ? -19.657 -9.178  40.976   1.00 58.51  ? 12  CYS   D CA    1 
ATOM   7022  C  C     . CYS   C 2  12  ? -19.590 -7.698  40.630   1.00 50.35  ? 12  CYS   D C     1 
ATOM   7023  O  O     . CYS   C 2  12  ? -18.509 -7.097  40.626   1.00 48.19  ? 12  CYS   D O     1 
ATOM   7024  C  CB    . CYS   C 2  12  ? -19.895 -10.018 39.716   1.00 58.00  ? 12  CYS   D CB    1 
ATOM   7025  S  SG    . CYS   C 2  12  ? -18.688 -9.739  38.377   1.00 58.07  ? 12  CYS   D SG    1 
ATOM   7026  N  N     . GLY   C 2  13  ? -20.742 -7.095  40.332   1.00 50.34  ? 13  GLY   D N     1 
ATOM   7027  C  CA    . GLY   C 2  13  ? -20.752 -5.699  39.930   1.00 48.67  ? 13  GLY   D CA    1 
ATOM   7028  C  C     . GLY   C 2  13  ? -20.242 -4.761  41.010   1.00 52.00  ? 13  GLY   D C     1 
ATOM   7029  O  O     . GLY   C 2  13  ? -19.554 -3.778  40.714   1.00 49.57  ? 13  GLY   D O     1 
ATOM   7030  N  N     . ASN   C 2  14  ? -20.583 -5.040  42.277   1.00 48.24  ? 14  ASN   D N     1 
ATOM   7031  C  CA    . ASN   C 2  14  ? -20.132 -4.166  43.354   1.00 52.10  ? 14  ASN   D CA    1 
ATOM   7032  C  C     . ASN   C 2  14  ? -18.643 -4.355  43.637   1.00 55.56  ? 14  ASN   D C     1 
ATOM   7033  O  O     . ASN   C 2  14  ? -17.950 -3.394  44.016   1.00 46.01  ? 14  ASN   D O     1 
ATOM   7034  C  CB    . ASN   C 2  14  ? -20.975 -4.404  44.606   1.00 51.30  ? 14  ASN   D CB    1 
ATOM   7035  C  CG    . ASN   C 2  14  ? -22.305 -3.657  44.568   1.00 47.88  ? 14  ASN   D CG    1 
ATOM   7036  O  OD1   . ASN   C 2  14  ? -22.360 -2.456  44.828   1.00 41.95  ? 14  ASN   D OD1   1 
ATOM   7037  N  ND2   . ASN   C 2  14  ? -23.380 -4.370  44.250   1.00 44.16  ? 14  ASN   D ND2   1 
ATOM   7038  N  N     . GLN   C 2  15  ? -18.137 -5.577  43.442   1.00 52.29  ? 15  GLN   D N     1 
ATOM   7039  C  CA    . GLN   C 2  15  ? -16.700 -5.827  43.532   1.00 65.44  ? 15  GLN   D CA    1 
ATOM   7040  C  C     . GLN   C 2  15  ? -15.931 -4.988  42.509   1.00 58.09  ? 15  GLN   D C     1 
ATOM   7041  O  O     . GLN   C 2  15  ? -15.099 -4.144  42.872   1.00 52.02  ? 15  GLN   D O     1 
ATOM   7042  C  CB    . GLN   C 2  15  ? -16.421 -7.320  43.330   1.00 70.03  ? 15  GLN   D CB    1 
ATOM   7043  C  CG    . GLN   C 2  15  ? -17.396 -8.262  44.049   1.00 72.36  ? 15  GLN   D CG    1 
ATOM   7044  C  CD    . GLN   C 2  15  ? -17.027 -8.497  45.500   1.00 71.56  ? 15  GLN   D CD    1 
ATOM   7045  O  OE1   . GLN   C 2  15  ? -17.630 -9.341  46.174   1.00 64.84  ? 15  GLN   D OE1   1 
ATOM   7046  N  NE2   . GLN   C 2  15  ? -16.032 -7.748  45.992   1.00 61.24  ? 15  GLN   D NE2   1 
ATOM   7047  N  N     . ILE   C 2  16  ? -16.209 -5.198  41.216   1.00 60.26  ? 16  ILE   D N     1 
ATOM   7048  C  CA    . ILE   C 2  16  ? -15.528 -4.410  40.187   1.00 53.80  ? 16  ILE   D CA    1 
ATOM   7049  C  C     . ILE   C 2  16  ? -15.971 -2.959  40.262   1.00 49.85  ? 16  ILE   D C     1 
ATOM   7050  O  O     . ILE   C 2  16  ? -15.185 -2.042  39.978   1.00 44.14  ? 16  ILE   D O     1 
ATOM   7051  C  CB    . ILE   C 2  16  ? -15.749 -5.008  38.781   1.00 47.94  ? 16  ILE   D CB    1 
ATOM   7052  C  CG1   . ILE   C 2  16  ? -17.188 -4.816  38.304   1.00 48.23  ? 16  ILE   D CG1   1 
ATOM   7053  C  CG2   . ILE   C 2  16  ? -15.405 -6.497  38.763   1.00 48.82  ? 16  ILE   D CG2   1 
ATOM   7054  C  CD1   . ILE   C 2  16  ? -17.499 -5.613  37.040   1.00 47.23  ? 16  ILE   D CD1   1 
ATOM   7055  N  N     . GLY   C 2  17  ? -17.218 -2.715  40.656   1.00 51.64  ? 17  GLY   D N     1 
ATOM   7056  C  CA    . GLY   C 2  17  ? -17.637 -1.345  40.880   1.00 51.73  ? 17  GLY   D CA    1 
ATOM   7057  C  C     . GLY   C 2  17  ? -16.701 -0.622  41.822   1.00 53.31  ? 17  GLY   D C     1 
ATOM   7058  O  O     . GLY   C 2  17  ? -16.191 0.459   41.511   1.00 57.71  ? 17  GLY   D O     1 
ATOM   7059  N  N     . ALA   C 2  18  ? -16.433 -1.234  42.976   1.00 55.35  ? 18  ALA   D N     1 
ATOM   7060  C  CA    . ALA   C 2  18  ? -15.618 -0.586  43.999   1.00 56.58  ? 18  ALA   D CA    1 
ATOM   7061  C  C     . ALA   C 2  18  ? -14.205 -0.310  43.494   1.00 53.97  ? 18  ALA   D C     1 
ATOM   7062  O  O     . ALA   C 2  18  ? -13.664 0.788   43.683   1.00 46.11  ? 18  ALA   D O     1 
ATOM   7063  C  CB    . ALA   C 2  18  ? -15.591 -1.461  45.255   1.00 55.31  ? 18  ALA   D CB    1 
ATOM   7064  N  N     . LYS   C 2  19  ? -13.582 -1.305  42.859   1.00 55.51  ? 19  LYS   D N     1 
ATOM   7065  C  CA    . LYS   C 2  19  ? -12.225 -1.118  42.352   1.00 56.68  ? 19  LYS   D CA    1 
ATOM   7066  C  C     . LYS   C 2  19  ? -12.181 -0.019  41.300   1.00 56.95  ? 19  LYS   D C     1 
ATOM   7067  O  O     . LYS   C 2  19  ? -11.328 0.876   41.356   1.00 56.18  ? 19  LYS   D O     1 
ATOM   7068  C  CB    . LYS   C 2  19  ? -11.694 -2.439  41.805   1.00 48.38  ? 19  LYS   D CB    1 
ATOM   7069  C  CG    . LYS   C 2  19  ? -11.377 -3.426  42.918   1.00 53.37  ? 19  LYS   D CG    1 
ATOM   7070  C  CD    . LYS   C 2  19  ? -10.538 -2.723  43.987   1.00 67.22  ? 19  LYS   D CD    1 
ATOM   7071  C  CE    . LYS   C 2  19  ? -10.227 -3.619  45.188   1.00 77.83  ? 19  LYS   D CE    1 
ATOM   7072  N  NZ    . LYS   C 2  19  ? -9.298  -2.945  46.141   1.00 56.13  ? 19  LYS   D NZ    1 
ATOM   7073  N  N     . PHE   C 2  20  ? -13.115 -0.055  40.343   1.00 52.49  ? 20  PHE   D N     1 
ATOM   7074  C  CA    . PHE   C 2  20  ? -13.245 1.043   39.394   1.00 51.18  ? 20  PHE   D CA    1 
ATOM   7075  C  C     . PHE   C 2  20  ? -13.180 2.388   40.093   1.00 50.60  ? 20  PHE   D C     1 
ATOM   7076  O  O     . PHE   C 2  20  ? -12.384 3.255   39.718   1.00 55.55  ? 20  PHE   D O     1 
ATOM   7077  C  CB    . PHE   C 2  20  ? -14.553 0.931   38.604   1.00 59.63  ? 20  PHE   D CB    1 
ATOM   7078  C  CG    . PHE   C 2  20  ? -14.831 2.130   37.732   1.00 53.65  ? 20  PHE   D CG    1 
ATOM   7079  C  CD1   . PHE   C 2  20  ? -14.085 2.358   36.592   1.00 51.90  ? 20  PHE   D CD1   1 
ATOM   7080  C  CD2   . PHE   C 2  20  ? -15.822 3.039   38.073   1.00 53.81  ? 20  PHE   D CD2   1 
ATOM   7081  C  CE1   . PHE   C 2  20  ? -14.321 3.459   35.804   1.00 48.12  ? 20  PHE   D CE1   1 
ATOM   7082  C  CE2   . PHE   C 2  20  ? -16.067 4.147   37.293   1.00 54.09  ? 20  PHE   D CE2   1 
ATOM   7083  C  CZ    . PHE   C 2  20  ? -15.318 4.355   36.148   1.00 57.18  ? 20  PHE   D CZ    1 
ATOM   7084  N  N     . TRP   C 2  21  ? -14.016 2.582   41.119   1.00 56.10  ? 21  TRP   D N     1 
ATOM   7085  C  CA    . TRP   C 2  21  ? -14.097 3.892   41.763   1.00 54.26  ? 21  TRP   D CA    1 
ATOM   7086  C  C     . TRP   C 2  21  ? -12.828 4.220   42.542   1.00 53.79  ? 21  TRP   D C     1 
ATOM   7087  O  O     . TRP   C 2  21  ? -12.427 5.391   42.614   1.00 51.54  ? 21  TRP   D O     1 
ATOM   7088  C  CB    . TRP   C 2  21  ? -15.332 3.952   42.664   1.00 50.86  ? 21  TRP   D CB    1 
ATOM   7089  C  CG    . TRP   C 2  21  ? -16.580 4.271   41.911   1.00 51.81  ? 21  TRP   D CG    1 
ATOM   7090  C  CD1   . TRP   C 2  21  ? -17.646 3.443   41.690   1.00 56.21  ? 21  TRP   D CD1   1 
ATOM   7091  C  CD2   . TRP   C 2  21  ? -16.889 5.508   41.254   1.00 49.10  ? 21  TRP   D CD2   1 
ATOM   7092  N  NE1   . TRP   C 2  21  ? -18.601 4.091   40.937   1.00 47.62  ? 21  TRP   D NE1   1 
ATOM   7093  C  CE2   . TRP   C 2  21  ? -18.166 5.361   40.664   1.00 42.83  ? 21  TRP   D CE2   1 
ATOM   7094  C  CE3   . TRP   C 2  21  ? -16.213 6.727   41.113   1.00 44.25  ? 21  TRP   D CE3   1 
ATOM   7095  C  CZ2   . TRP   C 2  21  ? -18.776 6.382   39.943   1.00 37.65  ? 21  TRP   D CZ2   1 
ATOM   7096  C  CZ3   . TRP   C 2  21  ? -16.825 7.746   40.406   1.00 48.50  ? 21  TRP   D CZ3   1 
ATOM   7097  C  CH2   . TRP   C 2  21  ? -18.094 7.564   39.822   1.00 48.09  ? 21  TRP   D CH2   1 
ATOM   7098  N  N     . GLU   C 2  22  ? -12.189 3.207   43.131   1.00 55.39  ? 22  GLU   D N     1 
ATOM   7099  C  CA    . GLU   C 2  22  ? -10.872 3.404   43.721   1.00 55.75  ? 22  GLU   D CA    1 
ATOM   7100  C  C     . GLU   C 2  22  ? -9.906  3.966   42.690   1.00 62.07  ? 22  GLU   D C     1 
ATOM   7101  O  O     . GLU   C 2  22  ? -9.341  5.052   42.871   1.00 52.66  ? 22  GLU   D O     1 
ATOM   7102  C  CB    . GLU   C 2  22  ? -10.344 2.079   44.280   1.00 63.97  ? 22  GLU   D CB    1 
ATOM   7103  C  CG    . GLU   C 2  22  ? -11.220 1.431   45.349   1.00 70.08  ? 22  GLU   D CG    1 
ATOM   7104  C  CD    . GLU   C 2  22  ? -10.736 0.044   45.735   1.00 73.01  ? 22  GLU   D CD    1 
ATOM   7105  O  OE1   . GLU   C 2  22  ? -9.584  -0.304  45.375   1.00 74.17  ? 22  GLU   D OE1   1 
ATOM   7106  O  OE2   . GLU   C 2  22  ? -11.509 -0.699  46.391   1.00 73.07  ? 22  GLU   D OE2   1 
ATOM   7107  N  N     . VAL   C 2  23  ? -9.740  3.240   41.575   1.00 64.75  ? 23  VAL   D N     1 
ATOM   7108  C  CA    . VAL   C 2  23  ? -8.699  3.544   40.592   1.00 54.14  ? 23  VAL   D CA    1 
ATOM   7109  C  C     . VAL   C 2  23  ? -8.813  4.984   40.105   1.00 58.68  ? 23  VAL   D C     1 
ATOM   7110  O  O     . VAL   C 2  23  ? -7.842  5.751   40.165   1.00 59.17  ? 23  VAL   D O     1 
ATOM   7111  C  CB    . VAL   C 2  23  ? -8.764  2.558   39.412   1.00 54.22  ? 23  VAL   D CB    1 
ATOM   7112  C  CG1   . VAL   C 2  23  ? -7.571  2.775   38.496   1.00 55.63  ? 23  VAL   D CG1   1 
ATOM   7113  C  CG2   . VAL   C 2  23  ? -8.841  1.109   39.901   1.00 49.80  ? 23  VAL   D CG2   1 
ATOM   7114  N  N     . ILE   C 2  24  ? -9.991  5.363   39.578   1.00 55.82  ? 24  ILE   D N     1 
ATOM   7115  C  CA    . ILE   C 2  24  ? -10.122 6.684   38.952   1.00 55.78  ? 24  ILE   D CA    1 
ATOM   7116  C  C     . ILE   C 2  24  ? -10.042 7.773   40.004   1.00 55.95  ? 24  ILE   D C     1 
ATOM   7117  O  O     . ILE   C 2  24  ? -9.539  8.873   39.733   1.00 53.54  ? 24  ILE   D O     1 
ATOM   7118  C  CB    . ILE   C 2  24  ? -11.422 6.820   38.127   1.00 60.07  ? 24  ILE   D CB    1 
ATOM   7119  C  CG1   . ILE   C 2  24  ? -12.587 7.256   39.017   1.00 56.04  ? 24  ILE   D CG1   1 
ATOM   7120  C  CG2   . ILE   C 2  24  ? -11.769 5.528   37.358   1.00 46.42  ? 24  ILE   D CG2   1 
ATOM   7121  C  CD1   . ILE   C 2  24  ? -13.864 7.425   38.248   1.00 59.21  ? 24  ILE   D CD1   1 
ATOM   7122  N  N     . SER   C 2  25  ? -10.532 7.490   41.216   1.00 58.32  ? 25  SER   D N     1 
ATOM   7123  C  CA    . SER   C 2  25  ? -10.332 8.402   42.341   1.00 65.33  ? 25  SER   D CA    1 
ATOM   7124  C  C     . SER   C 2  25  ? -8.845  8.631   42.612   1.00 61.27  ? 25  SER   D C     1 
ATOM   7125  O  O     . SER   C 2  25  ? -8.415  9.768   42.848   1.00 61.93  ? 25  SER   D O     1 
ATOM   7126  C  CB    . SER   C 2  25  ? -11.038 7.854   43.585   1.00 62.72  ? 25  SER   D CB    1 
ATOM   7127  O  OG    . SER   C 2  25  ? -12.139 8.671   43.944   1.00 58.23  ? 25  SER   D OG    1 
ATOM   7128  N  N     . ASP   C 2  26  ? -8.045  7.559   42.592   1.00 56.23  ? 26  ASP   D N     1 
ATOM   7129  C  CA    . ASP   C 2  26  ? -6.593  7.708   42.576   1.00 55.08  ? 26  ASP   D CA    1 
ATOM   7130  C  C     . ASP   C 2  26  ? -6.168  8.606   41.414   1.00 64.67  ? 26  ASP   D C     1 
ATOM   7131  O  O     . ASP   C 2  26  ? -5.640  9.706   41.629   1.00 62.22  ? 26  ASP   D O     1 
ATOM   7132  C  CB    . ASP   C 2  26  ? -5.935  6.314   42.540   1.00 64.19  ? 26  ASP   D CB    1 
ATOM   7133  C  CG    . ASP   C 2  26  ? -4.764  6.198   41.552   1.00 67.76  ? 26  ASP   D CG    1 
ATOM   7134  O  OD1   . ASP   C 2  26  ? -3.853  7.053   41.585   1.00 66.92  ? 26  ASP   D OD1   1 
ATOM   7135  O  OD2   . ASP   C 2  26  ? -4.738  5.208   40.774   1.00 58.00  ? 26  ASP   D OD2   1 
ATOM   7136  N  N     . GLU   C 2  27  ? -6.462  8.191   40.175   1.00 51.74  ? 27  GLU   D N     1 
ATOM   7137  C  CA    . GLU   C 2  27  ? -6.110  9.012   39.019   1.00 50.95  ? 27  GLU   D CA    1 
ATOM   7138  C  C     . GLU   C 2  27  ? -6.489  10.478  39.237   1.00 60.43  ? 27  GLU   D C     1 
ATOM   7139  O  O     . GLU   C 2  27  ? -5.637  11.370  39.177   1.00 62.15  ? 27  GLU   D O     1 
ATOM   7140  C  CB    . GLU   C 2  27  ? -6.785  8.464   37.758   1.00 50.46  ? 27  GLU   D CB    1 
ATOM   7141  C  CG    . GLU   C 2  27  ? -6.468  7.018   37.449   1.00 47.60  ? 27  GLU   D CG    1 
ATOM   7142  C  CD    . GLU   C 2  27  ? -6.740  6.674   36.005   1.00 52.18  ? 27  GLU   D CD    1 
ATOM   7143  O  OE1   . GLU   C 2  27  ? -7.319  7.529   35.291   1.00 51.63  ? 27  GLU   D OE1   1 
ATOM   7144  O  OE2   . GLU   C 2  27  ? -6.365  5.555   35.582   1.00 47.76  ? 27  GLU   D OE2   1 
ATOM   7145  N  N     . HIS   C 2  28  ? -7.769  10.743  39.519   1.00 59.44  ? 28  HIS   D N     1 
ATOM   7146  C  CA    . HIS   C 2  28  ? -8.291  12.105  39.522   1.00 55.96  ? 28  HIS   D CA    1 
ATOM   7147  C  C     . HIS   C 2  28  ? -7.905  12.917  40.745   1.00 60.60  ? 28  HIS   D C     1 
ATOM   7148  O  O     . HIS   C 2  28  ? -8.217  14.111  40.789   1.00 52.19  ? 28  HIS   D O     1 
ATOM   7149  C  CB    . HIS   C 2  28  ? -9.814  12.083  39.418   1.00 58.98  ? 28  HIS   D CB    1 
ATOM   7150  C  CG    . HIS   C 2  28  ? -10.311 11.787  38.043   1.00 58.96  ? 28  HIS   D CG    1 
ATOM   7151  N  ND1   . HIS   C 2  28  ? -10.541 12.774  37.109   1.00 48.84  ? 28  HIS   D ND1   1 
ATOM   7152  C  CD2   . HIS   C 2  28  ? -10.607 10.613  37.438   1.00 55.86  ? 28  HIS   D CD2   1 
ATOM   7153  C  CE1   . HIS   C 2  28  ? -10.967 12.218  35.989   1.00 58.20  ? 28  HIS   D CE1   1 
ATOM   7154  N  NE2   . HIS   C 2  28  ? -11.010 10.908  36.160   1.00 53.49  ? 28  HIS   D NE2   1 
ATOM   7155  N  N     . GLY   C 2  29  ? -7.270  12.312  41.742   1.00 66.06  ? 29  GLY   D N     1 
ATOM   7156  C  CA    . GLY   C 2  29  ? -6.912  13.059  42.935   1.00 68.94  ? 29  GLY   D CA    1 
ATOM   7157  C  C     . GLY   C 2  29  ? -8.029  13.253  43.941   1.00 69.75  ? 29  GLY   D C     1 
ATOM   7158  O  O     . GLY   C 2  29  ? -8.178  14.355  44.484   1.00 69.97  ? 29  GLY   D O     1 
ATOM   7159  N  N     . ILE   C 2  30  ? -8.822  12.213  44.210   1.00 61.14  ? 30  ILE   D N     1 
ATOM   7160  C  CA    . ILE   C 2  30  ? -9.858  12.249  45.237   1.00 74.35  ? 30  ILE   D CA    1 
ATOM   7161  C  C     . ILE   C 2  30  ? -9.582  11.145  46.250   1.00 72.43  ? 30  ILE   D C     1 
ATOM   7162  O  O     . ILE   C 2  30  ? -9.374  9.982   45.872   1.00 63.78  ? 30  ILE   D O     1 
ATOM   7163  C  CB    . ILE   C 2  30  ? -11.271 12.107  44.639   1.00 65.39  ? 30  ILE   D CB    1 
ATOM   7164  C  CG1   . ILE   C 2  30  ? -11.702 13.416  43.986   1.00 59.96  ? 30  ILE   D CG1   1 
ATOM   7165  C  CG2   . ILE   C 2  30  ? -12.269 11.725  45.711   1.00 64.71  ? 30  ILE   D CG2   1 
ATOM   7166  C  CD1   . ILE   C 2  30  ? -11.219 13.564  42.584   1.00 63.06  ? 30  ILE   D CD1   1 
ATOM   7167  N  N     . ASP   C 2  31  ? -9.583  11.511  47.539   1.00 72.46  ? 31  ASP   D N     1 
ATOM   7168  C  CA    . ASP   C 2  31  ? -9.325  10.551  48.611   1.00 77.28  ? 31  ASP   D CA    1 
ATOM   7169  C  C     . ASP   C 2  31  ? -10.637 9.964   49.131   1.00 79.75  ? 31  ASP   D C     1 
ATOM   7170  O  O     . ASP   C 2  31  ? -11.716 10.345  48.655   1.00 75.75  ? 31  ASP   D O     1 
ATOM   7171  C  CB    . ASP   C 2  31  ? -8.525  11.202  49.744   1.00 70.76  ? 31  ASP   D CB    1 
ATOM   7172  C  CG    . ASP   C 2  31  ? -9.253  12.373  50.388   1.00 73.91  ? 31  ASP   D CG    1 
ATOM   7173  O  OD1   . ASP   C 2  31  ? -10.451 12.237  50.707   1.00 74.39  ? 31  ASP   D OD1   1 
ATOM   7174  O  OD2   . ASP   C 2  31  ? -8.616  13.425  50.602   1.00 68.38  ? 31  ASP   D OD2   1 
ATOM   7175  N  N     . PRO   C 2  32  ? -10.595 9.023   50.101   1.00 83.45  ? 32  PRO   D N     1 
ATOM   7176  C  CA    . PRO   C 2  32  ? -11.830 8.326   50.498   1.00 82.23  ? 32  PRO   D CA    1 
ATOM   7177  C  C     . PRO   C 2  32  ? -12.810 9.201   51.266   1.00 86.30  ? 32  PRO   D C     1 
ATOM   7178  O  O     . PRO   C 2  32  ? -13.837 8.707   51.746   1.00 91.64  ? 32  PRO   D O     1 
ATOM   7179  C  CB    . PRO   C 2  32  ? -11.320 7.165   51.366   1.00 73.89  ? 32  PRO   D CB    1 
ATOM   7180  C  CG    . PRO   C 2  32  ? -9.884  7.008   50.990   1.00 79.38  ? 32  PRO   D CG    1 
ATOM   7181  C  CD    . PRO   C 2  32  ? -9.404  8.396   50.698   1.00 76.67  ? 32  PRO   D CD    1 
ATOM   7182  N  N     . THR   C 2  33  ? -12.513 10.498  51.386   1.00 80.86  ? 33  THR   D N     1 
ATOM   7183  C  CA    . THR   C 2  33  ? -13.404 11.447  52.046   1.00 79.62  ? 33  THR   D CA    1 
ATOM   7184  C  C     . THR   C 2  33  ? -13.882 12.528  51.080   1.00 87.72  ? 33  THR   D C     1 
ATOM   7185  O  O     . THR   C 2  33  ? -14.221 13.642  51.503   1.00 86.28  ? 33  THR   D O     1 
ATOM   7186  C  CB    . THR   C 2  33  ? -12.727 12.084  53.261   1.00 77.87  ? 33  THR   D CB    1 
ATOM   7187  O  OG1   . THR   C 2  33  ? -11.621 12.891  52.832   1.00 71.66  ? 33  THR   D OG1   1 
ATOM   7188  C  CG2   . THR   C 2  33  ? -12.245 11.004  54.243   1.00 69.90  ? 33  THR   D CG2   1 
ATOM   7189  N  N     . GLY   C 2  34  ? -13.910 12.209  49.781   1.00 77.42  ? 34  GLY   D N     1 
ATOM   7190  C  CA    . GLY   C 2  34  ? -14.350 13.156  48.771   1.00 80.60  ? 34  GLY   D CA    1 
ATOM   7191  C  C     . GLY   C 2  34  ? -13.494 14.399  48.643   1.00 81.48  ? 34  GLY   D C     1 
ATOM   7192  O  O     . GLY   C 2  34  ? -13.961 15.414  48.111   1.00 78.01  ? 34  GLY   D O     1 
ATOM   7193  N  N     . SER   C 2  35  ? -12.250 14.350  49.114   1.00 78.15  ? 35  SER   D N     1 
ATOM   7194  C  CA    . SER   C 2  35  ? -11.330 15.479  49.071   1.00 85.51  ? 35  SER   D CA    1 
ATOM   7195  C  C     . SER   C 2  35  ? -10.411 15.376  47.852   1.00 79.91  ? 35  SER   D C     1 
ATOM   7196  O  O     . SER   C 2  35  ? -10.160 14.289  47.315   1.00 73.67  ? 35  SER   D O     1 
ATOM   7197  C  CB    . SER   C 2  35  ? -10.499 15.551  50.363   1.00 78.11  ? 35  SER   D CB    1 
ATOM   7198  O  OG    . SER   C 2  35  ? -11.317 15.704  51.519   1.00 74.31  ? 35  SER   D OG    1 
ATOM   7199  N  N     . TYR   C 2  36  ? -9.909  16.530  47.412   1.00 73.77  ? 36  TYR   D N     1 
ATOM   7200  C  CA    . TYR   C 2  36  ? -9.040  16.594  46.239   1.00 78.19  ? 36  TYR   D CA    1 
ATOM   7201  C  C     . TYR   C 2  36  ? -7.621  16.961  46.669   1.00 72.92  ? 36  TYR   D C     1 
ATOM   7202  O  O     . TYR   C 2  36  ? -7.305  18.140  46.855   1.00 69.82  ? 36  TYR   D O     1 
ATOM   7203  C  CB    . TYR   C 2  36  ? -9.569  17.579  45.205   1.00 66.47  ? 36  TYR   D CB    1 
ATOM   7204  C  CG    . TYR   C 2  36  ? -8.564  17.829  44.109   1.00 67.62  ? 36  TYR   D CG    1 
ATOM   7205  C  CD1   . TYR   C 2  36  ? -8.325  16.875  43.132   1.00 65.77  ? 36  TYR   D CD1   1 
ATOM   7206  C  CD2   . TYR   C 2  36  ? -7.834  19.010  44.067   1.00 68.63  ? 36  TYR   D CD2   1 
ATOM   7207  C  CE1   . TYR   C 2  36  ? -7.391  17.092  42.137   1.00 72.16  ? 36  TYR   D CE1   1 
ATOM   7208  C  CE2   . TYR   C 2  36  ? -6.906  19.239  43.078   1.00 71.93  ? 36  TYR   D CE2   1 
ATOM   7209  C  CZ    . TYR   C 2  36  ? -6.686  18.278  42.116   1.00 70.99  ? 36  TYR   D CZ    1 
ATOM   7210  O  OH    . TYR   C 2  36  ? -5.758  18.508  41.135   1.00 72.03  ? 36  TYR   D OH    1 
ATOM   7211  N  N     . HIS   C 2  37  ? -6.771  15.936  46.802   1.00 76.55  ? 37  HIS   D N     1 
ATOM   7212  C  CA    . HIS   C 2  37  ? -5.344  16.085  47.103   1.00 75.62  ? 37  HIS   D CA    1 
ATOM   7213  C  C     . HIS   C 2  37  ? -4.555  15.928  45.803   1.00 77.30  ? 37  HIS   D C     1 
ATOM   7214  O  O     . HIS   C 2  37  ? -3.914  14.907  45.555   1.00 82.16  ? 37  HIS   D O     1 
ATOM   7215  C  CB    . HIS   C 2  37  ? -4.905  15.049  48.143   1.00 78.73  ? 37  HIS   D CB    1 
ATOM   7216  C  CG    . HIS   C 2  37  ? -5.461  15.283  49.519   1.00 97.69  ? 37  HIS   D CG    1 
ATOM   7217  N  ND1   . HIS   C 2  37  ? -6.417  16.241  49.791   1.00 90.68  ? 37  HIS   D ND1   1 
ATOM   7218  C  CD2   . HIS   C 2  37  ? -5.189  14.681  50.703   1.00 99.24  ? 37  HIS   D CD2   1 
ATOM   7219  C  CE1   . HIS   C 2  37  ? -6.712  16.215  51.080   1.00 85.57  ? 37  HIS   D CE1   1 
ATOM   7220  N  NE2   . HIS   C 2  37  ? -5.981  15.277  51.656   1.00 90.77  ? 37  HIS   D NE2   1 
ATOM   7221  N  N     . GLY   C 2  38  ? -4.589  16.971  44.967   1.00 76.15  ? 38  GLY   D N     1 
ATOM   7222  C  CA    . GLY   C 2  38  ? -4.069  16.862  43.613   1.00 73.67  ? 38  GLY   D CA    1 
ATOM   7223  C  C     . GLY   C 2  38  ? -2.926  17.784  43.231   1.00 74.24  ? 38  GLY   D C     1 
ATOM   7224  O  O     . GLY   C 2  38  ? -2.317  18.432  44.087   1.00 87.03  ? 38  GLY   D O     1 
ATOM   7225  N  N     . ASP   C 2  39  ? -2.614  17.836  41.936   1.00 75.05  ? 39  ASP   D N     1 
ATOM   7226  C  CA    . ASP   C 2  39  ? -1.568  18.717  41.420   1.00 82.86  ? 39  ASP   D CA    1 
ATOM   7227  C  C     . ASP   C 2  39  ? -1.923  19.412  40.109   1.00 81.12  ? 39  ASP   D C     1 
ATOM   7228  O  O     . ASP   C 2  39  ? -1.498  20.555  39.903   1.00 83.54  ? 39  ASP   D O     1 
ATOM   7229  C  CB    . ASP   C 2  39  ? -0.259  17.932  41.227   1.00 84.12  ? 39  ASP   D CB    1 
ATOM   7230  C  CG    . ASP   C 2  39  ? -0.323  16.948  40.058   1.00 80.59  ? 39  ASP   D CG    1 
ATOM   7231  O  OD1   . ASP   C 2  39  ? -1.323  16.952  39.311   1.00 78.65  ? 39  ASP   D OD1   1 
ATOM   7232  O  OD2   . ASP   C 2  39  ? 0.636   16.170  39.882   1.00 79.61  ? 39  ASP   D OD2   1 
ATOM   7233  N  N     . SER   C 2  40  ? -2.688  18.780  39.223   1.00 76.24  ? 40  SER   D N     1 
ATOM   7234  C  CA    . SER   C 2  40  ? -2.952  19.290  37.886   1.00 81.96  ? 40  SER   D CA    1 
ATOM   7235  C  C     . SER   C 2  40  ? -4.434  19.594  37.701   1.00 76.04  ? 40  SER   D C     1 
ATOM   7236  O  O     . SER   C 2  40  ? -5.298  18.851  38.182   1.00 66.96  ? 40  SER   D O     1 
ATOM   7237  C  CB    . SER   C 2  40  ? -2.498  18.278  36.825   1.00 70.96  ? 40  SER   D CB    1 
ATOM   7238  O  OG    . SER   C 2  40  ? -3.228  18.445  35.624   1.00 71.51  ? 40  SER   D OG    1 
ATOM   7239  N  N     . ASP   C 2  41  ? -4.723  20.690  36.990   1.00 72.33  ? 41  ASP   D N     1 
ATOM   7240  C  CA    . ASP   C 2  41  ? -6.093  20.956  36.566   1.00 69.46  ? 41  ASP   D CA    1 
ATOM   7241  C  C     . ASP   C 2  41  ? -6.606  19.892  35.592   1.00 70.24  ? 41  ASP   D C     1 
ATOM   7242  O  O     . ASP   C 2  41  ? -7.822  19.690  35.494   1.00 65.80  ? 41  ASP   D O     1 
ATOM   7243  C  CB    . ASP   C 2  41  ? -6.184  22.349  35.934   1.00 86.02  ? 41  ASP   D CB    1 
ATOM   7244  C  CG    . ASP   C 2  41  ? -5.898  23.475  36.929   1.00 76.04  ? 41  ASP   D CG    1 
ATOM   7245  O  OD1   . ASP   C 2  41  ? -6.535  23.495  38.002   1.00 59.50  ? 41  ASP   D OD1   1 
ATOM   7246  O  OD2   . ASP   C 2  41  ? -5.044  24.343  36.624   1.00 68.42  ? 41  ASP   D OD2   1 
ATOM   7247  N  N     . LEU   C 2  42  ? -5.707  19.200  34.881   1.00 60.52  ? 42  LEU   D N     1 
ATOM   7248  C  CA    . LEU   C 2  42  ? -6.091  18.033  34.092   1.00 68.35  ? 42  LEU   D CA    1 
ATOM   7249  C  C     . LEU   C 2  42  ? -6.920  17.024  34.884   1.00 71.71  ? 42  LEU   D C     1 
ATOM   7250  O  O     . LEU   C 2  42  ? -7.570  16.160  34.280   1.00 68.37  ? 42  LEU   D O     1 
ATOM   7251  C  CB    . LEU   C 2  42  ? -4.843  17.319  33.545   1.00 64.05  ? 42  LEU   D CB    1 
ATOM   7252  C  CG    . LEU   C 2  42  ? -4.365  17.694  32.143   1.00 57.24  ? 42  LEU   D CG    1 
ATOM   7253  C  CD1   . LEU   C 2  42  ? -5.389  18.616  31.489   1.00 57.13  ? 42  LEU   D CD1   1 
ATOM   7254  C  CD2   . LEU   C 2  42  ? -2.955  18.332  32.165   1.00 52.64  ? 42  LEU   D CD2   1 
ATOM   7255  N  N     . GLN   C 2  43  ? -6.893  17.088  36.216   1.00 70.82  ? 45  GLN   D N     1 
ATOM   7256  C  CA    . GLN   C 2  43  ? -7.631  16.141  37.043   1.00 69.01  ? 45  GLN   D CA    1 
ATOM   7257  C  C     . GLN   C 2  43  ? -9.049  16.596  37.352   1.00 62.63  ? 45  GLN   D C     1 
ATOM   7258  O  O     . GLN   C 2  43  ? -9.900  15.762  37.683   1.00 56.00  ? 45  GLN   D O     1 
ATOM   7259  C  CB    . GLN   C 2  43  ? -6.903  15.916  38.364   1.00 57.94  ? 45  GLN   D CB    1 
ATOM   7260  C  CG    . GLN   C 2  43  ? -5.479  15.489  38.230   1.00 64.24  ? 45  GLN   D CG    1 
ATOM   7261  C  CD    . GLN   C 2  43  ? -4.835  15.297  39.580   1.00 68.50  ? 45  GLN   D CD    1 
ATOM   7262  O  OE1   . GLN   C 2  43  ? -4.349  16.256  40.185   1.00 67.90  ? 45  GLN   D OE1   1 
ATOM   7263  N  NE2   . GLN   C 2  43  ? -4.852  14.055  40.080   1.00 51.13  ? 45  GLN   D NE2   1 
ATOM   7264  N  N     . LEU   C 2  44  ? -9.317  17.892  37.278   1.00 58.34  ? 46  LEU   D N     1 
ATOM   7265  C  CA    . LEU   C 2  44  ? -10.613 18.419  37.664   1.00 62.19  ? 46  LEU   D CA    1 
ATOM   7266  C  C     . LEU   C 2  44  ? -11.498 18.712  36.460   1.00 64.36  ? 46  LEU   D C     1 
ATOM   7267  O  O     . LEU   C 2  44  ? -12.656 18.289  36.436   1.00 61.09  ? 46  LEU   D O     1 
ATOM   7268  C  CB    . LEU   C 2  44  ? -10.431 19.687  38.517   1.00 59.62  ? 46  LEU   D CB    1 
ATOM   7269  C  CG    . LEU   C 2  44  ? -10.665 19.583  40.036   1.00 57.61  ? 46  LEU   D CG    1 
ATOM   7270  C  CD1   . LEU   C 2  44  ? -9.567  18.810  40.731   1.00 58.56  ? 46  LEU   D CD1   1 
ATOM   7271  C  CD2   . LEU   C 2  44  ? -10.804 20.966  40.670   1.00 63.12  ? 46  LEU   D CD2   1 
ATOM   7272  N  N     . GLU   C 2  45  ? -10.955 19.395  35.447   1.00 64.18  ? 47  GLU   D N     1 
ATOM   7273  C  CA    . GLU   C 2  45  ? -11.719 19.974  34.347   1.00 60.21  ? 47  GLU   D CA    1 
ATOM   7274  C  C     . GLU   C 2  45  ? -12.955 19.154  33.994   1.00 61.05  ? 47  GLU   D C     1 
ATOM   7275  O  O     . GLU   C 2  45  ? -14.054 19.704  33.853   1.00 65.64  ? 47  GLU   D O     1 
ATOM   7276  C  CB    . GLU   C 2  45  ? -10.817 20.141  33.114   1.00 76.07  ? 47  GLU   D CB    1 
ATOM   7277  C  CG    . GLU   C 2  45  ? -11.454 20.928  31.946   1.00 79.88  ? 47  GLU   D CG    1 
ATOM   7278  C  CD    . GLU   C 2  45  ? -10.473 21.223  30.823   1.00 78.24  ? 47  GLU   D CD    1 
ATOM   7279  O  OE1   . GLU   C 2  45  ? -9.614  22.113  31.018   1.00 62.58  ? 47  GLU   D OE1   1 
ATOM   7280  O  OE2   . GLU   C 2  45  ? -10.557 20.560  29.757   1.00 78.38  ? 47  GLU   D OE2   1 
ATOM   7281  N  N     . ARG   C 2  46  ? -12.792 17.839  33.865   1.00 57.74  ? 48  ARG   D N     1 
ATOM   7282  C  CA    . ARG   C 2  46  ? -13.875 16.943  33.483   1.00 57.80  ? 48  ARG   D CA    1 
ATOM   7283  C  C     . ARG   C 2  46  ? -14.318 16.046  34.639   1.00 61.15  ? 48  ARG   D C     1 
ATOM   7284  O  O     . ARG   C 2  46  ? -14.718 14.895  34.428   1.00 54.25  ? 48  ARG   D O     1 
ATOM   7285  C  CB    . ARG   C 2  46  ? -13.449 16.114  32.276   1.00 52.89  ? 48  ARG   D CB    1 
ATOM   7286  C  CG    . ARG   C 2  46  ? -13.192 16.972  31.063   1.00 51.74  ? 48  ARG   D CG    1 
ATOM   7287  C  CD    . ARG   C 2  46  ? -14.151 16.600  29.987   1.00 55.20  ? 48  ARG   D CD    1 
ATOM   7288  N  NE    . ARG   C 2  46  ? -13.757 15.322  29.417   1.00 51.83  ? 48  ARG   D NE    1 
ATOM   7289  C  CZ    . ARG   C 2  46  ? -14.333 14.763  28.365   1.00 57.18  ? 48  ARG   D CZ    1 
ATOM   7290  N  NH1   . ARG   C 2  46  ? -15.378 15.324  27.770   1.00 59.66  ? 48  ARG   D NH1   1 
ATOM   7291  N  NH2   . ARG   C 2  46  ? -13.850 13.614  27.896   1.00 52.02  ? 48  ARG   D NH2   1 
ATOM   7292  N  N     . ILE   C 2  47  ? -14.264 16.569  35.867   1.00 57.67  ? 49  ILE   D N     1 
ATOM   7293  C  CA    . ILE   C 2  47  ? -14.581 15.759  37.039   1.00 55.52  ? 49  ILE   D CA    1 
ATOM   7294  C  C     . ILE   C 2  47  ? -16.082 15.562  37.207   1.00 51.69  ? 49  ILE   D C     1 
ATOM   7295  O  O     . ILE   C 2  47  ? -16.503 14.627  37.896   1.00 46.85  ? 49  ILE   D O     1 
ATOM   7296  C  CB    . ILE   C 2  47  ? -13.975 16.391  38.301   1.00 46.56  ? 49  ILE   D CB    1 
ATOM   7297  C  CG1   . ILE   C 2  47  ? -13.929 15.377  39.440   1.00 48.90  ? 49  ILE   D CG1   1 
ATOM   7298  C  CG2   . ILE   C 2  47  ? -14.756 17.636  38.704   1.00 49.71  ? 49  ILE   D CG2   1 
ATOM   7299  C  CD1   . ILE   C 2  47  ? -12.856 14.342  39.283   1.00 45.57  ? 49  ILE   D CD1   1 
ATOM   7300  N  N     . ASN   C 2  48  ? -16.903 16.404  36.578   1.00 52.29  ? 50  ASN   D N     1 
ATOM   7301  C  CA    . ASN   C 2  48  ? -18.350 16.232  36.658   1.00 48.09  ? 50  ASN   D CA    1 
ATOM   7302  C  C     . ASN   C 2  48  ? -18.808 14.929  36.021   1.00 55.29  ? 50  ASN   D C     1 
ATOM   7303  O  O     . ASN   C 2  48  ? -19.837 14.375  36.430   1.00 59.29  ? 50  ASN   D O     1 
ATOM   7304  C  CB    . ASN   C 2  48  ? -19.047 17.404  35.983   1.00 56.63  ? 50  ASN   D CB    1 
ATOM   7305  C  CG    . ASN   C 2  48  ? -18.231 17.974  34.828   1.00 80.56  ? 50  ASN   D CG    1 
ATOM   7306  O  OD1   . ASN   C 2  48  ? -16.994 17.910  34.837   1.00 80.78  ? 50  ASN   D OD1   1 
ATOM   7307  N  ND2   . ASN   C 2  48  ? -18.916 18.536  33.831   1.00 86.33  ? 50  ASN   D ND2   1 
ATOM   7308  N  N     . VAL   C 2  49  ? -18.077 14.424  35.022   1.00 53.01  ? 51  VAL   D N     1 
ATOM   7309  C  CA    . VAL   C 2  49  ? -18.574 13.273  34.263   1.00 57.49  ? 51  VAL   D CA    1 
ATOM   7310  C  C     . VAL   C 2  49  ? -18.923 12.118  35.193   1.00 49.47  ? 51  VAL   D C     1 
ATOM   7311  O  O     . VAL   C 2  49  ? -19.921 11.415  34.986   1.00 52.23  ? 51  VAL   D O     1 
ATOM   7312  C  CB    . VAL   C 2  49  ? -17.561 12.837  33.183   1.00 45.30  ? 51  VAL   D CB    1 
ATOM   7313  C  CG1   . VAL   C 2  49  ? -18.136 11.680  32.358   1.00 44.29  ? 51  VAL   D CG1   1 
ATOM   7314  C  CG2   . VAL   C 2  49  ? -17.217 13.990  32.286   1.00 42.67  ? 51  VAL   D CG2   1 
ATOM   7315  N  N     . TYR   C 2  50  ? -18.115 11.903  36.235   1.00 45.29  ? 52  TYR   D N     1 
ATOM   7316  C  CA    . TYR   C 2  50  ? -18.355 10.801  37.149   1.00 43.21  ? 52  TYR   D CA    1 
ATOM   7317  C  C     . TYR   C 2  50  ? -18.591 11.210  38.600   1.00 49.14  ? 52  TYR   D C     1 
ATOM   7318  O  O     . TYR   C 2  50  ? -18.999 10.357  39.400   1.00 46.56  ? 52  TYR   D O     1 
ATOM   7319  C  CB    . TYR   C 2  50  ? -17.186 9.813   37.094   1.00 36.03  ? 52  TYR   D CB    1 
ATOM   7320  C  CG    . TYR   C 2  50  ? -17.240 8.816   35.947   1.00 48.69  ? 52  TYR   D CG    1 
ATOM   7321  C  CD1   . TYR   C 2  50  ? -18.095 7.716   35.992   1.00 49.25  ? 52  TYR   D CD1   1 
ATOM   7322  C  CD2   . TYR   C 2  50  ? -16.398 8.942   34.850   1.00 43.90  ? 52  TYR   D CD2   1 
ATOM   7323  C  CE1   . TYR   C 2  50  ? -18.124 6.780   34.972   1.00 41.37  ? 52  TYR   D CE1   1 
ATOM   7324  C  CE2   . TYR   C 2  50  ? -16.425 8.026   33.818   1.00 39.13  ? 52  TYR   D CE2   1 
ATOM   7325  C  CZ    . TYR   C 2  50  ? -17.284 6.946   33.883   1.00 45.07  ? 52  TYR   D CZ    1 
ATOM   7326  O  OH    . TYR   C 2  50  ? -17.295 6.029   32.856   1.00 36.30  ? 52  TYR   D OH    1 
ATOM   7327  N  N     . TYR   C 2  51  ? -18.360 12.472  38.967   1.00 48.65  ? 53  TYR   D N     1 
ATOM   7328  C  CA    . TYR   C 2  51  ? -18.464 12.931  40.351   1.00 49.65  ? 53  TYR   D CA    1 
ATOM   7329  C  C     . TYR   C 2  51  ? -19.458 14.078  40.452   1.00 49.82  ? 53  TYR   D C     1 
ATOM   7330  O  O     . TYR   C 2  51  ? -19.395 15.033  39.668   1.00 49.81  ? 53  TYR   D O     1 
ATOM   7331  C  CB    . TYR   C 2  51  ? -17.099 13.403  40.898   1.00 54.77  ? 53  TYR   D CB    1 
ATOM   7332  C  CG    . TYR   C 2  51  ? -16.079 12.297  41.070   1.00 58.41  ? 53  TYR   D CG    1 
ATOM   7333  C  CD1   . TYR   C 2  51  ? -16.014 11.559  42.252   1.00 61.94  ? 53  TYR   D CD1   1 
ATOM   7334  C  CD2   . TYR   C 2  51  ? -15.182 11.986  40.056   1.00 49.23  ? 53  TYR   D CD2   1 
ATOM   7335  C  CE1   . TYR   C 2  51  ? -15.090 10.538  42.415   1.00 60.54  ? 53  TYR   D CE1   1 
ATOM   7336  C  CE2   . TYR   C 2  51  ? -14.258 10.968  40.211   1.00 54.74  ? 53  TYR   D CE2   1 
ATOM   7337  C  CZ    . TYR   C 2  51  ? -14.220 10.249  41.389   1.00 56.52  ? 53  TYR   D CZ    1 
ATOM   7338  O  OH    . TYR   C 2  51  ? -13.307 9.243   41.542   1.00 57.47  ? 53  TYR   D OH    1 
ATOM   7339  N  N     . ASN   C 2  52  ? -20.363 13.992  41.421   1.00 52.26  ? 54  ASN   D N     1 
ATOM   7340  C  CA    . ASN   C 2  52  ? -21.039 15.192  41.902   1.00 58.99  ? 54  ASN   D CA    1 
ATOM   7341  C  C     . ASN   C 2  52  ? -20.098 15.975  42.817   1.00 58.40  ? 54  ASN   D C     1 
ATOM   7342  O  O     . ASN   C 2  52  ? -19.143 15.429  43.373   1.00 70.05  ? 54  ASN   D O     1 
ATOM   7343  C  CB    . ASN   C 2  52  ? -22.319 14.839  42.663   1.00 56.80  ? 54  ASN   D CB    1 
ATOM   7344  C  CG    . ASN   C 2  52  ? -23.369 14.222  41.779   1.00 54.89  ? 54  ASN   D CG    1 
ATOM   7345  O  OD1   . ASN   C 2  52  ? -23.692 14.761  40.722   1.00 55.42  ? 54  ASN   D OD1   1 
ATOM   7346  N  ND2   . ASN   C 2  52  ? -23.906 13.078  42.202   1.00 47.47  ? 54  ASN   D ND2   1 
ATOM   7347  N  N     . GLU   C 2  53  ? -20.358 17.265  42.966   1.00 59.27  ? 55  GLU   D N     1 
ATOM   7348  C  CA    . GLU   C 2  53  ? -19.549 18.106  43.843   1.00 67.43  ? 55  GLU   D CA    1 
ATOM   7349  C  C     . GLU   C 2  53  ? -20.405 18.499  45.046   1.00 76.91  ? 55  GLU   D C     1 
ATOM   7350  O  O     . GLU   C 2  53  ? -21.163 19.473  44.997   1.00 70.47  ? 55  GLU   D O     1 
ATOM   7351  C  CB    . GLU   C 2  53  ? -18.995 19.326  43.110   1.00 69.15  ? 55  GLU   D CB    1 
ATOM   7352  C  CG    . GLU   C 2  53  ? -17.983 20.118  43.956   1.00 82.85  ? 55  GLU   D CG    1 
ATOM   7353  C  CD    . GLU   C 2  53  ? -17.269 21.221  43.184   1.00 81.61  ? 55  GLU   D CD    1 
ATOM   7354  O  OE1   . GLU   C 2  53  ? -17.521 21.359  41.967   1.00 69.21  ? 55  GLU   D OE1   1 
ATOM   7355  O  OE2   . GLU   C 2  53  ? -16.453 21.947  43.801   1.00 80.74  ? 55  GLU   D OE2   1 
ATOM   7356  N  N     . ALA   C 2  54  ? -20.282 17.736  46.126   1.00 84.94  ? 56  ALA   D N     1 
ATOM   7357  C  CA    . ALA   C 2  54  ? -20.961 18.079  47.366   1.00 91.48  ? 56  ALA   D CA    1 
ATOM   7358  C  C     . ALA   C 2  54  ? -20.341 19.323  47.996   1.00 89.53  ? 56  ALA   D C     1 
ATOM   7359  O  O     . ALA   C 2  54  ? -19.143 19.592  47.857   1.00 90.27  ? 56  ALA   D O     1 
ATOM   7360  C  CB    . ALA   C 2  54  ? -20.904 16.912  48.352   1.00 92.70  ? 56  ALA   D CB    1 
ATOM   7361  N  N     . THR   C 2  55  ? -21.176 20.079  48.704   1.00 97.93  ? 57  THR   D N     1 
ATOM   7362  C  CA    . THR   C 2  55  ? -20.756 21.323  49.341   1.00 106.20 ? 57  THR   D CA    1 
ATOM   7363  C  C     . THR   C 2  55  ? -19.475 21.151  50.157   1.00 92.84  ? 57  THR   D C     1 
ATOM   7364  O  O     . THR   C 2  55  ? -19.060 20.023  50.448   1.00 87.37  ? 57  THR   D O     1 
ATOM   7365  C  CB    . THR   C 2  55  ? -21.889 21.860  50.219   1.00 103.44 ? 57  THR   D CB    1 
ATOM   7366  O  OG1   . THR   C 2  55  ? -22.409 20.796  51.025   1.00 101.17 ? 57  THR   D OG1   1 
ATOM   7367  C  CG2   . THR   C 2  55  ? -23.010 22.425  49.351   1.00 92.99  ? 57  THR   D CG2   1 
ATOM   7368  N  N     . GLY   C 2  56  ? -18.837 22.262  50.522   1.00 84.53  ? 58  GLY   D N     1 
ATOM   7369  C  CA    . GLY   C 2  56  ? -17.545 22.198  51.166   1.00 82.25  ? 58  GLY   D CA    1 
ATOM   7370  C  C     . GLY   C 2  56  ? -16.405 21.790  50.261   1.00 80.16  ? 58  GLY   D C     1 
ATOM   7371  O  O     . GLY   C 2  56  ? -15.273 21.659  50.742   1.00 87.21  ? 58  GLY   D O     1 
ATOM   7372  N  N     . ASN   C 2  57  ? -16.663 21.591  48.971   1.00 79.24  ? 59  ASN   D N     1 
ATOM   7373  C  CA    . ASN   C 2  57  ? -15.686 21.159  47.978   1.00 73.54  ? 59  ASN   D CA    1 
ATOM   7374  C  C     . ASN   C 2  57  ? -15.450 19.655  48.005   1.00 81.58  ? 59  ASN   D C     1 
ATOM   7375  O  O     . ASN   C 2  57  ? -14.395 19.183  47.550   1.00 79.63  ? 59  ASN   D O     1 
ATOM   7376  C  CB    . ASN   C 2  57  ? -14.348 21.891  48.135   1.00 82.37  ? 59  ASN   D CB    1 
ATOM   7377  C  CG    . ASN   C 2  57  ? -14.214 23.090  47.197   1.00 86.03  ? 59  ASN   D CG    1 
ATOM   7378  O  OD1   . ASN   C 2  57  ? -14.464 24.234  47.586   1.00 76.73  ? 59  ASN   D OD1   1 
ATOM   7379  N  ND2   . ASN   C 2  57  ? -13.805 22.828  45.957   1.00 83.33  ? 59  ASN   D ND2   1 
ATOM   7380  N  N     . LYS   C 2  58  ? -16.396 18.878  48.529   1.00 71.39  ? 60  LYS   D N     1 
ATOM   7381  C  CA    . LYS   C 2  58  ? -16.261 17.433  48.462   1.00 77.37  ? 60  LYS   D CA    1 
ATOM   7382  C  C     . LYS   C 2  58  ? -16.770 16.925  47.114   1.00 79.26  ? 60  LYS   D C     1 
ATOM   7383  O  O     . LYS   C 2  58  ? -17.529 17.605  46.419   1.00 82.06  ? 60  LYS   D O     1 
ATOM   7384  C  CB    . LYS   C 2  58  ? -17.016 16.766  49.616   1.00 84.02  ? 60  LYS   D CB    1 
ATOM   7385  C  CG    . LYS   C 2  58  ? -16.202 16.626  50.913   1.00 92.04  ? 60  LYS   D CG    1 
ATOM   7386  C  CD    . LYS   C 2  58  ? -17.033 16.004  52.042   1.00 95.84  ? 60  LYS   D CD    1 
ATOM   7387  C  CE    . LYS   C 2  58  ? -16.177 15.682  53.268   1.00 89.18  ? 60  LYS   D CE    1 
ATOM   7388  N  NZ    . LYS   C 2  58  ? -16.990 15.148  54.411   1.00 77.48  ? 60  LYS   D NZ    1 
ATOM   7389  N  N     . TYR   C 2  59  ? -16.334 15.718  46.739   1.00 73.56  ? 61  TYR   D N     1 
ATOM   7390  C  CA    . TYR   C 2  59  ? -16.716 15.102  45.468   1.00 66.42  ? 61  TYR   D CA    1 
ATOM   7391  C  C     . TYR   C 2  59  ? -17.312 13.726  45.738   1.00 61.54  ? 61  TYR   D C     1 
ATOM   7392  O  O     . TYR   C 2  59  ? -16.616 12.837  46.242   1.00 60.63  ? 61  TYR   D O     1 
ATOM   7393  C  CB    . TYR   C 2  59  ? -15.512 14.992  44.514   1.00 61.45  ? 61  TYR   D CB    1 
ATOM   7394  C  CG    . TYR   C 2  59  ? -14.989 16.324  44.029   1.00 61.42  ? 61  TYR   D CG    1 
ATOM   7395  C  CD1   . TYR   C 2  59  ? -15.640 17.014  43.020   1.00 68.52  ? 61  TYR   D CD1   1 
ATOM   7396  C  CD2   . TYR   C 2  59  ? -13.850 16.897  44.580   1.00 62.66  ? 61  TYR   D CD2   1 
ATOM   7397  C  CE1   . TYR   C 2  59  ? -15.177 18.241  42.570   1.00 62.00  ? 61  TYR   D CE1   1 
ATOM   7398  C  CE2   . TYR   C 2  59  ? -13.381 18.123  44.137   1.00 54.15  ? 61  TYR   D CE2   1 
ATOM   7399  C  CZ    . TYR   C 2  59  ? -14.052 18.789  43.127   1.00 59.20  ? 61  TYR   D CZ    1 
ATOM   7400  O  OH    . TYR   C 2  59  ? -13.611 20.010  42.666   1.00 59.52  ? 61  TYR   D OH    1 
ATOM   7401  N  N     . VAL   C 2  60  ? -18.578 13.539  45.381   1.00 56.38  ? 62  VAL   D N     1 
ATOM   7402  C  CA    . VAL   C 2  60  ? -19.308 12.311  45.688   1.00 63.00  ? 62  VAL   D CA    1 
ATOM   7403  C  C     . VAL   C 2  60  ? -19.402 11.465  44.421   1.00 56.95  ? 62  VAL   D C     1 
ATOM   7404  O  O     . VAL   C 2  60  ? -19.971 11.931  43.422   1.00 56.58  ? 62  VAL   D O     1 
ATOM   7405  C  CB    . VAL   C 2  60  ? -20.705 12.602  46.253   1.00 60.04  ? 62  VAL   D CB    1 
ATOM   7406  C  CG1   . VAL   C 2  60  ? -21.125 11.480  47.182   1.00 63.77  ? 62  VAL   D CG1   1 
ATOM   7407  C  CG2   . VAL   C 2  60  ? -20.722 13.928  46.973   1.00 66.53  ? 62  VAL   D CG2   1 
ATOM   7408  N  N     . PRO   C 2  61  ? -18.898 10.227  44.423   1.00 53.34  ? 63  PRO   D N     1 
ATOM   7409  C  CA    . PRO   C 2  61  ? -19.091 9.346   43.259   1.00 49.73  ? 63  PRO   D CA    1 
ATOM   7410  C  C     . PRO   C 2  61  ? -20.551 9.207   42.872   1.00 48.23  ? 63  PRO   D C     1 
ATOM   7411  O  O     . PRO   C 2  61  ? -21.283 8.448   43.516   1.00 49.63  ? 63  PRO   D O     1 
ATOM   7412  C  CB    . PRO   C 2  61  ? -18.528 7.996   43.728   1.00 45.66  ? 63  PRO   D CB    1 
ATOM   7413  C  CG    . PRO   C 2  61  ? -17.605 8.337   44.859   1.00 54.21  ? 63  PRO   D CG    1 
ATOM   7414  C  CD    . PRO   C 2  61  ? -18.175 9.562   45.518   1.00 52.18  ? 63  PRO   D CD    1 
ATOM   7415  N  N     . ARG   C 2  62  ? -20.989 9.914   41.827   1.00 52.91  ? 64  ARG   D N     1 
ATOM   7416  C  CA    . ARG   C 2  62  ? -22.348 9.724   41.324   1.00 50.25  ? 64  ARG   D CA    1 
ATOM   7417  C  C     . ARG   C 2  62  ? -22.603 8.251   41.044   1.00 45.91  ? 64  ARG   D C     1 
ATOM   7418  O  O     . ARG   C 2  62  ? -22.701 7.846   39.880   1.00 50.02  ? 64  ARG   D O     1 
ATOM   7419  C  CB    . ARG   C 2  62  ? -22.600 10.542  40.056   1.00 48.41  ? 64  ARG   D CB    1 
ATOM   7420  C  CG    . ARG   C 2  62  ? -24.058 10.511  39.620   1.00 49.81  ? 64  ARG   D CG    1 
ATOM   7421  C  CD    . ARG   C 2  62  ? -24.302 11.324  38.362   1.00 51.93  ? 64  ARG   D CD    1 
ATOM   7422  N  NE    . ARG   C 2  62  ? -23.770 12.678  38.468   1.00 52.78  ? 64  ARG   D NE    1 
ATOM   7423  C  CZ    . ARG   C 2  62  ? -22.670 13.112  37.866   1.00 45.40  ? 64  ARG   D CZ    1 
ATOM   7424  N  NH1   . ARG   C 2  62  ? -21.935 12.317  37.102   1.00 40.56  ? 64  ARG   D NH1   1 
ATOM   7425  N  NH2   . ARG   C 2  62  ? -22.304 14.379  38.029   1.00 36.96  ? 64  ARG   D NH2   1 
ATOM   7426  N  N     . ALA   C 2  63  ? -22.715 7.446   42.105   1.00 56.85  ? 65  ALA   D N     1 
ATOM   7427  C  CA    . ALA   C 2  63  ? -22.861 6.002   41.989   1.00 52.77  ? 65  ALA   D CA    1 
ATOM   7428  C  C     . ALA   C 2  63  ? -24.046 5.514   42.818   1.00 50.55  ? 65  ALA   D C     1 
ATOM   7429  O  O     . ALA   C 2  63  ? -24.504 6.177   43.750   1.00 57.50  ? 65  ALA   D O     1 
ATOM   7430  C  CB    . ALA   C 2  63  ? -21.576 5.279   42.416   1.00 37.89  ? 65  ALA   D CB    1 
ATOM   7431  N  N     . ILE   C 2  64  ? -24.508 4.318   42.470   1.00 43.31  ? 66  ILE   D N     1 
ATOM   7432  C  CA    . ILE   C 2  64  ? -25.765 3.738   42.919   1.00 42.90  ? 66  ILE   D CA    1 
ATOM   7433  C  C     . ILE   C 2  64  ? -25.510 2.240   43.068   1.00 53.61  ? 66  ILE   D C     1 
ATOM   7434  O  O     . ILE   C 2  64  ? -25.149 1.574   42.088   1.00 48.19  ? 66  ILE   D O     1 
ATOM   7435  C  CB    . ILE   C 2  64  ? -26.892 4.020   41.900   1.00 41.99  ? 66  ILE   D CB    1 
ATOM   7436  C  CG1   . ILE   C 2  64  ? -27.278 5.494   41.899   1.00 44.08  ? 66  ILE   D CG1   1 
ATOM   7437  C  CG2   . ILE   C 2  64  ? -28.120 3.124   42.062   1.00 30.18  ? 66  ILE   D CG2   1 
ATOM   7438  C  CD1   . ILE   C 2  64  ? -28.172 5.855   40.697   1.00 43.25  ? 66  ILE   D CD1   1 
ATOM   7439  N  N     . LEU   C 2  65  ? -25.670 1.710   44.286   1.00 55.41  ? 67  LEU   D N     1 
ATOM   7440  C  CA    . LEU   C 2  65  ? -25.169 0.383   44.648   1.00 49.33  ? 67  LEU   D CA    1 
ATOM   7441  C  C     . LEU   C 2  65  ? -26.329 -0.528  45.026   1.00 52.02  ? 67  LEU   D C     1 
ATOM   7442  O  O     . LEU   C 2  65  ? -27.058 -0.243  45.982   1.00 52.40  ? 67  LEU   D O     1 
ATOM   7443  C  CB    . LEU   C 2  65  ? -24.169 0.481   45.799   1.00 44.90  ? 67  LEU   D CB    1 
ATOM   7444  C  CG    . LEU   C 2  65  ? -22.998 1.456   45.650   1.00 49.65  ? 67  LEU   D CG    1 
ATOM   7445  C  CD1   . LEU   C 2  65  ? -23.348 2.852   46.149   1.00 46.79  ? 67  LEU   D CD1   1 
ATOM   7446  C  CD2   . LEU   C 2  65  ? -21.756 0.913   46.365   1.00 53.72  ? 67  LEU   D CD2   1 
ATOM   7447  N  N     . VAL   C 2  66  ? -26.471 -1.641  44.308   1.00 45.86  ? 68  VAL   D N     1 
ATOM   7448  C  CA    . VAL   C 2  66  ? -27.686 -2.450  44.324   1.00 45.79  ? 68  VAL   D CA    1 
ATOM   7449  C  C     . VAL   C 2  66  ? -27.309 -3.902  44.586   1.00 55.07  ? 68  VAL   D C     1 
ATOM   7450  O  O     . VAL   C 2  66  ? -26.492 -4.476  43.857   1.00 58.01  ? 68  VAL   D O     1 
ATOM   7451  C  CB    . VAL   C 2  66  ? -28.463 -2.324  42.993   1.00 47.36  ? 68  VAL   D CB    1 
ATOM   7452  C  CG1   . VAL   C 2  66  ? -29.790 -3.086  43.034   1.00 46.42  ? 68  VAL   D CG1   1 
ATOM   7453  C  CG2   . VAL   C 2  66  ? -28.691 -0.859  42.633   1.00 46.94  ? 68  VAL   D CG2   1 
ATOM   7454  N  N     . ASP   C 2  67  ? -27.912 -4.501  45.614   1.00 58.23  ? 69  ASP   D N     1 
ATOM   7455  C  CA    . ASP   C 2  67  ? -27.772 -5.936  45.834   1.00 57.03  ? 69  ASP   D CA    1 
ATOM   7456  C  C     . ASP   C 2  67  ? -29.035 -6.474  46.482   1.00 59.70  ? 69  ASP   D C     1 
ATOM   7457  O  O     . ASP   C 2  67  ? -29.510 -5.913  47.472   1.00 66.33  ? 69  ASP   D O     1 
ATOM   7458  C  CB    . ASP   C 2  67  ? -26.566 -6.256  46.714   1.00 60.68  ? 69  ASP   D CB    1 
ATOM   7459  C  CG    . ASP   C 2  67  ? -25.863 -7.526  46.288   1.00 57.65  ? 69  ASP   D CG    1 
ATOM   7460  O  OD1   . ASP   C 2  67  ? -26.511 -8.375  45.628   1.00 51.48  ? 69  ASP   D OD1   1 
ATOM   7461  O  OD2   . ASP   C 2  67  ? -24.664 -7.666  46.608   1.00 53.30  ? 69  ASP   D OD2   1 
ATOM   7462  N  N     . LEU   C 2  68  ? -29.566 -7.558  45.924   1.00 58.62  ? 70  LEU   D N     1 
ATOM   7463  C  CA    . LEU   C 2  68  ? -30.712 -8.244  46.504   1.00 61.43  ? 70  LEU   D CA    1 
ATOM   7464  C  C     . LEU   C 2  68  ? -30.429 -8.830  47.881   1.00 68.49  ? 70  LEU   D C     1 
ATOM   7465  O  O     . LEU   C 2  68  ? -31.332 -9.382  48.503   1.00 70.74  ? 70  LEU   D O     1 
ATOM   7466  C  CB    . LEU   C 2  68  ? -31.176 -9.371  45.584   1.00 54.11  ? 70  LEU   D CB    1 
ATOM   7467  C  CG    . LEU   C 2  68  ? -32.120 -8.941  44.478   1.00 54.29  ? 70  LEU   D CG    1 
ATOM   7468  C  CD1   . LEU   C 2  68  ? -32.833 -10.144 43.912   1.00 54.53  ? 70  LEU   D CD1   1 
ATOM   7469  C  CD2   . LEU   C 2  68  ? -33.102 -7.903  45.012   1.00 60.53  ? 70  LEU   D CD2   1 
ATOM   7470  N  N     . GLU   C 2  69  ? -29.183 -8.739  48.345   1.00 73.92  ? 71  GLU   D N     1 
ATOM   7471  C  CA    . GLU   C 2  69  ? -28.685 -9.351  49.569   1.00 71.04  ? 71  GLU   D CA    1 
ATOM   7472  C  C     . GLU   C 2  69  ? -27.584 -8.430  50.068   1.00 69.05  ? 71  GLU   D C     1 
ATOM   7473  O  O     . GLU   C 2  69  ? -26.637 -8.160  49.322   1.00 67.21  ? 71  GLU   D O     1 
ATOM   7474  C  CB    . GLU   C 2  69  ? -28.174 -10.772 49.292   1.00 78.96  ? 71  GLU   D CB    1 
ATOM   7475  C  CG    . GLU   C 2  69  ? -27.570 -11.519 50.486   1.00 83.49  ? 71  GLU   D CG    1 
ATOM   7476  C  CD    . GLU   C 2  69  ? -26.190 -11.006 50.856   1.00 88.41  ? 71  GLU   D CD    1 
ATOM   7477  O  OE1   . GLU   C 2  69  ? -25.530 -10.407 49.968   1.00 76.24  ? 71  GLU   D OE1   1 
ATOM   7478  O  OE2   . GLU   C 2  69  ? -25.779 -11.190 52.030   1.00 74.29  ? 71  GLU   D OE2   1 
ATOM   7479  N  N     . PRO   C 2  70  ? -27.678 -7.908  51.300   1.00 80.46  ? 72  PRO   D N     1 
ATOM   7480  C  CA    . PRO   C 2  70  ? -26.730 -6.867  51.743   1.00 84.21  ? 72  PRO   D CA    1 
ATOM   7481  C  C     . PRO   C 2  70  ? -25.289 -7.339  51.728   1.00 85.39  ? 72  PRO   D C     1 
ATOM   7482  O  O     . PRO   C 2  70  ? -24.700 -7.544  50.661   1.00 83.11  ? 72  PRO   D O     1 
ATOM   7483  C  CB    . PRO   C 2  70  ? -27.184 -6.546  53.174   1.00 74.02  ? 72  PRO   D CB    1 
ATOM   7484  C  CG    . PRO   C 2  70  ? -28.595 -7.043  53.253   1.00 83.13  ? 72  PRO   D CG    1 
ATOM   7485  C  CD    . PRO   C 2  70  ? -28.667 -8.237  52.338   1.00 79.11  ? 72  PRO   D CD    1 
ATOM   7486  N  N     . GLY   C 2  71  ? -24.713 -7.513  52.913   1.00 79.67  ? 73  GLY   D N     1 
ATOM   7487  C  CA    . GLY   C 2  71  ? -23.359 -8.016  53.007   1.00 83.19  ? 73  GLY   D CA    1 
ATOM   7488  C  C     . GLY   C 2  71  ? -22.395 -7.294  52.090   1.00 82.87  ? 73  GLY   D C     1 
ATOM   7489  O  O     . GLY   C 2  71  ? -21.599 -6.468  52.549   1.00 84.45  ? 73  GLY   D O     1 
ATOM   7490  N  N     . THR   C 2  72  ? -22.463 -7.594  50.786   1.00 85.86  ? 74  THR   D N     1 
ATOM   7491  C  CA    . THR   C 2  72  ? -21.581 -6.935  49.823   1.00 88.29  ? 74  THR   D CA    1 
ATOM   7492  C  C     . THR   C 2  72  ? -21.682 -5.414  49.935   1.00 85.72  ? 74  THR   D C     1 
ATOM   7493  O  O     . THR   C 2  72  ? -20.673 -4.704  49.811   1.00 80.10  ? 74  THR   D O     1 
ATOM   7494  C  CB    . THR   C 2  72  ? -21.893 -7.415  48.395   1.00 83.59  ? 74  THR   D CB    1 
ATOM   7495  O  OG1   . THR   C 2  72  ? -23.216 -7.973  48.332   1.00 70.10  ? 74  THR   D OG1   1 
ATOM   7496  C  CG2   . THR   C 2  72  ? -20.873 -8.477  47.944   1.00 72.48  ? 74  THR   D CG2   1 
ATOM   7497  N  N     . MET   C 2  73  ? -22.887 -4.897  50.198   1.00 78.00  ? 75  MET   D N     1 
ATOM   7498  C  CA    . MET   C 2  73  ? -23.031 -3.482  50.532   1.00 84.54  ? 75  MET   D CA    1 
ATOM   7499  C  C     . MET   C 2  73  ? -22.188 -3.123  51.757   1.00 81.47  ? 75  MET   D C     1 
ATOM   7500  O  O     . MET   C 2  73  ? -21.489 -2.102  51.769   1.00 75.69  ? 75  MET   D O     1 
ATOM   7501  C  CB    . MET   C 2  73  ? -24.509 -3.136  50.773   1.00 90.19  ? 75  MET   D CB    1 
ATOM   7502  C  CG    . MET   C 2  73  ? -25.525 -3.689  49.742   1.00 89.84  ? 75  MET   D CG    1 
ATOM   7503  S  SD    . MET   C 2  73  ? -25.809 -2.752  48.199   1.00 73.88  ? 75  MET   D SD    1 
ATOM   7504  C  CE    . MET   C 2  73  ? -26.005 -1.080  48.820   1.00 59.36  ? 75  MET   D CE    1 
ATOM   7505  N  N     . ASP   C 2  74  ? -22.252 -3.955  52.805   1.00 80.62  ? 76  ASP   D N     1 
ATOM   7506  C  CA    . ASP   C 2  74  ? -21.454 -3.722  54.010   1.00 87.90  ? 76  ASP   D CA    1 
ATOM   7507  C  C     . ASP   C 2  74  ? -19.968 -3.628  53.675   1.00 81.63  ? 76  ASP   D C     1 
ATOM   7508  O  O     . ASP   C 2  74  ? -19.294 -2.650  54.030   1.00 68.33  ? 76  ASP   D O     1 
ATOM   7509  C  CB    . ASP   C 2  74  ? -21.692 -4.849  55.024   1.00 84.66  ? 76  ASP   D CB    1 
ATOM   7510  C  CG    . ASP   C 2  74  ? -22.942 -4.650  55.854   1.00 83.76  ? 76  ASP   D CG    1 
ATOM   7511  O  OD1   . ASP   C 2  74  ? -24.055 -4.842  55.315   1.00 79.94  ? 76  ASP   D OD1   1 
ATOM   7512  O  OD2   . ASP   C 2  74  ? -22.805 -4.320  57.053   1.00 87.15  ? 76  ASP   D OD2   1 
ATOM   7513  N  N     . SER   C 2  75  ? -19.446 -4.660  53.004   1.00 77.42  ? 77  SER   D N     1 
ATOM   7514  C  CA    . SER   C 2  75  ? -18.044 -4.726  52.601   1.00 73.47  ? 77  SER   D CA    1 
ATOM   7515  C  C     . SER   C 2  75  ? -17.573 -3.428  51.953   1.00 80.25  ? 77  SER   D C     1 
ATOM   7516  O  O     . SER   C 2  75  ? -16.591 -2.816  52.391   1.00 76.57  ? 77  SER   D O     1 
ATOM   7517  C  CB    . SER   C 2  75  ? -17.874 -5.896  51.642   1.00 72.06  ? 77  SER   D CB    1 
ATOM   7518  O  OG    . SER   C 2  75  ? -18.911 -5.863  50.677   1.00 77.57  ? 77  SER   D OG    1 
ATOM   7519  N  N     . VAL   C 2  76  ? -18.258 -3.005  50.885   1.00 81.64  ? 78  VAL   D N     1 
ATOM   7520  C  CA    . VAL   C 2  76  ? -17.930 -1.736  50.232   1.00 77.88  ? 78  VAL   D CA    1 
ATOM   7521  C  C     . VAL   C 2  76  ? -17.850 -0.611  51.259   1.00 79.19  ? 78  VAL   D C     1 
ATOM   7522  O  O     . VAL   C 2  76  ? -16.877 0.155   51.294   1.00 83.82  ? 78  VAL   D O     1 
ATOM   7523  C  CB    . VAL   C 2  76  ? -18.956 -1.425  49.124   1.00 69.25  ? 78  VAL   D CB    1 
ATOM   7524  C  CG1   . VAL   C 2  76  ? -19.217 0.079   49.033   1.00 54.39  ? 78  VAL   D CG1   1 
ATOM   7525  C  CG2   . VAL   C 2  76  ? -18.486 -2.001  47.778   1.00 43.77  ? 78  VAL   D CG2   1 
ATOM   7526  N  N     . ARG   C 2  77  ? -18.874 -0.501  52.118   1.00 81.29  ? 79  ARG   D N     1 
ATOM   7527  C  CA    . ARG   C 2  77  ? -18.916 0.568   53.116   1.00 78.63  ? 79  ARG   D CA    1 
ATOM   7528  C  C     . ARG   C 2  77  ? -17.628 0.628   53.930   1.00 83.37  ? 79  ARG   D C     1 
ATOM   7529  O  O     . ARG   C 2  77  ? -17.094 1.713   54.190   1.00 81.12  ? 79  ARG   D O     1 
ATOM   7530  C  CB    . ARG   C 2  77  ? -20.116 0.373   54.049   1.00 77.84  ? 79  ARG   D CB    1 
ATOM   7531  C  CG    . ARG   C 2  77  ? -21.406 1.089   53.652   1.00 72.37  ? 79  ARG   D CG    1 
ATOM   7532  C  CD    . ARG   C 2  77  ? -22.428 0.971   54.782   1.00 70.27  ? 79  ARG   D CD    1 
ATOM   7533  N  NE    . ARG   C 2  77  ? -23.680 1.685   54.545   1.00 64.38  ? 79  ARG   D NE    1 
ATOM   7534  C  CZ    . ARG   C 2  77  ? -24.809 1.117   54.132   1.00 72.45  ? 79  ARG   D CZ    1 
ATOM   7535  N  NH1   . ARG   C 2  77  ? -24.867 -0.172  53.825   1.00 75.29  ? 79  ARG   D NH1   1 
ATOM   7536  N  NH2   . ARG   C 2  77  ? -25.908 1.861   54.023   1.00 70.47  ? 79  ARG   D NH2   1 
ATOM   7537  N  N     . SER   C 2  78  ? -17.110 -0.534  54.339   1.00 88.32  ? 80  SER   D N     1 
ATOM   7538  C  CA    . SER   C 2  78  ? -15.949 -0.569  55.224   1.00 90.64  ? 80  SER   D CA    1 
ATOM   7539  C  C     . SER   C 2  78  ? -14.651 -0.305  54.471   1.00 87.04  ? 80  SER   D C     1 
ATOM   7540  O  O     . SER   C 2  78  ? -13.748 0.364   54.993   1.00 74.80  ? 80  SER   D O     1 
ATOM   7541  C  CB    . SER   C 2  78  ? -15.881 -1.922  55.935   1.00 88.30  ? 80  SER   D CB    1 
ATOM   7542  O  OG    . SER   C 2  78  ? -17.113 -2.233  56.567   1.00 94.46  ? 80  SER   D OG    1 
ATOM   7543  N  N     . GLY   C 2  79  ? -14.554 -0.809  53.242   1.00 93.40  ? 81  GLY   D N     1 
ATOM   7544  C  CA    . GLY   C 2  79  ? -13.322 -0.813  52.491   1.00 91.29  ? 81  GLY   D CA    1 
ATOM   7545  C  C     . GLY   C 2  79  ? -12.787 0.562   52.143   1.00 91.02  ? 81  GLY   D C     1 
ATOM   7546  O  O     . GLY   C 2  79  ? -13.281 1.600   52.607   1.00 82.74  ? 81  GLY   D O     1 
ATOM   7547  N  N     . PRO   C 2  80  ? -11.743 0.580   51.308   1.00 96.91  ? 82  PRO   D N     1 
ATOM   7548  C  CA    . PRO   C 2  80  ? -11.128 1.850   50.883   1.00 92.91  ? 82  PRO   D CA    1 
ATOM   7549  C  C     . PRO   C 2  80  ? -12.057 2.590   49.933   1.00 89.20  ? 82  PRO   D C     1 
ATOM   7550  O  O     . PRO   C 2  80  ? -12.404 2.085   48.860   1.00 80.48  ? 82  PRO   D O     1 
ATOM   7551  C  CB    . PRO   C 2  80  ? -9.842  1.401   50.180   1.00 80.77  ? 82  PRO   D CB    1 
ATOM   7552  C  CG    . PRO   C 2  80  ? -10.202 0.050   49.621   1.00 86.58  ? 82  PRO   D CG    1 
ATOM   7553  C  CD    . PRO   C 2  80  ? -11.136 -0.583  50.633   1.00 90.07  ? 82  PRO   D CD    1 
ATOM   7554  N  N     . PHE   C 2  81  ? -12.460 3.791   50.338   1.00 88.12  ? 83  PHE   D N     1 
ATOM   7555  C  CA    . PHE   C 2  81  ? -13.428 4.603   49.620   1.00 86.21  ? 83  PHE   D CA    1 
ATOM   7556  C  C     . PHE   C 2  81  ? -14.859 4.135   49.843   1.00 79.10  ? 83  PHE   D C     1 
ATOM   7557  O  O     . PHE   C 2  81  ? -15.761 4.539   49.103   1.00 78.77  ? 83  PHE   D O     1 
ATOM   7558  C  CB    . PHE   C 2  81  ? -13.104 4.655   48.121   1.00 81.36  ? 83  PHE   D CB    1 
ATOM   7559  C  CG    . PHE   C 2  81  ? -11.824 5.375   47.817   1.00 75.35  ? 83  PHE   D CG    1 
ATOM   7560  C  CD1   . PHE   C 2  81  ? -10.609 4.725   47.925   1.00 77.18  ? 83  PHE   D CD1   1 
ATOM   7561  C  CD2   . PHE   C 2  81  ? -11.836 6.714   47.457   1.00 74.84  ? 83  PHE   D CD2   1 
ATOM   7562  C  CE1   . PHE   C 2  81  ? -9.423  5.393   47.663   1.00 83.05  ? 83  PHE   D CE1   1 
ATOM   7563  C  CE2   . PHE   C 2  81  ? -10.657 7.390   47.190   1.00 78.30  ? 83  PHE   D CE2   1 
ATOM   7564  C  CZ    . PHE   C 2  81  ? -9.446  6.729   47.295   1.00 81.65  ? 83  PHE   D CZ    1 
ATOM   7565  N  N     . GLY   C 2  82  ? -15.100 3.299   50.856   1.00 79.84  ? 84  GLY   D N     1 
ATOM   7566  C  CA    . GLY   C 2  82  ? -16.472 2.993   51.225   1.00 79.48  ? 84  GLY   D CA    1 
ATOM   7567  C  C     . GLY   C 2  82  ? -17.232 4.223   51.688   1.00 81.51  ? 84  GLY   D C     1 
ATOM   7568  O  O     . GLY   C 2  82  ? -18.418 4.388   51.382   1.00 74.46  ? 84  GLY   D O     1 
ATOM   7569  N  N     . GLN   C 2  83  ? -16.551 5.113   52.416   1.00 81.48  ? 85  GLN   D N     1 
ATOM   7570  C  CA    . GLN   C 2  83  ? -17.154 6.294   53.024   1.00 84.99  ? 85  GLN   D CA    1 
ATOM   7571  C  C     . GLN   C 2  83  ? -17.273 7.463   52.062   1.00 82.32  ? 85  GLN   D C     1 
ATOM   7572  O  O     . GLN   C 2  83  ? -17.547 8.585   52.505   1.00 85.30  ? 85  GLN   D O     1 
ATOM   7573  C  CB    . GLN   C 2  83  ? -16.349 6.731   54.256   1.00 88.38  ? 85  GLN   D CB    1 
ATOM   7574  C  CG    . GLN   C 2  83  ? -16.633 5.922   55.528   1.00 92.66  ? 85  GLN   D CG    1 
ATOM   7575  C  CD    . GLN   C 2  83  ? -15.956 4.558   55.540   1.00 93.79  ? 85  GLN   D CD    1 
ATOM   7576  O  OE1   . GLN   C 2  83  ? -14.817 4.410   55.086   1.00 93.29  ? 85  GLN   D OE1   1 
ATOM   7577  N  NE2   . GLN   C 2  83  ? -16.658 3.553   56.064   1.00 89.70  ? 85  GLN   D NE2   1 
ATOM   7578  N  N     . ILE   C 2  84  ? -17.063 7.235   50.766   1.00 87.02  ? 86  ILE   D N     1 
ATOM   7579  C  CA    . ILE   C 2  84  ? -17.151 8.304   49.775   1.00 85.28  ? 86  ILE   D CA    1 
ATOM   7580  C  C     . ILE   C 2  84  ? -18.518 8.335   49.091   1.00 72.14  ? 86  ILE   D C     1 
ATOM   7581  O  O     . ILE   C 2  84  ? -18.951 9.410   48.643   1.00 67.58  ? 86  ILE   D O     1 
ATOM   7582  C  CB    . ILE   C 2  84  ? -16.012 8.174   48.734   1.00 72.28  ? 86  ILE   D CB    1 
ATOM   7583  C  CG1   . ILE   C 2  84  ? -15.870 9.449   47.906   1.00 66.97  ? 86  ILE   D CG1   1 
ATOM   7584  C  CG2   . ILE   C 2  84  ? -16.231 6.975   47.827   1.00 70.11  ? 86  ILE   D CG2   1 
ATOM   7585  C  CD1   . ILE   C 2  84  ? -14.804 9.340   46.833   1.00 66.03  ? 86  ILE   D CD1   1 
ATOM   7586  N  N     . PHE   C 2  85  ? -19.224 7.210   49.049   1.00 61.86  ? 87  PHE   D N     1 
ATOM   7587  C  CA    . PHE   C 2  85  ? -20.504 7.129   48.370   1.00 69.27  ? 87  PHE   D CA    1 
ATOM   7588  C  C     . PHE   C 2  85  ? -21.613 7.845   49.148   1.00 76.11  ? 87  PHE   D C     1 
ATOM   7589  O  O     . PHE   C 2  85  ? -21.538 8.028   50.366   1.00 77.47  ? 87  PHE   D O     1 
ATOM   7590  C  CB    . PHE   C 2  85  ? -20.853 5.661   48.141   1.00 62.10  ? 87  PHE   D CB    1 
ATOM   7591  C  CG    . PHE   C 2  85  ? -19.819 4.922   47.321   1.00 72.86  ? 87  PHE   D CG    1 
ATOM   7592  C  CD1   . PHE   C 2  85  ? -19.723 5.125   45.948   1.00 61.92  ? 87  PHE   D CD1   1 
ATOM   7593  C  CD2   . PHE   C 2  85  ? -18.936 4.036   47.919   1.00 74.88  ? 87  PHE   D CD2   1 
ATOM   7594  C  CE1   . PHE   C 2  85  ? -18.773 4.450   45.194   1.00 58.72  ? 87  PHE   D CE1   1 
ATOM   7595  C  CE2   . PHE   C 2  85  ? -17.986 3.360   47.162   1.00 67.84  ? 87  PHE   D CE2   1 
ATOM   7596  C  CZ    . PHE   C 2  85  ? -17.910 3.565   45.799   1.00 53.83  ? 87  PHE   D CZ    1 
ATOM   7597  N  N     . ARG   C 2  86  ? -22.644 8.283   48.406   1.00 78.27  ? 88  ARG   D N     1 
ATOM   7598  C  CA    . ARG   C 2  86  ? -23.870 8.865   48.951   1.00 73.80  ? 88  ARG   D CA    1 
ATOM   7599  C  C     . ARG   C 2  86  ? -24.676 7.752   49.608   1.00 69.04  ? 88  ARG   D C     1 
ATOM   7600  O  O     . ARG   C 2  86  ? -25.297 6.941   48.909   1.00 67.34  ? 88  ARG   D O     1 
ATOM   7601  C  CB    . ARG   C 2  86  ? -24.677 9.564   47.846   1.00 71.39  ? 88  ARG   D CB    1 
ATOM   7602  C  CG    . ARG   C 2  86  ? -26.153 9.842   48.154   1.00 72.96  ? 88  ARG   D CG    1 
ATOM   7603  C  CD    . ARG   C 2  86  ? -26.731 10.960  47.261   1.00 66.00  ? 88  ARG   D CD    1 
ATOM   7604  N  NE    . ARG   C 2  86  ? -26.209 12.274  47.627   1.00 75.23  ? 88  ARG   D NE    1 
ATOM   7605  C  CZ    . ARG   C 2  86  ? -25.240 12.915  46.980   1.00 79.18  ? 88  ARG   D CZ    1 
ATOM   7606  N  NH1   . ARG   C 2  86  ? -24.704 12.426  45.872   1.00 82.31  ? 88  ARG   D NH1   1 
ATOM   7607  N  NH2   . ARG   C 2  86  ? -24.797 14.076  47.456   1.00 73.84  ? 88  ARG   D NH2   1 
ATOM   7608  N  N     . PRO   C 2  87  ? -24.691 7.684   50.944   1.00 68.94  ? 89  PRO   D N     1 
ATOM   7609  C  CA    . PRO   C 2  87  ? -25.244 6.498   51.615   1.00 62.72  ? 89  PRO   D CA    1 
ATOM   7610  C  C     . PRO   C 2  87  ? -26.706 6.259   51.300   1.00 63.84  ? 89  PRO   D C     1 
ATOM   7611  O  O     . PRO   C 2  87  ? -27.214 5.156   51.548   1.00 65.73  ? 89  PRO   D O     1 
ATOM   7612  C  CB    . PRO   C 2  87  ? -25.019 6.803   53.102   1.00 60.54  ? 89  PRO   D CB    1 
ATOM   7613  C  CG    . PRO   C 2  87  ? -24.986 8.283   53.176   1.00 60.64  ? 89  PRO   D CG    1 
ATOM   7614  C  CD    . PRO   C 2  87  ? -24.361 8.756   51.898   1.00 69.16  ? 89  PRO   D CD    1 
ATOM   7615  N  N     . ASP   C 2  88  ? -27.398 7.248   50.750   1.00 54.64  ? 90  ASP   D N     1 
ATOM   7616  C  CA    . ASP   C 2  88  ? -28.734 7.027   50.226   1.00 59.82  ? 90  ASP   D CA    1 
ATOM   7617  C  C     . ASP   C 2  88  ? -28.729 6.324   48.880   1.00 67.81  ? 90  ASP   D C     1 
ATOM   7618  O  O     . ASP   C 2  88  ? -29.783 5.859   48.442   1.00 69.74  ? 90  ASP   D O     1 
ATOM   7619  C  CB    . ASP   C 2  88  ? -29.438 8.360   50.116   1.00 61.77  ? 90  ASP   D CB    1 
ATOM   7620  C  CG    . ASP   C 2  88  ? -29.000 9.303   51.200   1.00 81.17  ? 90  ASP   D CG    1 
ATOM   7621  O  OD1   . ASP   C 2  88  ? -29.586 9.247   52.308   1.00 85.34  ? 90  ASP   D OD1   1 
ATOM   7622  O  OD2   . ASP   C 2  88  ? -28.024 10.054  50.962   1.00 81.09  ? 90  ASP   D OD2   1 
ATOM   7623  N  N     . ASN   C 2  89  ? -27.575 6.240   48.212   1.00 71.19  ? 91  ASN   D N     1 
ATOM   7624  C  CA    . ASN   C 2  89  ? -27.465 5.506   46.958   1.00 62.56  ? 91  ASN   D CA    1 
ATOM   7625  C  C     . ASN   C 2  89  ? -27.242 4.011   47.169   1.00 63.70  ? 91  ASN   D C     1 
ATOM   7626  O  O     . ASN   C 2  89  ? -27.387 3.234   46.214   1.00 48.56  ? 91  ASN   D O     1 
ATOM   7627  C  CB    . ASN   C 2  89  ? -26.342 6.101   46.100   1.00 63.45  ? 91  ASN   D CB    1 
ATOM   7628  C  CG    . ASN   C 2  89  ? -26.681 7.496   45.575   1.00 58.49  ? 91  ASN   D CG    1 
ATOM   7629  O  OD1   . ASN   C 2  89  ? -27.631 8.128   46.032   1.00 57.02  ? 91  ASN   D OD1   1 
ATOM   7630  N  ND2   . ASN   C 2  89  ? -25.895 7.979   44.622   1.00 47.26  ? 91  ASN   D ND2   1 
ATOM   7631  N  N     . PHE   C 2  90  ? -26.900 3.586   48.388   1.00 60.14  ? 92  PHE   D N     1 
ATOM   7632  C  CA    . PHE   C 2  90  ? -26.976 2.172   48.716   1.00 54.79  ? 92  PHE   D CA    1 
ATOM   7633  C  C     . PHE   C 2  90  ? -28.442 1.766   48.755   1.00 52.91  ? 92  PHE   D C     1 
ATOM   7634  O  O     . PHE   C 2  90  ? -29.215 2.305   49.548   1.00 70.77  ? 92  PHE   D O     1 
ATOM   7635  C  CB    . PHE   C 2  90  ? -26.319 1.877   50.061   1.00 53.14  ? 92  PHE   D CB    1 
ATOM   7636  C  CG    . PHE   C 2  90  ? -24.855 2.224   50.138   1.00 51.47  ? 92  PHE   D CG    1 
ATOM   7637  C  CD1   . PHE   C 2  90  ? -24.445 3.500   50.509   1.00 58.20  ? 92  PHE   D CD1   1 
ATOM   7638  C  CD2   . PHE   C 2  90  ? -23.889 1.260   49.908   1.00 50.90  ? 92  PHE   D CD2   1 
ATOM   7639  C  CE1   . PHE   C 2  90  ? -23.101 3.815   50.620   1.00 55.98  ? 92  PHE   D CE1   1 
ATOM   7640  C  CE2   . PHE   C 2  90  ? -22.545 1.567   50.011   1.00 58.32  ? 92  PHE   D CE2   1 
ATOM   7641  C  CZ    . PHE   C 2  90  ? -22.148 2.848   50.373   1.00 56.06  ? 92  PHE   D CZ    1 
ATOM   7642  N  N     . VAL   C 2  91  ? -28.828 0.839   47.890   1.00 48.78  ? 93  VAL   D N     1 
ATOM   7643  C  CA    . VAL   C 2  91  ? -30.150 0.233   47.892   1.00 50.02  ? 93  VAL   D CA    1 
ATOM   7644  C  C     . VAL   C 2  91  ? -29.935 -1.267  47.837   1.00 57.37  ? 93  VAL   D C     1 
ATOM   7645  O  O     . VAL   C 2  91  ? -29.367 -1.774  46.864   1.00 60.55  ? 93  VAL   D O     1 
ATOM   7646  C  CB    . VAL   C 2  91  ? -31.019 0.699   46.709   1.00 52.65  ? 93  VAL   D CB    1 
ATOM   7647  C  CG1   . VAL   C 2  91  ? -32.209 -0.226  46.520   1.00 46.37  ? 93  VAL   D CG1   1 
ATOM   7648  C  CG2   . VAL   C 2  91  ? -31.490 2.132   46.901   1.00 48.18  ? 93  VAL   D CG2   1 
ATOM   7649  N  N     . PHE   C 2  92  ? -30.386 -1.977  48.869   1.00 64.91  ? 94  PHE   D N     1 
ATOM   7650  C  CA    . PHE   C 2  92  ? -30.094 -3.392  49.031   1.00 65.68  ? 94  PHE   D CA    1 
ATOM   7651  C  C     . PHE   C 2  92  ? -31.366 -4.154  49.373   1.00 61.64  ? 94  PHE   D C     1 
ATOM   7652  O  O     . PHE   C 2  92  ? -32.259 -3.628  50.038   1.00 65.02  ? 94  PHE   D O     1 
ATOM   7653  C  CB    . PHE   C 2  92  ? -29.050 -3.604  50.132   1.00 71.72  ? 94  PHE   D CB    1 
ATOM   7654  C  CG    . PHE   C 2  92  ? -29.401 -2.925  51.428   1.00 78.24  ? 94  PHE   D CG    1 
ATOM   7655  C  CD1   . PHE   C 2  92  ? -30.309 -3.506  52.311   1.00 85.44  ? 94  PHE   D CD1   1 
ATOM   7656  C  CD2   . PHE   C 2  92  ? -28.831 -1.700  51.765   1.00 75.06  ? 94  PHE   D CD2   1 
ATOM   7657  C  CE1   . PHE   C 2  92  ? -30.644 -2.875  53.512   1.00 91.89  ? 94  PHE   D CE1   1 
ATOM   7658  C  CE2   . PHE   C 2  92  ? -29.156 -1.059  52.963   1.00 79.23  ? 94  PHE   D CE2   1 
ATOM   7659  C  CZ    . PHE   C 2  92  ? -30.065 -1.646  53.838   1.00 92.66  ? 94  PHE   D CZ    1 
ATOM   7660  N  N     . GLY   C 2  93  ? -31.441 -5.402  48.910   1.00 64.39  ? 95  GLY   D N     1 
ATOM   7661  C  CA    . GLY   C 2  93  ? -32.509 -6.308  49.295   1.00 64.59  ? 95  GLY   D CA    1 
ATOM   7662  C  C     . GLY   C 2  93  ? -32.207 -7.012  50.601   1.00 67.98  ? 95  GLY   D C     1 
ATOM   7663  O  O     . GLY   C 2  93  ? -31.494 -6.488  51.464   1.00 71.80  ? 95  GLY   D O     1 
ATOM   7664  N  N     . GLN   C 2  94  ? -32.762 -8.214  50.759   1.00 69.20  ? 96  GLN   D N     1 
ATOM   7665  C  CA    . GLN   C 2  94  ? -32.425 -9.072  51.891   1.00 69.87  ? 96  GLN   D CA    1 
ATOM   7666  C  C     . GLN   C 2  94  ? -32.465 -10.537 51.473   1.00 77.03  ? 96  GLN   D C     1 
ATOM   7667  O  O     . GLN   C 2  94  ? -31.510 -11.287 51.703   1.00 79.66  ? 96  GLN   D O     1 
ATOM   7668  C  CB    . GLN   C 2  94  ? -33.384 -8.855  53.070   1.00 76.64  ? 96  GLN   D CB    1 
ATOM   7669  C  CG    . GLN   C 2  94  ? -33.649 -7.407  53.470   1.00 75.39  ? 96  GLN   D CG    1 
ATOM   7670  C  CD    . GLN   C 2  94  ? -32.459 -6.737  54.142   1.00 84.49  ? 96  GLN   D CD    1 
ATOM   7671  O  OE1   . GLN   C 2  94  ? -31.534 -7.401  54.622   1.00 78.73  ? 96  GLN   D OE1   1 
ATOM   7672  N  NE2   . GLN   C 2  94  ? -32.475 -5.409  54.170   1.00 86.63  ? 96  GLN   D NE2   1 
ATOM   7673  N  N     . SER   C 2  95  ? -33.572 -10.945 50.845   1.00 79.56  ? 97  SER   D N     1 
ATOM   7674  C  CA    . SER   C 2  95  ? -33.792 -12.358 50.537   1.00 88.29  ? 97  SER   D CA    1 
ATOM   7675  C  C     . SER   C 2  95  ? -32.688 -12.940 49.657   1.00 90.31  ? 97  SER   D C     1 
ATOM   7676  O  O     . SER   C 2  95  ? -32.403 -14.142 49.743   1.00 86.89  ? 97  SER   D O     1 
ATOM   7677  C  CB    . SER   C 2  95  ? -35.161 -12.532 49.866   1.00 92.12  ? 97  SER   D CB    1 
ATOM   7678  O  OG    . SER   C 2  95  ? -35.516 -13.899 49.725   1.00 84.43  ? 97  SER   D OG    1 
ATOM   7679  N  N     . GLY   C 2  96  ? -32.066 -12.117 48.803   1.00 83.08  ? 98  GLY   D N     1 
ATOM   7680  C  CA    . GLY   C 2  96  ? -31.000 -12.577 47.928   1.00 73.81  ? 98  GLY   D CA    1 
ATOM   7681  C  C     . GLY   C 2  96  ? -31.504 -13.391 46.750   1.00 83.56  ? 98  GLY   D C     1 
ATOM   7682  O  O     . GLY   C 2  96  ? -32.495 -14.122 46.870   1.00 91.57  ? 98  GLY   D O     1 
ATOM   7683  N  N     . ALA   C 2  97  ? -30.833 -13.282 45.603   1.00 77.66  ? 99  ALA   D N     1 
ATOM   7684  C  CA    . ALA   C 2  97  ? -31.307 -13.922 44.381   1.00 70.61  ? 99  ALA   D CA    1 
ATOM   7685  C  C     . ALA   C 2  97  ? -30.739 -15.319 44.183   1.00 63.13  ? 99  ALA   D C     1 
ATOM   7686  O  O     . ALA   C 2  97  ? -31.335 -16.127 43.457   1.00 58.55  ? 99  ALA   D O     1 
ATOM   7687  C  CB    . ALA   C 2  97  ? -30.962 -13.052 43.165   1.00 58.97  ? 99  ALA   D CB    1 
ATOM   7688  N  N     . GLY   C 2  98  ? -29.603 -15.614 44.801   1.00 56.07  ? 100 GLY   D N     1 
ATOM   7689  C  CA    . GLY   C 2  98  ? -29.046 -16.945 44.749   1.00 57.95  ? 100 GLY   D CA    1 
ATOM   7690  C  C     . GLY   C 2  98  ? -28.891 -17.480 43.346   1.00 71.89  ? 100 GLY   D C     1 
ATOM   7691  O  O     . GLY   C 2  98  ? -29.462 -18.528 43.008   1.00 71.72  ? 100 GLY   D O     1 
ATOM   7692  N  N     . ASN   C 2  99  ? -28.136 -16.757 42.512   1.00 62.90  ? 101 ASN   D N     1 
ATOM   7693  C  CA    . ASN   C 2  99  ? -27.703 -17.282 41.220   1.00 55.79  ? 101 ASN   D CA    1 
ATOM   7694  C  C     . ASN   C 2  99  ? -28.879 -17.805 40.397   1.00 59.19  ? 101 ASN   D C     1 
ATOM   7695  O  O     . ASN   C 2  99  ? -28.746 -18.779 39.655   1.00 68.63  ? 101 ASN   D O     1 
ATOM   7696  C  CB    . ASN   C 2  99  ? -26.652 -18.385 41.411   1.00 59.33  ? 101 ASN   D CB    1 
ATOM   7697  C  CG    . ASN   C 2  99  ? -25.311 -17.855 41.932   1.00 67.78  ? 101 ASN   D CG    1 
ATOM   7698  O  OD1   . ASN   C 2  99  ? -24.252 -18.242 41.435   1.00 74.98  ? 101 ASN   D OD1   1 
ATOM   7699  N  ND2   . ASN   C 2  99  ? -25.351 -16.979 42.933   1.00 65.91  ? 101 ASN   D ND2   1 
ATOM   7700  N  N     . ASN   C 2  100 ? -30.050 -17.182 40.536   1.00 62.85  ? 102 ASN   D N     1 
ATOM   7701  C  CA    . ASN   C 2  100 ? -31.243 -17.540 39.768   1.00 67.13  ? 102 ASN   D CA    1 
ATOM   7702  C  C     . ASN   C 2  100 ? -31.689 -16.299 39.002   1.00 70.83  ? 102 ASN   D C     1 
ATOM   7703  O  O     . ASN   C 2  100 ? -32.166 -15.330 39.605   1.00 67.18  ? 102 ASN   D O     1 
ATOM   7704  C  CB    . ASN   C 2  100 ? -32.361 -18.063 40.679   1.00 71.11  ? 102 ASN   D CB    1 
ATOM   7705  C  CG    . ASN   C 2  100 ? -33.545 -18.659 39.897   1.00 73.33  ? 102 ASN   D CG    1 
ATOM   7706  O  OD1   . ASN   C 2  100 ? -33.896 -18.178 38.817   1.00 70.40  ? 102 ASN   D OD1   1 
ATOM   7707  N  ND2   . ASN   C 2  100 ? -34.166 -19.707 40.453   1.00 67.59  ? 102 ASN   D ND2   1 
ATOM   7708  N  N     . TRP   C 2  101 ? -31.519 -16.327 37.675   1.00 72.10  ? 103 TRP   D N     1 
ATOM   7709  C  CA    . TRP   C 2  101 ? -31.896 -15.181 36.853   1.00 68.30  ? 103 TRP   D CA    1 
ATOM   7710  C  C     . TRP   C 2  101 ? -33.345 -14.784 37.113   1.00 57.14  ? 103 TRP   D C     1 
ATOM   7711  O  O     . TRP   C 2  101 ? -33.631 -13.635 37.467   1.00 59.36  ? 103 TRP   D O     1 
ATOM   7712  C  CB    . TRP   C 2  101 ? -31.658 -15.494 35.364   1.00 63.33  ? 103 TRP   D CB    1 
ATOM   7713  C  CG    . TRP   C 2  101 ? -31.689 -14.269 34.457   1.00 65.12  ? 103 TRP   D CG    1 
ATOM   7714  C  CD1   . TRP   C 2  101 ? -30.696 -13.338 34.302   1.00 58.37  ? 103 TRP   D CD1   1 
ATOM   7715  C  CD2   . TRP   C 2  101 ? -32.766 -13.851 33.595   1.00 58.61  ? 103 TRP   D CD2   1 
ATOM   7716  N  NE1   . TRP   C 2  101 ? -31.088 -12.375 33.402   1.00 60.19  ? 103 TRP   D NE1   1 
ATOM   7717  C  CE2   . TRP   C 2  101 ? -32.349 -12.668 32.950   1.00 53.98  ? 103 TRP   D CE2   1 
ATOM   7718  C  CE3   . TRP   C 2  101 ? -34.037 -14.364 33.307   1.00 51.81  ? 103 TRP   D CE3   1 
ATOM   7719  C  CZ2   . TRP   C 2  101 ? -33.158 -11.986 32.046   1.00 47.98  ? 103 TRP   D CZ2   1 
ATOM   7720  C  CZ3   . TRP   C 2  101 ? -34.838 -13.687 32.399   1.00 58.35  ? 103 TRP   D CZ3   1 
ATOM   7721  C  CH2   . TRP   C 2  101 ? -34.393 -12.512 31.777   1.00 53.64  ? 103 TRP   D CH2   1 
ATOM   7722  N  N     . ALA   C 2  102 ? -34.269 -15.742 36.979   1.00 59.95  ? 104 ALA   D N     1 
ATOM   7723  C  CA    . ALA   C 2  102 ? -35.690 -15.464 37.190   1.00 61.01  ? 104 ALA   D CA    1 
ATOM   7724  C  C     . ALA   C 2  102 ? -35.940 -14.673 38.461   1.00 60.60  ? 104 ALA   D C     1 
ATOM   7725  O  O     . ALA   C 2  102 ? -36.888 -13.885 38.525   1.00 66.10  ? 104 ALA   D O     1 
ATOM   7726  C  CB    . ALA   C 2  102 ? -36.485 -16.764 37.246   1.00 55.97  ? 104 ALA   D CB    1 
ATOM   7727  N  N     . LYS   C 2  103 ? -35.115 -14.862 39.484   1.00 59.36  ? 105 LYS   D N     1 
ATOM   7728  C  CA    . LYS   C 2  103 ? -35.373 -14.171 40.737   1.00 67.95  ? 105 LYS   D CA    1 
ATOM   7729  C  C     . LYS   C 2  103 ? -34.840 -12.741 40.746   1.00 64.27  ? 105 LYS   D C     1 
ATOM   7730  O  O     . LYS   C 2  103 ? -35.344 -11.913 41.512   1.00 58.93  ? 105 LYS   D O     1 
ATOM   7731  C  CB    . LYS   C 2  103 ? -34.809 -14.989 41.910   1.00 73.58  ? 105 LYS   D CB    1 
ATOM   7732  C  CG    . LYS   C 2  103 ? -35.533 -16.343 42.101   1.00 70.54  ? 105 LYS   D CG    1 
ATOM   7733  C  CD    . LYS   C 2  103 ? -35.171 -17.050 43.408   1.00 81.59  ? 105 LYS   D CD    1 
ATOM   7734  C  CE    . LYS   C 2  103 ? -35.637 -16.265 44.636   1.00 84.48  ? 105 LYS   D CE    1 
ATOM   7735  N  NZ    . LYS   C 2  103 ? -35.359 -16.985 45.919   1.00 87.31  ? 105 LYS   D NZ    1 
ATOM   7736  N  N     . GLY   C 2  104 ? -33.864 -12.415 39.901   1.00 71.64  ? 106 GLY   D N     1 
ATOM   7737  C  CA    . GLY   C 2  104 ? -33.390 -11.043 39.807   1.00 68.61  ? 106 GLY   D CA    1 
ATOM   7738  C  C     . GLY   C 2  104 ? -34.172 -10.216 38.800   1.00 58.72  ? 106 GLY   D C     1 
ATOM   7739  O  O     . GLY   C 2  104 ? -34.225 -8.986  38.877   1.00 49.55  ? 106 GLY   D O     1 
ATOM   7740  N  N     . HIS   C 2  105 ? -34.806 -10.894 37.855   1.00 53.73  ? 107 HIS   D N     1 
ATOM   7741  C  CA    . HIS   C 2  105 ? -35.511 -10.231 36.770   1.00 62.05  ? 107 HIS   D CA    1 
ATOM   7742  C  C     . HIS   C 2  105 ? -36.999 -10.090 37.054   1.00 62.23  ? 107 HIS   D C     1 
ATOM   7743  O  O     . HIS   C 2  105 ? -37.561 -9.002  36.912   1.00 65.44  ? 107 HIS   D O     1 
ATOM   7744  C  CB    . HIS   C 2  105 ? -35.295 -11.019 35.465   1.00 61.57  ? 107 HIS   D CB    1 
ATOM   7745  C  CG    . HIS   C 2  105 ? -35.444 -10.199 34.222   1.00 62.46  ? 107 HIS   D CG    1 
ATOM   7746  N  ND1   . HIS   C 2  105 ? -34.645 -9.109  33.948   1.00 62.09  ? 107 HIS   D ND1   1 
ATOM   7747  C  CD2   . HIS   C 2  105 ? -36.289 -10.320 33.172   1.00 57.01  ? 107 HIS   D CD2   1 
ATOM   7748  C  CE1   . HIS   C 2  105 ? -35.000 -8.588  32.787   1.00 55.08  ? 107 HIS   D CE1   1 
ATOM   7749  N  NE2   . HIS   C 2  105 ? -35.994 -9.305  32.295   1.00 55.05  ? 107 HIS   D NE2   1 
ATOM   7750  N  N     . TYR   C 2  106 ? -37.640 -11.178 37.486   1.00 66.02  ? 108 TYR   D N     1 
ATOM   7751  C  CA    . TYR   C 2  106 ? -39.089 -11.297 37.466   1.00 63.98  ? 108 TYR   D CA    1 
ATOM   7752  C  C     . TYR   C 2  106 ? -39.756 -11.224 38.834   1.00 66.93  ? 108 TYR   D C     1 
ATOM   7753  O  O     . TYR   C 2  106 ? -40.955 -10.932 38.887   1.00 66.52  ? 108 TYR   D O     1 
ATOM   7754  C  CB    . TYR   C 2  106 ? -39.494 -12.618 36.798   1.00 61.30  ? 108 TYR   D CB    1 
ATOM   7755  C  CG    . TYR   C 2  106 ? -39.360 -12.625 35.294   1.00 59.02  ? 108 TYR   D CG    1 
ATOM   7756  C  CD1   . TYR   C 2  106 ? -39.391 -11.441 34.565   1.00 68.19  ? 108 TYR   D CD1   1 
ATOM   7757  C  CD2   . TYR   C 2  106 ? -39.225 -13.818 34.599   1.00 60.14  ? 108 TYR   D CD2   1 
ATOM   7758  C  CE1   . TYR   C 2  106 ? -39.279 -11.442 33.178   1.00 54.43  ? 108 TYR   D CE1   1 
ATOM   7759  C  CE2   . TYR   C 2  106 ? -39.115 -13.836 33.220   1.00 65.50  ? 108 TYR   D CE2   1 
ATOM   7760  C  CZ    . TYR   C 2  106 ? -39.138 -12.641 32.511   1.00 66.66  ? 108 TYR   D CZ    1 
ATOM   7761  O  OH    . TYR   C 2  106 ? -39.031 -12.656 31.136   1.00 59.41  ? 108 TYR   D OH    1 
ATOM   7762  N  N     . THR   C 2  107 ? -39.027 -11.481 39.932   1.00 64.77  ? 109 THR   D N     1 
ATOM   7763  C  CA    . THR   C 2  107 ? -39.649 -11.546 41.258   1.00 58.79  ? 109 THR   D CA    1 
ATOM   7764  C  C     . THR   C 2  107 ? -38.931 -10.681 42.300   1.00 55.40  ? 109 THR   D C     1 
ATOM   7765  O  O     . THR   C 2  107 ? -39.333 -9.538  42.542   1.00 59.81  ? 109 THR   D O     1 
ATOM   7766  C  CB    . THR   C 2  107 ? -39.726 -13.002 41.750   1.00 59.23  ? 109 THR   D CB    1 
ATOM   7767  O  OG1   . THR   C 2  107 ? -38.407 -13.551 41.850   1.00 67.01  ? 109 THR   D OG1   1 
ATOM   7768  C  CG2   . THR   C 2  107 ? -40.567 -13.880 40.815   1.00 53.71  ? 109 THR   D CG2   1 
ATOM   7769  N  N     . GLU   C 2  108 ? -37.893 -11.215 42.950   1.00 42.91  ? 110 GLU   D N     1 
ATOM   7770  C  CA    . GLU   C 2  108 ? -37.237 -10.477 44.027   1.00 57.00  ? 110 GLU   D CA    1 
ATOM   7771  C  C     . GLU   C 2  108 ? -36.709 -9.132  43.535   1.00 60.93  ? 110 GLU   D C     1 
ATOM   7772  O  O     . GLU   C 2  108 ? -37.018 -8.076  44.111   1.00 48.05  ? 110 GLU   D O     1 
ATOM   7773  C  CB    . GLU   C 2  108 ? -36.099 -11.307 44.621   1.00 58.36  ? 110 GLU   D CB    1 
ATOM   7774  C  CG    . GLU   C 2  108 ? -36.336 -11.796 46.023   1.00 54.52  ? 110 GLU   D CG    1 
ATOM   7775  C  CD    . GLU   C 2  108 ? -36.498 -13.285 46.065   1.00 67.90  ? 110 GLU   D CD    1 
ATOM   7776  O  OE1   . GLU   C 2  108 ? -36.990 -13.856 45.069   1.00 64.99  ? 110 GLU   D OE1   1 
ATOM   7777  O  OE2   . GLU   C 2  108 ? -36.127 -13.890 47.089   1.00 83.75  ? 110 GLU   D OE2   1 
ATOM   7778  N  N     . GLY   C 2  109 ? -35.891 -9.159  42.475   1.00 57.62  ? 111 GLY   D N     1 
ATOM   7779  C  CA    . GLY   C 2  109 ? -35.438 -7.921  41.862   1.00 53.55  ? 111 GLY   D CA    1 
ATOM   7780  C  C     . GLY   C 2  109 ? -36.588 -7.047  41.400   1.00 54.27  ? 111 GLY   D C     1 
ATOM   7781  O  O     . GLY   C 2  109 ? -36.555 -5.822  41.571   1.00 55.26  ? 111 GLY   D O     1 
ATOM   7782  N  N     . ALA   C 2  110 ? -37.633 -7.668  40.829   1.00 52.68  ? 112 ALA   D N     1 
ATOM   7783  C  CA    . ALA   C 2  110 ? -38.818 -6.940  40.368   1.00 59.06  ? 112 ALA   D CA    1 
ATOM   7784  C  C     . ALA   C 2  110 ? -39.487 -6.134  41.478   1.00 59.38  ? 112 ALA   D C     1 
ATOM   7785  O  O     . ALA   C 2  110 ? -40.184 -5.156  41.186   1.00 62.30  ? 112 ALA   D O     1 
ATOM   7786  C  CB    . ALA   C 2  110 ? -39.831 -7.913  39.746   1.00 50.15  ? 112 ALA   D CB    1 
ATOM   7787  N  N     . GLU   C 2  111 ? -39.296 -6.516  42.739   1.00 56.46  ? 113 GLU   D N     1 
ATOM   7788  C  CA    . GLU   C 2  111 ? -39.873 -5.755  43.836   1.00 62.17  ? 113 GLU   D CA    1 
ATOM   7789  C  C     . GLU   C 2  111 ? -38.944 -4.644  44.311   1.00 61.69  ? 113 GLU   D C     1 
ATOM   7790  O  O     . GLU   C 2  111 ? -39.403 -3.549  44.652   1.00 63.13  ? 113 GLU   D O     1 
ATOM   7791  C  CB    . GLU   C 2  111 ? -40.214 -6.699  44.988   1.00 65.52  ? 113 GLU   D CB    1 
ATOM   7792  C  CG    . GLU   C 2  111 ? -41.087 -7.862  44.571   1.00 61.67  ? 113 GLU   D CG    1 
ATOM   7793  C  CD    . GLU   C 2  111 ? -41.252 -8.897  45.667   1.00 72.21  ? 113 GLU   D CD    1 
ATOM   7794  O  OE1   . GLU   C 2  111 ? -40.306 -9.078  46.470   1.00 63.52  ? 113 GLU   D OE1   1 
ATOM   7795  O  OE2   . GLU   C 2  111 ? -42.330 -9.532  45.721   1.00 80.65  ? 113 GLU   D OE2   1 
ATOM   7796  N  N     . LEU   C 2  112 ? -37.639 -4.900  44.331   1.00 60.09  ? 114 LEU   D N     1 
ATOM   7797  C  CA    . LEU   C 2  112 ? -36.684 -3.867  44.703   1.00 59.53  ? 114 LEU   D CA    1 
ATOM   7798  C  C     . LEU   C 2  112 ? -36.468 -2.837  43.594   1.00 62.30  ? 114 LEU   D C     1 
ATOM   7799  O  O     . LEU   C 2  112 ? -35.976 -1.734  43.873   1.00 57.67  ? 114 LEU   D O     1 
ATOM   7800  C  CB    . LEU   C 2  112 ? -35.352 -4.518  45.083   1.00 62.51  ? 114 LEU   D CB    1 
ATOM   7801  C  CG    . LEU   C 2  112 ? -34.265 -3.638  45.702   1.00 62.58  ? 114 LEU   D CG    1 
ATOM   7802  C  CD1   . LEU   C 2  112 ? -34.729 -3.116  47.050   1.00 54.61  ? 114 LEU   D CD1   1 
ATOM   7803  C  CD2   . LEU   C 2  112 ? -32.939 -4.399  45.815   1.00 51.31  ? 114 LEU   D CD2   1 
ATOM   7804  N  N     . VAL   C 2  113 ? -36.846 -3.154  42.353   1.00 60.13  ? 115 VAL   D N     1 
ATOM   7805  C  CA    . VAL   C 2  113 ? -36.406 -2.342  41.220   1.00 57.04  ? 115 VAL   D CA    1 
ATOM   7806  C  C     . VAL   C 2  113 ? -36.888 -0.905  41.362   1.00 54.14  ? 115 VAL   D C     1 
ATOM   7807  O  O     . VAL   C 2  113 ? -36.169 0.045   41.025   1.00 54.36  ? 115 VAL   D O     1 
ATOM   7808  C  CB    . VAL   C 2  113 ? -36.870 -2.972  39.897   1.00 53.59  ? 115 VAL   D CB    1 
ATOM   7809  C  CG1   . VAL   C 2  113 ? -38.378 -2.860  39.757   1.00 55.75  ? 115 VAL   D CG1   1 
ATOM   7810  C  CG2   . VAL   C 2  113 ? -36.140 -2.332  38.723   1.00 49.70  ? 115 VAL   D CG2   1 
ATOM   7811  N  N     . ASP   C 2  114 ? -38.102 -0.713  41.868   1.00 54.81  ? 116 ASP   D N     1 
ATOM   7812  C  CA    . ASP   C 2  114 ? -38.614 0.648   41.945   1.00 53.43  ? 116 ASP   D CA    1 
ATOM   7813  C  C     . ASP   C 2  114 ? -37.830 1.488   42.950   1.00 52.46  ? 116 ASP   D C     1 
ATOM   7814  O  O     . ASP   C 2  114 ? -37.687 2.700   42.770   1.00 43.28  ? 116 ASP   D O     1 
ATOM   7815  C  CB    . ASP   C 2  114 ? -40.101 0.600   42.263   1.00 44.61  ? 116 ASP   D CB    1 
ATOM   7816  C  CG    . ASP   C 2  114 ? -40.902 0.008   41.121   1.00 54.67  ? 116 ASP   D CG    1 
ATOM   7817  O  OD1   . ASP   C 2  114 ? -40.905 0.615   40.036   1.00 57.36  ? 116 ASP   D OD1   1 
ATOM   7818  O  OD2   . ASP   C 2  114 ? -41.493 -1.078  41.276   1.00 68.39  ? 116 ASP   D OD2   1 
ATOM   7819  N  N     . SER   C 2  115 ? -37.283 0.865   43.991   1.00 59.25  ? 117 SER   D N     1 
ATOM   7820  C  CA    . SER   C 2  115 ? -36.438 1.609   44.918   1.00 57.08  ? 117 SER   D CA    1 
ATOM   7821  C  C     . SER   C 2  115 ? -35.136 2.058   44.256   1.00 58.88  ? 117 SER   D C     1 
ATOM   7822  O  O     . SER   C 2  115 ? -34.586 3.112   44.610   1.00 50.23  ? 117 SER   D O     1 
ATOM   7823  C  CB    . SER   C 2  115 ? -36.152 0.752   46.150   1.00 54.80  ? 117 SER   D CB    1 
ATOM   7824  O  OG    . SER   C 2  115 ? -37.164 -0.232  46.311   1.00 66.89  ? 117 SER   D OG    1 
ATOM   7825  N  N     . VAL   C 2  116 ? -34.620 1.274   43.305   1.00 57.77  ? 118 VAL   D N     1 
ATOM   7826  C  CA    . VAL   C 2  116 ? -33.420 1.690   42.587   1.00 55.67  ? 118 VAL   D CA    1 
ATOM   7827  C  C     . VAL   C 2  116 ? -33.752 2.830   41.634   1.00 51.23  ? 118 VAL   D C     1 
ATOM   7828  O  O     . VAL   C 2  116 ? -33.070 3.864   41.615   1.00 41.17  ? 118 VAL   D O     1 
ATOM   7829  C  CB    . VAL   C 2  116 ? -32.788 0.502   41.838   1.00 56.09  ? 118 VAL   D CB    1 
ATOM   7830  C  CG1   . VAL   C 2  116 ? -31.546 0.968   41.052   1.00 44.44  ? 118 VAL   D CG1   1 
ATOM   7831  C  CG2   . VAL   C 2  116 ? -32.449 -0.618  42.806   1.00 55.24  ? 118 VAL   D CG2   1 
ATOM   7832  N  N     . LEU   C 2  117 ? -34.807 2.651   40.831   1.00 49.17  ? 119 LEU   D N     1 
ATOM   7833  C  CA    . LEU   C 2  117 ? -35.211 3.696   39.896   1.00 56.07  ? 119 LEU   D CA    1 
ATOM   7834  C  C     . LEU   C 2  117 ? -35.374 5.028   40.611   1.00 53.60  ? 119 LEU   D C     1 
ATOM   7835  O  O     . LEU   C 2  117 ? -35.026 6.082   40.063   1.00 55.57  ? 119 LEU   D O     1 
ATOM   7836  C  CB    . LEU   C 2  117 ? -36.501 3.287   39.180   1.00 50.82  ? 119 LEU   D CB    1 
ATOM   7837  C  CG    . LEU   C 2  117 ? -36.284 2.053   38.297   1.00 59.26  ? 119 LEU   D CG    1 
ATOM   7838  C  CD1   . LEU   C 2  117 ? -37.567 1.541   37.668   1.00 55.45  ? 119 LEU   D CD1   1 
ATOM   7839  C  CD2   . LEU   C 2  117 ? -35.242 2.351   37.220   1.00 60.22  ? 119 LEU   D CD2   1 
ATOM   7840  N  N     . ASP   C 2  118 ? -35.861 4.996   41.857   1.00 47.77  ? 120 ASP   D N     1 
ATOM   7841  C  CA    . ASP   C 2  118 ? -36.022 6.232   42.621   1.00 50.68  ? 120 ASP   D CA    1 
ATOM   7842  C  C     . ASP   C 2  118 ? -34.691 6.948   42.811   1.00 39.93  ? 120 ASP   D C     1 
ATOM   7843  O  O     . ASP   C 2  118 ? -34.613 8.167   42.669   1.00 48.45  ? 120 ASP   D O     1 
ATOM   7844  C  CB    . ASP   C 2  118 ? -36.673 5.943   43.974   1.00 56.26  ? 120 ASP   D CB    1 
ATOM   7845  C  CG    . ASP   C 2  118 ? -38.178 5.930   43.900   1.00 50.78  ? 120 ASP   D CG    1 
ATOM   7846  O  OD1   . ASP   C 2  118 ? -38.728 6.722   43.112   1.00 45.93  ? 120 ASP   D OD1   1 
ATOM   7847  O  OD2   . ASP   C 2  118 ? -38.810 5.126   44.619   1.00 61.54  ? 120 ASP   D OD2   1 
ATOM   7848  N  N     . VAL   C 2  119 ? -33.630 6.210   43.122   1.00 48.75  ? 121 VAL   D N     1 
ATOM   7849  C  CA    . VAL   C 2  119 ? -32.323 6.842   43.258   1.00 51.93  ? 121 VAL   D CA    1 
ATOM   7850  C  C     . VAL   C 2  119 ? -31.824 7.351   41.908   1.00 52.73  ? 121 VAL   D C     1 
ATOM   7851  O  O     . VAL   C 2  119 ? -31.315 8.474   41.805   1.00 48.98  ? 121 VAL   D O     1 
ATOM   7852  C  CB    . VAL   C 2  119 ? -31.332 5.856   43.894   1.00 47.96  ? 121 VAL   D CB    1 
ATOM   7853  C  CG1   . VAL   C 2  119 ? -30.168 6.613   44.527   1.00 46.96  ? 121 VAL   D CG1   1 
ATOM   7854  C  CG2   . VAL   C 2  119 ? -32.060 4.985   44.900   1.00 52.40  ? 121 VAL   D CG2   1 
ATOM   7855  N  N     . VAL   C 2  120 ? -31.961 6.540   40.852   1.00 44.61  ? 122 VAL   D N     1 
ATOM   7856  C  CA    . VAL   C 2  120 ? -31.500 6.960   39.531   1.00 49.87  ? 122 VAL   D CA    1 
ATOM   7857  C  C     . VAL   C 2  120 ? -32.127 8.304   39.152   1.00 57.73  ? 122 VAL   D C     1 
ATOM   7858  O  O     . VAL   C 2  120 ? -31.424 9.256   38.779   1.00 46.91  ? 122 VAL   D O     1 
ATOM   7859  C  CB    . VAL   C 2  120 ? -31.801 5.872   38.483   1.00 50.73  ? 122 VAL   D CB    1 
ATOM   7860  C  CG1   . VAL   C 2  120 ? -31.056 6.159   37.186   1.00 44.59  ? 122 VAL   D CG1   1 
ATOM   7861  C  CG2   . VAL   C 2  120 ? -31.418 4.496   39.004   1.00 48.57  ? 122 VAL   D CG2   1 
ATOM   7862  N  N     . ARG   C 2  121 ? -33.463 8.400   39.256   1.00 63.83  ? 123 ARG   D N     1 
ATOM   7863  C  CA    . ARG   C 2  121 ? -34.168 9.655   38.995   1.00 49.59  ? 123 ARG   D CA    1 
ATOM   7864  C  C     . ARG   C 2  121 ? -33.553 10.810  39.780   1.00 56.83  ? 123 ARG   D C     1 
ATOM   7865  O  O     . ARG   C 2  121 ? -33.221 11.859  39.213   1.00 54.28  ? 123 ARG   D O     1 
ATOM   7866  C  CB    . ARG   C 2  121 ? -35.653 9.512   39.347   1.00 50.92  ? 123 ARG   D CB    1 
ATOM   7867  C  CG    . ARG   C 2  121 ? -36.469 8.616   38.426   1.00 56.87  ? 123 ARG   D CG    1 
ATOM   7868  C  CD    . ARG   C 2  121 ? -37.700 8.033   39.151   1.00 54.84  ? 123 ARG   D CD    1 
ATOM   7869  N  NE    . ARG   C 2  121 ? -38.481 7.140   38.298   1.00 56.77  ? 123 ARG   D NE    1 
ATOM   7870  C  CZ    . ARG   C 2  121 ? -39.163 6.083   38.730   1.00 63.05  ? 123 ARG   D CZ    1 
ATOM   7871  N  NH1   . ARG   C 2  121 ? -39.183 5.742   40.011   1.00 57.26  ? 123 ARG   D NH1   1 
ATOM   7872  N  NH2   . ARG   C 2  121 ? -39.832 5.337   37.851   1.00 59.07  ? 123 ARG   D NH2   1 
ATOM   7873  N  N     . LYS   C 2  122 ? -33.414 10.641  41.101   1.00 52.40  ? 124 LYS   D N     1 
ATOM   7874  C  CA    . LYS   C 2  122 ? -32.768 11.671  41.911   1.00 60.48  ? 124 LYS   D CA    1 
ATOM   7875  C  C     . LYS   C 2  122 ? -31.425 12.063  41.309   1.00 56.06  ? 124 LYS   D C     1 
ATOM   7876  O  O     . LYS   C 2  122 ? -31.089 13.249  41.213   1.00 57.91  ? 124 LYS   D O     1 
ATOM   7877  C  CB    . LYS   C 2  122 ? -32.584 11.171  43.349   1.00 58.80  ? 124 LYS   D CB    1 
ATOM   7878  C  CG    . LYS   C 2  122 ? -33.195 12.053  44.431   1.00 66.83  ? 124 LYS   D CG    1 
ATOM   7879  C  CD    . LYS   C 2  122 ? -32.372 13.308  44.730   1.00 68.29  ? 124 LYS   D CD    1 
ATOM   7880  C  CE    . LYS   C 2  122 ? -33.104 14.198  45.764   1.00 82.49  ? 124 LYS   D CE    1 
ATOM   7881  N  NZ    . LYS   C 2  122 ? -32.437 15.502  46.088   1.00 69.11  ? 124 LYS   D NZ    1 
ATOM   7882  N  N     . GLU   C 2  123 ? -30.646 11.070  40.893   1.00 53.80  ? 125 GLU   D N     1 
ATOM   7883  C  CA    . GLU   C 2  123 ? -29.361 11.345  40.276   1.00 52.36  ? 125 GLU   D CA    1 
ATOM   7884  C  C     . GLU   C 2  123 ? -29.538 11.992  38.911   1.00 54.15  ? 125 GLU   D C     1 
ATOM   7885  O  O     . GLU   C 2  123 ? -28.894 13.002  38.606   1.00 54.84  ? 125 GLU   D O     1 
ATOM   7886  C  CB    . GLU   C 2  123 ? -28.559 10.049  40.181   1.00 53.76  ? 125 GLU   D CB    1 
ATOM   7887  C  CG    . GLU   C 2  123 ? -27.808 9.744   41.468   1.00 47.96  ? 125 GLU   D CG    1 
ATOM   7888  C  CD    . GLU   C 2  123 ? -26.859 10.874  41.842   1.00 57.08  ? 125 GLU   D CD    1 
ATOM   7889  O  OE1   . GLU   C 2  123 ? -26.659 11.794  41.008   1.00 61.36  ? 125 GLU   D OE1   1 
ATOM   7890  O  OE2   . GLU   C 2  123 ? -26.312 10.847  42.966   1.00 61.06  ? 125 GLU   D OE2   1 
ATOM   7891  N  N     . SER   C 2  124 ? -30.427 11.441  38.082   1.00 53.77  ? 126 SER   D N     1 
ATOM   7892  C  CA    . SER   C 2  124 ? -30.563 11.944  36.718   1.00 54.53  ? 126 SER   D CA    1 
ATOM   7893  C  C     . SER   C 2  124 ? -31.080 13.375  36.697   1.00 54.09  ? 126 SER   D C     1 
ATOM   7894  O  O     . SER   C 2  124 ? -30.539 14.233  35.988   1.00 52.16  ? 126 SER   D O     1 
ATOM   7895  C  CB    . SER   C 2  124 ? -31.475 11.033  35.908   1.00 42.36  ? 126 SER   D CB    1 
ATOM   7896  O  OG    . SER   C 2  124 ? -30.903 9.750   35.827   1.00 46.10  ? 126 SER   D OG    1 
ATOM   7897  N  N     . GLU   C 2  125 ? -32.127 13.657  37.463   1.00 69.38  ? 127 GLU   D N     1 
ATOM   7898  C  CA    . GLU   C 2  125 ? -32.785 14.950  37.337   1.00 67.21  ? 127 GLU   D CA    1 
ATOM   7899  C  C     . GLU   C 2  125 ? -32.015 16.079  37.997   1.00 57.40  ? 127 GLU   D C     1 
ATOM   7900  O  O     . GLU   C 2  125 ? -32.521 17.201  38.030   1.00 76.35  ? 127 GLU   D O     1 
ATOM   7901  C  CB    . GLU   C 2  125 ? -34.213 14.882  37.888   1.00 69.04  ? 127 GLU   D CB    1 
ATOM   7902  C  CG    . GLU   C 2  125 ? -34.327 14.428  39.324   1.00 72.11  ? 127 GLU   D CG    1 
ATOM   7903  C  CD    . GLU   C 2  125 ? -35.778 14.217  39.737   1.00 77.46  ? 127 GLU   D CD    1 
ATOM   7904  O  OE1   . GLU   C 2  125 ? -36.650 14.233  38.840   1.00 71.50  ? 127 GLU   D OE1   1 
ATOM   7905  O  OE2   . GLU   C 2  125 ? -36.045 14.037  40.951   1.00 78.10  ? 127 GLU   D OE2   1 
ATOM   7906  N  N     . SER   C 2  126 ? -30.809 15.834  38.502   1.00 52.09  ? 128 SER   D N     1 
ATOM   7907  C  CA    . SER   C 2  126 ? -29.924 16.929  38.881   1.00 64.78  ? 128 SER   D CA    1 
ATOM   7908  C  C     . SER   C 2  126 ? -28.835 17.215  37.846   1.00 69.41  ? 128 SER   D C     1 
ATOM   7909  O  O     . SER   C 2  126 ? -27.984 18.078  38.089   1.00 74.30  ? 128 SER   D O     1 
ATOM   7910  C  CB    . SER   C 2  126 ? -29.267 16.650  40.239   1.00 63.41  ? 128 SER   D CB    1 
ATOM   7911  O  OG    . SER   C 2  126 ? -28.329 17.672  40.568   1.00 55.05  ? 128 SER   D OG    1 
ATOM   7912  N  N     . CYS   C 2  127 ? -28.839 16.530  36.705   1.00 56.28  ? 129 CYS   D N     1 
ATOM   7913  C  CA    . CYS   C 2  127 ? -27.729 16.617  35.765   1.00 58.57  ? 129 CYS   D CA    1 
ATOM   7914  C  C     . CYS   C 2  127 ? -27.882 17.803  34.816   1.00 65.89  ? 129 CYS   D C     1 
ATOM   7915  O  O     . CYS   C 2  127 ? -28.971 18.080  34.302   1.00 64.76  ? 129 CYS   D O     1 
ATOM   7916  C  CB    . CYS   C 2  127 ? -27.598 15.321  34.964   1.00 53.91  ? 129 CYS   D CB    1 
ATOM   7917  S  SG    . CYS   C 2  127 ? -27.019 13.921  35.936   1.00 56.36  ? 129 CYS   D SG    1 
ATOM   7918  N  N     . ASP   C 2  128 ? -26.767 18.506  34.597   1.00 65.39  ? 130 ASP   D N     1 
ATOM   7919  C  CA    . ASP   C 2  128 ? -26.727 19.583  33.614   1.00 58.34  ? 130 ASP   D CA    1 
ATOM   7920  C  C     . ASP   C 2  128 ? -27.134 19.079  32.239   1.00 48.16  ? 130 ASP   D C     1 
ATOM   7921  O  O     . ASP   C 2  128 ? -27.831 19.775  31.497   1.00 51.49  ? 130 ASP   D O     1 
ATOM   7922  C  CB    . ASP   C 2  128 ? -25.317 20.181  33.580   1.00 56.55  ? 130 ASP   D CB    1 
ATOM   7923  C  CG    . ASP   C 2  128 ? -25.237 21.459  32.776   1.00 73.63  ? 130 ASP   D CG    1 
ATOM   7924  O  OD1   . ASP   C 2  128 ? -26.133 21.700  31.938   1.00 74.26  ? 130 ASP   D OD1   1 
ATOM   7925  O  OD2   . ASP   C 2  128 ? -24.265 22.222  32.981   1.00 84.34  ? 130 ASP   D OD2   1 
ATOM   7926  N  N     . CYS   C 2  129 ? -26.707 17.862  31.891   1.00 57.97  ? 131 CYS   D N     1 
ATOM   7927  C  CA    . CYS   C 2  129 ? -26.896 17.268  30.574   1.00 56.77  ? 131 CYS   D CA    1 
ATOM   7928  C  C     . CYS   C 2  129 ? -26.436 15.813  30.595   1.00 55.97  ? 131 CYS   D C     1 
ATOM   7929  O  O     . CYS   C 2  129 ? -25.332 15.488  30.141   1.00 61.01  ? 131 CYS   D O     1 
ATOM   7930  C  CB    . CYS   C 2  129 ? -26.141 18.075  29.515   1.00 61.48  ? 131 CYS   D CB    1 
ATOM   7931  S  SG    . CYS   C 2  129 ? -25.942 17.258  27.913   1.00 69.77  ? 131 CYS   D SG    1 
ATOM   7932  N  N     . LEU   C 2  130 ? -27.285 14.938  31.130   1.00 47.66  ? 132 LEU   D N     1 
ATOM   7933  C  CA    . LEU   C 2  130 ? -26.940 13.537  31.342   1.00 49.82  ? 132 LEU   D CA    1 
ATOM   7934  C  C     . LEU   C 2  130 ? -26.498 12.859  30.047   1.00 48.92  ? 132 LEU   D C     1 
ATOM   7935  O  O     . LEU   C 2  130 ? -27.171 12.961  29.019   1.00 49.47  ? 132 LEU   D O     1 
ATOM   7936  C  CB    . LEU   C 2  130 ? -28.153 12.810  31.935   1.00 47.89  ? 132 LEU   D CB    1 
ATOM   7937  C  CG    . LEU   C 2  130 ? -28.170 11.279  31.985   1.00 39.01  ? 132 LEU   D CG    1 
ATOM   7938  C  CD1   . LEU   C 2  130 ? -27.262 10.758  33.082   1.00 39.11  ? 132 LEU   D CD1   1 
ATOM   7939  C  CD2   . LEU   C 2  130 ? -29.576 10.770  32.167   1.00 33.63  ? 132 LEU   D CD2   1 
ATOM   7940  N  N     . GLN   C 2  131 ? -25.373 12.140  30.099   1.00 49.69  ? 133 GLN   D N     1 
ATOM   7941  C  CA    . GLN   C 2  131 ? -24.938 11.383  28.923   1.00 47.00  ? 133 GLN   D CA    1 
ATOM   7942  C  C     . GLN   C 2  131 ? -25.700 10.078  28.797   1.00 46.85  ? 133 GLN   D C     1 
ATOM   7943  O  O     . GLN   C 2  131 ? -26.145 9.711   27.705   1.00 45.68  ? 133 GLN   D O     1 
ATOM   7944  C  CB    . GLN   C 2  131 ? -23.449 11.044  28.989   1.00 47.29  ? 133 GLN   D CB    1 
ATOM   7945  C  CG    . GLN   C 2  131 ? -22.479 12.153  29.230   1.00 47.25  ? 133 GLN   D CG    1 
ATOM   7946  C  CD    . GLN   C 2  131 ? -21.081 11.680  28.955   1.00 44.57  ? 133 GLN   D CD    1 
ATOM   7947  O  OE1   . GLN   C 2  131 ? -20.868 10.841  28.070   1.00 37.41  ? 133 GLN   D OE1   1 
ATOM   7948  N  NE2   . GLN   C 2  131 ? -20.118 12.192  29.710   1.00 44.03  ? 133 GLN   D NE2   1 
ATOM   7949  N  N     . GLY   C 2  132 ? -25.806 9.347   29.898   1.00 42.79  ? 134 GLY   D N     1 
ATOM   7950  C  CA    . GLY   C 2  132 ? -26.366 8.012   29.909   1.00 39.94  ? 134 GLY   D CA    1 
ATOM   7951  C  C     . GLY   C 2  132 ? -25.955 7.294   31.183   1.00 45.04  ? 134 GLY   D C     1 
ATOM   7952  O  O     . GLY   C 2  132 ? -25.717 7.924   32.216   1.00 46.12  ? 134 GLY   D O     1 
ATOM   7953  N  N     . PHE   C 2  133 ? -25.837 5.973   31.068   1.00 39.61  ? 135 PHE   D N     1 
ATOM   7954  C  CA    . PHE   C 2  133 ? -25.705 5.094   32.217   1.00 38.12  ? 135 PHE   D CA    1 
ATOM   7955  C  C     . PHE   C 2  133 ? -24.621 4.054   31.971   1.00 47.47  ? 135 PHE   D C     1 
ATOM   7956  O  O     . PHE   C 2  133 ? -24.460 3.554   30.847   1.00 40.78  ? 135 PHE   D O     1 
ATOM   7957  C  CB    . PHE   C 2  133 ? -27.051 4.403   32.522   1.00 37.78  ? 135 PHE   D CB    1 
ATOM   7958  C  CG    . PHE   C 2  133 ? -28.182 5.357   32.670   1.00 35.57  ? 135 PHE   D CG    1 
ATOM   7959  C  CD1   . PHE   C 2  133 ? -28.898 5.772   31.568   1.00 39.42  ? 135 PHE   D CD1   1 
ATOM   7960  C  CD2   . PHE   C 2  133 ? -28.501 5.875   33.903   1.00 31.74  ? 135 PHE   D CD2   1 
ATOM   7961  C  CE1   . PHE   C 2  133 ? -29.931 6.680   31.707   1.00 47.59  ? 135 PHE   D CE1   1 
ATOM   7962  C  CE2   . PHE   C 2  133 ? -29.524 6.788   34.048   1.00 41.51  ? 135 PHE   D CE2   1 
ATOM   7963  C  CZ    . PHE   C 2  133 ? -30.242 7.192   32.956   1.00 41.75  ? 135 PHE   D CZ    1 
ATOM   7964  N  N     . GLN   C 2  134 ? -23.899 3.715   33.042   1.00 43.28  ? 136 GLN   D N     1 
ATOM   7965  C  CA    . GLN   C 2  134 ? -22.828 2.728   32.999   1.00 42.34  ? 136 GLN   D CA    1 
ATOM   7966  C  C     . GLN   C 2  134 ? -23.078 1.710   34.098   1.00 42.72  ? 136 GLN   D C     1 
ATOM   7967  O  O     . GLN   C 2  134 ? -23.076 2.063   35.278   1.00 48.51  ? 136 GLN   D O     1 
ATOM   7968  C  CB    . GLN   C 2  134 ? -21.472 3.424   33.166   1.00 46.64  ? 136 GLN   D CB    1 
ATOM   7969  C  CG    . GLN   C 2  134 ? -20.314 2.562   33.598   1.00 45.73  ? 136 GLN   D CG    1 
ATOM   7970  C  CD    . GLN   C 2  134 ? -19.070 3.401   33.867   1.00 52.84  ? 136 GLN   D CD    1 
ATOM   7971  O  OE1   . GLN   C 2  134 ? -18.519 4.021   32.951   1.00 53.67  ? 136 GLN   D OE1   1 
ATOM   7972  N  NE2   . GLN   C 2  134 ? -18.631 3.438   35.125   1.00 43.35  ? 136 GLN   D NE2   1 
ATOM   7973  N  N     . LEU   C 2  135 ? -23.298 0.453   33.714   1.00 42.41  ? 137 LEU   D N     1 
ATOM   7974  C  CA    . LEU   C 2  135 ? -23.706 -0.604  34.633   1.00 45.26  ? 137 LEU   D CA    1 
ATOM   7975  C  C     . LEU   C 2  135 ? -22.636 -1.689  34.700   1.00 48.95  ? 137 LEU   D C     1 
ATOM   7976  O  O     . LEU   C 2  135 ? -22.414 -2.397  33.715   1.00 54.29  ? 137 LEU   D O     1 
ATOM   7977  C  CB    . LEU   C 2  135 ? -25.040 -1.211  34.199   1.00 42.14  ? 137 LEU   D CB    1 
ATOM   7978  C  CG    . LEU   C 2  135 ? -25.289 -2.581  34.844   1.00 45.28  ? 137 LEU   D CG    1 
ATOM   7979  C  CD1   . LEU   C 2  135 ? -25.451 -2.428  36.345   1.00 48.07  ? 137 LEU   D CD1   1 
ATOM   7980  C  CD2   . LEU   C 2  135 ? -26.483 -3.316  34.240   1.00 44.40  ? 137 LEU   D CD2   1 
ATOM   7981  N  N     . THR   C 2  136 ? -21.996 -1.847  35.865   1.00 52.08  ? 138 THR   D N     1 
ATOM   7982  C  CA    . THR   C 2  136 ? -21.077 -2.961  36.103   1.00 44.00  ? 138 THR   D CA    1 
ATOM   7983  C  C     . THR   C 2  136 ? -21.842 -4.113  36.713   1.00 49.14  ? 138 THR   D C     1 
ATOM   7984  O  O     . THR   C 2  136 ? -22.519 -3.945  37.730   1.00 51.13  ? 138 THR   D O     1 
ATOM   7985  C  CB    . THR   C 2  136 ? -19.947 -2.585  37.049   1.00 46.04  ? 138 THR   D CB    1 
ATOM   7986  O  OG1   . THR   C 2  136 ? -20.500 -1.953  38.213   1.00 51.56  ? 138 THR   D OG1   1 
ATOM   7987  C  CG2   . THR   C 2  136 ? -18.960 -1.673  36.373   1.00 51.70  ? 138 THR   D CG2   1 
ATOM   7988  N  N     . HIS   C 2  137 ? -21.727 -5.282  36.102   1.00 54.12  ? 139 HIS   D N     1 
ATOM   7989  C  CA    . HIS   C 2  137 ? -22.505 -6.413  36.581   1.00 57.29  ? 139 HIS   D CA    1 
ATOM   7990  C  C     . HIS   C 2  137 ? -21.934 -7.678  35.969   1.00 59.05  ? 139 HIS   D C     1 
ATOM   7991  O  O     . HIS   C 2  137 ? -21.378 -7.644  34.866   1.00 58.34  ? 139 HIS   D O     1 
ATOM   7992  C  CB    . HIS   C 2  137 ? -23.989 -6.265  36.214   1.00 47.82  ? 139 HIS   D CB    1 
ATOM   7993  C  CG    . HIS   C 2  137 ? -24.279 -6.475  34.760   1.00 45.09  ? 139 HIS   D CG    1 
ATOM   7994  N  ND1   . HIS   C 2  137 ? -25.466 -7.011  34.308   1.00 51.99  ? 139 HIS   D ND1   1 
ATOM   7995  C  CD2   . HIS   C 2  137 ? -23.545 -6.210  33.653   1.00 50.78  ? 139 HIS   D CD2   1 
ATOM   7996  C  CE1   . HIS   C 2  137 ? -25.449 -7.079  32.988   1.00 46.23  ? 139 HIS   D CE1   1 
ATOM   7997  N  NE2   . HIS   C 2  137 ? -24.293 -6.600  32.566   1.00 52.40  ? 139 HIS   D NE2   1 
ATOM   7998  N  N     . SER   C 2  138 ? -22.069 -8.786  36.688   1.00 49.35  ? 140 SER   D N     1 
ATOM   7999  C  CA    . SER   C 2  138 ? -21.784 -10.076 36.079   1.00 47.10  ? 140 SER   D CA    1 
ATOM   8000  C  C     . SER   C 2  138 ? -23.037 -10.616 35.402   1.00 47.07  ? 140 SER   D C     1 
ATOM   8001  O  O     . SER   C 2  138 ? -24.158 -10.140 35.629   1.00 40.46  ? 140 SER   D O     1 
ATOM   8002  C  CB    . SER   C 2  138 ? -21.272 -11.078 37.111   1.00 53.61  ? 140 SER   D CB    1 
ATOM   8003  O  OG    . SER   C 2  138 ? -22.133 -12.201 37.197   1.00 48.89  ? 140 SER   D OG    1 
ATOM   8004  N  N     . LEU   C 2  139 ? -22.826 -11.640 34.574   1.00 39.78  ? 141 LEU   D N     1 
ATOM   8005  C  CA    . LEU   C 2  139 ? -23.853 -12.242 33.736   1.00 43.99  ? 141 LEU   D CA    1 
ATOM   8006  C  C     . LEU   C 2  139 ? -24.139 -13.699 34.077   1.00 55.75  ? 141 LEU   D C     1 
ATOM   8007  O  O     . LEU   C 2  139 ? -24.885 -14.360 33.337   1.00 54.54  ? 141 LEU   D O     1 
ATOM   8008  C  CB    . LEU   C 2  139 ? -23.441 -12.152 32.263   1.00 41.58  ? 141 LEU   D CB    1 
ATOM   8009  C  CG    . LEU   C 2  139 ? -23.769 -10.835 31.558   1.00 54.75  ? 141 LEU   D CG    1 
ATOM   8010  C  CD1   . LEU   C 2  139 ? -23.134 -9.663  32.298   1.00 49.18  ? 141 LEU   D CD1   1 
ATOM   8011  C  CD2   . LEU   C 2  139 ? -23.342 -10.866 30.082   1.00 54.07  ? 141 LEU   D CD2   1 
ATOM   8012  N  N     . GLY   C 2  140 ? -23.549 -14.227 35.151   1.00 58.37  ? 142 GLY   D N     1 
ATOM   8013  C  CA    . GLY   C 2  140 ? -23.643 -15.645 35.453   1.00 62.62  ? 142 GLY   D CA    1 
ATOM   8014  C  C     . GLY   C 2  140 ? -24.310 -15.930 36.780   1.00 60.30  ? 142 GLY   D C     1 
ATOM   8015  O  O     . GLY   C 2  140 ? -24.942 -16.982 36.957   1.00 53.80  ? 142 GLY   D O     1 
ATOM   8016  N  N     . GLY   C 2  141 ? -24.155 -14.990 37.716   1.00 59.56  ? 143 GLY   D N     1 
ATOM   8017  C  CA    . GLY   C 2  141 ? -24.883 -14.987 38.970   1.00 57.26  ? 143 GLY   D CA    1 
ATOM   8018  C  C     . GLY   C 2  141 ? -26.362 -14.674 38.816   1.00 57.62  ? 143 GLY   D C     1 
ATOM   8019  O  O     . GLY   C 2  141 ? -26.979 -15.026 37.803   1.00 51.76  ? 143 GLY   D O     1 
ATOM   8020  N  N     . GLY   C 2  142 ? -26.943 -14.005 39.813   1.00 59.48  ? 144 GLY   D N     1 
ATOM   8021  C  CA    . GLY   C 2  142 ? -28.385 -13.847 39.850   1.00 47.98  ? 144 GLY   D CA    1 
ATOM   8022  C  C     . GLY   C 2  142 ? -28.898 -12.424 39.887   1.00 51.49  ? 144 GLY   D C     1 
ATOM   8023  O  O     . GLY   C 2  142 ? -29.832 -12.101 39.148   1.00 51.01  ? 144 GLY   D O     1 
ATOM   8024  N  N     . THR   C 2  143 ? -28.330 -11.569 40.746   1.00 53.82  ? 145 THR   D N     1 
ATOM   8025  C  CA    . THR   C 2  143 ? -28.812 -10.188 40.845   1.00 51.19  ? 145 THR   D CA    1 
ATOM   8026  C  C     . THR   C 2  143 ? -28.310 -9.363  39.665   1.00 59.16  ? 145 THR   D C     1 
ATOM   8027  O  O     . THR   C 2  143 ? -29.084 -9.003  38.772   1.00 62.61  ? 145 THR   D O     1 
ATOM   8028  C  CB    . THR   C 2  143 ? -28.383 -9.534  42.167   1.00 54.12  ? 145 THR   D CB    1 
ATOM   8029  O  OG1   . THR   C 2  143 ? -28.795 -10.332 43.282   1.00 57.79  ? 145 THR   D OG1   1 
ATOM   8030  C  CG2   . THR   C 2  143 ? -29.009 -8.149  42.298   1.00 50.50  ? 145 THR   D CG2   1 
ATOM   8031  N  N     . GLY   C 2  144 ? -27.009 -9.044  39.659   1.00 60.41  ? 146 GLY   D N     1 
ATOM   8032  C  CA    . GLY   C 2  144 ? -26.454 -8.238  38.579   1.00 59.05  ? 146 GLY   D CA    1 
ATOM   8033  C  C     . GLY   C 2  144 ? -26.895 -8.713  37.207   1.00 57.32  ? 146 GLY   D C     1 
ATOM   8034  O  O     . GLY   C 2  144 ? -27.246 -7.908  36.339   1.00 52.15  ? 146 GLY   D O     1 
ATOM   8035  N  N     . SER   C 2  145 ? -26.904 -10.025 37.000   1.00 49.23  ? 147 SER   D N     1 
ATOM   8036  C  CA    . SER   C 2  145 ? -27.415 -10.574 35.759   1.00 50.86  ? 147 SER   D CA    1 
ATOM   8037  C  C     . SER   C 2  145 ? -28.900 -10.262 35.614   1.00 57.64  ? 147 SER   D C     1 
ATOM   8038  O  O     . SER   C 2  145 ? -29.297 -9.473  34.749   1.00 61.06  ? 147 SER   D O     1 
ATOM   8039  C  CB    . SER   C 2  145 ? -27.176 -12.081 35.706   1.00 54.13  ? 147 SER   D CB    1 
ATOM   8040  O  OG    . SER   C 2  145 ? -27.981 -12.664 34.701   1.00 57.17  ? 147 SER   D OG    1 
ATOM   8041  N  N     . GLY   C 2  146 ? -29.726 -10.857 36.478   1.00 60.26  ? 148 GLY   D N     1 
ATOM   8042  C  CA    . GLY   C 2  146 ? -31.169 -10.786 36.289   1.00 62.08  ? 148 GLY   D CA    1 
ATOM   8043  C  C     . GLY   C 2  146 ? -31.772 -9.430  36.620   1.00 57.57  ? 148 GLY   D C     1 
ATOM   8044  O  O     . GLY   C 2  146 ? -32.726 -8.995  35.965   1.00 59.07  ? 148 GLY   D O     1 
ATOM   8045  N  N     . MET   C 2  147 ? -31.243 -8.751  37.640   1.00 39.66  ? 149 MET   D N     1 
ATOM   8046  C  CA    . MET   C 2  147 ? -31.795 -7.457  38.033   1.00 54.66  ? 149 MET   D CA    1 
ATOM   8047  C  C     . MET   C 2  147 ? -31.142 -6.289  37.304   1.00 57.51  ? 149 MET   D C     1 
ATOM   8048  O  O     . MET   C 2  147 ? -31.762 -5.222  37.173   1.00 51.49  ? 149 MET   D O     1 
ATOM   8049  C  CB    . MET   C 2  147 ? -31.657 -7.240  39.551   1.00 58.87  ? 149 MET   D CB    1 
ATOM   8050  C  CG    . MET   C 2  147 ? -32.598 -6.148  40.104   1.00 56.31  ? 149 MET   D CG    1 
ATOM   8051  S  SD    . MET   C 2  147 ? -32.197 -5.410  41.711   1.00 49.48  ? 149 MET   D SD    1 
ATOM   8052  C  CE    . MET   C 2  147 ? -33.550 -4.248  41.889   1.00 47.45  ? 149 MET   D CE    1 
ATOM   8053  N  N     . GLY   C 2  148 ? -29.891 -6.455  36.864   1.00 57.24  ? 150 GLY   D N     1 
ATOM   8054  C  CA    . GLY   C 2  148 ? -29.263 -5.429  36.054   1.00 44.43  ? 150 GLY   D CA    1 
ATOM   8055  C  C     . GLY   C 2  148 ? -29.911 -5.306  34.689   1.00 44.13  ? 150 GLY   D C     1 
ATOM   8056  O  O     . GLY   C 2  148 ? -30.046 -4.203  34.159   1.00 48.75  ? 150 GLY   D O     1 
ATOM   8057  N  N     . THR   C 2  149 ? -30.338 -6.432  34.110   1.00 42.53  ? 151 THR   D N     1 
ATOM   8058  C  CA    . THR   C 2  149 ? -31.033 -6.377  32.829   1.00 47.33  ? 151 THR   D CA    1 
ATOM   8059  C  C     . THR   C 2  149 ? -32.433 -5.800  32.982   1.00 48.70  ? 151 THR   D C     1 
ATOM   8060  O  O     . THR   C 2  149 ? -32.895 -5.046  32.119   1.00 53.73  ? 151 THR   D O     1 
ATOM   8061  C  CB    . THR   C 2  149 ? -31.095 -7.763  32.179   1.00 51.86  ? 151 THR   D CB    1 
ATOM   8062  O  OG1   . THR   C 2  149 ? -31.384 -8.759  33.168   1.00 57.14  ? 151 THR   D OG1   1 
ATOM   8063  C  CG2   . THR   C 2  149 ? -29.775 -8.087  31.493   1.00 51.51  ? 151 THR   D CG2   1 
ATOM   8064  N  N     . LEU   C 2  150 ? -33.126 -6.135  34.068   1.00 48.18  ? 152 LEU   D N     1 
ATOM   8065  C  CA    . LEU   C 2  150 ? -34.401 -5.479  34.322   1.00 49.54  ? 152 LEU   D CA    1 
ATOM   8066  C  C     . LEU   C 2  150 ? -34.206 -3.987  34.561   1.00 44.29  ? 152 LEU   D C     1 
ATOM   8067  O  O     . LEU   C 2  150 ? -34.955 -3.163  34.030   1.00 42.15  ? 152 LEU   D O     1 
ATOM   8068  C  CB    . LEU   C 2  150 ? -35.105 -6.127  35.514   1.00 55.22  ? 152 LEU   D CB    1 
ATOM   8069  C  CG    . LEU   C 2  150 ? -36.599 -5.798  35.640   1.00 54.82  ? 152 LEU   D CG    1 
ATOM   8070  C  CD1   . LEU   C 2  150 ? -37.402 -6.491  34.538   1.00 43.13  ? 152 LEU   D CD1   1 
ATOM   8071  C  CD2   . LEU   C 2  150 ? -37.115 -6.174  37.035   1.00 62.60  ? 152 LEU   D CD2   1 
ATOM   8072  N  N     . LEU   C 2  151 ? -33.205 -3.622  35.364   1.00 45.76  ? 153 LEU   D N     1 
ATOM   8073  C  CA    . LEU   C 2  151 ? -32.841 -2.215  35.514   1.00 45.94  ? 153 LEU   D CA    1 
ATOM   8074  C  C     . LEU   C 2  151 ? -32.548 -1.553  34.160   1.00 53.66  ? 153 LEU   D C     1 
ATOM   8075  O  O     . LEU   C 2  151 ? -32.943 -0.398  33.919   1.00 46.94  ? 153 LEU   D O     1 
ATOM   8076  C  CB    . LEU   C 2  151 ? -31.629 -2.095  36.440   1.00 42.69  ? 153 LEU   D CB    1 
ATOM   8077  C  CG    . LEU   C 2  151 ? -31.916 -1.875  37.915   1.00 51.18  ? 153 LEU   D CG    1 
ATOM   8078  C  CD1   . LEU   C 2  151 ? -30.623 -1.726  38.688   1.00 48.70  ? 153 LEU   D CD1   1 
ATOM   8079  C  CD2   . LEU   C 2  151 ? -32.769 -0.627  38.065   1.00 55.55  ? 153 LEU   D CD2   1 
ATOM   8080  N  N     . ILE   C 2  152 ? -31.841 -2.257  33.267   1.00 41.89  ? 154 ILE   D N     1 
ATOM   8081  C  CA    . ILE   C 2  152 ? -31.504 -1.660  31.977   1.00 45.08  ? 154 ILE   D CA    1 
ATOM   8082  C  C     . ILE   C 2  152 ? -32.777 -1.296  31.219   1.00 51.25  ? 154 ILE   D C     1 
ATOM   8083  O  O     . ILE   C 2  152 ? -32.914 -0.179  30.704   1.00 47.26  ? 154 ILE   D O     1 
ATOM   8084  C  CB    . ILE   C 2  152 ? -30.602 -2.599  31.156   1.00 49.00  ? 154 ILE   D CB    1 
ATOM   8085  C  CG1   . ILE   C 2  152 ? -29.181 -2.633  31.713   1.00 46.19  ? 154 ILE   D CG1   1 
ATOM   8086  C  CG2   . ILE   C 2  152 ? -30.548 -2.167  29.705   1.00 45.20  ? 154 ILE   D CG2   1 
ATOM   8087  C  CD1   . ILE   C 2  152 ? -28.354 -3.769  31.116   1.00 48.09  ? 154 ILE   D CD1   1 
ATOM   8088  N  N     . SER   C 2  153 ? -33.743 -2.223  31.165   1.00 42.34  ? 155 SER   D N     1 
ATOM   8089  C  CA    A SER   C 2  153 ? -34.994 -1.942  30.466   0.00 43.00  ? 155 SER   D CA    1 
ATOM   8090  C  CA    B SER   C 2  153 ? -34.990 -1.933  30.468   1.00 42.84  ? 155 SER   D CA    1 
ATOM   8091  C  C     . SER   C 2  153 ? -35.770 -0.816  31.142   1.00 43.87  ? 155 SER   D C     1 
ATOM   8092  O  O     . SER   C 2  153 ? -36.330 0.058   30.469   1.00 46.64  ? 155 SER   D O     1 
ATOM   8093  C  CB    A SER   C 2  153 ? -35.846 -3.209  30.387   0.00 39.18  ? 155 SER   D CB    1 
ATOM   8094  C  CB    B SER   C 2  153 ? -35.825 -3.184  30.376   1.00 38.46  ? 155 SER   D CB    1 
ATOM   8095  O  OG    A SER   C 2  153 ? -35.168 -4.237  29.686   0.00 48.37  ? 155 SER   D OG    1 
ATOM   8096  O  OG    B SER   C 2  153 ? -35.136 -4.064  29.537   1.00 49.35  ? 155 SER   D OG    1 
ATOM   8097  N  N     . LYS   C 2  154 ? -35.819 -0.814  32.465   1.00 40.47  ? 156 LYS   D N     1 
ATOM   8098  C  CA    . LYS   C 2  154 ? -36.576 0.239   33.128   1.00 47.80  ? 156 LYS   D CA    1 
ATOM   8099  C  C     . LYS   C 2  154 ? -35.961 1.598   32.846   1.00 47.47  ? 156 LYS   D C     1 
ATOM   8100  O  O     . LYS   C 2  154 ? -36.679 2.548   32.519   1.00 49.24  ? 156 LYS   D O     1 
ATOM   8101  C  CB    . LYS   C 2  154 ? -36.675 -0.031  34.632   1.00 50.38  ? 156 LYS   D CB    1 
ATOM   8102  C  CG    . LYS   C 2  154 ? -37.383 -1.358  34.968   1.00 49.84  ? 156 LYS   D CG    1 
ATOM   8103  C  CD    . LYS   C 2  154 ? -38.613 -1.588  34.085   1.00 42.29  ? 156 LYS   D CD    1 
ATOM   8104  C  CE    . LYS   C 2  154 ? -39.902 -1.566  34.905   1.00 37.40  ? 156 LYS   D CE    1 
ATOM   8105  N  NZ    . LYS   C 2  154 ? -41.068 -2.101  34.150   1.00 43.31  ? 156 LYS   D NZ    1 
ATOM   8106  N  N     . ILE   C 2  155 ? -34.628 1.704   32.915   1.00 47.77  ? 157 ILE   D N     1 
ATOM   8107  C  CA    . ILE   C 2  155 ? -33.981 2.987   32.632   1.00 49.69  ? 157 ILE   D CA    1 
ATOM   8108  C  C     . ILE   C 2  155 ? -34.177 3.369   31.167   1.00 49.71  ? 157 ILE   D C     1 
ATOM   8109  O  O     . ILE   C 2  155 ? -34.412 4.541   30.834   1.00 44.02  ? 157 ILE   D O     1 
ATOM   8110  C  CB    . ILE   C 2  155 ? -32.491 2.940   33.022   1.00 41.17  ? 157 ILE   D CB    1 
ATOM   8111  C  CG1   . ILE   C 2  155 ? -32.349 2.499   34.485   1.00 45.86  ? 157 ILE   D CG1   1 
ATOM   8112  C  CG2   . ILE   C 2  155 ? -31.843 4.295   32.819   1.00 32.39  ? 157 ILE   D CG2   1 
ATOM   8113  C  CD1   . ILE   C 2  155 ? -30.969 2.725   35.087   1.00 44.32  ? 157 ILE   D CD1   1 
ATOM   8114  N  N     . ARG   C 2  156 ? -34.098 2.380   30.276   1.00 48.28  ? 158 ARG   D N     1 
ATOM   8115  C  CA    . ARG   C 2  156 ? -34.450 2.573   28.877   1.00 48.53  ? 158 ARG   D CA    1 
ATOM   8116  C  C     . ARG   C 2  156 ? -35.861 3.127   28.723   1.00 51.40  ? 158 ARG   D C     1 
ATOM   8117  O  O     . ARG   C 2  156 ? -36.129 3.888   27.788   1.00 59.43  ? 158 ARG   D O     1 
ATOM   8118  C  CB    . ARG   C 2  156 ? -34.325 1.240   28.140   1.00 46.27  ? 158 ARG   D CB    1 
ATOM   8119  C  CG    . ARG   C 2  156 ? -33.948 1.331   26.709   1.00 43.01  ? 158 ARG   D CG    1 
ATOM   8120  C  CD    . ARG   C 2  156 ? -32.447 1.385   26.548   1.00 52.13  ? 158 ARG   D CD    1 
ATOM   8121  N  NE    . ARG   C 2  156 ? -32.055 1.191   25.155   1.00 54.36  ? 158 ARG   D NE    1 
ATOM   8122  C  CZ    . ARG   C 2  156 ? -31.031 1.808   24.577   1.00 52.25  ? 158 ARG   D CZ    1 
ATOM   8123  N  NH1   . ARG   C 2  156 ? -30.292 2.687   25.242   1.00 41.23  ? 158 ARG   D NH1   1 
ATOM   8124  N  NH2   . ARG   C 2  156 ? -30.754 1.547   23.297   1.00 33.10  ? 158 ARG   D NH2   1 
ATOM   8125  N  N     . GLU   C 2  157 ? -36.782 2.752   29.615   1.00 52.44  ? 159 GLU   D N     1 
ATOM   8126  C  CA    . GLU   C 2  157 ? -38.144 3.274   29.521   1.00 49.13  ? 159 GLU   D CA    1 
ATOM   8127  C  C     . GLU   C 2  157 ? -38.194 4.761   29.854   1.00 48.54  ? 159 GLU   D C     1 
ATOM   8128  O  O     . GLU   C 2  157 ? -38.808 5.547   29.127   1.00 46.97  ? 159 GLU   D O     1 
ATOM   8129  C  CB    . GLU   C 2  157 ? -39.075 2.490   30.439   1.00 50.84  ? 159 GLU   D CB    1 
ATOM   8130  C  CG    . GLU   C 2  157 ? -39.834 1.372   29.755   1.00 54.02  ? 159 GLU   D CG    1 
ATOM   8131  C  CD    . GLU   C 2  157 ? -41.123 1.043   30.481   1.00 66.40  ? 159 GLU   D CD    1 
ATOM   8132  O  OE1   . GLU   C 2  157 ? -41.086 0.900   31.727   1.00 55.92  ? 159 GLU   D OE1   1 
ATOM   8133  O  OE2   . GLU   C 2  157 ? -42.176 0.945   29.806   1.00 73.90  ? 159 GLU   D OE2   1 
ATOM   8134  N  N     . GLU   C 2  158 ? -37.547 5.172   30.949   1.00 49.02  ? 160 GLU   D N     1 
ATOM   8135  C  CA    . GLU   C 2  158 ? -37.573 6.580   31.328   1.00 44.00  ? 160 GLU   D CA    1 
ATOM   8136  C  C     . GLU   C 2  158 ? -36.580 7.428   30.556   1.00 46.41  ? 160 GLU   D C     1 
ATOM   8137  O  O     . GLU   C 2  158 ? -36.791 8.639   30.449   1.00 45.67  ? 160 GLU   D O     1 
ATOM   8138  C  CB    . GLU   C 2  158 ? -37.295 6.759   32.816   1.00 43.18  ? 160 GLU   D CB    1 
ATOM   8139  C  CG    . GLU   C 2  158 ? -38.474 6.473   33.692   1.00 52.02  ? 160 GLU   D CG    1 
ATOM   8140  C  CD    . GLU   C 2  158 ? -38.206 6.842   35.130   1.00 59.06  ? 160 GLU   D CD    1 
ATOM   8141  O  OE1   . GLU   C 2  158 ? -37.588 7.902   35.349   1.00 61.13  ? 160 GLU   D OE1   1 
ATOM   8142  O  OE2   . GLU   C 2  158 ? -38.602 6.075   36.034   1.00 54.84  ? 160 GLU   D OE2   1 
ATOM   8143  N  N     . TYR   C 2  159 ? -35.503 6.836   30.036   1.00 51.60  ? 161 TYR   D N     1 
ATOM   8144  C  CA    . TYR   C 2  159 ? -34.453 7.572   29.323   1.00 42.91  ? 161 TYR   D CA    1 
ATOM   8145  C  C     . TYR   C 2  159 ? -34.167 6.890   27.995   1.00 47.36  ? 161 TYR   D C     1 
ATOM   8146  O  O     . TYR   C 2  159 ? -33.036 6.477   27.716   1.00 38.57  ? 161 TYR   D O     1 
ATOM   8147  C  CB    . TYR   C 2  159 ? -33.190 7.656   30.166   1.00 38.06  ? 161 TYR   D CB    1 
ATOM   8148  C  CG    . TYR   C 2  159 ? -33.417 8.144   31.579   1.00 47.22  ? 161 TYR   D CG    1 
ATOM   8149  C  CD1   . TYR   C 2  159 ? -33.735 7.253   32.606   1.00 46.85  ? 161 TYR   D CD1   1 
ATOM   8150  C  CD2   . TYR   C 2  159 ? -33.293 9.490   31.889   1.00 38.58  ? 161 TYR   D CD2   1 
ATOM   8151  C  CE1   . TYR   C 2  159 ? -33.924 7.697   33.896   1.00 41.02  ? 161 TYR   D CE1   1 
ATOM   8152  C  CE2   . TYR   C 2  159 ? -33.492 9.946   33.165   1.00 53.49  ? 161 TYR   D CE2   1 
ATOM   8153  C  CZ    . TYR   C 2  159 ? -33.805 9.052   34.173   1.00 60.49  ? 161 TYR   D CZ    1 
ATOM   8154  O  OH    . TYR   C 2  159 ? -33.992 9.541   35.453   1.00 60.49  ? 161 TYR   D OH    1 
ATOM   8155  N  N     . PRO   C 2  160 ? -35.182 6.757   27.145   1.00 44.27  ? 162 PRO   D N     1 
ATOM   8156  C  CA    . PRO   C 2  160 ? -35.018 5.954   25.930   1.00 45.65  ? 162 PRO   D CA    1 
ATOM   8157  C  C     . PRO   C 2  160 ? -33.942 6.472   25.003   1.00 43.44  ? 162 PRO   D C     1 
ATOM   8158  O  O     . PRO   C 2  160 ? -33.482 5.719   24.139   1.00 49.92  ? 162 PRO   D O     1 
ATOM   8159  C  CB    . PRO   C 2  160 ? -36.401 6.047   25.280   1.00 46.64  ? 162 PRO   D CB    1 
ATOM   8160  C  CG    . PRO   C 2  160 ? -36.876 7.362   25.696   1.00 43.82  ? 162 PRO   D CG    1 
ATOM   8161  C  CD    . PRO   C 2  160 ? -36.427 7.533   27.111   1.00 37.08  ? 162 PRO   D CD    1 
ATOM   8162  N  N     . ASP   C 2  161 ? -33.522 7.726   25.153   1.00 37.07  ? 163 ASP   D N     1 
ATOM   8163  C  CA    . ASP   C 2  161 ? -32.598 8.367   24.229   1.00 45.02  ? 163 ASP   D CA    1 
ATOM   8164  C  C     . ASP   C 2  161 ? -31.300 8.772   24.926   1.00 45.32  ? 163 ASP   D C     1 
ATOM   8165  O  O     . ASP   C 2  161 ? -30.629 9.721   24.514   1.00 43.86  ? 163 ASP   D O     1 
ATOM   8166  C  CB    . ASP   C 2  161 ? -33.261 9.576   23.560   1.00 42.33  ? 163 ASP   D CB    1 
ATOM   8167  C  CG    . ASP   C 2  161 ? -33.491 10.732  24.523   1.00 56.06  ? 163 ASP   D CG    1 
ATOM   8168  O  OD1   . ASP   C 2  161 ? -33.896 10.513  25.694   1.00 58.28  ? 163 ASP   D OD1   1 
ATOM   8169  O  OD2   . ASP   C 2  161 ? -33.261 11.879  24.101   1.00 62.72  ? 163 ASP   D OD2   1 
ATOM   8170  N  N     . ARG   C 2  162 ? -30.949 8.070   25.996   1.00 42.24  ? 164 ARG   D N     1 
ATOM   8171  C  CA    . ARG   C 2  162 ? -29.664 8.217   26.656   1.00 40.64  ? 164 ARG   D CA    1 
ATOM   8172  C  C     . ARG   C 2  162 ? -28.880 6.930   26.454   1.00 30.58  ? 164 ARG   D C     1 
ATOM   8173  O  O     . ARG   C 2  162 ? -29.454 5.871   26.201   1.00 32.32  ? 164 ARG   D O     1 
ATOM   8174  C  CB    . ARG   C 2  162 ? -29.829 8.537   28.150   1.00 41.55  ? 164 ARG   D CB    1 
ATOM   8175  C  CG    . ARG   C 2  162 ? -30.467 9.891   28.469   1.00 42.39  ? 164 ARG   D CG    1 
ATOM   8176  C  CD    . ARG   C 2  162 ? -29.569 11.074  28.124   1.00 47.70  ? 164 ARG   D CD    1 
ATOM   8177  N  NE    . ARG   C 2  162 ? -29.757 11.518  26.742   1.00 65.51  ? 164 ARG   D NE    1 
ATOM   8178  C  CZ    . ARG   C 2  162 ? -29.019 12.442  26.131   1.00 62.95  ? 164 ARG   D CZ    1 
ATOM   8179  N  NH1   . ARG   C 2  162 ? -27.997 13.027  26.737   1.00 61.39  ? 164 ARG   D NH1   1 
ATOM   8180  N  NH2   . ARG   C 2  162 ? -29.324 12.801  24.884   1.00 64.94  ? 164 ARG   D NH2   1 
ATOM   8181  N  N     . ILE   C 2  163 ? -27.561 7.038   26.529   1.00 32.83  ? 165 ILE   D N     1 
ATOM   8182  C  CA    . ILE   C 2  163 ? -26.689 5.936   26.138   1.00 30.77  ? 165 ILE   D CA    1 
ATOM   8183  C  C     . ILE   C 2  163 ? -26.646 4.923   27.268   1.00 36.33  ? 165 ILE   D C     1 
ATOM   8184  O  O     . ILE   C 2  163 ? -26.372 5.281   28.422   1.00 40.71  ? 165 ILE   D O     1 
ATOM   8185  C  CB    . ILE   C 2  163 ? -25.277 6.448   25.797   1.00 28.06  ? 165 ILE   D CB    1 
ATOM   8186  C  CG1   . ILE   C 2  163 ? -25.293 7.338   24.558   1.00 31.95  ? 165 ILE   D CG1   1 
ATOM   8187  C  CG2   . ILE   C 2  163 ? -24.353 5.279   25.582   1.00 34.60  ? 165 ILE   D CG2   1 
ATOM   8188  C  CD1   . ILE   C 2  163 ? -25.612 6.600   23.231   1.00 26.58  ? 165 ILE   D CD1   1 
ATOM   8189  N  N     . MET   C 2  164 ? -26.939 3.663   26.947   1.00 34.24  ? 166 MET   D N     1 
ATOM   8190  C  CA    . MET   C 2  164 ? -26.880 2.565   27.905   1.00 33.39  ? 166 MET   D CA    1 
ATOM   8191  C  C     . MET   C 2  164 ? -25.571 1.814   27.708   1.00 44.29  ? 166 MET   D C     1 
ATOM   8192  O  O     . MET   C 2  164 ? -25.342 1.228   26.637   1.00 35.99  ? 166 MET   D O     1 
ATOM   8193  C  CB    . MET   C 2  164 ? -28.058 1.608   27.735   1.00 40.33  ? 166 MET   D CB    1 
ATOM   8194  C  CG    . MET   C 2  164 ? -28.282 0.618   28.907   1.00 38.52  ? 166 MET   D CG    1 
ATOM   8195  S  SD    . MET   C 2  164 ? -28.694 1.502   30.427   1.00 47.57  ? 166 MET   D SD    1 
ATOM   8196  C  CE    . MET   C 2  164 ? -27.026 1.980   30.845   1.00 44.07  ? 166 MET   D CE    1 
ATOM   8197  N  N     . ASN   C 2  165 ? -24.733 1.810   28.745   1.00 36.42  ? 167 ASN   D N     1 
ATOM   8198  C  CA    . ASN   C 2  165 ? -23.393 1.236   28.687   1.00 41.18  ? 167 ASN   D CA    1 
ATOM   8199  C  C     . ASN   C 2  165 ? -23.213 0.214   29.802   1.00 41.44  ? 167 ASN   D C     1 
ATOM   8200  O  O     . ASN   C 2  165 ? -23.384 0.547   30.979   1.00 52.12  ? 167 ASN   D O     1 
ATOM   8201  C  CB    . ASN   C 2  165 ? -22.343 2.349   28.812   1.00 46.86  ? 167 ASN   D CB    1 
ATOM   8202  C  CG    . ASN   C 2  165 ? -20.945 1.814   28.945   1.00 46.96  ? 167 ASN   D CG    1 
ATOM   8203  O  OD1   . ASN   C 2  165 ? -20.668 0.709   28.492   1.00 48.79  ? 167 ASN   D OD1   1 
ATOM   8204  N  ND2   . ASN   C 2  165 ? -20.054 2.584   29.573   1.00 38.16  ? 167 ASN   D ND2   1 
ATOM   8205  N  N     . THR   C 2  166 ? -22.827 -1.008  29.457   1.00 40.14  ? 168 THR   D N     1 
ATOM   8206  C  CA    . THR   C 2  166 ? -22.603 -2.030  30.474   1.00 49.25  ? 168 THR   D CA    1 
ATOM   8207  C  C     . THR   C 2  166 ? -21.164 -2.546  30.486   1.00 54.41  ? 168 THR   D C     1 
ATOM   8208  O  O     . THR   C 2  166 ? -20.452 -2.505  29.471   1.00 52.44  ? 168 THR   D O     1 
ATOM   8209  C  CB    . THR   C 2  166 ? -23.535 -3.217  30.286   1.00 46.44  ? 168 THR   D CB    1 
ATOM   8210  O  OG1   . THR   C 2  166 ? -23.077 -3.996  29.174   1.00 46.98  ? 168 THR   D OG1   1 
ATOM   8211  C  CG2   . THR   C 2  166 ? -24.971 -2.728  30.046   1.00 44.46  ? 168 THR   D CG2   1 
ATOM   8212  N  N     . PHE   C 2  167 ? -20.750 -3.037  31.662   1.00 55.95  ? 169 PHE   D N     1 
ATOM   8213  C  CA    . PHE   C 2  167 ? -19.538 -3.840  31.856   1.00 46.15  ? 169 PHE   D CA    1 
ATOM   8214  C  C     . PHE   C 2  167 ? -19.987 -5.234  32.286   1.00 50.47  ? 169 PHE   D C     1 
ATOM   8215  O  O     . PHE   C 2  167 ? -20.076 -5.531  33.478   1.00 54.91  ? 169 PHE   D O     1 
ATOM   8216  C  CB    . PHE   C 2  167 ? -18.624 -3.229  32.882   1.00 43.89  ? 169 PHE   D CB    1 
ATOM   8217  C  CG    . PHE   C 2  167 ? -17.962 -1.976  32.426   1.00 45.21  ? 169 PHE   D CG    1 
ATOM   8218  C  CD1   . PHE   C 2  167 ? -18.614 -0.761  32.528   1.00 47.35  ? 169 PHE   D CD1   1 
ATOM   8219  C  CD2   . PHE   C 2  167 ? -16.680 -2.009  31.910   1.00 37.78  ? 169 PHE   D CD2   1 
ATOM   8220  C  CE1   . PHE   C 2  167 ? -17.996 0.404   32.113   1.00 47.17  ? 169 PHE   D CE1   1 
ATOM   8221  C  CE2   . PHE   C 2  167 ? -16.061 -0.861  31.497   1.00 40.73  ? 169 PHE   D CE2   1 
ATOM   8222  C  CZ    . PHE   C 2  167 ? -16.713 0.351   31.596   1.00 46.18  ? 169 PHE   D CZ    1 
ATOM   8223  N  N     . SER   C 2  168 ? -20.276 -6.082  31.305   1.00 41.70  ? 170 SER   D N     1 
ATOM   8224  C  CA    . SER   C 2  168 ? -20.826 -7.405  31.540   1.00 43.75  ? 170 SER   D CA    1 
ATOM   8225  C  C     . SER   C 2  168 ? -19.700 -8.426  31.664   1.00 50.30  ? 170 SER   D C     1 
ATOM   8226  O  O     . SER   C 2  168 ? -18.938 -8.625  30.711   1.00 52.82  ? 170 SER   D O     1 
ATOM   8227  C  CB    . SER   C 2  168 ? -21.765 -7.780  30.397   1.00 46.41  ? 170 SER   D CB    1 
ATOM   8228  O  OG    . SER   C 2  168 ? -22.762 -6.790  30.222   1.00 48.24  ? 170 SER   D OG    1 
ATOM   8229  N  N     . VAL   C 2  169 ? -19.612 -9.098  32.826   1.00 50.80  ? 171 VAL   D N     1 
ATOM   8230  C  CA    . VAL   C 2  169 ? -18.576 -10.102 33.064   1.00 42.96  ? 171 VAL   D CA    1 
ATOM   8231  C  C     . VAL   C 2  169 ? -19.092 -11.488 32.714   1.00 42.42  ? 171 VAL   D C     1 
ATOM   8232  O  O     . VAL   C 2  169 ? -20.195 -11.871 33.116   1.00 49.55  ? 171 VAL   D O     1 
ATOM   8233  C  CB    . VAL   C 2  169 ? -18.085 -10.065 34.507   1.00 35.65  ? 171 VAL   D CB    1 
ATOM   8234  C  CG1   . VAL   C 2  169 ? -17.143 -11.236 34.705   1.00 47.92  ? 171 VAL   D CG1   1 
ATOM   8235  C  CG2   . VAL   C 2  169 ? -17.366 -8.771  34.775   1.00 33.29  ? 171 VAL   D CG2   1 
ATOM   8236  N  N     . MET   C 2  170 ? -18.296 -12.254 31.986   1.00 50.74  ? 172 MET   D N     1 
ATOM   8237  C  CA    . MET   C 2  170 ? -18.906 -13.476 31.482   1.00 57.59  ? 172 MET   D CA    1 
ATOM   8238  C  C     . MET   C 2  170 ? -18.463 -14.675 32.282   1.00 55.72  ? 172 MET   D C     1 
ATOM   8239  O  O     . MET   C 2  170 ? -17.409 -14.657 32.929   1.00 47.89  ? 172 MET   D O     1 
ATOM   8240  C  CB    . MET   C 2  170 ? -18.560 -13.709 30.008   1.00 53.09  ? 172 MET   D CB    1 
ATOM   8241  C  CG    . MET   C 2  170 ? -18.587 -12.456 29.135   1.00 54.90  ? 172 MET   D CG    1 
ATOM   8242  S  SD    . MET   C 2  170 ? -20.231 -12.008 28.570   0.50 45.89  ? 172 MET   D SD    1 
ATOM   8243  C  CE    . MET   C 2  170 ? -20.814 -13.591 27.960   0.93 48.78  ? 172 MET   D CE    1 
ATOM   8244  N  N     . PRO   C 2  171 ? -19.266 -15.750 32.245   1.00 67.26  ? 173 PRO   D N     1 
ATOM   8245  C  CA    . PRO   C 2  171 ? -18.932 -16.987 32.966   1.00 65.61  ? 173 PRO   D CA    1 
ATOM   8246  C  C     . PRO   C 2  171 ? -17.821 -17.789 32.302   1.00 56.29  ? 173 PRO   D C     1 
ATOM   8247  O  O     . PRO   C 2  171 ? -17.796 -17.951 31.079   1.00 52.57  ? 173 PRO   D O     1 
ATOM   8248  C  CB    . PRO   C 2  171 ? -20.247 -17.786 32.930   1.00 58.38  ? 173 PRO   D CB    1 
ATOM   8249  C  CG    . PRO   C 2  171 ? -21.297 -16.818 32.549   1.00 55.05  ? 173 PRO   D CG    1 
ATOM   8250  C  CD    . PRO   C 2  171 ? -20.649 -15.760 31.731   1.00 55.36  ? 173 PRO   D CD    1 
ATOM   8251  N  N     . SER   C 2  172 ? -16.927 -18.341 33.138   1.00 63.72  ? 174 SER   D N     1 
ATOM   8252  C  CA    . SER   C 2  172 ? -16.048 -19.482 32.761   1.00 65.55  ? 174 SER   D CA    1 
ATOM   8253  C  C     . SER   C 2  172 ? -15.989 -20.524 33.881   1.00 62.59  ? 174 SER   D C     1 
ATOM   8254  O  O     . SER   C 2  172 ? -15.680 -20.173 35.036   1.00 61.83  ? 174 SER   D O     1 
ATOM   8255  C  CB    . SER   C 2  172 ? -14.631 -19.027 32.418   1.00 61.64  ? 174 SER   D CB    1 
ATOM   8256  O  OG    . SER   C 2  172 ? -13.839 -20.143 32.050   1.00 55.53  ? 174 SER   D OG    1 
ATOM   8257  N  N     . PRO   C 2  173 ? -16.238 -21.807 33.582   1.00 62.29  ? 175 PRO   D N     1 
ATOM   8258  C  CA    . PRO   C 2  173 ? -16.043 -22.849 34.602   1.00 64.14  ? 175 PRO   D CA    1 
ATOM   8259  C  C     . PRO   C 2  173 ? -14.660 -22.809 35.242   1.00 64.79  ? 175 PRO   D C     1 
ATOM   8260  O  O     . PRO   C 2  173 ? -14.453 -23.368 36.326   1.00 70.23  ? 175 PRO   D O     1 
ATOM   8261  C  CB    . PRO   C 2  173 ? -16.258 -24.149 33.816   1.00 54.56  ? 175 PRO   D CB    1 
ATOM   8262  C  CG    . PRO   C 2  173 ? -17.198 -23.760 32.721   1.00 60.30  ? 175 PRO   D CG    1 
ATOM   8263  C  CD    . PRO   C 2  173 ? -16.753 -22.369 32.319   1.00 60.62  ? 175 PRO   D CD    1 
ATOM   8264  N  N     . LYS   C 2  174 ? -13.705 -22.159 34.574   1.00 55.58  ? 176 LYS   D N     1 
ATOM   8265  C  CA    . LYS   C 2  174 ? -12.372 -21.977 35.126   1.00 65.93  ? 176 LYS   D CA    1 
ATOM   8266  C  C     . LYS   C 2  174 ? -12.386 -21.044 36.320   1.00 66.98  ? 176 LYS   D C     1 
ATOM   8267  O  O     . LYS   C 2  174 ? -11.322 -20.721 36.871   1.00 70.00  ? 176 LYS   D O     1 
ATOM   8268  C  CB    . LYS   C 2  174 ? -11.409 -21.432 34.059   1.00 68.65  ? 176 LYS   D CB    1 
ATOM   8269  C  CG    . LYS   C 2  174 ? -11.193 -22.309 32.834   1.00 65.60  ? 176 LYS   D CG    1 
ATOM   8270  C  CD    . LYS   C 2  174 ? -10.019 -21.759 32.007   1.00 70.24  ? 176 LYS   D CD    1 
ATOM   8271  C  CE    . LYS   C 2  174 ? -9.793  -22.527 30.706   1.00 63.67  ? 176 LYS   D CE    1 
ATOM   8272  N  NZ    . LYS   C 2  174 ? -8.582  -22.027 29.991   1.00 73.33  ? 176 LYS   D NZ    1 
ATOM   8273  N  N     . VAL   C 2  175 ? -13.569 -20.586 36.726   1.00 62.12  ? 177 VAL   D N     1 
ATOM   8274  C  CA    . VAL   C 2  175 ? -13.651 -19.589 37.787   1.00 73.86  ? 177 VAL   D CA    1 
ATOM   8275  C  C     . VAL   C 2  175 ? -14.902 -19.722 38.648   1.00 76.88  ? 177 VAL   D C     1 
ATOM   8276  O  O     . VAL   C 2  175 ? -15.003 -19.069 39.693   1.00 81.23  ? 177 VAL   D O     1 
ATOM   8277  C  CB    . VAL   C 2  175 ? -13.591 -18.168 37.210   1.00 69.45  ? 177 VAL   D CB    1 
ATOM   8278  C  CG1   . VAL   C 2  175 ? -14.950 -17.804 36.606   1.00 63.71  ? 177 VAL   D CG1   1 
ATOM   8279  C  CG2   . VAL   C 2  175 ? -13.195 -17.197 38.311   1.00 65.84  ? 177 VAL   D CG2   1 
ATOM   8280  N  N     . SER   C 2  176 ? -15.876 -20.523 38.214   1.00 68.62  ? 178 SER   D N     1 
ATOM   8281  C  CA    . SER   C 2  176 ? -17.095 -20.676 38.993   1.00 71.12  ? 178 SER   D CA    1 
ATOM   8282  C  C     . SER   C 2  176 ? -17.763 -21.994 38.648   1.00 80.05  ? 178 SER   D C     1 
ATOM   8283  O  O     . SER   C 2  176 ? -17.850 -22.371 37.475   1.00 65.95  ? 178 SER   D O     1 
ATOM   8284  C  CB    . SER   C 2  176 ? -18.085 -19.529 38.763   1.00 79.28  ? 178 SER   D CB    1 
ATOM   8285  O  OG    . SER   C 2  176 ? -19.372 -19.877 39.264   1.00 72.86  ? 178 SER   D OG    1 
ATOM   8286  N  N     . ASP   C 2  177 ? -18.270 -22.654 39.689   1.00 88.36  ? 179 ASP   D N     1 
ATOM   8287  C  CA    . ASP   C 2  177 ? -18.864 -23.980 39.614   1.00 81.01  ? 179 ASP   D CA    1 
ATOM   8288  C  C     . ASP   C 2  177 ? -20.371 -23.947 39.389   1.00 77.55  ? 179 ASP   D C     1 
ATOM   8289  O  O     . ASP   C 2  177 ? -20.955 -24.977 39.019   1.00 70.26  ? 179 ASP   D O     1 
ATOM   8290  C  CB    . ASP   C 2  177 ? -18.549 -24.737 40.914   1.00 87.88  ? 179 ASP   D CB    1 
ATOM   8291  C  CG    . ASP   C 2  177 ? -18.340 -26.219 40.702   1.00 97.31  ? 179 ASP   D CG    1 
ATOM   8292  O  OD1   . ASP   C 2  177 ? -19.058 -26.814 39.874   1.00 104.83 ? 179 ASP   D OD1   1 
ATOM   8293  O  OD2   . ASP   C 2  177 ? -17.458 -26.791 41.377   1.00 102.92 ? 179 ASP   D OD2   1 
ATOM   8294  N  N     . THR   C 2  178 ? -21.014 -22.795 39.597   1.00 72.66  ? 180 THR   D N     1 
ATOM   8295  C  CA    . THR   C 2  178 ? -22.469 -22.741 39.553   1.00 62.28  ? 180 THR   D CA    1 
ATOM   8296  C  C     . THR   C 2  178 ? -22.973 -23.328 38.243   1.00 61.68  ? 180 THR   D C     1 
ATOM   8297  O  O     . THR   C 2  178 ? -22.847 -22.708 37.185   1.00 67.89  ? 180 THR   D O     1 
ATOM   8298  C  CB    . THR   C 2  178 ? -22.977 -21.311 39.734   1.00 65.65  ? 180 THR   D CB    1 
ATOM   8299  O  OG1   . THR   C 2  178 ? -22.452 -20.750 40.948   1.00 58.59  ? 180 THR   D OG1   1 
ATOM   8300  C  CG2   . THR   C 2  178 ? -24.497 -21.302 39.790   1.00 62.25  ? 180 THR   D CG2   1 
ATOM   8301  N  N     . VAL   C 2  179 ? -23.549 -24.529 38.311   1.00 66.12  ? 181 VAL   D N     1 
ATOM   8302  C  CA    . VAL   C 2  179 ? -23.959 -25.264 37.119   1.00 73.04  ? 181 VAL   D CA    1 
ATOM   8303  C  C     . VAL   C 2  179 ? -24.914 -24.488 36.207   1.00 70.87  ? 181 VAL   D C     1 
ATOM   8304  O  O     . VAL   C 2  179 ? -25.009 -24.802 35.015   1.00 72.23  ? 181 VAL   D O     1 
ATOM   8305  C  CB    . VAL   C 2  179 ? -24.591 -26.611 37.535   1.00 67.61  ? 181 VAL   D CB    1 
ATOM   8306  C  CG1   . VAL   C 2  179 ? -24.921 -27.450 36.306   1.00 58.47  ? 181 VAL   D CG1   1 
ATOM   8307  C  CG2   . VAL   C 2  179 ? -23.669 -27.358 38.483   1.00 73.20  ? 181 VAL   D CG2   1 
ATOM   8308  N  N     . VAL   C 2  180 ? -25.635 -23.486 36.718   1.00 67.85  ? 182 VAL   D N     1 
ATOM   8309  C  CA    . VAL   C 2  180 ? -26.667 -22.838 35.904   1.00 72.83  ? 182 VAL   D CA    1 
ATOM   8310  C  C     . VAL   C 2  180 ? -26.185 -21.560 35.213   1.00 68.62  ? 182 VAL   D C     1 
ATOM   8311  O  O     . VAL   C 2  180 ? -26.967 -20.949 34.471   1.00 67.11  ? 182 VAL   D O     1 
ATOM   8312  C  CB    . VAL   C 2  180 ? -27.948 -22.536 36.717   1.00 66.59  ? 182 VAL   D CB    1 
ATOM   8313  C  CG1   . VAL   C 2  180 ? -28.841 -23.760 36.794   1.00 68.23  ? 182 VAL   D CG1   1 
ATOM   8314  C  CG2   . VAL   C 2  180 ? -27.613 -22.000 38.099   1.00 58.78  ? 182 VAL   D CG2   1 
ATOM   8315  N  N     . GLU   C 2  181 ? -24.932 -21.145 35.407   1.00 67.42  ? 183 GLU   D N     1 
ATOM   8316  C  CA    . GLU   C 2  181 ? -24.470 -19.893 34.804   1.00 71.83  ? 183 GLU   D CA    1 
ATOM   8317  C  C     . GLU   C 2  181 ? -24.682 -19.816 33.289   1.00 65.92  ? 183 GLU   D C     1 
ATOM   8318  O  O     . GLU   C 2  181 ? -25.028 -18.726 32.802   1.00 59.67  ? 183 GLU   D O     1 
ATOM   8319  C  CB    . GLU   C 2  181 ? -22.999 -19.652 35.179   1.00 62.49  ? 183 GLU   D CB    1 
ATOM   8320  C  CG    . GLU   C 2  181 ? -22.819 -19.456 36.677   1.00 63.66  ? 183 GLU   D CG    1 
ATOM   8321  C  CD    . GLU   C 2  181 ? -21.469 -18.877 37.064   1.00 69.85  ? 183 GLU   D CD    1 
ATOM   8322  O  OE1   . GLU   C 2  181 ? -20.836 -18.201 36.223   1.00 77.02  ? 183 GLU   D OE1   1 
ATOM   8323  O  OE2   . GLU   C 2  181 ? -21.042 -19.092 38.221   1.00 67.31  ? 183 GLU   D OE2   1 
ATOM   8324  N  N     . PRO   C 2  182 ? -24.525 -20.888 32.503   1.00 70.77  ? 184 PRO   D N     1 
ATOM   8325  C  CA    . PRO   C 2  182 ? -24.914 -20.808 31.077   1.00 58.73  ? 184 PRO   D CA    1 
ATOM   8326  C  C     . PRO   C 2  182 ? -26.367 -20.421 30.856   1.00 58.51  ? 184 PRO   D C     1 
ATOM   8327  O  O     . PRO   C 2  182 ? -26.718 -19.982 29.755   1.00 58.70  ? 184 PRO   D O     1 
ATOM   8328  C  CB    . PRO   C 2  182 ? -24.626 -22.222 30.546   1.00 60.15  ? 184 PRO   D CB    1 
ATOM   8329  C  CG    . PRO   C 2  182 ? -23.563 -22.756 31.463   1.00 66.44  ? 184 PRO   D CG    1 
ATOM   8330  C  CD    . PRO   C 2  182 ? -23.831 -22.149 32.825   1.00 64.91  ? 184 PRO   D CD    1 
ATOM   8331  N  N     . TYR   C 2  183 ? -27.237 -20.598 31.845   1.00 61.32  ? 185 TYR   D N     1 
ATOM   8332  C  CA    . TYR   C 2  183 ? -28.578 -20.038 31.727   1.00 64.81  ? 185 TYR   D CA    1 
ATOM   8333  C  C     . TYR   C 2  183 ? -28.563 -18.540 32.009   1.00 63.68  ? 185 TYR   D C     1 
ATOM   8334  O  O     . TYR   C 2  183 ? -29.049 -17.743 31.198   1.00 59.17  ? 185 TYR   D O     1 
ATOM   8335  C  CB    . TYR   C 2  183 ? -29.542 -20.754 32.680   1.00 66.35  ? 185 TYR   D CB    1 
ATOM   8336  C  CG    . TYR   C 2  183 ? -29.749 -22.218 32.372   1.00 70.04  ? 185 TYR   D CG    1 
ATOM   8337  C  CD1   . TYR   C 2  183 ? -30.325 -22.621 31.169   1.00 70.60  ? 185 TYR   D CD1   1 
ATOM   8338  C  CD2   . TYR   C 2  183 ? -29.380 -23.199 33.286   1.00 70.22  ? 185 TYR   D CD2   1 
ATOM   8339  C  CE1   . TYR   C 2  183 ? -30.517 -23.964 30.882   1.00 72.52  ? 185 TYR   D CE1   1 
ATOM   8340  C  CE2   . TYR   C 2  183 ? -29.567 -24.543 33.007   1.00 67.79  ? 185 TYR   D CE2   1 
ATOM   8341  C  CZ    . TYR   C 2  183 ? -30.138 -24.917 31.808   1.00 69.31  ? 185 TYR   D CZ    1 
ATOM   8342  O  OH    . TYR   C 2  183 ? -30.320 -26.246 31.530   1.00 65.69  ? 185 TYR   D OH    1 
ATOM   8343  N  N     . ASN   C 2  184 ? -27.988 -18.144 33.155   1.00 55.15  ? 186 ASN   D N     1 
ATOM   8344  C  CA    . ASN   C 2  184 ? -27.971 -16.745 33.571   1.00 55.95  ? 186 ASN   D CA    1 
ATOM   8345  C  C     . ASN   C 2  184 ? -27.274 -15.841 32.560   1.00 62.73  ? 186 ASN   D C     1 
ATOM   8346  O  O     . ASN   C 2  184 ? -27.443 -14.613 32.617   1.00 53.14  ? 186 ASN   D O     1 
ATOM   8347  C  CB    . ASN   C 2  184 ? -27.277 -16.602 34.933   1.00 57.47  ? 186 ASN   D CB    1 
ATOM   8348  C  CG    . ASN   C 2  184 ? -27.975 -17.367 36.037   1.00 52.23  ? 186 ASN   D CG    1 
ATOM   8349  O  OD1   . ASN   C 2  184 ? -29.186 -17.555 36.015   1.00 46.47  ? 186 ASN   D OD1   1 
ATOM   8350  N  ND2   . ASN   C 2  184 ? -27.200 -17.814 37.013   1.00 56.98  ? 186 ASN   D ND2   1 
ATOM   8351  N  N     . ALA   C 2  185 ? -26.473 -16.412 31.657   1.00 63.03  ? 187 ALA   D N     1 
ATOM   8352  C  CA    . ALA   C 2  185 ? -25.735 -15.636 30.672   1.00 55.08  ? 187 ALA   D CA    1 
ATOM   8353  C  C     . ALA   C 2  185 ? -26.460 -15.563 29.333   1.00 48.62  ? 187 ALA   D C     1 
ATOM   8354  O  O     . ALA   C 2  185 ? -26.626 -14.476 28.780   1.00 49.62  ? 187 ALA   D O     1 
ATOM   8355  C  CB    . ALA   C 2  185 ? -24.331 -16.218 30.497   1.00 57.90  ? 187 ALA   D CB    1 
ATOM   8356  N  N     . THR   C 2  186 ? -26.920 -16.698 28.809   1.00 49.07  ? 188 THR   D N     1 
ATOM   8357  C  CA    . THR   C 2  186 ? -27.677 -16.668 27.567   1.00 44.19  ? 188 THR   D CA    1 
ATOM   8358  C  C     . THR   C 2  186 ? -28.983 -15.905 27.735   1.00 53.22  ? 188 THR   D C     1 
ATOM   8359  O  O     . THR   C 2  186 ? -29.378 -15.139 26.848   1.00 57.40  ? 188 THR   D O     1 
ATOM   8360  C  CB    . THR   C 2  186 ? -27.942 -18.086 27.067   1.00 43.14  ? 188 THR   D CB    1 
ATOM   8361  O  OG1   . THR   C 2  186 ? -26.715 -18.652 26.597   1.00 59.79  ? 188 THR   D OG1   1 
ATOM   8362  C  CG2   . THR   C 2  186 ? -28.950 -18.073 25.916   1.00 43.01  ? 188 THR   D CG2   1 
ATOM   8363  N  N     . LEU   C 2  187 ? -29.678 -16.105 28.856   1.00 57.20  ? 189 LEU   D N     1 
ATOM   8364  C  CA    . LEU   C 2  187 ? -30.855 -15.285 29.122   1.00 57.42  ? 189 LEU   D CA    1 
ATOM   8365  C  C     . LEU   C 2  187 ? -30.471 -13.821 29.272   1.00 55.35  ? 189 LEU   D C     1 
ATOM   8366  O  O     . LEU   C 2  187 ? -31.234 -12.932 28.876   1.00 51.23  ? 189 LEU   D O     1 
ATOM   8367  C  CB    . LEU   C 2  187 ? -31.581 -15.768 30.380   1.00 57.19  ? 189 LEU   D CB    1 
ATOM   8368  C  CG    . LEU   C 2  187 ? -32.330 -17.104 30.342   1.00 61.03  ? 189 LEU   D CG    1 
ATOM   8369  C  CD1   . LEU   C 2  187 ? -32.772 -17.490 31.750   1.00 59.39  ? 189 LEU   D CD1   1 
ATOM   8370  C  CD2   . LEU   C 2  187 ? -33.526 -17.039 29.387   1.00 59.05  ? 189 LEU   D CD2   1 
ATOM   8371  N  N     . SER   C 2  188 ? -29.293 -13.552 29.831   1.00 49.00  ? 190 SER   D N     1 
ATOM   8372  C  CA    . SER   C 2  188 ? -28.898 -12.173 30.062   1.00 51.87  ? 190 SER   D CA    1 
ATOM   8373  C  C     . SER   C 2  188 ? -28.472 -11.498 28.759   1.00 60.15  ? 190 SER   D C     1 
ATOM   8374  O  O     . SER   C 2  188 ? -29.004 -10.440 28.398   1.00 51.93  ? 190 SER   D O     1 
ATOM   8375  C  CB    . SER   C 2  188 ? -27.779 -12.126 31.105   1.00 55.05  ? 190 SER   D CB    1 
ATOM   8376  O  OG    . SER   C 2  188 ? -27.406 -10.789 31.402   1.00 58.09  ? 190 SER   D OG    1 
ATOM   8377  N  N     . VAL   C 2  189 ? -27.525 -12.107 28.036   1.00 53.63  ? 191 VAL   D N     1 
ATOM   8378  C  CA    . VAL   C 2  189 ? -27.066 -11.546 26.769   1.00 46.69  ? 191 VAL   D CA    1 
ATOM   8379  C  C     . VAL   C 2  189 ? -28.247 -11.253 25.862   1.00 52.73  ? 191 VAL   D C     1 
ATOM   8380  O  O     . VAL   C 2  189 ? -28.232 -10.275 25.104   1.00 48.48  ? 191 VAL   D O     1 
ATOM   8381  C  CB    . VAL   C 2  189 ? -26.055 -12.502 26.097   1.00 51.80  ? 191 VAL   D CB    1 
ATOM   8382  C  CG1   . VAL   C 2  189 ? -26.265 -12.539 24.571   1.00 52.21  ? 191 VAL   D CG1   1 
ATOM   8383  C  CG2   . VAL   C 2  189 ? -24.630 -12.092 26.442   1.00 44.37  ? 191 VAL   D CG2   1 
ATOM   8384  N  N     . HIS   C 2  190 ? -29.288 -12.090 25.929   1.00 51.29  ? 192 HIS   D N     1 
ATOM   8385  C  CA    . HIS   C 2  190 ? -30.499 -11.881 25.138   1.00 53.51  ? 192 HIS   D CA    1 
ATOM   8386  C  C     . HIS   C 2  190 ? -31.204 -10.594 25.533   1.00 55.20  ? 192 HIS   D C     1 
ATOM   8387  O  O     . HIS   C 2  190 ? -31.900 -9.989  24.712   1.00 60.15  ? 192 HIS   D O     1 
ATOM   8388  C  CB    . HIS   C 2  190 ? -31.429 -13.086 25.306   1.00 56.31  ? 192 HIS   D CB    1 
ATOM   8389  C  CG    . HIS   C 2  190 ? -32.823 -12.876 24.801   1.00 53.74  ? 192 HIS   D CG    1 
ATOM   8390  N  ND1   . HIS   C 2  190 ? -33.108 -12.610 23.480   1.00 57.66  ? 192 HIS   D ND1   1 
ATOM   8391  C  CD2   . HIS   C 2  190 ? -34.018 -12.943 25.436   1.00 56.27  ? 192 HIS   D CD2   1 
ATOM   8392  C  CE1   . HIS   C 2  190 ? -34.417 -12.499 23.328   1.00 62.01  ? 192 HIS   D CE1   1 
ATOM   8393  N  NE2   . HIS   C 2  190 ? -34.992 -12.696 24.501   1.00 42.81  ? 192 HIS   D NE2   1 
ATOM   8394  N  N     . GLN   C 2  191 ? -31.033 -10.154 26.780   1.00 47.62  ? 193 GLN   D N     1 
ATOM   8395  C  CA    . GLN   C 2  191 ? -31.481 -8.818  27.147   1.00 47.06  ? 193 GLN   D CA    1 
ATOM   8396  C  C     . GLN   C 2  191 ? -30.540 -7.755  26.580   1.00 51.14  ? 193 GLN   D C     1 
ATOM   8397  O  O     . GLN   C 2  191 ? -30.987 -6.705  26.103   1.00 45.39  ? 193 GLN   D O     1 
ATOM   8398  C  CB    . GLN   C 2  191 ? -31.586 -8.704  28.673   1.00 49.09  ? 193 GLN   D CB    1 
ATOM   8399  C  CG    . GLN   C 2  191 ? -32.741 -9.484  29.295   1.00 52.41  ? 193 GLN   D CG    1 
ATOM   8400  C  CD    . GLN   C 2  191 ? -34.111 -9.015  28.813   1.00 58.01  ? 193 GLN   D CD    1 
ATOM   8401  O  OE1   . GLN   C 2  191 ? -34.507 -7.867  29.045   1.00 62.60  ? 193 GLN   D OE1   1 
ATOM   8402  N  NE2   . GLN   C 2  191 ? -34.838 -9.901  28.135   1.00 53.66  ? 193 GLN   D NE2   1 
ATOM   8403  N  N     . LEU   C 2  192 ? -29.232 -8.022  26.607   1.00 52.04  ? 194 LEU   D N     1 
ATOM   8404  C  CA    . LEU   C 2  192 ? -28.254 -7.005  26.239   1.00 46.42  ? 194 LEU   D CA    1 
ATOM   8405  C  C     . LEU   C 2  192 ? -28.293 -6.708  24.743   1.00 49.45  ? 194 LEU   D C     1 
ATOM   8406  O  O     . LEU   C 2  192 ? -28.200 -5.543  24.329   1.00 42.43  ? 194 LEU   D O     1 
ATOM   8407  C  CB    . LEU   C 2  192 ? -26.863 -7.453  26.671   1.00 40.54  ? 194 LEU   D CB    1 
ATOM   8408  C  CG    . LEU   C 2  192 ? -26.577 -7.435  28.168   1.00 40.62  ? 194 LEU   D CG    1 
ATOM   8409  C  CD1   . LEU   C 2  192 ? -25.287 -8.179  28.444   1.00 49.33  ? 194 LEU   D CD1   1 
ATOM   8410  C  CD2   . LEU   C 2  192 ? -26.475 -6.010  28.673   1.00 41.67  ? 194 LEU   D CD2   1 
ATOM   8411  N  N     . VAL   C 2  193 ? -28.459 -7.741  23.921   1.00 41.14  ? 195 VAL   D N     1 
ATOM   8412  C  CA    . VAL   C 2  193 ? -28.504 -7.583  22.476   1.00 39.46  ? 195 VAL   D CA    1 
ATOM   8413  C  C     . VAL   C 2  193 ? -29.504 -6.501  22.096   1.00 47.78  ? 195 VAL   D C     1 
ATOM   8414  O  O     . VAL   C 2  193 ? -29.379 -5.890  21.031   1.00 47.59  ? 195 VAL   D O     1 
ATOM   8415  C  CB    . VAL   C 2  193 ? -28.859 -8.916  21.785   1.00 49.51  ? 195 VAL   D CB    1 
ATOM   8416  C  CG1   . VAL   C 2  193 ? -29.056 -8.726  20.256   1.00 50.91  ? 195 VAL   D CG1   1 
ATOM   8417  C  CG2   . VAL   C 2  193 ? -27.791 -9.937  22.060   1.00 49.01  ? 195 VAL   D CG2   1 
ATOM   8418  N  N     . GLU   C 2  194 ? -30.494 -6.248  22.961   1.00 42.84  ? 196 GLU   D N     1 
ATOM   8419  C  CA    . GLU   C 2  194 ? -31.661 -5.466  22.584   1.00 40.48  ? 196 GLU   D CA    1 
ATOM   8420  C  C     . GLU   C 2  194 ? -31.757 -4.117  23.268   1.00 43.18  ? 196 GLU   D C     1 
ATOM   8421  O  O     . GLU   C 2  194 ? -32.441 -3.234  22.745   1.00 48.33  ? 196 GLU   D O     1 
ATOM   8422  C  CB    . GLU   C 2  194 ? -32.954 -6.237  22.889   1.00 42.76  ? 196 GLU   D CB    1 
ATOM   8423  C  CG    . GLU   C 2  194 ? -32.937 -7.686  22.440   1.00 49.83  ? 196 GLU   D CG    1 
ATOM   8424  C  CD    . GLU   C 2  194 ? -33.233 -7.889  20.950   1.00 48.77  ? 196 GLU   D CD    1 
ATOM   8425  O  OE1   . GLU   C 2  194 ? -34.246 -7.365  20.441   1.00 48.70  ? 196 GLU   D OE1   1 
ATOM   8426  O  OE2   . GLU   C 2  194 ? -32.458 -8.607  20.289   1.00 51.75  ? 196 GLU   D OE2   1 
ATOM   8427  N  N     . ASN   C 2  195 ? -31.106 -3.925  24.409   1.00 42.65  ? 197 ASN   D N     1 
ATOM   8428  C  CA    . ASN   C 2  195 ? -31.385 -2.757  25.236   1.00 39.31  ? 197 ASN   D CA    1 
ATOM   8429  C  C     . ASN   C 2  195 ? -30.135 -2.048  25.746   1.00 46.56  ? 197 ASN   D C     1 
ATOM   8430  O  O     . ASN   C 2  195 ? -30.259 -1.122  26.561   1.00 45.84  ? 197 ASN   D O     1 
ATOM   8431  C  CB    . ASN   C 2  195 ? -32.267 -3.145  26.425   1.00 42.33  ? 197 ASN   D CB    1 
ATOM   8432  C  CG    . ASN   C 2  195 ? -33.664 -3.586  26.004   1.00 47.50  ? 197 ASN   D CG    1 
ATOM   8433  O  OD1   . ASN   C 2  195 ? -34.353 -2.908  25.227   1.00 51.52  ? 197 ASN   D OD1   1 
ATOM   8434  N  ND2   . ASN   C 2  195 ? -34.091 -4.727  26.522   1.00 42.20  ? 197 ASN   D ND2   1 
ATOM   8435  N  N     . THR   C 2  196 ? -28.940 -2.450  25.312   1.00 38.52  ? 198 THR   D N     1 
ATOM   8436  C  CA    . THR   C 2  196 ? -27.747 -1.658  25.558   1.00 38.69  ? 198 THR   D CA    1 
ATOM   8437  C  C     . THR   C 2  196 ? -27.206 -1.124  24.242   1.00 40.56  ? 198 THR   D C     1 
ATOM   8438  O  O     . THR   C 2  196 ? -27.422 -1.704  23.173   1.00 39.54  ? 198 THR   D O     1 
ATOM   8439  C  CB    . THR   C 2  196 ? -26.642 -2.448  26.279   1.00 39.67  ? 198 THR   D CB    1 
ATOM   8440  O  OG1   . THR   C 2  196 ? -26.327 -3.629  25.539   1.00 46.73  ? 198 THR   D OG1   1 
ATOM   8441  C  CG2   . THR   C 2  196 ? -27.071 -2.823  27.683   1.00 42.42  ? 198 THR   D CG2   1 
ATOM   8442  N  N     . ASP   C 2  197 ? -26.495 -0.006  24.345   1.00 42.30  ? 199 ASP   D N     1 
ATOM   8443  C  CA    . ASP   C 2  197 ? -25.829 0.640   23.226   1.00 32.62  ? 199 ASP   D CA    1 
ATOM   8444  C  C     . ASP   C 2  197 ? -24.420 0.114   23.009   1.00 41.74  ? 199 ASP   D C     1 
ATOM   8445  O  O     . ASP   C 2  197 ? -24.010 -0.093  21.861   1.00 46.10  ? 199 ASP   D O     1 
ATOM   8446  C  CB    . ASP   C 2  197 ? -25.798 2.143   23.473   1.00 32.20  ? 199 ASP   D CB    1 
ATOM   8447  C  CG    . ASP   C 2  197 ? -27.157 2.713   23.509   1.00 33.34  ? 199 ASP   D CG    1 
ATOM   8448  O  OD1   . ASP   C 2  197 ? -27.956 2.251   22.681   1.00 36.75  ? 199 ASP   D OD1   1 
ATOM   8449  O  OD2   . ASP   C 2  197 ? -27.448 3.569   24.367   1.00 37.14  ? 199 ASP   D OD2   1 
ATOM   8450  N  N     . GLU   C 2  198 ? -23.665 -0.095  24.089   1.00 43.52  ? 200 GLU   D N     1 
ATOM   8451  C  CA    . GLU   C 2  198 ? -22.270 -0.500  23.983   1.00 42.76  ? 200 GLU   D CA    1 
ATOM   8452  C  C     . GLU   C 2  198 ? -21.915 -1.330  25.203   1.00 44.64  ? 200 GLU   D C     1 
ATOM   8453  O  O     . GLU   C 2  198 ? -22.091 -0.870  26.335   1.00 47.82  ? 200 GLU   D O     1 
ATOM   8454  C  CB    . GLU   C 2  198 ? -21.359 0.719   23.859   1.00 40.87  ? 200 GLU   D CB    1 
ATOM   8455  C  CG    . GLU   C 2  198 ? -21.733 1.869   24.756   1.00 33.92  ? 200 GLU   D CG    1 
ATOM   8456  C  CD    . GLU   C 2  198 ? -21.066 3.144   24.321   1.00 38.06  ? 200 GLU   D CD    1 
ATOM   8457  O  OE1   . GLU   C 2  198 ? -20.756 3.278   23.132   1.00 44.59  ? 200 GLU   D OE1   1 
ATOM   8458  O  OE2   . GLU   C 2  198 ? -20.834 4.020   25.163   1.00 51.43  ? 200 GLU   D OE2   1 
ATOM   8459  N  N     . THR   C 2  199 ? -21.429 -2.551  24.970   1.00 46.75  ? 201 THR   D N     1 
ATOM   8460  C  CA    . THR   C 2  199 ? -21.204 -3.530  26.034   1.00 54.61  ? 201 THR   D CA    1 
ATOM   8461  C  C     . THR   C 2  199 ? -19.759 -4.007  25.971   1.00 45.70  ? 201 THR   D C     1 
ATOM   8462  O  O     . THR   C 2  199 ? -19.324 -4.549  24.951   1.00 39.53  ? 201 THR   D O     1 
ATOM   8463  C  CB    . THR   C 2  199 ? -22.183 -4.723  25.917   1.00 55.15  ? 201 THR   D CB    1 
ATOM   8464  O  OG1   . THR   C 2  199 ? -23.466 -4.378  26.471   1.00 47.02  ? 201 THR   D OG1   1 
ATOM   8465  C  CG2   . THR   C 2  199 ? -21.642 -5.984  26.617   1.00 46.02  ? 201 THR   D CG2   1 
ATOM   8466  N  N     . TYR   C 2  200 ? -19.020 -3.814  27.059   1.00 47.28  ? 202 TYR   D N     1 
ATOM   8467  C  CA    . TYR   C 2  200 ? -17.704 -4.435  27.198   1.00 48.09  ? 202 TYR   D CA    1 
ATOM   8468  C  C     . TYR   C 2  200 ? -17.858 -5.899  27.628   1.00 52.79  ? 202 TYR   D C     1 
ATOM   8469  O  O     . TYR   C 2  200 ? -18.274 -6.184  28.757   1.00 45.80  ? 202 TYR   D O     1 
ATOM   8470  C  CB    . TYR   C 2  200 ? -16.865 -3.645  28.194   1.00 37.49  ? 202 TYR   D CB    1 
ATOM   8471  C  CG    . TYR   C 2  200 ? -16.524 -2.260  27.706   1.00 38.81  ? 202 TYR   D CG    1 
ATOM   8472  C  CD1   . TYR   C 2  200 ? -15.554 -2.077  26.739   1.00 40.43  ? 202 TYR   D CD1   1 
ATOM   8473  C  CD2   . TYR   C 2  200 ? -17.168 -1.140  28.210   1.00 33.88  ? 202 TYR   D CD2   1 
ATOM   8474  C  CE1   . TYR   C 2  200 ? -15.235 -0.829  26.285   1.00 45.25  ? 202 TYR   D CE1   1 
ATOM   8475  C  CE2   . TYR   C 2  200 ? -16.859 0.108   27.770   1.00 27.63  ? 202 TYR   D CE2   1 
ATOM   8476  C  CZ    . TYR   C 2  200 ? -15.886 0.271   26.799   1.00 45.25  ? 202 TYR   D CZ    1 
ATOM   8477  O  OH    . TYR   C 2  200 ? -15.541 1.529   26.325   1.00 45.05  ? 202 TYR   D OH    1 
ATOM   8478  N  N     . CYS   C 2  201 ? -17.542 -6.833  26.727   1.00 42.65  ? 203 CYS   D N     1 
ATOM   8479  C  CA    . CYS   C 2  201 ? -17.411 -8.242  27.100   1.00 46.54  ? 203 CYS   D CA    1 
ATOM   8480  C  C     . CYS   C 2  201 ? -16.184 -8.421  27.990   1.00 51.68  ? 203 CYS   D C     1 
ATOM   8481  O  O     . CYS   C 2  201 ? -15.052 -8.444  27.512   1.00 48.34  ? 203 CYS   D O     1 
ATOM   8482  C  CB    . CYS   C 2  201 ? -17.297 -9.119  25.864   1.00 39.65  ? 203 CYS   D CB    1 
ATOM   8483  S  SG    . CYS   C 2  201 ? -18.673 -8.935  24.743   1.00 73.30  ? 203 CYS   D SG    1 
ATOM   8484  N  N     . ILE   C 2  202 ? -16.395 -8.561  29.293   1.00 53.09  ? 204 ILE   D N     1 
ATOM   8485  C  CA    . ILE   C 2  202 ? -15.321 -8.869  30.230   1.00 57.25  ? 204 ILE   D CA    1 
ATOM   8486  C  C     . ILE   C 2  202 ? -15.433 -10.358 30.548   1.00 58.11  ? 204 ILE   D C     1 
ATOM   8487  O  O     . ILE   C 2  202 ? -16.319 -10.777 31.301   1.00 53.53  ? 204 ILE   D O     1 
ATOM   8488  C  CB    . ILE   C 2  202 ? -15.401 -7.990  31.478   1.00 49.33  ? 204 ILE   D CB    1 
ATOM   8489  C  CG1   . ILE   C 2  202 ? -14.985 -6.563  31.110   1.00 44.44  ? 204 ILE   D CG1   1 
ATOM   8490  C  CG2   . ILE   C 2  202 ? -14.542 -8.563  32.578   1.00 46.44  ? 204 ILE   D CG2   1 
ATOM   8491  C  CD1   . ILE   C 2  202 ? -15.311 -5.541  32.151   1.00 47.11  ? 204 ILE   D CD1   1 
ATOM   8492  N  N     . ASP   C 2  203 ? -14.548 -11.168 29.946   1.00 56.93  ? 205 ASP   D N     1 
ATOM   8493  C  CA    . ASP   C 2  203 ? -14.661 -12.628 29.973   1.00 60.51  ? 205 ASP   D CA    1 
ATOM   8494  C  C     . ASP   C 2  203 ? -13.796 -13.201 31.093   1.00 62.85  ? 205 ASP   D C     1 
ATOM   8495  O  O     . ASP   C 2  203 ? -12.582 -12.965 31.137   1.00 59.29  ? 205 ASP   D O     1 
ATOM   8496  C  CB    . ASP   C 2  203 ? -14.273 -13.258 28.630   1.00 53.14  ? 205 ASP   D CB    1 
ATOM   8497  C  CG    . ASP   C 2  203 ? -14.805 -14.692 28.477   1.00 58.15  ? 205 ASP   D CG    1 
ATOM   8498  O  OD1   . ASP   C 2  203 ? -15.159 -15.303 29.512   1.00 63.08  ? 205 ASP   D OD1   1 
ATOM   8499  O  OD2   . ASP   C 2  203 ? -14.878 -15.211 27.335   1.00 50.58  ? 205 ASP   D OD2   1 
ATOM   8500  N  N     . ASN   C 2  204 ? -14.426 -13.965 31.987   1.00 63.04  ? 206 ASN   D N     1 
ATOM   8501  C  CA    . ASN   C 2  204 ? -13.694 -14.528 33.117   1.00 65.56  ? 206 ASN   D CA    1 
ATOM   8502  C  C     . ASN   C 2  204 ? -12.687 -15.575 32.660   1.00 65.55  ? 206 ASN   D C     1 
ATOM   8503  O  O     . ASN   C 2  204 ? -11.582 -15.663 33.212   1.00 56.94  ? 206 ASN   D O     1 
ATOM   8504  C  CB    . ASN   C 2  204 ? -14.670 -15.116 34.128   1.00 57.43  ? 206 ASN   D CB    1 
ATOM   8505  C  CG    . ASN   C 2  204 ? -14.745 -14.298 35.380   1.00 52.84  ? 206 ASN   D CG    1 
ATOM   8506  O  OD1   . ASN   C 2  204 ? -14.180 -13.214 35.456   1.00 50.61  ? 206 ASN   D OD1   1 
ATOM   8507  N  ND2   . ASN   C 2  204 ? -15.437 -14.814 36.379   1.00 67.62  ? 206 ASN   D ND2   1 
ATOM   8508  N  N     . GLU   C 2  205 ? -13.050 -16.378 31.652   1.00 64.32  ? 207 GLU   D N     1 
ATOM   8509  C  CA    . GLU   C 2  205 ? -12.067 -17.274 31.055   1.00 66.69  ? 207 GLU   D CA    1 
ATOM   8510  C  C     . GLU   C 2  205 ? -10.844 -16.498 30.599   1.00 66.34  ? 207 GLU   D C     1 
ATOM   8511  O  O     . GLU   C 2  205 ? -9.705  -16.945 30.779   1.00 66.60  ? 207 GLU   D O     1 
ATOM   8512  C  CB    . GLU   C 2  205 ? -12.668 -18.034 29.881   1.00 55.25  ? 207 GLU   D CB    1 
ATOM   8513  C  CG    . GLU   C 2  205 ? -11.627 -18.770 29.066   1.00 61.78  ? 207 GLU   D CG    1 
ATOM   8514  C  CD    . GLU   C 2  205 ? -11.925 -20.247 28.925   1.00 65.32  ? 207 GLU   D CD    1 
ATOM   8515  O  OE1   . GLU   C 2  205 ? -13.078 -20.642 29.215   1.00 57.85  ? 207 GLU   D OE1   1 
ATOM   8516  O  OE2   . GLU   C 2  205 ? -11.002 -21.009 28.534   1.00 62.22  ? 207 GLU   D OE2   1 
ATOM   8517  N  N     . ALA   C 2  206 ? -11.060 -15.321 30.023   1.00 58.06  ? 208 ALA   D N     1 
ATOM   8518  C  CA    . ALA   C 2  206 ? -9.926  -14.536 29.570   1.00 59.03  ? 208 ALA   D CA    1 
ATOM   8519  C  C     . ALA   C 2  206 ? -9.161  -13.939 30.747   1.00 61.26  ? 208 ALA   D C     1 
ATOM   8520  O  O     . ALA   C 2  206 ? -7.928  -13.856 30.708   1.00 69.48  ? 208 ALA   D O     1 
ATOM   8521  C  CB    . ALA   C 2  206 ? -10.404 -13.455 28.599   1.00 58.01  ? 208 ALA   D CB    1 
ATOM   8522  N  N     . LEU   C 2  207 ? -9.867  -13.505 31.800   1.00 64.47  ? 209 LEU   D N     1 
ATOM   8523  C  CA    . LEU   C 2  207 ? -9.179  -12.967 32.975   1.00 66.27  ? 209 LEU   D CA    1 
ATOM   8524  C  C     . LEU   C 2  207 ? -8.250  -14.004 33.584   1.00 70.49  ? 209 LEU   D C     1 
ATOM   8525  O  O     . LEU   C 2  207 ? -7.134  -13.685 34.014   1.00 68.66  ? 209 LEU   D O     1 
ATOM   8526  C  CB    . LEU   C 2  207 ? -10.192 -12.518 34.023   1.00 63.93  ? 209 LEU   D CB    1 
ATOM   8527  C  CG    . LEU   C 2  207 ? -10.820 -11.146 33.867   1.00 66.75  ? 209 LEU   D CG    1 
ATOM   8528  C  CD1   . LEU   C 2  207 ? -9.797  -10.059 34.189   1.00 63.45  ? 209 LEU   D CD1   1 
ATOM   8529  C  CD2   . LEU   C 2  207 ? -11.332 -11.031 32.456   1.00 56.74  ? 209 LEU   D CD2   1 
ATOM   8530  N  N     . TYR   C 2  208 ? -8.713  -15.251 33.633   1.00 69.25  ? 210 TYR   D N     1 
ATOM   8531  C  CA    . TYR   C 2  208 ? -7.986  -16.346 34.261   1.00 72.38  ? 210 TYR   D CA    1 
ATOM   8532  C  C     . TYR   C 2  208 ? -6.764  -16.740 33.438   1.00 76.92  ? 210 TYR   D C     1 
ATOM   8533  O  O     . TYR   C 2  208 ? -5.624  -16.654 33.915   1.00 71.40  ? 210 TYR   D O     1 
ATOM   8534  C  CB    . TYR   C 2  208 ? -8.956  -17.517 34.428   1.00 75.68  ? 210 TYR   D CB    1 
ATOM   8535  C  CG    . TYR   C 2  208 ? -8.390  -18.800 34.960   1.00 83.50  ? 210 TYR   D CG    1 
ATOM   8536  C  CD1   . TYR   C 2  208 ? -8.311  -19.031 36.331   1.00 84.42  ? 210 TYR   D CD1   1 
ATOM   8537  C  CD2   . TYR   C 2  208 ? -7.978  -19.806 34.094   1.00 78.63  ? 210 TYR   D CD2   1 
ATOM   8538  C  CE1   . TYR   C 2  208 ? -7.812  -20.221 36.826   1.00 81.85  ? 210 TYR   D CE1   1 
ATOM   8539  C  CE2   . TYR   C 2  208 ? -7.477  -20.999 34.577   1.00 82.42  ? 210 TYR   D CE2   1 
ATOM   8540  C  CZ    . TYR   C 2  208 ? -7.398  -21.202 35.942   1.00 86.71  ? 210 TYR   D CZ    1 
ATOM   8541  O  OH    . TYR   C 2  208 ? -6.901  -22.391 36.419   1.00 89.83  ? 210 TYR   D OH    1 
ATOM   8542  N  N     . ASP   C 2  209 ? -6.989  -17.154 32.180   1.00 75.30  ? 211 ASP   D N     1 
ATOM   8543  C  CA    . ASP   C 2  209 ? -5.904  -17.600 31.307   1.00 64.93  ? 211 ASP   D CA    1 
ATOM   8544  C  C     . ASP   C 2  209 ? -4.733  -16.623 31.311   1.00 66.11  ? 211 ASP   D C     1 
ATOM   8545  O  O     . ASP   C 2  209 ? -3.570  -17.035 31.239   1.00 68.52  ? 211 ASP   D O     1 
ATOM   8546  C  CB    . ASP   C 2  209 ? -6.422  -17.801 29.882   1.00 58.35  ? 211 ASP   D CB    1 
ATOM   8547  C  CG    . ASP   C 2  209 ? -7.328  -19.032 29.738   1.00 71.61  ? 211 ASP   D CG    1 
ATOM   8548  O  OD1   . ASP   C 2  209 ? -7.616  -19.703 30.751   1.00 72.29  ? 211 ASP   D OD1   1 
ATOM   8549  O  OD2   . ASP   C 2  209 ? -7.755  -19.335 28.598   1.00 73.06  ? 211 ASP   D OD2   1 
ATOM   8550  N  N     . ILE   C 2  210 ? -5.014  -15.325 31.387   1.00 64.40  ? 212 ILE   D N     1 
ATOM   8551  C  CA    . ILE   C 2  210 ? -3.928  -14.356 31.485   1.00 72.30  ? 212 ILE   D CA    1 
ATOM   8552  C  C     . ILE   C 2  210 ? -3.286  -14.434 32.860   1.00 72.45  ? 212 ILE   D C     1 
ATOM   8553  O  O     . ILE   C 2  210 ? -2.059  -14.502 32.990   1.00 75.11  ? 212 ILE   D O     1 
ATOM   8554  C  CB    . ILE   C 2  210 ? -4.435  -12.934 31.177   1.00 72.03  ? 212 ILE   D CB    1 
ATOM   8555  C  CG1   . ILE   C 2  210 ? -5.050  -12.879 29.771   1.00 68.42  ? 212 ILE   D CG1   1 
ATOM   8556  C  CG2   . ILE   C 2  210 ? -3.300  -11.915 31.331   1.00 49.50  ? 212 ILE   D CG2   1 
ATOM   8557  C  CD1   . ILE   C 2  210 ? -5.734  -11.553 29.445   1.00 61.36  ? 212 ILE   D CD1   1 
ATOM   8558  N  N     . CYS   C 2  211 ? -4.113  -14.424 33.908   1.00 80.89  ? 213 CYS   D N     1 
ATOM   8559  C  CA    . CYS   C 2  211 ? -3.616  -14.587 35.270   1.00 75.45  ? 213 CYS   D CA    1 
ATOM   8560  C  C     . CYS   C 2  211 ? -2.802  -15.865 35.404   1.00 74.74  ? 213 CYS   D C     1 
ATOM   8561  O  O     . CYS   C 2  211 ? -1.658  -15.846 35.872   1.00 69.06  ? 213 CYS   D O     1 
ATOM   8562  C  CB    . CYS   C 2  211 ? -4.793  -14.605 36.247   1.00 67.67  ? 213 CYS   D CB    1 
ATOM   8563  S  SG    . CYS   C 2  211 ? -5.381  -12.988 36.747   1.00 76.63  ? 213 CYS   D SG    1 
ATOM   8564  N  N     . PHE   C 2  212 ? -3.390  -16.989 34.993   1.00 71.79  ? 214 PHE   D N     1 
ATOM   8565  C  CA    . PHE   C 2  212 ? -2.781  -18.304 35.117   1.00 74.94  ? 214 PHE   D CA    1 
ATOM   8566  C  C     . PHE   C 2  212 ? -1.432  -18.328 34.416   1.00 83.71  ? 214 PHE   D C     1 
ATOM   8567  O  O     . PHE   C 2  212 ? -0.387  -18.147 35.056   1.00 81.51  ? 214 PHE   D O     1 
ATOM   8568  C  CB    . PHE   C 2  212 ? -3.708  -19.370 34.531   1.00 77.37  ? 214 PHE   D CB    1 
ATOM   8569  C  CG    . PHE   C 2  212 ? -3.235  -20.773 34.759   1.00 90.88  ? 214 PHE   D CG    1 
ATOM   8570  C  CD1   . PHE   C 2  212 ? -2.368  -21.064 35.803   1.00 84.65  ? 214 PHE   D CD1   1 
ATOM   8571  C  CD2   . PHE   C 2  212 ? -3.649  -21.804 33.923   1.00 91.85  ? 214 PHE   D CD2   1 
ATOM   8572  C  CE1   . PHE   C 2  212 ? -1.928  -22.358 36.015   1.00 97.88  ? 214 PHE   D CE1   1 
ATOM   8573  C  CE2   . PHE   C 2  212 ? -3.214  -23.100 34.129   1.00 93.35  ? 214 PHE   D CE2   1 
ATOM   8574  C  CZ    . PHE   C 2  212 ? -2.351  -23.380 35.177   1.00 100.94 ? 214 PHE   D CZ    1 
ATOM   8575  N  N     . ARG   C 2  213 ? -1.454  -18.564 33.102   1.00 84.35  ? 215 ARG   D N     1 
ATOM   8576  C  CA    . ARG   C 2  213 ? -0.278  -18.380 32.263   1.00 74.42  ? 215 ARG   D CA    1 
ATOM   8577  C  C     . ARG   C 2  213 ? 0.187   -16.932 32.350   1.00 80.65  ? 215 ARG   D C     1 
ATOM   8578  O  O     . ARG   C 2  213 ? 0.362   -16.394 33.451   1.00 82.88  ? 215 ARG   D O     1 
ATOM   8579  C  CB    . ARG   C 2  213 ? -0.587  -18.763 30.818   1.00 65.31  ? 215 ARG   D CB    1 
ATOM   8580  C  CG    . ARG   C 2  213 ? -1.385  -20.043 30.707   1.00 72.54  ? 215 ARG   D CG    1 
ATOM   8581  C  CD    . ARG   C 2  213 ? -1.539  -20.484 29.274   1.00 64.64  ? 215 ARG   D CD    1 
ATOM   8582  N  NE    . ARG   C 2  213 ? -2.925  -20.809 28.964   1.00 66.19  ? 215 ARG   D NE    1 
ATOM   8583  C  CZ    . ARG   C 2  213 ? -3.361  -21.163 27.762   1.00 74.28  ? 215 ARG   D CZ    1 
ATOM   8584  N  NH1   . ARG   C 2  213 ? -2.537  -21.256 26.729   1.00 60.21  ? 215 ARG   D NH1   1 
ATOM   8585  N  NH2   . ARG   C 2  213 ? -4.657  -21.431 27.592   1.00 74.80  ? 215 ARG   D NH2   1 
ATOM   8586  N  N     . THR   C 2  214 ? 0.372   -16.299 31.196   1.00 77.69  ? 216 THR   D N     1 
ATOM   8587  C  CA    . THR   C 2  214 ? 0.832   -14.918 31.101   1.00 83.76  ? 216 THR   D CA    1 
ATOM   8588  C  C     . THR   C 2  214 ? 1.294   -14.331 32.433   1.00 78.16  ? 216 THR   D C     1 
ATOM   8589  O  O     . THR   C 2  214 ? 2.488   -14.363 32.741   1.00 78.61  ? 216 THR   D O     1 
ATOM   8590  C  CB    . THR   C 2  214 ? -0.270  -14.054 30.500   1.00 81.40  ? 216 THR   D CB    1 
ATOM   8591  O  OG1   . THR   C 2  214 ? -0.687  -14.626 29.251   1.00 71.52  ? 216 THR   D OG1   1 
ATOM   8592  C  CG2   . THR   C 2  214 ? 0.243   -12.632 30.287   1.00 69.59  ? 216 THR   D CG2   1 
ATOM   8593  N  N     . LEU   C 2  215 ? 0.362   -13.824 33.247   1.00 80.77  ? 217 LEU   D N     1 
ATOM   8594  C  CA    . LEU   C 2  215 ? 0.758   -13.131 34.471   1.00 87.59  ? 217 LEU   D CA    1 
ATOM   8595  C  C     . LEU   C 2  215 ? 1.383   -14.058 35.519   1.00 95.00  ? 217 LEU   D C     1 
ATOM   8596  O  O     . LEU   C 2  215 ? 1.887   -13.559 36.537   1.00 94.88  ? 217 LEU   D O     1 
ATOM   8597  C  CB    . LEU   C 2  215 ? -0.436  -12.378 35.068   1.00 80.87  ? 217 LEU   D CB    1 
ATOM   8598  C  CG    . LEU   C 2  215 ? -0.227  -10.860 35.188   1.00 79.34  ? 217 LEU   D CG    1 
ATOM   8599  C  CD1   . LEU   C 2  215 ? -1.159  -10.245 36.227   1.00 70.91  ? 217 LEU   D CD1   1 
ATOM   8600  C  CD2   . LEU   C 2  215 ? 1.231   -10.523 35.493   1.00 76.89  ? 217 LEU   D CD2   1 
ATOM   8601  N  N     . LYS   C 2  216 ? 1.366   -15.378 35.310   1.00 84.79  ? 218 LYS   D N     1 
ATOM   8602  C  CA    . LYS   C 2  216 ? 2.289   -16.251 36.032   1.00 87.89  ? 218 LYS   D CA    1 
ATOM   8603  C  C     . LYS   C 2  216 ? 1.804   -16.557 37.442   1.00 89.91  ? 218 LYS   D C     1 
ATOM   8604  O  O     . LYS   C 2  216 ? 2.559   -16.410 38.410   1.00 90.50  ? 218 LYS   D O     1 
ATOM   8605  C  CB    . LYS   C 2  216 ? 3.679   -15.599 36.080   1.00 95.85  ? 218 LYS   D CB    1 
ATOM   8606  C  CG    . LYS   C 2  216 ? 4.830   -16.501 36.519   1.00 95.02  ? 218 LYS   D CG    1 
ATOM   8607  C  CD    . LYS   C 2  216 ? 6.145   -15.716 36.555   1.00 82.79  ? 218 LYS   D CD    1 
ATOM   8608  C  CE    . LYS   C 2  216 ? 7.352   -16.634 36.664   1.00 85.11  ? 218 LYS   D CE    1 
ATOM   8609  N  NZ    . LYS   C 2  216 ? 8.619   -15.922 36.352   1.00 86.89  ? 218 LYS   D NZ    1 
ATOM   8610  N  N     . LEU   C 2  217 ? 0.554   -16.989 37.573   1.00 90.59  ? 219 LEU   D N     1 
ATOM   8611  C  CA    . LEU   C 2  217 ? -0.036  -17.205 38.884   1.00 80.15  ? 219 LEU   D CA    1 
ATOM   8612  C  C     . LEU   C 2  217 ? -0.823  -18.498 38.886   1.00 79.93  ? 219 LEU   D C     1 
ATOM   8613  O  O     . LEU   C 2  217 ? -1.639  -18.735 37.994   1.00 80.63  ? 219 LEU   D O     1 
ATOM   8614  C  CB    . LEU   C 2  217 ? -0.959  -16.053 39.287   1.00 83.90  ? 219 LEU   D CB    1 
ATOM   8615  C  CG    . LEU   C 2  217 ? -0.378  -14.644 39.273   1.00 80.66  ? 219 LEU   D CG    1 
ATOM   8616  C  CD1   . LEU   C 2  217 ? -1.422  -13.677 39.814   1.00 81.07  ? 219 LEU   D CD1   1 
ATOM   8617  C  CD2   . LEU   C 2  217 ? 0.930   -14.571 40.066   1.00 75.22  ? 219 LEU   D CD2   1 
ATOM   8618  N  N     . THR   C 2  218 ? -0.580  -19.322 39.890   1.00 88.46  ? 220 THR   D N     1 
ATOM   8619  C  CA    . THR   C 2  218 ? -1.439  -20.456 40.163   1.00 88.04  ? 220 THR   D CA    1 
ATOM   8620  C  C     . THR   C 2  218 ? -2.513  -20.028 41.148   1.00 91.73  ? 220 THR   D C     1 
ATOM   8621  O  O     . THR   C 2  218 ? -2.298  -19.127 41.966   1.00 97.56  ? 220 THR   D O     1 
ATOM   8622  C  CB    . THR   C 2  218 ? -0.630  -21.619 40.730   1.00 93.14  ? 220 THR   D CB    1 
ATOM   8623  O  OG1   . THR   C 2  218 ? 0.414   -21.100 41.566   1.00 80.19  ? 220 THR   D OG1   1 
ATOM   8624  C  CG2   . THR   C 2  218 ? -0.028  -22.443 39.601   1.00 96.93  ? 220 THR   D CG2   1 
ATOM   8625  N  N     . THR   C 2  219 ? -3.679  -20.682 41.058   1.00 81.71  ? 221 THR   D N     1 
ATOM   8626  C  CA    . THR   C 2  219 ? -4.826  -20.387 41.914   1.00 87.32  ? 221 THR   D CA    1 
ATOM   8627  C  C     . THR   C 2  219 ? -5.051  -18.874 41.968   1.00 88.28  ? 221 THR   D C     1 
ATOM   8628  O  O     . THR   C 2  219 ? -4.812  -18.236 43.006   1.00 77.86  ? 221 THR   D O     1 
ATOM   8629  C  CB    . THR   C 2  219 ? -4.637  -20.982 43.323   1.00 78.92  ? 221 THR   D CB    1 
ATOM   8630  O  OG1   . THR   C 2  219 ? -3.533  -20.356 43.989   1.00 68.92  ? 221 THR   D OG1   1 
ATOM   8631  C  CG2   . THR   C 2  219 ? -4.380  -22.490 43.251   1.00 54.72  ? 221 THR   D CG2   1 
ATOM   8632  N  N     . PRO   C 2  220 ? -5.500  -18.267 40.866   1.00 86.40  ? 222 PRO   D N     1 
ATOM   8633  C  CA    . PRO   C 2  220 ? -5.698  -16.812 40.853   1.00 84.30  ? 222 PRO   D CA    1 
ATOM   8634  C  C     . PRO   C 2  220 ? -6.884  -16.397 41.714   1.00 79.52  ? 222 PRO   D C     1 
ATOM   8635  O  O     . PRO   C 2  220 ? -7.905  -17.088 41.768   1.00 70.21  ? 222 PRO   D O     1 
ATOM   8636  C  CB    . PRO   C 2  220 ? -5.952  -16.509 39.373   1.00 77.41  ? 222 PRO   D CB    1 
ATOM   8637  C  CG    . PRO   C 2  220 ? -6.527  -17.793 38.827   1.00 69.60  ? 222 PRO   D CG    1 
ATOM   8638  C  CD    . PRO   C 2  220 ? -5.838  -18.890 39.572   1.00 77.52  ? 222 PRO   D CD    1 
ATOM   8639  N  N     . THR   C 2  221 ? -6.743  -15.246 42.376   1.00 72.54  ? 223 THR   D N     1 
ATOM   8640  C  CA    . THR   C 2  221 ? -7.777  -14.710 43.253   1.00 62.14  ? 223 THR   D CA    1 
ATOM   8641  C  C     . THR   C 2  221 ? -8.678  -13.724 42.508   1.00 76.32  ? 223 THR   D C     1 
ATOM   8642  O  O     . THR   C 2  221 ? -8.265  -13.093 41.528   1.00 71.18  ? 223 THR   D O     1 
ATOM   8643  C  CB    . THR   C 2  221 ? -7.149  -14.015 44.466   1.00 68.73  ? 223 THR   D CB    1 
ATOM   8644  O  OG1   . THR   C 2  221 ? -8.159  -13.300 45.194   1.00 77.93  ? 223 THR   D OG1   1 
ATOM   8645  C  CG2   . THR   C 2  221 ? -6.052  -13.033 44.036   1.00 66.33  ? 223 THR   D CG2   1 
ATOM   8646  N  N     . TYR   C 2  222 ? -9.922  -13.589 42.994   1.00 73.94  ? 224 TYR   D N     1 
ATOM   8647  C  CA    . TYR   C 2  222 ? -10.841 -12.603 42.429   1.00 60.23  ? 224 TYR   D CA    1 
ATOM   8648  C  C     . TYR   C 2  222 ? -10.213 -11.221 42.402   1.00 64.18  ? 224 TYR   D C     1 
ATOM   8649  O  O     . TYR   C 2  222 ? -10.214 -10.545 41.368   1.00 65.39  ? 224 TYR   D O     1 
ATOM   8650  C  CB    . TYR   C 2  222 ? -12.152 -12.564 43.214   1.00 60.32  ? 224 TYR   D CB    1 
ATOM   8651  C  CG    . TYR   C 2  222 ? -13.185 -13.511 42.663   1.00 64.33  ? 224 TYR   D CG    1 
ATOM   8652  C  CD1   . TYR   C 2  222 ? -13.609 -13.415 41.344   1.00 55.36  ? 224 TYR   D CD1   1 
ATOM   8653  C  CD2   . TYR   C 2  222 ? -13.727 -14.513 43.453   1.00 58.74  ? 224 TYR   D CD2   1 
ATOM   8654  C  CE1   . TYR   C 2  222 ? -14.546 -14.297 40.828   1.00 60.81  ? 224 TYR   D CE1   1 
ATOM   8655  C  CE2   . TYR   C 2  222 ? -14.665 -15.391 42.948   1.00 54.78  ? 224 TYR   D CE2   1 
ATOM   8656  C  CZ    . TYR   C 2  222 ? -15.073 -15.282 41.643   1.00 59.31  ? 224 TYR   D CZ    1 
ATOM   8657  O  OH    . TYR   C 2  222 ? -16.007 -16.165 41.154   1.00 62.95  ? 224 TYR   D OH    1 
ATOM   8658  N  N     . GLY   C 2  223 ? -9.684  -10.777 43.539   1.00 66.04  ? 225 GLY   D N     1 
ATOM   8659  C  CA    . GLY   C 2  223 ? -8.963  -9.520  43.550   1.00 66.44  ? 225 GLY   D CA    1 
ATOM   8660  C  C     . GLY   C 2  223 ? -7.953  -9.418  42.426   1.00 73.41  ? 225 GLY   D C     1 
ATOM   8661  O  O     . GLY   C 2  223 ? -7.672  -8.318  41.936   1.00 75.72  ? 225 GLY   D O     1 
ATOM   8662  N  N     . ASP   C 2  224 ? -7.400  -10.558 41.991   1.00 65.57  ? 226 ASP   D N     1 
ATOM   8663  C  CA    . ASP   C 2  224 ? -6.430  -10.544 40.901   1.00 67.15  ? 226 ASP   D CA    1 
ATOM   8664  C  C     . ASP   C 2  224 ? -7.115  -10.558 39.535   1.00 74.74  ? 226 ASP   D C     1 
ATOM   8665  O  O     . ASP   C 2  224 ? -6.714  -9.801  38.638   1.00 70.86  ? 226 ASP   D O     1 
ATOM   8666  C  CB    . ASP   C 2  224 ? -5.457  -11.717 41.043   1.00 74.58  ? 226 ASP   D CB    1 
ATOM   8667  C  CG    . ASP   C 2  224 ? -4.288  -11.402 41.971   1.00 73.32  ? 226 ASP   D CG    1 
ATOM   8668  O  OD1   . ASP   C 2  224 ? -4.226  -10.270 42.515   1.00 73.73  ? 226 ASP   D OD1   1 
ATOM   8669  O  OD2   . ASP   C 2  224 ? -3.429  -12.293 42.153   1.00 72.76  ? 226 ASP   D OD2   1 
ATOM   8670  N  N     . LEU   C 2  225 ? -8.141  -11.404 39.351   1.00 66.39  ? 227 LEU   D N     1 
ATOM   8671  C  CA    . LEU   C 2  225 ? -9.011  -11.255 38.186   1.00 58.54  ? 227 LEU   D CA    1 
ATOM   8672  C  C     . LEU   C 2  225 ? -9.544  -9.836  38.087   1.00 66.02  ? 227 LEU   D C     1 
ATOM   8673  O  O     . LEU   C 2  225 ? -9.716  -9.300  36.984   1.00 66.52  ? 227 LEU   D O     1 
ATOM   8674  C  CB    . LEU   C 2  225 ? -10.181 -12.231 38.234   1.00 55.33  ? 227 LEU   D CB    1 
ATOM   8675  C  CG    . LEU   C 2  225 ? -9.900  -13.703 37.954   1.00 66.34  ? 227 LEU   D CG    1 
ATOM   8676  C  CD1   . LEU   C 2  225 ? -11.139 -14.417 37.373   1.00 57.12  ? 227 LEU   D CD1   1 
ATOM   8677  C  CD2   . LEU   C 2  225 ? -8.677  -13.866 37.056   1.00 66.30  ? 227 LEU   D CD2   1 
ATOM   8678  N  N     . ASN   C 2  226 ? -9.810  -9.209  39.236   1.00 62.02  ? 228 ASN   D N     1 
ATOM   8679  C  CA    . ASN   C 2  226 ? -10.238 -7.818  39.264   1.00 63.67  ? 228 ASN   D CA    1 
ATOM   8680  C  C     . ASN   C 2  226 ? -9.082  -6.845  39.073   1.00 62.57  ? 228 ASN   D C     1 
ATOM   8681  O  O     . ASN   C 2  226 ? -9.320  -5.684  38.723   1.00 64.20  ? 228 ASN   D O     1 
ATOM   8682  C  CB    . ASN   C 2  226 ? -10.975 -7.519  40.577   1.00 60.29  ? 228 ASN   D CB    1 
ATOM   8683  C  CG    . ASN   C 2  226 ? -12.330 -8.231  40.666   1.00 58.95  ? 228 ASN   D CG    1 
ATOM   8684  O  OD1   . ASN   C 2  226 ? -12.813 -8.815  39.695   1.00 57.22  ? 228 ASN   D OD1   1 
ATOM   8685  N  ND2   . ASN   C 2  226 ? -12.948 -8.172  41.833   1.00 63.52  ? 228 ASN   D ND2   1 
ATOM   8686  N  N     . HIS   C 2  227 ? -7.841  -7.273  39.312   1.00 66.98  ? 229 HIS   D N     1 
ATOM   8687  C  CA    . HIS   C 2  227 ? -6.712  -6.416  38.972   1.00 64.70  ? 229 HIS   D CA    1 
ATOM   8688  C  C     . HIS   C 2  227 ? -6.759  -6.055  37.501   1.00 63.12  ? 229 HIS   D C     1 
ATOM   8689  O  O     . HIS   C 2  227 ? -6.482  -4.910  37.111   1.00 51.19  ? 229 HIS   D O     1 
ATOM   8690  C  CB    . HIS   C 2  227 ? -5.393  -7.114  39.286   1.00 60.84  ? 229 HIS   D CB    1 
ATOM   8691  C  CG    . HIS   C 2  227 ? -4.198  -6.392  38.744   1.00 68.93  ? 229 HIS   D CG    1 
ATOM   8692  N  ND1   . HIS   C 2  227 ? -3.919  -5.077  39.058   1.00 62.76  ? 229 HIS   D ND1   1 
ATOM   8693  C  CD2   . HIS   C 2  227 ? -3.220  -6.794  37.896   1.00 68.70  ? 229 HIS   D CD2   1 
ATOM   8694  C  CE1   . HIS   C 2  227 ? -2.814  -4.705  38.434   1.00 69.96  ? 229 HIS   D CE1   1 
ATOM   8695  N  NE2   . HIS   C 2  227 ? -2.368  -5.728  37.725   1.00 67.24  ? 229 HIS   D NE2   1 
ATOM   8696  N  N     . LEU   C 2  228 ? -7.112  -7.036  36.673   1.00 59.80  ? 230 LEU   D N     1 
ATOM   8697  C  CA    . LEU   C 2  228 ? -7.231  -6.839  35.243   1.00 62.02  ? 230 LEU   D CA    1 
ATOM   8698  C  C     . LEU   C 2  228 ? -8.481  -6.047  34.880   1.00 57.98  ? 230 LEU   D C     1 
ATOM   8699  O  O     . LEU   C 2  228 ? -8.524  -5.438  33.808   1.00 54.48  ? 230 LEU   D O     1 
ATOM   8700  C  CB    . LEU   C 2  228 ? -7.226  -8.206  34.544   1.00 61.33  ? 230 LEU   D CB    1 
ATOM   8701  C  CG    . LEU   C 2  228 ? -6.035  -9.122  34.864   1.00 53.77  ? 230 LEU   D CG    1 
ATOM   8702  C  CD1   . LEU   C 2  228 ? -6.060  -10.408 34.037   1.00 51.81  ? 230 LEU   D CD1   1 
ATOM   8703  C  CD2   . LEU   C 2  228 ? -4.697  -8.368  34.701   1.00 52.82  ? 230 LEU   D CD2   1 
ATOM   8704  N  N     . VAL   C 2  229 ? -9.495  -6.028  35.741   1.00 57.07  ? 231 VAL   D N     1 
ATOM   8705  C  CA    . VAL   C 2  229 ? -10.723 -5.347  35.353   1.00 53.46  ? 231 VAL   D CA    1 
ATOM   8706  C  C     . VAL   C 2  229 ? -10.624 -3.854  35.633   1.00 47.84  ? 231 VAL   D C     1 
ATOM   8707  O  O     . VAL   C 2  229 ? -11.144 -3.038  34.872   1.00 52.27  ? 231 VAL   D O     1 
ATOM   8708  C  CB    . VAL   C 2  229 ? -11.941 -5.990  36.041   1.00 53.20  ? 231 VAL   D CB    1 
ATOM   8709  C  CG1   . VAL   C 2  229 ? -13.228 -5.314  35.586   1.00 50.79  ? 231 VAL   D CG1   1 
ATOM   8710  C  CG2   . VAL   C 2  229 ? -11.983 -7.485  35.745   1.00 44.22  ? 231 VAL   D CG2   1 
ATOM   8711  N  N     . SER   C 2  230 ? -9.953  -3.453  36.711   1.00 59.17  ? 232 SER   D N     1 
ATOM   8712  C  CA    . SER   C 2  230 ? -9.840  -2.022  36.972   1.00 52.30  ? 232 SER   D CA    1 
ATOM   8713  C  C     . SER   C 2  230 ? -8.959  -1.361  35.921   1.00 52.96  ? 232 SER   D C     1 
ATOM   8714  O  O     . SER   C 2  230 ? -9.387  -0.412  35.251   1.00 54.40  ? 232 SER   D O     1 
ATOM   8715  C  CB    . SER   C 2  230 ? -9.323  -1.758  38.392   1.00 40.63  ? 232 SER   D CB    1 
ATOM   8716  O  OG    . SER   C 2  230 ? -8.482  -2.794  38.839   1.00 57.12  ? 232 SER   D OG    1 
ATOM   8717  N  N     . ALA   C 2  231 ? -7.735  -1.868  35.741   1.00 49.38  ? 233 ALA   D N     1 
ATOM   8718  C  CA    . ALA   C 2  231 ? -6.882  -1.393  34.657   1.00 50.85  ? 233 ALA   D CA    1 
ATOM   8719  C  C     . ALA   C 2  231 ? -7.674  -1.214  33.360   1.00 51.11  ? 233 ALA   D C     1 
ATOM   8720  O  O     . ALA   C 2  231 ? -7.651  -0.143  32.743   1.00 44.41  ? 233 ALA   D O     1 
ATOM   8721  C  CB    . ALA   C 2  231 ? -5.719  -2.364  34.454   1.00 39.83  ? 233 ALA   D CB    1 
ATOM   8722  N  N     . THR   C 2  232 ? -8.395  -2.265  32.953   1.00 43.15  ? 234 THR   D N     1 
ATOM   8723  C  CA    . THR   C 2  232 ? -9.225  -2.213  31.758   1.00 41.32  ? 234 THR   D CA    1 
ATOM   8724  C  C     . THR   C 2  232 ? -10.248 -1.086  31.832   1.00 53.26  ? 234 THR   D C     1 
ATOM   8725  O  O     . THR   C 2  232 ? -10.364 -0.279  30.902   1.00 52.96  ? 234 THR   D O     1 
ATOM   8726  C  CB    . THR   C 2  232 ? -9.931  -3.546  31.570   1.00 46.27  ? 234 THR   D CB    1 
ATOM   8727  O  OG1   . THR   C 2  232 ? -8.961  -4.596  31.577   1.00 51.41  ? 234 THR   D OG1   1 
ATOM   8728  C  CG2   . THR   C 2  232 ? -10.706 -3.566  30.237   1.00 51.76  ? 234 THR   D CG2   1 
ATOM   8729  N  N     . MET   C 2  233 ? -11.013 -1.027  32.927   1.00 54.67  ? 235 MET   D N     1 
ATOM   8730  C  CA    . MET   C 2  233 ? -12.047 -0.007  33.062   1.00 46.44  ? 235 MET   D CA    1 
ATOM   8731  C  C     . MET   C 2  233 ? -11.457 1.397   33.094   1.00 48.65  ? 235 MET   D C     1 
ATOM   8732  O  O     . MET   C 2  233 ? -12.072 2.344   32.590   1.00 42.28  ? 235 MET   D O     1 
ATOM   8733  C  CB    . MET   C 2  233 ? -12.881 -0.283  34.310   1.00 38.24  ? 235 MET   D CB    1 
ATOM   8734  C  CG    . MET   C 2  233 ? -13.743 -1.525  34.152   1.00 50.60  ? 235 MET   D CG    1 
ATOM   8735  S  SD    . MET   C 2  233 ? -15.113 -1.653  35.321   1.00 57.12  ? 235 MET   D SD    1 
ATOM   8736  C  CE    . MET   C 2  233 ? -14.192 -1.540  36.845   1.00 63.29  ? 235 MET   D CE    1 
ATOM   8737  N  N     . SER   C 2  234 ? -10.269 1.561   33.670   1.00 52.18  ? 236 SER   D N     1 
ATOM   8738  C  CA    . SER   C 2  234 ? -9.679  2.891   33.684   1.00 49.95  ? 236 SER   D CA    1 
ATOM   8739  C  C     . SER   C 2  234 ? -9.282  3.323   32.289   1.00 47.41  ? 236 SER   D C     1 
ATOM   8740  O  O     . SER   C 2  234 ? -9.364  4.513   31.963   1.00 52.17  ? 236 SER   D O     1 
ATOM   8741  C  CB    . SER   C 2  234 ? -8.461  2.942   34.603   1.00 50.82  ? 236 SER   D CB    1 
ATOM   8742  O  OG    . SER   C 2  234 ? -7.905  4.246   34.583   1.00 52.45  ? 236 SER   D OG    1 
ATOM   8743  N  N     . GLY   C 2  235 ? -8.852  2.377   31.458   1.00 47.44  ? 237 GLY   D N     1 
ATOM   8744  C  CA    . GLY   C 2  235 ? -8.426  2.690   30.110   1.00 54.15  ? 237 GLY   D CA    1 
ATOM   8745  C  C     . GLY   C 2  235 ? -9.573  3.104   29.208   1.00 49.70  ? 237 GLY   D C     1 
ATOM   8746  O  O     . GLY   C 2  235 ? -9.565  4.199   28.642   1.00 49.44  ? 237 GLY   D O     1 
ATOM   8747  N  N     . VAL   C 2  236 ? -10.577 2.240   29.093   1.00 43.82  ? 238 VAL   D N     1 
ATOM   8748  C  CA    . VAL   C 2  236 ? -11.705 2.454   28.202   1.00 46.88  ? 238 VAL   D CA    1 
ATOM   8749  C  C     . VAL   C 2  236 ? -12.578 3.611   28.680   1.00 49.12  ? 238 VAL   D C     1 
ATOM   8750  O  O     . VAL   C 2  236 ? -13.615 3.897   28.067   1.00 48.55  ? 238 VAL   D O     1 
ATOM   8751  C  CB    . VAL   C 2  236 ? -12.535 1.168   28.062   1.00 40.86  ? 238 VAL   D CB    1 
ATOM   8752  C  CG1   . VAL   C 2  236 ? -11.646 0.006   27.661   1.00 37.80  ? 238 VAL   D CG1   1 
ATOM   8753  C  CG2   . VAL   C 2  236 ? -13.259 0.875   29.365   1.00 42.53  ? 238 VAL   D CG2   1 
ATOM   8754  N  N     . THR   C 2  237 ? -12.172 4.295   29.760   1.00 41.68  ? 239 THR   D N     1 
ATOM   8755  C  CA    . THR   C 2  237 ? -12.863 5.508   30.188   1.00 43.09  ? 239 THR   D CA    1 
ATOM   8756  C  C     . THR   C 2  237 ? -11.952 6.726   30.309   1.00 45.04  ? 239 THR   D C     1 
ATOM   8757  O  O     . THR   C 2  237 ? -12.444 7.821   30.630   1.00 43.42  ? 239 THR   D O     1 
ATOM   8758  C  CB    . THR   C 2  237 ? -13.620 5.282   31.513   1.00 43.11  ? 239 THR   D CB    1 
ATOM   8759  O  OG1   . THR   C 2  237 ? -12.709 5.196   32.627   1.00 45.68  ? 239 THR   D OG1   1 
ATOM   8760  C  CG2   . THR   C 2  237 ? -14.466 4.015   31.423   1.00 30.00  ? 239 THR   D CG2   1 
ATOM   8761  N  N     . THR   C 2  238 ? -10.650 6.581   30.059   1.00 41.05  ? 240 THR   D N     1 
ATOM   8762  C  CA    A THR   C 2  238 ? -9.776  7.746   30.024   0.00 43.28  ? 240 THR   D CA    1 
ATOM   8763  C  CA    B THR   C 2  238 ? -9.770  7.745   30.014   1.00 42.77  ? 240 THR   D CA    1 
ATOM   8764  C  C     . THR   C 2  238 ? -10.370 8.839   29.143   1.00 49.67  ? 240 THR   D C     1 
ATOM   8765  O  O     . THR   C 2  238 ? -10.460 10.002  29.554   1.00 49.78  ? 240 THR   D O     1 
ATOM   8766  C  CB    A THR   C 2  238 ? -8.385  7.348   29.526   0.00 45.36  ? 240 THR   D CB    1 
ATOM   8767  C  CB    B THR   C 2  238 ? -8.401  7.351   29.470   1.00 45.04  ? 240 THR   D CB    1 
ATOM   8768  O  OG1   A THR   C 2  238 ? -7.820  6.372   30.410   0.00 51.13  ? 240 THR   D OG1   1 
ATOM   8769  O  OG1   B THR   C 2  238 ? -7.921  6.200   30.161   1.00 52.82  ? 240 THR   D OG1   1 
ATOM   8770  C  CG2   A THR   C 2  238 ? -7.472  8.563   29.471   0.00 47.34  ? 240 THR   D CG2   1 
ATOM   8771  C  CG2   B THR   C 2  238 ? -7.422  8.457   29.652   1.00 46.52  ? 240 THR   D CG2   1 
ATOM   8772  N  N     . CYS   C 2  239 ? -10.795 8.474   27.923   1.00 50.46  ? 241 CYS   D N     1 
ATOM   8773  C  CA    A CYS   C 2  239 ? -11.340 9.466   27.002   0.60 43.86  ? 241 CYS   D CA    1 
ATOM   8774  C  CA    B CYS   C 2  239 ? -11.350 9.453   26.992   0.40 43.89  ? 241 CYS   D CA    1 
ATOM   8775  C  C     . CYS   C 2  239 ? -12.636 10.086  27.509   1.00 45.77  ? 241 CYS   D C     1 
ATOM   8776  O  O     . CYS   C 2  239 ? -12.980 11.194  27.085   1.00 44.76  ? 241 CYS   D O     1 
ATOM   8777  C  CB    A CYS   C 2  239 ? -11.553 8.846   25.618   0.60 43.26  ? 241 CYS   D CB    1 
ATOM   8778  C  CB    B CYS   C 2  239 ? -11.593 8.809   25.620   0.40 43.26  ? 241 CYS   D CB    1 
ATOM   8779  S  SG    A CYS   C 2  239 ? -10.094 8.951   24.537   0.60 43.90  ? 241 CYS   D SG    1 
ATOM   8780  S  SG    B CYS   C 2  239 ? -12.822 7.472   25.553   0.40 41.91  ? 241 CYS   D SG    1 
ATOM   8781  N  N     . LEU   C 2  240 ? -13.358 9.416   28.416   1.00 48.87  ? 242 LEU   D N     1 
ATOM   8782  C  CA    . LEU   C 2  240 ? -14.541 10.043  28.999   1.00 43.30  ? 242 LEU   D CA    1 
ATOM   8783  C  C     . LEU   C 2  240 ? -14.184 10.984  30.145   1.00 43.40  ? 242 LEU   D C     1 
ATOM   8784  O  O     . LEU   C 2  240 ? -14.920 11.944  30.397   1.00 37.46  ? 242 LEU   D O     1 
ATOM   8785  C  CB    . LEU   C 2  240 ? -15.519 8.979   29.488   1.00 41.01  ? 242 LEU   D CB    1 
ATOM   8786  C  CG    . LEU   C 2  240 ? -16.023 7.930   28.502   1.00 36.61  ? 242 LEU   D CG    1 
ATOM   8787  C  CD1   . LEU   C 2  240 ? -16.925 6.894   29.196   1.00 23.25  ? 242 LEU   D CD1   1 
ATOM   8788  C  CD2   . LEU   C 2  240 ? -16.752 8.615   27.348   1.00 32.89  ? 242 LEU   D CD2   1 
ATOM   8789  N  N     . ARG   C 2  241 ? -13.046 10.749  30.817   1.00 50.55  ? 243 ARG   D N     1 
ATOM   8790  C  CA    . ARG   C 2  241 ? -12.697 11.425  32.073   1.00 58.88  ? 243 ARG   D CA    1 
ATOM   8791  C  C     . ARG   C 2  241 ? -11.662 12.535  31.931   1.00 48.76  ? 243 ARG   D C     1 
ATOM   8792  O  O     . ARG   C 2  241 ? -11.498 13.320  32.870   1.00 47.55  ? 243 ARG   D O     1 
ATOM   8793  C  CB    . ARG   C 2  241 ? -12.151 10.421  33.108   1.00 51.84  ? 243 ARG   D CB    1 
ATOM   8794  C  CG    . ARG   C 2  241 ? -13.160 9.386   33.588   1.00 53.05  ? 243 ARG   D CG    1 
ATOM   8795  C  CD    . ARG   C 2  241 ? -12.593 8.514   34.694   1.00 58.64  ? 243 ARG   D CD    1 
ATOM   8796  N  NE    . ARG   C 2  241 ? -11.597 7.540   34.249   1.00 53.65  ? 243 ARG   D NE    1 
ATOM   8797  C  CZ    . ARG   C 2  241 ? -10.301 7.619   34.525   1.00 52.73  ? 243 ARG   D CZ    1 
ATOM   8798  N  NH1   . ARG   C 2  241 ? -9.800  8.646   35.187   1.00 42.93  ? 243 ARG   D NH1   1 
ATOM   8799  N  NH2   . ARG   C 2  241 ? -9.486  6.639   34.129   1.00 50.40  ? 243 ARG   D NH2   1 
ATOM   8800  N  N     . PHE   C 2  242 ? -10.942 12.603  30.815   1.00 46.10  ? 244 PHE   D N     1 
ATOM   8801  C  CA    . PHE   C 2  242 ? -9.927  13.624  30.636   1.00 46.89  ? 244 PHE   D CA    1 
ATOM   8802  C  C     . PHE   C 2  242 ? -10.189 14.417  29.362   1.00 49.88  ? 244 PHE   D C     1 
ATOM   8803  O  O     . PHE   C 2  242 ? -10.787 13.902  28.412   1.00 46.60  ? 244 PHE   D O     1 
ATOM   8804  C  CB    . PHE   C 2  242 ? -8.518  13.019  30.567   1.00 53.01  ? 244 PHE   D CB    1 
ATOM   8805  C  CG    . PHE   C 2  242 ? -8.069  12.367  31.850   1.00 59.91  ? 244 PHE   D CG    1 
ATOM   8806  C  CD1   . PHE   C 2  242 ? -7.758  13.133  32.961   1.00 47.43  ? 244 PHE   D CD1   1 
ATOM   8807  C  CD2   . PHE   C 2  242 ? -7.941  10.984  31.936   1.00 60.01  ? 244 PHE   D CD2   1 
ATOM   8808  C  CE1   . PHE   C 2  242 ? -7.349  12.546  34.117   1.00 49.65  ? 244 PHE   D CE1   1 
ATOM   8809  C  CE2   . PHE   C 2  242 ? -7.527  10.384  33.104   1.00 53.97  ? 244 PHE   D CE2   1 
ATOM   8810  C  CZ    . PHE   C 2  242 ? -7.230  11.170  34.196   1.00 58.96  ? 244 PHE   D CZ    1 
ATOM   8811  N  N     . PRO   C 2  243 ? -9.738  15.667  29.309   1.00 54.23  ? 245 PRO   D N     1 
ATOM   8812  C  CA    . PRO   C 2  243 ? -9.994  16.489  28.124   1.00 51.96  ? 245 PRO   D CA    1 
ATOM   8813  C  C     . PRO   C 2  243 ? -9.334  15.881  26.893   1.00 59.20  ? 245 PRO   D C     1 
ATOM   8814  O  O     . PRO   C 2  243 ? -8.221  15.352  26.955   1.00 48.94  ? 245 PRO   D O     1 
ATOM   8815  C  CB    . PRO   C 2  243 ? -9.389  17.845  28.500   1.00 60.42  ? 245 PRO   D CB    1 
ATOM   8816  C  CG    . PRO   C 2  243 ? -8.321  17.506  29.499   1.00 58.72  ? 245 PRO   D CG    1 
ATOM   8817  C  CD    . PRO   C 2  243 ? -8.800  16.306  30.250   1.00 58.64  ? 245 PRO   D CD    1 
ATOM   8818  N  N     . GLY   C 2  244 ? -10.050 15.931  25.774   1.00 61.99  ? 246 GLY   D N     1 
ATOM   8819  C  CA    . GLY   C 2  244 ? -9.612  15.229  24.582   1.00 57.11  ? 246 GLY   D CA    1 
ATOM   8820  C  C     . GLY   C 2  244 ? -10.545 15.493  23.418   1.00 57.87  ? 246 GLY   D C     1 
ATOM   8821  O  O     . GLY   C 2  244 ? -11.521 16.243  23.522   1.00 59.59  ? 246 GLY   D O     1 
ATOM   8822  N  N     . GLN   C 2  245 ? -10.222 14.848  22.293   1.00 50.99  ? 247 GLN   D N     1 
ATOM   8823  C  CA    . GLN   C 2  245 ? -10.939 15.009  21.037   1.00 49.87  ? 247 GLN   D CA    1 
ATOM   8824  C  C     . GLN   C 2  245 ? -11.608 13.743  20.553   1.00 49.34  ? 247 GLN   D C     1 
ATOM   8825  O  O     . GLN   C 2  245 ? -12.559 13.834  19.777   1.00 55.73  ? 247 GLN   D O     1 
ATOM   8826  C  CB    . GLN   C 2  245 ? -9.985  15.475  19.923   1.00 50.91  ? 247 GLN   D CB    1 
ATOM   8827  C  CG    . GLN   C 2  245 ? -9.427  16.880  20.074   1.00 49.49  ? 247 GLN   D CG    1 
ATOM   8828  C  CD    . GLN   C 2  245 ? -10.514 17.944  20.068   1.00 52.07  ? 247 GLN   D CD    1 
ATOM   8829  O  OE1   . GLN   C 2  245 ? -10.675 18.676  19.089   1.00 51.93  ? 247 GLN   D OE1   1 
ATOM   8830  N  NE2   . GLN   C 2  245 ? -11.269 18.031  21.161   1.00 52.05  ? 247 GLN   D NE2   1 
ATOM   8831  N  N     . LEU   C 2  246 ? -11.121 12.577  20.963   1.00 48.65  ? 248 LEU   D N     1 
ATOM   8832  C  CA    . LEU   C 2  246 ? -11.548 11.285  20.446   1.00 45.34  ? 248 LEU   D CA    1 
ATOM   8833  C  C     . LEU   C 2  246 ? -12.472 10.606  21.443   1.00 37.03  ? 248 LEU   D C     1 
ATOM   8834  O  O     . LEU   C 2  246 ? -12.130 10.479  22.625   1.00 42.36  ? 248 LEU   D O     1 
ATOM   8835  C  CB    . LEU   C 2  246 ? -10.342 10.377  20.176   1.00 41.28  ? 248 LEU   D CB    1 
ATOM   8836  C  CG    . LEU   C 2  246 ? -10.749 8.984   19.696   1.00 40.33  ? 248 LEU   D CG    1 
ATOM   8837  C  CD1   . LEU   C 2  246 ? -11.492 9.085   18.356   1.00 41.49  ? 248 LEU   D CD1   1 
ATOM   8838  C  CD2   . LEU   C 2  246 ? -9.563  8.065   19.589   1.00 43.82  ? 248 LEU   D CD2   1 
ATOM   8839  N  N     . ASN   C 2  247 ? -13.620 10.151  20.958   1.00 33.20  ? 249 ASN   D N     1 
ATOM   8840  C  CA    . ASN   C 2  247 ? -14.610 9.443   21.765   1.00 39.59  ? 249 ASN   D CA    1 
ATOM   8841  C  C     . ASN   C 2  247 ? -14.691 10.025  23.186   1.00 40.10  ? 249 ASN   D C     1 
ATOM   8842  O  O     . ASN   C 2  247 ? -14.542 9.331   24.193   1.00 42.63  ? 249 ASN   D O     1 
ATOM   8843  C  CB    . ASN   C 2  247 ? -14.295 7.941   21.783   1.00 39.46  ? 249 ASN   D CB    1 
ATOM   8844  C  CG    . ASN   C 2  247 ? -14.113 7.355   20.371   1.00 41.65  ? 249 ASN   D CG    1 
ATOM   8845  O  OD1   . ASN   C 2  247 ? -15.063 7.273   19.583   1.00 35.86  ? 249 ASN   D OD1   1 
ATOM   8846  N  ND2   . ASN   C 2  247 ? -12.893 6.937   20.059   1.00 36.51  ? 249 ASN   D ND2   1 
ATOM   8847  N  N     . ALA   C 2  248 ? -14.941 11.328  23.260   1.00 32.39  ? 250 ALA   D N     1 
ATOM   8848  C  CA    . ALA   C 2  248 ? -14.891 12.003  24.547   1.00 36.78  ? 250 ALA   D CA    1 
ATOM   8849  C  C     . ALA   C 2  248 ? -16.210 11.938  25.307   1.00 43.03  ? 250 ALA   D C     1 
ATOM   8850  O  O     . ALA   C 2  248 ? -16.277 12.434  26.440   1.00 41.95  ? 250 ALA   D O     1 
ATOM   8851  C  CB    . ALA   C 2  248 ? -14.459 13.459  24.373   1.00 28.36  ? 250 ALA   D CB    1 
ATOM   8852  N  N     . ASP   C 2  249 ? -17.249 11.344  24.721   1.00 35.37  ? 251 ASP   D N     1 
ATOM   8853  C  CA    . ASP   C 2  249 ? -18.496 11.088  25.422   1.00 30.48  ? 251 ASP   D CA    1 
ATOM   8854  C  C     . ASP   C 2  249 ? -19.065 9.789   24.879   1.00 32.01  ? 251 ASP   D C     1 
ATOM   8855  O  O     . ASP   C 2  249 ? -18.643 9.303   23.823   1.00 34.05  ? 251 ASP   D O     1 
ATOM   8856  C  CB    . ASP   C 2  249 ? -19.502 12.249  25.280   1.00 30.18  ? 251 ASP   D CB    1 
ATOM   8857  C  CG    . ASP   C 2  249 ? -20.047 12.376  23.876   1.00 29.52  ? 251 ASP   D CG    1 
ATOM   8858  O  OD1   . ASP   C 2  249 ? -20.763 11.460  23.429   1.00 30.40  ? 251 ASP   D OD1   1 
ATOM   8859  O  OD2   . ASP   C 2  249 ? -19.746 13.384  23.204   1.00 38.97  ? 251 ASP   D OD2   1 
ATOM   8860  N  N     . LEU   C 2  250 ? -20.035 9.232   25.625   1.00 32.94  ? 252 LEU   D N     1 
ATOM   8861  C  CA    . LEU   C 2  250 ? -20.548 7.884   25.375   1.00 30.45  ? 252 LEU   D CA    1 
ATOM   8862  C  C     . LEU   C 2  250 ? -21.236 7.734   24.019   1.00 38.41  ? 252 LEU   D C     1 
ATOM   8863  O  O     . LEU   C 2  250 ? -21.346 6.601   23.518   1.00 38.98  ? 252 LEU   D O     1 
ATOM   8864  C  CB    . LEU   C 2  250 ? -21.538 7.473   26.477   1.00 38.59  ? 252 LEU   D CB    1 
ATOM   8865  C  CG    . LEU   C 2  250 ? -21.072 7.165   27.903   1.00 37.37  ? 252 LEU   D CG    1 
ATOM   8866  C  CD1   . LEU   C 2  250 ? -22.294 6.975   28.744   1.00 40.41  ? 252 LEU   D CD1   1 
ATOM   8867  C  CD2   . LEU   C 2  250 ? -20.145 5.934   28.008   1.00 24.62  ? 252 LEU   D CD2   1 
ATOM   8868  N  N     . ARG   C 2  251 ? -21.723 8.832   23.424   1.00 38.04  ? 253 ARG   D N     1 
ATOM   8869  C  CA    . ARG   C 2  251 ? -22.444 8.725   22.160   1.00 39.28  ? 253 ARG   D CA    1 
ATOM   8870  C  C     . ARG   C 2  251 ? -21.500 8.784   20.963   1.00 38.56  ? 253 ARG   D C     1 
ATOM   8871  O  O     . ARG   C 2  251 ? -21.608 7.971   20.038   1.00 35.77  ? 253 ARG   D O     1 
ATOM   8872  C  CB    . ARG   C 2  251 ? -23.510 9.817   22.036   1.00 30.54  ? 253 ARG   D CB    1 
ATOM   8873  C  CG    . ARG   C 2  251 ? -24.327 9.672   20.735   1.00 30.19  ? 253 ARG   D CG    1 
ATOM   8874  C  CD    . ARG   C 2  251 ? -25.348 10.789  20.571   1.00 32.15  ? 253 ARG   D CD    1 
ATOM   8875  N  NE    . ARG   C 2  251 ? -26.131 10.878  21.789   1.00 41.62  ? 253 ARG   D NE    1 
ATOM   8876  C  CZ    . ARG   C 2  251 ? -27.051 9.994   22.128   1.00 39.65  ? 253 ARG   D CZ    1 
ATOM   8877  N  NH1   . ARG   C 2  251 ? -27.458 9.063   21.277   1.00 30.18  ? 253 ARG   D NH1   1 
ATOM   8878  N  NH2   . ARG   C 2  251 ? -27.561 10.034  23.354   1.00 44.66  ? 253 ARG   D NH2   1 
ATOM   8879  N  N     . LYS   C 2  252 ? -20.581 9.746   20.948   1.00 31.86  ? 254 LYS   D N     1 
ATOM   8880  C  CA    . LYS   C 2  252 ? -19.564 9.726   19.905   1.00 32.11  ? 254 LYS   D CA    1 
ATOM   8881  C  C     . LYS   C 2  252 ? -18.875 8.374   19.864   1.00 36.94  ? 254 LYS   D C     1 
ATOM   8882  O  O     . LYS   C 2  252 ? -18.669 7.800   18.788   1.00 35.79  ? 254 LYS   D O     1 
ATOM   8883  C  CB    . LYS   C 2  252 ? -18.563 10.850  20.134   1.00 26.46  ? 254 LYS   D CB    1 
ATOM   8884  C  CG    . LYS   C 2  252 ? -19.190 12.156  19.867   1.00 28.15  ? 254 LYS   D CG    1 
ATOM   8885  C  CD    . LYS   C 2  252 ? -18.204 13.237  19.818   1.00 27.95  ? 254 LYS   D CD    1 
ATOM   8886  C  CE    . LYS   C 2  252 ? -18.674 14.279  18.846   1.00 27.36  ? 254 LYS   D CE    1 
ATOM   8887  N  NZ    . LYS   C 2  252 ? -18.104 15.573  19.220   1.00 25.23  ? 254 LYS   D NZ    1 
ATOM   8888  N  N     . LEU   C 2  253 ? -18.543 7.834   21.038   1.00 37.61  ? 255 LEU   D N     1 
ATOM   8889  C  CA    . LEU   C 2  253 ? -18.008 6.482   21.109   1.00 39.30  ? 255 LEU   D CA    1 
ATOM   8890  C  C     . LEU   C 2  253 ? -18.937 5.494   20.413   1.00 35.37  ? 255 LEU   D C     1 
ATOM   8891  O  O     . LEU   C 2  253 ? -18.526 4.752   19.515   1.00 35.77  ? 255 LEU   D O     1 
ATOM   8892  C  CB    . LEU   C 2  253 ? -17.797 6.086   22.573   1.00 42.25  ? 255 LEU   D CB    1 
ATOM   8893  C  CG    . LEU   C 2  253 ? -16.990 4.804   22.742   1.00 34.95  ? 255 LEU   D CG    1 
ATOM   8894  C  CD1   . LEU   C 2  253 ? -15.546 5.109   22.378   1.00 33.53  ? 255 LEU   D CD1   1 
ATOM   8895  C  CD2   . LEU   C 2  253 ? -17.132 4.219   24.150   1.00 34.00  ? 255 LEU   D CD2   1 
ATOM   8896  N  N     . ALA   C 2  254 ? -20.204 5.467   20.831   1.00 37.69  ? 256 ALA   D N     1 
ATOM   8897  C  CA    . ALA   C 2  254 ? -21.154 4.538   20.230   1.00 34.24  ? 256 ALA   D CA    1 
ATOM   8898  C  C     . ALA   C 2  254 ? -21.176 4.674   18.712   1.00 34.11  ? 256 ALA   D C     1 
ATOM   8899  O  O     . ALA   C 2  254 ? -21.243 3.672   17.992   1.00 31.25  ? 256 ALA   D O     1 
ATOM   8900  C  CB    . ALA   C 2  254 ? -22.547 4.771   20.820   1.00 36.58  ? 256 ALA   D CB    1 
ATOM   8901  N  N     . VAL   C 2  255 ? -21.101 5.914   18.211   1.00 37.47  ? 257 VAL   D N     1 
ATOM   8902  C  CA    . VAL   C 2  255 ? -21.172 6.172   16.777   1.00 34.64  ? 257 VAL   D CA    1 
ATOM   8903  C  C     . VAL   C 2  255 ? -19.886 5.767   16.070   1.00 36.43  ? 257 VAL   D C     1 
ATOM   8904  O  O     . VAL   C 2  255 ? -19.916 5.391   14.891   1.00 37.73  ? 257 VAL   D O     1 
ATOM   8905  C  CB    . VAL   C 2  255 ? -21.495 7.654   16.521   1.00 34.06  ? 257 VAL   D CB    1 
ATOM   8906  C  CG1   . VAL   C 2  255 ? -21.310 7.973   15.058   1.00 27.64  ? 257 VAL   D CG1   1 
ATOM   8907  C  CG2   . VAL   C 2  255 ? -22.905 7.955   16.964   1.00 28.60  ? 257 VAL   D CG2   1 
ATOM   8908  N  N     . ASN   C 2  256 ? -18.737 5.845   16.756   1.00 34.05  ? 258 ASN   D N     1 
ATOM   8909  C  CA    . ASN   C 2  256 ? -17.481 5.366   16.171   1.00 36.90  ? 258 ASN   D CA    1 
ATOM   8910  C  C     . ASN   C 2  256 ? -17.322 3.844   16.223   1.00 34.56  ? 258 ASN   D C     1 
ATOM   8911  O  O     . ASN   C 2  256 ? -16.539 3.285   15.451   1.00 32.76  ? 258 ASN   D O     1 
ATOM   8912  C  CB    . ASN   C 2  256 ? -16.294 6.033   16.872   1.00 32.28  ? 258 ASN   D CB    1 
ATOM   8913  C  CG    . ASN   C 2  256 ? -15.967 7.401   16.289   1.00 36.42  ? 258 ASN   D CG    1 
ATOM   8914  O  OD1   . ASN   C 2  256 ? -16.449 7.749   15.216   1.00 37.80  ? 258 ASN   D OD1   1 
ATOM   8915  N  ND2   . ASN   C 2  256 ? -15.127 8.172   16.983   1.00 31.95  ? 258 ASN   D ND2   1 
ATOM   8916  N  N     . MET   C 2  257 ? -18.063 3.157   17.096   1.00 41.05  ? 259 MET   D N     1 
ATOM   8917  C  CA    . MET   C 2  257 ? -17.813 1.757   17.390   1.00 32.71  ? 259 MET   D CA    1 
ATOM   8918  C  C     . MET   C 2  257 ? -18.904 0.805   16.947   1.00 34.49  ? 259 MET   D C     1 
ATOM   8919  O  O     . MET   C 2  257 ? -18.626 -0.389  16.808   1.00 37.26  ? 259 MET   D O     1 
ATOM   8920  C  CB    . MET   C 2  257 ? -17.606 1.579   18.890   1.00 38.28  ? 259 MET   D CB    1 
ATOM   8921  C  CG    . MET   C 2  257 ? -16.346 2.251   19.351   1.00 40.26  ? 259 MET   D CG    1 
ATOM   8922  S  SD    . MET   C 2  257 ? -14.932 1.430   18.595   1.00 41.83  ? 259 MET   D SD    1 
ATOM   8923  C  CE    . MET   C 2  257 ? -13.793 2.816   18.621   1.00 40.66  ? 259 MET   D CE    1 
ATOM   8924  N  N     . VAL   C 2  258 ? -20.123 1.283   16.719   1.00 31.91  ? 260 VAL   D N     1 
ATOM   8925  C  CA    . VAL   C 2  258 ? -21.234 0.368   16.471   1.00 32.74  ? 260 VAL   D CA    1 
ATOM   8926  C  C     . VAL   C 2  258 ? -21.782 0.601   15.067   1.00 34.13  ? 260 VAL   D C     1 
ATOM   8927  O  O     . VAL   C 2  258 ? -22.669 1.446   14.863   1.00 29.37  ? 260 VAL   D O     1 
ATOM   8928  C  CB    . VAL   C 2  258 ? -22.311 0.520   17.560   1.00 37.44  ? 260 VAL   D CB    1 
ATOM   8929  C  CG1   . VAL   C 2  258 ? -23.429 -0.517  17.391   1.00 30.84  ? 260 VAL   D CG1   1 
ATOM   8930  C  CG2   . VAL   C 2  258 ? -21.663 0.389   18.924   1.00 25.84  ? 260 VAL   D CG2   1 
ATOM   8931  N  N     . PRO   C 2  259 ? -21.262 -0.110  14.066   1.00 33.99  ? 261 PRO   D N     1 
ATOM   8932  C  CA    . PRO   C 2  259 ? -21.790 0.055   12.706   1.00 34.65  ? 261 PRO   D CA    1 
ATOM   8933  C  C     . PRO   C 2  259 ? -23.186 -0.512  12.548   1.00 39.22  ? 261 PRO   D C     1 
ATOM   8934  O  O     . PRO   C 2  259 ? -23.927 -0.071  11.660   1.00 39.15  ? 261 PRO   D O     1 
ATOM   8935  C  CB    . PRO   C 2  259 ? -20.777 -0.716  11.850   1.00 39.57  ? 261 PRO   D CB    1 
ATOM   8936  C  CG    . PRO   C 2  259 ? -20.282 -1.810  12.789   1.00 33.93  ? 261 PRO   D CG    1 
ATOM   8937  C  CD    . PRO   C 2  259 ? -20.178 -1.105  14.127   1.00 33.23  ? 261 PRO   D CD    1 
ATOM   8938  N  N     . PHE   C 2  260 ? -23.553 -1.511  13.360   1.00 45.11  ? 262 PHE   D N     1 
ATOM   8939  C  CA    . PHE   C 2  260 ? -24.890 -2.095  13.389   1.00 34.66  ? 262 PHE   D CA    1 
ATOM   8940  C  C     . PHE   C 2  260 ? -25.348 -2.204  14.835   1.00 39.74  ? 262 PHE   D C     1 
ATOM   8941  O  O     . PHE   C 2  260 ? -24.527 -2.461  15.737   1.00 39.46  ? 262 PHE   D O     1 
ATOM   8942  C  CB    . PHE   C 2  260 ? -24.906 -3.457  12.709   1.00 29.90  ? 262 PHE   D CB    1 
ATOM   8943  C  CG    . PHE   C 2  260 ? -24.332 -3.417  11.329   1.00 42.68  ? 262 PHE   D CG    1 
ATOM   8944  C  CD1   . PHE   C 2  260 ? -25.109 -2.986  10.255   1.00 32.97  ? 262 PHE   D CD1   1 
ATOM   8945  C  CD2   . PHE   C 2  260 ? -22.998 -3.744  11.110   1.00 34.12  ? 262 PHE   D CD2   1 
ATOM   8946  C  CE1   . PHE   C 2  260 ? -24.571 -2.906  8.988    1.00 30.05  ? 262 PHE   D CE1   1 
ATOM   8947  C  CE2   . PHE   C 2  260 ? -22.460 -3.675  9.857    1.00 34.00  ? 262 PHE   D CE2   1 
ATOM   8948  C  CZ    . PHE   C 2  260 ? -23.251 -3.253  8.788    1.00 36.48  ? 262 PHE   D CZ    1 
ATOM   8949  N  N     . PRO   C 2  261 ? -26.641 -1.984  15.091   1.00 35.76  ? 263 PRO   D N     1 
ATOM   8950  C  CA    . PRO   C 2  261 ? -27.075 -1.778  16.483   1.00 36.67  ? 263 PRO   D CA    1 
ATOM   8951  C  C     . PRO   C 2  261 ? -26.895 -2.999  17.379   1.00 40.20  ? 263 PRO   D C     1 
ATOM   8952  O  O     . PRO   C 2  261 ? -26.527 -2.850  18.552   1.00 36.10  ? 263 PRO   D O     1 
ATOM   8953  C  CB    . PRO   C 2  261 ? -28.546 -1.389  16.322   1.00 21.94  ? 263 PRO   D CB    1 
ATOM   8954  C  CG    . PRO   C 2  261 ? -28.962 -2.027  15.056   1.00 28.65  ? 263 PRO   D CG    1 
ATOM   8955  C  CD    . PRO   C 2  261 ? -27.768 -1.952  14.151   1.00 37.96  ? 263 PRO   D CD    1 
ATOM   8956  N  N     . ARG   C 2  262 ? -27.140 -4.207  16.864   1.00 40.13  ? 264 ARG   D N     1 
ATOM   8957  C  CA    . ARG   C 2  262 ? -26.978 -5.392  17.700   1.00 35.25  ? 264 ARG   D CA    1 
ATOM   8958  C  C     . ARG   C 2  262 ? -25.513 -5.676  18.000   1.00 35.42  ? 264 ARG   D C     1 
ATOM   8959  O  O     . ARG   C 2  262 ? -25.197 -6.155  19.090   1.00 38.70  ? 264 ARG   D O     1 
ATOM   8960  C  CB    . ARG   C 2  262 ? -27.629 -6.604  17.035   1.00 28.67  ? 264 ARG   D CB    1 
ATOM   8961  C  CG    . ARG   C 2  262 ? -29.125 -6.479  16.883   1.00 20.20  ? 264 ARG   D CG    1 
ATOM   8962  C  CD    . ARG   C 2  262 ? -29.621 -7.431  15.843   1.00 39.49  ? 264 ARG   D CD    1 
ATOM   8963  N  NE    . ARG   C 2  262 ? -29.189 -8.799  16.101   1.00 52.82  ? 264 ARG   D NE    1 
ATOM   8964  C  CZ    . ARG   C 2  262 ? -29.838 -9.637  16.895   1.00 48.28  ? 264 ARG   D CZ    1 
ATOM   8965  N  NH1   . ARG   C 2  262 ? -30.932 -9.266  17.535   1.00 43.45  ? 264 ARG   D NH1   1 
ATOM   8966  N  NH2   . ARG   C 2  262 ? -29.373 -10.874 17.056   1.00 46.67  ? 264 ARG   D NH2   1 
ATOM   8967  N  N     . LEU   C 2  263 ? -24.607 -5.389  17.065   1.00 40.29  ? 265 LEU   D N     1 
ATOM   8968  C  CA    . LEU   C 2  263 ? -23.200 -5.782  17.207   1.00 41.83  ? 265 LEU   D CA    1 
ATOM   8969  C  C     . LEU   C 2  263 ? -22.449 -4.721  18.003   1.00 41.33  ? 265 LEU   D C     1 
ATOM   8970  O  O     . LEU   C 2  263 ? -21.556 -4.034  17.500   1.00 39.89  ? 265 LEU   D O     1 
ATOM   8971  C  CB    . LEU   C 2  263 ? -22.560 -5.996  15.845   1.00 37.79  ? 265 LEU   D CB    1 
ATOM   8972  C  CG    . LEU   C 2  263 ? -23.383 -6.804  14.858   1.00 41.01  ? 265 LEU   D CG    1 
ATOM   8973  C  CD1   . LEU   C 2  263 ? -22.677 -6.856  13.518   1.00 37.08  ? 265 LEU   D CD1   1 
ATOM   8974  C  CD2   . LEU   C 2  263 ? -23.646 -8.194  15.422   1.00 41.80  ? 265 LEU   D CD2   1 
ATOM   8975  N  N     . HIS   C 2  264 ? -22.825 -4.620  19.283   1.00 38.83  ? 266 HIS   D N     1 
ATOM   8976  C  CA    . HIS   C 2  264 ? -22.321 -3.610  20.212   1.00 42.43  ? 266 HIS   D CA    1 
ATOM   8977  C  C     . HIS   C 2  264 ? -21.552 -4.241  21.384   1.00 42.22  ? 266 HIS   D C     1 
ATOM   8978  O  O     . HIS   C 2  264 ? -21.581 -3.732  22.512   1.00 46.31  ? 266 HIS   D O     1 
ATOM   8979  C  CB    . HIS   C 2  264 ? -23.475 -2.734  20.719   1.00 33.79  ? 266 HIS   D CB    1 
ATOM   8980  C  CG    . HIS   C 2  264 ? -24.572 -3.505  21.396   1.00 42.29  ? 266 HIS   D CG    1 
ATOM   8981  N  ND1   . HIS   C 2  264 ? -25.833 -3.642  20.853   1.00 41.56  ? 266 HIS   D ND1   1 
ATOM   8982  C  CD2   . HIS   C 2  264 ? -24.592 -4.195  22.563   1.00 47.42  ? 266 HIS   D CD2   1 
ATOM   8983  C  CE1   . HIS   C 2  264 ? -26.582 -4.377  21.657   1.00 35.80  ? 266 HIS   D CE1   1 
ATOM   8984  N  NE2   . HIS   C 2  264 ? -25.852 -4.727  22.701   1.00 45.15  ? 266 HIS   D NE2   1 
ATOM   8985  N  N     . PHE   C 2  265 ? -20.838 -5.334  21.124   1.00 38.93  ? 267 PHE   D N     1 
ATOM   8986  C  CA    . PHE   C 2  265 ? -20.097 -6.085  22.135   1.00 38.67  ? 267 PHE   D CA    1 
ATOM   8987  C  C     . PHE   C 2  265 ? -18.605 -6.023  21.821   1.00 42.16  ? 267 PHE   D C     1 
ATOM   8988  O  O     . PHE   C 2  265 ? -18.165 -6.498  20.768   1.00 49.41  ? 267 PHE   D O     1 
ATOM   8989  C  CB    . PHE   C 2  265 ? -20.592 -7.536  22.187   1.00 41.87  ? 267 PHE   D CB    1 
ATOM   8990  C  CG    . PHE   C 2  265 ? -22.044 -7.657  22.547   1.00 41.98  ? 267 PHE   D CG    1 
ATOM   8991  C  CD1   . PHE   C 2  265 ? -23.015 -7.638  21.570   1.00 40.18  ? 267 PHE   D CD1   1 
ATOM   8992  C  CD2   . PHE   C 2  265 ? -22.435 -7.760  23.868   1.00 41.13  ? 267 PHE   D CD2   1 
ATOM   8993  C  CE1   . PHE   C 2  265 ? -24.335 -7.721  21.906   1.00 42.77  ? 267 PHE   D CE1   1 
ATOM   8994  C  CE2   . PHE   C 2  265 ? -23.761 -7.857  24.205   1.00 39.49  ? 267 PHE   D CE2   1 
ATOM   8995  C  CZ    . PHE   C 2  265 ? -24.708 -7.834  23.228   1.00 41.54  ? 267 PHE   D CZ    1 
ATOM   8996  N  N     . PHE   C 2  266 ? -17.831 -5.467  22.744   1.00 45.64  ? 268 PHE   D N     1 
ATOM   8997  C  CA    . PHE   C 2  266 ? -16.449 -5.081  22.510   1.00 43.04  ? 268 PHE   D CA    1 
ATOM   8998  C  C     . PHE   C 2  266 ? -15.481 -5.990  23.253   1.00 45.87  ? 268 PHE   D C     1 
ATOM   8999  O  O     . PHE   C 2  266 ? -15.743 -6.440  24.370   1.00 48.39  ? 268 PHE   D O     1 
ATOM   9000  C  CB    . PHE   C 2  266 ? -16.194 -3.632  22.951   1.00 41.22  ? 268 PHE   D CB    1 
ATOM   9001  C  CG    . PHE   C 2  266 ? -17.176 -2.637  22.390   1.00 39.02  ? 268 PHE   D CG    1 
ATOM   9002  C  CD1   . PHE   C 2  266 ? -17.810 -2.867  21.186   1.00 34.80  ? 268 PHE   D CD1   1 
ATOM   9003  C  CD2   . PHE   C 2  266 ? -17.467 -1.467  23.076   1.00 44.04  ? 268 PHE   D CD2   1 
ATOM   9004  C  CE1   . PHE   C 2  266 ? -18.712 -1.958  20.688   1.00 31.59  ? 268 PHE   D CE1   1 
ATOM   9005  C  CE2   . PHE   C 2  266 ? -18.371 -0.548  22.567   1.00 35.19  ? 268 PHE   D CE2   1 
ATOM   9006  C  CZ    . PHE   C 2  266 ? -18.990 -0.801  21.387   1.00 31.52  ? 268 PHE   D CZ    1 
ATOM   9007  N  N     . MET   C 2  267 ? -14.341 -6.225  22.622   1.00 53.91  ? 269 MET   D N     1 
ATOM   9008  C  CA    . MET   C 2  267 ? -13.256 -7.009  23.186   1.00 44.66  ? 269 MET   D CA    1 
ATOM   9009  C  C     . MET   C 2  267 ? -12.271 -6.044  23.820   1.00 41.14  ? 269 MET   D C     1 
ATOM   9010  O  O     . MET   C 2  267 ? -11.586 -5.323  23.088   1.00 50.27  ? 269 MET   D O     1 
ATOM   9011  C  CB    . MET   C 2  267 ? -12.590 -7.807  22.069   1.00 55.11  ? 269 MET   D CB    1 
ATOM   9012  C  CG    . MET   C 2  267 ? -11.830 -9.053  22.459   1.00 62.61  ? 269 MET   D CG    1 
ATOM   9013  S  SD    . MET   C 2  267 ? -11.368 -9.929  20.943   1.00 62.02  ? 269 MET   D SD    1 
ATOM   9014  C  CE    . MET   C 2  267 ? -12.972 -10.446 20.336   1.00 60.74  ? 269 MET   D CE    1 
ATOM   9015  N  N     . PRO   C 2  268 ? -12.191 -5.935  25.146   1.00 45.36  ? 270 PRO   D N     1 
ATOM   9016  C  CA    . PRO   C 2  268 ? -11.197 -5.032  25.740   1.00 43.12  ? 270 PRO   D CA    1 
ATOM   9017  C  C     . PRO   C 2  268 ? -9.804  -5.633  25.649   1.00 47.77  ? 270 PRO   D C     1 
ATOM   9018  O  O     . PRO   C 2  268 ? -9.623  -6.833  25.429   1.00 44.55  ? 270 PRO   D O     1 
ATOM   9019  C  CB    . PRO   C 2  268 ? -11.646 -4.887  27.201   1.00 32.30  ? 270 PRO   D CB    1 
ATOM   9020  C  CG    . PRO   C 2  268 ? -12.982 -5.478  27.263   1.00 45.37  ? 270 PRO   D CG    1 
ATOM   9021  C  CD    . PRO   C 2  268 ? -13.053 -6.518  26.172   1.00 43.89  ? 270 PRO   D CD    1 
ATOM   9022  N  N     . GLY   C 2  269 ? -8.810  -4.765  25.802   1.00 45.14  ? 271 GLY   D N     1 
ATOM   9023  C  CA    . GLY   C 2  269 ? -7.423  -5.157  25.651   1.00 42.64  ? 271 GLY   D CA    1 
ATOM   9024  C  C     . GLY   C 2  269 ? -6.548  -4.147  26.345   1.00 45.28  ? 271 GLY   D C     1 
ATOM   9025  O  O     . GLY   C 2  269 ? -6.886  -2.962  26.415   1.00 57.60  ? 271 GLY   D O     1 
ATOM   9026  N  N     . PHE   C 2  270 ? -5.421  -4.619  26.877   1.00 47.70  ? 272 PHE   D N     1 
ATOM   9027  C  CA    . PHE   C 2  270 ? -4.592  -3.798  27.751   1.00 50.44  ? 272 PHE   D CA    1 
ATOM   9028  C  C     . PHE   C 2  270 ? -3.135  -4.223  27.597   1.00 51.53  ? 272 PHE   D C     1 
ATOM   9029  O  O     . PHE   C 2  270 ? -2.831  -5.337  27.158   1.00 50.77  ? 272 PHE   D O     1 
ATOM   9030  C  CB    . PHE   C 2  270 ? -5.057  -3.911  29.217   1.00 45.73  ? 272 PHE   D CB    1 
ATOM   9031  C  CG    . PHE   C 2  270 ? -4.617  -2.761  30.094   1.00 62.65  ? 272 PHE   D CG    1 
ATOM   9032  C  CD1   . PHE   C 2  270 ? -5.170  -1.487  29.931   1.00 66.98  ? 272 PHE   D CD1   1 
ATOM   9033  C  CD2   . PHE   C 2  270 ? -3.659  -2.947  31.091   1.00 64.22  ? 272 PHE   D CD2   1 
ATOM   9034  C  CE1   . PHE   C 2  270 ? -4.765  -0.408  30.748   1.00 66.31  ? 272 PHE   D CE1   1 
ATOM   9035  C  CE2   . PHE   C 2  270 ? -3.247  -1.884  31.912   1.00 64.81  ? 272 PHE   D CE2   1 
ATOM   9036  C  CZ    . PHE   C 2  270 ? -3.801  -0.612  31.742   1.00 74.74  ? 272 PHE   D CZ    1 
ATOM   9037  N  N     . ALA   C 2  271 ? -2.235  -3.311  27.946   1.00 48.94  ? 273 ALA   D N     1 
ATOM   9038  C  CA    . ALA   C 2  271 ? -0.801  -3.561  27.944   1.00 55.15  ? 273 ALA   D CA    1 
ATOM   9039  C  C     . ALA   C 2  271 ? -0.095  -2.404  28.638   1.00 59.60  ? 273 ALA   D C     1 
ATOM   9040  O  O     . ALA   C 2  271 ? -0.543  -1.253  28.559   1.00 58.10  ? 273 ALA   D O     1 
ATOM   9041  C  CB    . ALA   C 2  271 ? -0.259  -3.746  26.523   1.00 57.63  ? 273 ALA   D CB    1 
ATOM   9042  N  N     . PRO   C 2  272 ? 0.986   -2.676  29.351   1.00 60.27  ? 274 PRO   D N     1 
ATOM   9043  C  CA    . PRO   C 2  272 ? 1.535   -4.004  29.606   1.00 61.62  ? 274 PRO   D CA    1 
ATOM   9044  C  C     . PRO   C 2  272 ? 0.676   -4.695  30.649   1.00 61.40  ? 274 PRO   D C     1 
ATOM   9045  O  O     . PRO   C 2  272 ? 0.099   -4.006  31.484   1.00 69.01  ? 274 PRO   D O     1 
ATOM   9046  C  CB    . PRO   C 2  272 ? 2.943   -3.689  30.108   1.00 64.77  ? 274 PRO   D CB    1 
ATOM   9047  C  CG    . PRO   C 2  272 ? 2.739   -2.407  30.888   1.00 67.17  ? 274 PRO   D CG    1 
ATOM   9048  C  CD    . PRO   C 2  272 ? 1.713   -1.629  30.091   1.00 62.69  ? 274 PRO   D CD    1 
ATOM   9049  N  N     . LEU   C 2  273 ? 0.560   -6.023  30.627   1.00 61.88  ? 275 LEU   D N     1 
ATOM   9050  C  CA    . LEU   C 2  273 ? -0.132  -6.759  31.683   1.00 61.67  ? 275 LEU   D CA    1 
ATOM   9051  C  C     . LEU   C 2  273 ? 0.750   -6.897  32.921   1.00 69.43  ? 275 LEU   D C     1 
ATOM   9052  O  O     . LEU   C 2  273 ? 1.871   -7.413  32.843   1.00 70.14  ? 275 LEU   D O     1 
ATOM   9053  C  CB    . LEU   C 2  273 ? -0.526  -8.151  31.195   1.00 61.40  ? 275 LEU   D CB    1 
ATOM   9054  C  CG    . LEU   C 2  273 ? -1.167  -8.306  29.820   1.00 60.17  ? 275 LEU   D CG    1 
ATOM   9055  C  CD1   . LEU   C 2  273 ? -0.309  -9.215  28.940   1.00 55.43  ? 275 LEU   D CD1   1 
ATOM   9056  C  CD2   . LEU   C 2  273 ? -2.575  -8.859  29.980   1.00 57.80  ? 275 LEU   D CD2   1 
ATOM   9057  N  N     . THR   C 2  274 ? 0.236   -6.461  34.068   1.00 80.00  ? 276 THR   D N     1 
ATOM   9058  C  CA    . THR   C 2  274 ? 0.911   -6.711  35.343   1.00 78.62  ? 276 THR   D CA    1 
ATOM   9059  C  C     . THR   C 2  274 ? -0.092  -7.146  36.420   1.00 79.98  ? 276 THR   D C     1 
ATOM   9060  O  O     . THR   C 2  274 ? 0.185   -8.039  37.232   1.00 89.78  ? 276 THR   D O     1 
ATOM   9061  C  CB    . THR   C 2  274 ? 1.688   -5.468  35.829   1.00 77.25  ? 276 THR   D CB    1 
ATOM   9062  O  OG1   . THR   C 2  274 ? 0.779   -4.376  36.035   1.00 74.52  ? 276 THR   D OG1   1 
ATOM   9063  C  CG2   . THR   C 2  274 ? 2.771   -5.076  34.813   1.00 55.16  ? 276 THR   D CG2   1 
ATOM   9064  N  N     . ARG   C 2  282 ? 9.084   -2.262  34.716   1.00 115.98 ? 284 ARG   D N     1 
ATOM   9065  C  CA    . ARG   C 2  282 ? 9.704   -2.413  33.401   1.00 118.59 ? 284 ARG   D CA    1 
ATOM   9066  C  C     . ARG   C 2  282 ? 8.830   -1.780  32.295   1.00 114.44 ? 284 ARG   D C     1 
ATOM   9067  O  O     . ARG   C 2  282 ? 7.716   -2.240  32.030   1.00 108.08 ? 284 ARG   D O     1 
ATOM   9068  C  CB    . ARG   C 2  282 ? 9.970   -3.898  33.114   1.00 111.49 ? 284 ARG   D CB    1 
ATOM   9069  C  CG    . ARG   C 2  282 ? 10.602  -4.669  34.285   1.00 103.91 ? 284 ARG   D CG    1 
ATOM   9070  C  CD    . ARG   C 2  282 ? 11.706  -3.865  34.956   1.00 100.94 ? 284 ARG   D CD    1 
ATOM   9071  N  NE    . ARG   C 2  282 ? 12.584  -3.246  33.973   1.00 99.02  ? 284 ARG   D NE    1 
ATOM   9072  C  CZ    . ARG   C 2  282 ? 13.078  -2.020  34.077   1.00 100.72 ? 284 ARG   D CZ    1 
ATOM   9073  N  NH1   . ARG   C 2  282 ? 12.819  -1.256  35.124   1.00 92.59  ? 284 ARG   D NH1   1 
ATOM   9074  N  NH2   . ARG   C 2  282 ? 13.839  -1.542  33.096   1.00 111.11 ? 284 ARG   D NH2   1 
ATOM   9075  N  N     . ALA   C 2  283 ? 9.347   -0.726  31.655   1.00 105.29 ? 285 ALA   D N     1 
ATOM   9076  C  CA    . ALA   C 2  283 ? 8.579   0.097   30.721   1.00 98.21  ? 285 ALA   D CA    1 
ATOM   9077  C  C     . ALA   C 2  283 ? 8.925   -0.260  29.277   1.00 100.52 ? 285 ALA   D C     1 
ATOM   9078  O  O     . ALA   C 2  283 ? 10.094  -0.191  28.875   1.00 88.77  ? 285 ALA   D O     1 
ATOM   9079  C  CB    . ALA   C 2  283 ? 8.832   1.582   30.973   1.00 87.34  ? 285 ALA   D CB    1 
ATOM   9080  N  N     . LEU   C 2  284 ? 7.902   -0.602  28.495   1.00 95.02  ? 286 LEU   D N     1 
ATOM   9081  C  CA    . LEU   C 2  284 ? 8.059   -1.123  27.144   1.00 84.01  ? 286 LEU   D CA    1 
ATOM   9082  C  C     . LEU   C 2  284 ? 7.735   -0.055  26.103   1.00 77.94  ? 286 LEU   D C     1 
ATOM   9083  O  O     . LEU   C 2  284 ? 7.033   0.921   26.377   1.00 82.71  ? 286 LEU   D O     1 
ATOM   9084  C  CB    . LEU   C 2  284 ? 7.174   -2.353  26.939   1.00 78.17  ? 286 LEU   D CB    1 
ATOM   9085  C  CG    . LEU   C 2  284 ? 5.691   -2.208  27.281   1.00 79.72  ? 286 LEU   D CG    1 
ATOM   9086  C  CD1   . LEU   C 2  284 ? 4.935   -3.381  26.713   1.00 64.39  ? 286 LEU   D CD1   1 
ATOM   9087  C  CD2   . LEU   C 2  284 ? 5.453   -2.102  28.794   1.00 84.32  ? 286 LEU   D CD2   1 
ATOM   9088  N  N     . THR   C 2  285 ? 8.254   -0.262  24.890   1.00 72.97  ? 287 THR   D N     1 
ATOM   9089  C  CA    . THR   C 2  285 ? 8.290   0.790   23.877   1.00 81.99  ? 287 THR   D CA    1 
ATOM   9090  C  C     . THR   C 2  285 ? 6.913   1.020   23.250   1.00 68.21  ? 287 THR   D C     1 
ATOM   9091  O  O     . THR   C 2  285 ? 5.987   0.214   23.387   1.00 68.19  ? 287 THR   D O     1 
ATOM   9092  C  CB    . THR   C 2  285 ? 9.296   0.458   22.767   1.00 70.10  ? 287 THR   D CB    1 
ATOM   9093  O  OG1   . THR   C 2  285 ? 8.869   -0.715  22.060   1.00 65.40  ? 287 THR   D OG1   1 
ATOM   9094  C  CG2   . THR   C 2  285 ? 10.690  0.231   23.338   1.00 66.28  ? 287 THR   D CG2   1 
ATOM   9095  N  N     . VAL   C 2  286 ? 6.795   2.156   22.548   1.00 63.88  ? 288 VAL   D N     1 
ATOM   9096  C  CA    . VAL   C 2  286 ? 5.592   2.411   21.752   1.00 59.20  ? 288 VAL   D CA    1 
ATOM   9097  C  C     . VAL   C 2  286 ? 5.349   1.273   20.779   1.00 59.18  ? 288 VAL   D C     1 
ATOM   9098  O  O     . VAL   C 2  286 ? 4.194   0.837   20.636   1.00 56.27  ? 288 VAL   D O     1 
ATOM   9099  C  CB    . VAL   C 2  286 ? 5.688   3.782   21.068   1.00 56.57  ? 288 VAL   D CB    1 
ATOM   9100  C  CG1   . VAL   C 2  286 ? 4.498   4.000   20.146   1.00 53.58  ? 288 VAL   D CG1   1 
ATOM   9101  C  CG2   . VAL   C 2  286 ? 5.778   4.905   22.103   1.00 42.58  ? 288 VAL   D CG2   1 
ATOM   9102  N  N     . PRO   C 2  287 ? 6.358   0.746   20.083   1.00 59.70  ? 289 PRO   D N     1 
ATOM   9103  C  CA    . PRO   C 2  287 ? 6.129   -0.406  19.203   1.00 50.84  ? 289 PRO   D CA    1 
ATOM   9104  C  C     . PRO   C 2  287 ? 5.618   -1.641  19.917   1.00 61.54  ? 289 PRO   D C     1 
ATOM   9105  O  O     . PRO   C 2  287 ? 4.850   -2.411  19.320   1.00 63.69  ? 289 PRO   D O     1 
ATOM   9106  C  CB    . PRO   C 2  287 ? 7.512   -0.639  18.593   1.00 51.34  ? 289 PRO   D CB    1 
ATOM   9107  C  CG    . PRO   C 2  287 ? 8.150   0.725   18.603   1.00 52.26  ? 289 PRO   D CG    1 
ATOM   9108  C  CD    . PRO   C 2  287 ? 7.676   1.366   19.858   1.00 63.33  ? 289 PRO   D CD    1 
ATOM   9109  N  N     . GLU   C 2  288 ? 6.029   -1.868  21.168   1.00 66.74  ? 290 GLU   D N     1 
ATOM   9110  C  CA    . GLU   C 2  288 ? 5.630   -3.081  21.881   1.00 69.74  ? 290 GLU   D CA    1 
ATOM   9111  C  C     . GLU   C 2  288 ? 4.222   -2.956  22.451   1.00 73.42  ? 290 GLU   D C     1 
ATOM   9112  O  O     . GLU   C 2  288 ? 3.415   -3.895  22.351   1.00 69.66  ? 290 GLU   D O     1 
ATOM   9113  C  CB    . GLU   C 2  288 ? 6.635   -3.395  22.990   1.00 70.37  ? 290 GLU   D CB    1 
ATOM   9114  C  CG    . GLU   C 2  288 ? 7.936   -3.997  22.483   1.00 75.07  ? 290 GLU   D CG    1 
ATOM   9115  C  CD    . GLU   C 2  288 ? 9.044   -3.977  23.525   1.00 70.29  ? 290 GLU   D CD    1 
ATOM   9116  O  OE1   . GLU   C 2  288 ? 9.228   -2.927  24.183   1.00 62.40  ? 290 GLU   D OE1   1 
ATOM   9117  O  OE2   . GLU   C 2  288 ? 9.730   -5.012  23.679   1.00 72.37  ? 290 GLU   D OE2   1 
ATOM   9118  N  N     . LEU   C 2  289 ? 3.909   -1.809  23.056   1.00 67.08  ? 291 LEU   D N     1 
ATOM   9119  C  CA    . LEU   C 2  289 ? 2.515   -1.490  23.331   1.00 64.17  ? 291 LEU   D CA    1 
ATOM   9120  C  C     . LEU   C 2  289 ? 1.648   -1.774  22.111   1.00 65.92  ? 291 LEU   D C     1 
ATOM   9121  O  O     . LEU   C 2  289 ? 0.637   -2.483  22.197   1.00 58.98  ? 291 LEU   D O     1 
ATOM   9122  C  CB    . LEU   C 2  289 ? 2.392   -0.028  23.747   1.00 58.93  ? 291 LEU   D CB    1 
ATOM   9123  C  CG    . LEU   C 2  289 ? 2.643   0.190   25.229   1.00 56.90  ? 291 LEU   D CG    1 
ATOM   9124  C  CD1   . LEU   C 2  289 ? 2.565   1.654   25.575   1.00 47.35  ? 291 LEU   D CD1   1 
ATOM   9125  C  CD2   . LEU   C 2  289 ? 1.616   -0.608  25.995   1.00 60.01  ? 291 LEU   D CD2   1 
ATOM   9126  N  N     . THR   C 2  290 ? 2.062   -1.258  20.948   1.00 64.22  ? 292 THR   D N     1 
ATOM   9127  C  CA    . THR   C 2  290 ? 1.193   -1.283  19.779   1.00 57.32  ? 292 THR   D CA    1 
ATOM   9128  C  C     . THR   C 2  290 ? 0.994   -2.690  19.236   1.00 64.41  ? 292 THR   D C     1 
ATOM   9129  O  O     . THR   C 2  290 ? -0.096  -3.007  18.750   1.00 68.31  ? 292 THR   D O     1 
ATOM   9130  C  CB    . THR   C 2  290 ? 1.743   -0.364  18.696   1.00 53.40  ? 292 THR   D CB    1 
ATOM   9131  O  OG1   . THR   C 2  290 ? 1.409   0.990   19.018   1.00 53.69  ? 292 THR   D OG1   1 
ATOM   9132  C  CG2   . THR   C 2  290 ? 1.140   -0.716  17.353   1.00 52.09  ? 292 THR   D CG2   1 
ATOM   9133  N  N     . GLN   C 2  291 ? 2.012   -3.549  19.307   1.00 72.01  ? 293 GLN   D N     1 
ATOM   9134  C  CA    . GLN   C 2  291 ? 1.838   -4.917  18.833   1.00 62.77  ? 293 GLN   D CA    1 
ATOM   9135  C  C     . GLN   C 2  291 ? 1.254   -5.838  19.895   1.00 61.24  ? 293 GLN   D C     1 
ATOM   9136  O  O     . GLN   C 2  291 ? 0.604   -6.829  19.548   1.00 56.89  ? 293 GLN   D O     1 
ATOM   9137  C  CB    . GLN   C 2  291 ? 3.164   -5.483  18.330   1.00 63.42  ? 293 GLN   D CB    1 
ATOM   9138  C  CG    . GLN   C 2  291 ? 4.331   -5.239  19.256   1.00 74.33  ? 293 GLN   D CG    1 
ATOM   9139  C  CD    . GLN   C 2  291 ? 5.459   -6.214  18.996   1.00 89.26  ? 293 GLN   D CD    1 
ATOM   9140  O  OE1   . GLN   C 2  291 ? 5.314   -7.134  18.177   1.00 86.96  ? 293 GLN   D OE1   1 
ATOM   9141  N  NE2   . GLN   C 2  291 ? 6.589   -6.028  19.690   1.00 72.01  ? 293 GLN   D NE2   1 
ATOM   9142  N  N     . GLN   C 2  292 ? 1.450   -5.535  21.179   1.00 62.64  ? 294 GLN   D N     1 
ATOM   9143  C  CA    . GLN   C 2  292 ? 0.811   -6.334  22.221   1.00 63.95  ? 294 GLN   D CA    1 
ATOM   9144  C  C     . GLN   C 2  292 ? -0.712  -6.228  22.144   1.00 66.44  ? 294 GLN   D C     1 
ATOM   9145  O  O     . GLN   C 2  292 ? -1.416  -7.237  21.996   1.00 58.99  ? 294 GLN   D O     1 
ATOM   9146  C  CB    . GLN   C 2  292 ? 1.311   -5.901  23.595   1.00 56.08  ? 294 GLN   D CB    1 
ATOM   9147  C  CG    . GLN   C 2  292 ? 2.578   -6.598  24.045   1.00 64.14  ? 294 GLN   D CG    1 
ATOM   9148  C  CD    . GLN   C 2  292 ? 2.894   -6.351  25.524   1.00 79.16  ? 294 GLN   D CD    1 
ATOM   9149  O  OE1   . GLN   C 2  292 ? 2.059   -6.583  26.410   1.00 78.21  ? 294 GLN   D OE1   1 
ATOM   9150  N  NE2   . GLN   C 2  292 ? 4.104   -5.882  25.792   1.00 59.61  ? 294 GLN   D NE2   1 
ATOM   9151  N  N     . MET   C 2  293 ? -1.243  -5.001  22.227   1.00 68.98  ? 295 MET   D N     1 
ATOM   9152  C  CA    . MET   C 2  293 ? -2.688  -4.818  22.339   1.00 63.60  ? 295 MET   D CA    1 
ATOM   9153  C  C     . MET   C 2  293 ? -3.450  -5.391  21.154   1.00 60.31  ? 295 MET   D C     1 
ATOM   9154  O  O     . MET   C 2  293 ? -4.684  -5.410  21.189   1.00 63.42  ? 295 MET   D O     1 
ATOM   9155  C  CB    . MET   C 2  293 ? -3.043  -3.331  22.536   1.00 57.85  ? 295 MET   D CB    1 
ATOM   9156  C  CG    . MET   C 2  293 ? -2.851  -2.428  21.312   1.00 64.94  ? 295 MET   D CG    1 
ATOM   9157  S  SD    . MET   C 2  293 ? -3.045  -0.648  21.662   1.00 57.49  ? 295 MET   D SD    1 
ATOM   9158  C  CE    . MET   C 2  293 ? -4.683  -0.635  22.337   1.00 42.54  ? 295 MET   D CE    1 
ATOM   9159  N  N     . PHE   C 2  294 ? -2.763  -5.870  20.118   1.00 61.50  ? 296 PHE   D N     1 
ATOM   9160  C  CA    . PHE   C 2  294 ? -3.412  -6.602  19.036   1.00 66.37  ? 296 PHE   D CA    1 
ATOM   9161  C  C     . PHE   C 2  294 ? -3.118  -8.099  19.101   1.00 67.04  ? 296 PHE   D C     1 
ATOM   9162  O  O     . PHE   C 2  294 ? -3.476  -8.847  18.174   1.00 56.37  ? 296 PHE   D O     1 
ATOM   9163  C  CB    . PHE   C 2  294 ? -2.999  -6.031  17.677   1.00 64.11  ? 296 PHE   D CB    1 
ATOM   9164  C  CG    . PHE   C 2  294 ? -3.610  -4.697  17.364   1.00 54.04  ? 296 PHE   D CG    1 
ATOM   9165  C  CD1   . PHE   C 2  294 ? -3.053  -3.534  17.858   1.00 55.76  ? 296 PHE   D CD1   1 
ATOM   9166  C  CD2   . PHE   C 2  294 ? -4.735  -4.609  16.564   1.00 53.20  ? 296 PHE   D CD2   1 
ATOM   9167  C  CE1   . PHE   C 2  294 ? -3.607  -2.308  17.569   1.00 48.31  ? 296 PHE   D CE1   1 
ATOM   9168  C  CE2   . PHE   C 2  294 ? -5.296  -3.387  16.274   1.00 46.04  ? 296 PHE   D CE2   1 
ATOM   9169  C  CZ    . PHE   C 2  294 ? -4.732  -2.236  16.779   1.00 46.20  ? 296 PHE   D CZ    1 
ATOM   9170  N  N     . ASP   C 2  295 ? -2.465  -8.547  20.172   1.00 72.94  ? 297 ASP   D N     1 
ATOM   9171  C  CA    . ASP   C 2  295 ? -2.207  -9.958  20.412   1.00 65.55  ? 297 ASP   D CA    1 
ATOM   9172  C  C     . ASP   C 2  295 ? -3.352  -10.516 21.243   1.00 62.06  ? 297 ASP   D C     1 
ATOM   9173  O  O     . ASP   C 2  295 ? -3.681  -9.963  22.298   1.00 72.28  ? 297 ASP   D O     1 
ATOM   9174  C  CB    . ASP   C 2  295 ? -0.874  -10.133 21.143   1.00 65.76  ? 297 ASP   D CB    1 
ATOM   9175  C  CG    . ASP   C 2  295 ? -0.560  -11.590 21.471   1.00 79.63  ? 297 ASP   D CG    1 
ATOM   9176  O  OD1   . ASP   C 2  295 ? -1.087  -12.499 20.780   1.00 69.84  ? 297 ASP   D OD1   1 
ATOM   9177  O  OD2   . ASP   C 2  295 ? 0.218   -11.818 22.432   1.00 74.63  ? 297 ASP   D OD2   1 
ATOM   9178  N  N     . SER   C 2  296 ? -3.959  -11.599 20.772   1.00 54.68  ? 298 SER   D N     1 
ATOM   9179  C  CA    . SER   C 2  296 ? -5.059  -12.220 21.497   1.00 60.76  ? 298 SER   D CA    1 
ATOM   9180  C  C     . SER   C 2  296 ? -4.733  -12.526 22.957   1.00 47.92  ? 298 SER   D C     1 
ATOM   9181  O  O     . SER   C 2  296 ? -5.643  -12.810 23.728   1.00 54.28  ? 298 SER   D O     1 
ATOM   9182  C  CB    . SER   C 2  296 ? -5.508  -13.504 20.794   1.00 59.20  ? 298 SER   D CB    1 
ATOM   9183  O  OG    . SER   C 2  296 ? -6.617  -14.082 21.459   0.07 57.73  ? 298 SER   D OG    1 
ATOM   9184  N  N     . LYS   C 2  297 ? -3.469  -12.475 23.356   1.00 48.85  ? 299 LYS   D N     1 
ATOM   9185  C  CA    . LYS   C 2  297 ? -3.100  -12.773 24.735   1.00 62.90  ? 299 LYS   D CA    1 
ATOM   9186  C  C     . LYS   C 2  297 ? -3.126  -11.550 25.638   1.00 63.23  ? 299 LYS   D C     1 
ATOM   9187  O  O     . LYS   C 2  297 ? -2.640  -11.633 26.773   1.00 68.28  ? 299 LYS   D O     1 
ATOM   9188  C  CB    . LYS   C 2  297 ? -1.711  -13.424 24.803   1.00 71.87  ? 299 LYS   D CB    1 
ATOM   9189  C  CG    . LYS   C 2  297 ? -1.678  -14.923 24.465   1.00 69.30  ? 299 LYS   D CG    1 
ATOM   9190  C  CD    . LYS   C 2  297 ? -0.250  -15.469 24.465   1.00 77.22  ? 299 LYS   D CD    1 
ATOM   9191  C  CE    . LYS   C 2  297 ? 0.583   -14.873 23.329   1.00 77.68  ? 299 LYS   D CE    1 
ATOM   9192  N  NZ    . LYS   C 2  297 ? 2.054   -14.992 23.563   1.00 74.65  ? 299 LYS   D NZ    1 
ATOM   9193  N  N     . ASN   C 2  298 ? -3.646  -10.413 25.159   1.00 63.05  ? 300 ASN   D N     1 
ATOM   9194  C  CA    . ASN   C 2  298 ? -4.039  -9.311  26.036   1.00 53.61  ? 300 ASN   D CA    1 
ATOM   9195  C  C     . ASN   C 2  298 ? -5.523  -8.992  25.919   1.00 52.26  ? 300 ASN   D C     1 
ATOM   9196  O  O     . ASN   C 2  298 ? -5.972  -7.997  26.492   1.00 55.53  ? 300 ASN   D O     1 
ATOM   9197  C  CB    . ASN   C 2  298 ? -3.233  -8.040  25.766   1.00 51.76  ? 300 ASN   D CB    1 
ATOM   9198  C  CG    . ASN   C 2  298 ? -1.751  -8.261  25.855   1.00 53.20  ? 300 ASN   D CG    1 
ATOM   9199  O  OD1   . ASN   C 2  298 ? -1.239  -9.213  25.285   1.00 49.43  ? 300 ASN   D OD1   1 
ATOM   9200  N  ND2   . ASN   C 2  298 ? -1.045  -7.370  26.561   1.00 47.04  ? 300 ASN   D ND2   1 
ATOM   9201  N  N     . MET   C 2  299 ? -6.294  -9.813  25.201   1.00 54.41  ? 301 MET   D N     1 
ATOM   9202  C  CA    . MET   C 2  299 ? -7.735  -9.604  25.060   1.00 56.32  ? 301 MET   D CA    1 
ATOM   9203  C  C     . MET   C 2  299 ? -8.462  -10.011 26.345   1.00 58.19  ? 301 MET   D C     1 
ATOM   9204  O  O     . MET   C 2  299 ? -8.429  -11.183 26.736   1.00 63.62  ? 301 MET   D O     1 
ATOM   9205  C  CB    . MET   C 2  299 ? -8.275  -10.400 23.870   1.00 54.68  ? 301 MET   D CB    1 
ATOM   9206  C  CG    . MET   C 2  299 ? -7.634  -10.100 22.490   1.00 60.66  ? 301 MET   D CG    1 
ATOM   9207  S  SD    . MET   C 2  299 ? -8.011  -8.471  21.780   1.00 56.18  ? 301 MET   D SD    1 
ATOM   9208  C  CE    . MET   C 2  299 ? -6.996  -7.412  22.803   1.00 47.47  ? 301 MET   D CE    1 
ATOM   9209  N  N     . MET   C 2  300 ? -9.139  -9.051  26.994   1.00 54.45  ? 302 MET   D N     1 
ATOM   9210  C  CA    . MET   C 2  300 ? -9.927  -9.371  28.178   1.00 49.44  ? 302 MET   D CA    1 
ATOM   9211  C  C     . MET   C 2  300 ? -11.138 -10.227 27.872   1.00 51.65  ? 302 MET   D C     1 
ATOM   9212  O  O     . MET   C 2  300 ? -11.915 -10.474 28.794   1.00 54.54  ? 302 MET   D O     1 
ATOM   9213  C  CB    . MET   C 2  300 ? -10.394 -8.113  28.893   1.00 43.53  ? 302 MET   D CB    1 
ATOM   9214  C  CG    . MET   C 2  300 ? -9.277  -7.211  29.345   1.00 49.62  ? 302 MET   D CG    1 
ATOM   9215  S  SD    . MET   C 2  300 ? -8.115  -8.029  30.435   1.00 52.12  ? 302 MET   D SD    1 
ATOM   9216  C  CE    . MET   C 2  300 ? -6.791  -6.796  30.457   1.00 46.60  ? 302 MET   D CE    1 
ATOM   9217  N  N     . ALA   C 2  301 ? -11.319 -10.680 26.632   1.00 52.82  ? 303 ALA   D N     1 
ATOM   9218  C  CA    . ALA   C 2  301 ? -12.343 -11.653 26.277   1.00 52.83  ? 303 ALA   D CA    1 
ATOM   9219  C  C     . ALA   C 2  301 ? -11.675 -12.840 25.600   1.00 58.61  ? 303 ALA   D C     1 
ATOM   9220  O  O     . ALA   C 2  301 ? -10.831 -12.661 24.715   1.00 56.56  ? 303 ALA   D O     1 
ATOM   9221  C  CB    . ALA   C 2  301 ? -13.399 -11.045 25.354   1.00 53.18  ? 303 ALA   D CB    1 
ATOM   9222  N  N     . ALA   C 2  302 ? -12.055 -14.049 26.018   1.00 63.36  ? 304 ALA   D N     1 
ATOM   9223  C  CA    . ALA   C 2  302 ? -11.480 -15.282 25.489   1.00 62.59  ? 304 ALA   D CA    1 
ATOM   9224  C  C     . ALA   C 2  302 ? -11.750 -15.413 23.998   1.00 63.18  ? 304 ALA   D C     1 
ATOM   9225  O  O     . ALA   C 2  302 ? -12.475 -16.321 23.563   1.00 49.52  ? 304 ALA   D O     1 
ATOM   9226  C  CB    . ALA   C 2  302 ? -12.034 -16.504 26.226   1.00 61.86  ? 304 ALA   D CB    1 
ATOM   9227  N  N     . CYS   C 2  303 ? -11.162 -14.508 23.215   1.00 68.59  ? 305 CYS   D N     1 
ATOM   9228  C  CA    . CYS   C 2  303 ? -11.326 -14.496 21.772   1.00 66.59  ? 305 CYS   D CA    1 
ATOM   9229  C  C     . CYS   C 2  303 ? -9.988  -14.237 21.103   1.00 55.85  ? 305 CYS   D C     1 
ATOM   9230  O  O     . CYS   C 2  303 ? -9.122  -13.541 21.645   1.00 55.22  ? 305 CYS   D O     1 
ATOM   9231  C  CB    . CYS   C 2  303 ? -12.340 -13.441 21.334   1.00 60.43  ? 305 CYS   D CB    1 
ATOM   9232  S  SG    . CYS   C 2  303 ? -14.013 -14.007 21.547   1.00 73.83  ? 305 CYS   D SG    1 
ATOM   9233  N  N     . ASP   C 2  304 ? -9.839  -14.801 19.912   1.00 54.33  ? 306 ASP   D N     1 
ATOM   9234  C  CA    . ASP   C 2  304 ? -8.643  -14.607 19.100   1.00 63.68  ? 306 ASP   D CA    1 
ATOM   9235  C  C     . ASP   C 2  304 ? -8.973  -13.726 17.899   1.00 60.28  ? 306 ASP   D C     1 
ATOM   9236  O  O     . ASP   C 2  304 ? -9.763  -14.142 17.031   1.00 56.81  ? 306 ASP   D O     1 
ATOM   9237  C  CB    . ASP   C 2  304 ? -8.089  -15.963 18.649   1.00 58.35  ? 306 ASP   D CB    1 
ATOM   9238  C  CG    . ASP   C 2  304 ? -7.056  -15.844 17.560   1.00 55.85  ? 306 ASP   D CG    1 
ATOM   9239  O  OD1   . ASP   C 2  304 ? -6.072  -15.080 17.724   1.00 54.69  ? 306 ASP   D OD1   1 
ATOM   9240  O  OD2   . ASP   C 2  304 ? -7.238  -16.535 16.538   1.00 58.34  ? 306 ASP   D OD2   1 
ATOM   9241  N  N     . PRO   C 2  305 ? -8.413  -12.511 17.809   1.00 44.05  ? 307 PRO   D N     1 
ATOM   9242  C  CA    . PRO   C 2  305 ? -8.788  -11.611 16.700   1.00 49.55  ? 307 PRO   D CA    1 
ATOM   9243  C  C     . PRO   C 2  305 ? -8.385  -12.126 15.330   1.00 53.92  ? 307 PRO   D C     1 
ATOM   9244  O  O     . PRO   C 2  305 ? -9.112  -11.889 14.356   1.00 50.44  ? 307 PRO   D O     1 
ATOM   9245  C  CB    . PRO   C 2  305 ? -8.072  -10.299 17.048   1.00 46.98  ? 307 PRO   D CB    1 
ATOM   9246  C  CG    . PRO   C 2  305 ? -7.037  -10.662 18.077   1.00 50.53  ? 307 PRO   D CG    1 
ATOM   9247  C  CD    . PRO   C 2  305 ? -7.532  -11.867 18.794   1.00 52.22  ? 307 PRO   D CD    1 
ATOM   9248  N  N     . ARG   C 2  306 ? -7.255  -12.831 15.223   1.00 53.83  ? 308 ARG   D N     1 
ATOM   9249  C  CA    . ARG   C 2  306 ? -6.849  -13.478 13.980   1.00 46.19  ? 308 ARG   D CA    1 
ATOM   9250  C  C     . ARG   C 2  306 ? -7.886  -14.476 13.472   1.00 53.02  ? 308 ARG   D C     1 
ATOM   9251  O  O     . ARG   C 2  306 ? -7.673  -15.100 12.424   1.00 50.55  ? 308 ARG   D O     1 
ATOM   9252  C  CB    . ARG   C 2  306 ? -5.522  -14.206 14.163   1.00 51.25  ? 308 ARG   D CB    1 
ATOM   9253  C  CG    . ARG   C 2  306 ? -4.323  -13.475 13.659   1.00 51.96  ? 308 ARG   D CG    1 
ATOM   9254  C  CD    . ARG   C 2  306 ? -3.809  -12.500 14.672   1.00 50.60  ? 308 ARG   D CD    1 
ATOM   9255  N  NE    . ARG   C 2  306 ? -2.531  -11.958 14.239   1.00 52.58  ? 308 ARG   D NE    1 
ATOM   9256  C  CZ    . ARG   C 2  306 ? -2.038  -10.782 14.608   1.00 62.74  ? 308 ARG   D CZ    1 
ATOM   9257  N  NH1   . ARG   C 2  306 ? -2.707  -9.968  15.414   1.00 53.69  ? 308 ARG   D NH1   1 
ATOM   9258  N  NH2   . ARG   C 2  306 ? -0.838  -10.416 14.159   1.00 72.34  ? 308 ARG   D NH2   1 
ATOM   9259  N  N     . HIS   C 2  307 ? -8.994  -14.663 14.199   1.00 44.75  ? 309 HIS   D N     1 
ATOM   9260  C  CA    . HIS   C 2  307 ? -10.032 -15.592 13.766   1.00 47.94  ? 309 HIS   D CA    1 
ATOM   9261  C  C     . HIS   C 2  307 ? -11.252 -14.890 13.203   1.00 44.90  ? 309 HIS   D C     1 
ATOM   9262  O  O     . HIS   C 2  307 ? -12.206 -15.556 12.796   1.00 43.89  ? 309 HIS   D O     1 
ATOM   9263  C  CB    . HIS   C 2  307 ? -10.452 -16.506 14.922   1.00 53.70  ? 309 HIS   D CB    1 
ATOM   9264  C  CG    . HIS   C 2  307 ? -9.492  -17.627 15.191   1.00 56.74  ? 309 HIS   D CG    1 
ATOM   9265  N  ND1   . HIS   C 2  307 ? -9.355  -18.207 16.433   1.00 54.18  ? 309 HIS   D ND1   1 
ATOM   9266  C  CD2   . HIS   C 2  307 ? -8.625  -18.275 14.377   1.00 56.38  ? 309 HIS   D CD2   1 
ATOM   9267  C  CE1   . HIS   C 2  307 ? -8.447  -19.165 16.372   1.00 55.25  ? 309 HIS   D CE1   1 
ATOM   9268  N  NE2   . HIS   C 2  307 ? -7.986  -19.226 15.137   1.00 57.00  ? 309 HIS   D NE2   1 
ATOM   9269  N  N     . GLY   C 2  308 ? -11.253 -13.569 13.182   1.00 46.56  ? 310 GLY   D N     1 
ATOM   9270  C  CA    . GLY   C 2  308 ? -12.328 -12.822 12.565   1.00 49.27  ? 310 GLY   D CA    1 
ATOM   9271  C  C     . GLY   C 2  308 ? -11.798 -11.490 12.082   1.00 55.32  ? 310 GLY   D C     1 
ATOM   9272  O  O     . GLY   C 2  308 ? -10.580 -11.355 11.879   1.00 44.77  ? 310 GLY   D O     1 
ATOM   9273  N  N     . ARG   C 2  309 ? -12.683 -10.493 11.930   1.00 44.07  ? 311 ARG   D N     1 
ATOM   9274  C  CA    . ARG   C 2  309 ? -12.280 -9.171  11.473   1.00 42.60  ? 311 ARG   D CA    1 
ATOM   9275  C  C     . ARG   C 2  309 ? -12.830 -8.077  12.384   1.00 43.95  ? 311 ARG   D C     1 
ATOM   9276  O  O     . ARG   C 2  309 ? -13.948 -8.182  12.910   1.00 38.03  ? 311 ARG   D O     1 
ATOM   9277  C  CB    . ARG   C 2  309 ? -12.727 -8.939  10.015   1.00 38.16  ? 311 ARG   D CB    1 
ATOM   9278  C  CG    . ARG   C 2  309 ? -12.127 -9.949  9.027    1.00 40.70  ? 311 ARG   D CG    1 
ATOM   9279  C  CD    . ARG   C 2  309 ? -12.178 -9.455  7.592    1.00 45.25  ? 311 ARG   D CD    1 
ATOM   9280  N  NE    . ARG   C 2  309 ? -12.670 -10.472 6.667    1.00 49.41  ? 311 ARG   D NE    1 
ATOM   9281  C  CZ    . ARG   C 2  309 ? -11.923 -11.134 5.790    1.00 58.80  ? 311 ARG   D CZ    1 
ATOM   9282  N  NH1   . ARG   C 2  309 ? -10.616 -10.925 5.690    1.00 42.24  ? 311 ARG   D NH1   1 
ATOM   9283  N  NH2   . ARG   C 2  309 ? -12.502 -12.032 4.992    1.00 56.82  ? 311 ARG   D NH2   1 
ATOM   9284  N  N     . TYR   C 2  310 ? -12.024 -7.022  12.552   1.00 45.15  ? 312 TYR   D N     1 
ATOM   9285  C  CA    . TYR   C 2  310 ? -12.405 -5.792  13.249   1.00 37.81  ? 312 TYR   D CA    1 
ATOM   9286  C  C     . TYR   C 2  310 ? -13.322 -4.931  12.379   1.00 40.40  ? 312 TYR   D C     1 
ATOM   9287  O  O     . TYR   C 2  310 ? -12.883 -4.370  11.371   1.00 47.30  ? 312 TYR   D O     1 
ATOM   9288  C  CB    . TYR   C 2  310 ? -11.163 -4.986  13.601   1.00 39.41  ? 312 TYR   D CB    1 
ATOM   9289  C  CG    . TYR   C 2  310 ? -10.239 -5.616  14.607   1.00 44.41  ? 312 TYR   D CG    1 
ATOM   9290  C  CD1   . TYR   C 2  310 ? -10.721 -6.167  15.783   1.00 47.75  ? 312 TYR   D CD1   1 
ATOM   9291  C  CD2   . TYR   C 2  310 ? -8.873  -5.635  14.390   1.00 45.86  ? 312 TYR   D CD2   1 
ATOM   9292  C  CE1   . TYR   C 2  310 ? -9.859  -6.721  16.710   1.00 55.27  ? 312 TYR   D CE1   1 
ATOM   9293  C  CE2   . TYR   C 2  310 ? -8.007  -6.187  15.308   1.00 40.65  ? 312 TYR   D CE2   1 
ATOM   9294  C  CZ    . TYR   C 2  310 ? -8.501  -6.731  16.457   1.00 50.17  ? 312 TYR   D CZ    1 
ATOM   9295  O  OH    . TYR   C 2  310 ? -7.626  -7.271  17.362   1.00 59.28  ? 312 TYR   D OH    1 
ATOM   9296  N  N     . LEU   C 2  311 ? -14.592 -4.817  12.771   1.00 39.47  ? 313 LEU   D N     1 
ATOM   9297  C  CA    . LEU   C 2  311 ? -15.444 -3.760  12.236   1.00 37.38  ? 313 LEU   D CA    1 
ATOM   9298  C  C     . LEU   C 2  311 ? -14.923 -2.376  12.617   1.00 33.23  ? 313 LEU   D C     1 
ATOM   9299  O  O     . LEU   C 2  311 ? -15.022 -1.430  11.830   1.00 40.47  ? 313 LEU   D O     1 
ATOM   9300  C  CB    . LEU   C 2  311 ? -16.875 -3.936  12.748   1.00 32.76  ? 313 LEU   D CB    1 
ATOM   9301  C  CG    . LEU   C 2  311 ? -17.375 -5.367  12.585   1.00 41.17  ? 313 LEU   D CG    1 
ATOM   9302  C  CD1   . LEU   C 2  311 ? -18.743 -5.562  13.249   1.00 40.91  ? 313 LEU   D CD1   1 
ATOM   9303  C  CD2   . LEU   C 2  311 ? -17.429 -5.706  11.106   1.00 36.56  ? 313 LEU   D CD2   1 
ATOM   9304  N  N     . THR   C 2  312 ? -14.402 -2.232  13.833   1.00 35.32  ? 314 THR   D N     1 
ATOM   9305  C  CA    . THR   C 2  312 ? -13.953 -0.957  14.375   1.00 34.04  ? 314 THR   D CA    1 
ATOM   9306  C  C     . THR   C 2  312 ? -13.001 -1.226  15.520   1.00 29.12  ? 314 THR   D C     1 
ATOM   9307  O  O     . THR   C 2  312 ? -13.035 -2.288  16.138   1.00 36.06  ? 314 THR   D O     1 
ATOM   9308  C  CB    . THR   C 2  312 ? -15.100 -0.118  14.917   1.00 35.64  ? 314 THR   D CB    1 
ATOM   9309  O  OG1   . THR   C 2  312 ? -15.729 -0.876  15.941   1.00 25.11  ? 314 THR   D OG1   1 
ATOM   9310  C  CG2   . THR   C 2  312 ? -16.110 0.234   13.812   1.00 37.98  ? 314 THR   D CG2   1 
ATOM   9311  N  N     . VAL   C 2  313 ? -12.190 -0.225  15.830   1.00 25.50  ? 315 VAL   D N     1 
ATOM   9312  C  CA    . VAL   C 2  313 ? -11.192 -0.333  16.881   1.00 35.56  ? 315 VAL   D CA    1 
ATOM   9313  C  C     . VAL   C 2  313 ? -10.956 1.058   17.441   1.00 35.55  ? 315 VAL   D C     1 
ATOM   9314  O  O     . VAL   C 2  313 ? -10.886 2.033   16.691   1.00 41.03  ? 315 VAL   D O     1 
ATOM   9315  C  CB    . VAL   C 2  313 ? -9.878  -0.957  16.347   1.00 31.15  ? 315 VAL   D CB    1 
ATOM   9316  C  CG1   . VAL   C 2  313 ? -8.745  -0.838  17.378   1.00 26.76  ? 315 VAL   D CG1   1 
ATOM   9317  C  CG2   . VAL   C 2  313 ? -10.103 -2.399  15.954   1.00 32.69  ? 315 VAL   D CG2   1 
ATOM   9318  N  N     . ALA   C 2  314 ? -10.818 1.157   18.756   1.00 36.03  ? 316 ALA   D N     1 
ATOM   9319  C  CA    . ALA   C 2  314 ? -10.336 2.382   19.378   1.00 37.86  ? 316 ALA   D CA    1 
ATOM   9320  C  C     . ALA   C 2  314 ? -9.047  2.047   20.116   1.00 44.36  ? 316 ALA   D C     1 
ATOM   9321  O  O     . ALA   C 2  314 ? -8.975  1.031   20.806   1.00 41.41  ? 316 ALA   D O     1 
ATOM   9322  C  CB    . ALA   C 2  314 ? -11.387 2.989   20.320   1.00 23.73  ? 316 ALA   D CB    1 
ATOM   9323  N  N     . ALA   C 2  315 ? -8.024  2.875   19.940   1.00 51.59  ? 317 ALA   D N     1 
ATOM   9324  C  CA    . ALA   C 2  315 ? -6.740  2.719   20.611   1.00 43.63  ? 317 ALA   D CA    1 
ATOM   9325  C  C     . ALA   C 2  315 ? -6.511  3.935   21.500   1.00 38.02  ? 317 ALA   D C     1 
ATOM   9326  O  O     . ALA   C 2  315 ? -6.680  5.069   21.050   1.00 50.88  ? 317 ALA   D O     1 
ATOM   9327  C  CB    . ALA   C 2  315 ? -5.604  2.563   19.585   1.00 37.56  ? 317 ALA   D CB    1 
ATOM   9328  N  N     . ILE   C 2  316 ? -6.152  3.707   22.761   1.00 47.62  ? 318 ILE   D N     1 
ATOM   9329  C  CA    . ILE   C 2  316 ? -5.905  4.786   23.716   1.00 43.80  ? 318 ILE   D CA    1 
ATOM   9330  C  C     . ILE   C 2  316 ? -4.507  4.604   24.303   1.00 44.26  ? 318 ILE   D C     1 
ATOM   9331  O  O     . ILE   C 2  316 ? -4.187  3.538   24.840   1.00 51.50  ? 318 ILE   D O     1 
ATOM   9332  C  CB    . ILE   C 2  316 ? -6.970  4.814   24.834   1.00 42.22  ? 318 ILE   D CB    1 
ATOM   9333  C  CG1   . ILE   C 2  316 ? -8.358  4.550   24.252   1.00 36.25  ? 318 ILE   D CG1   1 
ATOM   9334  C  CG2   . ILE   C 2  316 ? -6.936  6.149   25.577   1.00 32.73  ? 318 ILE   D CG2   1 
ATOM   9335  C  CD1   . ILE   C 2  316 ? -8.798  5.577   23.231   0.00 41.55  ? 318 ILE   D CD1   1 
ATOM   9336  N  N     . PHE   C 2  317 ? -3.682  5.641   24.205   1.00 44.58  ? 319 PHE   D N     1 
ATOM   9337  C  CA    . PHE   C 2  317 ? -2.303  5.619   24.676   1.00 41.55  ? 319 PHE   D CA    1 
ATOM   9338  C  C     . PHE   C 2  317 ? -2.138  6.606   25.818   1.00 48.62  ? 319 PHE   D C     1 
ATOM   9339  O  O     . PHE   C 2  317 ? -2.522  7.774   25.691   1.00 51.39  ? 319 PHE   D O     1 
ATOM   9340  C  CB    . PHE   C 2  317 ? -1.339  5.969   23.542   1.00 40.08  ? 319 PHE   D CB    1 
ATOM   9341  C  CG    . PHE   C 2  317 ? -1.128  4.848   22.566   1.00 46.35  ? 319 PHE   D CG    1 
ATOM   9342  C  CD1   . PHE   C 2  317 ? -0.123  3.917   22.769   1.00 42.28  ? 319 PHE   D CD1   1 
ATOM   9343  C  CD2   . PHE   C 2  317 ? -1.931  4.721   21.454   1.00 44.70  ? 319 PHE   D CD2   1 
ATOM   9344  C  CE1   . PHE   C 2  317 ? 0.079   2.889   21.896   1.00 43.31  ? 319 PHE   D CE1   1 
ATOM   9345  C  CE2   . PHE   C 2  317 ? -1.734  3.688   20.562   1.00 50.29  ? 319 PHE   D CE2   1 
ATOM   9346  C  CZ    . PHE   C 2  317 ? -0.727  2.769   20.785   1.00 60.46  ? 319 PHE   D CZ    1 
ATOM   9347  N  N     . ARG   C 2  318 ? -1.547  6.150   26.921   1.00 53.25  ? 320 ARG   D N     1 
ATOM   9348  C  CA    . ARG   C 2  318 ? -1.375  6.971   28.112   1.00 52.28  ? 320 ARG   D CA    1 
ATOM   9349  C  C     . ARG   C 2  318 ? 0.096   7.028   28.499   1.00 59.15  ? 320 ARG   D C     1 
ATOM   9350  O  O     . ARG   C 2  318 ? 0.815   6.031   28.396   1.00 52.43  ? 320 ARG   D O     1 
ATOM   9351  C  CB    . ARG   C 2  318 ? -2.201  6.429   29.276   1.00 52.47  ? 320 ARG   D CB    1 
ATOM   9352  C  CG    . ARG   C 2  318 ? -3.439  5.673   28.859   1.00 54.51  ? 320 ARG   D CG    1 
ATOM   9353  C  CD    . ARG   C 2  318 ? -4.287  5.385   30.062   1.00 59.40  ? 320 ARG   D CD    1 
ATOM   9354  N  NE    . ARG   C 2  318 ? -4.496  6.608   30.825   1.00 64.31  ? 320 ARG   D NE    1 
ATOM   9355  C  CZ    . ARG   C 2  318 ? -5.094  6.659   32.006   1.00 59.27  ? 320 ARG   D CZ    1 
ATOM   9356  N  NH1   . ARG   C 2  318 ? -5.542  5.564   32.599   1.00 56.89  ? 320 ARG   D NH1   1 
ATOM   9357  N  NH2   . ARG   C 2  318 ? -5.246  7.839   32.606   1.00 63.90  ? 320 ARG   D NH2   1 
ATOM   9358  N  N     . GLY   C 2  319 ? 0.531   8.195   28.964   1.00 60.95  ? 321 GLY   D N     1 
ATOM   9359  C  CA    . GLY   C 2  319 ? 1.922   8.442   29.264   1.00 66.66  ? 321 GLY   D CA    1 
ATOM   9360  C  C     . GLY   C 2  319 ? 2.589   9.303   28.206   1.00 64.41  ? 321 GLY   D C     1 
ATOM   9361  O  O     . GLY   C 2  319 ? 2.125   9.422   27.070   1.00 50.45  ? 321 GLY   D O     1 
ATOM   9362  N  N     . ARG   C 2  320 ? 3.707   9.922   28.595   1.00 70.29  ? 322 ARG   D N     1 
ATOM   9363  C  CA    . ARG   C 2  320 ? 4.421   10.813  27.691   1.00 72.78  ? 322 ARG   D CA    1 
ATOM   9364  C  C     . ARG   C 2  320 ? 5.176   10.009  26.639   1.00 61.68  ? 322 ARG   D C     1 
ATOM   9365  O  O     . ARG   C 2  320 ? 5.822   9.002   26.942   1.00 61.99  ? 322 ARG   D O     1 
ATOM   9366  C  CB    . ARG   C 2  320 ? 5.385   11.724  28.459   1.00 69.41  ? 322 ARG   D CB    1 
ATOM   9367  C  CG    . ARG   C 2  320 ? 5.896   12.897  27.611   1.00 82.04  ? 322 ARG   D CG    1 
ATOM   9368  C  CD    . ARG   C 2  320 ? 6.888   13.807  28.344   1.00 95.29  ? 322 ARG   D CD    1 
ATOM   9369  N  NE    . ARG   C 2  320 ? 7.568   14.715  27.421   1.00 91.24  ? 322 ARG   D NE    1 
ATOM   9370  C  CZ    . ARG   C 2  320 ? 7.050   15.849  26.965   1.00 92.08  ? 322 ARG   D CZ    1 
ATOM   9371  N  NH1   . ARG   C 2  320 ? 5.851   16.263  27.345   1.00 95.40  ? 322 ARG   D NH1   1 
ATOM   9372  N  NH2   . ARG   C 2  320 ? 7.751   16.584  26.102   1.00 69.46  ? 322 ARG   D NH2   1 
ATOM   9373  N  N     . MET   C 2  321 ? 5.085   10.455  25.392   1.00 54.78  ? 323 MET   D N     1 
ATOM   9374  C  CA    . MET   C 2  321 ? 5.619   9.678   24.280   1.00 62.09  ? 323 MET   D CA    1 
ATOM   9375  C  C     . MET   C 2  321 ? 5.482   10.501  23.001   1.00 63.56  ? 323 MET   D C     1 
ATOM   9376  O  O     . MET   C 2  321 ? 4.924   11.605  22.998   1.00 65.95  ? 323 MET   D O     1 
ATOM   9377  C  CB    . MET   C 2  321 ? 4.903   8.332   24.168   1.00 47.76  ? 323 MET   D CB    1 
ATOM   9378  C  CG    . MET   C 2  321 ? 3.425   8.489   23.843   1.00 52.15  ? 323 MET   D CG    1 
ATOM   9379  S  SD    . MET   C 2  321 ? 2.471   6.960   23.921   1.00 52.72  ? 323 MET   D SD    1 
ATOM   9380  C  CE    . MET   C 2  321 ? 2.428   6.687   25.687   1.00 64.72  ? 323 MET   D CE    1 
ATOM   9381  N  N     . SER   C 2  322 ? 6.000   9.938   21.908   1.00 63.98  ? 324 SER   D N     1 
ATOM   9382  C  CA    . SER   C 2  322 ? 6.015   10.576  20.589   1.00 54.51  ? 324 SER   D CA    1 
ATOM   9383  C  C     . SER   C 2  322 ? 4.727   10.221  19.862   1.00 59.19  ? 324 SER   D C     1 
ATOM   9384  O  O     . SER   C 2  322 ? 4.565   9.099   19.372   1.00 50.22  ? 324 SER   D O     1 
ATOM   9385  C  CB    . SER   C 2  322 ? 7.228   10.116  19.786   1.00 50.13  ? 324 SER   D CB    1 
ATOM   9386  O  OG    . SER   C 2  322 ? 7.338   10.813  18.557   1.00 61.74  ? 324 SER   D OG    1 
ATOM   9387  N  N     . MET   C 2  323 ? 3.790   11.170  19.804   1.00 59.77  ? 325 MET   D N     1 
ATOM   9388  C  CA    . MET   C 2  323 ? 2.627   10.956  18.954   1.00 57.91  ? 325 MET   D CA    1 
ATOM   9389  C  C     . MET   C 2  323 ? 3.059   10.591  17.541   1.00 53.34  ? 325 MET   D C     1 
ATOM   9390  O  O     . MET   C 2  323 ? 2.382   9.807   16.862   1.00 47.98  ? 325 MET   D O     1 
ATOM   9391  C  CB    . MET   C 2  323 ? 1.736   12.196  18.940   1.00 51.76  ? 325 MET   D CB    1 
ATOM   9392  C  CG    . MET   C 2  323 ? 0.656   12.204  20.003   1.00 51.93  ? 325 MET   D CG    1 
ATOM   9393  S  SD    . MET   C 2  323 ? -0.865  12.860  19.284   1.00 78.33  ? 325 MET   D SD    1 
ATOM   9394  C  CE    . MET   C 2  323 ? -0.241  14.263  18.343   1.00 58.91  ? 325 MET   D CE    1 
ATOM   9395  N  N     . LYS   C 2  324 ? 4.201   11.128  17.092   1.00 56.67  ? 326 LYS   D N     1 
ATOM   9396  C  CA    . LYS   C 2  324 ? 4.719   10.774  15.777   1.00 50.45  ? 326 LYS   D CA    1 
ATOM   9397  C  C     . LYS   C 2  324 ? 5.081   9.295   15.718   1.00 47.80  ? 326 LYS   D C     1 
ATOM   9398  O  O     . LYS   C 2  324 ? 4.760   8.612   14.741   1.00 52.32  ? 326 LYS   D O     1 
ATOM   9399  C  CB    . LYS   C 2  324 ? 5.920   11.652  15.432   1.00 56.65  ? 326 LYS   D CB    1 
ATOM   9400  C  CG    . LYS   C 2  324 ? 6.280   11.663  13.947   1.00 59.71  ? 326 LYS   D CG    1 
ATOM   9401  C  CD    . LYS   C 2  324 ? 7.601   12.380  13.675   1.00 63.49  ? 326 LYS   D CD    1 
ATOM   9402  C  CE    . LYS   C 2  324 ? 8.036   12.233  12.213   1.00 66.52  ? 326 LYS   D CE    1 
ATOM   9403  N  NZ    . LYS   C 2  324 ? 9.288   12.999  11.907   1.00 79.89  ? 326 LYS   D NZ    1 
ATOM   9404  N  N     . GLU   C 2  325 ? 5.722   8.775   16.766   1.00 46.20  ? 327 GLU   D N     1 
ATOM   9405  C  CA    . GLU   C 2  325 ? 5.964   7.332   16.850   1.00 45.60  ? 327 GLU   D CA    1 
ATOM   9406  C  C     . GLU   C 2  325 ? 4.650   6.557   16.904   1.00 42.33  ? 327 GLU   D C     1 
ATOM   9407  O  O     . GLU   C 2  325 ? 4.466   5.574   16.181   1.00 43.81  ? 327 GLU   D O     1 
ATOM   9408  C  CB    . GLU   C 2  325 ? 6.839   7.021   18.075   1.00 51.02  ? 327 GLU   D CB    1 
ATOM   9409  C  CG    . GLU   C 2  325 ? 7.359   5.595   18.166   1.00 47.62  ? 327 GLU   D CG    1 
ATOM   9410  C  CD    . GLU   C 2  325 ? 8.591   5.448   19.081   1.00 62.20  ? 327 GLU   D CD    1 
ATOM   9411  O  OE1   . GLU   C 2  325 ? 9.557   6.242   18.951   1.00 54.06  ? 327 GLU   D OE1   1 
ATOM   9412  O  OE2   . GLU   C 2  325 ? 8.597   4.521   19.929   1.00 62.70  ? 327 GLU   D OE2   1 
ATOM   9413  N  N     . VAL   C 2  326 ? 3.724   6.997   17.764   1.00 48.51  ? 328 VAL   D N     1 
ATOM   9414  C  CA    . VAL   C 2  326 ? 2.426   6.339   17.919   1.00 48.53  ? 328 VAL   D CA    1 
ATOM   9415  C  C     . VAL   C 2  326 ? 1.712   6.247   16.578   1.00 44.91  ? 328 VAL   D C     1 
ATOM   9416  O  O     . VAL   C 2  326 ? 1.106   5.218   16.245   1.00 43.93  ? 328 VAL   D O     1 
ATOM   9417  C  CB    . VAL   C 2  326 ? 1.562   7.097   18.954   1.00 49.75  ? 328 VAL   D CB    1 
ATOM   9418  C  CG1   . VAL   C 2  326 ? 0.239   6.403   19.164   1.00 39.92  ? 328 VAL   D CG1   1 
ATOM   9419  C  CG2   . VAL   C 2  326 ? 2.294   7.277   20.267   1.00 49.93  ? 328 VAL   D CG2   1 
ATOM   9420  N  N     . ASP   C 2  327 ? 1.743   7.329   15.802   1.00 40.96  ? 329 ASP   D N     1 
ATOM   9421  C  CA    . ASP   C 2  327 ? 1.029   7.328   14.532   1.00 42.41  ? 329 ASP   D CA    1 
ATOM   9422  C  C     . ASP   C 2  327 ? 1.689   6.389   13.542   1.00 39.70  ? 329 ASP   D C     1 
ATOM   9423  O  O     . ASP   C 2  327 ? 1.004   5.633   12.846   1.00 42.35  ? 329 ASP   D O     1 
ATOM   9424  C  CB    . ASP   C 2  327 ? 0.950   8.746   13.970   1.00 38.37  ? 329 ASP   D CB    1 
ATOM   9425  C  CG    . ASP   C 2  327 ? 0.077   9.658   14.824   1.00 48.05  ? 329 ASP   D CG    1 
ATOM   9426  O  OD1   . ASP   C 2  327 ? -0.823  9.129   15.521   1.00 43.16  ? 329 ASP   D OD1   1 
ATOM   9427  O  OD2   . ASP   C 2  327 ? 0.293   10.894  14.801   1.00 44.08  ? 329 ASP   D OD2   1 
ATOM   9428  N  N     . GLU   C 2  328 ? 3.020   6.432   13.460   1.00 43.27  ? 330 GLU   D N     1 
ATOM   9429  C  CA    . GLU   C 2  328 ? 3.741   5.494   12.614   1.00 43.02  ? 330 GLU   D CA    1 
ATOM   9430  C  C     . GLU   C 2  328 ? 3.406   4.053   12.999   1.00 50.64  ? 330 GLU   D C     1 
ATOM   9431  O  O     . GLU   C 2  328 ? 3.148   3.202   12.131   1.00 44.18  ? 330 GLU   D O     1 
ATOM   9432  C  CB    . GLU   C 2  328 ? 5.246   5.766   12.716   1.00 41.83  ? 330 GLU   D CB    1 
ATOM   9433  C  CG    . GLU   C 2  328 ? 5.708   7.113   12.119   1.00 46.43  ? 330 GLU   D CG    1 
ATOM   9434  C  CD    . GLU   C 2  328 ? 7.113   7.544   12.565   1.00 54.69  ? 330 GLU   D CD    1 
ATOM   9435  O  OE1   . GLU   C 2  328 ? 7.806   6.776   13.274   1.00 55.17  ? 330 GLU   D OE1   1 
ATOM   9436  O  OE2   . GLU   C 2  328 ? 7.524   8.669   12.208   1.00 62.72  ? 330 GLU   D OE2   1 
ATOM   9437  N  N     . GLN   C 2  329 ? 3.367   3.774   14.306   1.00 48.23  ? 331 GLN   D N     1 
ATOM   9438  C  CA    . GLN   C 2  329 ? 3.185   2.405   14.769   1.00 49.80  ? 331 GLN   D CA    1 
ATOM   9439  C  C     . GLN   C 2  329 ? 1.760   1.923   14.520   1.00 42.32  ? 331 GLN   D C     1 
ATOM   9440  O  O     . GLN   C 2  329 ? 1.555   0.803   14.028   1.00 36.54  ? 331 GLN   D O     1 
ATOM   9441  C  CB    . GLN   C 2  329 ? 3.573   2.303   16.249   1.00 51.93  ? 331 GLN   D CB    1 
ATOM   9442  C  CG    . GLN   C 2  329 ? 5.075   2.441   16.480   1.00 46.79  ? 331 GLN   D CG    1 
ATOM   9443  C  CD    . GLN   C 2  329 ? 5.898   1.768   15.366   1.00 64.15  ? 331 GLN   D CD    1 
ATOM   9444  O  OE1   . GLN   C 2  329 ? 5.686   0.586   15.025   1.00 46.68  ? 331 GLN   D OE1   1 
ATOM   9445  N  NE2   . GLN   C 2  329 ? 6.826   2.533   14.780   1.00 58.63  ? 331 GLN   D NE2   1 
ATOM   9446  N  N     . MET   C 2  330 ? 0.762   2.756   14.847   1.00 38.11  ? 332 MET   D N     1 
ATOM   9447  C  CA    . MET   C 2  330 ? -0.619  2.424   14.493   1.00 37.96  ? 332 MET   D CA    1 
ATOM   9448  C  C     . MET   C 2  330 ? -0.756  2.190   12.987   1.00 37.34  ? 332 MET   D C     1 
ATOM   9449  O  O     . MET   C 2  330 ? -1.443  1.253   12.557   1.00 40.81  ? 332 MET   D O     1 
ATOM   9450  C  CB    . MET   C 2  330 ? -1.574  3.532   14.958   1.00 39.03  ? 332 MET   D CB    1 
ATOM   9451  C  CG    . MET   C 2  330 ? -1.909  3.563   16.444   1.00 38.17  ? 332 MET   D CG    1 
ATOM   9452  S  SD    . MET   C 2  330 ? -2.430  1.971   17.106   1.00 50.26  ? 332 MET   D SD    1 
ATOM   9453  C  CE    . MET   C 2  330 ? -3.959  1.646   16.211   1.00 37.28  ? 332 MET   D CE    1 
ATOM   9454  N  N     . LEU   C 2  331 ? -0.112  3.036   12.169   1.00 34.45  ? 333 LEU   D N     1 
ATOM   9455  C  CA    . LEU   C 2  331 ? -0.049  2.785   10.726   1.00 49.31  ? 333 LEU   D CA    1 
ATOM   9456  C  C     . LEU   C 2  331 ? 0.605   1.441   10.430   1.00 41.38  ? 333 LEU   D C     1 
ATOM   9457  O  O     . LEU   C 2  331 ? 0.098   0.642   9.631    1.00 38.67  ? 333 LEU   D O     1 
ATOM   9458  C  CB    . LEU   C 2  331 ? 0.715   3.911   10.017   1.00 41.08  ? 333 LEU   D CB    1 
ATOM   9459  C  CG    . LEU   C 2  331 ? -0.129  5.138   9.690    1.00 34.66  ? 333 LEU   D CG    1 
ATOM   9460  C  CD1   . LEU   C 2  331 ? 0.693   6.189   8.969    1.00 38.86  ? 333 LEU   D CD1   1 
ATOM   9461  C  CD2   . LEU   C 2  331 ? -1.336  4.720   8.882    1.00 20.52  ? 333 LEU   D CD2   1 
ATOM   9462  N  N     . ASN   C 2  332 ? 1.748   1.189   11.065   1.00 47.08  ? 334 ASN   D N     1 
ATOM   9463  C  CA    . ASN   C 2  332 ? 2.429   -0.091  10.933   1.00 46.93  ? 334 ASN   D CA    1 
ATOM   9464  C  C     . ASN   C 2  332 ? 1.464   -1.253  11.166   1.00 40.86  ? 334 ASN   D C     1 
ATOM   9465  O  O     . ASN   C 2  332 ? 1.382   -2.183  10.354   1.00 42.17  ? 334 ASN   D O     1 
ATOM   9466  C  CB    . ASN   C 2  332 ? 3.603   -0.118  11.918   1.00 44.53  ? 334 ASN   D CB    1 
ATOM   9467  C  CG    . ASN   C 2  332 ? 4.679   -1.079  11.522   0.00 52.93  ? 334 ASN   D CG    1 
ATOM   9468  O  OD1   . ASN   C 2  332 ? 4.401   -2.144  10.985   1.00 61.45  ? 334 ASN   D OD1   1 
ATOM   9469  N  ND2   . ASN   C 2  332 ? 5.927   -0.713  11.796   1.00 61.52  ? 334 ASN   D ND2   1 
ATOM   9470  N  N     . VAL   C 2  333 ? 0.690   -1.194  12.254   1.00 37.16  ? 335 VAL   D N     1 
ATOM   9471  C  CA    . VAL   C 2  333 ? -0.090  -2.365  12.649   1.00 46.44  ? 335 VAL   D CA    1 
ATOM   9472  C  C     . VAL   C 2  333 ? -1.178  -2.653  11.629   1.00 41.34  ? 335 VAL   D C     1 
ATOM   9473  O  O     . VAL   C 2  333 ? -1.499  -3.817  11.367   1.00 48.91  ? 335 VAL   D O     1 
ATOM   9474  C  CB    . VAL   C 2  333 ? -0.675  -2.208  14.072   1.00 42.41  ? 335 VAL   D CB    1 
ATOM   9475  C  CG1   . VAL   C 2  333 ? -2.113  -1.746  14.008   1.00 47.30  ? 335 VAL   D CG1   1 
ATOM   9476  C  CG2   . VAL   C 2  333 ? -0.626  -3.523  14.803   1.00 44.74  ? 335 VAL   D CG2   1 
ATOM   9477  N  N     . GLN   C 2  334 ? -1.751  -1.623  11.020   1.00 43.92  ? 336 GLN   D N     1 
ATOM   9478  C  CA    . GLN   C 2  334 ? -2.831  -1.875  10.072   1.00 39.39  ? 336 GLN   D CA    1 
ATOM   9479  C  C     . GLN   C 2  334 ? -2.312  -2.404  8.740    1.00 42.14  ? 336 GLN   D C     1 
ATOM   9480  O  O     . GLN   C 2  334 ? -2.930  -3.305  8.160    1.00 43.07  ? 336 GLN   D O     1 
ATOM   9481  C  CB    . GLN   C 2  334 ? -3.653  -0.606  9.879    1.00 40.82  ? 336 GLN   D CB    1 
ATOM   9482  C  CG    . GLN   C 2  334 ? -4.511  -0.290  11.078   1.00 35.20  ? 336 GLN   D CG    1 
ATOM   9483  C  CD    . GLN   C 2  334 ? -4.998  1.139   11.071   1.00 37.91  ? 336 GLN   D CD    1 
ATOM   9484  O  OE1   . GLN   C 2  334 ? -6.126  1.422   10.654   1.00 41.26  ? 336 GLN   D OE1   1 
ATOM   9485  N  NE2   . GLN   C 2  334 ? -4.159  2.052   11.551   1.00 35.19  ? 336 GLN   D NE2   1 
ATOM   9486  N  N     . ASN   C 2  335 ? -1.190  -1.870  8.233    1.00 41.77  ? 337 ASN   D N     1 
ATOM   9487  C  CA    . ASN   C 2  335 ? -0.547  -2.469  7.061    1.00 41.18  ? 337 ASN   D CA    1 
ATOM   9488  C  C     . ASN   C 2  335 ? -0.363  -3.968  7.271    1.00 43.20  ? 337 ASN   D C     1 
ATOM   9489  O  O     . ASN   C 2  335 ? -0.981  -4.784  6.577    1.00 45.10  ? 337 ASN   D O     1 
ATOM   9490  C  CB    . ASN   C 2  335 ? 0.821   -1.842  6.768    1.00 42.86  ? 337 ASN   D CB    1 
ATOM   9491  C  CG    . ASN   C 2  335 ? 0.740   -0.364  6.433    1.00 58.54  ? 337 ASN   D CG    1 
ATOM   9492  O  OD1   . ASN   C 2  335 ? -0.275  0.121   5.923    1.00 51.47  ? 337 ASN   D OD1   1 
ATOM   9493  N  ND2   . ASN   C 2  335 ? 1.823   0.364   6.715    0.81 54.36  ? 337 ASN   D ND2   1 
ATOM   9494  N  N     . LYS   C 2  336 ? 0.481   -4.341  8.235    1.00 42.83  ? 338 LYS   D N     1 
ATOM   9495  C  CA    . LYS   C 2  336 ? 0.813   -5.752  8.414    1.00 52.18  ? 338 LYS   D CA    1 
ATOM   9496  C  C     . LYS   C 2  336 ? -0.441  -6.617  8.500    1.00 47.71  ? 338 LYS   D C     1 
ATOM   9497  O  O     . LYS   C 2  336 ? -0.579  -7.602  7.769    1.00 49.59  ? 338 LYS   D O     1 
ATOM   9498  C  CB    . LYS   C 2  336 ? 1.671   -5.939  9.662    1.00 60.16  ? 338 LYS   D CB    1 
ATOM   9499  N  N     . ASN   C 2  337 ? -1.377  -6.253  9.379    1.00 52.27  ? 339 ASN   D N     1 
ATOM   9500  C  CA    . ASN   C 2  337 ? -2.558  -7.063  9.655    1.00 47.28  ? 339 ASN   D CA    1 
ATOM   9501  C  C     . ASN   C 2  337 ? -3.787  -6.604  8.868    1.00 46.58  ? 339 ASN   D C     1 
ATOM   9502  O  O     . ASN   C 2  337 ? -4.922  -6.774  9.332    1.00 46.90  ? 339 ASN   D O     1 
ATOM   9503  C  CB    . ASN   C 2  337 ? -2.840  -7.055  11.157   1.00 50.81  ? 339 ASN   D CB    1 
ATOM   9504  C  CG    . ASN   C 2  337 ? -1.561  -7.072  11.994   1.00 46.96  ? 339 ASN   D CG    1 
ATOM   9505  O  OD1   . ASN   C 2  337 ? -1.312  -6.161  12.776   1.00 51.67  ? 339 ASN   D OD1   1 
ATOM   9506  N  ND2   . ASN   C 2  337 ? -0.754  -8.110  11.833   1.00 44.54  ? 339 ASN   D ND2   1 
ATOM   9507  N  N     . SER   C 2  338 ? -3.581  -6.059  7.661    1.00 40.70  ? 340 SER   D N     1 
ATOM   9508  C  CA    . SER   C 2  338 ? -4.674  -5.426  6.929    1.00 41.14  ? 340 SER   D CA    1 
ATOM   9509  C  C     . SER   C 2  338 ? -5.853  -6.367  6.683    1.00 42.15  ? 340 SER   D C     1 
ATOM   9510  O  O     . SER   C 2  338 ? -6.985  -5.899  6.520    1.00 49.53  ? 340 SER   D O     1 
ATOM   9511  C  CB    . SER   C 2  338 ? -4.167  -4.877  5.602    1.00 38.18  ? 340 SER   D CB    1 
ATOM   9512  O  OG    . SER   C 2  338 ? -3.725  -5.929  4.779    1.00 45.31  ? 340 SER   D OG    1 
ATOM   9513  N  N     . SER   C 2  339 ? -5.622  -7.680  6.621    1.00 43.67  ? 341 SER   D N     1 
ATOM   9514  C  CA    . SER   C 2  339 ? -6.729  -8.607  6.380    1.00 46.93  ? 341 SER   D CA    1 
ATOM   9515  C  C     . SER   C 2  339 ? -7.728  -8.617  7.535    1.00 47.97  ? 341 SER   D C     1 
ATOM   9516  O  O     . SER   C 2  339 ? -8.911  -8.914  7.325    1.00 43.35  ? 341 SER   D O     1 
ATOM   9517  C  CB    . SER   C 2  339 ? -6.209  -10.029 6.163    1.00 42.33  ? 341 SER   D CB    1 
ATOM   9518  O  OG    . SER   C 2  339 ? -5.222  -10.067 5.171    1.00 42.20  ? 341 SER   D OG    1 
ATOM   9519  N  N     . TYR   C 2  340 ? -7.273  -8.324  8.756    1.00 36.12  ? 342 TYR   D N     1 
ATOM   9520  C  CA    . TYR   C 2  340 ? -8.115  -8.409  9.937    1.00 40.29  ? 342 TYR   D CA    1 
ATOM   9521  C  C     . TYR   C 2  340 ? -8.871  -7.103  10.218   1.00 48.90  ? 342 TYR   D C     1 
ATOM   9522  O  O     . TYR   C 2  340 ? -9.326  -6.880  11.351   1.00 44.77  ? 342 TYR   D O     1 
ATOM   9523  C  CB    . TYR   C 2  340 ? -7.264  -8.826  11.141   1.00 45.87  ? 342 TYR   D CB    1 
ATOM   9524  C  CG    . TYR   C 2  340 ? -6.411  -10.059 10.889   1.00 45.86  ? 342 TYR   D CG    1 
ATOM   9525  C  CD1   . TYR   C 2  340 ? -6.989  -11.335 10.802   1.00 44.15  ? 342 TYR   D CD1   1 
ATOM   9526  C  CD2   . TYR   C 2  340 ? -5.028  -9.951  10.723   1.00 44.74  ? 342 TYR   D CD2   1 
ATOM   9527  C  CE1   . TYR   C 2  340 ? -6.203  -12.470 10.563   1.00 43.82  ? 342 TYR   D CE1   1 
ATOM   9528  C  CE2   . TYR   C 2  340 ? -4.234  -11.084 10.478   1.00 42.01  ? 342 TYR   D CE2   1 
ATOM   9529  C  CZ    . TYR   C 2  340 ? -4.827  -12.335 10.402   1.00 42.96  ? 342 TYR   D CZ    1 
ATOM   9530  O  OH    . TYR   C 2  340 ? -4.040  -13.442 10.165   1.00 47.15  ? 342 TYR   D OH    1 
ATOM   9531  N  N     . PHE   C 2  341 ? -8.999  -6.232  9.213    1.00 46.69  ? 343 PHE   D N     1 
ATOM   9532  C  CA    . PHE   C 2  341 ? -9.827  -5.031  9.286    1.00 40.82  ? 343 PHE   D CA    1 
ATOM   9533  C  C     . PHE   C 2  341 ? -10.746 -5.028  8.074    1.00 44.15  ? 343 PHE   D C     1 
ATOM   9534  O  O     . PHE   C 2  341 ? -10.256 -5.056  6.942    1.00 50.62  ? 343 PHE   D O     1 
ATOM   9535  C  CB    . PHE   C 2  341 ? -8.973  -3.765  9.287    1.00 33.52  ? 343 PHE   D CB    1 
ATOM   9536  C  CG    . PHE   C 2  341 ? -8.006  -3.670  10.424   1.00 32.07  ? 343 PHE   D CG    1 
ATOM   9537  C  CD1   . PHE   C 2  341 ? -8.379  -3.063  11.623   1.00 29.40  ? 343 PHE   D CD1   1 
ATOM   9538  C  CD2   . PHE   C 2  341 ? -6.710  -4.153  10.286   1.00 32.96  ? 343 PHE   D CD2   1 
ATOM   9539  C  CE1   . PHE   C 2  341 ? -7.488  -2.955  12.676   1.00 28.96  ? 343 PHE   D CE1   1 
ATOM   9540  C  CE2   . PHE   C 2  341 ? -5.800  -4.037  11.322   1.00 35.52  ? 343 PHE   D CE2   1 
ATOM   9541  C  CZ    . PHE   C 2  341 ? -6.191  -3.430  12.526   1.00 39.47  ? 343 PHE   D CZ    1 
ATOM   9542  N  N     . VAL   C 2  342 ? -12.067 -4.999  8.292    1.00 35.04  ? 344 VAL   D N     1 
ATOM   9543  C  CA    . VAL   C 2  342 ? -12.972 -5.049  7.149    1.00 37.04  ? 344 VAL   D CA    1 
ATOM   9544  C  C     . VAL   C 2  342 ? -12.685 -3.871  6.234    1.00 41.20  ? 344 VAL   D C     1 
ATOM   9545  O  O     . VAL   C 2  342 ? -12.683 -2.712  6.661    1.00 42.09  ? 344 VAL   D O     1 
ATOM   9546  C  CB    . VAL   C 2  342 ? -14.444 -5.066  7.589    1.00 39.15  ? 344 VAL   D CB    1 
ATOM   9547  C  CG1   . VAL   C 2  342 ? -14.746 -6.361  8.312    1.00 47.61  ? 344 VAL   D CG1   1 
ATOM   9548  C  CG2   . VAL   C 2  342 ? -14.790 -3.837  8.431    1.00 35.64  ? 344 VAL   D CG2   1 
ATOM   9549  N  N     . GLU   C 2  343 ? -12.430 -4.162  4.967    1.00 44.28  ? 345 GLU   D N     1 
ATOM   9550  C  CA    . GLU   C 2  343 ? -12.029 -3.096  4.065    1.00 42.10  ? 345 GLU   D CA    1 
ATOM   9551  C  C     . GLU   C 2  343 ? -13.193 -2.166  3.732    1.00 40.86  ? 345 GLU   D C     1 
ATOM   9552  O  O     . GLU   C 2  343 ? -12.960 -0.996  3.419    1.00 41.66  ? 345 GLU   D O     1 
ATOM   9553  C  CB    . GLU   C 2  343 ? -11.386 -3.698  2.798    1.00 38.14  ? 345 GLU   D CB    1 
ATOM   9554  C  CG    . GLU   C 2  343 ? -12.328 -4.080  1.664    1.00 44.28  ? 345 GLU   D CG    1 
ATOM   9555  C  CD    . GLU   C 2  343 ? -12.753 -5.541  1.699    1.00 57.76  ? 345 GLU   D CD    1 
ATOM   9556  O  OE1   . GLU   C 2  343 ? -12.561 -6.180  2.758    1.00 66.88  ? 345 GLU   D OE1   1 
ATOM   9557  O  OE2   . GLU   C 2  343 ? -13.289 -6.050  0.682    1.00 46.10  ? 345 GLU   D OE2   1 
ATOM   9558  N  N     . TRP   C 2  344 ? -14.436 -2.627  3.847    1.00 38.47  ? 346 TRP   D N     1 
ATOM   9559  C  CA    . TRP   C 2  344 ? -15.575 -1.773  3.518    1.00 38.90  ? 346 TRP   D CA    1 
ATOM   9560  C  C     . TRP   C 2  344 ? -15.994 -0.835  4.658    1.00 41.34  ? 346 TRP   D C     1 
ATOM   9561  O  O     . TRP   C 2  344 ? -17.066 -0.217  4.559    1.00 36.19  ? 346 TRP   D O     1 
ATOM   9562  C  CB    . TRP   C 2  344 ? -16.768 -2.618  3.080    1.00 44.02  ? 346 TRP   D CB    1 
ATOM   9563  C  CG    . TRP   C 2  344 ? -17.014 -3.777  3.954    1.00 44.83  ? 346 TRP   D CG    1 
ATOM   9564  C  CD1   . TRP   C 2  344 ? -16.456 -5.014  3.842    1.00 44.17  ? 346 TRP   D CD1   1 
ATOM   9565  C  CD2   . TRP   C 2  344 ? -17.878 -3.822  5.094    1.00 51.08  ? 346 TRP   D CD2   1 
ATOM   9566  N  NE1   . TRP   C 2  344 ? -16.920 -5.829  4.841    1.00 50.62  ? 346 TRP   D NE1   1 
ATOM   9567  C  CE2   . TRP   C 2  344 ? -17.799 -5.127  5.623    1.00 50.56  ? 346 TRP   D CE2   1 
ATOM   9568  C  CE3   . TRP   C 2  344 ? -18.713 -2.886  5.722    1.00 47.37  ? 346 TRP   D CE3   1 
ATOM   9569  C  CZ2   . TRP   C 2  344 ? -18.527 -5.524  6.749    1.00 47.06  ? 346 TRP   D CZ2   1 
ATOM   9570  C  CZ3   . TRP   C 2  344 ? -19.426 -3.274  6.840    1.00 39.37  ? 346 TRP   D CZ3   1 
ATOM   9571  C  CH2   . TRP   C 2  344 ? -19.330 -4.583  7.343    1.00 45.82  ? 346 TRP   D CH2   1 
ATOM   9572  N  N     . ILE   C 2  345 ? -15.196 -0.709  5.713    1.00 34.21  ? 347 ILE   D N     1 
ATOM   9573  C  CA    . ILE   C 2  345 ? -15.253 0.429   6.620    1.00 30.72  ? 347 ILE   D CA    1 
ATOM   9574  C  C     . ILE   C 2  345 ? -13.885 1.105   6.619    1.00 32.32  ? 347 ILE   D C     1 
ATOM   9575  O  O     . ILE   C 2  345 ? -12.943 0.631   7.253    1.00 30.68  ? 347 ILE   D O     1 
ATOM   9576  C  CB    . ILE   C 2  345 ? -15.661 0.015   8.045    1.00 34.35  ? 347 ILE   D CB    1 
ATOM   9577  C  CG1   . ILE   C 2  345 ? -17.027 -0.656  8.067    1.00 32.35  ? 347 ILE   D CG1   1 
ATOM   9578  C  CG2   . ILE   C 2  345 ? -15.655 1.236   8.969    1.00 28.25  ? 347 ILE   D CG2   1 
ATOM   9579  C  CD1   . ILE   C 2  345 ? -17.409 -1.120  9.460    1.00 36.84  ? 347 ILE   D CD1   1 
ATOM   9580  N  N     . PRO   C 2  346 ? -13.741 2.225   5.925    1.00 31.21  ? 348 PRO   D N     1 
ATOM   9581  C  CA    . PRO   C 2  346 ? -12.442 2.893   5.858    1.00 24.58  ? 348 PRO   D CA    1 
ATOM   9582  C  C     . PRO   C 2  346 ? -12.147 3.669   7.120    1.00 31.33  ? 348 PRO   D C     1 
ATOM   9583  O  O     . PRO   C 2  346 ? -13.036 4.239   7.753    1.00 35.49  ? 348 PRO   D O     1 
ATOM   9584  C  CB    . PRO   C 2  346 ? -12.591 3.856   4.671    1.00 22.33  ? 348 PRO   D CB    1 
ATOM   9585  C  CG    . PRO   C 2  346 ? -13.903 3.550   4.060    1.00 33.13  ? 348 PRO   D CG    1 
ATOM   9586  C  CD    . PRO   C 2  346 ? -14.747 2.921   5.121    1.00 33.45  ? 348 PRO   D CD    1 
ATOM   9587  N  N     . ASN   C 2  347 ? -10.866 3.712   7.465    1.00 31.05  ? 349 ASN   D N     1 
ATOM   9588  C  CA    . ASN   C 2  347 ? -10.406 4.548   8.571    1.00 34.53  ? 349 ASN   D CA    1 
ATOM   9589  C  C     . ASN   C 2  347 ? -11.149 4.212   9.857    1.00 35.85  ? 349 ASN   D C     1 
ATOM   9590  O  O     . ASN   C 2  347 ? -11.543 5.105   10.611   1.00 41.79  ? 349 ASN   D O     1 
ATOM   9591  C  CB    . ASN   C 2  347 ? -10.562 6.031   8.239    1.00 23.02  ? 349 ASN   D CB    1 
ATOM   9592  C  CG    . ASN   C 2  347 ? -10.034 6.379   6.858    1.00 31.03  ? 349 ASN   D CG    1 
ATOM   9593  O  OD1   . ASN   C 2  347 ? -10.789 6.720   5.952    1.00 37.06  ? 349 ASN   D OD1   1 
ATOM   9594  N  ND2   . ASN   C 2  347 ? -8.729  6.308   6.698    1.00 41.74  ? 349 ASN   D ND2   1 
ATOM   9595  N  N     . ASN   C 2  348 ? -11.333 2.914   10.115   1.00 32.51  ? 350 ASN   D N     1 
ATOM   9596  C  CA    . ASN   C 2  348 ? -12.142 2.453   11.235   1.00 33.95  ? 350 ASN   D CA    1 
ATOM   9597  C  C     . ASN   C 2  348 ? -11.331 2.211   12.506   1.00 34.32  ? 350 ASN   D C     1 
ATOM   9598  O  O     . ASN   C 2  348 ? -11.890 1.745   13.496   1.00 33.46  ? 350 ASN   D O     1 
ATOM   9599  C  CB    . ASN   C 2  348 ? -12.894 1.178   10.841   1.00 38.61  ? 350 ASN   D CB    1 
ATOM   9600  C  CG    . ASN   C 2  348 ? -11.956 0.057   10.419   1.00 40.84  ? 350 ASN   D CG    1 
ATOM   9601  O  OD1   . ASN   C 2  348 ? -10.733 0.199   10.501   1.00 39.51  ? 350 ASN   D OD1   1 
ATOM   9602  N  ND2   . ASN   C 2  348 ? -12.524 -1.067  9.974    1.00 32.69  ? 350 ASN   D ND2   1 
ATOM   9603  N  N     . VAL   C 2  349 ? -10.046 2.523   12.514   1.00 32.00  ? 351 VAL   D N     1 
ATOM   9604  C  CA    . VAL   C 2  349 ? -9.219  2.411   13.704   1.00 29.84  ? 351 VAL   D CA    1 
ATOM   9605  C  C     . VAL   C 2  349 ? -8.908  3.828   14.174   1.00 38.47  ? 351 VAL   D C     1 
ATOM   9606  O  O     . VAL   C 2  349 ? -8.059  4.524   13.602   1.00 35.92  ? 351 VAL   D O     1 
ATOM   9607  C  CB    . VAL   C 2  349 ? -7.941  1.609   13.432   1.00 29.82  ? 351 VAL   D CB    1 
ATOM   9608  C  CG1   . VAL   C 2  349 ? -7.037  1.600   14.655   1.00 23.33  ? 351 VAL   D CG1   1 
ATOM   9609  C  CG2   . VAL   C 2  349 ? -8.309  0.202   12.984   1.00 30.08  ? 351 VAL   D CG2   1 
ATOM   9610  N  N     . LYS   C 2  350 ? -9.592  4.267   15.218   1.00 40.69  ? 352 LYS   D N     1 
ATOM   9611  C  CA    . LYS   C 2  350 ? -9.323  5.569   15.802   1.00 41.14  ? 352 LYS   D CA    1 
ATOM   9612  C  C     . LYS   C 2  350 ? -8.317  5.439   16.948   1.00 39.15  ? 352 LYS   D C     1 
ATOM   9613  O  O     . LYS   C 2  350 ? -8.248  4.413   17.625   1.00 43.99  ? 352 LYS   D O     1 
ATOM   9614  C  CB    . LYS   C 2  350 ? -10.631 6.220   16.279   1.00 41.30  ? 352 LYS   D CB    1 
ATOM   9615  C  CG    . LYS   C 2  350 ? -11.535 6.702   15.136   1.00 29.77  ? 352 LYS   D CG    1 
ATOM   9616  C  CD    . LYS   C 2  350 ? -10.702 7.301   14.002   1.00 26.38  ? 352 LYS   D CD    1 
ATOM   9617  C  CE    . LYS   C 2  350 ? -11.530 8.170   13.055   1.00 44.09  ? 352 LYS   D CE    1 
ATOM   9618  N  NZ    . LYS   C 2  350 ? -11.661 7.673   11.629   1.00 30.98  ? 352 LYS   D NZ    1 
ATOM   9619  N  N     . THR   C 2  351 ? -7.537  6.497   17.166   1.00 43.97  ? 353 THR   D N     1 
ATOM   9620  C  CA    . THR   C 2  351 ? -6.447  6.477   18.135   1.00 41.99  ? 353 THR   D CA    1 
ATOM   9621  C  C     . THR   C 2  351 ? -6.435  7.757   18.956   1.00 42.69  ? 353 THR   D C     1 
ATOM   9622  O  O     . THR   C 2  351 ? -6.599  8.854   18.412   1.00 45.74  ? 353 THR   D O     1 
ATOM   9623  C  CB    . THR   C 2  351 ? -5.084  6.322   17.448   1.00 44.62  ? 353 THR   D CB    1 
ATOM   9624  O  OG1   . THR   C 2  351 ? -4.804  4.932   17.242   1.00 59.24  ? 353 THR   D OG1   1 
ATOM   9625  C  CG2   . THR   C 2  351 ? -3.987  6.926   18.306   1.00 51.67  ? 353 THR   D CG2   1 
ATOM   9626  N  N     . ALA   C 2  352 ? -6.211  7.609   20.261   1.00 36.73  ? 354 ALA   D N     1 
ATOM   9627  C  CA    . ALA   C 2  352 ? -6.138  8.729   21.197   1.00 44.15  ? 354 ALA   D CA    1 
ATOM   9628  C  C     . ALA   C 2  352 ? -4.883  8.618   22.056   1.00 42.62  ? 354 ALA   D C     1 
ATOM   9629  O  O     . ALA   C 2  352 ? -4.517  7.522   22.493   1.00 51.42  ? 354 ALA   D O     1 
ATOM   9630  C  CB    . ALA   C 2  352 ? -7.384  8.778   22.106   1.00 38.07  ? 354 ALA   D CB    1 
ATOM   9631  N  N     . VAL   C 2  353 ? -4.225  9.745   22.303   1.00 39.38  ? 355 VAL   D N     1 
ATOM   9632  C  CA    . VAL   C 2  353 ? -3.107  9.809   23.240   1.00 44.75  ? 355 VAL   D CA    1 
ATOM   9633  C  C     . VAL   C 2  353 ? -3.522  10.744  24.359   1.00 42.08  ? 355 VAL   D C     1 
ATOM   9634  O  O     . VAL   C 2  353 ? -3.741  11.937  24.122   1.00 42.31  ? 355 VAL   D O     1 
ATOM   9635  C  CB    . VAL   C 2  353 ? -1.797  10.289  22.588   1.00 45.80  ? 355 VAL   D CB    1 
ATOM   9636  C  CG1   . VAL   C 2  353 ? -1.317  9.327   21.507   1.00 38.59  ? 355 VAL   D CG1   1 
ATOM   9637  C  CG2   . VAL   C 2  353 ? -1.940  11.689  22.062   1.00 47.91  ? 355 VAL   D CG2   1 
ATOM   9638  N  N     . CYS   C 2  354 ? -3.671  10.196  25.565   1.00 50.39  ? 356 CYS   D N     1 
ATOM   9639  C  CA    . CYS   C 2  354 ? -3.795  10.964  26.799   1.00 56.05  ? 356 CYS   D CA    1 
ATOM   9640  C  C     . CYS   C 2  354 ? -2.517  10.779  27.604   1.00 56.20  ? 356 CYS   D C     1 
ATOM   9641  O  O     . CYS   C 2  354 ? -1.998  9.663   27.705   1.00 60.26  ? 356 CYS   D O     1 
ATOM   9642  C  CB    . CYS   C 2  354 ? -5.003  10.520  27.628   1.00 59.88  ? 356 CYS   D CB    1 
ATOM   9643  S  SG    . CYS   C 2  354 ? -4.970  11.088  29.364   1.00 70.91  ? 356 CYS   D SG    1 
ATOM   9644  N  N     . ASP   C 2  355 ? -2.000  11.865  28.170   1.00 55.05  ? 357 ASP   D N     1 
ATOM   9645  C  CA    . ASP   C 2  355 ? -0.622  11.852  28.638   1.00 68.10  ? 357 ASP   D CA    1 
ATOM   9646  C  C     . ASP   C 2  355 ? -0.484  11.757  30.154   1.00 72.35  ? 357 ASP   D C     1 
ATOM   9647  O  O     . ASP   C 2  355 ? 0.623   11.943  30.671   1.00 74.86  ? 357 ASP   D O     1 
ATOM   9648  C  CB    . ASP   C 2  355 ? 0.137   13.071  28.102   1.00 70.09  ? 357 ASP   D CB    1 
ATOM   9649  C  CG    . ASP   C 2  355 ? -0.481  14.389  28.520   1.00 74.30  ? 357 ASP   D CG    1 
ATOM   9650  O  OD1   . ASP   C 2  355 ? -1.221  14.426  29.529   1.00 76.66  ? 357 ASP   D OD1   1 
ATOM   9651  O  OD2   . ASP   C 2  355 ? -0.216  15.393  27.827   1.00 70.74  ? 357 ASP   D OD2   1 
ATOM   9652  N  N     . ILE   C 2  356 ? -1.556  11.449  30.881   1.00 66.43  ? 358 ILE   D N     1 
ATOM   9653  C  CA    . ILE   C 2  356 ? -1.447  10.998  32.266   1.00 62.63  ? 358 ILE   D CA    1 
ATOM   9654  C  C     . ILE   C 2  356 ? -1.505  9.471   32.258   1.00 66.88  ? 358 ILE   D C     1 
ATOM   9655  O  O     . ILE   C 2  356 ? -2.561  8.905   31.919   1.00 61.39  ? 358 ILE   D O     1 
ATOM   9656  C  CB    . ILE   C 2  356 ? -2.544  11.582  33.158   1.00 63.11  ? 358 ILE   D CB    1 
ATOM   9657  C  CG1   . ILE   C 2  356 ? -2.528  13.106  33.092   1.00 56.69  ? 358 ILE   D CG1   1 
ATOM   9658  C  CG2   . ILE   C 2  356 ? -2.349  11.077  34.584   1.00 59.06  ? 358 ILE   D CG2   1 
ATOM   9659  C  CD1   . ILE   C 2  356 ? -3.834  13.722  33.508   1.00 68.33  ? 358 ILE   D CD1   1 
ATOM   9660  N  N     . PRO   C 2  357 ? -0.422  8.775   32.595   1.00 62.99  ? 359 PRO   D N     1 
ATOM   9661  C  CA    . PRO   C 2  357 ? -0.468  7.317   32.627   1.00 57.95  ? 359 PRO   D CA    1 
ATOM   9662  C  C     . PRO   C 2  357 ? -1.208  6.845   33.860   1.00 55.13  ? 359 PRO   D C     1 
ATOM   9663  O  O     . PRO   C 2  357 ? -1.508  7.650   34.754   1.00 51.54  ? 359 PRO   D O     1 
ATOM   9664  C  CB    . PRO   C 2  357 ? 1.014   6.909   32.669   1.00 63.31  ? 359 PRO   D CB    1 
ATOM   9665  C  CG    . PRO   C 2  357 ? 1.711   8.081   33.259   1.00 55.79  ? 359 PRO   D CG    1 
ATOM   9666  C  CD    . PRO   C 2  357 ? 0.919   9.306   32.912   1.00 45.83  ? 359 PRO   D CD    1 
ATOM   9667  N  N     . PRO   C 2  358 ? -1.535  5.558   33.930   1.00 58.69  ? 360 PRO   D N     1 
ATOM   9668  C  CA    . PRO   C 2  358 ? -2.212  5.025   35.121   1.00 62.29  ? 360 PRO   D CA    1 
ATOM   9669  C  C     . PRO   C 2  358 ? -1.236  4.615   36.215   1.00 74.76  ? 360 PRO   D C     1 
ATOM   9670  O  O     . PRO   C 2  358 ? -0.323  3.823   35.960   1.00 78.29  ? 360 PRO   D O     1 
ATOM   9671  C  CB    . PRO   C 2  358 ? -2.968  3.811   34.571   1.00 55.71  ? 360 PRO   D CB    1 
ATOM   9672  C  CG    . PRO   C 2  358 ? -2.125  3.347   33.431   1.00 54.83  ? 360 PRO   D CG    1 
ATOM   9673  C  CD    . PRO   C 2  358 ? -1.441  4.563   32.848   1.00 57.76  ? 360 PRO   D CD    1 
ATOM   9674  N  N     . ARG   C 2  359 ? -1.420  5.151   37.427   1.00 78.58  ? 369 ARG   D N     1 
ATOM   9675  C  CA    . ARG   C 2  359 ? -0.616  4.797   38.597   1.00 79.78  ? 369 ARG   D CA    1 
ATOM   9676  C  C     . ARG   C 2  359 ? -0.093  3.364   38.493   1.00 76.78  ? 369 ARG   D C     1 
ATOM   9677  O  O     . ARG   C 2  359 ? -0.875  2.405   38.450   1.00 74.73  ? 369 ARG   D O     1 
ATOM   9678  C  CB    . ARG   C 2  359 ? -1.446  4.990   39.875   1.00 74.05  ? 369 ARG   D CB    1 
ATOM   9679  C  CG    . ARG   C 2  359 ? -0.651  5.064   41.180   1.00 81.22  ? 369 ARG   D CG    1 
ATOM   9680  C  CD    . ARG   C 2  359 ? -1.579  5.126   42.407   1.00 83.82  ? 369 ARG   D CD    1 
ATOM   9681  N  NE    . ARG   C 2  359 ? -0.960  4.573   43.610   1.00 96.46  ? 369 ARG   D NE    1 
ATOM   9682  C  CZ    . ARG   C 2  359 ? -1.625  4.193   44.696   1.00 98.45  ? 369 ARG   D CZ    1 
ATOM   9683  N  NH1   . ARG   C 2  359 ? -2.941  4.303   44.776   1.00 88.71  ? 369 ARG   D NH1   1 
ATOM   9684  N  NH2   . ARG   C 2  359 ? -0.952  3.683   45.728   1.00 96.37  ? 369 ARG   D NH2   1 
ATOM   9685  N  N     . GLY   C 2  360 ? 1.227   3.211   38.414   1.00 66.63  ? 370 GLY   D N     1 
ATOM   9686  C  CA    . GLY   C 2  360 ? 1.809   1.893   38.260   1.00 65.96  ? 370 GLY   D CA    1 
ATOM   9687  C  C     . GLY   C 2  360 ? 2.755   1.785   37.082   1.00 70.50  ? 370 GLY   D C     1 
ATOM   9688  O  O     . GLY   C 2  360 ? 3.814   1.158   37.185   1.00 59.12  ? 370 GLY   D O     1 
ATOM   9689  N  N     . LEU   C 2  361 ? 2.391   2.399   35.956   1.00 71.29  ? 371 LEU   D N     1 
ATOM   9690  C  CA    . LEU   C 2  361 ? 3.146   2.266   34.721   1.00 55.92  ? 371 LEU   D CA    1 
ATOM   9691  C  C     . LEU   C 2  361 ? 3.448   3.640   34.151   1.00 64.31  ? 371 LEU   D C     1 
ATOM   9692  O  O     . LEU   C 2  361 ? 2.693   4.594   34.356   1.00 69.56  ? 371 LEU   D O     1 
ATOM   9693  C  CB    . LEU   C 2  361 ? 2.386   1.442   33.687   1.00 63.03  ? 371 LEU   D CB    1 
ATOM   9694  C  CG    . LEU   C 2  361 ? 1.371   0.444   34.238   1.00 59.57  ? 371 LEU   D CG    1 
ATOM   9695  C  CD1   . LEU   C 2  361 ? -0.030  1.028   34.141   1.00 64.96  ? 371 LEU   D CD1   1 
ATOM   9696  C  CD2   . LEU   C 2  361 ? 1.457   -0.895  33.514   1.00 69.96  ? 371 LEU   D CD2   1 
ATOM   9697  N  N     . LYS   C 2  362 ? 4.567   3.726   33.422   1.00 71.70  ? 372 LYS   D N     1 
ATOM   9698  C  CA    . LYS   C 2  362 ? 5.004   4.988   32.833   1.00 70.57  ? 372 LYS   D CA    1 
ATOM   9699  C  C     . LYS   C 2  362 ? 4.280   5.304   31.532   1.00 65.70  ? 372 LYS   D C     1 
ATOM   9700  O  O     . LYS   C 2  362 ? 4.238   6.473   31.128   1.00 61.40  ? 372 LYS   D O     1 
ATOM   9701  C  CB    . LYS   C 2  362 ? 6.517   4.963   32.598   1.00 67.08  ? 372 LYS   D CB    1 
ATOM   9702  C  CG    . LYS   C 2  362 ? 7.087   6.307   32.164   1.00 81.30  ? 372 LYS   D CG    1 
ATOM   9703  C  CD    . LYS   C 2  362 ? 8.613   6.273   32.087   1.00 96.50  ? 372 LYS   D CD    1 
ATOM   9704  C  CE    . LYS   C 2  362 ? 9.177   7.645   31.743   1.00 96.38  ? 372 LYS   D CE    1 
ATOM   9705  N  NZ    . LYS   C 2  362 ? 10.648  7.699   31.942   1.00 93.25  ? 372 LYS   D NZ    1 
ATOM   9706  N  N     . MET   C 2  363 ? 3.709   4.292   30.880   1.00 62.08  ? 373 MET   D N     1 
ATOM   9707  C  CA    . MET   C 2  363 ? 2.882   4.491   29.700   1.00 68.09  ? 373 MET   D CA    1 
ATOM   9708  C  C     . MET   C 2  363 ? 2.255   3.163   29.301   1.00 64.41  ? 373 MET   D C     1 
ATOM   9709  O  O     . MET   C 2  363 ? 2.909   2.121   29.383   1.00 54.62  ? 373 MET   D O     1 
ATOM   9710  C  CB    . MET   C 2  363 ? 3.700   5.075   28.544   1.00 77.87  ? 373 MET   D CB    1 
ATOM   9711  C  CG    . MET   C 2  363 ? 4.800   4.181   27.996   1.00 74.08  ? 373 MET   D CG    1 
ATOM   9712  S  SD    . MET   C 2  363 ? 5.817   5.183   26.901   1.00 87.67  ? 373 MET   D SD    1 
ATOM   9713  C  CE    . MET   C 2  363 ? 6.302   6.480   28.049   1.00 70.24  ? 373 MET   D CE    1 
ATOM   9714  N  N     . SER   C 2  364 ? 0.989   3.213   28.867   1.00 62.44  ? 374 SER   D N     1 
ATOM   9715  C  CA    . SER   C 2  364 ? 0.209   2.015   28.583   1.00 56.36  ? 374 SER   D CA    1 
ATOM   9716  C  C     . SER   C 2  364 ? -0.693  2.231   27.370   1.00 57.34  ? 374 SER   D C     1 
ATOM   9717  O  O     . SER   C 2  364 ? -0.837  3.340   26.846   1.00 55.06  ? 374 SER   D O     1 
ATOM   9718  C  CB    . SER   C 2  364 ? -0.645  1.601   29.787   1.00 55.12  ? 374 SER   D CB    1 
ATOM   9719  O  OG    . SER   C 2  364 ? -1.736  2.483   29.956   1.00 55.01  ? 374 SER   D OG    1 
ATOM   9720  N  N     . ALA   C 2  365 ? -1.316  1.140   26.942   1.00 44.84  ? 375 ALA   D N     1 
ATOM   9721  C  CA    . ALA   C 2  365 ? -2.195  1.108   25.791   1.00 47.33  ? 375 ALA   D CA    1 
ATOM   9722  C  C     . ALA   C 2  365 ? -3.465  0.367   26.170   1.00 51.39  ? 375 ALA   D C     1 
ATOM   9723  O  O     . ALA   C 2  365 ? -3.405  -0.688  26.809   1.00 50.32  ? 375 ALA   D O     1 
ATOM   9724  C  CB    . ALA   C 2  365 ? -1.532  0.407   24.600   1.00 45.99  ? 375 ALA   D CB    1 
ATOM   9725  N  N     . THR   C 2  366 ? -4.612  0.906   25.764   1.00 46.17  ? 376 THR   D N     1 
ATOM   9726  C  CA    . THR   C 2  366 ? -5.890  0.247   25.983   1.00 43.14  ? 376 THR   D CA    1 
ATOM   9727  C  C     . THR   C 2  366 ? -6.586  0.029   24.648   1.00 44.29  ? 376 THR   D C     1 
ATOM   9728  O  O     . THR   C 2  366 ? -6.739  0.964   23.853   1.00 47.18  ? 376 THR   D O     1 
ATOM   9729  C  CB    . THR   C 2  366 ? -6.776  1.059   26.929   1.00 52.07  ? 376 THR   D CB    1 
ATOM   9730  O  OG1   . THR   C 2  366 ? -5.954  1.826   27.813   1.00 50.05  ? 376 THR   D OG1   1 
ATOM   9731  C  CG2   . THR   C 2  366 ? -7.648  0.141   27.744   1.00 42.93  ? 376 THR   D CG2   1 
ATOM   9732  N  N     . PHE   C 2  367 ? -7.023  -1.200  24.425   1.00 38.14  ? 377 PHE   D N     1 
ATOM   9733  C  CA    . PHE   C 2  367 ? -7.608  -1.641  23.172   1.00 40.68  ? 377 PHE   D CA    1 
ATOM   9734  C  C     . PHE   C 2  367 ? -9.103  -1.819  23.372   1.00 39.97  ? 377 PHE   D C     1 
ATOM   9735  O  O     . PHE   C 2  367 ? -9.529  -2.460  24.334   1.00 45.55  ? 377 PHE   D O     1 
ATOM   9736  C  CB    . PHE   C 2  367 ? -6.953  -2.962  22.720   1.00 48.29  ? 377 PHE   D CB    1 
ATOM   9737  C  CG    . PHE   C 2  367 ? -7.615  -3.628  21.540   1.00 35.05  ? 377 PHE   D CG    1 
ATOM   9738  C  CD1   . PHE   C 2  367 ? -8.787  -4.331  21.688   1.00 42.41  ? 377 PHE   D CD1   1 
ATOM   9739  C  CD2   . PHE   C 2  367 ? -7.041  -3.580  20.295   1.00 49.69  ? 377 PHE   D CD2   1 
ATOM   9740  C  CE1   . PHE   C 2  367 ? -9.394  -4.962  20.603   1.00 50.16  ? 377 PHE   D CE1   1 
ATOM   9741  C  CE2   . PHE   C 2  367 ? -7.640  -4.211  19.197   1.00 55.15  ? 377 PHE   D CE2   1 
ATOM   9742  C  CZ    . PHE   C 2  367 ? -8.819  -4.907  19.357   1.00 46.29  ? 377 PHE   D CZ    1 
ATOM   9743  N  N     . ILE   C 2  368 ? -9.893  -1.276  22.455   1.00 40.27  ? 378 ILE   D N     1 
ATOM   9744  C  CA    . ILE   C 2  368 ? -11.327 -1.506  22.423   1.00 40.76  ? 378 ILE   D CA    1 
ATOM   9745  C  C     . ILE   C 2  368 ? -11.685 -1.977  21.023   1.00 40.01  ? 378 ILE   D C     1 
ATOM   9746  O  O     . ILE   C 2  368 ? -11.669 -1.185  20.071   1.00 45.79  ? 378 ILE   D O     1 
ATOM   9747  C  CB    . ILE   C 2  368 ? -12.128 -0.260  22.805   1.00 33.83  ? 378 ILE   D CB    1 
ATOM   9748  C  CG1   . ILE   C 2  368 ? -11.499 0.411   24.027   1.00 42.67  ? 378 ILE   D CG1   1 
ATOM   9749  C  CG2   . ILE   C 2  368 ? -13.542 -0.663  23.116   1.00 36.42  ? 378 ILE   D CG2   1 
ATOM   9750  C  CD1   . ILE   C 2  368 ? -12.198 1.693   24.470   1.00 47.69  ? 378 ILE   D CD1   1 
ATOM   9751  N  N     . GLY   C 2  369 ? -12.029 -3.253  20.895   1.00 31.63  ? 379 GLY   D N     1 
ATOM   9752  C  CA    . GLY   C 2  369 ? -12.254 -3.820  19.588   1.00 41.44  ? 379 GLY   D CA    1 
ATOM   9753  C  C     . GLY   C 2  369 ? -13.628 -4.390  19.329   1.00 36.34  ? 379 GLY   D C     1 
ATOM   9754  O  O     . GLY   C 2  369 ? -14.152 -5.178  20.115   1.00 41.32  ? 379 GLY   D O     1 
ATOM   9755  N  N     . ASN   C 2  370 ? -14.219 -3.993  18.210   1.00 36.74  ? 380 ASN   D N     1 
ATOM   9756  C  CA    . ASN   C 2  370 ? -15.472 -4.570  17.750   1.00 35.75  ? 380 ASN   D CA    1 
ATOM   9757  C  C     . ASN   C 2  370 ? -15.150 -5.570  16.638   1.00 38.71  ? 380 ASN   D C     1 
ATOM   9758  O  O     . ASN   C 2  370 ? -15.469 -5.394  15.461   1.00 37.57  ? 380 ASN   D O     1 
ATOM   9759  C  CB    . ASN   C 2  370 ? -16.426 -3.464  17.309   1.00 26.43  ? 380 ASN   D CB    1 
ATOM   9760  C  CG    . ASN   C 2  370 ? -17.827 -3.956  17.071   1.00 39.89  ? 380 ASN   D CG    1 
ATOM   9761  O  OD1   . ASN   C 2  370 ? -18.069 -5.163  16.981   1.00 45.71  ? 380 ASN   D OD1   1 
ATOM   9762  N  ND2   . ASN   C 2  370 ? -18.773 -3.019  16.953   1.00 33.27  ? 380 ASN   D ND2   1 
ATOM   9763  N  N     . SER   C 2  371 ? -14.469 -6.635  17.060   1.00 43.67  ? 381 SER   D N     1 
ATOM   9764  C  CA    . SER   C 2  371 ? -14.082 -7.736  16.184   1.00 38.56  ? 381 SER   D CA    1 
ATOM   9765  C  C     . SER   C 2  371 ? -15.225 -8.723  16.012   1.00 39.13  ? 381 SER   D C     1 
ATOM   9766  O  O     . SER   C 2  371 ? -15.912 -9.061  16.978   1.00 48.36  ? 381 SER   D O     1 
ATOM   9767  C  CB    . SER   C 2  371 ? -12.867 -8.465  16.763   1.00 36.95  ? 381 SER   D CB    1 
ATOM   9768  O  OG    . SER   C 2  371 ? -12.678 -9.708  16.121   1.00 45.31  ? 381 SER   D OG    1 
ATOM   9769  N  N     . THR   C 2  372 ? -15.431 -9.190  14.776   1.00 41.19  ? 382 THR   D N     1 
ATOM   9770  C  CA    . THR   C 2  372 ? -16.409 -10.254 14.551   1.00 39.20  ? 382 THR   D CA    1 
ATOM   9771  C  C     . THR   C 2  372 ? -16.004 -11.553 15.242   1.00 46.76  ? 382 THR   D C     1 
ATOM   9772  O  O     . THR   C 2  372 ? -16.804 -12.506 15.277   1.00 41.79  ? 382 THR   D O     1 
ATOM   9773  C  CB    . THR   C 2  372 ? -16.618 -10.504 13.044   1.00 41.97  ? 382 THR   D CB    1 
ATOM   9774  O  OG1   . THR   C 2  372 ? -15.499 -11.218 12.494   1.00 48.07  ? 382 THR   D OG1   1 
ATOM   9775  C  CG2   . THR   C 2  372 ? -16.776 -9.208  12.300   1.00 40.72  ? 382 THR   D CG2   1 
ATOM   9776  N  N     . ALA   C 2  373 ? -14.785 -11.611 15.798   1.00 42.47  ? 383 ALA   D N     1 
ATOM   9777  C  CA    . ALA   C 2  373 ? -14.348 -12.821 16.483   1.00 41.70  ? 383 ALA   D CA    1 
ATOM   9778  C  C     . ALA   C 2  373 ? -15.091 -13.020 17.793   1.00 48.60  ? 383 ALA   D C     1 
ATOM   9779  O  O     . ALA   C 2  373 ? -15.305 -14.167 18.202   1.00 54.57  ? 383 ALA   D O     1 
ATOM   9780  C  CB    . ALA   C 2  373 ? -12.841 -12.786 16.724   1.00 39.46  ? 383 ALA   D CB    1 
ATOM   9781  N  N     . ILE   C 2  374 ? -15.534 -11.934 18.437   1.00 44.76  ? 384 ILE   D N     1 
ATOM   9782  C  CA    A ILE   C 2  374 ? -16.216 -12.021 19.727   1.00 50.31  ? 384 ILE   D CA    1 
ATOM   9783  C  CA    B ILE   C 2  374 ? -16.231 -12.005 19.718   0.00 50.26  ? 384 ILE   D CA    1 
ATOM   9784  C  C     . ILE   C 2  374 ? -17.261 -13.127 19.694   1.00 50.77  ? 384 ILE   D C     1 
ATOM   9785  O  O     . ILE   C 2  374 ? -17.731 -13.571 20.742   1.00 49.23  ? 384 ILE   D O     1 
ATOM   9786  C  CB    A ILE   C 2  374 ? -16.873 -10.690 20.130   1.00 51.05  ? 384 ILE   D CB    1 
ATOM   9787  C  CB    B ILE   C 2  374 ? -16.896 -10.659 20.062   0.00 50.84  ? 384 ILE   D CB    1 
ATOM   9788  C  CG1   A ILE   C 2  374 ? -17.437 -10.785 21.551   1.00 45.99  ? 384 ILE   D CG1   1 
ATOM   9789  C  CG1   B ILE   C 2  374 ? -17.545 -10.722 21.446   0.00 46.66  ? 384 ILE   D CG1   1 
ATOM   9790  C  CG2   A ILE   C 2  374 ? -17.984 -10.331 19.159   1.00 49.11  ? 384 ILE   D CG2   1 
ATOM   9791  C  CG2   B ILE   C 2  374 ? -17.924 -10.287 19.005   0.00 48.95  ? 384 ILE   D CG2   1 
ATOM   9792  C  CD1   A ILE   C 2  374 ? -16.557 -10.144 22.592   1.00 46.48  ? 384 ILE   D CD1   1 
ATOM   9793  C  CD1   B ILE   C 2  374 ? -16.570 -11.020 22.564   0.00 49.41  ? 384 ILE   D CD1   1 
ATOM   9794  N  N     . GLN   C 2  375 ? -17.631 -13.578 18.492   1.00 49.17  ? 385 GLN   D N     1 
ATOM   9795  C  CA    . GLN   C 2  375 ? -18.547 -14.705 18.367   1.00 48.28  ? 385 GLN   D CA    1 
ATOM   9796  C  C     . GLN   C 2  375 ? -18.010 -15.948 19.061   1.00 55.95  ? 385 GLN   D C     1 
ATOM   9797  O  O     . GLN   C 2  375 ? -18.788 -16.817 19.468   1.00 54.72  ? 385 GLN   D O     1 
ATOM   9798  C  CB    . GLN   C 2  375 ? -18.787 -15.019 16.898   1.00 49.86  ? 385 GLN   D CB    1 
ATOM   9799  C  CG    . GLN   C 2  375 ? -17.523 -15.426 16.182   1.00 46.07  ? 385 GLN   D CG    1 
ATOM   9800  C  CD    . GLN   C 2  375 ? -17.803 -16.129 14.875   1.00 53.41  ? 385 GLN   D CD    1 
ATOM   9801  O  OE1   . GLN   C 2  375 ? -18.351 -17.232 14.847   1.00 44.63  ? 385 GLN   D OE1   1 
ATOM   9802  N  NE2   . GLN   C 2  375 ? -17.430 -15.489 13.776   1.00 57.36  ? 385 GLN   D NE2   1 
ATOM   9803  N  N     . GLU   C 2  376 ? -16.688 -16.083 19.166   1.00 55.76  ? 386 GLU   D N     1 
ATOM   9804  C  CA    . GLU   C 2  376 ? -16.150 -17.277 19.808   1.00 57.34  ? 386 GLU   D CA    1 
ATOM   9805  C  C     . GLU   C 2  376 ? -16.633 -17.372 21.245   1.00 59.07  ? 386 GLU   D C     1 
ATOM   9806  O  O     . GLU   C 2  376 ? -16.993 -18.457 21.716   1.00 59.95  ? 386 GLU   D O     1 
ATOM   9807  C  CB    . GLU   C 2  376 ? -14.623 -17.281 19.732   1.00 54.65  ? 386 GLU   D CB    1 
ATOM   9808  C  CG    . GLU   C 2  376 ? -14.126 -17.388 18.291   1.00 57.78  ? 386 GLU   D CG    1 
ATOM   9809  C  CD    . GLU   C 2  376 ? -12.652 -17.700 18.178   1.00 53.06  ? 386 GLU   D CD    1 
ATOM   9810  O  OE1   . GLU   C 2  376 ? -11.841 -17.126 18.951   1.00 52.33  ? 386 GLU   D OE1   1 
ATOM   9811  O  OE2   . GLU   C 2  376 ? -12.319 -18.532 17.307   1.00 51.83  ? 386 GLU   D OE2   1 
ATOM   9812  N  N     . LEU   C 2  377 ? -16.676 -16.233 21.943   1.00 59.14  ? 387 LEU   D N     1 
ATOM   9813  C  CA    . LEU   C 2  377 ? -17.219 -16.190 23.295   1.00 52.76  ? 387 LEU   D CA    1 
ATOM   9814  C  C     . LEU   C 2  377 ? -18.696 -16.568 23.315   1.00 50.03  ? 387 LEU   D C     1 
ATOM   9815  O  O     . LEU   C 2  377 ? -19.147 -17.253 24.235   1.00 61.47  ? 387 LEU   D O     1 
ATOM   9816  C  CB    . LEU   C 2  377 ? -16.999 -14.803 23.896   1.00 53.00  ? 387 LEU   D CB    1 
ATOM   9817  C  CG    . LEU   C 2  377 ? -17.596 -14.465 25.261   1.00 54.59  ? 387 LEU   D CG    1 
ATOM   9818  C  CD1   . LEU   C 2  377 ? -16.841 -13.296 25.875   1.00 53.09  ? 387 LEU   D CD1   1 
ATOM   9819  C  CD2   . LEU   C 2  377 ? -19.085 -14.142 25.141   1.00 51.66  ? 387 LEU   D CD2   1 
ATOM   9820  N  N     . PHE   C 2  378 ? -19.464 -16.147 22.315   1.00 42.56  ? 388 PHE   D N     1 
ATOM   9821  C  CA    . PHE   C 2  378 ? -20.876 -16.515 22.290   1.00 49.46  ? 388 PHE   D CA    1 
ATOM   9822  C  C     . PHE   C 2  378 ? -21.058 -17.975 21.905   1.00 54.97  ? 388 PHE   D C     1 
ATOM   9823  O  O     . PHE   C 2  378 ? -21.965 -18.647 22.409   1.00 62.14  ? 388 PHE   D O     1 
ATOM   9824  C  CB    . PHE   C 2  378 ? -21.660 -15.613 21.334   1.00 50.56  ? 388 PHE   D CB    1 
ATOM   9825  C  CG    . PHE   C 2  378 ? -21.777 -14.199 21.811   1.00 53.54  ? 388 PHE   D CG    1 
ATOM   9826  C  CD1   . PHE   C 2  378 ? -22.384 -13.917 23.024   1.00 54.07  ? 388 PHE   D CD1   1 
ATOM   9827  C  CD2   . PHE   C 2  378 ? -21.267 -13.153 21.061   1.00 50.65  ? 388 PHE   D CD2   1 
ATOM   9828  C  CE1   . PHE   C 2  378 ? -22.490 -12.627 23.476   1.00 47.70  ? 388 PHE   D CE1   1 
ATOM   9829  C  CE2   . PHE   C 2  378 ? -21.360 -11.861 21.513   1.00 43.20  ? 388 PHE   D CE2   1 
ATOM   9830  C  CZ    . PHE   C 2  378 ? -21.981 -11.599 22.717   1.00 53.47  ? 388 PHE   D CZ    1 
ATOM   9831  N  N     . LYS   C 2  379 ? -20.226 -18.480 20.997   1.00 63.34  ? 389 LYS   D N     1 
ATOM   9832  C  CA    . LYS   C 2  379 ? -20.282 -19.903 20.684   1.00 62.01  ? 389 LYS   D CA    1 
ATOM   9833  C  C     . LYS   C 2  379 ? -20.020 -20.742 21.929   1.00 63.23  ? 389 LYS   D C     1 
ATOM   9834  O  O     . LYS   C 2  379 ? -20.557 -21.851 22.060   1.00 56.17  ? 389 LYS   D O     1 
ATOM   9835  C  CB    . LYS   C 2  379 ? -19.280 -20.238 19.574   1.00 57.43  ? 389 LYS   D CB    1 
ATOM   9836  C  CG    . LYS   C 2  379 ? -19.792 -19.974 18.154   1.00 61.59  ? 389 LYS   D CG    1 
ATOM   9837  C  CD    . LYS   C 2  379 ? -18.638 -19.705 17.197   1.00 56.39  ? 389 LYS   D CD    1 
ATOM   9838  C  CE    . LYS   C 2  379 ? -19.013 -20.014 15.757   1.00 44.92  ? 389 LYS   D CE    1 
ATOM   9839  N  NZ    . LYS   C 2  379 ? -19.132 -21.480 15.521   1.00 64.06  ? 389 LYS   D NZ    1 
ATOM   9840  N  N     . ARG   C 2  380 ? -19.220 -20.220 22.862   1.00 55.78  ? 390 ARG   D N     1 
ATOM   9841  C  CA    . ARG   C 2  380 ? -18.875 -20.987 24.049   1.00 52.63  ? 390 ARG   D CA    1 
ATOM   9842  C  C     . ARG   C 2  380 ? -19.994 -20.936 25.082   1.00 66.74  ? 390 ARG   D C     1 
ATOM   9843  O  O     . ARG   C 2  380 ? -20.410 -21.978 25.602   1.00 70.68  ? 390 ARG   D O     1 
ATOM   9844  C  CB    . ARG   C 2  380 ? -17.571 -20.477 24.651   1.00 45.07  ? 390 ARG   D CB    1 
ATOM   9845  C  CG    . ARG   C 2  380 ? -17.041 -21.358 25.752   1.00 47.88  ? 390 ARG   D CG    1 
ATOM   9846  C  CD    . ARG   C 2  380 ? -15.910 -20.678 26.464   1.00 48.29  ? 390 ARG   D CD    1 
ATOM   9847  N  NE    . ARG   C 2  380 ? -16.361 -19.520 27.221   1.00 49.76  ? 390 ARG   D NE    1 
ATOM   9848  C  CZ    . ARG   C 2  380 ? -15.543 -18.630 27.767   1.00 56.48  ? 390 ARG   D CZ    1 
ATOM   9849  N  NH1   . ARG   C 2  380 ? -14.234 -18.714 27.614   1.00 61.71  ? 390 ARG   D NH1   1 
ATOM   9850  N  NH2   . ARG   C 2  380 ? -16.050 -17.632 28.488   1.00 55.59  ? 390 ARG   D NH2   1 
ATOM   9851  N  N     . ILE   C 2  381 ? -20.496 -19.734 25.392   1.00 58.30  ? 391 ILE   D N     1 
ATOM   9852  C  CA    . ILE   C 2  381 ? -21.659 -19.634 26.270   1.00 54.96  ? 391 ILE   D CA    1 
ATOM   9853  C  C     . ILE   C 2  381 ? -22.796 -20.491 25.742   1.00 59.16  ? 391 ILE   D C     1 
ATOM   9854  O  O     . ILE   C 2  381 ? -23.596 -21.020 26.521   1.00 64.72  ? 391 ILE   D O     1 
ATOM   9855  C  CB    . ILE   C 2  381 ? -22.106 -18.165 26.441   1.00 51.30  ? 391 ILE   D CB    1 
ATOM   9856  C  CG1   . ILE   C 2  381 ? -21.030 -17.350 27.150   1.00 48.39  ? 391 ILE   D CG1   1 
ATOM   9857  C  CG2   . ILE   C 2  381 ? -23.424 -18.088 27.205   1.00 47.26  ? 391 ILE   D CG2   1 
ATOM   9858  C  CD1   . ILE   C 2  381 ? -20.338 -18.075 28.253   1.00 50.25  ? 391 ILE   D CD1   1 
ATOM   9859  N  N     . SER   C 2  382 ? -22.884 -20.657 24.420   1.00 53.16  ? 392 SER   D N     1 
ATOM   9860  C  CA    . SER   C 2  382 ? -24.014 -21.374 23.840   1.00 54.29  ? 392 SER   D CA    1 
ATOM   9861  C  C     . SER   C 2  382 ? -23.889 -22.886 24.023   1.00 66.23  ? 392 SER   D C     1 
ATOM   9862  O  O     . SER   C 2  382 ? -24.874 -23.555 24.361   1.00 63.47  ? 392 SER   D O     1 
ATOM   9863  C  CB    . SER   C 2  382 ? -24.153 -21.018 22.363   1.00 52.62  ? 392 SER   D CB    1 
ATOM   9864  O  OG    . SER   C 2  382 ? -25.098 -21.855 21.724   1.00 56.17  ? 392 SER   D OG    1 
ATOM   9865  N  N     . GLU   C 2  383 ? -22.698 -23.447 23.792   1.00 71.98  ? 393 GLU   D N     1 
ATOM   9866  C  CA    . GLU   C 2  383 ? -22.513 -24.884 23.977   1.00 65.93  ? 393 GLU   D CA    1 
ATOM   9867  C  C     . GLU   C 2  383 ? -22.834 -25.273 25.414   1.00 70.43  ? 393 GLU   D C     1 
ATOM   9868  O  O     . GLU   C 2  383 ? -23.737 -26.077 25.667   1.00 77.04  ? 393 GLU   D O     1 
ATOM   9869  C  CB    . GLU   C 2  383 ? -21.084 -25.287 23.599   1.00 66.69  ? 393 GLU   D CB    1 
ATOM   9870  C  CG    . GLU   C 2  383 ? -20.903 -26.770 23.282   1.00 62.94  ? 393 GLU   D CG    1 
ATOM   9871  C  CD    . GLU   C 2  383 ? -19.479 -27.115 22.849   1.00 84.25  ? 393 GLU   D CD    1 
ATOM   9872  O  OE1   . GLU   C 2  383 ? -18.579 -26.255 23.012   1.00 84.23  ? 393 GLU   D OE1   1 
ATOM   9873  O  OE2   . GLU   C 2  383 ? -19.256 -28.244 22.345   1.00 83.92  ? 393 GLU   D OE2   1 
ATOM   9874  N  N     . GLN   C 2  384 ? -22.119 -24.674 26.375   1.00 61.31  ? 394 GLN   D N     1 
ATOM   9875  C  CA    . GLN   C 2  384 ? -22.442 -24.810 27.792   1.00 62.19  ? 394 GLN   D CA    1 
ATOM   9876  C  C     . GLN   C 2  384 ? -23.931 -24.623 28.090   1.00 68.14  ? 394 GLN   D C     1 
ATOM   9877  O  O     . GLN   C 2  384 ? -24.406 -25.082 29.134   1.00 68.37  ? 394 GLN   D O     1 
ATOM   9878  C  CB    . GLN   C 2  384 ? -21.616 -23.800 28.598   1.00 44.47  ? 394 GLN   D CB    1 
ATOM   9879  C  CG    . GLN   C 2  384 ? -20.142 -23.895 28.330   1.00 44.41  ? 394 GLN   D CG    1 
ATOM   9880  C  CD    . GLN   C 2  384 ? -19.330 -22.849 29.071   1.00 65.34  ? 394 GLN   D CD    1 
ATOM   9881  O  OE1   . GLN   C 2  384 ? -19.868 -21.854 29.559   1.00 67.98  ? 394 GLN   D OE1   1 
ATOM   9882  N  NE2   . GLN   C 2  384 ? -18.017 -23.070 29.153   1.00 69.39  ? 394 GLN   D NE2   1 
ATOM   9883  N  N     . PHE   C 2  385 ? -24.671 -23.942 27.214   1.00 62.51  ? 395 PHE   D N     1 
ATOM   9884  C  CA    . PHE   C 2  385 ? -26.102 -23.749 27.416   1.00 62.36  ? 395 PHE   D CA    1 
ATOM   9885  C  C     . PHE   C 2  385 ? -26.884 -24.969 26.948   1.00 70.49  ? 395 PHE   D C     1 
ATOM   9886  O  O     . PHE   C 2  385 ? -27.683 -25.536 27.705   1.00 74.15  ? 395 PHE   D O     1 
ATOM   9887  C  CB    . PHE   C 2  385 ? -26.566 -22.483 26.677   1.00 62.80  ? 395 PHE   D CB    1 
ATOM   9888  C  CG    . PHE   C 2  385 ? -28.067 -22.286 26.642   1.00 44.17  ? 395 PHE   D CG    1 
ATOM   9889  C  CD1   . PHE   C 2  385 ? -28.853 -22.970 25.736   1.00 49.75  ? 395 PHE   D CD1   1 
ATOM   9890  C  CD2   . PHE   C 2  385 ? -28.677 -21.386 27.494   1.00 46.39  ? 395 PHE   D CD2   1 
ATOM   9891  C  CE1   . PHE   C 2  385 ? -30.222 -22.781 25.702   1.00 50.18  ? 395 PHE   D CE1   1 
ATOM   9892  C  CE2   . PHE   C 2  385 ? -30.036 -21.191 27.454   1.00 40.53  ? 395 PHE   D CE2   1 
ATOM   9893  C  CZ    . PHE   C 2  385 ? -30.808 -21.893 26.554   1.00 41.26  ? 395 PHE   D CZ    1 
ATOM   9894  N  N     . THR   C 2  386 ? -26.670 -25.388 25.701   1.00 72.11  ? 396 THR   D N     1 
ATOM   9895  C  CA    . THR   C 2  386 ? -27.414 -26.521 25.172   1.00 79.38  ? 396 THR   D CA    1 
ATOM   9896  C  C     . THR   C 2  386 ? -26.886 -27.864 25.674   1.00 78.39  ? 396 THR   D C     1 
ATOM   9897  O  O     . THR   C 2  386 ? -27.523 -28.893 25.418   1.00 80.26  ? 396 THR   D O     1 
ATOM   9898  C  CB    . THR   C 2  386 ? -27.419 -26.471 23.641   1.00 75.64  ? 396 THR   D CB    1 
ATOM   9899  O  OG1   . THR   C 2  386 ? -28.305 -27.476 23.133   1.00 75.17  ? 396 THR   D OG1   1 
ATOM   9900  C  CG2   . THR   C 2  386 ? -26.023 -26.687 23.099   1.00 76.82  ? 396 THR   D CG2   1 
ATOM   9901  N  N     . ALA   C 2  387 ? -25.752 -27.877 26.386   1.00 69.82  ? 397 ALA   D N     1 
ATOM   9902  C  CA    . ALA   C 2  387 ? -25.320 -29.020 27.185   1.00 71.43  ? 397 ALA   D CA    1 
ATOM   9903  C  C     . ALA   C 2  387 ? -26.097 -29.139 28.488   1.00 84.26  ? 397 ALA   D C     1 
ATOM   9904  O  O     . ALA   C 2  387 ? -25.739 -29.966 29.337   1.00 84.46  ? 397 ALA   D O     1 
ATOM   9905  C  CB    . ALA   C 2  387 ? -23.824 -28.929 27.502   1.00 65.80  ? 397 ALA   D CB    1 
ATOM   9906  N  N     . MET   C 2  388 ? -27.123 -28.304 28.666   1.00 77.01  ? 398 MET   D N     1 
ATOM   9907  C  CA    . MET   C 2  388 ? -28.034 -28.396 29.794   1.00 71.22  ? 398 MET   D CA    1 
ATOM   9908  C  C     . MET   C 2  388 ? -29.465 -28.276 29.291   1.00 76.02  ? 398 MET   D C     1 
ATOM   9909  O  O     . MET   C 2  388 ? -30.301 -29.130 29.593   1.00 79.05  ? 398 MET   D O     1 
ATOM   9910  C  CB    . MET   C 2  388 ? -27.728 -27.322 30.835   1.00 66.93  ? 398 MET   D CB    1 
ATOM   9911  C  CG    . MET   C 2  388 ? -26.334 -27.409 31.416   1.00 70.53  ? 398 MET   D CG    1 
ATOM   9912  S  SD    . MET   C 2  388 ? -26.113 -26.417 32.916   1.00 83.86  ? 398 MET   D SD    1 
ATOM   9913  C  CE    . MET   C 2  388 ? -24.324 -26.252 32.920   1.00 71.13  ? 398 MET   D CE    1 
ATOM   9914  N  N     . PHE   C 2  389 ? -29.759 -27.235 28.506   1.00 74.46  ? 399 PHE   D N     1 
ATOM   9915  C  CA    . PHE   C 2  389 ? -31.115 -27.078 27.989   1.00 76.15  ? 399 PHE   D CA    1 
ATOM   9916  C  C     . PHE   C 2  389 ? -31.554 -28.268 27.140   1.00 81.11  ? 399 PHE   D C     1 
ATOM   9917  O  O     . PHE   C 2  389 ? -32.761 -28.511 27.003   1.00 71.78  ? 399 PHE   D O     1 
ATOM   9918  C  CB    . PHE   C 2  389 ? -31.236 -25.791 27.178   1.00 62.98  ? 399 PHE   D CB    1 
ATOM   9919  C  CG    . PHE   C 2  389 ? -32.642 -25.485 26.740   1.00 60.15  ? 399 PHE   D CG    1 
ATOM   9920  C  CD1   . PHE   C 2  389 ? -33.559 -24.943 27.631   1.00 54.46  ? 399 PHE   D CD1   1 
ATOM   9921  C  CD2   . PHE   C 2  389 ? -33.049 -25.734 25.432   1.00 67.81  ? 399 PHE   D CD2   1 
ATOM   9922  C  CE1   . PHE   C 2  389 ? -34.855 -24.655 27.228   1.00 63.18  ? 399 PHE   D CE1   1 
ATOM   9923  C  CE2   . PHE   C 2  389 ? -34.348 -25.445 25.009   1.00 64.93  ? 399 PHE   D CE2   1 
ATOM   9924  C  CZ    . PHE   C 2  389 ? -35.254 -24.906 25.905   1.00 67.92  ? 399 PHE   D CZ    1 
ATOM   9925  N  N     . ARG   C 2  390 ? -30.603 -29.000 26.552   1.00 85.00  ? 400 ARG   D N     1 
ATOM   9926  C  CA    . ARG   C 2  390 ? -30.928 -30.278 25.928   1.00 84.35  ? 400 ARG   D CA    1 
ATOM   9927  C  C     . ARG   C 2  390 ? -31.651 -31.184 26.914   1.00 87.72  ? 400 ARG   D C     1 
ATOM   9928  O  O     . ARG   C 2  390 ? -32.724 -31.725 26.621   1.00 82.73  ? 400 ARG   D O     1 
ATOM   9929  C  CB    . ARG   C 2  390 ? -29.649 -30.953 25.425   1.00 83.06  ? 400 ARG   D CB    1 
ATOM   9930  C  CG    . ARG   C 2  390 ? -29.656 -31.249 23.943   1.00 93.96  ? 400 ARG   D CG    1 
ATOM   9931  C  CD    . ARG   C 2  390 ? -30.044 -30.001 23.166   1.00 102.24 ? 400 ARG   D CD    1 
ATOM   9932  N  NE    . ARG   C 2  390 ? -30.288 -30.260 21.750   1.00 110.63 ? 400 ARG   D NE    1 
ATOM   9933  C  CZ    . ARG   C 2  390 ? -29.373 -30.149 20.794   1.00 105.34 ? 400 ARG   D CZ    1 
ATOM   9934  N  NH1   . ARG   C 2  390 ? -28.117 -29.831 21.071   1.00 101.97 ? 400 ARG   D NH1   1 
ATOM   9935  N  NH2   . ARG   C 2  390 ? -29.730 -30.357 19.529   1.00 95.77  ? 400 ARG   D NH2   1 
ATOM   9936  N  N     . ARG   C 2  391 ? -31.071 -31.341 28.106   1.00 92.91  ? 401 ARG   D N     1 
ATOM   9937  C  CA    . ARG   C 2  391 ? -31.569 -32.225 29.149   1.00 83.84  ? 401 ARG   D CA    1 
ATOM   9938  C  C     . ARG   C 2  391 ? -32.485 -31.515 30.140   1.00 81.37  ? 401 ARG   D C     1 
ATOM   9939  O  O     . ARG   C 2  391 ? -32.601 -31.970 31.283   1.00 82.00  ? 401 ARG   D O     1 
ATOM   9940  C  CB    . ARG   C 2  391 ? -30.395 -32.854 29.907   1.00 80.02  ? 401 ARG   D CB    1 
ATOM   9941  C  CG    . ARG   C 2  391 ? -29.195 -33.257 29.050   1.00 82.59  ? 401 ARG   D CG    1 
ATOM   9942  C  CD    . ARG   C 2  391 ? -27.916 -32.827 29.738   1.00 81.09  ? 401 ARG   D CD    1 
ATOM   9943  N  NE    . ARG   C 2  391 ? -28.161 -32.624 31.161   1.00 82.18  ? 401 ARG   D NE    1 
ATOM   9944  C  CZ    . ARG   C 2  391 ? -27.275 -32.151 32.027   1.00 79.59  ? 401 ARG   D CZ    1 
ATOM   9945  N  NH1   . ARG   C 2  391 ? -26.056 -31.799 31.650   1.00 77.27  ? 401 ARG   D NH1   1 
ATOM   9946  N  NH2   . ARG   C 2  391 ? -27.621 -32.031 33.305   1.00 85.33  ? 401 ARG   D NH2   1 
ATOM   9947  N  N     . LYS   C 2  392 ? -33.089 -30.385 29.756   1.00 79.10  ? 402 LYS   D N     1 
ATOM   9948  C  CA    . LYS   C 2  392 ? -34.042 -29.679 30.611   1.00 71.72  ? 402 LYS   D CA    1 
ATOM   9949  C  C     . LYS   C 2  392 ? -33.491 -29.502 32.026   1.00 64.17  ? 402 LYS   D C     1 
ATOM   9950  O  O     . LYS   C 2  392 ? -34.214 -29.095 32.938   1.00 69.88  ? 402 LYS   D O     1 
ATOM   9951  C  CB    . LYS   C 2  392 ? -35.374 -30.438 30.623   1.00 77.23  ? 402 LYS   D CB    1 
ATOM   9952  C  CG    . LYS   C 2  392 ? -36.635 -29.586 30.801   1.00 90.12  ? 402 LYS   D CG    1 
ATOM   9953  C  CD    . LYS   C 2  392 ? -37.906 -30.457 30.873   1.00 82.61  ? 402 LYS   D CD    1 
ATOM   9954  C  CE    . LYS   C 2  392 ? -39.057 -29.725 31.574   1.00 81.79  ? 402 LYS   D CE    1 
ATOM   9955  N  NZ    . LYS   C 2  392 ? -40.137 -30.639 32.079   1.00 62.32  ? 402 LYS   D NZ    1 
ATOM   9956  N  N     . ALA   C 2  393 ? -32.198 -29.761 32.197   1.00 68.33  ? 403 ALA   D N     1 
ATOM   9957  C  CA    . ALA   C 2  393 ? -31.581 -29.869 33.512   1.00 71.94  ? 403 ALA   D CA    1 
ATOM   9958  C  C     . ALA   C 2  393 ? -31.612 -28.545 34.268   1.00 78.17  ? 403 ALA   D C     1 
ATOM   9959  O  O     . ALA   C 2  393 ? -31.224 -27.501 33.734   1.00 81.19  ? 403 ALA   D O     1 
ATOM   9960  C  CB    . ALA   C 2  393 ? -30.137 -30.351 33.366   1.00 72.71  ? 403 ALA   D CB    1 
ATOM   9961  N  N     . PHE   C 2  394 ? -32.041 -28.600 35.529   1.00 75.07  ? 404 PHE   D N     1 
ATOM   9962  C  CA    . PHE   C 2  394 ? -32.081 -27.468 36.447   1.00 70.68  ? 404 PHE   D CA    1 
ATOM   9963  C  C     . PHE   C 2  394 ? -33.104 -26.417 36.046   1.00 68.81  ? 404 PHE   D C     1 
ATOM   9964  O  O     . PHE   C 2  394 ? -33.138 -25.344 36.659   1.00 69.77  ? 404 PHE   D O     1 
ATOM   9965  C  CB    . PHE   C 2  394 ? -30.714 -26.792 36.581   1.00 78.53  ? 404 PHE   D CB    1 
ATOM   9966  C  CG    . PHE   C 2  394 ? -29.724 -27.557 37.420   1.00 82.74  ? 404 PHE   D CG    1 
ATOM   9967  C  CD1   . PHE   C 2  394 ? -29.672 -27.369 38.800   1.00 90.46  ? 404 PHE   D CD1   1 
ATOM   9968  C  CD2   . PHE   C 2  394 ? -28.820 -28.435 36.828   1.00 84.09  ? 404 PHE   D CD2   1 
ATOM   9969  C  CE1   . PHE   C 2  394 ? -28.747 -28.059 39.583   1.00 90.91  ? 404 PHE   D CE1   1 
ATOM   9970  C  CE2   . PHE   C 2  394 ? -27.892 -29.129 37.599   1.00 82.20  ? 404 PHE   D CE2   1 
ATOM   9971  C  CZ    . PHE   C 2  394 ? -27.854 -28.940 38.979   1.00 85.18  ? 404 PHE   D CZ    1 
ATOM   9972  N  N     . LEU   C 2  395 ? -33.940 -26.690 35.039   1.00 58.55  ? 405 LEU   D N     1 
ATOM   9973  C  CA    . LEU   C 2  395 ? -34.904 -25.695 34.579   1.00 75.56  ? 405 LEU   D CA    1 
ATOM   9974  C  C     . LEU   C 2  395 ? -36.021 -25.422 35.589   1.00 81.25  ? 405 LEU   D C     1 
ATOM   9975  O  O     . LEU   C 2  395 ? -36.726 -24.413 35.458   1.00 74.75  ? 405 LEU   D O     1 
ATOM   9976  C  CB    . LEU   C 2  395 ? -35.524 -26.130 33.256   1.00 74.68  ? 405 LEU   D CB    1 
ATOM   9977  C  CG    . LEU   C 2  395 ? -36.995 -26.534 33.396   1.00 87.77  ? 405 LEU   D CG    1 
ATOM   9978  C  CD1   . LEU   C 2  395 ? -37.653 -26.628 32.024   1.00 93.98  ? 405 LEU   D CD1   1 
ATOM   9979  C  CD2   . LEU   C 2  395 ? -37.157 -27.854 34.173   1.00 89.94  ? 405 LEU   D CD2   1 
ATOM   9980  N  N     . HIS   C 2  396 ? -36.226 -26.302 36.573   1.00 86.43  ? 406 HIS   D N     1 
ATOM   9981  C  CA    . HIS   C 2  396 ? -37.258 -26.034 37.568   1.00 79.15  ? 406 HIS   D CA    1 
ATOM   9982  C  C     . HIS   C 2  396 ? -36.968 -24.730 38.304   1.00 78.27  ? 406 HIS   D C     1 
ATOM   9983  O  O     . HIS   C 2  396 ? -37.890 -23.954 38.588   1.00 74.33  ? 406 HIS   D O     1 
ATOM   9984  C  CB    . HIS   C 2  396 ? -37.401 -27.219 38.540   1.00 88.85  ? 406 HIS   D CB    1 
ATOM   9985  C  CG    . HIS   C 2  396 ? -36.155 -27.561 39.309   1.00 88.31  ? 406 HIS   D CG    1 
ATOM   9986  N  ND1   . HIS   C 2  396 ? -35.335 -28.618 38.968   1.00 81.35  ? 406 HIS   D ND1   1 
ATOM   9987  C  CD2   . HIS   C 2  396 ? -35.614 -27.013 40.425   1.00 84.87  ? 406 HIS   D CD2   1 
ATOM   9988  C  CE1   . HIS   C 2  396 ? -34.331 -28.689 39.825   1.00 89.77  ? 406 HIS   D CE1   1 
ATOM   9989  N  NE2   . HIS   C 2  396 ? -34.475 -27.725 40.718   1.00 89.36  ? 406 HIS   D NE2   1 
ATOM   9990  N  N     . TRP   C 2  397 ? -35.687 -24.450 38.580   1.00 74.60  ? 407 TRP   D N     1 
ATOM   9991  C  CA    . TRP   C 2  397 ? -35.323 -23.176 39.197   1.00 73.78  ? 407 TRP   D CA    1 
ATOM   9992  C  C     . TRP   C 2  397 ? -35.998 -22.007 38.494   1.00 73.34  ? 407 TRP   D C     1 
ATOM   9993  O  O     . TRP   C 2  397 ? -36.306 -20.993 39.134   1.00 67.80  ? 407 TRP   D O     1 
ATOM   9994  C  CB    . TRP   C 2  397 ? -33.799 -22.961 39.175   1.00 79.24  ? 407 TRP   D CB    1 
ATOM   9995  C  CG    . TRP   C 2  397 ? -32.973 -23.707 40.212   1.00 88.68  ? 407 TRP   D CG    1 
ATOM   9996  C  CD1   . TRP   C 2  397 ? -33.358 -24.781 40.973   1.00 91.34  ? 407 TRP   D CD1   1 
ATOM   9997  C  CD2   . TRP   C 2  397 ? -31.614 -23.422 40.587   1.00 88.28  ? 407 TRP   D CD2   1 
ATOM   9998  N  NE1   . TRP   C 2  397 ? -32.325 -25.175 41.794   1.00 86.66  ? 407 TRP   D NE1   1 
ATOM   9999  C  CE2   . TRP   C 2  397 ? -31.246 -24.356 41.576   1.00 91.30  ? 407 TRP   D CE2   1 
ATOM   10000 C  CE3   . TRP   C 2  397 ? -30.675 -22.467 40.184   1.00 81.35  ? 407 TRP   D CE3   1 
ATOM   10001 C  CZ2   . TRP   C 2  397 ? -29.976 -24.359 42.161   1.00 93.82  ? 407 TRP   D CZ2   1 
ATOM   10002 C  CZ3   . TRP   C 2  397 ? -29.412 -22.471 40.777   1.00 73.19  ? 407 TRP   D CZ3   1 
ATOM   10003 C  CH2   . TRP   C 2  397 ? -29.078 -23.407 41.747   1.00 74.96  ? 407 TRP   D CH2   1 
ATOM   10004 N  N     . TYR   C 2  398 ? -36.233 -22.123 37.183   1.00 69.15  ? 408 TYR   D N     1 
ATOM   10005 C  CA    . TYR   C 2  398 ? -36.727 -20.999 36.395   1.00 69.96  ? 408 TYR   D CA    1 
ATOM   10006 C  C     . TYR   C 2  398 ? -38.227 -21.048 36.149   1.00 64.08  ? 408 TYR   D C     1 
ATOM   10007 O  O     . TYR   C 2  398 ? -38.878 -20.006 36.250   1.00 60.54  ? 408 TYR   D O     1 
ATOM   10008 C  CB    . TYR   C 2  398 ? -35.971 -20.890 35.057   1.00 63.43  ? 408 TYR   D CB    1 
ATOM   10009 C  CG    . TYR   C 2  398 ? -34.499 -20.592 35.255   1.00 60.47  ? 408 TYR   D CG    1 
ATOM   10010 C  CD1   . TYR   C 2  398 ? -34.062 -19.311 35.556   1.00 64.15  ? 408 TYR   D CD1   1 
ATOM   10011 C  CD2   . TYR   C 2  398 ? -33.553 -21.601 35.180   1.00 67.22  ? 408 TYR   D CD2   1 
ATOM   10012 C  CE1   . TYR   C 2  398 ? -32.721 -19.043 35.762   1.00 64.42  ? 408 TYR   D CE1   1 
ATOM   10013 C  CE2   . TYR   C 2  398 ? -32.209 -21.345 35.383   1.00 66.12  ? 408 TYR   D CE2   1 
ATOM   10014 C  CZ    . TYR   C 2  398 ? -31.796 -20.068 35.675   1.00 67.57  ? 408 TYR   D CZ    1 
ATOM   10015 O  OH    . TYR   C 2  398 ? -30.454 -19.823 35.878   1.00 61.81  ? 408 TYR   D OH    1 
ATOM   10016 N  N     . THR   C 2  399 ? -38.813 -22.214 35.836   1.00 61.96  ? 409 THR   D N     1 
ATOM   10017 C  CA    . THR   C 2  399 ? -40.274 -22.261 35.786   1.00 57.54  ? 409 THR   D CA    1 
ATOM   10018 C  C     . THR   C 2  399 ? -40.864 -21.992 37.161   1.00 67.84  ? 409 THR   D C     1 
ATOM   10019 O  O     . THR   C 2  399 ? -41.926 -21.363 37.273   1.00 63.09  ? 409 THR   D O     1 
ATOM   10020 C  CB    . THR   C 2  399 ? -40.792 -23.606 35.281   1.00 58.33  ? 409 THR   D CB    1 
ATOM   10021 O  OG1   . THR   C 2  399 ? -40.002 -24.068 34.183   1.00 57.63  ? 409 THR   D OG1   1 
ATOM   10022 C  CG2   . THR   C 2  399 ? -42.243 -23.462 34.834   1.00 53.10  ? 409 THR   D CG2   1 
ATOM   10023 N  N     . GLY   C 2  400 ? -40.184 -22.450 38.218   1.00 61.81  ? 410 GLY   D N     1 
ATOM   10024 C  CA    . GLY   C 2  400 ? -40.642 -22.168 39.568   1.00 62.00  ? 410 GLY   D CA    1 
ATOM   10025 C  C     . GLY   C 2  400 ? -40.910 -20.697 39.821   1.00 68.38  ? 410 GLY   D C     1 
ATOM   10026 O  O     . GLY   C 2  400 ? -41.752 -20.346 40.657   1.00 70.38  ? 410 GLY   D O     1 
ATOM   10027 N  N     . GLU   C 2  401 ? -40.204 -19.818 39.116   1.00 73.19  ? 411 GLU   D N     1 
ATOM   10028 C  CA    . GLU   C 2  401 ? -40.378 -18.382 39.268   1.00 66.59  ? 411 GLU   D CA    1 
ATOM   10029 C  C     . GLU   C 2  401 ? -41.377 -17.803 38.289   1.00 59.62  ? 411 GLU   D C     1 
ATOM   10030 O  O     . GLU   C 2  401 ? -41.549 -16.584 38.262   1.00 65.62  ? 411 GLU   D O     1 
ATOM   10031 C  CB    . GLU   C 2  401 ? -39.037 -17.670 39.123   1.00 66.05  ? 411 GLU   D CB    1 
ATOM   10032 C  CG    . GLU   C 2  401 ? -38.130 -17.881 40.320   1.00 70.83  ? 411 GLU   D CG    1 
ATOM   10033 C  CD    . GLU   C 2  401 ? -38.859 -17.658 41.626   1.00 68.20  ? 411 GLU   D CD    1 
ATOM   10034 O  OE1   . GLU   C 2  401 ? -39.647 -18.543 42.000   1.00 73.73  ? 411 GLU   D OE1   1 
ATOM   10035 O  OE2   . GLU   C 2  401 ? -38.665 -16.599 42.264   1.00 66.88  ? 411 GLU   D OE2   1 
ATOM   10036 N  N     . GLY   C 2  402 ? -42.042 -18.648 37.498   1.00 55.70  ? 412 GLY   D N     1 
ATOM   10037 C  CA    . GLY   C 2  402 ? -43.082 -18.223 36.580   1.00 60.15  ? 412 GLY   D CA    1 
ATOM   10038 C  C     . GLY   C 2  402 ? -42.687 -18.260 35.122   1.00 63.49  ? 412 GLY   D C     1 
ATOM   10039 O  O     . GLY   C 2  402 ? -43.501 -17.893 34.263   1.00 53.49  ? 412 GLY   D O     1 
ATOM   10040 N  N     . MET   C 2  403 ? -41.474 -18.694 34.816   1.00 63.26  ? 413 MET   D N     1 
ATOM   10041 C  CA    . MET   C 2  403 ? -40.920 -18.605 33.476   1.00 63.20  ? 413 MET   D CA    1 
ATOM   10042 C  C     . MET   C 2  403 ? -41.347 -19.809 32.638   1.00 61.32  ? 413 MET   D C     1 
ATOM   10043 O  O     . MET   C 2  403 ? -41.706 -20.865 33.164   1.00 68.07  ? 413 MET   D O     1 
ATOM   10044 C  CB    . MET   C 2  403 ? -39.400 -18.510 33.564   1.00 58.68  ? 413 MET   D CB    1 
ATOM   10045 C  CG    . MET   C 2  403 ? -38.733 -17.755 32.470   1.00 60.68  ? 413 MET   D CG    1 
ATOM   10046 S  SD    . MET   C 2  403 ? -37.037 -17.475 32.964   1.00 60.96  ? 413 MET   D SD    1 
ATOM   10047 C  CE    . MET   C 2  403 ? -37.272 -16.358 34.335   1.00 55.41  ? 413 MET   D CE    1 
ATOM   10048 N  N     . ASP   C 2  404 ? -41.302 -19.632 31.317   1.00 64.46  ? 414 ASP   D N     1 
ATOM   10049 C  CA    . ASP   C 2  404 ? -41.836 -20.584 30.352   1.00 56.67  ? 414 ASP   D CA    1 
ATOM   10050 C  C     . ASP   C 2  404 ? -40.713 -21.219 29.542   1.00 65.33  ? 414 ASP   D C     1 
ATOM   10051 O  O     . ASP   C 2  404 ? -39.520 -21.005 29.775   1.00 65.13  ? 414 ASP   D O     1 
ATOM   10052 C  CB    . ASP   C 2  404 ? -42.860 -19.912 29.428   1.00 62.53  ? 414 ASP   D CB    1 
ATOM   10053 C  CG    . ASP   C 2  404 ? -42.371 -18.560 28.867   1.00 79.83  ? 414 ASP   D CG    1 
ATOM   10054 O  OD1   . ASP   C 2  404 ? -41.714 -17.777 29.603   1.00 64.51  ? 414 ASP   D OD1   1 
ATOM   10055 O  OD2   . ASP   C 2  404 ? -42.658 -18.271 27.681   1.00 81.99  ? 414 ASP   D OD2   1 
ATOM   10056 N  N     . GLU   C 2  405 ? -41.119 -22.022 28.571   1.00 70.18  ? 415 GLU   D N     1 
ATOM   10057 C  CA    . GLU   C 2  405 ? -40.152 -22.762 27.773   1.00 83.69  ? 415 GLU   D CA    1 
ATOM   10058 C  C     . GLU   C 2  405 ? -39.512 -21.865 26.721   1.00 77.22  ? 415 GLU   D C     1 
ATOM   10059 O  O     . GLU   C 2  405 ? -38.282 -21.807 26.613   1.00 70.25  ? 415 GLU   D O     1 
ATOM   10060 C  CB    . GLU   C 2  405 ? -40.846 -23.962 27.125   1.00 89.70  ? 415 GLU   D CB    1 
ATOM   10061 C  CG    . GLU   C 2  405 ? -42.329 -23.685 26.834   1.00 92.74  ? 415 GLU   D CG    1 
ATOM   10062 C  CD    . GLU   C 2  405 ? -42.991 -24.738 25.963   1.00 98.21  ? 415 GLU   D CD    1 
ATOM   10063 O  OE1   . GLU   C 2  405 ? -42.267 -25.542 25.333   1.00 90.68  ? 415 GLU   D OE1   1 
ATOM   10064 O  OE2   . GLU   C 2  405 ? -44.241 -24.753 25.909   1.00 102.09 ? 415 GLU   D OE2   1 
ATOM   10065 N  N     . MET   C 2  406 ? -40.342 -21.142 25.956   1.00 79.19  ? 416 MET   D N     1 
ATOM   10066 C  CA    . MET   C 2  406 ? -39.854 -20.317 24.852   1.00 76.30  ? 416 MET   D CA    1 
ATOM   10067 C  C     . MET   C 2  406 ? -38.711 -19.414 25.293   1.00 70.36  ? 416 MET   D C     1 
ATOM   10068 O  O     . MET   C 2  406 ? -37.677 -19.327 24.622   1.00 70.41  ? 416 MET   D O     1 
ATOM   10069 C  CB    . MET   C 2  406 ? -40.996 -19.472 24.284   1.00 76.13  ? 416 MET   D CB    1 
ATOM   10070 C  CG    . MET   C 2  406 ? -42.294 -20.214 24.147   1.00 81.52  ? 416 MET   D CG    1 
ATOM   10071 S  SD    . MET   C 2  406 ? -42.050 -21.798 23.328   1.00 112.56 ? 416 MET   D SD    1 
ATOM   10072 C  CE    . MET   C 2  406 ? -43.622 -22.601 23.672   1.00 96.09  ? 416 MET   D CE    1 
ATOM   10073 N  N     . GLU   C 2  407 ? -38.886 -18.734 26.429   1.00 65.92  ? 417 GLU   D N     1 
ATOM   10074 C  CA    . GLU   C 2  407 ? -37.912 -17.743 26.870   1.00 61.40  ? 417 GLU   D CA    1 
ATOM   10075 C  C     . GLU   C 2  407 ? -36.496 -18.298 26.870   1.00 63.59  ? 417 GLU   D C     1 
ATOM   10076 O  O     . GLU   C 2  407 ? -35.535 -17.551 26.663   1.00 58.64  ? 417 GLU   D O     1 
ATOM   10077 C  CB    . GLU   C 2  407 ? -38.291 -17.226 28.256   1.00 54.31  ? 417 GLU   D CB    1 
ATOM   10078 C  CG    . GLU   C 2  407 ? -37.528 -15.997 28.678   1.00 59.16  ? 417 GLU   D CG    1 
ATOM   10079 C  CD    . GLU   C 2  407 ? -38.333 -15.114 29.595   1.00 60.67  ? 417 GLU   D CD    1 
ATOM   10080 O  OE1   . GLU   C 2  407 ? -39.571 -15.274 29.621   1.00 63.51  ? 417 GLU   D OE1   1 
ATOM   10081 O  OE2   . GLU   C 2  407 ? -37.733 -14.259 30.280   1.00 61.97  ? 417 GLU   D OE2   1 
ATOM   10082 N  N     . PHE   C 2  408 ? -36.339 -19.597 27.097   1.00 62.68  ? 418 PHE   D N     1 
ATOM   10083 C  CA    . PHE   C 2  408 ? -35.006 -20.162 26.962   1.00 62.78  ? 418 PHE   D CA    1 
ATOM   10084 C  C     . PHE   C 2  408 ? -34.663 -20.401 25.495   1.00 59.48  ? 418 PHE   D C     1 
ATOM   10085 O  O     . PHE   C 2  408 ? -33.576 -20.035 25.041   1.00 61.09  ? 418 PHE   D O     1 
ATOM   10086 C  CB    . PHE   C 2  408 ? -34.893 -21.443 27.784   1.00 64.55  ? 418 PHE   D CB    1 
ATOM   10087 C  CG    . PHE   C 2  408 ? -34.664 -21.204 29.258   1.00 62.11  ? 418 PHE   D CG    1 
ATOM   10088 C  CD1   . PHE   C 2  408 ? -35.599 -20.519 30.019   1.00 62.68  ? 418 PHE   D CD1   1 
ATOM   10089 C  CD2   . PHE   C 2  408 ? -33.530 -21.688 29.886   1.00 59.21  ? 418 PHE   D CD2   1 
ATOM   10090 C  CE1   . PHE   C 2  408 ? -35.391 -20.304 31.372   1.00 58.37  ? 418 PHE   D CE1   1 
ATOM   10091 C  CE2   . PHE   C 2  408 ? -33.327 -21.483 31.237   1.00 61.29  ? 418 PHE   D CE2   1 
ATOM   10092 C  CZ    . PHE   C 2  408 ? -34.257 -20.788 31.979   1.00 59.14  ? 418 PHE   D CZ    1 
ATOM   10093 N  N     . THR   C 2  409 ? -35.579 -20.993 24.729   1.00 61.29  ? 419 THR   D N     1 
ATOM   10094 C  CA    . THR   C 2  409 ? -35.333 -21.157 23.299   1.00 66.52  ? 419 THR   D CA    1 
ATOM   10095 C  C     . THR   C 2  409 ? -35.041 -19.811 22.635   1.00 67.30  ? 419 THR   D C     1 
ATOM   10096 O  O     . THR   C 2  409 ? -34.022 -19.651 21.949   1.00 60.90  ? 419 THR   D O     1 
ATOM   10097 C  CB    . THR   C 2  409 ? -36.528 -21.841 22.628   1.00 57.02  ? 419 THR   D CB    1 
ATOM   10098 O  OG1   . THR   C 2  409 ? -37.739 -21.273 23.130   1.00 65.81  ? 419 THR   D OG1   1 
ATOM   10099 C  CG2   . THR   C 2  409 ? -36.516 -23.333 22.883   1.00 59.14  ? 419 THR   D CG2   1 
ATOM   10100 N  N     . GLU   C 2  410 ? -35.923 -18.825 22.844   1.00 68.04  ? 420 GLU   D N     1 
ATOM   10101 C  CA    . GLU   C 2  410 ? -35.780 -17.520 22.202   1.00 62.08  ? 420 GLU   D CA    1 
ATOM   10102 C  C     . GLU   C 2  410 ? -34.428 -16.882 22.512   1.00 59.14  ? 420 GLU   D C     1 
ATOM   10103 O  O     . GLU   C 2  410 ? -33.737 -16.404 21.608   1.00 64.27  ? 420 GLU   D O     1 
ATOM   10104 C  CB    . GLU   C 2  410 ? -36.917 -16.597 22.635   1.00 67.28  ? 420 GLU   D CB    1 
ATOM   10105 C  CG    . GLU   C 2  410 ? -38.291 -16.995 22.117   1.00 62.27  ? 420 GLU   D CG    1 
ATOM   10106 C  CD    . GLU   C 2  410 ? -39.354 -15.997 22.531   1.00 73.76  ? 420 GLU   D CD    1 
ATOM   10107 O  OE1   . GLU   C 2  410 ? -38.991 -14.842 22.847   1.00 81.23  ? 420 GLU   D OE1   1 
ATOM   10108 O  OE2   . GLU   C 2  410 ? -40.548 -16.364 22.548   1.00 80.72  ? 420 GLU   D OE2   1 
ATOM   10109 N  N     . ALA   C 2  411 ? -34.041 -16.842 23.788   1.00 59.14  ? 421 ALA   D N     1 
ATOM   10110 C  CA    . ALA   C 2  411 ? -32.701 -16.371 24.126   1.00 57.64  ? 421 ALA   D CA    1 
ATOM   10111 C  C     . ALA   C 2  411 ? -31.647 -17.182 23.388   1.00 58.29  ? 421 ALA   D C     1 
ATOM   10112 O  O     . ALA   C 2  411 ? -30.644 -16.633 22.915   1.00 55.03  ? 421 ALA   D O     1 
ATOM   10113 C  CB    . ALA   C 2  411 ? -32.475 -16.441 25.640   1.00 52.32  ? 421 ALA   D CB    1 
ATOM   10114 N  N     . GLU   C 2  412 ? -31.865 -18.496 23.280   1.00 60.12  ? 422 GLU   D N     1 
ATOM   10115 C  CA    . GLU   C 2  412 ? -30.959 -19.365 22.538   1.00 59.76  ? 422 GLU   D CA    1 
ATOM   10116 C  C     . GLU   C 2  412 ? -30.883 -18.947 21.076   1.00 60.13  ? 422 GLU   D C     1 
ATOM   10117 O  O     . GLU   C 2  412 ? -29.793 -18.879 20.496   1.00 56.35  ? 422 GLU   D O     1 
ATOM   10118 C  CB    . GLU   C 2  412 ? -31.427 -20.822 22.669   1.00 60.75  ? 422 GLU   D CB    1 
ATOM   10119 C  CG    . GLU   C 2  412 ? -30.641 -21.870 21.877   1.00 57.09  ? 422 GLU   D CG    1 
ATOM   10120 C  CD    . GLU   C 2  412 ? -31.045 -23.308 22.221   1.00 68.61  ? 422 GLU   D CD    1 
ATOM   10121 O  OE1   . GLU   C 2  412 ? -31.970 -23.857 21.579   1.00 68.21  ? 422 GLU   D OE1   1 
ATOM   10122 O  OE2   . GLU   C 2  412 ? -30.435 -23.895 23.144   1.00 66.94  ? 422 GLU   D OE2   1 
ATOM   10123 N  N     . SER   C 2  413 ? -32.034 -18.649 20.468   1.00 57.72  ? 423 SER   D N     1 
ATOM   10124 C  CA    . SER   C 2  413 ? -32.069 -18.307 19.051   1.00 61.91  ? 423 SER   D CA    1 
ATOM   10125 C  C     . SER   C 2  413 ? -31.555 -16.894 18.805   1.00 59.97  ? 423 SER   D C     1 
ATOM   10126 O  O     . SER   C 2  413 ? -30.778 -16.662 17.874   1.00 58.25  ? 423 SER   D O     1 
ATOM   10127 C  CB    . SER   C 2  413 ? -33.487 -18.428 18.514   1.00 68.83  ? 423 SER   D CB    1 
ATOM   10128 O  OG    . SER   C 2  413 ? -34.188 -17.240 18.835   1.00 77.05  ? 423 SER   D OG    1 
ATOM   10129 N  N     . ASN   C 2  414 ? -32.006 -15.935 19.612   1.00 56.69  ? 424 ASN   D N     1 
ATOM   10130 C  CA    . ASN   C 2  414 ? -31.542 -14.567 19.448   1.00 56.67  ? 424 ASN   D CA    1 
ATOM   10131 C  C     . ASN   C 2  414 ? -30.047 -14.447 19.682   1.00 55.53  ? 424 ASN   D C     1 
ATOM   10132 O  O     . ASN   C 2  414 ? -29.433 -13.503 19.181   1.00 56.43  ? 424 ASN   D O     1 
ATOM   10133 C  CB    . ASN   C 2  414 ? -32.277 -13.619 20.398   1.00 59.53  ? 424 ASN   D CB    1 
ATOM   10134 C  CG    . ASN   C 2  414 ? -32.028 -12.152 20.070   1.00 57.63  ? 424 ASN   D CG    1 
ATOM   10135 O  OD1   . ASN   C 2  414 ? -31.931 -11.781 18.903   1.00 57.45  ? 424 ASN   D OD1   1 
ATOM   10136 N  ND2   . ASN   C 2  414 ? -31.932 -11.315 21.099   1.00 52.77  ? 424 ASN   D ND2   1 
ATOM   10137 N  N     . MET   C 2  415 ? -29.447 -15.365 20.440   1.00 51.32  ? 425 MET   D N     1 
ATOM   10138 C  CA    . MET   C 2  415 ? -28.008 -15.307 20.653   1.00 49.28  ? 425 MET   D CA    1 
ATOM   10139 C  C     . MET   C 2  415 ? -27.229 -15.998 19.549   1.00 52.57  ? 425 MET   D C     1 
ATOM   10140 O  O     . MET   C 2  415 ? -26.121 -15.558 19.230   1.00 49.27  ? 425 MET   D O     1 
ATOM   10141 C  CB    . MET   C 2  415 ? -27.622 -15.930 21.991   1.00 45.94  ? 425 MET   D CB    1 
ATOM   10142 C  CG    . MET   C 2  415 ? -26.249 -15.484 22.456   1.00 50.36  ? 425 MET   D CG    1 
ATOM   10143 S  SD    . MET   C 2  415 ? -25.629 -16.479 23.824   1.00 64.31  ? 425 MET   D SD    1 
ATOM   10144 C  CE    . MET   C 2  415 ? -24.752 -15.226 24.763   1.00 40.22  ? 425 MET   D CE    1 
ATOM   10145 N  N     . ASN   C 2  416 ? -27.775 -17.072 18.960   1.00 48.85  ? 426 ASN   D N     1 
ATOM   10146 C  CA    . ASN   C 2  416 ? -27.153 -17.644 17.771   1.00 48.28  ? 426 ASN   D CA    1 
ATOM   10147 C  C     . ASN   C 2  416 ? -27.377 -16.759 16.544   1.00 57.03  ? 426 ASN   D C     1 
ATOM   10148 O  O     . ASN   C 2  416 ? -26.549 -16.759 15.627   1.00 52.91  ? 426 ASN   D O     1 
ATOM   10149 C  CB    . ASN   C 2  416 ? -27.672 -19.061 17.539   1.00 54.67  ? 426 ASN   D CB    1 
ATOM   10150 C  CG    . ASN   C 2  416 ? -27.206 -20.036 18.618   1.00 64.19  ? 426 ASN   D CG    1 
ATOM   10151 O  OD1   . ASN   C 2  416 ? -26.106 -19.901 19.152   1.00 63.79  ? 426 ASN   D OD1   1 
ATOM   10152 N  ND2   . ASN   C 2  416 ? -28.047 -21.017 18.947   1.00 63.91  ? 426 ASN   D ND2   1 
ATOM   10153 N  N     . ASP   C 2  417 ? -28.481 -16.001 16.510   1.00 60.77  ? 427 ASP   D N     1 
ATOM   10154 C  CA    . ASP   C 2  417 ? -28.598 -14.875 15.586   1.00 46.72  ? 427 ASP   D CA    1 
ATOM   10155 C  C     . ASP   C 2  417 ? -27.400 -13.942 15.711   1.00 48.58  ? 427 ASP   D C     1 
ATOM   10156 O  O     . ASP   C 2  417 ? -26.747 -13.605 14.719   1.00 58.04  ? 427 ASP   D O     1 
ATOM   10157 C  CB    . ASP   C 2  417 ? -29.878 -14.081 15.858   1.00 56.63  ? 427 ASP   D CB    1 
ATOM   10158 C  CG    . ASP   C 2  417 ? -31.143 -14.846 15.524   1.00 55.76  ? 427 ASP   D CG    1 
ATOM   10159 O  OD1   . ASP   C 2  417 ? -31.073 -15.838 14.769   1.00 45.43  ? 427 ASP   D OD1   1 
ATOM   10160 O  OD2   . ASP   C 2  417 ? -32.215 -14.425 16.020   1.00 62.83  ? 427 ASP   D OD2   1 
ATOM   10161 N  N     . LEU   C 2  418 ? -27.105 -13.500 16.930   1.00 45.80  ? 428 LEU   D N     1 
ATOM   10162 C  CA    . LEU   C 2  418 ? -26.006 -12.561 17.114   1.00 48.80  ? 428 LEU   D CA    1 
ATOM   10163 C  C     . LEU   C 2  418 ? -24.689 -13.119 16.585   1.00 55.90  ? 428 LEU   D C     1 
ATOM   10164 O  O     . LEU   C 2  418 ? -23.811 -12.350 16.170   1.00 52.41  ? 428 LEU   D O     1 
ATOM   10165 C  CB    . LEU   C 2  418 ? -25.861 -12.186 18.586   1.00 38.23  ? 428 LEU   D CB    1 
ATOM   10166 C  CG    . LEU   C 2  418 ? -24.685 -11.228 18.725   1.00 47.74  ? 428 LEU   D CG    1 
ATOM   10167 C  CD1   . LEU   C 2  418 ? -25.027 -9.925  18.006   1.00 44.75  ? 428 LEU   D CD1   1 
ATOM   10168 C  CD2   . LEU   C 2  418 ? -24.255 -10.982 20.174   1.00 41.05  ? 428 LEU   D CD2   1 
ATOM   10169 N  N     . VAL   C 2  419 ? -24.525 -14.442 16.586   1.00 54.25  ? 429 VAL   D N     1 
ATOM   10170 C  CA    . VAL   C 2  419 ? -23.282 -15.015 16.084   1.00 52.81  ? 429 VAL   D CA    1 
ATOM   10171 C  C     . VAL   C 2  419 ? -23.314 -15.119 14.567   1.00 46.32  ? 429 VAL   D C     1 
ATOM   10172 O  O     . VAL   C 2  419 ? -22.299 -14.912 13.901   1.00 50.83  ? 429 VAL   D O     1 
ATOM   10173 C  CB    . VAL   C 2  419 ? -23.004 -16.374 16.749   1.00 49.07  ? 429 VAL   D CB    1 
ATOM   10174 C  CG1   . VAL   C 2  419 ? -22.162 -17.264 15.825   1.00 35.39  ? 429 VAL   D CG1   1 
ATOM   10175 C  CG2   . VAL   C 2  419 ? -22.285 -16.157 18.084   1.00 50.13  ? 429 VAL   D CG2   1 
ATOM   10176 N  N     . SER   C 2  420 ? -24.471 -15.433 13.993   1.00 47.81  ? 430 SER   D N     1 
ATOM   10177 C  CA    . SER   C 2  420 ? -24.576 -15.462 12.538   1.00 56.01  ? 430 SER   D CA    1 
ATOM   10178 C  C     . SER   C 2  420 ? -24.355 -14.083 11.920   1.00 59.11  ? 430 SER   D C     1 
ATOM   10179 O  O     . SER   C 2  420 ? -23.828 -13.983 10.806   1.00 56.29  ? 430 SER   D O     1 
ATOM   10180 C  CB    . SER   C 2  420 ? -25.935 -16.010 12.134   1.00 48.54  ? 430 SER   D CB    1 
ATOM   10181 O  OG    . SER   C 2  420 ? -26.210 -17.159 12.902   1.00 65.39  ? 430 SER   D OG    1 
ATOM   10182 N  N     . GLU   C 2  421 ? -24.763 -13.015 12.612   1.00 55.60  ? 431 GLU   D N     1 
ATOM   10183 C  CA    . GLU   C 2  421 ? -24.522 -11.667 12.102   1.00 55.35  ? 431 GLU   D CA    1 
ATOM   10184 C  C     . GLU   C 2  421 ? -23.044 -11.315 12.172   1.00 42.70  ? 431 GLU   D C     1 
ATOM   10185 O  O     . GLU   C 2  421 ? -22.488 -10.771 11.217   1.00 56.20  ? 431 GLU   D O     1 
ATOM   10186 C  CB    . GLU   C 2  421 ? -25.364 -10.640 12.873   1.00 48.92  ? 431 GLU   D CB    1 
ATOM   10187 C  CG    . GLU   C 2  421 ? -26.860 -10.770 12.599   1.00 44.64  ? 431 GLU   D CG    1 
ATOM   10188 C  CD    . GLU   C 2  421 ? -27.746 -10.471 13.805   1.00 49.76  ? 431 GLU   D CD    1 
ATOM   10189 O  OE1   . GLU   C 2  421 ? -27.398 -9.606  14.652   1.00 48.45  ? 431 GLU   D OE1   1 
ATOM   10190 O  OE2   . GLU   C 2  421 ? -28.815 -11.113 13.894   1.00 58.99  ? 431 GLU   D OE2   1 
ATOM   10191 N  N     . TYR   C 2  422 ? -22.389 -11.620 13.287   1.00 43.41  ? 432 TYR   D N     1 
ATOM   10192 C  CA    . TYR   C 2  422 ? -20.955 -11.373 13.377   1.00 40.17  ? 432 TYR   D CA    1 
ATOM   10193 C  C     . TYR   C 2  422 ? -20.205 -12.113 12.283   1.00 49.52  ? 432 TYR   D C     1 
ATOM   10194 O  O     . TYR   C 2  422 ? -19.158 -11.641 11.815   1.00 49.43  ? 432 TYR   D O     1 
ATOM   10195 C  CB    . TYR   C 2  422 ? -20.436 -11.786 14.748   1.00 45.15  ? 432 TYR   D CB    1 
ATOM   10196 C  CG    . TYR   C 2  422 ? -20.509 -10.685 15.763   1.00 44.24  ? 432 TYR   D CG    1 
ATOM   10197 C  CD1   . TYR   C 2  422 ? -19.780 -9.535  15.581   1.00 42.20  ? 432 TYR   D CD1   1 
ATOM   10198 C  CD2   . TYR   C 2  422 ? -21.287 -10.806 16.919   1.00 47.29  ? 432 TYR   D CD2   1 
ATOM   10199 C  CE1   . TYR   C 2  422 ? -19.818 -8.519  16.493   1.00 49.96  ? 432 TYR   D CE1   1 
ATOM   10200 C  CE2   . TYR   C 2  422 ? -21.333 -9.782  17.858   1.00 43.78  ? 432 TYR   D CE2   1 
ATOM   10201 C  CZ    . TYR   C 2  422 ? -20.591 -8.631  17.629   1.00 48.36  ? 432 TYR   D CZ    1 
ATOM   10202 O  OH    . TYR   C 2  422 ? -20.581 -7.568  18.513   1.00 46.92  ? 432 TYR   D OH    1 
ATOM   10203 N  N     . GLN   C 2  423 ? -20.733 -13.265 11.858   1.00 46.04  ? 433 GLN   D N     1 
ATOM   10204 C  CA    . GLN   C 2  423 ? -20.109 -14.020 10.782   1.00 48.23  ? 433 GLN   D CA    1 
ATOM   10205 C  C     . GLN   C 2  423 ? -20.361 -13.343 9.443    1.00 47.62  ? 433 GLN   D C     1 
ATOM   10206 O  O     . GLN   C 2  423 ? -19.415 -13.078 8.692    1.00 49.75  ? 433 GLN   D O     1 
ATOM   10207 C  CB    . GLN   C 2  423 ? -20.630 -15.463 10.782   1.00 47.75  ? 433 GLN   D CB    1 
ATOM   10208 C  CG    . GLN   C 2  423 ? -19.957 -16.406 9.779    1.00 36.40  ? 433 GLN   D CG    1 
ATOM   10209 C  CD    . GLN   C 2  423 ? -18.528 -16.767 10.165   1.00 39.13  ? 433 GLN   D CD    1 
ATOM   10210 O  OE1   . GLN   C 2  423 ? -18.232 -16.995 11.331   1.00 44.73  ? 433 GLN   D OE1   1 
ATOM   10211 N  NE2   . GLN   C 2  423 ? -17.635 -16.811 9.180    1.00 40.99  ? 433 GLN   D NE2   1 
ATOM   10212 N  N     . GLN   C 2  424 ? -21.633 -13.041 9.141    1.00 42.63  ? 434 GLN   D N     1 
ATOM   10213 C  CA    . GLN   C 2  424 ? -22.019 -12.372 7.900    1.00 39.75  ? 434 GLN   D CA    1 
ATOM   10214 C  C     . GLN   C 2  424 ? -21.085 -11.222 7.559    1.00 52.23  ? 434 GLN   D C     1 
ATOM   10215 O  O     . GLN   C 2  424 ? -20.601 -11.107 6.425    1.00 48.47  ? 434 GLN   D O     1 
ATOM   10216 C  CB    . GLN   C 2  424 ? -23.448 -11.833 8.011    1.00 53.42  ? 434 GLN   D CB    1 
ATOM   10217 C  CG    . GLN   C 2  424 ? -24.566 -12.786 7.610    1.00 67.23  ? 434 GLN   D CG    1 
ATOM   10218 C  CD    . GLN   C 2  424 ? -25.945 -12.233 7.974    1.00 75.21  ? 434 GLN   D CD    1 
ATOM   10219 O  OE1   . GLN   C 2  424 ? -26.128 -11.014 8.078    1.00 64.92  ? 434 GLN   D OE1   1 
ATOM   10220 N  NE2   . GLN   C 2  424 ? -26.917 -13.129 8.180    1.00 67.71  ? 434 GLN   D NE2   1 
ATOM   10221 N  N     . TYR   C 2  425 ? -20.829 -10.348 8.536    1.00 48.32  ? 435 TYR   D N     1 
ATOM   10222 C  CA    . TYR   C 2  425 ? -20.021 -9.168  8.261    1.00 49.49  ? 435 TYR   D CA    1 
ATOM   10223 C  C     . TYR   C 2  425 ? -18.544 -9.513  8.140    1.00 48.76  ? 435 TYR   D C     1 
ATOM   10224 O  O     . TYR   C 2  425 ? -17.819 -8.879  7.362    1.00 57.95  ? 435 TYR   D O     1 
ATOM   10225 C  CB    . TYR   C 2  425 ? -20.293 -8.100  9.328    1.00 45.06  ? 435 TYR   D CB    1 
ATOM   10226 C  CG    . TYR   C 2  425 ? -21.671 -7.515  9.134    1.00 39.56  ? 435 TYR   D CG    1 
ATOM   10227 C  CD1   . TYR   C 2  425 ? -21.974 -6.828  7.984    1.00 40.70  ? 435 TYR   D CD1   1 
ATOM   10228 C  CD2   . TYR   C 2  425 ? -22.673 -7.689  10.065   1.00 43.16  ? 435 TYR   D CD2   1 
ATOM   10229 C  CE1   . TYR   C 2  425 ? -23.213 -6.310  7.769    1.00 41.97  ? 435 TYR   D CE1   1 
ATOM   10230 C  CE2   . TYR   C 2  425 ? -23.923 -7.168  9.857    1.00 41.31  ? 435 TYR   D CE2   1 
ATOM   10231 C  CZ    . TYR   C 2  425 ? -24.188 -6.477  8.702    1.00 40.75  ? 435 TYR   D CZ    1 
ATOM   10232 O  OH    . TYR   C 2  425 ? -25.434 -5.940  8.449    1.00 44.37  ? 435 TYR   D OH    1 
ATOM   10233 N  N     . GLN   C 2  426 ? -18.090 -10.536 8.854    1.00 42.70  ? 436 GLN   D N     1 
ATOM   10234 C  CA    . GLN   C 2  426 ? -16.746 -11.040 8.614    1.00 46.14  ? 436 GLN   D CA    1 
ATOM   10235 C  C     . GLN   C 2  426 ? -16.618 -11.615 7.198    1.00 45.88  ? 436 GLN   D C     1 
ATOM   10236 O  O     . GLN   C 2  426 ? -15.601 -11.420 6.526    1.00 49.11  ? 436 GLN   D O     1 
ATOM   10237 C  CB    . GLN   C 2  426 ? -16.417 -12.058 9.698    1.00 35.74  ? 436 GLN   D CB    1 
ATOM   10238 C  CG    . GLN   C 2  426 ? -15.317 -13.008 9.421    1.00 42.23  ? 436 GLN   D CG    1 
ATOM   10239 C  CD    . GLN   C 2  426 ? -15.144 -13.962 10.585   1.00 49.77  ? 436 GLN   D CD    1 
ATOM   10240 O  OE1   . GLN   C 2  426 ? -14.779 -13.554 11.679   1.00 50.76  ? 436 GLN   D OE1   1 
ATOM   10241 N  NE2   . GLN   C 2  426 ? -15.449 -15.230 10.363   1.00 49.60  ? 436 GLN   D NE2   1 
ATOM   10242 N  N     . ASP   C 2  427 ? -17.666 -12.267 6.699    1.00 42.99  ? 437 ASP   D N     1 
ATOM   10243 C  CA    . ASP   C 2  427 ? -17.632 -12.850 5.360    1.00 49.70  ? 437 ASP   D CA    1 
ATOM   10244 C  C     . ASP   C 2  427 ? -17.836 -11.828 4.238    1.00 50.44  ? 437 ASP   D C     1 
ATOM   10245 O  O     . ASP   C 2  427 ? -17.502 -12.116 3.084    1.00 46.75  ? 437 ASP   D O     1 
ATOM   10246 C  CB    . ASP   C 2  427 ? -18.700 -13.947 5.242    1.00 44.59  ? 437 ASP   D CB    1 
ATOM   10247 C  CG    . ASP   C 2  427 ? -18.286 -15.245 5.910    1.00 47.63  ? 437 ASP   D CG    1 
ATOM   10248 O  OD1   . ASP   C 2  427 ? -17.085 -15.402 6.255    1.00 43.97  ? 437 ASP   D OD1   1 
ATOM   10249 O  OD2   . ASP   C 2  427 ? -19.177 -16.107 6.089    1.00 50.94  ? 437 ASP   D OD2   1 
ATOM   10250 N  N     . ALA   C 2  428 ? -18.400 -10.664 4.526    1.00 43.35  ? 438 ALA   D N     1 
ATOM   10251 C  CA    . ALA   C 2  428 ? -18.620 -9.701  3.470    1.00 40.59  ? 438 ALA   D CA    1 
ATOM   10252 C  C     . ALA   C 2  428 ? -17.290 -9.198  2.906    1.00 46.69  ? 438 ALA   D C     1 
ATOM   10253 O  O     . ALA   C 2  428 ? -16.240 -9.271  3.548    1.00 46.61  ? 438 ALA   D O     1 
ATOM   10254 C  CB    . ALA   C 2  428 ? -19.451 -8.530  3.988    1.00 42.27  ? 438 ALA   D CB    1 
ATOM   10255 N  N     . THR   C 2  429 ? -17.351 -8.681  1.680    1.00 43.54  ? 439 THR   D N     1 
ATOM   10256 C  CA    . THR   C 2  429 ? -16.246 -7.957  1.074    1.00 52.22  ? 439 THR   D CA    1 
ATOM   10257 C  C     . THR   C 2  429 ? -16.792 -6.721  0.386    1.00 53.96  ? 439 THR   D C     1 
ATOM   10258 O  O     . THR   C 2  429 ? -17.995 -6.605  0.138    1.00 51.45  ? 439 THR   D O     1 
ATOM   10259 C  CB    . THR   C 2  429 ? -15.485 -8.785  0.039    1.00 55.42  ? 439 THR   D CB    1 
ATOM   10260 O  OG1   . THR   C 2  429 ? -16.429 -9.403  -0.848   1.00 55.90  ? 439 THR   D OG1   1 
ATOM   10261 C  CG2   . THR   C 2  429 ? -14.624 -9.827  0.718    1.00 48.49  ? 439 THR   D CG2   1 
ATOM   10262 N  N     . ALA   C 2  430 ? -15.884 -5.799  0.067    1.00 56.98  ? 440 ALA   D N     1 
ATOM   10263 C  CA    . ALA   C 2  430 ? -16.273 -4.633  -0.717   1.00 58.96  ? 440 ALA   D CA    1 
ATOM   10264 C  C     . ALA   C 2  430 ? -16.729 -5.045  -2.112   1.00 58.78  ? 440 ALA   D C     1 
ATOM   10265 O  O     . ALA   C 2  430 ? -17.765 -4.583  -2.602   1.00 66.80  ? 440 ALA   D O     1 
ATOM   10266 C  CB    . ALA   C 2  430 ? -15.113 -3.650  -0.790   1.00 50.51  ? 440 ALA   D CB    1 
ATOM   10267 N  N     . ASP   C 2  431 ? -15.975 -5.927  -2.758   1.00 57.15  ? 441 ASP   D N     1 
ATOM   10268 C  CA    . ASP   C 2  431 ? -16.313 -6.405  -4.098   1.00 73.46  ? 441 ASP   D CA    1 
ATOM   10269 C  C     . ASP   C 2  431 ? -16.580 -7.911  -4.078   1.00 73.80  ? 441 ASP   D C     1 
ATOM   10270 O  O     . ASP   C 2  431 ? -15.660 -8.720  -4.278   1.00 65.02  ? 441 ASP   D O     1 
ATOM   10271 C  CB    . ASP   C 2  431 ? -15.182 -6.097  -5.095   1.00 81.24  ? 441 ASP   D CB    1 
ATOM   10272 C  CG    . ASP   C 2  431 ? -14.679 -4.657  -5.004   1.00 86.33  ? 441 ASP   D CG    1 
ATOM   10273 O  OD1   . ASP   C 2  431 ? -15.497 -3.727  -5.206   1.00 84.84  ? 441 ASP   D OD1   1 
ATOM   10274 O  OD2   . ASP   C 2  431 ? -13.465 -4.461  -4.731   1.00 78.17  ? 441 ASP   D OD2   1 
ATOM   10275 N  N     . MET   D 3  4   ? -20.653 88.463  -91.820  1.00 76.73  ? 6   MET   E N     1 
ATOM   10276 C  CA    . MET   D 3  4   ? -20.248 89.407  -92.857  1.00 74.71  ? 6   MET   E CA    1 
ATOM   10277 C  C     . MET   D 3  4   ? -21.148 90.647  -92.831  1.00 74.19  ? 6   MET   E C     1 
ATOM   10278 O  O     . MET   D 3  4   ? -20.657 91.768  -92.963  1.00 77.37  ? 6   MET   E O     1 
ATOM   10279 C  CB    . MET   D 3  4   ? -20.287 88.739  -94.240  1.00 66.83  ? 6   MET   E CB    1 
ATOM   10280 C  CG    . MET   D 3  4   ? -19.435 89.410  -95.316  1.00 61.61  ? 6   MET   E CG    1 
ATOM   10281 S  SD    . MET   D 3  4   ? -19.367 88.376  -96.809  1.00 86.50  ? 6   MET   E SD    1 
ATOM   10282 C  CE    . MET   D 3  4   ? -19.427 86.737  -96.075  1.00 73.66  ? 6   MET   E CE    1 
ATOM   10283 N  N     . GLU   D 3  5   ? -22.456 90.453  -92.633  1.00 61.94  ? 7   GLU   E N     1 
ATOM   10284 C  CA    . GLU   D 3  5   ? -23.428 91.539  -92.723  1.00 64.26  ? 7   GLU   E CA    1 
ATOM   10285 C  C     . GLU   D 3  5   ? -23.790 92.064  -91.337  1.00 61.66  ? 7   GLU   E C     1 
ATOM   10286 O  O     . GLU   D 3  5   ? -24.273 91.301  -90.497  1.00 60.82  ? 7   GLU   E O     1 
ATOM   10287 C  CB    . GLU   D 3  5   ? -24.692 91.078  -93.441  1.00 64.50  ? 7   GLU   E CB    1 
ATOM   10288 C  CG    . GLU   D 3  5   ? -25.640 92.228  -93.706  1.00 73.14  ? 7   GLU   E CG    1 
ATOM   10289 C  CD    . GLU   D 3  5   ? -26.940 91.785  -94.312  1.00 75.89  ? 7   GLU   E CD    1 
ATOM   10290 O  OE1   . GLU   D 3  5   ? -27.055 90.585  -94.638  1.00 81.12  ? 7   GLU   E OE1   1 
ATOM   10291 O  OE2   . GLU   D 3  5   ? -27.843 92.638  -94.456  1.00 76.52  ? 7   GLU   E OE2   1 
ATOM   10292 N  N     . VAL   D 3  6   ? -23.613 93.372  -91.126  1.00 63.65  ? 8   VAL   E N     1 
ATOM   10293 C  CA    . VAL   D 3  6   ? -23.883 94.018  -89.838  1.00 55.74  ? 8   VAL   E CA    1 
ATOM   10294 C  C     . VAL   D 3  6   ? -25.300 94.586  -89.829  1.00 54.69  ? 8   VAL   E C     1 
ATOM   10295 O  O     . VAL   D 3  6   ? -25.605 95.528  -90.565  1.00 59.51  ? 8   VAL   E O     1 
ATOM   10296 C  CB    . VAL   D 3  6   ? -22.861 95.124  -89.542  1.00 50.64  ? 8   VAL   E CB    1 
ATOM   10297 C  CG1   . VAL   D 3  6   ? -23.440 96.096  -88.549  1.00 52.95  ? 8   VAL   E CG1   1 
ATOM   10298 C  CG2   . VAL   D 3  6   ? -21.575 94.536  -89.012  1.00 52.30  ? 8   VAL   E CG2   1 
ATOM   10299 N  N     . ILE   D 3  7   ? -26.143 94.052  -88.944  1.00 64.46  ? 9   ILE   E N     1 
ATOM   10300 C  CA    . ILE   D 3  7   ? -27.573 94.346  -88.891  1.00 59.94  ? 9   ILE   E CA    1 
ATOM   10301 C  C     . ILE   D 3  7   ? -27.901 95.181  -87.653  1.00 61.71  ? 9   ILE   E C     1 
ATOM   10302 O  O     . ILE   D 3  7   ? -27.117 95.295  -86.701  1.00 52.27  ? 9   ILE   E O     1 
ATOM   10303 C  CB    . ILE   D 3  7   ? -28.413 93.050  -88.894  1.00 62.06  ? 9   ILE   E CB    1 
ATOM   10304 C  CG1   . ILE   D 3  7   ? -27.869 92.082  -89.939  1.00 58.08  ? 9   ILE   E CG1   1 
ATOM   10305 C  CG2   . ILE   D 3  7   ? -29.883 93.347  -89.131  1.00 62.42  ? 9   ILE   E CG2   1 
ATOM   10306 C  CD1   . ILE   D 3  7   ? -27.550 92.735  -91.236  1.00 65.16  ? 9   ILE   E CD1   1 
ATOM   10307 N  N     . GLU   D 3  8   ? -29.091 95.781  -87.691  1.00 60.66  ? 10  GLU   E N     1 
ATOM   10308 C  CA    . GLU   D 3  8   ? -29.714 96.500  -86.583  1.00 57.48  ? 10  GLU   E CA    1 
ATOM   10309 C  C     . GLU   D 3  8   ? -28.764 97.254  -85.650  1.00 49.47  ? 10  GLU   E C     1 
ATOM   10310 O  O     . GLU   D 3  8   ? -28.918 97.180  -84.428  1.00 54.27  ? 10  GLU   E O     1 
ATOM   10311 C  CB    . GLU   D 3  8   ? -30.559 95.513  -85.771  1.00 55.97  ? 10  GLU   E CB    1 
ATOM   10312 C  CG    . GLU   D 3  8   ? -31.539 94.700  -86.609  1.00 59.13  ? 10  GLU   E CG    1 
ATOM   10313 C  CD    . GLU   D 3  8   ? -32.466 93.837  -85.762  1.00 79.13  ? 10  GLU   E CD    1 
ATOM   10314 O  OE1   . GLU   D 3  8   ? -32.265 93.775  -84.529  1.00 79.52  ? 10  GLU   E OE1   1 
ATOM   10315 O  OE2   . GLU   D 3  8   ? -33.395 93.219  -86.330  1.00 80.80  ? 10  GLU   E OE2   1 
ATOM   10316 N  N     . LEU   D 3  9   ? -27.814 98.016  -86.183  1.00 49.69  ? 11  LEU   E N     1 
ATOM   10317 C  CA    . LEU   D 3  9   ? -27.007 98.866  -85.312  1.00 51.45  ? 11  LEU   E CA    1 
ATOM   10318 C  C     . LEU   D 3  9   ? -27.901 99.831  -84.519  1.00 55.75  ? 11  LEU   E C     1 
ATOM   10319 O  O     . LEU   D 3  9   ? -28.882 100.379 -85.043  1.00 45.34  ? 11  LEU   E O     1 
ATOM   10320 C  CB    . LEU   D 3  9   ? -25.971 99.638  -86.132  1.00 47.15  ? 11  LEU   E CB    1 
ATOM   10321 C  CG    . LEU   D 3  9   ? -24.897 100.406 -85.345  1.00 55.21  ? 11  LEU   E CG    1 
ATOM   10322 C  CD1   . LEU   D 3  9   ? -24.049 99.496  -84.454  1.00 39.01  ? 11  LEU   E CD1   1 
ATOM   10323 C  CD2   . LEU   D 3  9   ? -24.004 101.226 -86.282  1.00 37.05  ? 11  LEU   E CD2   1 
ATOM   10324 N  N     . ASN   D 3  10  ? -27.555 100.018 -83.239  1.00 50.74  ? 12  ASN   E N     1 
ATOM   10325 C  CA    . ASN   D 3  10  ? -28.306 100.824 -82.272  1.00 43.24  ? 12  ASN   E CA    1 
ATOM   10326 C  C     . ASN   D 3  10  ? -27.302 101.507 -81.354  1.00 46.63  ? 12  ASN   E C     1 
ATOM   10327 O  O     . ASN   D 3  10  ? -26.550 100.820 -80.655  1.00 45.74  ? 12  ASN   E O     1 
ATOM   10328 C  CB    . ASN   D 3  10  ? -29.273 99.960  -81.444  1.00 40.01  ? 12  ASN   E CB    1 
ATOM   10329 C  CG    . ASN   D 3  10  ? -30.659 99.801  -82.101  1.00 56.71  ? 12  ASN   E CG    1 
ATOM   10330 O  OD1   . ASN   D 3  10  ? -31.415 100.772 -82.230  1.00 66.32  ? 12  ASN   E OD1   1 
ATOM   10331 N  ND2   . ASN   D 3  10  ? -31.000 98.573  -82.497  1.00 47.79  ? 12  ASN   E ND2   1 
ATOM   10332 N  N     . LYS   D 3  11  ? -27.280 102.844 -81.351  1.00 48.48  ? 13  LYS   E N     1 
ATOM   10333 C  CA    . LYS   D 3  11  ? -26.288 103.622 -80.610  1.00 51.72  ? 13  LYS   E CA    1 
ATOM   10334 C  C     . LYS   D 3  11  ? -26.906 104.363 -79.421  1.00 60.88  ? 13  LYS   E C     1 
ATOM   10335 O  O     . LYS   D 3  11  ? -28.017 104.901 -79.512  1.00 65.64  ? 13  LYS   E O     1 
ATOM   10336 C  CB    . LYS   D 3  11  ? -25.592 104.638 -81.525  1.00 55.76  ? 13  LYS   E CB    1 
ATOM   10337 C  CG    . LYS   D 3  11  ? -24.425 104.120 -82.365  1.00 45.32  ? 13  LYS   E CG    1 
ATOM   10338 C  CD    . LYS   D 3  11  ? -24.430 104.819 -83.723  1.00 51.83  ? 13  LYS   E CD    1 
ATOM   10339 C  CE    . LYS   D 3  11  ? -23.035 105.039 -84.277  1.00 53.93  ? 13  LYS   E CE    1 
ATOM   10340 N  NZ    . LYS   D 3  11  ? -22.328 106.133 -83.572  1.00 51.68  ? 13  LYS   E NZ    1 
ATOM   10341 N  N     . CYS   D 3  12  ? -26.169 104.387 -78.310  1.00 58.77  ? 14  CYS   E N     1 
ATOM   10342 C  CA    . CYS   D 3  12  ? -26.450 105.138 -77.084  1.00 57.04  ? 14  CYS   E CA    1 
ATOM   10343 C  C     . CYS   D 3  12  ? -25.241 106.006 -76.762  1.00 59.04  ? 14  CYS   E C     1 
ATOM   10344 O  O     . CYS   D 3  12  ? -24.222 105.967 -77.453  1.00 63.96  ? 14  CYS   E O     1 
ATOM   10345 C  CB    . CYS   D 3  12  ? -26.725 104.211 -75.886  1.00 48.75  ? 14  CYS   E CB    1 
ATOM   10346 S  SG    . CYS   D 3  12  ? -28.431 103.671 -75.669  1.00 86.46  ? 14  CYS   E SG    1 
ATOM   10347 N  N     . THR   D 3  13  ? -25.351 106.769 -75.681  1.00 59.68  ? 15  THR   E N     1 
ATOM   10348 C  CA    . THR   D 3  13  ? -24.174 107.357 -75.059  1.00 55.62  ? 15  THR   E CA    1 
ATOM   10349 C  C     . THR   D 3  13  ? -23.451 106.370 -74.146  1.00 67.70  ? 15  THR   E C     1 
ATOM   10350 O  O     . THR   D 3  13  ? -22.411 106.723 -73.577  1.00 68.41  ? 15  THR   E O     1 
ATOM   10351 C  CB    . THR   D 3  13  ? -24.569 108.607 -74.266  1.00 61.32  ? 15  THR   E CB    1 
ATOM   10352 O  OG1   . THR   D 3  13  ? -25.478 109.395 -75.045  1.00 68.14  ? 15  THR   E OG1   1 
ATOM   10353 C  CG2   . THR   D 3  13  ? -23.335 109.450 -73.925  1.00 55.25  ? 15  THR   E CG2   1 
ATOM   10354 N  N     . SER   D 3  14  ? -23.980 105.151 -73.989  1.00 63.64  ? 16  SER   E N     1 
ATOM   10355 C  CA    . SER   D 3  14  ? -23.379 104.124 -73.148  1.00 55.03  ? 16  SER   E CA    1 
ATOM   10356 C  C     . SER   D 3  14  ? -22.720 102.994 -73.931  1.00 59.09  ? 16  SER   E C     1 
ATOM   10357 O  O     . SER   D 3  14  ? -21.776 102.383 -73.424  1.00 54.13  ? 16  SER   E O     1 
ATOM   10358 C  CB    . SER   D 3  14  ? -24.430 103.526 -72.200  1.00 49.55  ? 16  SER   E CB    1 
ATOM   10359 O  OG    . SER   D 3  14  ? -25.630 104.275 -72.229  1.00 61.44  ? 16  SER   E OG    1 
ATOM   10360 N  N     . GLY   D 3  15  ? -23.183 102.701 -75.149  1.00 61.26  ? 17  GLY   E N     1 
ATOM   10361 C  CA    . GLY   D 3  15  ? -22.516 101.728 -76.002  1.00 53.81  ? 17  GLY   E CA    1 
ATOM   10362 C  C     . GLY   D 3  15  ? -23.139 101.631 -77.381  1.00 56.64  ? 17  GLY   E C     1 
ATOM   10363 O  O     . GLY   D 3  15  ? -23.678 102.619 -77.884  1.00 60.16  ? 17  GLY   E O     1 
ATOM   10364 N  N     . GLN   D 3  16  ? -23.063 100.455 -78.009  1.00 60.64  ? 18  GLN   E N     1 
ATOM   10365 C  CA    . GLN   D 3  16  ? -23.820 100.158 -79.223  1.00 53.83  ? 18  GLN   E CA    1 
ATOM   10366 C  C     . GLN   D 3  16  ? -24.234 98.699  -79.193  1.00 42.92  ? 18  GLN   E C     1 
ATOM   10367 O  O     . GLN   D 3  16  ? -23.705 97.905  -78.412  1.00 39.75  ? 18  GLN   E O     1 
ATOM   10368 C  CB    . GLN   D 3  16  ? -23.018 100.433 -80.495  1.00 46.96  ? 18  GLN   E CB    1 
ATOM   10369 C  CG    . GLN   D 3  16  ? -22.125 101.637 -80.390  1.00 52.37  ? 18  GLN   E CG    1 
ATOM   10370 C  CD    . GLN   D 3  16  ? -21.301 101.838 -81.632  1.00 47.39  ? 18  GLN   E CD    1 
ATOM   10371 O  OE1   . GLN   D 3  16  ? -21.650 101.345 -82.705  1.00 46.47  ? 18  GLN   E OE1   1 
ATOM   10372 N  NE2   . GLN   D 3  16  ? -20.195 102.564 -81.495  1.00 42.23  ? 18  GLN   E NE2   1 
ATOM   10373 N  N     . SER   D 3  17  ? -25.193 98.356  -80.054  1.00 41.28  ? 19  SER   E N     1 
ATOM   10374 C  CA    . SER   D 3  17  ? -25.687 96.990  -80.189  1.00 44.68  ? 19  SER   E CA    1 
ATOM   10375 C  C     . SER   D 3  17  ? -25.898 96.678  -81.666  1.00 43.62  ? 19  SER   E C     1 
ATOM   10376 O  O     . SER   D 3  17  ? -26.258 97.546  -82.461  1.00 46.83  ? 19  SER   E O     1 
ATOM   10377 C  CB    . SER   D 3  17  ? -27.006 96.757  -79.411  1.00 40.86  ? 19  SER   E CB    1 
ATOM   10378 O  OG    . SER   D 3  17  ? -28.115 96.494  -80.291  1.00 42.67  ? 19  SER   E OG    1 
ATOM   10379 N  N     . PHE   D 3  18  ? -25.692 95.423  -82.027  1.00 40.53  ? 20  PHE   E N     1 
ATOM   10380 C  CA    . PHE   D 3  18  ? -25.830 95.065  -83.426  1.00 40.95  ? 20  PHE   E CA    1 
ATOM   10381 C  C     . PHE   D 3  18  ? -25.703 93.555  -83.550  1.00 38.47  ? 20  PHE   E C     1 
ATOM   10382 O  O     . PHE   D 3  18  ? -25.101 92.894  -82.703  1.00 44.76  ? 20  PHE   E O     1 
ATOM   10383 C  CB    . PHE   D 3  18  ? -24.779 95.792  -84.305  1.00 42.87  ? 20  PHE   E CB    1 
ATOM   10384 C  CG    . PHE   D 3  18  ? -23.346 95.372  -84.038  1.00 39.94  ? 20  PHE   E CG    1 
ATOM   10385 C  CD1   . PHE   D 3  18  ? -22.579 96.019  -83.059  1.00 38.24  ? 20  PHE   E CD1   1 
ATOM   10386 C  CD2   . PHE   D 3  18  ? -22.764 94.337  -84.757  1.00 34.20  ? 20  PHE   E CD2   1 
ATOM   10387 C  CE1   . PHE   D 3  18  ? -21.256 95.646  -82.815  1.00 28.04  ? 20  PHE   E CE1   1 
ATOM   10388 C  CE2   . PHE   D 3  18  ? -21.446 93.955  -84.511  1.00 33.26  ? 20  PHE   E CE2   1 
ATOM   10389 C  CZ    . PHE   D 3  18  ? -20.698 94.610  -83.536  1.00 36.87  ? 20  PHE   E CZ    1 
ATOM   10390 N  N     . GLU   D 3  19  ? -26.305 93.021  -84.593  1.00 45.31  ? 21  GLU   E N     1 
ATOM   10391 C  CA    . GLU   D 3  19  ? -26.159 91.626  -84.958  1.00 37.90  ? 21  GLU   E CA    1 
ATOM   10392 C  C     . GLU   D 3  19  ? -25.220 91.553  -86.154  1.00 46.27  ? 21  GLU   E C     1 
ATOM   10393 O  O     . GLU   D 3  19  ? -25.107 92.499  -86.938  1.00 46.45  ? 21  GLU   E O     1 
ATOM   10394 C  CB    . GLU   D 3  19  ? -27.526 91.038  -85.295  1.00 41.73  ? 21  GLU   E CB    1 
ATOM   10395 C  CG    . GLU   D 3  19  ? -27.678 89.539  -85.214  1.00 38.61  ? 21  GLU   E CG    1 
ATOM   10396 C  CD    . GLU   D 3  19  ? -29.151 89.158  -85.123  1.00 50.21  ? 21  GLU   E CD    1 
ATOM   10397 O  OE1   . GLU   D 3  19  ? -29.932 89.991  -84.593  1.00 52.71  ? 21  GLU   E OE1   1 
ATOM   10398 O  OE2   . GLU   D 3  19  ? -29.534 88.055  -85.583  1.00 52.91  ? 21  GLU   E OE2   1 
ATOM   10399 N  N     . VAL   D 3  20  ? -24.520 90.436  -86.280  1.00 43.82  ? 22  VAL   E N     1 
ATOM   10400 C  CA    . VAL   D 3  20  ? -23.621 90.229  -87.403  1.00 41.12  ? 22  VAL   E CA    1 
ATOM   10401 C  C     . VAL   D 3  20  ? -23.739 88.773  -87.801  1.00 47.82  ? 22  VAL   E C     1 
ATOM   10402 O  O     . VAL   D 3  20  ? -23.416 87.889  -87.002  1.00 50.66  ? 22  VAL   E O     1 
ATOM   10403 C  CB    . VAL   D 3  20  ? -22.160 90.588  -87.073  1.00 42.05  ? 22  VAL   E CB    1 
ATOM   10404 C  CG1   . VAL   D 3  20  ? -21.871 90.391  -85.607  1.00 48.64  ? 22  VAL   E CG1   1 
ATOM   10405 C  CG2   . VAL   D 3  20  ? -21.202 89.741  -87.912  1.00 54.35  ? 22  VAL   E CG2   1 
ATOM   10406 N  N     . ILE   D 3  21  ? -24.200 88.514  -89.024  1.00 54.00  ? 23  ILE   E N     1 
ATOM   10407 C  CA    . ILE   D 3  21  ? -24.393 87.150  -89.504  1.00 60.54  ? 23  ILE   E CA    1 
ATOM   10408 C  C     . ILE   D 3  21  ? -23.379 86.863  -90.606  1.00 54.85  ? 23  ILE   E C     1 
ATOM   10409 O  O     . ILE   D 3  21  ? -23.282 87.606  -91.591  1.00 61.95  ? 23  ILE   E O     1 
ATOM   10410 C  CB    . ILE   D 3  21  ? -25.843 86.907  -89.959  1.00 53.80  ? 23  ILE   E CB    1 
ATOM   10411 C  CG1   . ILE   D 3  21  ? -25.917 86.568  -91.436  1.00 57.06  ? 23  ILE   E CG1   1 
ATOM   10412 C  CG2   . ILE   D 3  21  ? -26.743 88.081  -89.572  1.00 46.50  ? 23  ILE   E CG2   1 
ATOM   10413 C  CD1   . ILE   D 3  21  ? -27.278 86.009  -91.830  1.00 71.73  ? 23  ILE   E CD1   1 
ATOM   10414 N  N     . LEU   D 3  22  ? -22.599 85.796  -90.412  1.00 58.77  ? 24  LEU   E N     1 
ATOM   10415 C  CA    . LEU   D 3  22  ? -21.575 85.359  -91.354  1.00 63.95  ? 24  LEU   E CA    1 
ATOM   10416 C  C     . LEU   D 3  22  ? -22.107 84.406  -92.418  1.00 60.62  ? 24  LEU   E C     1 
ATOM   10417 O  O     . LEU   D 3  22  ? -21.471 84.259  -93.466  1.00 59.71  ? 24  LEU   E O     1 
ATOM   10418 C  CB    . LEU   D 3  22  ? -20.428 84.650  -90.620  1.00 52.59  ? 24  LEU   E CB    1 
ATOM   10419 C  CG    . LEU   D 3  22  ? -19.690 85.213  -89.401  1.00 58.26  ? 24  LEU   E CG    1 
ATOM   10420 C  CD1   . LEU   D 3  22  ? -20.619 85.532  -88.246  1.00 55.70  ? 24  LEU   E CD1   1 
ATOM   10421 C  CD2   . LEU   D 3  22  ? -18.662 84.202  -88.947  1.00 51.69  ? 24  LEU   E CD2   1 
ATOM   10422 N  N     . LYS   D 3  23  ? -23.244 83.756  -92.170  1.00 54.32  ? 25  LYS   E N     1 
ATOM   10423 C  CA    . LYS   D 3  23  ? -23.783 82.708  -93.028  1.00 56.93  ? 25  LYS   E CA    1 
ATOM   10424 C  C     . LYS   D 3  23  ? -25.205 82.378  -92.570  1.00 60.20  ? 25  LYS   E C     1 
ATOM   10425 O  O     . LYS   D 3  23  ? -25.418 82.123  -91.375  1.00 61.38  ? 25  LYS   E O     1 
ATOM   10426 C  CB    . LYS   D 3  23  ? -22.864 81.479  -92.982  1.00 54.88  ? 25  LYS   E CB    1 
ATOM   10427 C  CG    . LYS   D 3  23  ? -23.231 80.347  -93.943  1.00 67.52  ? 25  LYS   E CG    1 
ATOM   10428 C  CD    . LYS   D 3  23  ? -22.053 79.388  -94.175  1.00 72.52  ? 25  LYS   E CD    1 
ATOM   10429 C  CE    . LYS   D 3  23  ? -21.584 78.711  -92.883  1.00 72.23  ? 25  LYS   E CE    1 
ATOM   10430 N  NZ    . LYS   D 3  23  ? -20.090 78.780  -92.701  1.00 60.68  ? 25  LYS   E NZ    1 
ATOM   10431 N  N     . PRO   D 3  24  ? -26.204 82.394  -93.458  1.00 64.61  ? 26  PRO   E N     1 
ATOM   10432 C  CA    . PRO   D 3  24  ? -27.602 82.176  -93.016  1.00 66.53  ? 26  PRO   E CA    1 
ATOM   10433 C  C     . PRO   D 3  24  ? -27.874 80.697  -92.801  1.00 55.84  ? 26  PRO   E C     1 
ATOM   10434 O  O     . PRO   D 3  24  ? -27.030 79.854  -93.141  1.00 63.47  ? 26  PRO   E O     1 
ATOM   10435 C  CB    . PRO   D 3  24  ? -28.431 82.741  -94.181  1.00 54.14  ? 26  PRO   E CB    1 
ATOM   10436 C  CG    . PRO   D 3  24  ? -27.584 82.465  -95.369  1.00 54.20  ? 26  PRO   E CG    1 
ATOM   10437 C  CD    . PRO   D 3  24  ? -26.122 82.574  -94.918  1.00 58.01  ? 26  PRO   E CD    1 
ATOM   10438 N  N     . PRO   D 3  25  ? -29.051 80.333  -92.259  1.00 51.51  ? 27  PRO   E N     1 
ATOM   10439 C  CA    . PRO   D 3  25  ? -29.280 78.932  -91.842  1.00 57.24  ? 27  PRO   E CA    1 
ATOM   10440 C  C     . PRO   D 3  25  ? -29.339 77.893  -92.973  1.00 69.15  ? 27  PRO   E C     1 
ATOM   10441 O  O     . PRO   D 3  25  ? -28.375 77.723  -93.738  1.00 56.92  ? 27  PRO   E O     1 
ATOM   10442 C  CB    . PRO   D 3  25  ? -30.616 79.010  -91.080  1.00 48.43  ? 27  PRO   E CB    1 
ATOM   10443 C  CG    . PRO   D 3  25  ? -31.253 80.278  -91.496  1.00 51.67  ? 27  PRO   E CG    1 
ATOM   10444 C  CD    . PRO   D 3  25  ? -30.164 81.229  -91.893  1.00 53.46  ? 27  PRO   E CD    1 
ATOM   10445 N  N     . SER   D 3  26  ? -30.448 77.147  -93.045  1.00 69.83  ? 28  SER   E N     1 
ATOM   10446 C  CA    . SER   D 3  26  ? -30.675 76.143  -94.097  1.00 63.35  ? 28  SER   E CA    1 
ATOM   10447 C  C     . SER   D 3  26  ? -32.081 75.556  -93.993  1.00 70.24  ? 28  SER   E C     1 
ATOM   10448 O  O     . SER   D 3  26  ? -32.317 74.595  -93.258  1.00 74.01  ? 28  SER   E O     1 
ATOM   10449 C  CB    . SER   D 3  26  ? -29.635 75.019  -94.035  1.00 61.53  ? 28  SER   E CB    1 
ATOM   10450 O  OG    . SER   D 3  26  ? -28.375 75.454  -94.522  1.00 49.13  ? 28  SER   E OG    1 
ATOM   10451 N  N     . ASP   D 3  42  ? -47.462 72.160  -66.272  1.00 82.08  ? 44  ASP   E N     1 
ATOM   10452 C  CA    . ASP   D 3  42  ? -47.263 73.117  -65.182  1.00 90.08  ? 44  ASP   E CA    1 
ATOM   10453 C  C     . ASP   D 3  42  ? -48.091 72.710  -63.962  1.00 92.06  ? 44  ASP   E C     1 
ATOM   10454 O  O     . ASP   D 3  42  ? -49.317 72.890  -63.956  1.00 86.44  ? 44  ASP   E O     1 
ATOM   10455 C  CB    . ASP   D 3  42  ? -47.640 74.541  -65.627  1.00 90.37  ? 44  ASP   E CB    1 
ATOM   10456 C  CG    . ASP   D 3  42  ? -46.820 75.627  -64.916  1.00 88.00  ? 44  ASP   E CG    1 
ATOM   10457 O  OD1   . ASP   D 3  42  ? -45.948 75.289  -64.082  1.00 69.97  ? 44  ASP   E OD1   1 
ATOM   10458 O  OD2   . ASP   D 3  42  ? -47.046 76.827  -65.206  1.00 84.60  ? 44  ASP   E OD2   1 
ATOM   10459 N  N     . PRO   D 3  43  ? -47.429 72.170  -62.931  1.00 90.69  ? 45  PRO   E N     1 
ATOM   10460 C  CA    . PRO   D 3  43  ? -48.173 71.691  -61.758  1.00 80.62  ? 45  PRO   E CA    1 
ATOM   10461 C  C     . PRO   D 3  43  ? -48.804 72.850  -61.000  1.00 74.91  ? 45  PRO   E C     1 
ATOM   10462 O  O     . PRO   D 3  43  ? -48.235 73.942  -60.902  1.00 71.17  ? 45  PRO   E O     1 
ATOM   10463 C  CB    . PRO   D 3  43  ? -47.106 70.975  -60.913  1.00 69.06  ? 45  PRO   E CB    1 
ATOM   10464 C  CG    . PRO   D 3  43  ? -45.880 70.884  -61.781  1.00 63.29  ? 45  PRO   E CG    1 
ATOM   10465 C  CD    . PRO   D 3  43  ? -45.974 72.020  -62.753  1.00 74.33  ? 45  PRO   E CD    1 
ATOM   10466 N  N     . SER   D 3  44  ? -49.994 72.600  -60.467  1.00 72.97  ? 46  SER   E N     1 
ATOM   10467 C  CA    . SER   D 3  44  ? -50.754 73.599  -59.734  1.00 66.51  ? 46  SER   E CA    1 
ATOM   10468 C  C     . SER   D 3  44  ? -50.471 73.502  -58.235  1.00 64.81  ? 46  SER   E C     1 
ATOM   10469 O  O     . SER   D 3  44  ? -49.919 72.515  -57.738  1.00 58.61  ? 46  SER   E O     1 
ATOM   10470 C  CB    . SER   D 3  44  ? -52.247 73.428  -60.009  1.00 67.28  ? 46  SER   E CB    1 
ATOM   10471 O  OG    . SER   D 3  44  ? -52.660 72.096  -59.732  1.00 71.48  ? 46  SER   E OG    1 
ATOM   10472 N  N     . LEU   D 3  45  ? -50.874 74.547  -57.507  1.00 61.42  ? 47  LEU   E N     1 
ATOM   10473 C  CA    . LEU   D 3  45  ? -50.688 74.540  -56.063  1.00 56.12  ? 47  LEU   E CA    1 
ATOM   10474 C  C     . LEU   D 3  45  ? -51.218 73.257  -55.445  1.00 63.15  ? 47  LEU   E C     1 
ATOM   10475 O  O     . LEU   D 3  45  ? -50.660 72.769  -54.456  1.00 67.00  ? 47  LEU   E O     1 
ATOM   10476 C  CB    . LEU   D 3  45  ? -51.364 75.760  -55.442  1.00 58.71  ? 47  LEU   E CB    1 
ATOM   10477 C  CG    . LEU   D 3  45  ? -51.289 75.932  -53.918  1.00 74.88  ? 47  LEU   E CG    1 
ATOM   10478 C  CD1   . LEU   D 3  45  ? -49.967 75.403  -53.344  1.00 67.11  ? 47  LEU   E CD1   1 
ATOM   10479 C  CD2   . LEU   D 3  45  ? -51.513 77.396  -53.522  1.00 58.46  ? 47  LEU   E CD2   1 
ATOM   10480 N  N     . GLU   D 3  46  ? -52.273 72.682  -56.026  1.00 66.85  ? 48  GLU   E N     1 
ATOM   10481 C  CA    . GLU   D 3  46  ? -52.889 71.475  -55.482  1.00 68.08  ? 48  GLU   E CA    1 
ATOM   10482 C  C     . GLU   D 3  46  ? -51.924 70.305  -55.498  1.00 61.73  ? 48  GLU   E C     1 
ATOM   10483 O  O     . GLU   D 3  46  ? -51.506 69.835  -54.439  1.00 68.20  ? 48  GLU   E O     1 
ATOM   10484 C  CB    . GLU   D 3  46  ? -54.151 71.101  -56.256  1.00 69.43  ? 48  GLU   E CB    1 
ATOM   10485 C  CG    . GLU   D 3  46  ? -55.443 71.279  -55.478  1.00 74.91  ? 48  GLU   E CG    1 
ATOM   10486 C  CD    . GLU   D 3  46  ? -56.672 71.005  -56.333  1.00 95.83  ? 48  GLU   E CD    1 
ATOM   10487 O  OE1   . GLU   D 3  46  ? -56.618 70.080  -57.175  1.00 98.76  ? 48  GLU   E OE1   1 
ATOM   10488 O  OE2   . GLU   D 3  46  ? -57.689 71.718  -56.174  1.00 97.40  ? 48  GLU   E OE2   1 
ATOM   10489 N  N     . GLU   D 3  47  ? -51.570 69.826  -56.692  1.00 63.49  ? 49  GLU   E N     1 
ATOM   10490 C  CA    . GLU   D 3  47  ? -50.689 68.668  -56.805  1.00 57.51  ? 49  GLU   E CA    1 
ATOM   10491 C  C     . GLU   D 3  47  ? -49.417 68.837  -55.988  1.00 65.01  ? 49  GLU   E C     1 
ATOM   10492 O  O     . GLU   D 3  47  ? -48.881 67.851  -55.466  1.00 57.08  ? 49  GLU   E O     1 
ATOM   10493 C  CB    . GLU   D 3  47  ? -50.323 68.424  -58.264  1.00 65.40  ? 49  GLU   E CB    1 
ATOM   10494 C  CG    . GLU   D 3  47  ? -51.502 68.358  -59.205  1.00 77.88  ? 49  GLU   E CG    1 
ATOM   10495 C  CD    . GLU   D 3  47  ? -51.170 68.948  -60.553  1.00 84.30  ? 49  GLU   E CD    1 
ATOM   10496 O  OE1   . GLU   D 3  47  ? -50.919 70.173  -60.609  1.00 79.13  ? 49  GLU   E OE1   1 
ATOM   10497 O  OE2   . GLU   D 3  47  ? -51.136 68.186  -61.547  1.00 95.38  ? 49  GLU   E OE2   1 
ATOM   10498 N  N     . ILE   D 3  48  ? -48.912 70.070  -55.876  1.00 63.90  ? 50  ILE   E N     1 
ATOM   10499 C  CA    . ILE   D 3  48  ? -47.715 70.312  -55.074  1.00 59.74  ? 50  ILE   E CA    1 
ATOM   10500 C  C     . ILE   D 3  48  ? -47.985 70.015  -53.603  1.00 61.61  ? 50  ILE   E C     1 
ATOM   10501 O  O     . ILE   D 3  48  ? -47.158 69.399  -52.914  1.00 57.09  ? 50  ILE   E O     1 
ATOM   10502 C  CB    . ILE   D 3  48  ? -47.214 71.752  -55.281  1.00 58.58  ? 50  ILE   E CB    1 
ATOM   10503 C  CG1   . ILE   D 3  48  ? -46.216 71.816  -56.447  1.00 69.56  ? 50  ILE   E CG1   1 
ATOM   10504 C  CG2   . ILE   D 3  48  ? -46.582 72.293  -54.000  1.00 58.25  ? 50  ILE   E CG2   1 
ATOM   10505 C  CD1   . ILE   D 3  48  ? -46.784 71.493  -57.827  1.00 57.69  ? 50  ILE   E CD1   1 
ATOM   10506 N  N     . GLN   D 3  49  ? -49.141 70.452  -53.094  1.00 66.44  ? 51  GLN   E N     1 
ATOM   10507 C  CA    . GLN   D 3  49  ? -49.483 70.167  -51.706  1.00 58.72  ? 51  GLN   E CA    1 
ATOM   10508 C  C     . GLN   D 3  49  ? -49.617 68.669  -51.479  1.00 56.66  ? 51  GLN   E C     1 
ATOM   10509 O  O     . GLN   D 3  49  ? -49.056 68.124  -50.525  1.00 56.35  ? 51  GLN   E O     1 
ATOM   10510 C  CB    . GLN   D 3  49  ? -50.758 70.903  -51.310  1.00 54.69  ? 51  GLN   E CB    1 
ATOM   10511 C  CG    . GLN   D 3  49  ? -50.504 72.333  -50.853  1.00 71.98  ? 51  GLN   E CG    1 
ATOM   10512 C  CD    . GLN   D 3  49  ? -49.247 72.468  -49.988  1.00 85.21  ? 51  GLN   E CD    1 
ATOM   10513 O  OE1   . GLN   D 3  49  ? -48.810 71.505  -49.334  1.00 78.63  ? 51  GLN   E OE1   1 
ATOM   10514 N  NE2   . GLN   D 3  49  ? -48.654 73.669  -49.988  1.00 80.67  ? 51  GLN   E NE2   1 
ATOM   10515 N  N     . LYS   D 3  50  ? -50.341 67.980  -52.361  1.00 52.82  ? 52  LYS   E N     1 
ATOM   10516 C  CA    . LYS   D 3  50  ? -50.339 66.525  -52.329  1.00 49.77  ? 52  LYS   E CA    1 
ATOM   10517 C  C     . LYS   D 3  50  ? -48.914 66.008  -52.181  1.00 56.48  ? 52  LYS   E C     1 
ATOM   10518 O  O     . LYS   D 3  50  ? -48.635 65.136  -51.352  1.00 62.81  ? 52  LYS   E O     1 
ATOM   10519 C  CB    . LYS   D 3  50  ? -50.989 65.970  -53.602  1.00 49.63  ? 52  LYS   E CB    1 
ATOM   10520 C  CG    . LYS   D 3  50  ? -52.277 65.163  -53.400  1.00 50.92  ? 52  LYS   E CG    1 
ATOM   10521 C  CD    . LYS   D 3  50  ? -53.539 65.998  -53.703  1.00 70.48  ? 52  LYS   E CD    1 
ATOM   10522 C  CE    . LYS   D 3  50  ? -54.840 65.175  -53.620  1.00 68.89  ? 52  LYS   E CE    1 
ATOM   10523 N  NZ    . LYS   D 3  50  ? -55.026 64.202  -54.748  1.00 73.95  ? 52  LYS   E NZ    1 
ATOM   10524 N  N     . LYS   D 3  51  ? -47.993 66.564  -52.972  1.00 62.69  ? 53  LYS   E N     1 
ATOM   10525 C  CA    . LYS   D 3  51  ? -46.601 66.129  -52.975  1.00 56.78  ? 53  LYS   E CA    1 
ATOM   10526 C  C     . LYS   D 3  51  ? -45.998 66.227  -51.578  1.00 56.76  ? 53  LYS   E C     1 
ATOM   10527 O  O     . LYS   D 3  51  ? -45.551 65.229  -51.000  1.00 45.91  ? 53  LYS   E O     1 
ATOM   10528 C  CB    . LYS   D 3  51  ? -45.809 66.986  -53.976  1.00 62.92  ? 53  LYS   E CB    1 
ATOM   10529 C  CG    . LYS   D 3  51  ? -44.436 66.459  -54.395  1.00 61.77  ? 53  LYS   E CG    1 
ATOM   10530 C  CD    . LYS   D 3  51  ? -44.375 66.180  -55.915  1.00 81.84  ? 53  LYS   E CD    1 
ATOM   10531 C  CE    . LYS   D 3  51  ? -45.215 64.944  -56.327  1.00 66.43  ? 53  LYS   E CE    1 
ATOM   10532 N  NZ    . LYS   D 3  51  ? -45.167 64.612  -57.791  1.00 59.39  ? 53  LYS   E NZ    1 
ATOM   10533 N  N     . LEU   D 3  52  ? -45.979 67.437  -51.021  1.00 48.89  ? 54  LEU   E N     1 
ATOM   10534 C  CA    . LEU   D 3  52  ? -45.364 67.639  -49.718  1.00 53.37  ? 54  LEU   E CA    1 
ATOM   10535 C  C     . LEU   D 3  52  ? -46.082 66.832  -48.637  1.00 60.78  ? 54  LEU   E C     1 
ATOM   10536 O  O     . LEU   D 3  52  ? -45.451 66.087  -47.877  1.00 65.51  ? 54  LEU   E O     1 
ATOM   10537 C  CB    . LEU   D 3  52  ? -45.363 69.135  -49.382  1.00 60.51  ? 54  LEU   E CB    1 
ATOM   10538 C  CG    . LEU   D 3  52  ? -44.947 70.080  -50.514  1.00 58.71  ? 54  LEU   E CG    1 
ATOM   10539 C  CD1   . LEU   D 3  52  ? -44.616 71.451  -49.961  1.00 60.08  ? 54  LEU   E CD1   1 
ATOM   10540 C  CD2   . LEU   D 3  52  ? -43.765 69.516  -51.277  1.00 55.34  ? 54  LEU   E CD2   1 
ATOM   10541 N  N     . GLU   D 3  53  ? -47.411 66.966  -48.562  1.00 67.86  ? 55  GLU   E N     1 
ATOM   10542 C  CA    . GLU   D 3  53  ? -48.186 66.288  -47.525  1.00 64.51  ? 55  GLU   E CA    1 
ATOM   10543 C  C     . GLU   D 3  53  ? -47.938 64.786  -47.540  1.00 54.30  ? 55  GLU   E C     1 
ATOM   10544 O  O     . GLU   D 3  53  ? -47.746 64.168  -46.488  1.00 49.18  ? 55  GLU   E O     1 
ATOM   10545 C  CB    . GLU   D 3  53  ? -49.676 66.582  -47.711  1.00 49.44  ? 55  GLU   E CB    1 
ATOM   10546 C  CG    . GLU   D 3  53  ? -50.314 67.220  -46.518  1.00 50.28  ? 55  GLU   E CG    1 
ATOM   10547 C  CD    . GLU   D 3  53  ? -51.062 68.471  -46.874  1.00 68.13  ? 55  GLU   E CD    1 
ATOM   10548 O  OE1   . GLU   D 3  53  ? -51.981 68.375  -47.724  1.00 57.18  ? 55  GLU   E OE1   1 
ATOM   10549 O  OE2   . GLU   D 3  53  ? -50.720 69.544  -46.310  1.00 73.18  ? 55  GLU   E OE2   1 
ATOM   10550 N  N     . ALA   D 3  54  ? -47.954 64.179  -48.727  1.00 45.43  ? 56  ALA   E N     1 
ATOM   10551 C  CA    . ALA   D 3  54  ? -47.734 62.740  -48.820  1.00 48.58  ? 56  ALA   E CA    1 
ATOM   10552 C  C     . ALA   D 3  54  ? -46.355 62.357  -48.300  1.00 58.87  ? 56  ALA   E C     1 
ATOM   10553 O  O     . ALA   D 3  54  ? -46.196 61.330  -47.628  1.00 55.85  ? 56  ALA   E O     1 
ATOM   10554 C  CB    . ALA   D 3  54  ? -47.898 62.276  -50.264  1.00 37.38  ? 56  ALA   E CB    1 
ATOM   10555 N  N     . ALA   D 3  55  ? -45.341 63.167  -48.616  1.00 57.11  ? 57  ALA   E N     1 
ATOM   10556 C  CA    . ALA   D 3  55  ? -43.995 62.882  -48.146  1.00 53.12  ? 57  ALA   E CA    1 
ATOM   10557 C  C     . ALA   D 3  55  ? -43.926 62.974  -46.629  1.00 55.09  ? 57  ALA   E C     1 
ATOM   10558 O  O     . ALA   D 3  55  ? -43.338 62.106  -45.967  1.00 51.95  ? 57  ALA   E O     1 
ATOM   10559 C  CB    . ALA   D 3  55  ? -43.009 63.848  -48.794  1.00 50.72  ? 57  ALA   E CB    1 
ATOM   10560 N  N     . GLU   D 3  56  ? -44.531 64.018  -46.060  1.00 55.77  ? 58  GLU   E N     1 
ATOM   10561 C  CA    . GLU   D 3  56  ? -44.530 64.180  -44.609  1.00 58.10  ? 58  GLU   E CA    1 
ATOM   10562 C  C     . GLU   D 3  56  ? -45.218 63.010  -43.906  1.00 56.58  ? 58  GLU   E C     1 
ATOM   10563 O  O     . GLU   D 3  56  ? -44.799 62.599  -42.820  1.00 52.26  ? 58  GLU   E O     1 
ATOM   10564 C  CB    . GLU   D 3  56  ? -45.196 65.499  -44.239  1.00 47.01  ? 58  GLU   E CB    1 
ATOM   10565 C  CG    . GLU   D 3  56  ? -45.917 65.470  -42.928  1.00 49.23  ? 58  GLU   E CG    1 
ATOM   10566 C  CD    . GLU   D 3  56  ? -46.881 66.630  -42.809  1.00 72.62  ? 58  GLU   E CD    1 
ATOM   10567 O  OE1   . GLU   D 3  56  ? -47.740 66.789  -43.713  1.00 71.56  ? 58  GLU   E OE1   1 
ATOM   10568 O  OE2   . GLU   D 3  56  ? -46.769 67.397  -41.826  1.00 79.40  ? 58  GLU   E OE2   1 
ATOM   10569 N  N     . GLU   D 3  57  ? -46.269 62.452  -44.511  1.00 56.38  ? 59  GLU   E N     1 
ATOM   10570 C  CA    . GLU   D 3  57  ? -46.941 61.316  -43.890  1.00 61.18  ? 59  GLU   E CA    1 
ATOM   10571 C  C     . GLU   D 3  57  ? -46.114 60.035  -43.994  1.00 59.12  ? 59  GLU   E C     1 
ATOM   10572 O  O     . GLU   D 3  57  ? -46.253 59.145  -43.145  1.00 57.64  ? 59  GLU   E O     1 
ATOM   10573 C  CB    . GLU   D 3  57  ? -48.336 61.116  -44.498  1.00 53.49  ? 59  GLU   E CB    1 
ATOM   10574 C  CG    . GLU   D 3  57  ? -49.016 59.798  -44.088  1.00 66.45  ? 59  GLU   E CG    1 
ATOM   10575 C  CD    . GLU   D 3  57  ? -49.183 59.624  -42.559  1.00 86.55  ? 59  GLU   E CD    1 
ATOM   10576 O  OE1   . GLU   D 3  57  ? -49.676 60.567  -41.886  1.00 82.81  ? 59  GLU   E OE1   1 
ATOM   10577 O  OE2   . GLU   D 3  57  ? -48.824 58.535  -42.033  1.00 70.32  ? 59  GLU   E OE2   1 
ATOM   10578 N  N     . ARG   D 3  58  ? -45.252 59.913  -45.008  1.00 53.83  ? 60  ARG   E N     1 
ATOM   10579 C  CA    . ARG   D 3  58  ? -44.346 58.768  -45.042  1.00 48.99  ? 60  ARG   E CA    1 
ATOM   10580 C  C     . ARG   D 3  58  ? -43.294 58.869  -43.946  1.00 48.03  ? 60  ARG   E C     1 
ATOM   10581 O  O     . ARG   D 3  58  ? -43.008 57.883  -43.264  1.00 54.39  ? 60  ARG   E O     1 
ATOM   10582 C  CB    . ARG   D 3  58  ? -43.685 58.641  -46.410  1.00 48.87  ? 60  ARG   E CB    1 
ATOM   10583 C  CG    . ARG   D 3  58  ? -44.664 58.430  -47.540  1.00 52.91  ? 60  ARG   E CG    1 
ATOM   10584 C  CD    . ARG   D 3  58  ? -44.037 57.733  -48.759  1.00 61.33  ? 60  ARG   E CD    1 
ATOM   10585 N  NE    . ARG   D 3  58  ? -43.379 58.639  -49.695  1.00 55.19  ? 60  ARG   E NE    1 
ATOM   10586 C  CZ    . ARG   D 3  58  ? -43.945 59.722  -50.215  1.00 65.82  ? 60  ARG   E CZ    1 
ATOM   10587 N  NH1   . ARG   D 3  58  ? -45.150 60.122  -49.840  1.00 59.78  ? 60  ARG   E NH1   1 
ATOM   10588 N  NH2   . ARG   D 3  58  ? -43.283 60.428  -51.127  1.00 61.52  ? 60  ARG   E NH2   1 
ATOM   10589 N  N     . ARG   D 3  59  ? -42.726 60.056  -43.742  1.00 50.63  ? 61  ARG   E N     1 
ATOM   10590 C  CA    . ARG   D 3  59  ? -41.778 60.228  -42.647  1.00 47.27  ? 61  ARG   E CA    1 
ATOM   10591 C  C     . ARG   D 3  59  ? -42.486 60.208  -41.295  1.00 52.59  ? 61  ARG   E C     1 
ATOM   10592 O  O     . ARG   D 3  59  ? -41.888 59.806  -40.286  1.00 57.26  ? 61  ARG   E O     1 
ATOM   10593 C  CB    . ARG   D 3  59  ? -40.959 61.522  -42.847  1.00 40.50  ? 61  ARG   E CB    1 
ATOM   10594 C  CG    . ARG   D 3  59  ? -41.296 62.672  -41.915  1.00 37.46  ? 61  ARG   E CG    1 
ATOM   10595 C  CD    . ARG   D 3  59  ? -40.359 63.881  -42.088  1.00 40.24  ? 61  ARG   E CD    1 
ATOM   10596 N  NE    . ARG   D 3  59  ? -40.295 64.383  -43.462  1.00 60.39  ? 61  ARG   E NE    1 
ATOM   10597 C  CZ    . ARG   D 3  59  ? -41.123 65.275  -44.003  1.00 51.04  ? 61  ARG   E CZ    1 
ATOM   10598 N  NH1   . ARG   D 3  59  ? -42.128 65.799  -43.319  1.00 50.31  ? 61  ARG   E NH1   1 
ATOM   10599 N  NH2   . ARG   D 3  59  ? -40.941 65.648  -45.268  1.00 39.68  ? 61  ARG   E NH2   1 
ATOM   10600 N  N     . LYS   D 3  60  ? -43.758 60.622  -41.249  1.00 58.06  ? 62  LYS   E N     1 
ATOM   10601 C  CA    . LYS   D 3  60  ? -44.530 60.494  -40.011  1.00 52.41  ? 62  LYS   E CA    1 
ATOM   10602 C  C     . LYS   D 3  60  ? -44.770 59.031  -39.665  1.00 46.18  ? 62  LYS   E C     1 
ATOM   10603 O  O     . LYS   D 3  60  ? -44.752 58.657  -38.486  1.00 36.56  ? 62  LYS   E O     1 
ATOM   10604 C  CB    . LYS   D 3  60  ? -45.865 61.228  -40.129  1.00 53.86  ? 62  LYS   E CB    1 
ATOM   10605 C  CG    . LYS   D 3  60  ? -45.977 62.475  -39.276  1.00 45.32  ? 62  LYS   E CG    1 
ATOM   10606 C  CD    . LYS   D 3  60  ? -47.417 62.949  -39.206  1.00 52.81  ? 62  LYS   E CD    1 
ATOM   10607 C  CE    . LYS   D 3  60  ? -47.493 64.438  -38.903  1.00 55.01  ? 62  LYS   E CE    1 
ATOM   10608 N  NZ    . LYS   D 3  60  ? -48.177 65.156  -40.021  1.00 71.94  ? 62  LYS   E NZ    1 
ATOM   10609 N  N     . TYR   D 3  61  ? -45.007 58.200  -40.683  1.00 40.97  ? 63  TYR   E N     1 
ATOM   10610 C  CA    . TYR   D 3  61  ? -45.230 56.778  -40.464  1.00 39.68  ? 63  TYR   E CA    1 
ATOM   10611 C  C     . TYR   D 3  61  ? -43.945 56.098  -40.033  1.00 49.38  ? 63  TYR   E C     1 
ATOM   10612 O  O     . TYR   D 3  61  ? -43.908 55.405  -39.006  1.00 46.93  ? 63  TYR   E O     1 
ATOM   10613 C  CB    . TYR   D 3  61  ? -45.789 56.144  -41.738  1.00 45.94  ? 63  TYR   E CB    1 
ATOM   10614 C  CG    . TYR   D 3  61  ? -45.879 54.634  -41.754  1.00 43.61  ? 63  TYR   E CG    1 
ATOM   10615 C  CD1   . TYR   D 3  61  ? -46.901 53.957  -41.087  1.00 57.43  ? 63  TYR   E CD1   1 
ATOM   10616 C  CD2   . TYR   D 3  61  ? -44.965 53.883  -42.466  1.00 44.39  ? 63  TYR   E CD2   1 
ATOM   10617 C  CE1   . TYR   D 3  61  ? -46.982 52.565  -41.122  1.00 52.20  ? 63  TYR   E CE1   1 
ATOM   10618 C  CE2   . TYR   D 3  61  ? -45.038 52.509  -42.508  1.00 43.01  ? 63  TYR   E CE2   1 
ATOM   10619 C  CZ    . TYR   D 3  61  ? -46.039 51.853  -41.837  1.00 51.00  ? 63  TYR   E CZ    1 
ATOM   10620 O  OH    . TYR   D 3  61  ? -46.081 50.481  -41.902  1.00 55.07  ? 63  TYR   E OH    1 
ATOM   10621 N  N     . GLN   D 3  62  ? -42.873 56.312  -40.796  1.00 52.35  ? 64  GLN   E N     1 
ATOM   10622 C  CA    . GLN   D 3  62  ? -41.584 55.723  -40.462  1.00 53.47  ? 64  GLN   E CA    1 
ATOM   10623 C  C     . GLN   D 3  62  ? -41.220 55.970  -39.012  1.00 43.22  ? 64  GLN   E C     1 
ATOM   10624 O  O     . GLN   D 3  62  ? -40.720 55.070  -38.328  1.00 47.99  ? 64  GLN   E O     1 
ATOM   10625 C  CB    . GLN   D 3  62  ? -40.499 56.276  -41.381  1.00 48.11  ? 64  GLN   E CB    1 
ATOM   10626 C  CG    . GLN   D 3  62  ? -40.516 55.621  -42.744  1.00 61.53  ? 64  GLN   E CG    1 
ATOM   10627 C  CD    . GLN   D 3  62  ? -40.075 56.558  -43.838  1.00 65.12  ? 64  GLN   E CD    1 
ATOM   10628 O  OE1   . GLN   D 3  62  ? -39.398 57.567  -43.576  1.00 64.11  ? 64  GLN   E OE1   1 
ATOM   10629 N  NE2   . GLN   D 3  62  ? -40.458 56.241  -45.079  1.00 58.74  ? 64  GLN   E NE2   1 
ATOM   10630 N  N     . GLU   D 3  63  ? -41.468 57.176  -38.517  1.00 36.02  ? 65  GLU   E N     1 
ATOM   10631 C  CA    . GLU   D 3  63  ? -41.154 57.443  -37.123  1.00 47.24  ? 65  GLU   E CA    1 
ATOM   10632 C  C     . GLU   D 3  63  ? -42.023 56.578  -36.209  1.00 57.09  ? 65  GLU   E C     1 
ATOM   10633 O  O     . GLU   D 3  63  ? -41.511 55.793  -35.395  1.00 49.62  ? 65  GLU   E O     1 
ATOM   10634 C  CB    . GLU   D 3  63  ? -41.322 58.936  -36.817  1.00 41.99  ? 65  GLU   E CB    1 
ATOM   10635 C  CG    . GLU   D 3  63  ? -40.851 59.296  -35.417  1.00 41.62  ? 65  GLU   E CG    1 
ATOM   10636 C  CD    . GLU   D 3  63  ? -40.962 60.779  -35.092  1.00 52.52  ? 65  GLU   E CD    1 
ATOM   10637 O  OE1   . GLU   D 3  63  ? -40.015 61.544  -35.413  1.00 46.80  ? 65  GLU   E OE1   1 
ATOM   10638 O  OE2   . GLU   D 3  63  ? -41.988 61.169  -34.490  1.00 43.78  ? 65  GLU   E OE2   1 
ATOM   10639 N  N     . ALA   D 3  64  ? -43.351 56.695  -36.359  1.00 59.73  ? 66  ALA   E N     1 
ATOM   10640 C  CA    . ALA   D 3  64  ? -44.335 55.920  -35.606  1.00 56.69  ? 66  ALA   E CA    1 
ATOM   10641 C  C     . ALA   D 3  64  ? -43.929 54.452  -35.534  1.00 48.53  ? 66  ALA   E C     1 
ATOM   10642 O  O     . ALA   D 3  64  ? -44.062 53.817  -34.486  1.00 43.19  ? 66  ALA   E O     1 
ATOM   10643 C  CB    . ALA   D 3  64  ? -45.732 56.061  -36.234  1.00 32.15  ? 66  ALA   E CB    1 
ATOM   10644 N  N     . GLU   D 3  65  ? -43.442 53.904  -36.647  1.00 45.96  ? 67  GLU   E N     1 
ATOM   10645 C  CA    . GLU   D 3  65  ? -42.902 52.553  -36.614  1.00 45.28  ? 67  GLU   E CA    1 
ATOM   10646 C  C     . GLU   D 3  65  ? -41.720 52.475  -35.652  1.00 54.75  ? 67  GLU   E C     1 
ATOM   10647 O  O     . GLU   D 3  65  ? -41.593 51.514  -34.882  1.00 55.92  ? 67  GLU   E O     1 
ATOM   10648 C  CB    . GLU   D 3  65  ? -42.503 52.128  -38.023  1.00 39.38  ? 67  GLU   E CB    1 
ATOM   10649 C  CG    . GLU   D 3  65  ? -42.752 50.661  -38.357  1.00 58.57  ? 67  GLU   E CG    1 
ATOM   10650 C  CD    . GLU   D 3  65  ? -44.221 50.256  -38.291  1.00 61.28  ? 67  GLU   E CD    1 
ATOM   10651 O  OE1   . GLU   D 3  65  ? -45.096 51.144  -38.178  1.00 61.27  ? 67  GLU   E OE1   1 
ATOM   10652 O  OE2   . GLU   D 3  65  ? -44.492 49.035  -38.344  1.00 63.60  ? 67  GLU   E OE2   1 
ATOM   10653 N  N     . LEU   D 3  66  ? -40.869 53.502  -35.654  1.00 53.21  ? 68  LEU   E N     1 
ATOM   10654 C  CA    . LEU   D 3  66  ? -39.708 53.517  -34.772  1.00 51.48  ? 68  LEU   E CA    1 
ATOM   10655 C  C     . LEU   D 3  66  ? -40.129 53.554  -33.314  1.00 52.25  ? 68  LEU   E C     1 
ATOM   10656 O  O     . LEU   D 3  66  ? -39.672 52.744  -32.500  1.00 54.70  ? 68  LEU   E O     1 
ATOM   10657 C  CB    . LEU   D 3  66  ? -38.828 54.724  -35.083  1.00 51.97  ? 68  LEU   E CB    1 
ATOM   10658 C  CG    . LEU   D 3  66  ? -37.593 54.809  -34.191  1.00 43.17  ? 68  LEU   E CG    1 
ATOM   10659 C  CD1   . LEU   D 3  66  ? -36.397 54.277  -34.944  1.00 37.82  ? 68  LEU   E CD1   1 
ATOM   10660 C  CD2   . LEU   D 3  66  ? -37.365 56.230  -33.714  1.00 37.15  ? 68  LEU   E CD2   1 
ATOM   10661 N  N     . LEU   D 3  67  ? -40.965 54.529  -32.955  1.00 57.50  ? 69  LEU   E N     1 
ATOM   10662 C  CA    . LEU   D 3  67  ? -41.489 54.591  -31.596  1.00 48.77  ? 69  LEU   E CA    1 
ATOM   10663 C  C     . LEU   D 3  67  ? -42.168 53.284  -31.206  1.00 49.66  ? 69  LEU   E C     1 
ATOM   10664 O  O     . LEU   D 3  67  ? -42.025 52.819  -30.069  1.00 51.11  ? 69  LEU   E O     1 
ATOM   10665 C  CB    . LEU   D 3  67  ? -42.459 55.764  -31.474  1.00 38.63  ? 69  LEU   E CB    1 
ATOM   10666 C  CG    . LEU   D 3  67  ? -41.771 57.115  -31.679  1.00 43.14  ? 69  LEU   E CG    1 
ATOM   10667 C  CD1   . LEU   D 3  67  ? -42.782 58.239  -31.609  1.00 32.53  ? 69  LEU   E CD1   1 
ATOM   10668 C  CD2   . LEU   D 3  67  ? -40.675 57.313  -30.646  1.00 30.08  ? 69  LEU   E CD2   1 
ATOM   10669 N  N     . LYS   D 3  68  ? -42.907 52.671  -32.140  1.00 45.97  ? 70  LYS   E N     1 
ATOM   10670 C  CA    . LYS   D 3  68  ? -43.579 51.410  -31.841  1.00 46.48  ? 70  LYS   E CA    1 
ATOM   10671 C  C     . LYS   D 3  68  ? -42.571 50.315  -31.525  1.00 52.25  ? 70  LYS   E C     1 
ATOM   10672 O  O     . LYS   D 3  68  ? -42.767 49.532  -30.589  1.00 44.29  ? 70  LYS   E O     1 
ATOM   10673 C  CB    . LYS   D 3  68  ? -44.465 50.985  -33.009  1.00 54.21  ? 70  LYS   E CB    1 
ATOM   10674 C  CG    . LYS   D 3  68  ? -44.554 49.471  -33.183  1.00 55.12  ? 70  LYS   E CG    1 
ATOM   10675 C  CD    . LYS   D 3  68  ? -45.336 49.094  -34.435  1.00 70.56  ? 70  LYS   E CD    1 
ATOM   10676 C  CE    . LYS   D 3  68  ? -45.314 47.590  -34.678  1.00 77.79  ? 70  LYS   E CE    1 
ATOM   10677 N  NZ    . LYS   D 3  68  ? -45.467 47.272  -36.133  1.00 81.85  ? 70  LYS   E NZ    1 
ATOM   10678 N  N     . HIS   D 3  69  ? -41.486 50.240  -32.302  1.00 54.47  ? 71  HIS   E N     1 
ATOM   10679 C  CA    . HIS   D 3  69  ? -40.445 49.257  -32.027  1.00 50.85  ? 71  HIS   E CA    1 
ATOM   10680 C  C     . HIS   D 3  69  ? -39.766 49.530  -30.689  1.00 48.60  ? 71  HIS   E C     1 
ATOM   10681 O  O     . HIS   D 3  69  ? -39.451 48.595  -29.945  1.00 44.10  ? 71  HIS   E O     1 
ATOM   10682 C  CB    . HIS   D 3  69  ? -39.430 49.252  -33.168  1.00 51.43  ? 71  HIS   E CB    1 
ATOM   10683 C  CG    . HIS   D 3  69  ? -38.290 48.298  -32.973  1.00 59.98  ? 71  HIS   E CG    1 
ATOM   10684 N  ND1   . HIS   D 3  69  ? -37.104 48.665  -32.369  1.00 58.78  ? 71  HIS   E ND1   1 
ATOM   10685 C  CD2   . HIS   D 3  69  ? -38.144 47.000  -33.327  1.00 60.08  ? 71  HIS   E CD2   1 
ATOM   10686 C  CE1   . HIS   D 3  69  ? -36.278 47.634  -32.354  1.00 59.38  ? 71  HIS   E CE1   1 
ATOM   10687 N  NE2   . HIS   D 3  69  ? -36.884 46.610  -32.929  1.00 67.34  ? 71  HIS   E NE2   1 
ATOM   10688 N  N     . LEU   D 3  70  ? -39.541 50.804  -30.356  1.00 44.50  ? 72  LEU   E N     1 
ATOM   10689 C  CA    . LEU   D 3  70  ? -38.918 51.117  -29.073  1.00 42.79  ? 72  LEU   E CA    1 
ATOM   10690 C  C     . LEU   D 3  70  ? -39.859 50.806  -27.920  1.00 44.57  ? 72  LEU   E C     1 
ATOM   10691 O  O     . LEU   D 3  70  ? -39.439 50.259  -26.897  1.00 49.97  ? 72  LEU   E O     1 
ATOM   10692 C  CB    . LEU   D 3  70  ? -38.484 52.578  -29.028  1.00 37.24  ? 72  LEU   E CB    1 
ATOM   10693 C  CG    . LEU   D 3  70  ? -37.354 53.007  -29.967  1.00 39.53  ? 72  LEU   E CG    1 
ATOM   10694 C  CD1   . LEU   D 3  70  ? -37.329 54.526  -30.107  1.00 31.99  ? 72  LEU   E CD1   1 
ATOM   10695 C  CD2   . LEU   D 3  70  ? -36.002 52.491  -29.468  1.00 37.43  ? 72  LEU   E CD2   1 
ATOM   10696 N  N     . ALA   D 3  71  ? -41.136 51.142  -28.059  1.00 47.07  ? 73  ALA   E N     1 
ATOM   10697 C  CA    . ALA   D 3  71  ? -42.089 50.796  -27.014  1.00 39.56  ? 73  ALA   E CA    1 
ATOM   10698 C  C     . ALA   D 3  71  ? -42.184 49.286  -26.827  1.00 39.62  ? 73  ALA   E C     1 
ATOM   10699 O  O     . ALA   D 3  71  ? -42.464 48.816  -25.723  1.00 42.00  ? 73  ALA   E O     1 
ATOM   10700 C  CB    . ALA   D 3  71  ? -43.454 51.393  -27.336  1.00 42.32  ? 73  ALA   E CB    1 
ATOM   10701 N  N     . GLU   D 3  72  ? -41.944 48.507  -27.877  1.00 37.68  ? 74  GLU   E N     1 
ATOM   10702 C  CA    . GLU   D 3  72  ? -41.796 47.071  -27.679  1.00 36.18  ? 74  GLU   E CA    1 
ATOM   10703 C  C     . GLU   D 3  72  ? -40.600 46.777  -26.781  1.00 50.28  ? 74  GLU   E C     1 
ATOM   10704 O  O     . GLU   D 3  72  ? -40.669 45.892  -25.922  1.00 49.73  ? 74  GLU   E O     1 
ATOM   10705 C  CB    . GLU   D 3  72  ? -41.647 46.341  -29.019  1.00 37.82  ? 74  GLU   E CB    1 
ATOM   10706 C  CG    . GLU   D 3  72  ? -42.851 46.446  -29.985  1.00 48.51  ? 74  GLU   E CG    1 
ATOM   10707 C  CD    . GLU   D 3  72  ? -42.584 45.857  -31.385  1.00 63.20  ? 74  GLU   E CD    1 
ATOM   10708 O  OE1   . GLU   D 3  72  ? -41.401 45.723  -31.792  1.00 56.13  ? 74  GLU   E OE1   1 
ATOM   10709 O  OE2   . GLU   D 3  72  ? -43.576 45.529  -32.083  1.00 67.51  ? 74  GLU   E OE2   1 
ATOM   10710 N  N     . LYS   D 3  73  ? -39.491 47.510  -26.962  1.00 45.65  ? 75  LYS   E N     1 
ATOM   10711 C  CA    . LYS   D 3  73  ? -38.326 47.298  -26.108  1.00 45.12  ? 75  LYS   E CA    1 
ATOM   10712 C  C     . LYS   D 3  73  ? -38.593 47.730  -24.671  1.00 40.92  ? 75  LYS   E C     1 
ATOM   10713 O  O     . LYS   D 3  73  ? -37.919 47.239  -23.760  1.00 44.62  ? 75  LYS   E O     1 
ATOM   10714 C  CB    . LYS   D 3  73  ? -37.080 48.031  -26.669  1.00 42.34  ? 75  LYS   E CB    1 
ATOM   10715 C  CG    . LYS   D 3  73  ? -36.492 47.455  -28.000  1.00 47.01  ? 75  LYS   E CG    1 
ATOM   10716 C  CD    . LYS   D 3  73  ? -35.561 46.245  -27.772  1.00 45.31  ? 75  LYS   E CD    1 
ATOM   10717 C  CE    . LYS   D 3  73  ? -34.666 45.883  -28.994  1.00 58.66  ? 75  LYS   E CE    1 
ATOM   10718 N  NZ    . LYS   D 3  73  ? -33.419 45.063  -28.641  1.00 37.35  ? 75  LYS   E NZ    1 
ATOM   10719 N  N     . ARG   D 3  74  ? -39.546 48.643  -24.446  1.00 35.35  ? 76  ARG   E N     1 
ATOM   10720 C  CA    . ARG   D 3  74  ? -39.942 48.987  -23.081  1.00 46.64  ? 76  ARG   E CA    1 
ATOM   10721 C  C     . ARG   D 3  74  ? -40.626 47.827  -22.373  1.00 44.18  ? 76  ARG   E C     1 
ATOM   10722 O  O     . ARG   D 3  74  ? -40.500 47.690  -21.151  1.00 43.14  ? 76  ARG   E O     1 
ATOM   10723 C  CB    . ARG   D 3  74  ? -40.896 50.177  -23.065  1.00 41.70  ? 76  ARG   E CB    1 
ATOM   10724 C  CG    . ARG   D 3  74  ? -40.264 51.496  -23.355  1.00 46.11  ? 76  ARG   E CG    1 
ATOM   10725 C  CD    . ARG   D 3  74  ? -38.883 51.647  -22.743  1.00 47.99  ? 76  ARG   E CD    1 
ATOM   10726 N  NE    . ARG   D 3  74  ? -38.191 52.672  -23.507  1.00 54.84  ? 76  ARG   E NE    1 
ATOM   10727 C  CZ    . ARG   D 3  74  ? -37.162 52.462  -24.313  1.00 48.73  ? 76  ARG   E CZ    1 
ATOM   10728 N  NH1   . ARG   D 3  74  ? -36.459 51.335  -24.270  1.00 38.80  ? 76  ARG   E NH1   1 
ATOM   10729 N  NH2   . ARG   D 3  74  ? -36.833 53.407  -25.186  1.00 48.36  ? 76  ARG   E NH2   1 
ATOM   10730 N  N     . GLU   D 3  75  ? -41.380 47.018  -23.119  1.00 44.28  ? 77  GLU   E N     1 
ATOM   10731 C  CA    . GLU   D 3  75  ? -42.142 45.915  -22.555  1.00 45.59  ? 77  GLU   E CA    1 
ATOM   10732 C  C     . GLU   D 3  75  ? -41.225 44.749  -22.211  1.00 44.09  ? 77  GLU   E C     1 
ATOM   10733 O  O     . GLU   D 3  75  ? -41.383 44.104  -21.166  1.00 47.35  ? 77  GLU   E O     1 
ATOM   10734 C  CB    . GLU   D 3  75  ? -43.234 45.491  -23.546  1.00 46.98  ? 77  GLU   E CB    1 
ATOM   10735 C  CG    . GLU   D 3  75  ? -44.401 44.731  -22.935  1.00 75.21  ? 77  GLU   E CG    1 
ATOM   10736 C  CD    . GLU   D 3  75  ? -45.211 45.576  -21.939  1.00 90.18  ? 77  GLU   E CD    1 
ATOM   10737 O  OE1   . GLU   D 3  75  ? -45.302 46.817  -22.119  1.00 81.55  ? 77  GLU   E OE1   1 
ATOM   10738 O  OE2   . GLU   D 3  75  ? -45.756 44.993  -20.971  1.00 79.23  ? 77  GLU   E OE2   1 
ATOM   10739 N  N     . HIS   D 3  76  ? -40.253 44.478  -23.073  1.00 36.93  ? 78  HIS   E N     1 
ATOM   10740 C  CA    . HIS   D 3  76  ? -39.290 43.428  -22.795  1.00 34.96  ? 78  HIS   E CA    1 
ATOM   10741 C  C     . HIS   D 3  76  ? -38.418 43.788  -21.602  1.00 38.35  ? 78  HIS   E C     1 
ATOM   10742 O  O     . HIS   D 3  76  ? -37.974 42.899  -20.872  1.00 38.45  ? 78  HIS   E O     1 
ATOM   10743 C  CB    . HIS   D 3  76  ? -38.447 43.175  -24.034  1.00 30.64  ? 78  HIS   E CB    1 
ATOM   10744 C  CG    . HIS   D 3  76  ? -37.287 42.277  -23.787  1.00 44.74  ? 78  HIS   E CG    1 
ATOM   10745 N  ND1   . HIS   D 3  76  ? -37.423 40.912  -23.650  1.00 51.08  ? 78  HIS   E ND1   1 
ATOM   10746 C  CD2   . HIS   D 3  76  ? -35.970 42.547  -23.620  1.00 37.73  ? 78  HIS   E CD2   1 
ATOM   10747 C  CE1   . HIS   D 3  76  ? -36.236 40.376  -23.422  1.00 46.05  ? 78  HIS   E CE1   1 
ATOM   10748 N  NE2   . HIS   D 3  76  ? -35.338 41.346  -23.397  1.00 45.51  ? 78  HIS   E NE2   1 
ATOM   10749 N  N     . GLU   D 3  77  ? -38.179 45.080  -21.379  1.00 32.20  ? 79  GLU   E N     1 
ATOM   10750 C  CA    . GLU   D 3  77  ? -37.514 45.519  -20.159  1.00 30.11  ? 79  GLU   E CA    1 
ATOM   10751 C  C     . GLU   D 3  77  ? -38.329 45.155  -18.925  1.00 38.33  ? 79  GLU   E C     1 
ATOM   10752 O  O     . GLU   D 3  77  ? -37.821 44.502  -18.009  1.00 39.12  ? 79  GLU   E O     1 
ATOM   10753 C  CB    . GLU   D 3  77  ? -37.251 47.022  -20.227  1.00 29.46  ? 79  GLU   E CB    1 
ATOM   10754 C  CG    . GLU   D 3  77  ? -36.051 47.334  -21.110  1.00 37.47  ? 79  GLU   E CG    1 
ATOM   10755 C  CD    . GLU   D 3  77  ? -36.064 48.698  -21.789  1.00 38.21  ? 79  GLU   E CD    1 
ATOM   10756 O  OE1   . GLU   D 3  77  ? -36.753 49.638  -21.324  1.00 40.89  ? 79  GLU   E OE1   1 
ATOM   10757 O  OE2   . GLU   D 3  77  ? -35.347 48.820  -22.807  1.00 43.99  ? 79  GLU   E OE2   1 
ATOM   10758 N  N     . ARG   D 3  78  ? -39.596 45.574  -18.879  1.00 39.83  ? 80  ARG   E N     1 
ATOM   10759 C  CA    . ARG   D 3  78  ? -40.462 45.202  -17.763  1.00 36.25  ? 80  ARG   E CA    1 
ATOM   10760 C  C     . ARG   D 3  78  ? -40.446 43.690  -17.542  1.00 39.09  ? 80  ARG   E C     1 
ATOM   10761 O  O     . ARG   D 3  78  ? -40.266 43.208  -16.418  1.00 36.58  ? 80  ARG   E O     1 
ATOM   10762 C  CB    . ARG   D 3  78  ? -41.893 45.687  -18.026  1.00 40.38  ? 80  ARG   E CB    1 
ATOM   10763 C  CG    . ARG   D 3  78  ? -42.176 47.156  -17.730  1.00 44.30  ? 80  ARG   E CG    1 
ATOM   10764 C  CD    . ARG   D 3  78  ? -43.477 47.287  -16.914  1.00 62.09  ? 80  ARG   E CD    1 
ATOM   10765 N  NE    . ARG   D 3  78  ? -43.729 48.629  -16.387  1.00 61.12  ? 80  ARG   E NE    1 
ATOM   10766 C  CZ    . ARG   D 3  78  ? -42.987 49.241  -15.469  1.00 62.85  ? 80  ARG   E CZ    1 
ATOM   10767 N  NH1   . ARG   D 3  78  ? -41.871 48.697  -14.998  1.00 59.96  ? 80  ARG   E NH1   1 
ATOM   10768 N  NH2   . ARG   D 3  78  ? -43.367 50.435  -15.017  1.00 71.15  ? 80  ARG   E NH2   1 
ATOM   10769 N  N     . GLU   D 3  79  ? -40.614 42.922  -18.614  1.00 30.90  ? 81  GLU   E N     1 
ATOM   10770 C  CA    . GLU   D 3  79  ? -40.696 41.478  -18.463  1.00 34.09  ? 81  GLU   E CA    1 
ATOM   10771 C  C     . GLU   D 3  79  ? -39.410 40.886  -17.885  1.00 42.08  ? 81  GLU   E C     1 
ATOM   10772 O  O     . GLU   D 3  79  ? -39.471 39.984  -17.038  1.00 42.69  ? 81  GLU   E O     1 
ATOM   10773 C  CB    . GLU   D 3  79  ? -41.046 40.832  -19.806  1.00 31.12  ? 81  GLU   E CB    1 
ATOM   10774 C  CG    . GLU   D 3  79  ? -42.417 41.249  -20.300  1.00 43.27  ? 81  GLU   E CG    1 
ATOM   10775 C  CD    . GLU   D 3  79  ? -42.844 40.496  -21.531  1.00 57.29  ? 81  GLU   E CD    1 
ATOM   10776 O  OE1   . GLU   D 3  79  ? -42.162 39.500  -21.860  1.00 56.99  ? 81  GLU   E OE1   1 
ATOM   10777 O  OE2   . GLU   D 3  79  ? -43.854 40.901  -22.161  1.00 61.78  ? 81  GLU   E OE2   1 
ATOM   10778 N  N     . VAL   D 3  80  ? -38.236 41.360  -18.339  1.00 36.52  ? 82  VAL   E N     1 
ATOM   10779 C  CA    . VAL   D 3  80  ? -36.967 40.793  -17.867  1.00 31.72  ? 82  VAL   E CA    1 
ATOM   10780 C  C     . VAL   D 3  80  ? -36.838 40.973  -16.355  1.00 31.88  ? 82  VAL   E C     1 
ATOM   10781 O  O     . VAL   D 3  80  ? -36.484 40.035  -15.636  1.00 25.66  ? 82  VAL   E O     1 
ATOM   10782 C  CB    . VAL   D 3  80  ? -35.769 41.419  -18.618  1.00 32.00  ? 82  VAL   E CB    1 
ATOM   10783 C  CG1   . VAL   D 3  80  ? -34.468 41.236  -17.854  1.00 23.71  ? 82  VAL   E CG1   1 
ATOM   10784 C  CG2   . VAL   D 3  80  ? -35.634 40.840  -20.003  1.00 36.10  ? 82  VAL   E CG2   1 
ATOM   10785 N  N     . ILE   D 3  81  ? -37.134 42.175  -15.847  1.00 22.88  ? 83  ILE   E N     1 
ATOM   10786 C  CA    . ILE   D 3  81  ? -36.973 42.383  -14.417  1.00 27.30  ? 83  ILE   E CA    1 
ATOM   10787 C  C     . ILE   D 3  81  ? -38.034 41.624  -13.624  1.00 33.03  ? 83  ILE   E C     1 
ATOM   10788 O  O     . ILE   D 3  81  ? -37.830 41.347  -12.437  1.00 34.35  ? 83  ILE   E O     1 
ATOM   10789 C  CB    . ILE   D 3  81  ? -36.971 43.875  -14.033  1.00 18.77  ? 83  ILE   E CB    1 
ATOM   10790 C  CG1   . ILE   D 3  81  ? -36.715 44.014  -12.528  1.00 35.69  ? 83  ILE   E CG1   1 
ATOM   10791 C  CG2   . ILE   D 3  81  ? -38.288 44.509  -14.374  1.00 24.88  ? 83  ILE   E CG2   1 
ATOM   10792 C  CD1   . ILE   D 3  81  ? -36.217 45.375  -12.075  1.00 32.23  ? 83  ILE   E CD1   1 
ATOM   10793 N  N     . GLN   D 3  82  ? -39.150 41.254  -14.247  1.00 27.56  ? 84  GLN   E N     1 
ATOM   10794 C  CA    . GLN   D 3  82  ? -40.149 40.486  -13.520  1.00 29.39  ? 84  GLN   E CA    1 
ATOM   10795 C  C     . GLN   D 3  82  ? -39.737 39.025  -13.436  1.00 35.32  ? 84  GLN   E C     1 
ATOM   10796 O  O     . GLN   D 3  82  ? -39.913 38.389  -12.390  1.00 46.26  ? 84  GLN   E O     1 
ATOM   10797 C  CB    . GLN   D 3  82  ? -41.537 40.612  -14.175  1.00 32.57  ? 84  GLN   E CB    1 
ATOM   10798 C  CG    . GLN   D 3  82  ? -42.213 41.993  -14.112  1.00 38.92  ? 84  GLN   E CG    1 
ATOM   10799 C  CD    . GLN   D 3  82  ? -43.597 42.025  -14.832  1.00 60.07  ? 84  GLN   E CD    1 
ATOM   10800 O  OE1   . GLN   D 3  82  ? -44.517 41.255  -14.508  1.00 68.31  ? 84  GLN   E OE1   1 
ATOM   10801 N  NE2   . GLN   D 3  82  ? -43.735 42.925  -15.801  1.00 40.12  ? 84  GLN   E NE2   1 
ATOM   10802 N  N     . LYS   D 3  83  ? -39.204 38.470  -14.526  1.00 29.03  ? 85  LYS   E N     1 
ATOM   10803 C  CA    . LYS   D 3  83  ? -38.604 37.144  -14.458  1.00 35.26  ? 85  LYS   E CA    1 
ATOM   10804 C  C     . LYS   D 3  83  ? -37.652 37.043  -13.263  1.00 38.95  ? 85  LYS   E C     1 
ATOM   10805 O  O     . LYS   D 3  83  ? -37.829 36.201  -12.380  1.00 44.70  ? 85  LYS   E O     1 
ATOM   10806 C  CB    . LYS   D 3  83  ? -37.878 36.828  -15.766  1.00 36.37  ? 85  LYS   E CB    1 
ATOM   10807 C  CG    . LYS   D 3  83  ? -38.430 35.622  -16.497  1.00 43.66  ? 85  LYS   E CG    1 
ATOM   10808 C  CD    . LYS   D 3  83  ? -37.366 34.944  -17.359  1.00 52.43  ? 85  LYS   E CD    1 
ATOM   10809 C  CE    . LYS   D 3  83  ? -36.427 34.046  -16.529  1.00 56.89  ? 85  LYS   E CE    1 
ATOM   10810 N  NZ    . LYS   D 3  83  ? -34.938 34.367  -16.672  1.00 46.85  ? 85  LYS   E NZ    1 
ATOM   10811 N  N     . ALA   D 3  84  ? -36.652 37.927  -13.207  1.00 26.89  ? 86  ALA   E N     1 
ATOM   10812 C  CA    . ALA   D 3  84  ? -35.662 37.884  -12.144  1.00 31.10  ? 86  ALA   E CA    1 
ATOM   10813 C  C     . ALA   D 3  84  ? -36.327 37.892  -10.764  1.00 37.46  ? 86  ALA   E C     1 
ATOM   10814 O  O     . ALA   D 3  84  ? -36.015 37.060  -9.904   1.00 38.03  ? 86  ALA   E O     1 
ATOM   10815 C  CB    . ALA   D 3  84  ? -34.676 39.051  -12.304  1.00 30.70  ? 86  ALA   E CB    1 
ATOM   10816 N  N     . ILE   D 3  85  ? -37.250 38.823  -10.535  1.00 33.10  ? 87  ILE   E N     1 
ATOM   10817 C  CA    . ILE   D 3  85  ? -37.974 38.839  -9.273   1.00 31.10  ? 87  ILE   E CA    1 
ATOM   10818 C  C     . ILE   D 3  85  ? -38.653 37.494  -9.051   1.00 40.45  ? 87  ILE   E C     1 
ATOM   10819 O  O     . ILE   D 3  85  ? -38.439 36.833  -8.025   1.00 39.50  ? 87  ILE   E O     1 
ATOM   10820 C  CB    . ILE   D 3  85  ? -38.974 40.011  -9.235   1.00 30.41  ? 87  ILE   E CB    1 
ATOM   10821 C  CG1   . ILE   D 3  85  ? -38.235 41.353  -9.292   1.00 33.25  ? 87  ILE   E CG1   1 
ATOM   10822 C  CG2   . ILE   D 3  85  ? -39.750 39.998  -7.957   1.00 23.34  ? 87  ILE   E CG2   1 
ATOM   10823 C  CD1   . ILE   D 3  85  ? -39.155 42.547  -9.380   1.00 26.07  ? 87  ILE   E CD1   1 
ATOM   10824 N  N     . GLU   D 3  86  ? -39.432 37.037  -10.043  1.00 36.00  ? 88  GLU   E N     1 
ATOM   10825 C  CA    . GLU   D 3  86  ? -40.193 35.798  -9.891   1.00 38.79  ? 88  GLU   E CA    1 
ATOM   10826 C  C     . GLU   D 3  86  ? -39.297 34.589  -9.690   1.00 44.16  ? 88  GLU   E C     1 
ATOM   10827 O  O     . GLU   D 3  86  ? -39.725 33.597  -9.092   1.00 50.69  ? 88  GLU   E O     1 
ATOM   10828 C  CB    . GLU   D 3  86  ? -41.081 35.553  -11.105  1.00 42.99  ? 88  GLU   E CB    1 
ATOM   10829 C  CG    . GLU   D 3  86  ? -42.111 34.448  -10.892  1.00 40.99  ? 88  GLU   E CG    1 
ATOM   10830 C  CD    . GLU   D 3  86  ? -43.200 34.833  -9.891   1.00 57.52  ? 88  GLU   E CD    1 
ATOM   10831 O  OE1   . GLU   D 3  86  ? -42.906 35.491  -8.865   1.00 53.05  ? 88  GLU   E OE1   1 
ATOM   10832 O  OE2   . GLU   D 3  86  ? -44.370 34.481  -10.138  1.00 72.19  ? 88  GLU   E OE2   1 
ATOM   10833 N  N     . GLU   D 3  87  ? -38.066 34.633  -10.191  1.00 42.04  ? 89  GLU   E N     1 
ATOM   10834 C  CA    . GLU   D 3  87  ? -37.195 33.483  -10.013  1.00 43.00  ? 89  GLU   E CA    1 
ATOM   10835 C  C     . GLU   D 3  87  ? -36.508 33.516  -8.656   1.00 40.11  ? 89  GLU   E C     1 
ATOM   10836 O  O     . GLU   D 3  87  ? -36.331 32.465  -8.032   1.00 45.78  ? 89  GLU   E O     1 
ATOM   10837 C  CB    . GLU   D 3  87  ? -36.194 33.396  -11.164  1.00 44.42  ? 89  GLU   E CB    1 
ATOM   10838 C  CG    . GLU   D 3  87  ? -36.787 32.714  -12.411  1.00 49.96  ? 89  GLU   E CG    1 
ATOM   10839 C  CD    . GLU   D 3  87  ? -35.878 32.807  -13.628  1.00 63.72  ? 89  GLU   E CD    1 
ATOM   10840 O  OE1   . GLU   D 3  87  ? -34.964 33.670  -13.618  1.00 69.55  ? 89  GLU   E OE1   1 
ATOM   10841 O  OE2   . GLU   D 3  87  ? -36.072 32.022  -14.591  1.00 55.42  ? 89  GLU   E OE2   1 
ATOM   10842 N  N     . ASN   D 3  88  ? -36.147 34.700  -8.160   1.00 37.20  ? 90  ASN   E N     1 
ATOM   10843 C  CA    . ASN   D 3  88  ? -35.700 34.783  -6.774   1.00 43.35  ? 90  ASN   E CA    1 
ATOM   10844 C  C     . ASN   D 3  88  ? -36.837 34.428  -5.808   1.00 41.20  ? 90  ASN   E C     1 
ATOM   10845 O  O     . ASN   D 3  88  ? -36.601 33.813  -4.764   1.00 39.95  ? 90  ASN   E O     1 
ATOM   10846 C  CB    . ASN   D 3  88  ? -35.128 36.177  -6.454   1.00 34.35  ? 90  ASN   E CB    1 
ATOM   10847 C  CG    . ASN   D 3  88  ? -34.619 36.288  -4.978   1.00 64.10  ? 90  ASN   E CG    1 
ATOM   10848 O  OD1   . ASN   D 3  88  ? -33.886 35.404  -4.489   1.00 59.11  ? 90  ASN   E OD1   1 
ATOM   10849 N  ND2   . ASN   D 3  88  ? -35.025 37.362  -4.271   1.00 51.49  ? 90  ASN   E ND2   1 
ATOM   10850 N  N     . ASN   D 3  89  ? -38.075 34.800  -6.140   1.00 31.40  ? 91  ASN   E N     1 
ATOM   10851 C  CA    . ASN   D 3  89  ? -39.178 34.521  -5.228   1.00 40.55  ? 91  ASN   E CA    1 
ATOM   10852 C  C     . ASN   D 3  89  ? -39.473 33.029  -5.150   1.00 44.01  ? 91  ASN   E C     1 
ATOM   10853 O  O     . ASN   D 3  89  ? -39.753 32.501  -4.063   1.00 44.15  ? 91  ASN   E O     1 
ATOM   10854 C  CB    . ASN   D 3  89  ? -40.428 35.294  -5.647   1.00 35.70  ? 91  ASN   E CB    1 
ATOM   10855 C  CG    . ASN   D 3  89  ? -40.400 36.729  -5.171   1.00 42.65  ? 91  ASN   E CG    1 
ATOM   10856 O  OD1   . ASN   D 3  89  ? -39.457 37.150  -4.486   1.00 33.08  ? 91  ASN   E OD1   1 
ATOM   10857 N  ND2   . ASN   D 3  89  ? -41.425 37.501  -5.548   1.00 48.10  ? 91  ASN   E ND2   1 
ATOM   10858 N  N     . ASN   D 3  90  ? -39.419 32.336  -6.290   1.00 39.21  ? 92  ASN   E N     1 
ATOM   10859 C  CA    . ASN   D 3  90  ? -39.706 30.912  -6.294   1.00 35.82  ? 92  ASN   E CA    1 
ATOM   10860 C  C     . ASN   D 3  90  ? -38.585 30.127  -5.627   1.00 41.01  ? 92  ASN   E C     1 
ATOM   10861 O  O     . ASN   D 3  90  ? -38.843 29.213  -4.838   1.00 47.48  ? 92  ASN   E O     1 
ATOM   10862 C  CB    . ASN   D 3  90  ? -39.931 30.435  -7.723   1.00 50.58  ? 92  ASN   E CB    1 
ATOM   10863 C  CG    . ASN   D 3  90  ? -40.700 29.141  -7.777   1.00 60.60  ? 92  ASN   E CG    1 
ATOM   10864 O  OD1   . ASN   D 3  90  ? -41.817 29.053  -7.260   1.00 63.87  ? 92  ASN   E OD1   1 
ATOM   10865 N  ND2   . ASN   D 3  90  ? -40.119 28.131  -8.409   1.00 61.42  ? 92  ASN   E ND2   1 
ATOM   10866 N  N     . PHE   D 3  91  ? -37.334 30.473  -5.924   1.00 38.07  ? 93  PHE   E N     1 
ATOM   10867 C  CA    . PHE   D 3  91  ? -36.222 29.840  -5.228   1.00 46.98  ? 93  PHE   E CA    1 
ATOM   10868 C  C     . PHE   D 3  91  ? -36.319 30.024  -3.707   1.00 44.88  ? 93  PHE   E C     1 
ATOM   10869 O  O     . PHE   D 3  91  ? -36.033 29.092  -2.946   1.00 44.63  ? 93  PHE   E O     1 
ATOM   10870 C  CB    . PHE   D 3  91  ? -34.897 30.383  -5.747   1.00 35.89  ? 93  PHE   E CB    1 
ATOM   10871 C  CG    . PHE   D 3  91  ? -33.752 30.044  -4.866   1.00 44.80  ? 93  PHE   E CG    1 
ATOM   10872 C  CD1   . PHE   D 3  91  ? -33.217 28.759  -4.880   1.00 37.84  ? 93  PHE   E CD1   1 
ATOM   10873 C  CD2   . PHE   D 3  91  ? -33.232 30.988  -3.991   1.00 44.65  ? 93  PHE   E CD2   1 
ATOM   10874 C  CE1   . PHE   D 3  91  ? -32.181 28.414  -4.047   1.00 35.06  ? 93  PHE   E CE1   1 
ATOM   10875 C  CE2   . PHE   D 3  91  ? -32.181 30.654  -3.157   1.00 46.74  ? 93  PHE   E CE2   1 
ATOM   10876 C  CZ    . PHE   D 3  91  ? -31.653 29.355  -3.185   1.00 38.85  ? 93  PHE   E CZ    1 
ATOM   10877 N  N     . ILE   D 3  92  ? -36.682 31.220  -3.240   1.00 38.80  ? 94  ILE   E N     1 
ATOM   10878 C  CA    . ILE   D 3  92  ? -36.945 31.393  -1.815   1.00 40.84  ? 94  ILE   E CA    1 
ATOM   10879 C  C     . ILE   D 3  92  ? -38.097 30.499  -1.374   1.00 43.21  ? 94  ILE   E C     1 
ATOM   10880 O  O     . ILE   D 3  92  ? -38.075 29.917  -0.282   1.00 45.07  ? 94  ILE   E O     1 
ATOM   10881 C  CB    . ILE   D 3  92  ? -37.242 32.866  -1.493   1.00 45.39  ? 94  ILE   E CB    1 
ATOM   10882 C  CG1   . ILE   D 3  92  ? -35.954 33.688  -1.492   1.00 41.13  ? 94  ILE   E CG1   1 
ATOM   10883 C  CG2   . ILE   D 3  92  ? -38.013 32.990  -0.162   1.00 35.22  ? 94  ILE   E CG2   1 
ATOM   10884 C  CD1   . ILE   D 3  92  ? -36.170 35.111  -0.983   1.00 50.99  ? 94  ILE   E CD1   1 
ATOM   10885 N  N     . LYS   D 3  93  ? -39.109 30.364  -2.225   1.00 38.25  ? 95  LYS   E N     1 
ATOM   10886 C  CA    . LYS   D 3  93  ? -40.340 29.689  -1.838   1.00 43.02  ? 95  LYS   E CA    1 
ATOM   10887 C  C     . LYS   D 3  93  ? -40.229 28.172  -1.915   1.00 45.41  ? 95  LYS   E C     1 
ATOM   10888 O  O     . LYS   D 3  93  ? -40.945 27.477  -1.191   1.00 45.09  ? 95  LYS   E O     1 
ATOM   10889 C  CB    . LYS   D 3  93  ? -41.496 30.185  -2.711   1.00 37.63  ? 95  LYS   E CB    1 
ATOM   10890 C  CG    . LYS   D 3  93  ? -42.662 29.233  -2.785   1.00 45.81  ? 95  LYS   E CG    1 
ATOM   10891 C  CD    . LYS   D 3  93  ? -43.779 29.790  -3.643   1.00 55.51  ? 95  LYS   E CD    1 
ATOM   10892 C  CE    . LYS   D 3  93  ? -44.799 28.719  -3.933   1.00 56.62  ? 95  LYS   E CE    1 
ATOM   10893 N  NZ    . LYS   D 3  93  ? -44.952 27.834  -2.747   1.00 61.28  ? 95  LYS   E NZ    1 
ATOM   10894 N  N     . MET   D 3  94  ? -39.377 27.638  -2.797   1.00 46.61  ? 96  MET   E N     1 
ATOM   10895 C  CA    . MET   D 3  94  ? -39.118 26.202  -2.783   1.00 43.30  ? 96  MET   E CA    1 
ATOM   10896 C  C     . MET   D 3  94  ? -38.221 25.825  -1.610   1.00 43.23  ? 96  MET   E C     1 
ATOM   10897 O  O     . MET   D 3  94  ? -38.431 24.800  -0.959   1.00 40.81  ? 96  MET   E O     1 
ATOM   10898 C  CB    . MET   D 3  94  ? -38.480 25.761  -4.103   1.00 62.34  ? 96  MET   E CB    1 
ATOM   10899 C  CG    . MET   D 3  94  ? -39.390 25.893  -5.327   1.00 61.36  ? 96  MET   E CG    1 
ATOM   10900 S  SD    . MET   D 3  94  ? -40.919 24.937  -5.171   1.00 85.15  ? 96  MET   E SD    1 
ATOM   10901 C  CE    . MET   D 3  94  ? -40.421 23.371  -5.902   1.00 61.08  ? 96  MET   E CE    1 
ATOM   10902 N  N     . ALA   D 3  95  ? -37.213 26.643  -1.325   1.00 45.96  ? 97  ALA   E N     1 
ATOM   10903 C  CA    . ALA   D 3  95  ? -36.376 26.381  -0.165   1.00 38.92  ? 97  ALA   E CA    1 
ATOM   10904 C  C     . ALA   D 3  95  ? -37.229 26.282  1.084    1.00 46.80  ? 97  ALA   E C     1 
ATOM   10905 O  O     . ALA   D 3  95  ? -37.114 25.321  1.856    1.00 38.96  ? 97  ALA   E O     1 
ATOM   10906 C  CB    . ALA   D 3  95  ? -35.322 27.474  -0.015   1.00 29.70  ? 97  ALA   E CB    1 
ATOM   10907 N  N     . LYS   D 3  96  ? -38.101 27.273  1.291    1.00 45.56  ? 98  LYS   E N     1 
ATOM   10908 C  CA    . LYS   D 3  96  ? -39.041 27.223  2.399    1.00 42.53  ? 98  LYS   E CA    1 
ATOM   10909 C  C     . LYS   D 3  96  ? -39.807 25.902  2.408    1.00 43.05  ? 98  LYS   E C     1 
ATOM   10910 O  O     . LYS   D 3  96  ? -39.885 25.221  3.434    1.00 38.23  ? 98  LYS   E O     1 
ATOM   10911 C  CB    . LYS   D 3  96  ? -40.000 28.409  2.312    1.00 40.67  ? 98  LYS   E CB    1 
ATOM   10912 C  CG    . LYS   D 3  96  ? -40.510 28.892  3.654    1.00 40.89  ? 98  LYS   E CG    1 
ATOM   10913 C  CD    . LYS   D 3  96  ? -40.840 30.366  3.582    1.00 43.70  ? 98  LYS   E CD    1 
ATOM   10914 C  CE    . LYS   D 3  96  ? -40.990 30.986  4.951    1.00 50.26  ? 98  LYS   E CE    1 
ATOM   10915 N  NZ    . LYS   D 3  96  ? -40.742 32.466  4.865    1.00 54.67  ? 98  LYS   E NZ    1 
ATOM   10916 N  N     . GLU   D 3  97  ? -40.364 25.508  1.265    1.00 38.59  ? 99  GLU   E N     1 
ATOM   10917 C  CA    . GLU   D 3  97  ? -41.200 24.314  1.268    1.00 39.37  ? 99  GLU   E CA    1 
ATOM   10918 C  C     . GLU   D 3  97  ? -40.371 23.070  1.544    1.00 44.99  ? 99  GLU   E C     1 
ATOM   10919 O  O     . GLU   D 3  97  ? -40.703 22.287  2.438    1.00 53.87  ? 99  GLU   E O     1 
ATOM   10920 C  CB    . GLU   D 3  97  ? -41.963 24.184  -0.048   1.00 38.38  ? 99  GLU   E CB    1 
ATOM   10921 C  CG    . GLU   D 3  97  ? -43.301 24.911  -0.023   1.00 47.53  ? 99  GLU   E CG    1 
ATOM   10922 C  CD    . GLU   D 3  97  ? -43.861 25.192  -1.424   1.00 71.96  ? 99  GLU   E CD    1 
ATOM   10923 O  OE1   . GLU   D 3  97  ? -43.432 24.526  -2.411   1.00 52.45  ? 99  GLU   E OE1   1 
ATOM   10924 O  OE2   . GLU   D 3  97  ? -44.732 26.095  -1.525   1.00 65.09  ? 99  GLU   E OE2   1 
ATOM   10925 N  N     . LYS   D 3  98  ? -39.281 22.880  0.792    1.00 43.34  ? 100 LYS   E N     1 
ATOM   10926 C  CA    . LYS   D 3  98  ? -38.395 21.740  0.998    1.00 46.28  ? 100 LYS   E CA    1 
ATOM   10927 C  C     . LYS   D 3  98  ? -37.872 21.690  2.437    1.00 45.87  ? 100 LYS   E C     1 
ATOM   10928 O  O     . LYS   D 3  98  ? -37.680 20.607  3.000    1.00 41.31  ? 100 LYS   E O     1 
ATOM   10929 C  CB    . LYS   D 3  98  ? -37.249 21.810  -0.025   1.00 43.54  ? 100 LYS   E CB    1 
ATOM   10930 C  CG    . LYS   D 3  98  ? -36.395 20.553  -0.163   1.00 50.79  ? 100 LYS   E CG    1 
ATOM   10931 C  CD    . LYS   D 3  98  ? -35.447 20.660  -1.374   1.00 69.30  ? 100 LYS   E CD    1 
ATOM   10932 C  CE    . LYS   D 3  98  ? -34.564 19.411  -1.533   1.00 75.34  ? 100 LYS   E CE    1 
ATOM   10933 N  NZ    . LYS   D 3  98  ? -33.975 19.276  -2.904   1.00 53.83  ? 100 LYS   E NZ    1 
ATOM   10934 N  N     . LEU   D 3  99  ? -37.676 22.841  3.063    1.00 42.53  ? 101 LEU   E N     1 
ATOM   10935 C  CA    . LEU   D 3  99  ? -37.270 22.838  4.457    1.00 41.97  ? 101 LEU   E CA    1 
ATOM   10936 C  C     . LEU   D 3  99  ? -38.382 22.372  5.389    1.00 44.35  ? 101 LEU   E C     1 
ATOM   10937 O  O     . LEU   D 3  99  ? -38.100 21.953  6.516    1.00 51.28  ? 101 LEU   E O     1 
ATOM   10938 C  CB    . LEU   D 3  99  ? -36.806 24.231  4.871    1.00 30.45  ? 101 LEU   E CB    1 
ATOM   10939 C  CG    . LEU   D 3  99  ? -35.747 24.154  5.969    1.00 43.05  ? 101 LEU   E CG    1 
ATOM   10940 C  CD1   . LEU   D 3  99  ? -34.913 22.865  5.820    1.00 38.76  ? 101 LEU   E CD1   1 
ATOM   10941 C  CD2   . LEU   D 3  99  ? -34.872 25.415  5.974    1.00 42.40  ? 101 LEU   E CD2   1 
ATOM   10942 N  N     . ALA   D 3  100 ? -39.633 22.448  4.966    1.00 45.21  ? 102 ALA   E N     1 
ATOM   10943 C  CA    . ALA   D 3  100 ? -40.736 22.121  5.853    1.00 46.70  ? 102 ALA   E CA    1 
ATOM   10944 C  C     . ALA   D 3  100 ? -41.225 20.687  5.658    1.00 48.86  ? 102 ALA   E C     1 
ATOM   10945 O  O     . ALA   D 3  100 ? -41.539 20.010  6.639    1.00 44.54  ? 102 ALA   E O     1 
ATOM   10946 C  CB    . ALA   D 3  100 ? -41.873 23.137  5.664    1.00 29.73  ? 102 ALA   E CB    1 
ATOM   10947 N  N     . GLN   D 3  101 ? -41.258 20.181  4.422    1.00 45.58  ? 103 GLN   E N     1 
ATOM   10948 C  CA    . GLN   D 3  101 ? -41.385 18.736  4.242    1.00 50.97  ? 103 GLN   E CA    1 
ATOM   10949 C  C     . GLN   D 3  101 ? -40.245 17.991  4.934    1.00 51.92  ? 103 GLN   E C     1 
ATOM   10950 O  O     . GLN   D 3  101 ? -40.437 16.864  5.405    1.00 54.61  ? 103 GLN   E O     1 
ATOM   10951 C  CB    . GLN   D 3  101 ? -41.437 18.366  2.752    1.00 35.92  ? 103 GLN   E CB    1 
ATOM   10952 C  CG    . GLN   D 3  101 ? -40.488 19.196  1.870    1.00 62.63  ? 103 GLN   E CG    1 
ATOM   10953 C  CD    . GLN   D 3  101 ? -39.777 18.404  0.764    1.00 67.16  ? 103 GLN   E CD    1 
ATOM   10954 O  OE1   . GLN   D 3  101 ? -38.923 17.550  1.042    1.00 70.33  ? 103 GLN   E OE1   1 
ATOM   10955 N  NE2   . GLN   D 3  101 ? -40.112 18.707  -0.497   1.00 57.45  ? 103 GLN   E NE2   1 
ATOM   10956 N  N     . LYS   D 3  102 ? -39.065 18.610  5.029    1.00 51.57  ? 104 LYS   E N     1 
ATOM   10957 C  CA    . LYS   D 3  102 ? -37.920 17.943  5.647    1.00 53.35  ? 104 LYS   E CA    1 
ATOM   10958 C  C     . LYS   D 3  102 ? -38.064 17.867  7.173    1.00 49.03  ? 104 LYS   E C     1 
ATOM   10959 O  O     . LYS   D 3  102 ? -37.726 16.845  7.780    1.00 40.27  ? 104 LYS   E O     1 
ATOM   10960 C  CB    . LYS   D 3  102 ? -36.620 18.660  5.251    1.00 50.97  ? 104 LYS   E CB    1 
ATOM   10961 C  CG    . LYS   D 3  102 ? -36.050 18.261  3.874    1.00 50.16  ? 104 LYS   E CG    1 
ATOM   10962 C  CD    . LYS   D 3  102 ? -34.772 19.056  3.479    1.00 51.27  ? 104 LYS   E CD    1 
ATOM   10963 C  CE    . LYS   D 3  102 ? -33.531 18.685  4.291    1.00 37.97  ? 104 LYS   E CE    1 
ATOM   10964 N  NZ    . LYS   D 3  102 ? -32.266 19.306  3.794    1.00 41.11  ? 104 LYS   E NZ    1 
ATOM   10965 N  N     . MET   D 3  103 ? -38.562 18.936  7.805    1.00 50.04  ? 105 MET   E N     1 
ATOM   10966 C  CA    . MET   D 3  103 ? -38.751 18.946  9.258    1.00 49.07  ? 105 MET   E CA    1 
ATOM   10967 C  C     . MET   D 3  103 ? -39.949 18.102  9.693    1.00 48.50  ? 105 MET   E C     1 
ATOM   10968 O  O     . MET   D 3  103 ? -39.938 17.548  10.800   1.00 48.79  ? 105 MET   E O     1 
ATOM   10969 C  CB    . MET   D 3  103 ? -38.904 20.386  9.774    1.00 33.11  ? 105 MET   E CB    1 
ATOM   10970 C  CG    . MET   D 3  103 ? -37.665 21.284  9.577    1.00 52.45  ? 105 MET   E CG    1 
ATOM   10971 S  SD    . MET   D 3  103 ? -35.984 20.588  9.878    1.00 67.55  ? 105 MET   E SD    1 
ATOM   10972 C  CE    . MET   D 3  103 ? -35.264 20.875  8.255    1.00 49.49  ? 105 MET   E CE    1 
ATOM   10973 N  N     . GLU   D 3  104 ? -40.977 17.983  8.851    1.00 43.92  ? 106 GLU   E N     1 
ATOM   10974 C  CA    . GLU   D 3  104 ? -42.126 17.151  9.188    1.00 41.98  ? 106 GLU   E CA    1 
ATOM   10975 C  C     . GLU   D 3  104 ? -41.789 15.670  9.061    1.00 50.41  ? 106 GLU   E C     1 
ATOM   10976 O  O     . GLU   D 3  104 ? -41.895 14.909  10.030   1.00 51.31  ? 106 GLU   E O     1 
ATOM   10977 C  CB    . GLU   D 3  104 ? -43.312 17.499  8.294    1.00 57.31  ? 106 GLU   E CB    1 
ATOM   10978 C  CG    . GLU   D 3  104 ? -43.693 18.963  8.296    1.00 74.98  ? 106 GLU   E CG    1 
ATOM   10979 C  CD    . GLU   D 3  104 ? -44.952 19.220  9.081    1.00 87.59  ? 106 GLU   E CD    1 
ATOM   10980 O  OE1   . GLU   D 3  104 ? -44.974 18.852  10.277   1.00 86.60  ? 106 GLU   E OE1   1 
ATOM   10981 O  OE2   . GLU   D 3  104 ? -45.918 19.772  8.497    1.00 88.84  ? 106 GLU   E OE2   1 
ATOM   10982 N  N     . SER   D 3  105 ? -41.413 15.232  7.859    1.00 51.50  ? 107 SER   E N     1 
ATOM   10983 C  CA    . SER   D 3  105 ? -40.992 13.848  7.689    1.00 51.80  ? 107 SER   E CA    1 
ATOM   10984 C  C     . SER   D 3  105 ? -40.007 13.445  8.785    1.00 50.45  ? 107 SER   E C     1 
ATOM   10985 O  O     . SER   D 3  105 ? -40.123 12.368  9.387    1.00 44.18  ? 107 SER   E O     1 
ATOM   10986 C  CB    . SER   D 3  105 ? -40.364 13.656  6.309    1.00 48.40  ? 107 SER   E CB    1 
ATOM   10987 O  OG    . SER   D 3  105 ? -39.029 14.145  6.312    1.00 58.59  ? 107 SER   E OG    1 
ATOM   10988 N  N     . ASN   D 3  106 ? -39.028 14.310  9.064    1.00 38.26  ? 108 ASN   E N     1 
ATOM   10989 C  CA    . ASN   D 3  106 ? -38.056 13.976  10.090   1.00 44.79  ? 108 ASN   E CA    1 
ATOM   10990 C  C     . ASN   D 3  106 ? -38.742 13.789  11.437   1.00 50.19  ? 108 ASN   E C     1 
ATOM   10991 O  O     . ASN   D 3  106 ? -38.436 12.841  12.169   1.00 46.53  ? 108 ASN   E O     1 
ATOM   10992 C  CB    . ASN   D 3  106 ? -36.971 15.052  10.165   1.00 46.70  ? 108 ASN   E CB    1 
ATOM   10993 C  CG    . ASN   D 3  106 ? -35.960 14.783  11.268   1.00 54.89  ? 108 ASN   E CG    1 
ATOM   10994 O  OD1   . ASN   D 3  106 ? -36.035 15.354  12.374   1.00 53.14  ? 108 ASN   E OD1   1 
ATOM   10995 N  ND2   . ASN   D 3  106 ? -35.005 13.902  10.978   1.00 54.43  ? 108 ASN   E ND2   1 
ATOM   10996 N  N     . LYS   D 3  107 ? -39.708 14.651  11.762   1.00 49.82  ? 109 LYS   E N     1 
ATOM   10997 C  CA    . LYS   D 3  107 ? -40.305 14.605  13.093   1.00 47.20  ? 109 LYS   E CA    1 
ATOM   10998 C  C     . LYS   D 3  107 ? -41.175 13.373  13.271   1.00 44.12  ? 109 LYS   E C     1 
ATOM   10999 O  O     . LYS   D 3  107 ? -41.094 12.698  14.303   1.00 52.60  ? 109 LYS   E O     1 
ATOM   11000 C  CB    . LYS   D 3  107 ? -41.108 15.867  13.370   1.00 46.62  ? 109 LYS   E CB    1 
ATOM   11001 C  CG    . LYS   D 3  107 ? -41.712 15.876  14.757   1.00 49.44  ? 109 LYS   E CG    1 
ATOM   11002 C  CD    . LYS   D 3  107 ? -42.236 17.261  15.124   1.00 56.38  ? 109 LYS   E CD    1 
ATOM   11003 C  CE    . LYS   D 3  107 ? -43.508 17.179  15.935   1.00 41.44  ? 109 LYS   E CE    1 
ATOM   11004 N  NZ    . LYS   D 3  107 ? -43.951 18.526  16.336   1.00 44.94  ? 109 LYS   E NZ    1 
ATOM   11005 N  N     . GLU   D 3  108 ? -42.017 13.063  12.281   1.00 45.91  ? 110 GLU   E N     1 
ATOM   11006 C  CA    . GLU   D 3  108 ? -42.822 11.846  12.352   1.00 46.25  ? 110 GLU   E CA    1 
ATOM   11007 C  C     . GLU   D 3  108 ? -41.940 10.611  12.448   1.00 55.20  ? 110 GLU   E C     1 
ATOM   11008 O  O     . GLU   D 3  108 ? -42.279 9.644   13.143   1.00 61.57  ? 110 GLU   E O     1 
ATOM   11009 C  CB    . GLU   D 3  108 ? -43.728 11.728  11.137   1.00 33.55  ? 110 GLU   E CB    1 
ATOM   11010 C  CG    . GLU   D 3  108 ? -43.933 13.034  10.426   1.00 51.57  ? 110 GLU   E CG    1 
ATOM   11011 C  CD    . GLU   D 3  108 ? -45.067 12.981  9.440    1.00 66.26  ? 110 GLU   E CD    1 
ATOM   11012 O  OE1   . GLU   D 3  108 ? -45.167 11.979  8.689    1.00 62.14  ? 110 GLU   E OE1   1 
ATOM   11013 O  OE2   . GLU   D 3  108 ? -45.867 13.945  9.431    1.00 73.43  ? 110 GLU   E OE2   1 
ATOM   11014 N  N     . ASN   D 3  109 ? -40.801 10.629  11.756   1.00 49.21  ? 111 ASN   E N     1 
ATOM   11015 C  CA    . ASN   D 3  109 ? -39.945 9.452   11.717   1.00 47.04  ? 111 ASN   E CA    1 
ATOM   11016 C  C     . ASN   D 3  109 ? -39.286 9.204   13.069   1.00 46.71  ? 111 ASN   E C     1 
ATOM   11017 O  O     . ASN   D 3  109 ? -39.319 8.085   13.585   1.00 43.06  ? 111 ASN   E O     1 
ATOM   11018 C  CB    . ASN   D 3  109 ? -38.906 9.615   10.609   1.00 36.65  ? 111 ASN   E CB    1 
ATOM   11019 C  CG    . ASN   D 3  109 ? -39.463 9.275   9.257    1.00 33.79  ? 111 ASN   E CG    1 
ATOM   11020 O  OD1   . ASN   D 3  109 ? -40.499 8.629   9.172    1.00 40.43  ? 111 ASN   E OD1   1 
ATOM   11021 N  ND2   . ASN   D 3  109 ? -38.766 9.673   8.184    1.00 37.73  ? 111 ASN   E ND2   1 
ATOM   11022 N  N     . ARG   D 3  110 ? -38.696 10.245  13.664   1.00 46.46  ? 112 ARG   E N     1 
ATOM   11023 C  CA    . ARG   D 3  110 ? -37.966 10.081  14.916   1.00 42.73  ? 112 ARG   E CA    1 
ATOM   11024 C  C     . ARG   D 3  110 ? -38.896 9.724   16.067   1.00 56.11  ? 112 ARG   E C     1 
ATOM   11025 O  O     . ARG   D 3  110 ? -38.532 8.930   16.947   1.00 55.73  ? 112 ARG   E O     1 
ATOM   11026 C  CB    . ARG   D 3  110 ? -37.196 11.356  15.254   1.00 42.68  ? 112 ARG   E CB    1 
ATOM   11027 C  CG    . ARG   D 3  110 ? -36.412 11.203  16.556   1.00 49.17  ? 112 ARG   E CG    1 
ATOM   11028 C  CD    . ARG   D 3  110 ? -35.650 12.440  16.959   1.00 38.22  ? 112 ARG   E CD    1 
ATOM   11029 N  NE    . ARG   D 3  110 ? -34.591 12.069  17.883   1.00 48.94  ? 112 ARG   E NE    1 
ATOM   11030 C  CZ    . ARG   D 3  110 ? -34.654 12.214  19.200   1.00 63.39  ? 112 ARG   E CZ    1 
ATOM   11031 N  NH1   . ARG   D 3  110 ? -35.686 12.805  19.784   1.00 57.74  ? 112 ARG   E NH1   1 
ATOM   11032 N  NH2   . ARG   D 3  110 ? -33.655 11.753  19.950   1.00 56.48  ? 112 ARG   E NH2   1 
ATOM   11033 N  N     . GLU   D 3  111 ? -40.083 10.329  16.098   1.00 53.12  ? 113 GLU   E N     1 
ATOM   11034 C  CA    . GLU   D 3  111 ? -41.061 9.975   17.117   1.00 49.72  ? 113 GLU   E CA    1 
ATOM   11035 C  C     . GLU   D 3  111 ? -41.584 8.555   16.912   1.00 53.93  ? 113 GLU   E C     1 
ATOM   11036 O  O     . GLU   D 3  111 ? -41.741 7.808   17.883   1.00 60.18  ? 113 GLU   E O     1 
ATOM   11037 C  CB    . GLU   D 3  111 ? -42.194 11.001  17.118   1.00 58.48  ? 113 GLU   E CB    1 
ATOM   11038 C  CG    . GLU   D 3  111 ? -41.720 12.407  17.539   1.00 61.13  ? 113 GLU   E CG    1 
ATOM   11039 C  CD    . GLU   D 3  111 ? -42.809 13.487  17.473   1.00 72.70  ? 113 GLU   E CD    1 
ATOM   11040 O  OE1   . GLU   D 3  111 ? -43.951 13.184  17.051   1.00 59.66  ? 113 GLU   E OE1   1 
ATOM   11041 O  OE2   . GLU   D 3  111 ? -42.515 14.649  17.850   1.00 73.21  ? 113 GLU   E OE2   1 
ATOM   11042 N  N     . ALA   D 3  112 ? -41.828 8.146   15.663   1.00 53.79  ? 114 ALA   E N     1 
ATOM   11043 C  CA    . ALA   D 3  112 ? -42.259 6.769   15.416   1.00 58.40  ? 114 ALA   E CA    1 
ATOM   11044 C  C     . ALA   D 3  112 ? -41.195 5.768   15.874   1.00 57.12  ? 114 ALA   E C     1 
ATOM   11045 O  O     . ALA   D 3  112 ? -41.512 4.772   16.536   1.00 52.22  ? 114 ALA   E O     1 
ATOM   11046 C  CB    . ALA   D 3  112 ? -42.609 6.565   13.933   1.00 36.65  ? 114 ALA   E CB    1 
ATOM   11047 N  N     . HIS   D 3  113 ? -39.920 6.021   15.539   1.00 53.68  ? 115 HIS   E N     1 
ATOM   11048 C  CA    . HIS   D 3  113 ? -38.843 5.141   15.992   1.00 49.93  ? 115 HIS   E CA    1 
ATOM   11049 C  C     . HIS   D 3  113 ? -38.750 5.117   17.510   1.00 52.26  ? 115 HIS   E C     1 
ATOM   11050 O  O     . HIS   D 3  113 ? -38.432 4.079   18.096   1.00 49.45  ? 115 HIS   E O     1 
ATOM   11051 C  CB    . HIS   D 3  113 ? -37.505 5.571   15.385   1.00 50.58  ? 115 HIS   E CB    1 
ATOM   11052 C  CG    . HIS   D 3  113 ? -36.300 5.045   16.120   1.00 63.11  ? 115 HIS   E CG    1 
ATOM   11053 N  ND1   . HIS   D 3  113 ? -35.760 5.675   17.224   1.00 53.82  ? 115 HIS   E ND1   1 
ATOM   11054 C  CD2   . HIS   D 3  113 ? -35.516 3.958   15.894   1.00 63.62  ? 115 HIS   E CD2   1 
ATOM   11055 C  CE1   . HIS   D 3  113 ? -34.709 4.995   17.655   1.00 52.49  ? 115 HIS   E CE1   1 
ATOM   11056 N  NE2   . HIS   D 3  113 ? -34.542 3.946   16.867   1.00 53.72  ? 115 HIS   E NE2   1 
ATOM   11057 N  N     . LEU   D 3  114 ? -39.025 6.249   18.160   1.00 58.66  ? 116 LEU   E N     1 
ATOM   11058 C  CA    . LEU   D 3  114 ? -39.116 6.280   19.617   1.00 57.08  ? 116 LEU   E CA    1 
ATOM   11059 C  C     . LEU   D 3  114 ? -40.336 5.497   20.116   1.00 55.48  ? 116 LEU   E C     1 
ATOM   11060 O  O     . LEU   D 3  114 ? -40.232 4.707   21.061   1.00 55.24  ? 116 LEU   E O     1 
ATOM   11061 C  CB    . LEU   D 3  114 ? -39.161 7.739   20.100   1.00 51.71  ? 116 LEU   E CB    1 
ATOM   11062 C  CG    . LEU   D 3  114 ? -38.913 8.025   21.587   1.00 63.29  ? 116 LEU   E CG    1 
ATOM   11063 C  CD1   . LEU   D 3  114 ? -37.570 8.732   21.779   1.00 59.18  ? 116 LEU   E CD1   1 
ATOM   11064 C  CD2   . LEU   D 3  114 ? -40.061 8.820   22.233   1.00 59.69  ? 116 LEU   E CD2   1 
ATOM   11065 N  N     . ALA   D 3  115 ? -41.505 5.712   19.498   1.00 46.16  ? 117 ALA   E N     1 
ATOM   11066 C  CA    . ALA   D 3  115 ? -42.719 5.028   19.939   1.00 43.81  ? 117 ALA   E CA    1 
ATOM   11067 C  C     . ALA   D 3  115 ? -42.548 3.521   19.886   1.00 54.74  ? 117 ALA   E C     1 
ATOM   11068 O  O     . ALA   D 3  115 ? -42.973 2.805   20.804   1.00 63.71  ? 117 ALA   E O     1 
ATOM   11069 C  CB    . ALA   D 3  115 ? -43.917 5.444   19.080   1.00 39.45  ? 117 ALA   E CB    1 
ATOM   11070 N  N     . ALA   D 3  116 ? -41.936 3.018   18.813   1.00 41.44  ? 118 ALA   E N     1 
ATOM   11071 C  CA    . ALA   D 3  116 ? -41.719 1.584   18.700   1.00 46.65  ? 118 ALA   E CA    1 
ATOM   11072 C  C     . ALA   D 3  116 ? -40.942 1.063   19.899   1.00 49.45  ? 118 ALA   E C     1 
ATOM   11073 O  O     . ALA   D 3  116 ? -41.346 0.081   20.531   1.00 58.11  ? 118 ALA   E O     1 
ATOM   11074 C  CB    . ALA   D 3  116 ? -40.993 1.265   17.391   1.00 41.95  ? 118 ALA   E CB    1 
ATOM   11075 N  N     . MET   D 3  117 ? -39.841 1.733   20.253   1.00 40.96  ? 119 MET   E N     1 
ATOM   11076 C  CA    . MET   D 3  117 ? -38.967 1.215   21.300   1.00 52.00  ? 119 MET   E CA    1 
ATOM   11077 C  C     . MET   D 3  117 ? -39.650 1.274   22.663   1.00 67.84  ? 119 MET   E C     1 
ATOM   11078 O  O     . MET   D 3  117 ? -39.445 0.385   23.502   1.00 65.82  ? 119 MET   E O     1 
ATOM   11079 C  CB    . MET   D 3  117 ? -37.627 1.972   21.320   1.00 47.43  ? 119 MET   E CB    1 
ATOM   11080 C  CG    . MET   D 3  117 ? -37.437 2.935   22.516   1.00 52.64  ? 119 MET   E CG    1 
ATOM   11081 S  SD    . MET   D 3  117 ? -35.741 3.567   22.715   1.00 68.46  ? 119 MET   E SD    1 
ATOM   11082 C  CE    . MET   D 3  117 ? -35.481 4.312   21.101   1.00 49.38  ? 119 MET   E CE    1 
ATOM   11083 N  N     . LEU   D 3  118 ? -40.465 2.307   22.909   1.00 59.95  ? 120 LEU   E N     1 
ATOM   11084 C  CA    . LEU   D 3  118 ? -41.228 2.314   24.152   1.00 63.73  ? 120 LEU   E CA    1 
ATOM   11085 C  C     . LEU   D 3  118 ? -42.321 1.251   24.121   1.00 65.53  ? 120 LEU   E C     1 
ATOM   11086 O  O     . LEU   D 3  118 ? -42.603 0.615   25.144   1.00 58.83  ? 120 LEU   E O     1 
ATOM   11087 C  CB    . LEU   D 3  118 ? -41.809 3.701   24.426   1.00 59.77  ? 120 LEU   E CB    1 
ATOM   11088 C  CG    . LEU   D 3  118 ? -40.898 4.621   25.249   1.00 58.90  ? 120 LEU   E CG    1 
ATOM   11089 C  CD1   . LEU   D 3  118 ? -39.606 4.869   24.500   1.00 66.55  ? 120 LEU   E CD1   1 
ATOM   11090 C  CD2   . LEU   D 3  118 ? -41.578 5.944   25.594   1.00 64.27  ? 120 LEU   E CD2   1 
ATOM   11091 N  N     . GLU   D 3  119 ? -42.919 1.012   22.948   1.00 58.65  ? 121 GLU   E N     1 
ATOM   11092 C  CA    . GLU   D 3  119 ? -43.954 -0.016  22.864   1.00 66.99  ? 121 GLU   E CA    1 
ATOM   11093 C  C     . GLU   D 3  119 ? -43.383 -1.398  23.148   1.00 69.38  ? 121 GLU   E C     1 
ATOM   11094 O  O     . GLU   D 3  119 ? -43.999 -2.203  23.858   1.00 69.81  ? 121 GLU   E O     1 
ATOM   11095 C  CB    . GLU   D 3  119 ? -44.632 0.003   21.494   1.00 59.86  ? 121 GLU   E CB    1 
ATOM   11096 C  CG    . GLU   D 3  119 ? -45.225 -1.343  21.130   1.00 69.54  ? 121 GLU   E CG    1 
ATOM   11097 C  CD    . GLU   D 3  119 ? -46.432 -1.239  20.228   1.00 79.87  ? 121 GLU   E CD    1 
ATOM   11098 O  OE1   . GLU   D 3  119 ? -47.265 -0.331  20.447   1.00 89.69  ? 121 GLU   E OE1   1 
ATOM   11099 O  OE2   . GLU   D 3  119 ? -46.547 -2.071  19.300   1.00 72.32  ? 121 GLU   E OE2   1 
ATOM   11100 N  N     . ARG   D 3  120 ? -42.210 -1.703  22.595   1.00 66.11  ? 122 ARG   E N     1 
ATOM   11101 C  CA    . ARG   D 3  120 ? -41.625 -3.011  22.849   1.00 66.42  ? 122 ARG   E CA    1 
ATOM   11102 C  C     . ARG   D 3  120 ? -41.302 -3.180  24.326   1.00 64.93  ? 122 ARG   E C     1 
ATOM   11103 O  O     . ARG   D 3  120 ? -41.582 -4.232  24.909   1.00 67.05  ? 122 ARG   E O     1 
ATOM   11104 C  CB    . ARG   D 3  120 ? -40.379 -3.214  21.988   1.00 63.47  ? 122 ARG   E CB    1 
ATOM   11105 C  CG    . ARG   D 3  120 ? -40.488 -4.406  21.065   1.00 69.07  ? 122 ARG   E CG    1 
ATOM   11106 C  CD    . ARG   D 3  120 ? -39.127 -4.987  20.691   1.00 81.94  ? 122 ARG   E CD    1 
ATOM   11107 N  NE    . ARG   D 3  120 ? -39.287 -6.230  19.940   1.00 102.74 ? 122 ARG   E NE    1 
ATOM   11108 C  CZ    . ARG   D 3  120 ? -38.292 -7.018  19.552   1.00 104.17 ? 122 ARG   E CZ    1 
ATOM   11109 N  NH1   . ARG   D 3  120 ? -37.030 -6.730  19.833   1.00 99.38  ? 122 ARG   E NH1   1 
ATOM   11110 N  NH2   . ARG   D 3  120 ? -38.570 -8.127  18.867   1.00 99.07  ? 122 ARG   E NH2   1 
ATOM   11111 N  N     . LEU   D 3  121 ? -40.723 -2.145  24.949   1.00 64.63  ? 123 LEU   E N     1 
ATOM   11112 C  CA    . LEU   D 3  121 ? -40.438 -2.173  26.382   1.00 65.54  ? 123 LEU   E CA    1 
ATOM   11113 C  C     . LEU   D 3  121 ? -41.681 -2.514  27.189   1.00 66.99  ? 123 LEU   E C     1 
ATOM   11114 O  O     . LEU   D 3  121 ? -41.662 -3.408  28.042   1.00 64.89  ? 123 LEU   E O     1 
ATOM   11115 C  CB    . LEU   D 3  121 ? -39.880 -0.824  26.838   1.00 60.66  ? 123 LEU   E CB    1 
ATOM   11116 C  CG    . LEU   D 3  121 ? -38.567 -0.414  26.195   1.00 52.97  ? 123 LEU   E CG    1 
ATOM   11117 C  CD1   . LEU   D 3  121 ? -38.056 0.859   26.816   1.00 53.01  ? 123 LEU   E CD1   1 
ATOM   11118 C  CD2   . LEU   D 3  121 ? -37.587 -1.533  26.373   1.00 51.02  ? 123 LEU   E CD2   1 
ATOM   11119 N  N     . GLN   D 3  122 ? -42.777 -1.801  26.935   1.00 68.52  ? 124 GLN   E N     1 
ATOM   11120 C  CA    . GLN   D 3  122 ? -43.995 -2.023  27.702   1.00 69.56  ? 124 GLN   E CA    1 
ATOM   11121 C  C     . GLN   D 3  122 ? -44.523 -3.446  27.553   1.00 69.01  ? 124 GLN   E C     1 
ATOM   11122 O  O     . GLN   D 3  122 ? -45.240 -3.924  28.438   1.00 71.49  ? 124 GLN   E O     1 
ATOM   11123 C  CB    . GLN   D 3  122 ? -45.039 -0.994  27.284   1.00 65.89  ? 124 GLN   E CB    1 
ATOM   11124 C  CG    . GLN   D 3  122 ? -44.628 0.430   27.625   1.00 63.23  ? 124 GLN   E CG    1 
ATOM   11125 C  CD    . GLN   D 3  122 ? -45.223 1.459   26.676   1.00 69.66  ? 124 GLN   E CD    1 
ATOM   11126 O  OE1   . GLN   D 3  122 ? -45.930 1.116   25.723   1.00 69.43  ? 124 GLN   E OE1   1 
ATOM   11127 N  NE2   . GLN   D 3  122 ? -44.929 2.730   26.928   1.00 72.99  ? 124 GLN   E NE2   1 
ATOM   11128 N  N     . GLU   D 3  123 ? -44.186 -4.138  26.460   1.00 76.30  ? 125 GLU   E N     1 
ATOM   11129 C  CA    . GLU   D 3  123 ? -44.498 -5.558  26.371   1.00 69.99  ? 125 GLU   E CA    1 
ATOM   11130 C  C     . GLU   D 3  123 ? -43.550 -6.398  27.216   1.00 72.61  ? 125 GLU   E C     1 
ATOM   11131 O  O     . GLU   D 3  123 ? -43.954 -7.449  27.722   1.00 80.50  ? 125 GLU   E O     1 
ATOM   11132 C  CB    . GLU   D 3  123 ? -44.482 -6.020  24.919   1.00 56.95  ? 125 GLU   E CB    1 
ATOM   11133 C  CG    . GLU   D 3  123 ? -45.712 -5.585  24.156   1.00 76.65  ? 125 GLU   E CG    1 
ATOM   11134 C  CD    . GLU   D 3  123 ? -46.998 -6.087  24.793   1.00 91.56  ? 125 GLU   E CD    1 
ATOM   11135 O  OE1   . GLU   D 3  123 ? -46.914 -6.728  25.862   1.00 98.20  ? 125 GLU   E OE1   1 
ATOM   11136 O  OE2   . GLU   D 3  123 ? -48.093 -5.850  24.229   1.00 90.10  ? 125 GLU   E OE2   1 
ATOM   11137 N  N     . LYS   D 3  124 ? -42.299 -5.965  27.392   1.00 66.85  ? 126 LYS   E N     1 
ATOM   11138 C  CA    . LYS   D 3  124 ? -41.510 -6.514  28.491   1.00 77.91  ? 126 LYS   E CA    1 
ATOM   11139 C  C     . LYS   D 3  124 ? -42.331 -6.505  29.777   1.00 72.81  ? 126 LYS   E C     1 
ATOM   11140 O  O     . LYS   D 3  124 ? -42.277 -7.453  30.569   1.00 75.10  ? 126 LYS   E O     1 
ATOM   11141 C  CB    . LYS   D 3  124 ? -40.205 -5.721  28.681   1.00 73.08  ? 126 LYS   E CB    1 
ATOM   11142 C  CG    . LYS   D 3  124 ? -39.088 -5.992  27.669   1.00 64.42  ? 126 LYS   E CG    1 
ATOM   11143 C  CD    . LYS   D 3  124 ? -38.341 -7.302  27.950   1.00 70.21  ? 126 LYS   E CD    1 
ATOM   11144 C  CE    . LYS   D 3  124 ? -39.104 -8.509  27.390   1.00 73.20  ? 126 LYS   E CE    1 
ATOM   11145 N  NZ    . LYS   D 3  124 ? -38.750 -9.801  28.060   1.00 78.48  ? 126 LYS   E NZ    1 
ATOM   11146 N  N     . ASP   D 3  125 ? -43.113 -5.439  29.990   1.00 66.21  ? 127 ASP   E N     1 
ATOM   11147 C  CA    . ASP   D 3  125 ? -43.921 -5.323  31.200   1.00 72.38  ? 127 ASP   E CA    1 
ATOM   11148 C  C     . ASP   D 3  125 ? -45.079 -6.315  31.177   1.00 73.46  ? 127 ASP   E C     1 
ATOM   11149 O  O     . ASP   D 3  125 ? -45.276 -7.079  32.131   1.00 66.94  ? 127 ASP   E O     1 
ATOM   11150 C  CB    . ASP   D 3  125 ? -44.437 -3.885  31.361   1.00 68.78  ? 127 ASP   E CB    1 
ATOM   11151 C  CG    . ASP   D 3  125 ? -43.353 -2.909  31.823   1.00 70.92  ? 127 ASP   E CG    1 
ATOM   11152 O  OD1   . ASP   D 3  125 ? -42.232 -3.355  32.150   1.00 72.53  ? 127 ASP   E OD1   1 
ATOM   11153 O  OD2   . ASP   D 3  125 ? -43.622 -1.687  31.864   1.00 67.75  ? 127 ASP   E OD2   1 
ATOM   11154 N  N     . LYS   D 3  126 ? -45.857 -6.325  30.092   1.00 73.12  ? 128 LYS   E N     1 
ATOM   11155 C  CA    . LYS   D 3  126 ? -46.979 -7.251  30.013   1.00 72.21  ? 128 LYS   E CA    1 
ATOM   11156 C  C     . LYS   D 3  126 ? -46.508 -8.686  30.217   1.00 76.59  ? 128 LYS   E C     1 
ATOM   11157 O  O     . LYS   D 3  126 ? -47.051 -9.417  31.052   1.00 76.93  ? 128 LYS   E O     1 
ATOM   11158 C  CB    . LYS   D 3  126 ? -47.707 -7.092  28.679   1.00 68.93  ? 128 LYS   E CB    1 
ATOM   11159 C  CG    . LYS   D 3  126 ? -49.116 -7.660  28.689   1.00 68.79  ? 128 LYS   E CG    1 
ATOM   11160 C  CD    . LYS   D 3  126 ? -49.984 -7.003  27.633   1.00 81.05  ? 128 LYS   E CD    1 
ATOM   11161 C  CE    . LYS   D 3  126 ? -49.937 -5.486  27.756   1.00 82.24  ? 128 LYS   E CE    1 
ATOM   11162 N  NZ    . LYS   D 3  126 ? -50.838 -4.819  26.779   1.00 77.63  ? 128 LYS   E NZ    1 
ATOM   11163 N  N     . HIS   D 3  127 ? -45.476 -9.099  29.477   1.00 78.78  ? 129 HIS   E N     1 
ATOM   11164 C  CA    . HIS   D 3  127 ? -44.905 -10.428 29.669   1.00 68.53  ? 129 HIS   E CA    1 
ATOM   11165 C  C     . HIS   D 3  127 ? -44.371 -10.623 31.082   1.00 68.15  ? 129 HIS   E C     1 
ATOM   11166 O  O     . HIS   D 3  127 ? -44.343 -11.752 31.581   1.00 69.50  ? 129 HIS   E O     1 
ATOM   11167 C  CB    . HIS   D 3  127 ? -43.793 -10.669 28.660   1.00 58.94  ? 129 HIS   E CB    1 
ATOM   11168 C  CG    . HIS   D 3  127 ? -43.027 -11.932 28.895   1.00 69.18  ? 129 HIS   E CG    1 
ATOM   11169 N  ND1   . HIS   D 3  127 ? -43.448 -13.159 28.424   1.00 56.22  ? 129 HIS   E ND1   1 
ATOM   11170 C  CD2   . HIS   D 3  127 ? -41.857 -12.157 29.544   1.00 64.05  ? 129 HIS   E CD2   1 
ATOM   11171 C  CE1   . HIS   D 3  127 ? -42.565 -14.082 28.766   1.00 59.55  ? 129 HIS   E CE1   1 
ATOM   11172 N  NE2   . HIS   D 3  127 ? -41.592 -13.501 29.450   1.00 44.86  ? 129 HIS   E NE2   1 
ATOM   11173 N  N     . ALA   D 3  128 ? -43.929 -9.554  31.739   1.00 68.97  ? 130 ALA   E N     1 
ATOM   11174 C  CA    . ALA   D 3  128 ? -43.431 -9.714  33.100   1.00 67.54  ? 130 ALA   E CA    1 
ATOM   11175 C  C     . ALA   D 3  128 ? -44.569 -9.821  34.106   1.00 71.62  ? 130 ALA   E C     1 
ATOM   11176 O  O     . ALA   D 3  128 ? -44.439 -10.534 35.105   1.00 70.96  ? 130 ALA   E O     1 
ATOM   11177 C  CB    . ALA   D 3  128 ? -42.501 -8.558  33.464   1.00 56.44  ? 130 ALA   E CB    1 
ATOM   11178 N  N     . GLU   D 3  129 ? -45.680 -9.116  33.871   1.00 77.16  ? 131 GLU   E N     1 
ATOM   11179 C  CA    . GLU   D 3  129 ? -46.881 -9.347  34.669   1.00 71.20  ? 131 GLU   E CA    1 
ATOM   11180 C  C     . GLU   D 3  129 ? -47.357 -10.783 34.511   1.00 68.23  ? 131 GLU   E C     1 
ATOM   11181 O  O     . GLU   D 3  129 ? -47.846 -11.393 35.468   1.00 76.44  ? 131 GLU   E O     1 
ATOM   11182 C  CB    . GLU   D 3  129 ? -47.992 -8.371  34.265   1.00 68.58  ? 131 GLU   E CB    1 
ATOM   11183 C  CG    . GLU   D 3  129 ? -47.697 -6.909  34.535   1.00 67.24  ? 131 GLU   E CG    1 
ATOM   11184 C  CD    . GLU   D 3  129 ? -47.734 -6.577  36.015   1.00 84.10  ? 131 GLU   E CD    1 
ATOM   11185 O  OE1   . GLU   D 3  129 ? -46.762 -6.910  36.731   1.00 79.07  ? 131 GLU   E OE1   1 
ATOM   11186 O  OE2   . GLU   D 3  129 ? -48.746 -5.991  36.466   1.00 90.53  ? 131 GLU   E OE2   1 
ATOM   11187 N  N     . GLU   D 3  130 ? -47.202 -11.346 33.310   1.00 68.19  ? 132 GLU   E N     1 
ATOM   11188 C  CA    . GLU   D 3  130 ? -47.661 -12.707 33.059   1.00 71.87  ? 132 GLU   E CA    1 
ATOM   11189 C  C     . GLU   D 3  130 ? -46.749 -13.746 33.701   1.00 73.00  ? 132 GLU   E C     1 
ATOM   11190 O  O     . GLU   D 3  130 ? -47.198 -14.858 34.001   1.00 70.98  ? 132 GLU   E O     1 
ATOM   11191 C  CB    . GLU   D 3  130 ? -47.774 -12.952 31.557   1.00 64.27  ? 132 GLU   E CB    1 
ATOM   11192 C  CG    . GLU   D 3  130 ? -48.873 -12.144 30.908   1.00 74.83  ? 132 GLU   E CG    1 
ATOM   11193 C  CD    . GLU   D 3  130 ? -48.873 -12.261 29.398   1.00 93.16  ? 132 GLU   E CD    1 
ATOM   11194 O  OE1   . GLU   D 3  130 ? -49.179 -13.362 28.883   1.00 93.64  ? 132 GLU   E OE1   1 
ATOM   11195 O  OE2   . GLU   D 3  130 ? -48.556 -11.249 28.729   1.00 94.55  ? 132 GLU   E OE2   1 
ATOM   11196 N  N     . VAL   D 3  131 ? -45.472 -13.414 33.916   1.00 75.38  ? 133 VAL   E N     1 
ATOM   11197 C  CA    . VAL   D 3  131 ? -44.583 -14.356 34.587   1.00 63.03  ? 133 VAL   E CA    1 
ATOM   11198 C  C     . VAL   D 3  131 ? -44.923 -14.425 36.065   1.00 67.80  ? 133 VAL   E C     1 
ATOM   11199 O  O     . VAL   D 3  131 ? -45.027 -15.515 36.639   1.00 71.61  ? 133 VAL   E O     1 
ATOM   11200 C  CB    . VAL   D 3  131 ? -43.102 -13.990 34.353   1.00 63.00  ? 133 VAL   E CB    1 
ATOM   11201 C  CG1   . VAL   D 3  131 ? -42.697 -12.750 35.143   1.00 65.50  ? 133 VAL   E CG1   1 
ATOM   11202 C  CG2   . VAL   D 3  131 ? -42.208 -15.157 34.710   1.00 54.57  ? 133 VAL   E CG2   1 
ATOM   11203 N  N     . ARG   D 3  132 ? -45.136 -13.268 36.701   1.00 66.51  ? 134 ARG   E N     1 
ATOM   11204 C  CA    . ARG   D 3  132 ? -45.474 -13.274 38.117   1.00 62.70  ? 134 ARG   E CA    1 
ATOM   11205 C  C     . ARG   D 3  132 ? -46.872 -13.840 38.349   1.00 73.86  ? 134 ARG   E C     1 
ATOM   11206 O  O     . ARG   D 3  132 ? -47.108 -14.504 39.368   1.00 68.36  ? 134 ARG   E O     1 
ATOM   11207 C  CB    . ARG   D 3  132 ? -45.337 -11.867 38.690   1.00 60.56  ? 134 ARG   E CB    1 
ATOM   11208 C  CG    . ARG   D 3  132 ? -43.890 -11.415 38.812   1.00 55.89  ? 134 ARG   E CG    1 
ATOM   11209 C  CD    . ARG   D 3  132 ? -43.764 -10.048 39.467   1.00 57.96  ? 134 ARG   E CD    1 
ATOM   11210 N  NE    . ARG   D 3  132 ? -44.362 -8.977  38.677   1.00 71.01  ? 134 ARG   E NE    1 
ATOM   11211 C  CZ    . ARG   D 3  132 ? -43.697 -8.205  37.827   1.00 71.83  ? 134 ARG   E CZ    1 
ATOM   11212 N  NH1   . ARG   D 3  132 ? -42.399 -8.360  37.618   1.00 62.39  ? 134 ARG   E NH1   1 
ATOM   11213 N  NH2   . ARG   D 3  132 ? -44.352 -7.248  37.173   1.00 71.09  ? 134 ARG   E NH2   1 
ATOM   11214 N  N     . LYS   D 3  133 ? -47.793 -13.620 37.405   1.00 72.32  ? 135 LYS   E N     1 
ATOM   11215 C  CA    . LYS   D 3  133 ? -49.129 -14.203 37.464   1.00 72.46  ? 135 LYS   E CA    1 
ATOM   11216 C  C     . LYS   D 3  133 ? -49.105 -15.657 36.995   1.00 78.85  ? 135 LYS   E C     1 
ATOM   11217 O  O     . LYS   D 3  133 ? -50.058 -16.151 36.380   1.00 73.19  ? 135 LYS   E O     1 
ATOM   11218 C  CB    . LYS   D 3  133 ? -50.115 -13.380 36.626   1.00 66.73  ? 135 LYS   E CB    1 
ATOM   11219 C  CG    . LYS   D 3  133 ? -51.575 -13.816 36.795   1.00 82.71  ? 135 LYS   E CG    1 
ATOM   11220 C  CD    . LYS   D 3  133 ? -52.497 -13.221 35.737   1.00 93.01  ? 135 LYS   E CD    1 
ATOM   11221 C  CE    . LYS   D 3  133 ? -53.865 -13.908 35.729   1.00 85.68  ? 135 LYS   E CE    1 
ATOM   11222 N  NZ    . LYS   D 3  133 ? -54.814 -13.278 34.761   1.00 68.46  ? 135 LYS   E NZ    1 
ATOM   11223 N  N     . ASN   D 3  134 ? -48.008 -16.352 37.273   1.00 77.18  ? 136 ASN   E N     1 
ATOM   11224 C  CA    . ASN   D 3  134 ? -47.884 -17.749 36.884   1.00 79.65  ? 136 ASN   E CA    1 
ATOM   11225 C  C     . ASN   D 3  134 ? -47.116 -18.499 37.955   1.00 78.06  ? 136 ASN   E C     1 
ATOM   11226 O  O     . ASN   D 3  134 ? -47.459 -19.634 38.300   1.00 76.65  ? 136 ASN   E O     1 
ATOM   11227 C  CB    . ASN   D 3  134 ? -47.196 -17.879 35.529   1.00 70.75  ? 136 ASN   E CB    1 
ATOM   11228 C  CG    . ASN   D 3  134 ? -48.183 -17.922 34.397   1.00 88.63  ? 136 ASN   E CG    1 
ATOM   11229 O  OD1   . ASN   D 3  134 ? -48.479 -18.992 33.856   1.00 95.35  ? 136 ASN   E OD1   1 
ATOM   11230 N  ND2   . ASN   D 3  134 ? -48.731 -16.760 34.046   1.00 83.11  ? 136 ASN   E ND2   1 
ATOM   11231 N  N     . LYS   D 3  135 ? -46.068 -17.862 38.479   1.00 66.15  ? 137 LYS   E N     1 
ATOM   11232 C  CA    . LYS   D 3  135 ? -45.458 -18.359 39.701   1.00 67.98  ? 137 LYS   E CA    1 
ATOM   11233 C  C     . LYS   D 3  135 ? -46.505 -18.498 40.797   1.00 80.47  ? 137 LYS   E C     1 
ATOM   11234 O  O     . LYS   D 3  135 ? -46.550 -19.519 41.497   1.00 88.49  ? 137 LYS   E O     1 
ATOM   11235 C  CB    . LYS   D 3  135 ? -44.328 -17.430 40.142   1.00 62.54  ? 137 LYS   E CB    1 
ATOM   11236 C  CG    . LYS   D 3  135 ? -43.962 -17.574 41.593   1.00 60.36  ? 137 LYS   E CG    1 
ATOM   11237 C  CD    . LYS   D 3  135 ? -42.515 -17.228 41.843   1.00 63.06  ? 137 LYS   E CD    1 
ATOM   11238 C  CE    . LYS   D 3  135 ? -42.261 -17.155 43.325   1.00 51.27  ? 137 LYS   E CE    1 
ATOM   11239 N  NZ    . LYS   D 3  135 ? -43.345 -16.370 43.973   1.00 78.37  ? 137 LYS   E NZ    1 
ATOM   11240 N  N     . GLU   D 3  136 ? -47.374 -17.493 40.951   1.00 76.36  ? 138 GLU   E N     1 
ATOM   11241 C  CA    . GLU   D 3  136 ? -48.438 -17.564 41.952   1.00 83.83  ? 138 GLU   E CA    1 
ATOM   11242 C  C     . GLU   D 3  136 ? -49.568 -18.471 41.461   1.00 86.00  ? 138 GLU   E C     1 
ATOM   11243 O  O     . GLU   D 3  136 ? -50.733 -18.088 41.356   1.00 82.99  ? 138 GLU   E O     1 
ATOM   11244 C  CB    . GLU   D 3  136 ? -48.962 -16.183 42.321   1.00 82.30  ? 138 GLU   E CB    1 
ATOM   11245 C  CG    . GLU   D 3  136 ? -49.900 -16.250 43.524   1.00 80.35  ? 138 GLU   E CG    1 
ATOM   11246 C  CD    . GLU   D 3  136 ? -50.381 -14.896 43.982   1.00 90.95  ? 138 GLU   E CD    1 
ATOM   11247 O  OE1   . GLU   D 3  136 ? -51.020 -14.182 43.181   1.00 77.35  ? 138 GLU   E OE1   1 
ATOM   11248 O  OE2   . GLU   D 3  136 ? -50.116 -14.544 45.152   1.00 106.87 ? 138 GLU   E OE2   1 
ATOM   11249 N  N     . LEU   D 3  137 ? -49.178 -19.702 41.140   1.00 88.87  ? 139 LEU   E N     1 
ATOM   11250 C  CA    . LEU   D 3  137 ? -50.095 -20.810 40.915   1.00 81.69  ? 139 LEU   E CA    1 
ATOM   11251 C  C     . LEU   D 3  137 ? -49.580 -22.000 41.717   1.00 87.66  ? 139 LEU   E C     1 
ATOM   11252 O  O     . LEU   D 3  137 ? -48.511 -22.545 41.418   1.00 81.99  ? 139 LEU   E O     1 
ATOM   11253 C  CB    . LEU   D 3  137 ? -50.213 -21.143 39.430   1.00 81.31  ? 139 LEU   E CB    1 
ATOM   11254 C  CG    . LEU   D 3  137 ? -51.171 -20.252 38.649   1.00 74.83  ? 139 LEU   E CG    1 
ATOM   11255 C  CD1   . LEU   D 3  137 ? -50.692 -18.815 38.643   1.00 72.10  ? 139 LEU   E CD1   1 
ATOM   11256 C  CD2   . LEU   D 3  137 ? -51.327 -20.793 37.234   1.00 73.47  ? 139 LEU   E CD2   1 
ATOM   11257 N  N     . LYS   D 3  138 ? -50.328 -22.374 42.752   1.00 100.32 ? 140 LYS   E N     1 
ATOM   11258 C  CA    . LYS   D 3  138 ? -50.045 -23.552 43.564   1.00 96.82  ? 140 LYS   E CA    1 
ATOM   11259 C  C     . LYS   D 3  138 ? -51.252 -23.813 44.456   1.00 86.50  ? 140 LYS   E C     1 
ATOM   11260 O  O     . LYS   D 3  138 ? -52.086 -22.923 44.652   1.00 75.79  ? 140 LYS   E O     1 
ATOM   11261 C  CB    . LYS   D 3  138 ? -48.775 -23.364 44.404   1.00 90.96  ? 140 LYS   E CB    1 
ATOM   11262 C  CG    . LYS   D 3  138 ? -48.857 -22.243 45.426   1.00 80.87  ? 140 LYS   E CG    1 
ATOM   11263 C  CD    . LYS   D 3  138 ? -48.549 -20.905 44.793   1.00 83.98  ? 140 LYS   E CD    1 
ATOM   11264 C  CE    . LYS   D 3  138 ? -48.565 -19.796 45.833   1.00 86.45  ? 140 LYS   E CE    1 
ATOM   11265 N  NZ    . LYS   D 3  138 ? -47.984 -18.531 45.297   1.00 76.63  ? 140 LYS   E NZ    1 
ATOM   11266 N  N     . MET   E 4  1   ? 5.599   56.444  -59.465  1.00 60.11  ? 1   MET   F N     1 
ATOM   11267 C  CA    . MET   E 4  1   ? 4.554   55.583  -60.013  1.00 64.41  ? 1   MET   F CA    1 
ATOM   11268 C  C     . MET   E 4  1   ? 3.511   56.389  -60.787  1.00 59.56  ? 1   MET   F C     1 
ATOM   11269 O  O     . MET   E 4  1   ? 3.231   57.546  -60.459  1.00 59.86  ? 1   MET   F O     1 
ATOM   11270 C  CB    . MET   E 4  1   ? 3.867   54.783  -58.890  1.00 70.74  ? 1   MET   F CB    1 
ATOM   11271 C  CG    . MET   E 4  1   ? 3.072   53.547  -59.357  1.00 59.11  ? 1   MET   F CG    1 
ATOM   11272 S  SD    . MET   E 4  1   ? 4.100   52.064  -59.643  1.00 95.56  ? 1   MET   F SD    1 
ATOM   11273 C  CE    . MET   E 4  1   ? 2.859   50.752  -59.728  1.00 69.89  ? 1   MET   F CE    1 
ATOM   11274 N  N     . TYR   E 4  2   ? 2.948   55.768  -61.820  1.00 56.85  ? 2   TYR   F N     1 
ATOM   11275 C  CA    . TYR   E 4  2   ? 1.760   56.259  -62.498  1.00 46.83  ? 2   TYR   F CA    1 
ATOM   11276 C  C     . TYR   E 4  2   ? 0.771   55.112  -62.641  1.00 53.33  ? 2   TYR   F C     1 
ATOM   11277 O  O     . TYR   E 4  2   ? 1.118   53.937  -62.478  1.00 55.95  ? 2   TYR   F O     1 
ATOM   11278 C  CB    . TYR   E 4  2   ? 2.081   56.826  -63.872  1.00 43.31  ? 2   TYR   F CB    1 
ATOM   11279 C  CG    . TYR   E 4  2   ? 3.241   57.770  -63.900  1.00 44.90  ? 2   TYR   F CG    1 
ATOM   11280 C  CD1   . TYR   E 4  2   ? 3.123   59.048  -63.371  1.00 43.58  ? 2   TYR   F CD1   1 
ATOM   11281 C  CD2   . TYR   E 4  2   ? 4.453   57.403  -64.491  1.00 48.89  ? 2   TYR   F CD2   1 
ATOM   11282 C  CE1   . TYR   E 4  2   ? 4.184   59.943  -63.417  1.00 53.31  ? 2   TYR   F CE1   1 
ATOM   11283 C  CE2   . TYR   E 4  2   ? 5.529   58.294  -64.547  1.00 53.60  ? 2   TYR   F CE2   1 
ATOM   11284 C  CZ    . TYR   E 4  2   ? 5.384   59.567  -64.005  1.00 54.70  ? 2   TYR   F CZ    1 
ATOM   11285 O  OH    . TYR   E 4  2   ? 6.420   60.473  -64.036  1.00 52.02  ? 2   TYR   F OH    1 
ATOM   11286 N  N     . THR   E 4  3   ? -0.470  55.467  -62.961  1.00 47.36  ? 3   THR   F N     1 
ATOM   11287 C  CA    . THR   E 4  3   ? -1.561  54.513  -63.072  1.00 49.98  ? 3   THR   F CA    1 
ATOM   11288 C  C     . THR   E 4  3   ? -2.214  54.617  -64.440  1.00 49.49  ? 3   THR   F C     1 
ATOM   11289 O  O     . THR   E 4  3   ? -2.171  55.661  -65.094  1.00 52.10  ? 3   THR   F O     1 
ATOM   11290 C  CB    . THR   E 4  3   ? -2.616  54.771  -62.008  1.00 49.23  ? 3   THR   F CB    1 
ATOM   11291 O  OG1   . THR   E 4  3   ? -3.084  56.119  -62.159  1.00 48.50  ? 3   THR   F OG1   1 
ATOM   11292 C  CG2   . THR   E 4  3   ? -2.016  54.596  -60.641  1.00 41.11  ? 3   THR   F CG2   1 
ATOM   11293 N  N     . PHE   E 4  4   ? -2.856  53.531  -64.853  1.00 46.87  ? 4   PHE   F N     1 
ATOM   11294 C  CA    . PHE   E 4  4   ? -3.546  53.513  -66.130  1.00 47.09  ? 4   PHE   F CA    1 
ATOM   11295 C  C     . PHE   E 4  4   ? -4.654  52.471  -66.078  1.00 53.78  ? 4   PHE   F C     1 
ATOM   11296 O  O     . PHE   E 4  4   ? -4.543  51.463  -65.373  1.00 55.28  ? 4   PHE   F O     1 
ATOM   11297 C  CB    . PHE   E 4  4   ? -2.580  53.223  -67.284  1.00 46.90  ? 4   PHE   F CB    1 
ATOM   11298 C  CG    . PHE   E 4  4   ? -2.151  51.788  -67.375  1.00 49.39  ? 4   PHE   F CG    1 
ATOM   11299 C  CD1   . PHE   E 4  4   ? -1.070  51.326  -66.645  1.00 49.22  ? 4   PHE   F CD1   1 
ATOM   11300 C  CD2   . PHE   E 4  4   ? -2.831  50.897  -68.208  1.00 56.89  ? 4   PHE   F CD2   1 
ATOM   11301 C  CE1   . PHE   E 4  4   ? -0.667  50.003  -66.741  1.00 56.04  ? 4   PHE   F CE1   1 
ATOM   11302 C  CE2   . PHE   E 4  4   ? -2.440  49.564  -68.307  1.00 51.02  ? 4   PHE   F CE2   1 
ATOM   11303 C  CZ    . PHE   E 4  4   ? -1.355  49.119  -67.584  1.00 51.37  ? 4   PHE   F CZ    1 
ATOM   11304 N  N     . VAL   E 4  5   ? -5.733  52.740  -66.811  1.00 48.01  ? 5   VAL   F N     1 
ATOM   11305 C  CA    . VAL   E 4  5   ? -6.841  51.807  -66.962  1.00 54.15  ? 5   VAL   F CA    1 
ATOM   11306 C  C     . VAL   E 4  5   ? -6.833  51.304  -68.399  1.00 51.24  ? 5   VAL   F C     1 
ATOM   11307 O  O     . VAL   E 4  5   ? -6.270  51.935  -69.296  1.00 52.62  ? 5   VAL   F O     1 
ATOM   11308 C  CB    . VAL   E 4  5   ? -8.201  52.449  -66.607  1.00 49.99  ? 5   VAL   F CB    1 
ATOM   11309 C  CG1   . VAL   E 4  5   ? -8.256  52.817  -65.132  1.00 44.21  ? 5   VAL   F CG1   1 
ATOM   11310 C  CG2   . VAL   E 4  5   ? -8.454  53.684  -67.477  1.00 47.00  ? 5   VAL   F CG2   1 
ATOM   11311 N  N     . VAL   E 4  6   ? -7.471  50.157  -68.621  1.00 46.77  ? 6   VAL   F N     1 
ATOM   11312 C  CA    . VAL   E 4  6   ? -7.469  49.492  -69.925  1.00 47.38  ? 6   VAL   F CA    1 
ATOM   11313 C  C     . VAL   E 4  6   ? -8.920  49.219  -70.310  1.00 44.83  ? 6   VAL   F C     1 
ATOM   11314 O  O     . VAL   E 4  6   ? -9.581  48.382  -69.691  1.00 47.71  ? 6   VAL   F O     1 
ATOM   11315 C  CB    . VAL   E 4  6   ? -6.647  48.192  -69.907  1.00 44.62  ? 6   VAL   F CB    1 
ATOM   11316 C  CG1   . VAL   E 4  6   ? -6.983  47.324  -71.110  1.00 47.49  ? 6   VAL   F CG1   1 
ATOM   11317 C  CG2   . VAL   E 4  6   ? -5.141  48.490  -69.853  1.00 40.83  ? 6   VAL   F CG2   1 
ATOM   11318 N  N     . ARG   E 4  7   ? -9.414  49.903  -71.339  1.00 50.50  ? 7   ARG   F N     1 
ATOM   11319 C  CA    . ARG   E 4  7   ? -10.840 49.873  -71.635  1.00 56.10  ? 7   ARG   F CA    1 
ATOM   11320 C  C     . ARG   E 4  7   ? -11.209 49.385  -73.034  1.00 53.65  ? 7   ARG   F C     1 
ATOM   11321 O  O     . ARG   E 4  7   ? -12.400 49.389  -73.371  1.00 52.88  ? 7   ARG   F O     1 
ATOM   11322 C  CB    . ARG   E 4  7   ? -11.442 51.261  -71.399  1.00 47.98  ? 7   ARG   F CB    1 
ATOM   11323 C  CG    . ARG   E 4  7   ? -11.364 51.665  -69.958  1.00 43.67  ? 7   ARG   F CG    1 
ATOM   11324 C  CD    . ARG   E 4  7   ? -11.784 53.081  -69.811  1.00 45.98  ? 7   ARG   F CD    1 
ATOM   11325 N  NE    . ARG   E 4  7   ? -13.143 53.298  -70.284  1.00 41.23  ? 7   ARG   F NE    1 
ATOM   11326 C  CZ    . ARG   E 4  7   ? -14.208 53.286  -69.495  1.00 46.52  ? 7   ARG   F CZ    1 
ATOM   11327 N  NH1   . ARG   E 4  7   ? -14.106 52.997  -68.204  1.00 43.52  ? 7   ARG   F NH1   1 
ATOM   11328 N  NH2   . ARG   E 4  7   ? -15.401 53.577  -70.011  1.00 40.56  ? 7   ARG   F NH2   1 
ATOM   11329 N  N     . ASP   E 4  8   ? -10.240 48.972  -73.852  1.00 53.15  ? 8   ASP   F N     1 
ATOM   11330 C  CA    . ASP   E 4  8   ? -10.480 48.255  -75.109  1.00 50.87  ? 8   ASP   F CA    1 
ATOM   11331 C  C     . ASP   E 4  8   ? -9.709  46.944  -74.974  1.00 60.47  ? 8   ASP   F C     1 
ATOM   11332 O  O     . ASP   E 4  8   ? -8.556  46.842  -75.400  1.00 57.48  ? 8   ASP   F O     1 
ATOM   11333 C  CB    . ASP   E 4  8   ? -10.035 49.064  -76.335  1.00 48.16  ? 8   ASP   F CB    1 
ATOM   11334 C  CG    . ASP   E 4  8   ? -10.101 48.265  -77.642  1.00 59.19  ? 8   ASP   F CG    1 
ATOM   11335 O  OD1   . ASP   E 4  8   ? -10.371 47.046  -77.599  1.00 58.30  ? 8   ASP   F OD1   1 
ATOM   11336 O  OD2   . ASP   E 4  8   ? -9.883  48.864  -78.724  1.00 62.28  ? 8   ASP   F OD2   1 
ATOM   11337 N  N     . GLU   E 4  9   ? -10.360 45.942  -74.375  1.00 67.99  ? 9   GLU   F N     1 
ATOM   11338 C  CA    . GLU   E 4  9   ? -9.728  44.673  -74.031  1.00 63.22  ? 9   GLU   F CA    1 
ATOM   11339 C  C     . GLU   E 4  9   ? -9.422  43.816  -75.258  1.00 62.23  ? 9   GLU   F C     1 
ATOM   11340 O  O     . GLU   E 4  9   ? -9.189  42.617  -75.119  1.00 66.29  ? 9   GLU   F O     1 
ATOM   11341 C  CB    . GLU   E 4  9   ? -10.617 43.889  -73.053  1.00 65.55  ? 9   GLU   F CB    1 
ATOM   11342 C  CG    . GLU   E 4  9   ? -9.898  42.782  -72.278  1.00 73.97  ? 9   GLU   F CG    1 
ATOM   11343 C  CD    . GLU   E 4  9   ? -9.040  43.313  -71.143  1.00 67.20  ? 9   GLU   F CD    1 
ATOM   11344 O  OE1   . GLU   E 4  9   ? -9.215  44.495  -70.778  1.00 64.57  ? 9   GLU   F OE1   1 
ATOM   11345 O  OE2   . GLU   E 4  9   ? -8.194  42.548  -70.616  1.00 53.25  ? 9   GLU   F OE2   1 
ATOM   11346 N  N     . ASN   E 4  10  ? -9.412  44.411  -76.462  1.00 61.27  ? 10  ASN   F N     1 
ATOM   11347 C  CA    . ASN   E 4  10  ? -9.063  43.677  -77.672  1.00 56.19  ? 10  ASN   F CA    1 
ATOM   11348 C  C     . ASN   E 4  10  ? -7.848  44.222  -78.409  1.00 59.50  ? 10  ASN   F C     1 
ATOM   11349 O  O     . ASN   E 4  10  ? -7.281  43.502  -79.239  1.00 63.45  ? 10  ASN   F O     1 
ATOM   11350 C  CB    . ASN   E 4  10  ? -10.254 43.635  -78.635  1.00 36.81  ? 10  ASN   F CB    1 
ATOM   11351 C  CG    . ASN   E 4  10  ? -11.314 42.673  -78.172  1.00 53.12  ? 10  ASN   F CG    1 
ATOM   11352 O  OD1   . ASN   E 4  10  ? -11.006 41.690  -77.499  1.00 51.59  ? 10  ASN   F OD1   1 
ATOM   11353 N  ND2   . ASN   E 4  10  ? -12.571 42.953  -78.504  1.00 60.40  ? 10  ASN   F ND2   1 
ATOM   11354 N  N     . SER   E 4  11  ? -7.419  45.446  -78.118  1.00 56.47  ? 11  SER   F N     1 
ATOM   11355 C  CA    . SER   E 4  11  ? -6.276  46.031  -78.802  1.00 51.37  ? 11  SER   F CA    1 
ATOM   11356 C  C     . SER   E 4  11  ? -5.052  45.136  -78.669  1.00 47.32  ? 11  SER   F C     1 
ATOM   11357 O  O     . SER   E 4  11  ? -4.509  44.967  -77.576  1.00 50.23  ? 11  SER   F O     1 
ATOM   11358 C  CB    . SER   E 4  11  ? -5.989  47.434  -78.248  1.00 58.98  ? 11  SER   F CB    1 
ATOM   11359 O  OG    . SER   E 4  11  ? -4.797  48.001  -78.775  1.00 50.58  ? 11  SER   F OG    1 
ATOM   11360 N  N     . SER   E 4  12  ? -4.628  44.539  -79.779  1.00 46.12  ? 12  SER   F N     1 
ATOM   11361 C  CA    . SER   E 4  12  ? -3.289  43.964  -79.856  1.00 53.52  ? 12  SER   F CA    1 
ATOM   11362 C  C     . SER   E 4  12  ? -2.230  44.992  -79.450  1.00 49.71  ? 12  SER   F C     1 
ATOM   11363 O  O     . SER   E 4  12  ? -1.458  44.781  -78.509  1.00 46.21  ? 12  SER   F O     1 
ATOM   11364 C  CB    . SER   E 4  12  ? -3.036  43.451  -81.284  1.00 52.18  ? 12  SER   F CB    1 
ATOM   11365 O  OG    . SER   E 4  12  ? -4.198  43.581  -82.113  1.00 56.77  ? 12  SER   F OG    1 
ATOM   11366 N  N     . VAL   E 4  13  ? -2.211  46.129  -80.149  1.00 52.59  ? 13  VAL   F N     1 
ATOM   11367 C  CA    . VAL   E 4  13  ? -1.181  47.148  -79.965  1.00 49.86  ? 13  VAL   F CA    1 
ATOM   11368 C  C     . VAL   E 4  13  ? -1.104  47.595  -78.512  1.00 56.10  ? 13  VAL   F C     1 
ATOM   11369 O  O     . VAL   E 4  13  ? -0.010  47.779  -77.960  1.00 57.03  ? 13  VAL   F O     1 
ATOM   11370 C  CB    . VAL   E 4  13  ? -1.452  48.346  -80.898  1.00 49.26  ? 13  VAL   F CB    1 
ATOM   11371 C  CG1   . VAL   E 4  13  ? -0.706  49.563  -80.410  1.00 45.44  ? 13  VAL   F CG1   1 
ATOM   11372 C  CG2   . VAL   E 4  13  ? -1.067  48.022  -82.330  1.00 44.29  ? 13  VAL   F CG2   1 
ATOM   11373 N  N     . TYR   E 4  14  ? -2.251  47.815  -77.873  1.00 55.18  ? 14  TYR   F N     1 
ATOM   11374 C  CA    . TYR   E 4  14  ? -2.190  48.330  -76.510  1.00 59.55  ? 14  TYR   F CA    1 
ATOM   11375 C  C     . TYR   E 4  14  ? -2.107  47.237  -75.460  1.00 50.02  ? 14  TYR   F C     1 
ATOM   11376 O  O     . TYR   E 4  14  ? -1.743  47.532  -74.318  1.00 51.31  ? 14  TYR   F O     1 
ATOM   11377 C  CB    . TYR   E 4  14  ? -3.361  49.285  -76.255  1.00 50.11  ? 14  TYR   F CB    1 
ATOM   11378 C  CG    . TYR   E 4  14  ? -3.088  50.564  -77.010  1.00 53.57  ? 14  TYR   F CG    1 
ATOM   11379 C  CD1   . TYR   E 4  14  ? -2.162  51.492  -76.531  1.00 44.25  ? 14  TYR   F CD1   1 
ATOM   11380 C  CD2   . TYR   E 4  14  ? -3.669  50.798  -78.246  1.00 48.47  ? 14  TYR   F CD2   1 
ATOM   11381 C  CE1   . TYR   E 4  14  ? -1.875  52.640  -77.228  1.00 40.26  ? 14  TYR   F CE1   1 
ATOM   11382 C  CE2   . TYR   E 4  14  ? -3.379  51.942  -78.955  1.00 46.92  ? 14  TYR   F CE2   1 
ATOM   11383 C  CZ    . TYR   E 4  14  ? -2.486  52.864  -78.445  1.00 47.07  ? 14  TYR   F CZ    1 
ATOM   11384 O  OH    . TYR   E 4  14  ? -2.217  54.008  -79.170  1.00 48.21  ? 14  TYR   F OH    1 
ATOM   11385 N  N     . ALA   E 4  15  ? -2.396  45.989  -75.828  1.00 49.75  ? 15  ALA   F N     1 
ATOM   11386 C  CA    . ALA   E 4  15  ? -1.972  44.853  -75.016  1.00 49.69  ? 15  ALA   F CA    1 
ATOM   11387 C  C     . ALA   E 4  15  ? -0.476  44.916  -74.726  1.00 54.24  ? 15  ALA   F C     1 
ATOM   11388 O  O     . ALA   E 4  15  ? -0.046  44.828  -73.570  1.00 50.39  ? 15  ALA   F O     1 
ATOM   11389 C  CB    . ALA   E 4  15  ? -2.323  43.551  -75.732  1.00 47.22  ? 15  ALA   F CB    1 
ATOM   11390 N  N     . GLU   E 4  16  ? 0.337   45.069  -75.777  1.00 53.69  ? 16  GLU   F N     1 
ATOM   11391 C  CA    . GLU   E 4  16  ? 1.780   45.120  -75.596  1.00 54.52  ? 16  GLU   F CA    1 
ATOM   11392 C  C     . GLU   E 4  16  ? 2.212   46.391  -74.893  1.00 56.77  ? 16  GLU   F C     1 
ATOM   11393 O  O     . GLU   E 4  16  ? 3.287   46.418  -74.280  1.00 63.03  ? 16  GLU   F O     1 
ATOM   11394 C  CB    . GLU   E 4  16  ? 2.491   45.006  -76.948  1.00 54.38  ? 16  GLU   F CB    1 
ATOM   11395 C  CG    . GLU   E 4  16  ? 4.009   44.855  -76.859  1.00 54.42  ? 16  GLU   F CG    1 
ATOM   11396 C  CD    . GLU   E 4  16  ? 4.428   43.516  -76.260  1.00 65.95  ? 16  GLU   F CD    1 
ATOM   11397 O  OE1   . GLU   E 4  16  ? 3.536   42.670  -76.051  1.00 60.05  ? 16  GLU   F OE1   1 
ATOM   11398 O  OE2   . GLU   E 4  16  ? 5.640   43.314  -75.988  1.00 66.55  ? 16  GLU   F OE2   1 
ATOM   11399 N  N     . VAL   E 4  17  ? 1.387   47.435  -74.968  1.00 59.23  ? 17  VAL   F N     1 
ATOM   11400 C  CA    . VAL   E 4  17  ? 1.683   48.703  -74.306  1.00 63.36  ? 17  VAL   F CA    1 
ATOM   11401 C  C     . VAL   E 4  17  ? 1.481   48.603  -72.787  1.00 56.08  ? 17  VAL   F C     1 
ATOM   11402 O  O     . VAL   E 4  17  ? 2.312   49.088  -72.012  1.00 58.47  ? 17  VAL   F O     1 
ATOM   11403 C  CB    . VAL   E 4  17  ? 0.833   49.823  -74.937  1.00 59.04  ? 17  VAL   F CB    1 
ATOM   11404 C  CG1   . VAL   E 4  17  ? 1.000   51.133  -74.179  1.00 47.80  ? 17  VAL   F CG1   1 
ATOM   11405 C  CG2   . VAL   E 4  17  ? 1.205   49.987  -76.405  1.00 57.32  ? 17  VAL   F CG2   1 
ATOM   11406 N  N     . SER   E 4  18  ? 0.390   47.982  -72.328  1.00 50.07  ? 18  SER   F N     1 
ATOM   11407 C  CA    . SER   E 4  18  ? 0.255   47.817  -70.882  1.00 56.01  ? 18  SER   F CA    1 
ATOM   11408 C  C     . SER   E 4  18  ? 1.278   46.816  -70.346  1.00 62.11  ? 18  SER   F C     1 
ATOM   11409 O  O     . SER   E 4  18  ? 1.868   47.038  -69.277  1.00 56.13  ? 18  SER   F O     1 
ATOM   11410 C  CB    . SER   E 4  18  ? -1.172  47.409  -70.503  1.00 57.41  ? 18  SER   F CB    1 
ATOM   11411 O  OG    . SER   E 4  18  ? -1.733  46.486  -71.415  1.00 63.54  ? 18  SER   F OG    1 
ATOM   11412 N  N     . ARG   E 4  19  ? 1.527   45.721  -71.081  1.00 56.45  ? 19  ARG   F N     1 
ATOM   11413 C  CA    . ARG   E 4  19  ? 2.549   44.777  -70.627  1.00 61.31  ? 19  ARG   F CA    1 
ATOM   11414 C  C     . ARG   E 4  19  ? 3.893   45.471  -70.470  1.00 60.72  ? 19  ARG   F C     1 
ATOM   11415 O  O     . ARG   E 4  19  ? 4.607   45.252  -69.481  1.00 59.50  ? 19  ARG   F O     1 
ATOM   11416 C  CB    . ARG   E 4  19  ? 2.678   43.600  -71.588  1.00 62.95  ? 19  ARG   F CB    1 
ATOM   11417 C  CG    . ARG   E 4  19  ? 3.690   42.571  -71.111  1.00 64.13  ? 19  ARG   F CG    1 
ATOM   11418 C  CD    . ARG   E 4  19  ? 4.144   41.624  -72.228  1.00 78.04  ? 19  ARG   F CD    1 
ATOM   11419 N  NE    . ARG   E 4  19  ? 5.250   42.162  -73.016  1.00 77.15  ? 19  ARG   F NE    1 
ATOM   11420 C  CZ    . ARG   E 4  19  ? 6.520   42.161  -72.627  1.00 84.02  ? 19  ARG   F CZ    1 
ATOM   11421 N  NH1   . ARG   E 4  19  ? 6.883   41.697  -71.439  1.00 84.51  ? 19  ARG   F NH1   1 
ATOM   11422 N  NH2   . ARG   E 4  19  ? 7.451   42.644  -73.447  1.00 75.87  ? 19  ARG   F NH2   1 
ATOM   11423 N  N     . LEU   E 4  20  ? 4.250   46.317  -71.438  1.00 54.79  ? 20  LEU   F N     1 
ATOM   11424 C  CA    . LEU   E 4  20  ? 5.460   47.116  -71.327  1.00 52.40  ? 20  LEU   F CA    1 
ATOM   11425 C  C     . LEU   E 4  20  ? 5.430   47.988  -70.076  1.00 64.50  ? 20  LEU   F C     1 
ATOM   11426 O  O     . LEU   E 4  20  ? 6.419   48.061  -69.335  1.00 67.34  ? 20  LEU   F O     1 
ATOM   11427 C  CB    . LEU   E 4  20  ? 5.627   47.972  -72.582  1.00 57.23  ? 20  LEU   F CB    1 
ATOM   11428 C  CG    . LEU   E 4  20  ? 6.290   47.304  -73.780  1.00 58.05  ? 20  LEU   F CG    1 
ATOM   11429 C  CD1   . LEU   E 4  20  ? 6.208   48.202  -75.007  1.00 58.63  ? 20  LEU   F CD1   1 
ATOM   11430 C  CD2   . LEU   E 4  20  ? 7.745   46.975  -73.448  1.00 48.81  ? 20  LEU   F CD2   1 
ATOM   11431 N  N     . LEU   E 4  21  ? 4.296   48.653  -69.820  1.00 63.07  ? 21  LEU   F N     1 
ATOM   11432 C  CA    . LEU   E 4  21  ? 4.220   49.583  -68.695  1.00 55.90  ? 21  LEU   F CA    1 
ATOM   11433 C  C     . LEU   E 4  21  ? 4.329   48.849  -67.365  1.00 52.28  ? 21  LEU   F C     1 
ATOM   11434 O  O     . LEU   E 4  21  ? 5.172   49.191  -66.530  1.00 52.89  ? 21  LEU   F O     1 
ATOM   11435 C  CB    . LEU   E 4  21  ? 2.928   50.400  -68.759  1.00 63.47  ? 21  LEU   F CB    1 
ATOM   11436 C  CG    . LEU   E 4  21  ? 2.684   51.371  -69.924  1.00 60.51  ? 21  LEU   F CG    1 
ATOM   11437 C  CD1   . LEU   E 4  21  ? 1.248   51.886  -69.842  1.00 56.21  ? 21  LEU   F CD1   1 
ATOM   11438 C  CD2   . LEU   E 4  21  ? 3.688   52.539  -69.968  1.00 46.29  ? 21  LEU   F CD2   1 
ATOM   11439 N  N     . LEU   E 4  22  ? 3.483   47.841  -67.143  1.00 57.61  ? 22  LEU   F N     1 
ATOM   11440 C  CA    . LEU   E 4  22  ? 3.617   47.018  -65.942  1.00 60.55  ? 22  LEU   F CA    1 
ATOM   11441 C  C     . LEU   E 4  22  ? 5.068   46.595  -65.728  1.00 63.50  ? 22  LEU   F C     1 
ATOM   11442 O  O     . LEU   E 4  22  ? 5.665   46.862  -64.679  1.00 59.52  ? 22  LEU   F O     1 
ATOM   11443 C  CB    . LEU   E 4  22  ? 2.719   45.783  -66.033  1.00 55.27  ? 22  LEU   F CB    1 
ATOM   11444 C  CG    . LEU   E 4  22  ? 1.202   45.950  -65.970  1.00 54.17  ? 22  LEU   F CG    1 
ATOM   11445 C  CD1   . LEU   E 4  22  ? 0.570   44.582  -65.931  1.00 49.29  ? 22  LEU   F CD1   1 
ATOM   11446 C  CD2   . LEU   E 4  22  ? 0.773   46.773  -64.769  1.00 43.94  ? 22  LEU   F CD2   1 
ATOM   11447 N  N     . ALA   E 4  23  ? 5.662   45.961  -66.743  1.00 70.82  ? 23  ALA   F N     1 
ATOM   11448 C  CA    . ALA   E 4  23  ? 7.016   45.430  -66.651  1.00 64.20  ? 23  ALA   F CA    1 
ATOM   11449 C  C     . ALA   E 4  23  ? 8.098   46.493  -66.415  1.00 66.64  ? 23  ALA   F C     1 
ATOM   11450 O  O     . ALA   E 4  23  ? 9.279   46.150  -66.383  1.00 68.58  ? 23  ALA   F O     1 
ATOM   11451 C  CB    . ALA   E 4  23  ? 7.330   44.614  -67.915  1.00 45.09  ? 23  ALA   F CB    1 
ATOM   11452 N  N     . THR   E 4  24  ? 7.742   47.778  -66.244  1.00 62.64  ? 24  THR   F N     1 
ATOM   11453 C  CA    . THR   E 4  24  ? 8.728   48.786  -65.851  1.00 57.08  ? 24  THR   F CA    1 
ATOM   11454 C  C     . THR   E 4  24  ? 8.782   48.994  -64.344  1.00 65.78  ? 24  THR   F C     1 
ATOM   11455 O  O     . THR   E 4  24  ? 9.652   49.732  -63.863  1.00 72.91  ? 24  THR   F O     1 
ATOM   11456 C  CB    . THR   E 4  24  ? 8.440   50.147  -66.512  1.00 64.51  ? 24  THR   F CB    1 
ATOM   11457 O  OG1   . THR   E 4  24  ? 7.274   50.741  -65.915  1.00 66.72  ? 24  THR   F OG1   1 
ATOM   11458 C  CG2   . THR   E 4  24  ? 8.241   50.008  -68.026  1.00 49.45  ? 24  THR   F CG2   1 
ATOM   11459 N  N     . GLY   E 4  25  ? 7.870   48.377  -63.593  1.00 58.31  ? 25  GLY   F N     1 
ATOM   11460 C  CA    . GLY   E 4  25  ? 7.792   48.574  -62.162  1.00 59.19  ? 25  GLY   F CA    1 
ATOM   11461 C  C     . GLY   E 4  25  ? 7.310   49.935  -61.714  1.00 61.37  ? 25  GLY   F C     1 
ATOM   11462 O  O     . GLY   E 4  25  ? 7.062   50.117  -60.514  1.00 63.89  ? 25  GLY   F O     1 
ATOM   11463 N  N     . GLN   E 4  26  ? 7.150   50.893  -62.633  1.00 66.46  ? 26  GLN   F N     1 
ATOM   11464 C  CA    . GLN   E 4  26  ? 6.713   52.247  -62.312  1.00 61.21  ? 26  GLN   F CA    1 
ATOM   11465 C  C     . GLN   E 4  26  ? 5.286   52.556  -62.762  1.00 61.55  ? 26  GLN   F C     1 
ATOM   11466 O  O     . GLN   E 4  26  ? 4.884   53.723  -62.728  1.00 62.04  ? 26  GLN   F O     1 
ATOM   11467 C  CB    . GLN   E 4  26  ? 7.651   53.269  -62.946  1.00 64.32  ? 26  GLN   F CB    1 
ATOM   11468 C  CG    . GLN   E 4  26  ? 9.094   53.238  -62.504  1.00 61.83  ? 26  GLN   F CG    1 
ATOM   11469 C  CD    . GLN   E 4  26  ? 9.837   54.461  -63.005  1.00 59.32  ? 26  GLN   F CD    1 
ATOM   11470 O  OE1   . GLN   E 4  26  ? 10.954  54.369  -63.504  1.00 64.44  ? 26  GLN   F OE1   1 
ATOM   11471 N  NE2   . GLN   E 4  26  ? 9.198   55.617  -62.899  1.00 64.08  ? 26  GLN   F NE2   1 
ATOM   11472 N  N     . TRP   E 4  27  ? 4.515   51.562  -63.199  1.00 58.31  ? 27  TRP   F N     1 
ATOM   11473 C  CA    . TRP   E 4  27  ? 3.162   51.801  -63.689  1.00 51.94  ? 27  TRP   F CA    1 
ATOM   11474 C  C     . TRP   E 4  27  ? 2.242   50.736  -63.134  1.00 55.77  ? 27  TRP   F C     1 
ATOM   11475 O  O     . TRP   E 4  27  ? 2.441   49.551  -63.408  1.00 62.87  ? 27  TRP   F O     1 
ATOM   11476 C  CB    . TRP   E 4  27  ? 3.111   51.795  -65.219  1.00 52.34  ? 27  TRP   F CB    1 
ATOM   11477 C  CG    . TRP   E 4  27  ? 3.485   53.100  -65.808  1.00 57.74  ? 27  TRP   F CG    1 
ATOM   11478 C  CD1   . TRP   E 4  27  ? 4.745   53.615  -65.941  1.00 59.62  ? 27  TRP   F CD1   1 
ATOM   11479 C  CD2   . TRP   E 4  27  ? 2.590   54.083  -66.337  1.00 56.37  ? 27  TRP   F CD2   1 
ATOM   11480 N  NE1   . TRP   E 4  27  ? 4.687   54.859  -66.527  1.00 56.64  ? 27  TRP   F NE1   1 
ATOM   11481 C  CE2   . TRP   E 4  27  ? 3.375   55.166  -66.780  1.00 50.40  ? 27  TRP   F CE2   1 
ATOM   11482 C  CE3   . TRP   E 4  27  ? 1.203   54.150  -66.479  1.00 51.54  ? 27  TRP   F CE3   1 
ATOM   11483 C  CZ2   . TRP   E 4  27  ? 2.819   56.295  -67.357  1.00 44.03  ? 27  TRP   F CZ2   1 
ATOM   11484 C  CZ3   . TRP   E 4  27  ? 0.658   55.262  -67.047  1.00 49.75  ? 27  TRP   F CZ3   1 
ATOM   11485 C  CH2   . TRP   E 4  27  ? 1.462   56.325  -67.484  1.00 50.52  ? 27  TRP   F CH2   1 
ATOM   11486 N  N     . LYS   E 4  28  ? 1.240   51.157  -62.368  1.00 58.93  ? 28  LYS   F N     1 
ATOM   11487 C  CA    . LYS   E 4  28  ? 0.214   50.278  -61.825  1.00 57.80  ? 28  LYS   F CA    1 
ATOM   11488 C  C     . LYS   E 4  28  ? -1.008  50.312  -62.738  1.00 54.34  ? 28  LYS   F C     1 
ATOM   11489 O  O     . LYS   E 4  28  ? -1.294  51.330  -63.369  1.00 62.03  ? 28  LYS   F O     1 
ATOM   11490 C  CB    . LYS   E 4  28  ? -0.153  50.712  -60.397  1.00 55.53  ? 28  LYS   F CB    1 
ATOM   11491 C  CG    . LYS   E 4  28  ? -1.196  49.845  -59.655  1.00 69.17  ? 28  LYS   F CG    1 
ATOM   11492 C  CD    . LYS   E 4  28  ? -1.348  50.282  -58.172  1.00 65.18  ? 28  LYS   F CD    1 
ATOM   11493 C  CE    . LYS   E 4  28  ? -2.253  49.354  -57.351  1.00 69.73  ? 28  LYS   F CE    1 
ATOM   11494 N  NZ    . LYS   E 4  28  ? -3.674  49.319  -57.830  1.00 67.25  ? 28  LYS   F NZ    1 
ATOM   11495 N  N     . ARG   E 4  29  ? -1.721  49.192  -62.823  1.00 58.89  ? 29  ARG   F N     1 
ATOM   11496 C  CA    . ARG   E 4  29  ? -2.947  49.100  -63.612  1.00 52.36  ? 29  ARG   F CA    1 
ATOM   11497 C  C     . ARG   E 4  29  ? -4.159  49.018  -62.690  1.00 50.08  ? 29  ARG   F C     1 
ATOM   11498 O  O     . ARG   E 4  29  ? -4.227  48.133  -61.835  1.00 57.40  ? 29  ARG   F O     1 
ATOM   11499 C  CB    . ARG   E 4  29  ? -2.917  47.885  -64.546  1.00 47.73  ? 29  ARG   F CB    1 
ATOM   11500 C  CG    . ARG   E 4  29  ? -4.271  47.639  -65.182  1.00 44.35  ? 29  ARG   F CG    1 
ATOM   11501 C  CD    . ARG   E 4  29  ? -4.287  46.533  -66.209  1.00 44.99  ? 29  ARG   F CD    1 
ATOM   11502 N  NE    . ARG   E 4  29  ? -5.644  46.349  -66.717  1.00 49.96  ? 29  ARG   F NE    1 
ATOM   11503 C  CZ    . ARG   E 4  29  ? -5.985  45.551  -67.718  1.00 48.97  ? 29  ARG   F CZ    1 
ATOM   11504 N  NH1   . ARG   E 4  29  ? -5.086  44.831  -68.364  1.00 62.86  ? 29  ARG   F NH1   1 
ATOM   11505 N  NH2   . ARG   E 4  29  ? -7.261  45.479  -68.084  1.00 51.51  ? 29  ARG   F NH2   1 
ATOM   11506 N  N     . LEU   E 4  30  ? -5.128  49.911  -62.891  1.00 49.72  ? 30  LEU   F N     1 
ATOM   11507 C  CA    . LEU   E 4  30  ? -6.288  50.059  -62.017  1.00 44.53  ? 30  LEU   F CA    1 
ATOM   11508 C  C     . LEU   E 4  30  ? -7.532  49.367  -62.582  1.00 48.16  ? 30  LEU   F C     1 
ATOM   11509 O  O     . LEU   E 4  30  ? -7.598  49.007  -63.762  1.00 41.94  ? 30  LEU   F O     1 
ATOM   11510 C  CB    . LEU   E 4  30  ? -6.598  51.544  -61.784  1.00 42.78  ? 30  LEU   F CB    1 
ATOM   11511 C  CG    . LEU   E 4  30  ? -5.455  52.485  -61.389  1.00 43.26  ? 30  LEU   F CG    1 
ATOM   11512 C  CD1   . LEU   E 4  30  ? -5.965  53.889  -61.108  1.00 39.08  ? 30  LEU   F CD1   1 
ATOM   11513 C  CD2   . LEU   E 4  30  ? -4.706  51.954  -60.190  1.00 48.34  ? 30  LEU   F CD2   1 
ATOM   11514 N  N     . ARG   E 4  31  ? -8.539  49.198  -61.706  1.00 52.05  ? 31  ARG   F N     1 
ATOM   11515 C  CA    . ARG   E 4  31  ? -9.862  48.752  -62.143  1.00 53.44  ? 31  ARG   F CA    1 
ATOM   11516 C  C     . ARG   E 4  31  ? -10.423 49.753  -63.145  1.00 54.76  ? 31  ARG   F C     1 
ATOM   11517 O  O     . ARG   E 4  31  ? -10.510 50.948  -62.852  1.00 55.96  ? 31  ARG   F O     1 
ATOM   11518 C  CB    . ARG   E 4  31  ? -10.836 48.623  -60.962  1.00 57.97  ? 31  ARG   F CB    1 
ATOM   11519 C  CG    . ARG   E 4  31  ? -10.401 47.786  -59.757  1.00 68.50  ? 31  ARG   F CG    1 
ATOM   11520 C  CD    . ARG   E 4  31  ? -10.355 46.282  -60.039  1.00 82.86  ? 31  ARG   F CD    1 
ATOM   11521 N  NE    . ARG   E 4  31  ? -11.666 45.643  -60.132  1.00 78.39  ? 31  ARG   F NE    1 
ATOM   11522 C  CZ    . ARG   E 4  31  ? -11.858 44.327  -60.123  1.00 88.38  ? 31  ARG   F CZ    1 
ATOM   11523 N  NH1   . ARG   E 4  31  ? -10.849 43.478  -59.989  1.00 86.94  ? 31  ARG   F NH1   1 
ATOM   11524 N  NH2   . ARG   E 4  31  ? -13.094 43.850  -60.249  1.00 88.39  ? 31  ARG   F NH2   1 
ATOM   11525 N  N     . LYS   E 4  32  ? -10.852 49.254  -64.308  1.00 55.11  ? 32  LYS   F N     1 
ATOM   11526 C  CA    . LYS   E 4  32  ? -11.111 50.122  -65.460  1.00 56.57  ? 32  LYS   F CA    1 
ATOM   11527 C  C     . LYS   E 4  32  ? -12.036 51.293  -65.139  1.00 53.30  ? 32  LYS   F C     1 
ATOM   11528 O  O     . LYS   E 4  32  ? -11.960 52.339  -65.797  1.00 61.69  ? 32  LYS   F O     1 
ATOM   11529 C  CB    . LYS   E 4  32  ? -11.686 49.303  -66.628  1.00 60.68  ? 32  LYS   F CB    1 
ATOM   11530 C  CG    . LYS   E 4  32  ? -13.117 48.801  -66.442  1.00 58.70  ? 32  LYS   F CG    1 
ATOM   11531 C  CD    . LYS   E 4  32  ? -13.528 47.884  -67.598  1.00 66.96  ? 32  LYS   F CD    1 
ATOM   11532 C  CE    . LYS   E 4  32  ? -13.329 48.559  -68.964  1.00 73.12  ? 32  LYS   F CE    1 
ATOM   11533 N  NZ    . LYS   E 4  32  ? -13.618 47.662  -70.140  1.00 70.73  ? 32  LYS   F NZ    1 
ATOM   11534 N  N     . ASP   E 4  33  ? -12.911 51.152  -64.149  1.00 51.64  ? 33  ASP   F N     1 
ATOM   11535 C  CA    . ASP   E 4  33  ? -13.786 52.247  -63.748  1.00 46.69  ? 33  ASP   F CA    1 
ATOM   11536 C  C     . ASP   E 4  33  ? -13.275 53.007  -62.531  1.00 48.58  ? 33  ASP   F C     1 
ATOM   11537 O  O     . ASP   E 4  33  ? -14.007 53.824  -61.957  1.00 49.93  ? 33  ASP   F O     1 
ATOM   11538 C  CB    . ASP   E 4  33  ? -15.194 51.720  -63.499  1.00 63.49  ? 33  ASP   F CB    1 
ATOM   11539 C  CG    . ASP   E 4  33  ? -16.113 52.008  -64.651  1.00 67.35  ? 33  ASP   F CG    1 
ATOM   11540 O  OD1   . ASP   E 4  33  ? -16.721 53.106  -64.651  1.00 55.97  ? 33  ASP   F OD1   1 
ATOM   11541 O  OD2   . ASP   E 4  33  ? -16.185 51.152  -65.567  1.00 63.97  ? 33  ASP   F OD2   1 
ATOM   11542 N  N     . ASN   E 4  34  ? -12.044 52.760  -62.124  1.00 55.05  ? 34  ASN   F N     1 
ATOM   11543 C  CA    . ASN   E 4  34  ? -11.410 53.612  -61.138  1.00 50.89  ? 34  ASN   F CA    1 
ATOM   11544 C  C     . ASN   E 4  34  ? -10.927 54.883  -61.826  1.00 52.50  ? 34  ASN   F C     1 
ATOM   11545 O  O     . ASN   E 4  34  ? -10.068 54.804  -62.712  1.00 58.57  ? 34  ASN   F O     1 
ATOM   11546 C  CB    . ASN   E 4  34  ? -10.250 52.889  -60.486  1.00 42.31  ? 34  ASN   F CB    1 
ATOM   11547 C  CG    . ASN   E 4  34  ? -9.432  53.797  -59.611  1.00 43.58  ? 34  ASN   F CG    1 
ATOM   11548 O  OD1   . ASN   E 4  34  ? -9.874  54.885  -59.243  1.00 51.38  ? 34  ASN   F OD1   1 
ATOM   11549 N  ND2   . ASN   E 4  34  ? -8.235  53.358  -59.262  1.00 47.36  ? 34  ASN   F ND2   1 
ATOM   11550 N  N     . PRO   E 4  35  ? -11.436 56.060  -61.458  1.00 45.26  ? 35  PRO   F N     1 
ATOM   11551 C  CA    . PRO   E 4  35  ? -11.114 57.282  -62.201  1.00 41.65  ? 35  PRO   F CA    1 
ATOM   11552 C  C     . PRO   E 4  35  ? -9.782  57.916  -61.821  1.00 45.34  ? 35  PRO   F C     1 
ATOM   11553 O  O     . PRO   E 4  35  ? -9.536  59.077  -62.160  1.00 37.62  ? 35  PRO   F O     1 
ATOM   11554 C  CB    . PRO   E 4  35  ? -12.280 58.204  -61.806  1.00 37.34  ? 35  PRO   F CB    1 
ATOM   11555 C  CG    . PRO   E 4  35  ? -12.537 57.844  -60.365  1.00 30.70  ? 35  PRO   F CG    1 
ATOM   11556 C  CD    . PRO   E 4  35  ? -12.143 56.371  -60.200  1.00 46.17  ? 35  PRO   F CD    1 
ATOM   11557 N  N     . ARG   E 4  36  ? -8.929  57.234  -61.077  1.00 45.64  ? 36  ARG   F N     1 
ATOM   11558 C  CA    . ARG   E 4  36  ? -7.740  57.931  -60.626  1.00 40.31  ? 36  ARG   F CA    1 
ATOM   11559 C  C     . ARG   E 4  36  ? -6.542  57.432  -61.416  1.00 46.21  ? 36  ARG   F C     1 
ATOM   11560 O  O     . ARG   E 4  36  ? -5.574  56.924  -60.839  1.00 53.88  ? 36  ARG   F O     1 
ATOM   11561 C  CB    . ARG   E 4  36  ? -7.577  57.763  -59.118  1.00 41.76  ? 36  ARG   F CB    1 
ATOM   11562 C  CG    . ARG   E 4  36  ? -8.769  58.327  -58.348  1.00 40.88  ? 36  ARG   F CG    1 
ATOM   11563 C  CD    . ARG   E 4  36  ? -8.526  58.361  -56.854  1.00 53.07  ? 36  ARG   F CD    1 
ATOM   11564 N  NE    . ARG   E 4  36  ? -9.465  59.253  -56.185  1.00 39.92  ? 36  ARG   F NE    1 
ATOM   11565 C  CZ    . ARG   E 4  36  ? -9.382  60.573  -56.236  1.00 40.69  ? 36  ARG   F CZ    1 
ATOM   11566 N  NH1   . ARG   E 4  36  ? -8.388  61.176  -56.867  1.00 56.03  ? 36  ARG   F NH1   1 
ATOM   11567 N  NH2   . ARG   E 4  36  ? -10.333 61.307  -55.664  1.00 38.89  ? 36  ARG   F NH2   1 
ATOM   11568 N  N     . PHE   E 4  37  ? -6.612  57.589  -62.742  1.00 38.11  ? 37  PHE   F N     1 
ATOM   11569 C  CA    . PHE   E 4  37  ? -5.581  57.176  -63.684  1.00 47.50  ? 37  PHE   F CA    1 
ATOM   11570 C  C     . PHE   E 4  37  ? -4.885  58.387  -64.311  1.00 49.06  ? 37  PHE   F C     1 
ATOM   11571 O  O     . PHE   E 4  37  ? -5.441  59.490  -64.397  1.00 40.53  ? 37  PHE   F O     1 
ATOM   11572 C  CB    . PHE   E 4  37  ? -6.192  56.322  -64.800  1.00 44.79  ? 37  PHE   F CB    1 
ATOM   11573 C  CG    . PHE   E 4  37  ? -7.286  57.028  -65.547  1.00 43.80  ? 37  PHE   F CG    1 
ATOM   11574 C  CD1   . PHE   E 4  37  ? -6.983  57.941  -66.549  1.00 35.56  ? 37  PHE   F CD1   1 
ATOM   11575 C  CD2   . PHE   E 4  37  ? -8.621  56.810  -65.219  1.00 48.71  ? 37  PHE   F CD2   1 
ATOM   11576 C  CE1   . PHE   E 4  37  ? -7.984  58.616  -67.223  1.00 37.51  ? 37  PHE   F CE1   1 
ATOM   11577 C  CE2   . PHE   E 4  37  ? -9.639  57.479  -65.897  1.00 44.42  ? 37  PHE   F CE2   1 
ATOM   11578 C  CZ    . PHE   E 4  37  ? -9.313  58.386  -66.905  1.00 43.37  ? 37  PHE   F CZ    1 
ATOM   11579 N  N     . ASN   E 4  38  ? -3.654  58.159  -64.772  1.00 43.49  ? 38  ASN   F N     1 
ATOM   11580 C  CA    . ASN   E 4  38  ? -3.002  59.100  -65.672  1.00 39.69  ? 38  ASN   F CA    1 
ATOM   11581 C  C     . ASN   E 4  38  ? -3.256  58.730  -67.122  1.00 45.98  ? 38  ASN   F C     1 
ATOM   11582 O  O     . ASN   E 4  38  ? -3.501  59.606  -67.964  1.00 47.33  ? 38  ASN   F O     1 
ATOM   11583 C  CB    . ASN   E 4  38  ? -1.490  59.134  -65.431  1.00 41.84  ? 38  ASN   F CB    1 
ATOM   11584 C  CG    . ASN   E 4  38  ? -1.134  59.374  -63.995  1.00 37.12  ? 38  ASN   F CG    1 
ATOM   11585 O  OD1   . ASN   E 4  38  ? -0.621  58.482  -63.320  1.00 52.05  ? 38  ASN   F OD1   1 
ATOM   11586 N  ND2   . ASN   E 4  38  ? -1.399  60.580  -63.511  1.00 31.53  ? 38  ASN   F ND2   1 
ATOM   11587 N  N     . LEU   E 4  39  ? -3.202  57.439  -67.423  1.00 40.73  ? 39  LEU   F N     1 
ATOM   11588 C  CA    . LEU   E 4  39  ? -3.339  56.942  -68.778  1.00 40.59  ? 39  LEU   F CA    1 
ATOM   11589 C  C     . LEU   E 4  39  ? -4.653  56.189  -68.909  1.00 43.17  ? 39  LEU   F C     1 
ATOM   11590 O  O     . LEU   E 4  39  ? -4.946  55.295  -68.106  1.00 47.56  ? 39  LEU   F O     1 
ATOM   11591 C  CB    . LEU   E 4  39  ? -2.161  56.038  -69.140  1.00 36.58  ? 39  LEU   F CB    1 
ATOM   11592 C  CG    . LEU   E 4  39  ? -2.172  55.576  -70.597  1.00 45.54  ? 39  LEU   F CG    1 
ATOM   11593 C  CD1   . LEU   E 4  39  ? -2.211  56.784  -71.531  1.00 38.40  ? 39  LEU   F CD1   1 
ATOM   11594 C  CD2   . LEU   E 4  39  ? -0.969  54.687  -70.913  1.00 45.30  ? 39  LEU   F CD2   1 
ATOM   11595 N  N     . MET   E 4  40  ? -5.453  56.569  -69.890  1.00 35.04  ? 40  MET   F N     1 
ATOM   11596 C  CA    . MET   E 4  40  ? -6.580  55.758  -70.317  1.00 35.48  ? 40  MET   F CA    1 
ATOM   11597 C  C     . MET   E 4  40  ? -6.234  55.247  -71.703  1.00 44.84  ? 40  MET   F C     1 
ATOM   11598 O  O     . MET   E 4  40  ? -6.198  56.023  -72.666  1.00 44.47  ? 40  MET   F O     1 
ATOM   11599 C  CB    . MET   E 4  40  ? -7.894  56.540  -70.321  1.00 35.73  ? 40  MET   F CB    1 
ATOM   11600 C  CG    . MET   E 4  40  ? -9.063  55.829  -71.013  1.00 33.67  ? 40  MET   F CG    1 
ATOM   11601 S  SD    . MET   E 4  40  ? -10.616 56.785  -70.959  1.00 37.53  ? 40  MET   F SD    1 
ATOM   11602 C  CE    . MET   E 4  40  ? -11.174 56.437  -69.301  1.00 30.87  ? 40  MET   F CE    1 
ATOM   11603 N  N     . LEU   E 4  41  ? -5.920  53.957  -71.788  1.00 41.82  ? 41  LEU   F N     1 
ATOM   11604 C  CA    . LEU   E 4  41  ? -6.036  53.227  -73.042  1.00 39.62  ? 41  LEU   F CA    1 
ATOM   11605 C  C     . LEU   E 4  41  ? -7.523  52.956  -73.251  1.00 41.91  ? 41  LEU   F C     1 
ATOM   11606 O  O     . LEU   E 4  41  ? -8.119  52.135  -72.547  1.00 49.00  ? 41  LEU   F O     1 
ATOM   11607 C  CB    . LEU   E 4  41  ? -5.201  51.956  -72.976  1.00 40.10  ? 41  LEU   F CB    1 
ATOM   11608 C  CG    . LEU   E 4  41  ? -3.850  52.290  -72.325  1.00 44.15  ? 41  LEU   F CG    1 
ATOM   11609 C  CD1   . LEU   E 4  41  ? -2.931  51.068  -72.205  1.00 50.85  ? 41  LEU   F CD1   1 
ATOM   11610 C  CD2   . LEU   E 4  41  ? -3.130  53.421  -73.051  1.00 33.35  ? 41  LEU   F CD2   1 
ATOM   11611 N  N     . GLY   E 4  42  ? -8.132  53.672  -74.187  1.00 41.81  ? 42  GLY   F N     1 
ATOM   11612 C  CA    . GLY   E 4  42  ? -9.560  53.889  -74.172  1.00 39.46  ? 42  GLY   F CA    1 
ATOM   11613 C  C     . GLY   E 4  42  ? -10.352 52.967  -75.066  1.00 45.16  ? 42  GLY   F C     1 
ATOM   11614 O  O     . GLY   E 4  42  ? -9.839  52.397  -76.025  1.00 51.06  ? 42  GLY   F O     1 
ATOM   11615 N  N     . GLU   E 4  43  ? -11.633 52.826  -74.734  1.00 51.00  ? 43  GLU   F N     1 
ATOM   11616 C  CA    . GLU   E 4  43  ? -12.494 51.985  -75.545  1.00 50.01  ? 43  GLU   F CA    1 
ATOM   11617 C  C     . GLU   E 4  43  ? -12.585 52.554  -76.963  1.00 50.17  ? 43  GLU   F C     1 
ATOM   11618 O  O     . GLU   E 4  43  ? -12.159 53.675  -77.247  1.00 40.90  ? 43  GLU   F O     1 
ATOM   11619 C  CB    . GLU   E 4  43  ? -13.874 51.831  -74.898  1.00 38.70  ? 43  GLU   F CB    1 
ATOM   11620 C  CG    . GLU   E 4  43  ? -14.685 53.092  -74.711  1.00 33.97  ? 43  GLU   F CG    1 
ATOM   11621 C  CD    . GLU   E 4  43  ? -14.807 53.498  -73.263  1.00 42.33  ? 43  GLU   F CD    1 
ATOM   11622 O  OE1   . GLU   E 4  43  ? -13.750 53.772  -72.659  1.00 40.50  ? 43  GLU   F OE1   1 
ATOM   11623 O  OE2   . GLU   E 4  43  ? -15.948 53.535  -72.728  1.00 41.03  ? 43  GLU   F OE2   1 
ATOM   11624 N  N     . ARG   E 4  44  ? -13.129 51.741  -77.869  1.00 61.34  ? 44  ARG   F N     1 
ATOM   11625 C  CA    . ARG   E 4  44  ? -13.053 52.068  -79.290  1.00 66.83  ? 44  ARG   F CA    1 
ATOM   11626 C  C     . ARG   E 4  44  ? -14.163 53.006  -79.725  1.00 51.22  ? 44  ARG   F C     1 
ATOM   11627 O  O     . ARG   E 4  44  ? -13.974 53.782  -80.665  1.00 61.23  ? 44  ARG   F O     1 
ATOM   11628 C  CB    . ARG   E 4  44  ? -13.089 50.793  -80.137  1.00 65.89  ? 44  ARG   F CB    1 
ATOM   11629 C  CG    . ARG   E 4  44  ? -11.717 50.294  -80.553  1.00 62.87  ? 44  ARG   F CG    1 
ATOM   11630 C  CD    . ARG   E 4  44  ? -11.579 50.260  -82.072  1.00 75.00  ? 44  ARG   F CD    1 
ATOM   11631 N  NE    . ARG   E 4  44  ? -11.857 48.946  -82.650  1.00 82.44  ? 44  ARG   F NE    1 
ATOM   11632 C  CZ    . ARG   E 4  44  ? -11.710 48.649  -83.937  1.00 86.92  ? 44  ARG   F CZ    1 
ATOM   11633 N  NH1   . ARG   E 4  44  ? -11.322 49.562  -84.817  1.00 85.01  ? 44  ARG   F NH1   1 
ATOM   11634 N  NH2   . ARG   E 4  44  ? -11.955 47.407  -84.353  1.00 73.98  ? 44  ARG   F NH2   1 
ATOM   11635 N  N     . ASN   E 4  45  ? -15.306 52.962  -79.063  1.00 50.03  ? 45  ASN   F N     1 
ATOM   11636 C  CA    . ASN   E 4  45  ? -16.437 53.767  -79.478  1.00 54.53  ? 45  ASN   F CA    1 
ATOM   11637 C  C     . ASN   E 4  45  ? -17.114 54.349  -78.244  1.00 57.46  ? 45  ASN   F C     1 
ATOM   11638 O  O     . ASN   E 4  45  ? -17.204 53.689  -77.208  1.00 52.53  ? 45  ASN   F O     1 
ATOM   11639 C  CB    . ASN   E 4  45  ? -17.408 52.931  -80.315  1.00 67.65  ? 45  ASN   F CB    1 
ATOM   11640 C  CG    . ASN   E 4  45  ? -18.554 53.748  -80.855  1.00 84.33  ? 45  ASN   F CG    1 
ATOM   11641 O  OD1   . ASN   E 4  45  ? -19.701 53.585  -80.422  1.00 84.42  ? 45  ASN   F OD1   1 
ATOM   11642 N  ND2   . ASN   E 4  45  ? -18.254 54.653  -81.795  1.00 75.11  ? 45  ASN   F ND2   1 
ATOM   11643 N  N     . ARG   E 4  46  ? -17.580 55.595  -78.361  1.00 60.68  ? 46  ARG   F N     1 
ATOM   11644 C  CA    . ARG   E 4  46  ? -18.158 56.338  -77.241  1.00 48.00  ? 46  ARG   F CA    1 
ATOM   11645 C  C     . ARG   E 4  46  ? -17.195 56.380  -76.057  1.00 52.11  ? 46  ARG   F C     1 
ATOM   11646 O  O     . ARG   E 4  46  ? -17.597 56.318  -74.892  1.00 50.49  ? 46  ARG   F O     1 
ATOM   11647 C  CB    . ARG   E 4  46  ? -19.513 55.767  -76.825  1.00 58.60  ? 46  ARG   F CB    1 
ATOM   11648 C  CG    . ARG   E 4  46  ? -20.095 54.753  -77.799  1.00 70.58  ? 46  ARG   F CG    1 
ATOM   11649 C  CD    . ARG   E 4  46  ? -21.606 54.652  -77.687  1.00 77.43  ? 46  ARG   F CD    1 
ATOM   11650 N  NE    . ARG   E 4  46  ? -22.276 55.783  -78.319  1.00 80.90  ? 46  ARG   F NE    1 
ATOM   11651 C  CZ    . ARG   E 4  46  ? -22.669 56.875  -77.678  1.00 85.98  ? 46  ARG   F CZ    1 
ATOM   11652 N  NH1   . ARG   E 4  46  ? -22.484 57.015  -76.375  1.00 95.26  ? 46  ARG   F NH1   1 
ATOM   11653 N  NH2   . ARG   E 4  46  ? -23.263 57.851  -78.363  1.00 76.03  ? 46  ARG   F NH2   1 
ATOM   11654 N  N     . LEU   E 4  47  ? -15.904 56.480  -76.360  1.00 50.31  ? 47  LEU   F N     1 
ATOM   11655 C  CA    . LEU   E 4  47  ? -14.932 56.810  -75.333  1.00 40.31  ? 47  LEU   F CA    1 
ATOM   11656 C  C     . LEU   E 4  47  ? -15.396 58.069  -74.608  1.00 42.79  ? 47  LEU   F C     1 
ATOM   11657 O  O     . LEU   E 4  47  ? -15.726 59.067  -75.265  1.00 40.96  ? 47  LEU   F O     1 
ATOM   11658 C  CB    . LEU   E 4  47  ? -13.548 57.021  -75.951  1.00 35.08  ? 47  LEU   F CB    1 
ATOM   11659 C  CG    . LEU   E 4  47  ? -12.329 57.114  -75.043  1.00 38.35  ? 47  LEU   F CG    1 
ATOM   11660 C  CD1   . LEU   E 4  47  ? -11.068 56.865  -75.835  1.00 36.19  ? 47  LEU   F CD1   1 
ATOM   11661 C  CD2   . LEU   E 4  47  ? -12.268 58.482  -74.367  1.00 37.42  ? 47  LEU   F CD2   1 
ATOM   11662 N  N     . PRO   E 4  48  ? -15.454 58.060  -73.278  1.00 42.08  ? 48  PRO   F N     1 
ATOM   11663 C  CA    . PRO   E 4  48  ? -16.093 59.158  -72.516  1.00 34.37  ? 48  PRO   F CA    1 
ATOM   11664 C  C     . PRO   E 4  48  ? -15.176 60.362  -72.331  1.00 33.78  ? 48  PRO   F C     1 
ATOM   11665 O  O     . PRO   E 4  48  ? -14.695 60.685  -71.233  1.00 38.34  ? 48  PRO   F O     1 
ATOM   11666 C  CB    . PRO   E 4  48  ? -16.434 58.471  -71.191  1.00 35.68  ? 48  PRO   F CB    1 
ATOM   11667 C  CG    . PRO   E 4  48  ? -15.278 57.483  -71.017  1.00 42.02  ? 48  PRO   F CG    1 
ATOM   11668 C  CD    . PRO   E 4  48  ? -14.895 57.019  -72.398  1.00 35.52  ? 48  PRO   F CD    1 
ATOM   11669 N  N     . PHE   E 4  49  ? -14.935 61.075  -73.430  1.00 34.48  ? 49  PHE   F N     1 
ATOM   11670 C  CA    . PHE   E 4  49  ? -13.925 62.127  -73.424  1.00 27.66  ? 49  PHE   F CA    1 
ATOM   11671 C  C     . PHE   E 4  49  ? -14.242 63.185  -72.390  1.00 31.45  ? 49  PHE   F C     1 
ATOM   11672 O  O     . PHE   E 4  49  ? -13.349 63.660  -71.682  1.00 37.65  ? 49  PHE   F O     1 
ATOM   11673 C  CB    . PHE   E 4  49  ? -13.813 62.756  -74.817  1.00 33.39  ? 49  PHE   F CB    1 
ATOM   11674 C  CG    . PHE   E 4  49  ? -12.981 61.957  -75.777  1.00 31.47  ? 49  PHE   F CG    1 
ATOM   11675 C  CD1   . PHE   E 4  49  ? -11.599 61.992  -75.710  1.00 29.95  ? 49  PHE   F CD1   1 
ATOM   11676 C  CD2   . PHE   E 4  49  ? -13.578 61.165  -76.744  1.00 29.94  ? 49  PHE   F CD2   1 
ATOM   11677 C  CE1   . PHE   E 4  49  ? -10.823 61.249  -76.609  1.00 39.24  ? 49  PHE   F CE1   1 
ATOM   11678 C  CE2   . PHE   E 4  49  ? -12.813 60.424  -77.646  1.00 30.94  ? 49  PHE   F CE2   1 
ATOM   11679 C  CZ    . PHE   E 4  49  ? -11.435 60.465  -77.582  1.00 33.88  ? 49  PHE   F CZ    1 
ATOM   11680 N  N     . GLY   E 4  50  ? -15.513 63.565  -72.282  1.00 38.57  ? 50  GLY   F N     1 
ATOM   11681 C  CA    . GLY   E 4  50  ? -15.929 64.593  -71.343  1.00 26.70  ? 50  GLY   F CA    1 
ATOM   11682 C  C     . GLY   E 4  50  ? -15.649 64.280  -69.897  1.00 29.77  ? 50  GLY   F C     1 
ATOM   11683 O  O     . GLY   E 4  50  ? -15.795 65.178  -69.059  1.00 37.29  ? 50  GLY   F O     1 
ATOM   11684 N  N     . ARG   E 4  51  ? -15.254 63.043  -69.575  1.00 32.50  ? 51  ARG   F N     1 
ATOM   11685 C  CA    . ARG   E 4  51  ? -14.880 62.705  -68.207  1.00 37.64  ? 51  ARG   F CA    1 
ATOM   11686 C  C     . ARG   E 4  51  ? -13.407 62.965  -67.896  1.00 32.91  ? 51  ARG   F C     1 
ATOM   11687 O  O     . ARG   E 4  51  ? -13.006 62.874  -66.732  1.00 38.34  ? 51  ARG   F O     1 
ATOM   11688 C  CB    . ARG   E 4  51  ? -15.219 61.234  -67.904  1.00 36.66  ? 51  ARG   F CB    1 
ATOM   11689 C  CG    . ARG   E 4  51  ? -16.725 60.940  -67.869  1.00 49.10  ? 51  ARG   F CG    1 
ATOM   11690 C  CD    . ARG   E 4  51  ? -17.129 59.891  -66.817  1.00 49.00  ? 51  ARG   F CD    1 
ATOM   11691 N  NE    . ARG   E 4  51  ? -16.687 58.531  -67.118  1.00 51.27  ? 51  ARG   F NE    1 
ATOM   11692 C  CZ    . ARG   E 4  51  ? -17.392 57.646  -67.812  1.00 44.53  ? 51  ARG   F CZ    1 
ATOM   11693 N  NH1   . ARG   E 4  51  ? -18.560 57.959  -68.348  1.00 43.76  ? 51  ARG   F NH1   1 
ATOM   11694 N  NH2   . ARG   E 4  51  ? -16.913 56.417  -67.973  1.00 42.15  ? 51  ARG   F NH2   1 
ATOM   11695 N  N     . LEU   E 4  52  ? -12.596 63.292  -68.887  1.00 33.75  ? 52  LEU   F N     1 
ATOM   11696 C  CA    . LEU   E 4  52  ? -11.155 63.365  -68.706  1.00 30.86  ? 52  LEU   F CA    1 
ATOM   11697 C  C     . LEU   E 4  52  ? -10.761 64.768  -68.260  1.00 33.13  ? 52  LEU   F C     1 
ATOM   11698 O  O     . LEU   E 4  52  ? -11.486 65.738  -68.496  1.00 36.89  ? 52  LEU   F O     1 
ATOM   11699 C  CB    . LEU   E 4  52  ? -10.438 62.974  -70.004  1.00 28.85  ? 52  LEU   F CB    1 
ATOM   11700 C  CG    . LEU   E 4  52  ? -11.012 61.709  -70.648  1.00 32.18  ? 52  LEU   F CG    1 
ATOM   11701 C  CD1   . LEU   E 4  52  ? -10.507 61.489  -72.062  1.00 29.59  ? 52  LEU   F CD1   1 
ATOM   11702 C  CD2   . LEU   E 4  52  ? -10.734 60.484  -69.771  1.00 33.58  ? 52  LEU   F CD2   1 
ATOM   11703 N  N     . GLY   E 4  53  ? -9.625  64.861  -67.568  1.00 30.85  ? 53  GLY   F N     1 
ATOM   11704 C  CA    . GLY   E 4  53  ? -9.172  66.145  -67.050  1.00 29.91  ? 53  GLY   F CA    1 
ATOM   11705 C  C     . GLY   E 4  53  ? -10.082 66.817  -66.037  1.00 32.09  ? 53  GLY   F C     1 
ATOM   11706 O  O     . GLY   E 4  53  ? -10.130 68.048  -65.999  1.00 44.23  ? 53  GLY   F O     1 
ATOM   11707 N  N     . HIS   E 4  54  ? -10.801 66.057  -65.206  1.00 31.70  ? 54  HIS   F N     1 
ATOM   11708 C  CA    . HIS   E 4  54  ? -11.486 66.666  -64.064  1.00 42.76  ? 54  HIS   F CA    1 
ATOM   11709 C  C     . HIS   E 4  54  ? -11.123 66.002  -62.732  1.00 41.94  ? 54  HIS   F C     1 
ATOM   11710 O  O     . HIS   E 4  54  ? -11.939 65.995  -61.801  1.00 40.33  ? 54  HIS   F O     1 
ATOM   11711 C  CB    . HIS   E 4  54  ? -13.000 66.633  -64.232  1.00 29.63  ? 54  HIS   F CB    1 
ATOM   11712 C  CG    . HIS   E 4  54  ? -13.500 67.382  -65.418  1.00 37.52  ? 54  HIS   F CG    1 
ATOM   11713 N  ND1   . HIS   E 4  54  ? -13.862 68.710  -65.357  1.00 32.81  ? 54  HIS   F ND1   1 
ATOM   11714 C  CD2   . HIS   E 4  54  ? -13.747 66.976  -66.687  1.00 28.92  ? 54  HIS   F CD2   1 
ATOM   11715 C  CE1   . HIS   E 4  54  ? -14.295 69.091  -66.545  1.00 34.99  ? 54  HIS   F CE1   1 
ATOM   11716 N  NE2   . HIS   E 4  54  ? -14.248 68.054  -67.365  1.00 27.66  ? 54  HIS   F NE2   1 
ATOM   11717 N  N     . GLU   E 4  55  ? -9.923  65.426  -62.627  1.00 37.76  ? 55  GLU   F N     1 
ATOM   11718 C  CA    . GLU   E 4  55  ? -9.451  64.749  -61.420  1.00 34.49  ? 55  GLU   F CA    1 
ATOM   11719 C  C     . GLU   E 4  55  ? -8.294  65.557  -60.875  1.00 39.00  ? 55  GLU   F C     1 
ATOM   11720 O  O     . GLU   E 4  55  ? -7.144  65.373  -61.303  1.00 48.69  ? 55  GLU   F O     1 
ATOM   11721 C  CB    . GLU   E 4  55  ? -9.001  63.317  -61.715  1.00 38.03  ? 55  GLU   F CB    1 
ATOM   11722 C  CG    . GLU   E 4  55  ? -10.123 62.335  -61.914  1.00 43.72  ? 55  GLU   F CG    1 
ATOM   11723 C  CD    . GLU   E 4  55  ? -11.077 62.302  -60.739  1.00 45.56  ? 55  GLU   F CD    1 
ATOM   11724 O  OE1   . GLU   E 4  55  ? -10.798 62.982  -59.722  1.00 48.23  ? 55  GLU   F OE1   1 
ATOM   11725 O  OE2   . GLU   E 4  55  ? -12.112 61.600  -60.838  1.00 56.81  ? 55  GLU   F OE2   1 
ATOM   11726 N  N     . PRO   E 4  56  ? -8.526  66.476  -59.956  1.00 37.51  ? 56  PRO   F N     1 
ATOM   11727 C  CA    . PRO   E 4  56  ? -7.402  67.283  -59.461  1.00 39.25  ? 56  PRO   F CA    1 
ATOM   11728 C  C     . PRO   E 4  56  ? -6.313  66.379  -58.876  1.00 39.58  ? 56  PRO   F C     1 
ATOM   11729 O  O     . PRO   E 4  56  ? -6.590  65.317  -58.310  1.00 42.62  ? 56  PRO   F O     1 
ATOM   11730 C  CB    . PRO   E 4  56  ? -8.048  68.204  -58.414  1.00 30.14  ? 56  PRO   F CB    1 
ATOM   11731 C  CG    . PRO   E 4  56  ? -9.379  67.579  -58.095  1.00 36.21  ? 56  PRO   F CG    1 
ATOM   11732 C  CD    . PRO   E 4  56  ? -9.809  66.799  -59.312  1.00 31.56  ? 56  PRO   F CD    1 
ATOM   11733 N  N     . GLY   E 4  57  ? -5.062  66.784  -59.067  1.00 38.03  ? 57  GLY   F N     1 
ATOM   11734 C  CA    . GLY   E 4  57  ? -3.919  65.991  -58.682  1.00 34.41  ? 57  GLY   F CA    1 
ATOM   11735 C  C     . GLY   E 4  57  ? -3.370  65.106  -59.775  1.00 38.62  ? 57  GLY   F C     1 
ATOM   11736 O  O     . GLY   E 4  57  ? -2.250  64.599  -59.642  1.00 46.52  ? 57  GLY   F O     1 
ATOM   11737 N  N     . LEU   E 4  58  ? -4.114  64.917  -60.853  1.00 39.02  ? 58  LEU   F N     1 
ATOM   11738 C  CA    . LEU   E 4  58  ? -3.782  63.966  -61.904  1.00 41.27  ? 58  LEU   F CA    1 
ATOM   11739 C  C     . LEU   E 4  58  ? -3.659  64.686  -63.239  1.00 32.34  ? 58  LEU   F C     1 
ATOM   11740 O  O     . LEU   E 4  58  ? -4.568  65.423  -63.635  1.00 31.02  ? 58  LEU   F O     1 
ATOM   11741 C  CB    . LEU   E 4  58  ? -4.855  62.886  -62.016  1.00 35.68  ? 58  LEU   F CB    1 
ATOM   11742 C  CG    . LEU   E 4  58  ? -4.946  61.859  -60.899  1.00 44.68  ? 58  LEU   F CG    1 
ATOM   11743 C  CD1   . LEU   E 4  58  ? -6.021  60.827  -61.239  1.00 37.04  ? 58  LEU   F CD1   1 
ATOM   11744 C  CD2   . LEU   E 4  58  ? -3.589  61.196  -60.679  1.00 44.39  ? 58  LEU   F CD2   1 
ATOM   11745 N  N     . VAL   E 4  59  ? -2.518  64.512  -63.900  1.00 29.27  ? 59  VAL   F N     1 
ATOM   11746 C  CA    . VAL   E 4  59  ? -2.423  64.750  -65.331  1.00 23.93  ? 59  VAL   F CA    1 
ATOM   11747 C  C     . VAL   E 4  59  ? -3.011  63.527  -66.001  1.00 31.26  ? 59  VAL   F C     1 
ATOM   11748 O  O     . VAL   E 4  59  ? -2.731  62.398  -65.582  1.00 36.34  ? 59  VAL   F O     1 
ATOM   11749 C  CB    . VAL   E 4  59  ? -0.966  64.968  -65.765  1.00 27.05  ? 59  VAL   F CB    1 
ATOM   11750 C  CG1   . VAL   E 4  59  ? -0.847  64.850  -67.274  1.00 26.50  ? 59  VAL   F CG1   1 
ATOM   11751 C  CG2   . VAL   E 4  59  ? -0.432  66.299  -65.281  1.00 22.31  ? 59  VAL   F CG2   1 
ATOM   11752 N  N     . GLN   E 4  60  ? -3.855  63.736  -67.005  1.00 25.18  ? 60  GLN   F N     1 
ATOM   11753 C  CA    . GLN   E 4  60  ? -4.519  62.619  -67.658  1.00 30.34  ? 60  GLN   F CA    1 
ATOM   11754 C  C     . GLN   E 4  60  ? -4.303  62.653  -69.163  1.00 31.87  ? 60  GLN   F C     1 
ATOM   11755 O  O     . GLN   E 4  60  ? -4.395  63.706  -69.805  1.00 33.30  ? 60  GLN   F O     1 
ATOM   11756 C  CB    . GLN   E 4  60  ? -6.007  62.594  -67.343  1.00 24.71  ? 60  GLN   F CB    1 
ATOM   11757 C  CG    . GLN   E 4  60  ? -6.323  62.246  -65.906  1.00 28.05  ? 60  GLN   F CG    1 
ATOM   11758 C  CD    . GLN   E 4  60  ? -7.819  62.040  -65.693  1.00 36.51  ? 60  GLN   F CD    1 
ATOM   11759 O  OE1   . GLN   E 4  60  ? -8.629  62.907  -66.051  1.00 30.76  ? 60  GLN   F OE1   1 
ATOM   11760 N  NE2   . GLN   E 4  60  ? -8.196  60.877  -65.147  1.00 30.10  ? 60  GLN   F NE2   1 
ATOM   11761 N  N     . LEU   E 4  61  ? -4.037  61.473  -69.711  1.00 37.49  ? 61  LEU   F N     1 
ATOM   11762 C  CA    . LEU   E 4  61  ? -3.670  61.271  -71.100  1.00 32.20  ? 61  LEU   F CA    1 
ATOM   11763 C  C     . LEU   E 4  61  ? -4.458  60.079  -71.625  1.00 35.42  ? 61  LEU   F C     1 
ATOM   11764 O  O     . LEU   E 4  61  ? -4.616  59.080  -70.917  1.00 44.08  ? 61  LEU   F O     1 
ATOM   11765 C  CB    . LEU   E 4  61  ? -2.159  61.033  -71.216  1.00 31.71  ? 61  LEU   F CB    1 
ATOM   11766 C  CG    . LEU   E 4  61  ? -1.616  60.747  -72.621  1.00 45.98  ? 61  LEU   F CG    1 
ATOM   11767 C  CD1   . LEU   E 4  61  ? -1.843  61.933  -73.578  1.00 36.59  ? 61  LEU   F CD1   1 
ATOM   11768 C  CD2   . LEU   E 4  61  ? -0.135  60.375  -72.532  1.00 38.21  ? 61  LEU   F CD2   1 
ATOM   11769 N  N     . VAL   E 4  62  ? -4.986  60.195  -72.840  1.00 27.99  ? 62  VAL   F N     1 
ATOM   11770 C  CA    . VAL   E 4  62  ? -5.757  59.122  -73.446  1.00 32.37  ? 62  VAL   F CA    1 
ATOM   11771 C  C     . VAL   E 4  62  ? -5.259  58.922  -74.871  1.00 38.53  ? 62  VAL   F C     1 
ATOM   11772 O  O     . VAL   E 4  62  ? -4.681  59.830  -75.485  1.00 38.60  ? 62  VAL   F O     1 
ATOM   11773 C  CB    . VAL   E 4  62  ? -7.285  59.390  -73.400  1.00 36.25  ? 62  VAL   F CB    1 
ATOM   11774 C  CG1   . VAL   E 4  62  ? -7.639  60.704  -74.085  1.00 28.55  ? 62  VAL   F CG1   1 
ATOM   11775 C  CG2   . VAL   E 4  62  ? -8.058  58.215  -73.995  1.00 34.67  ? 62  VAL   F CG2   1 
ATOM   11776 N  N     . ASN   E 4  63  ? -5.456  57.707  -75.384  1.00 38.97  ? 63  ASN   F N     1 
ATOM   11777 C  CA    . ASN   E 4  63  ? -4.846  57.255  -76.631  1.00 39.21  ? 63  ASN   F CA    1 
ATOM   11778 C  C     . ASN   E 4  63  ? -5.783  57.384  -77.839  1.00 37.46  ? 63  ASN   F C     1 
ATOM   11779 O  O     . ASN   E 4  63  ? -5.624  56.665  -78.832  1.00 40.42  ? 63  ASN   F O     1 
ATOM   11780 C  CB    . ASN   E 4  63  ? -4.344  55.819  -76.476  1.00 41.60  ? 63  ASN   F CB    1 
ATOM   11781 C  CG    . ASN   E 4  63  ? -5.470  54.804  -76.305  1.00 43.99  ? 63  ASN   F CG    1 
ATOM   11782 O  OD1   . ASN   E 4  63  ? -6.625  55.162  -76.051  1.00 33.70  ? 63  ASN   F OD1   1 
ATOM   11783 N  ND2   . ASN   E 4  63  ? -5.124  53.516  -76.435  1.00 43.81  ? 63  ASN   F ND2   1 
ATOM   11784 N  N     . TYR   E 4  64  ? -6.735  58.312  -77.785  1.00 30.84  ? 64  TYR   F N     1 
ATOM   11785 C  CA    . TYR   E 4  64  ? -7.454  58.742  -78.968  1.00 34.30  ? 64  TYR   F CA    1 
ATOM   11786 C  C     . TYR   E 4  64  ? -7.578  60.255  -78.968  1.00 36.95  ? 64  TYR   F C     1 
ATOM   11787 O  O     . TYR   E 4  64  ? -7.593  60.890  -77.910  1.00 31.68  ? 64  TYR   F O     1 
ATOM   11788 C  CB    . TYR   E 4  64  ? -8.837  58.102  -79.064  1.00 32.37  ? 64  TYR   F CB    1 
ATOM   11789 C  CG    . TYR   E 4  64  ? -8.719  56.639  -79.338  1.00 39.93  ? 64  TYR   F CG    1 
ATOM   11790 C  CD1   . TYR   E 4  64  ? -8.661  56.160  -80.646  1.00 38.26  ? 64  TYR   F CD1   1 
ATOM   11791 C  CD2   . TYR   E 4  64  ? -8.609  55.729  -78.291  1.00 40.74  ? 64  TYR   F CD2   1 
ATOM   11792 C  CE1   . TYR   E 4  64  ? -8.517  54.796  -80.905  1.00 46.14  ? 64  TYR   F CE1   1 
ATOM   11793 C  CE2   . TYR   E 4  64  ? -8.474  54.362  -78.538  1.00 44.14  ? 64  TYR   F CE2   1 
ATOM   11794 C  CZ    . TYR   E 4  64  ? -8.427  53.903  -79.844  1.00 44.61  ? 64  TYR   F CZ    1 
ATOM   11795 O  OH    . TYR   E 4  64  ? -8.291  52.556  -80.083  1.00 54.49  ? 64  TYR   F OH    1 
ATOM   11796 N  N     . TYR   E 4  65  ? -7.631  60.821  -80.184  1.00 36.26  ? 65  TYR   F N     1 
ATOM   11797 C  CA    . TYR   E 4  65  ? -7.988  62.219  -80.422  1.00 31.50  ? 65  TYR   F CA    1 
ATOM   11798 C  C     . TYR   E 4  65  ? -9.471  62.288  -80.748  1.00 33.26  ? 65  TYR   F C     1 
ATOM   11799 O  O     . TYR   E 4  65  ? -9.885  61.996  -81.872  1.00 33.74  ? 65  TYR   F O     1 
ATOM   11800 C  CB    . TYR   E 4  65  ? -7.187  62.821  -81.570  1.00 29.76  ? 65  TYR   F CB    1 
ATOM   11801 C  CG    . TYR   E 4  65  ? -5.875  63.452  -81.198  1.00 29.53  ? 65  TYR   F CG    1 
ATOM   11802 C  CD1   . TYR   E 4  65  ? -5.809  64.766  -80.758  1.00 31.82  ? 65  TYR   F CD1   1 
ATOM   11803 C  CD2   . TYR   E 4  65  ? -4.695  62.747  -81.327  1.00 30.04  ? 65  TYR   F CD2   1 
ATOM   11804 C  CE1   . TYR   E 4  65  ? -4.594  65.343  -80.446  1.00 39.07  ? 65  TYR   F CE1   1 
ATOM   11805 C  CE2   . TYR   E 4  65  ? -3.485  63.311  -81.012  1.00 30.40  ? 65  TYR   F CE2   1 
ATOM   11806 C  CZ    . TYR   E 4  65  ? -3.432  64.600  -80.584  1.00 33.73  ? 65  TYR   F CZ    1 
ATOM   11807 O  OH    . TYR   E 4  65  ? -2.210  65.136  -80.279  1.00 34.70  ? 65  TYR   F OH    1 
ATOM   11808 N  N     . ARG   E 4  66  ? -10.273 62.695  -79.772  1.00 35.28  ? 66  ARG   F N     1 
ATOM   11809 C  CA    . ARG   E 4  66  ? -11.654 63.044  -80.053  1.00 33.23  ? 66  ARG   F CA    1 
ATOM   11810 C  C     . ARG   E 4  66  ? -11.749 63.875  -81.326  1.00 36.54  ? 66  ARG   F C     1 
ATOM   11811 O  O     . ARG   E 4  66  ? -11.047 64.877  -81.487  1.00 31.64  ? 66  ARG   F O     1 
ATOM   11812 C  CB    . ARG   E 4  66  ? -12.234 63.819  -78.883  1.00 31.96  ? 66  ARG   F CB    1 
ATOM   11813 C  CG    . ARG   E 4  66  ? -13.630 64.322  -79.107  1.00 30.23  ? 66  ARG   F CG    1 
ATOM   11814 C  CD    . ARG   E 4  66  ? -14.036 65.049  -77.857  1.00 36.31  ? 66  ARG   F CD    1 
ATOM   11815 N  NE    . ARG   E 4  66  ? -15.453 64.966  -77.550  1.00 31.62  ? 66  ARG   F NE    1 
ATOM   11816 C  CZ    . ARG   E 4  66  ? -16.030 65.740  -76.646  1.00 30.52  ? 66  ARG   F CZ    1 
ATOM   11817 N  NH1   . ARG   E 4  66  ? -15.334 66.655  -75.987  1.00 23.45  ? 66  ARG   F NH1   1 
ATOM   11818 N  NH2   . ARG   E 4  66  ? -17.335 65.596  -76.400  1.00 25.61  ? 66  ARG   F NH2   1 
ATOM   11819 N  N     . GLY   E 4  67  ? -12.627 63.448  -82.232  1.00 43.19  ? 67  GLY   F N     1 
ATOM   11820 C  CA    . GLY   E 4  67  ? -12.824 64.120  -83.489  1.00 30.26  ? 67  GLY   F CA    1 
ATOM   11821 C  C     . GLY   E 4  67  ? -11.934 63.624  -84.593  1.00 37.31  ? 67  GLY   F C     1 
ATOM   11822 O  O     . GLY   E 4  67  ? -12.083 64.071  -85.732  1.00 42.75  ? 67  GLY   F O     1 
ATOM   11823 N  N     . ALA   E 4  68  ? -10.998 62.727  -84.293  1.00 40.04  ? 68  ALA   F N     1 
ATOM   11824 C  CA    . ALA   E 4  68  ? -10.193 62.121  -85.344  1.00 43.17  ? 68  ALA   F CA    1 
ATOM   11825 C  C     . ALA   E 4  68  ? -10.945 61.031  -86.085  1.00 46.45  ? 68  ALA   F C     1 
ATOM   11826 O  O     . ALA   E 4  68  ? -10.354 60.372  -86.948  1.00 48.14  ? 68  ALA   F O     1 
ATOM   11827 C  CB    . ALA   E 4  68  ? -8.886  61.566  -84.781  1.00 32.18  ? 68  ALA   F CB    1 
ATOM   11828 N  N     . ASP   E 4  69  ? -12.230 60.830  -85.773  1.00 44.27  ? 69  ASP   F N     1 
ATOM   11829 C  CA    . ASP   E 4  69  ? -13.065 59.978  -86.618  1.00 53.64  ? 69  ASP   F CA    1 
ATOM   11830 C  C     . ASP   E 4  69  ? -13.324 60.636  -87.964  1.00 53.21  ? 69  ASP   F C     1 
ATOM   11831 O  O     . ASP   E 4  69  ? -13.573 59.943  -88.954  1.00 57.44  ? 69  ASP   F O     1 
ATOM   11832 C  CB    . ASP   E 4  69  ? -14.395 59.660  -85.924  1.00 34.43  ? 69  ASP   F CB    1 
ATOM   11833 C  CG    . ASP   E 4  69  ? -15.007 60.882  -85.268  1.00 50.87  ? 69  ASP   F CG    1 
ATOM   11834 O  OD1   . ASP   E 4  69  ? -14.544 61.264  -84.170  1.00 53.86  ? 69  ASP   F OD1   1 
ATOM   11835 O  OD2   . ASP   E 4  69  ? -15.924 61.490  -85.863  1.00 56.86  ? 69  ASP   F OD2   1 
ATOM   11836 N  N     . LYS   E 4  70  ? -13.289 61.970  -88.008  1.00 50.29  ? 70  LYS   F N     1 
ATOM   11837 C  CA    . LYS   E 4  70  ? -13.403 62.687  -89.271  1.00 54.90  ? 70  LYS   F CA    1 
ATOM   11838 C  C     . LYS   E 4  70  ? -12.487 62.086  -90.331  1.00 52.99  ? 70  LYS   F C     1 
ATOM   11839 O  O     . LYS   E 4  70  ? -12.868 61.952  -91.496  1.00 51.75  ? 70  LYS   F O     1 
ATOM   11840 C  CB    . LYS   E 4  70  ? -13.052 64.164  -89.054  1.00 62.60  ? 70  LYS   F CB    1 
ATOM   11841 C  CG    . LYS   E 4  70  ? -14.198 65.163  -89.136  1.00 61.91  ? 70  LYS   F CG    1 
ATOM   11842 C  CD    . LYS   E 4  70  ? -13.646 66.571  -89.445  1.00 67.91  ? 70  LYS   F CD    1 
ATOM   11843 C  CE    . LYS   E 4  70  ? -12.796 67.157  -88.293  1.00 50.60  ? 70  LYS   F CE    1 
ATOM   11844 N  NZ    . LYS   E 4  70  ? -13.659 67.792  -87.245  1.00 62.24  ? 70  LYS   F NZ    1 
ATOM   11845 N  N     . LEU   E 4  71  ? -11.269 61.723  -89.937  1.00 57.43  ? 71  LEU   F N     1 
ATOM   11846 C  CA    . LEU   E 4  71  ? -10.238 61.235  -90.844  1.00 55.31  ? 71  LEU   F CA    1 
ATOM   11847 C  C     . LEU   E 4  71  ? -10.323 59.737  -91.103  1.00 56.40  ? 71  LEU   F C     1 
ATOM   11848 O  O     . LEU   E 4  71  ? -9.786  59.266  -92.118  1.00 58.72  ? 71  LEU   F O     1 
ATOM   11849 C  CB    . LEU   E 4  71  ? -8.862  61.557  -90.252  1.00 43.45  ? 71  LEU   F CB    1 
ATOM   11850 C  CG    . LEU   E 4  71  ? -7.618  61.792  -91.078  1.00 41.93  ? 71  LEU   F CG    1 
ATOM   11851 C  CD1   . LEU   E 4  71  ? -7.909  62.765  -92.185  1.00 47.49  ? 71  LEU   F CD1   1 
ATOM   11852 C  CD2   . LEU   E 4  71  ? -6.596  62.382  -90.144  1.00 44.92  ? 71  LEU   F CD2   1 
ATOM   11853 N  N     . CYS   E 4  72  ? -10.981 58.985  -90.212  1.00 53.55  ? 72  CYS   F N     1 
ATOM   11854 C  CA    . CYS   E 4  72  ? -10.882 57.532  -90.165  1.00 48.59  ? 72  CYS   F CA    1 
ATOM   11855 C  C     . CYS   E 4  72  ? -12.194 56.819  -90.492  1.00 48.85  ? 72  CYS   F C     1 
ATOM   11856 O  O     . CYS   E 4  72  ? -12.276 55.598  -90.328  1.00 47.79  ? 72  CYS   F O     1 
ATOM   11857 C  CB    . CYS   E 4  72  ? -10.373 57.092  -88.789  1.00 47.43  ? 72  CYS   F CB    1 
ATOM   11858 S  SG    . CYS   E 4  72  ? -8.781  57.844  -88.272  1.00 47.67  ? 72  CYS   F SG    1 
ATOM   11859 N  N     . ARG   E 4  73  ? -13.214 57.544  -90.947  1.00 44.19  ? 73  ARG   F N     1 
ATOM   11860 C  CA    . ARG   E 4  73  ? -14.447 56.956  -91.455  1.00 56.89  ? 73  ARG   F CA    1 
ATOM   11861 C  C     . ARG   E 4  73  ? -14.516 57.190  -92.959  1.00 59.93  ? 73  ARG   F C     1 
ATOM   11862 O  O     . ARG   E 4  73  ? -14.274 58.310  -93.430  1.00 55.06  ? 73  ARG   F O     1 
ATOM   11863 C  CB    . ARG   E 4  73  ? -15.683 57.551  -90.767  1.00 59.95  ? 73  ARG   F CB    1 
ATOM   11864 C  CG    . ARG   E 4  73  ? -15.968 57.035  -89.353  1.00 59.10  ? 73  ARG   F CG    1 
ATOM   11865 C  CD    . ARG   E 4  73  ? -17.211 57.720  -88.742  1.00 75.68  ? 73  ARG   F CD    1 
ATOM   11866 N  NE    . ARG   E 4  73  ? -18.464 57.179  -89.268  1.00 92.83  ? 73  ARG   F NE    1 
ATOM   11867 C  CZ    . ARG   E 4  73  ? -19.681 57.520  -88.856  1.00 84.75  ? 73  ARG   F CZ    1 
ATOM   11868 N  NH1   . ARG   E 4  73  ? -19.870 58.448  -87.928  1.00 78.06  ? 73  ARG   F NH1   1 
ATOM   11869 N  NH2   . ARG   E 4  73  ? -20.738 56.910  -89.388  1.00 76.16  ? 73  ARG   F NH2   1 
ATOM   11870 N  N     . LYS   E 4  74  ? -14.847 56.136  -93.711  1.00 56.39  ? 74  LYS   F N     1 
ATOM   11871 C  CA    . LYS   E 4  74  ? -14.793 56.231  -95.166  1.00 55.94  ? 74  LYS   F CA    1 
ATOM   11872 C  C     . LYS   E 4  74  ? -15.737 57.297  -95.703  1.00 57.58  ? 74  LYS   F C     1 
ATOM   11873 O  O     . LYS   E 4  74  ? -15.460 57.899  -96.744  1.00 62.36  ? 74  LYS   F O     1 
ATOM   11874 C  CB    . LYS   E 4  74  ? -15.097 54.867  -95.792  1.00 57.48  ? 74  LYS   F CB    1 
ATOM   11875 C  CG    . LYS   E 4  74  ? -14.123 53.796  -95.317  1.00 66.46  ? 74  LYS   F CG    1 
ATOM   11876 C  CD    . LYS   E 4  74  ? -14.139 52.539  -96.162  1.00 61.47  ? 74  LYS   F CD    1 
ATOM   11877 C  CE    . LYS   E 4  74  ? -13.199 51.509  -95.560  1.00 65.22  ? 74  LYS   F CE    1 
ATOM   11878 N  NZ    . LYS   E 4  74  ? -11.849 52.087  -95.297  1.00 62.61  ? 74  LYS   F NZ    1 
ATOM   11879 N  N     . ALA   E 4  75  ? -16.846 57.554  -95.014  1.00 56.27  ? 75  ALA   F N     1 
ATOM   11880 C  CA    . ALA   E 4  75  ? -17.742 58.619  -95.450  1.00 62.47  ? 75  ALA   F CA    1 
ATOM   11881 C  C     . ALA   E 4  75  ? -17.189 59.998  -95.097  1.00 58.43  ? 75  ALA   F C     1 
ATOM   11882 O  O     . ALA   E 4  75  ? -17.230 60.924  -95.916  1.00 50.09  ? 75  ALA   F O     1 
ATOM   11883 C  CB    . ALA   E 4  75  ? -19.127 58.425  -94.826  1.00 66.61  ? 75  ALA   F CB    1 
ATOM   11884 N  N     . SER   E 4  76  ? -16.675 60.152  -93.879  1.00 61.36  ? 76  SER   F N     1 
ATOM   11885 C  CA    . SER   E 4  76  ? -16.171 61.449  -93.456  1.00 54.38  ? 76  SER   F CA    1 
ATOM   11886 C  C     . SER   E 4  76  ? -14.866 61.803  -94.163  1.00 55.10  ? 76  SER   F C     1 
ATOM   11887 O  O     . SER   E 4  76  ? -14.675 62.963  -94.548  1.00 54.98  ? 76  SER   F O     1 
ATOM   11888 C  CB    . SER   E 4  76  ? -16.002 61.471  -91.938  1.00 55.93  ? 76  SER   F CB    1 
ATOM   11889 O  OG    . SER   E 4  76  ? -17.170 61.986  -91.322  1.00 68.49  ? 76  SER   F OG    1 
ATOM   11890 N  N     . LEU   E 4  77  ? -13.959 60.829  -94.359  1.00 42.88  ? 77  LEU   F N     1 
ATOM   11891 C  CA    . LEU   E 4  77  ? -12.697 61.147  -95.027  1.00 49.05  ? 77  LEU   F CA    1 
ATOM   11892 C  C     . LEU   E 4  77  ? -12.946 61.829  -96.362  1.00 52.96  ? 77  LEU   F C     1 
ATOM   11893 O  O     . LEU   E 4  77  ? -12.367 62.881  -96.657  1.00 50.48  ? 77  LEU   F O     1 
ATOM   11894 C  CB    . LEU   E 4  77  ? -11.833 59.902  -95.244  1.00 53.01  ? 77  LEU   F CB    1 
ATOM   11895 C  CG    . LEU   E 4  77  ? -10.620 60.267  -96.129  1.00 48.95  ? 77  LEU   F CG    1 
ATOM   11896 C  CD1   . LEU   E 4  77  ? -9.840  61.394  -95.511  1.00 46.50  ? 77  LEU   F CD1   1 
ATOM   11897 C  CD2   . LEU   E 4  77  ? -9.685  59.105  -96.414  1.00 38.34  ? 77  LEU   F CD2   1 
ATOM   11898 N  N     . VAL   E 4  78  ? -13.812 61.238  -97.185  1.00 51.13  ? 78  VAL   F N     1 
ATOM   11899 C  CA    . VAL   E 4  78  ? -14.183 61.857  -98.456  1.00 50.96  ? 78  VAL   F CA    1 
ATOM   11900 C  C     . VAL   E 4  78  ? -14.639 63.296  -98.241  1.00 56.46  ? 78  VAL   F C     1 
ATOM   11901 O  O     . VAL   E 4  78  ? -14.105 64.239  -98.839  1.00 56.10  ? 78  VAL   F O     1 
ATOM   11902 C  CB    . VAL   E 4  78  ? -15.274 61.030  -99.152  1.00 57.39  ? 78  VAL   F CB    1 
ATOM   11903 C  CG1   . VAL   E 4  78  ? -15.855 61.815  -100.341 1.00 56.66  ? 78  VAL   F CG1   1 
ATOM   11904 C  CG2   . VAL   E 4  78  ? -14.706 59.678  -99.565  1.00 57.41  ? 78  VAL   F CG2   1 
ATOM   11905 N  N     . LYS   E 4  79  ? -15.657 63.479  -97.398  1.00 63.62  ? 79  LYS   F N     1 
ATOM   11906 C  CA    . LYS   E 4  79  ? -16.181 64.819  -97.172  1.00 62.88  ? 79  LYS   F CA    1 
ATOM   11907 C  C     . LYS   E 4  79  ? -15.129 65.719  -96.540  1.00 55.80  ? 79  LYS   F C     1 
ATOM   11908 O  O     . LYS   E 4  79  ? -15.174 66.945  -96.704  1.00 58.96  ? 79  LYS   F O     1 
ATOM   11909 C  CB    . LYS   E 4  79  ? -17.440 64.751  -96.303  1.00 61.31  ? 79  LYS   F CB    1 
ATOM   11910 C  CG    . LYS   E 4  79  ? -18.008 66.118  -95.931  1.00 69.36  ? 79  LYS   F CG    1 
ATOM   11911 C  CD    . LYS   E 4  79  ? -19.225 65.997  -95.026  1.00 74.17  ? 79  LYS   F CD    1 
ATOM   11912 C  CE    . LYS   E 4  79  ? -19.494 67.298  -94.284  1.00 64.18  ? 79  LYS   F CE    1 
ATOM   11913 N  NZ    . LYS   E 4  79  ? -19.805 68.420  -95.206  1.00 66.41  ? 79  LYS   F NZ    1 
ATOM   11914 N  N     . LEU   E 4  80  ? -14.164 65.137  -95.831  1.00 41.82  ? 80  LEU   F N     1 
ATOM   11915 C  CA    . LEU   E 4  80  ? -13.117 65.958  -95.235  1.00 50.26  ? 80  LEU   F CA    1 
ATOM   11916 C  C     . LEU   E 4  80  ? -12.301 66.644  -96.316  1.00 58.44  ? 80  LEU   F C     1 
ATOM   11917 O  O     . LEU   E 4  80  ? -12.059 67.854  -96.253  1.00 56.61  ? 80  LEU   F O     1 
ATOM   11918 C  CB    . LEU   E 4  80  ? -12.213 65.108  -94.342  1.00 46.76  ? 80  LEU   F CB    1 
ATOM   11919 C  CG    . LEU   E 4  80  ? -11.038 65.868  -93.734  1.00 48.79  ? 80  LEU   F CG    1 
ATOM   11920 C  CD1   . LEU   E 4  80  ? -11.556 66.998  -92.870  1.00 44.12  ? 80  LEU   F CD1   1 
ATOM   11921 C  CD2   . LEU   E 4  80  ? -10.118 64.943  -92.938  1.00 50.94  ? 80  LEU   F CD2   1 
ATOM   11922 N  N     . ILE   E 4  81  ? -11.896 65.874  -97.332  1.00 55.43  ? 81  ILE   F N     1 
ATOM   11923 C  CA    . ILE   E 4  81  ? -11.021 66.369  -98.389  1.00 56.49  ? 81  ILE   F CA    1 
ATOM   11924 C  C     . ILE   E 4  81  ? -11.782 67.308  -99.315  1.00 60.37  ? 81  ILE   F C     1 
ATOM   11925 O  O     . ILE   E 4  81  ? -11.292 68.382  -99.672  1.00 62.70  ? 81  ILE   F O     1 
ATOM   11926 C  CB    . ILE   E 4  81  ? -10.410 65.188  -99.164  1.00 58.23  ? 81  ILE   F CB    1 
ATOM   11927 C  CG1   . ILE   E 4  81  ? -9.724  64.218  -98.193  1.00 53.89  ? 81  ILE   F CG1   1 
ATOM   11928 C  CG2   . ILE   E 4  81  ? -9.432  65.692  -100.218 1.00 56.04  ? 81  ILE   F CG2   1 
ATOM   11929 C  CD1   . ILE   E 4  81  ? -9.477  62.836  -98.734  1.00 47.06  ? 81  ILE   F CD1   1 
ATOM   11930 N  N     . LYS   E 4  82  ? -12.994 66.918  -99.712  1.00 64.08  ? 82  LYS   F N     1 
ATOM   11931 C  CA    . LYS   E 4  82  ? -13.764 67.753  -100.629 1.00 65.10  ? 82  LYS   F CA    1 
ATOM   11932 C  C     . LYS   E 4  82  ? -13.998 69.145  -100.050 1.00 69.35  ? 82  LYS   F C     1 
ATOM   11933 O  O     . LYS   E 4  82  ? -13.831 70.152  -100.751 1.00 74.10  ? 82  LYS   F O     1 
ATOM   11934 C  CB    . LYS   E 4  82  ? -15.097 67.075  -100.968 1.00 67.49  ? 82  LYS   F CB    1 
ATOM   11935 C  CG    . LYS   E 4  82  ? -15.013 65.964  -102.023 1.00 63.27  ? 82  LYS   F CG    1 
ATOM   11936 C  CD    . LYS   E 4  82  ? -16.356 65.238  -102.208 1.00 68.01  ? 82  LYS   F CD    1 
ATOM   11937 C  CE    . LYS   E 4  82  ? -16.407 64.404  -103.490 1.00 60.89  ? 82  LYS   F CE    1 
ATOM   11938 N  NZ    . LYS   E 4  82  ? -16.374 65.255  -104.723 1.00 70.63  ? 82  LYS   F NZ    1 
ATOM   11939 N  N     . THR   E 4  83  ? -14.363 69.228  -98.768  1.00 66.32  ? 83  THR   F N     1 
ATOM   11940 C  CA    . THR   E 4  83  ? -14.872 70.463  -98.181  1.00 69.10  ? 83  THR   F CA    1 
ATOM   11941 C  C     . THR   E 4  83  ? -13.849 71.173  -97.303  1.00 67.55  ? 83  THR   F C     1 
ATOM   11942 O  O     . THR   E 4  83  ? -14.226 71.938  -96.412  1.00 74.61  ? 83  THR   F O     1 
ATOM   11943 C  CB    . THR   E 4  83  ? -16.128 70.185  -97.360  1.00 64.42  ? 83  THR   F CB    1 
ATOM   11944 O  OG1   . THR   E 4  83  ? -15.753 70.047  -95.989  1.00 53.73  ? 83  THR   F OG1   1 
ATOM   11945 C  CG2   . THR   E 4  83  ? -16.809 68.903  -97.828  1.00 65.97  ? 83  THR   F CG2   1 
ATOM   11946 N  N     . SER   E 4  84  ? -12.561 70.956  -97.538  1.00 62.26  ? 84  SER   F N     1 
ATOM   11947 C  CA    . SER   E 4  84  ? -11.523 71.448  -96.640  1.00 53.00  ? 84  SER   F CA    1 
ATOM   11948 C  C     . SER   E 4  84  ? -10.424 72.091  -97.471  1.00 65.22  ? 84  SER   F C     1 
ATOM   11949 O  O     . SER   E 4  84  ? -9.519  71.391  -97.955  1.00 67.92  ? 84  SER   F O     1 
ATOM   11950 C  CB    . SER   E 4  84  ? -10.987 70.307  -95.787  1.00 62.45  ? 84  SER   F CB    1 
ATOM   11951 O  OG    . SER   E 4  84  ? -10.351 70.776  -94.616  1.00 75.81  ? 84  SER   F OG    1 
ATOM   11952 N  N     . PRO   E 4  85  ? -10.448 73.411  -97.635  1.00 71.56  ? 85  PRO   F N     1 
ATOM   11953 C  CA    . PRO   E 4  85  ? -9.574  74.053  -98.630  1.00 65.52  ? 85  PRO   F CA    1 
ATOM   11954 C  C     . PRO   E 4  85  ? -8.125  73.616  -98.585  1.00 68.15  ? 85  PRO   F C     1 
ATOM   11955 O  O     . PRO   E 4  85  ? -7.453  73.680  -99.620  1.00 73.81  ? 85  PRO   F O     1 
ATOM   11956 C  CB    . PRO   E 4  85  ? -9.713  75.549  -98.307  1.00 70.10  ? 85  PRO   F CB    1 
ATOM   11957 C  CG    . PRO   E 4  85  ? -10.323 75.604  -96.934  1.00 77.71  ? 85  PRO   F CG    1 
ATOM   11958 C  CD    . PRO   E 4  85  ? -11.189 74.395  -96.833  1.00 73.50  ? 85  PRO   F CD    1 
ATOM   11959 N  N     . GLU   E 4  86  ? -7.605  73.186  -97.430  1.00 72.28  ? 86  GLU   F N     1 
ATOM   11960 C  CA    . GLU   E 4  86  ? -6.199  72.783  -97.380  1.00 63.87  ? 86  GLU   F CA    1 
ATOM   11961 C  C     . GLU   E 4  86  ? -5.946  71.565  -98.247  1.00 65.79  ? 86  GLU   F C     1 
ATOM   11962 O  O     . GLU   E 4  86  ? -4.856  71.415  -98.804  1.00 58.61  ? 86  GLU   F O     1 
ATOM   11963 C  CB    . GLU   E 4  86  ? -5.762  72.491  -95.947  1.00 64.20  ? 86  GLU   F CB    1 
ATOM   11964 C  CG    . GLU   E 4  86  ? -6.023  73.612  -94.962  1.00 65.45  ? 86  GLU   F CG    1 
ATOM   11965 C  CD    . GLU   E 4  86  ? -7.414  73.538  -94.373  1.00 69.41  ? 86  GLU   F CD    1 
ATOM   11966 O  OE1   . GLU   E 4  86  ? -8.349  74.165  -94.921  1.00 73.84  ? 86  GLU   F OE1   1 
ATOM   11967 O  OE2   . GLU   E 4  86  ? -7.572  72.830  -93.360  1.00 82.14  ? 86  GLU   F OE2   1 
ATOM   11968 N  N     . LEU   E 4  87  ? -6.934  70.678  -98.350  1.00 73.65  ? 87  LEU   F N     1 
ATOM   11969 C  CA    . LEU   E 4  87  ? -6.898  69.539  -99.255  1.00 65.23  ? 87  LEU   F CA    1 
ATOM   11970 C  C     . LEU   E 4  87  ? -7.710  69.850  -100.505 1.00 76.01  ? 87  LEU   F C     1 
ATOM   11971 O  O     . LEU   E 4  87  ? -7.150  70.181  -101.556 1.00 80.76  ? 87  LEU   F O     1 
ATOM   11972 C  CB    . LEU   E 4  87  ? -7.448  68.298  -98.562  1.00 61.62  ? 87  LEU   F CB    1 
ATOM   11973 C  CG    . LEU   E 4  87  ? -7.020  68.063  -97.114  1.00 57.24  ? 87  LEU   F CG    1 
ATOM   11974 C  CD1   . LEU   E 4  87  ? -7.805  66.898  -96.562  1.00 48.92  ? 87  LEU   F CD1   1 
ATOM   11975 C  CD2   . LEU   E 4  87  ? -5.537  67.802  -97.006  1.00 42.27  ? 87  LEU   F CD2   1 
ATOM   11976 N  N     . SER   E 4  88  ? -9.034  69.740  -100.389 1.00 73.93  ? 88  SER   F N     1 
ATOM   11977 C  CA    . SER   E 4  88  ? -9.963  70.174  -101.426 1.00 77.42  ? 88  SER   F CA    1 
ATOM   11978 C  C     . SER   E 4  88  ? -9.507  69.750  -102.809 1.00 88.99  ? 88  SER   F C     1 
ATOM   11979 O  O     . SER   E 4  88  ? -9.353  68.556  -103.089 1.00 90.82  ? 88  SER   F O     1 
ATOM   11980 C  CB    . SER   E 4  88  ? -10.106 71.694  -101.414 1.00 92.69  ? 88  SER   F CB    1 
ATOM   11981 O  OG    . SER   E 4  88  ? -9.097  72.286  -102.228 1.00 90.90  ? 88  SER   F OG    1 
ATOM   11982 N  N     . GLU   E 4  89  ? -9.302  70.749  -103.674 1.00 97.00  ? 89  GLU   F N     1 
ATOM   11983 C  CA    . GLU   E 4  89  ? -8.674  70.582  -104.978 1.00 97.36  ? 89  GLU   F CA    1 
ATOM   11984 C  C     . GLU   E 4  89  ? -7.260  71.148  -104.996 1.00 100.76 ? 89  GLU   F C     1 
ATOM   11985 O  O     . GLU   E 4  89  ? -6.756  71.532  -106.058 1.00 103.36 ? 89  GLU   F O     1 
ATOM   11986 C  CB    . GLU   E 4  89  ? -9.529  71.210  -106.081 1.00 97.69  ? 89  GLU   F CB    1 
ATOM   11987 C  CG    . GLU   E 4  89  ? -10.843 70.467  -106.298 1.00 104.00 ? 89  GLU   F CG    1 
ATOM   11988 C  CD    . GLU   E 4  89  ? -10.851 69.085  -105.646 1.00 83.11  ? 89  GLU   F CD    1 
ATOM   11989 O  OE1   . GLU   E 4  89  ? -9.894  68.312  -105.881 1.00 67.82  ? 89  GLU   F OE1   1 
ATOM   11990 O  OE2   . GLU   E 4  89  ? -11.807 68.788  -104.887 1.00 74.85  ? 89  GLU   F OE2   1 
ATOM   11991 N  N     . SER   E 4  90  ? -6.636  71.254  -103.823 1.00 95.88  ? 90  SER   F N     1 
ATOM   11992 C  CA    . SER   E 4  90  ? -5.193  71.110  -103.704 1.00 99.35  ? 90  SER   F CA    1 
ATOM   11993 C  C     . SER   E 4  90  ? -4.780  69.637  -103.757 1.00 98.07  ? 90  SER   F C     1 
ATOM   11994 O  O     . SER   E 4  90  ? -3.612  69.317  -103.495 1.00 94.54  ? 90  SER   F O     1 
ATOM   11995 C  CB    . SER   E 4  90  ? -4.696  71.751  -102.396 1.00 86.93  ? 90  SER   F CB    1 
ATOM   11996 O  OG    . SER   E 4  90  ? -4.038  72.997  -102.597 1.00 61.46  ? 90  SER   F OG    1 
ATOM   11997 N  N     . CYS   E 4  91  ? -5.716  68.742  -104.104 1.00 91.52  ? 91  CYS   F N     1 
ATOM   11998 C  CA    . CYS   E 4  91  ? -5.576  67.311  -103.862 1.00 84.89  ? 91  CYS   F CA    1 
ATOM   11999 C  C     . CYS   E 4  91  ? -5.329  66.556  -105.158 1.00 72.09  ? 91  CYS   F C     1 
ATOM   12000 O  O     . CYS   E 4  91  ? -6.203  66.504  -106.029 1.00 69.08  ? 91  CYS   F O     1 
ATOM   12001 C  CB    . CYS   E 4  91  ? -6.806  66.744  -103.159 1.00 71.51  ? 91  CYS   F CB    1 
ATOM   12002 S  SG    . CYS   E 4  91  ? -6.347  65.329  -102.141 1.00 77.07  ? 91  CYS   F SG    1 
ATOM   12003 N  N     . THR   E 4  92  ? -4.147  65.945  -105.253 1.00 58.63  ? 92  THR   F N     1 
ATOM   12004 C  CA    . THR   E 4  92  ? -3.738  65.119  -106.374 1.00 54.38  ? 92  THR   F CA    1 
ATOM   12005 C  C     . THR   E 4  92  ? -3.578  63.645  -105.992 1.00 55.16  ? 92  THR   F C     1 
ATOM   12006 O  O     . THR   E 4  92  ? -3.296  62.816  -106.867 1.00 47.30  ? 92  THR   F O     1 
ATOM   12007 C  CB    . THR   E 4  92  ? -2.419  65.663  -106.962 1.00 47.78  ? 92  THR   F CB    1 
ATOM   12008 O  OG1   . THR   E 4  92  ? -1.286  65.117  -106.268 1.00 51.79  ? 92  THR   F OG1   1 
ATOM   12009 C  CG2   . THR   E 4  92  ? -2.354  67.157  -106.807 1.00 50.06  ? 92  THR   F CG2   1 
ATOM   12010 N  N     . TRP   E 4  93  ? -3.772  63.293  -104.715 1.00 51.80  ? 93  TRP   F N     1 
ATOM   12011 C  CA    . TRP   E 4  93  ? -3.373  61.989  -104.192 1.00 51.14  ? 93  TRP   F CA    1 
ATOM   12012 C  C     . TRP   E 4  93  ? -4.523  61.190  -103.578 1.00 46.55  ? 93  TRP   F C     1 
ATOM   12013 O  O     . TRP   E 4  93  ? -4.274  60.138  -102.969 1.00 44.51  ? 93  TRP   F O     1 
ATOM   12014 C  CB    . TRP   E 4  93  ? -2.238  62.153  -103.166 1.00 49.01  ? 93  TRP   F CB    1 
ATOM   12015 C  CG    . TRP   E 4  93  ? -2.451  63.297  -102.186 1.00 59.85  ? 93  TRP   F CG    1 
ATOM   12016 C  CD1   . TRP   E 4  93  ? -1.798  64.501  -102.172 1.00 52.39  ? 93  TRP   F CD1   1 
ATOM   12017 C  CD2   . TRP   E 4  93  ? -3.386  63.341  -101.093 1.00 57.78  ? 93  TRP   F CD2   1 
ATOM   12018 N  NE1   . TRP   E 4  93  ? -2.264  65.285  -101.144 1.00 54.00  ? 93  TRP   F NE1   1 
ATOM   12019 C  CE2   . TRP   E 4  93  ? -3.241  64.600  -100.469 1.00 63.30  ? 93  TRP   F CE2   1 
ATOM   12020 C  CE3   . TRP   E 4  93  ? -4.327  62.440  -100.582 1.00 51.63  ? 93  TRP   F CE3   1 
ATOM   12021 C  CZ2   . TRP   E 4  93  ? -4.003  64.977  -99.360  1.00 60.37  ? 93  TRP   F CZ2   1 
ATOM   12022 C  CZ3   . TRP   E 4  93  ? -5.084  62.817  -99.481  1.00 56.41  ? 93  TRP   F CZ3   1 
ATOM   12023 C  CH2   . TRP   E 4  93  ? -4.917  64.074  -98.883  1.00 58.00  ? 93  TRP   F CH2   1 
ATOM   12024 N  N     . PHE   E 4  94  ? -5.769  61.640  -103.720 1.00 43.99  ? 94  PHE   F N     1 
ATOM   12025 C  CA    . PHE   E 4  94  ? -6.912  60.873  -103.234 1.00 49.49  ? 94  PHE   F CA    1 
ATOM   12026 C  C     . PHE   E 4  94  ? -7.843  60.555  -104.396 1.00 52.64  ? 94  PHE   F C     1 
ATOM   12027 O  O     . PHE   E 4  94  ? -8.319  61.484  -105.071 1.00 52.10  ? 94  PHE   F O     1 
ATOM   12028 C  CB    . PHE   E 4  94  ? -7.676  61.615  -102.134 1.00 54.94  ? 94  PHE   F CB    1 
ATOM   12029 C  CG    . PHE   E 4  94  ? -8.821  60.818  -101.567 1.00 53.72  ? 94  PHE   F CG    1 
ATOM   12030 C  CD1   . PHE   E 4  94  ? -8.577  59.718  -100.759 1.00 47.64  ? 94  PHE   F CD1   1 
ATOM   12031 C  CD2   . PHE   E 4  94  ? -10.135 61.147  -101.870 1.00 44.31  ? 94  PHE   F CD2   1 
ATOM   12032 C  CE1   . PHE   E 4  94  ? -9.622  58.965  -100.255 1.00 50.05  ? 94  PHE   F CE1   1 
ATOM   12033 C  CE2   . PHE   E 4  94  ? -11.178 60.405  -101.369 1.00 45.51  ? 94  PHE   F CE2   1 
ATOM   12034 C  CZ    . PHE   E 4  94  ? -10.924 59.313  -100.558 1.00 53.80  ? 94  PHE   F CZ    1 
ATOM   12035 N  N     . PRO   E 4  95  ? -8.149  59.285  -104.660 1.00 55.35  ? 95  PRO   F N     1 
ATOM   12036 C  CA    . PRO   E 4  95  ? -8.940  58.950  -105.848 1.00 53.26  ? 95  PRO   F CA    1 
ATOM   12037 C  C     . PRO   E 4  95  ? -10.301 59.626  -105.806 1.00 57.88  ? 95  PRO   F C     1 
ATOM   12038 O  O     . PRO   E 4  95  ? -10.772 60.055  -104.753 1.00 59.50  ? 95  PRO   F O     1 
ATOM   12039 C  CB    . PRO   E 4  95  ? -9.065  57.421  -105.779 1.00 47.17  ? 95  PRO   F CB    1 
ATOM   12040 C  CG    . PRO   E 4  95  ? -7.930  56.981  -104.919 1.00 57.33  ? 95  PRO   F CG    1 
ATOM   12041 C  CD    . PRO   E 4  95  ? -7.764  58.085  -103.895 1.00 55.99  ? 95  PRO   F CD    1 
ATOM   12042 N  N     . GLU   E 4  96  ? -10.929 59.734  -106.981 1.00 59.11  ? 96  GLU   F N     1 
ATOM   12043 C  CA    . GLU   E 4  96  ? -12.261 60.321  -107.057 1.00 67.02  ? 96  GLU   F CA    1 
ATOM   12044 C  C     . GLU   E 4  96  ? -13.222 59.552  -106.159 1.00 75.56  ? 96  GLU   F C     1 
ATOM   12045 O  O     . GLU   E 4  96  ? -13.162 58.321  -106.068 1.00 74.30  ? 96  GLU   F O     1 
ATOM   12046 C  CB    . GLU   E 4  96  ? -12.780 60.314  -108.496 1.00 79.80  ? 96  GLU   F CB    1 
ATOM   12047 C  CG    . GLU   E 4  96  ? -12.553 61.610  -109.269 1.00 81.22  ? 96  GLU   F CG    1 
ATOM   12048 C  CD    . GLU   E 4  96  ? -13.546 61.794  -110.409 1.00 79.78  ? 96  GLU   F CD    1 
ATOM   12049 O  OE1   . GLU   E 4  96  ? -14.661 61.236  -110.326 1.00 75.60  ? 96  GLU   F OE1   1 
ATOM   12050 O  OE2   . GLU   E 4  96  ? -13.210 62.498  -111.385 1.00 85.99  ? 96  GLU   F OE2   1 
ATOM   12051 N  N     . SER   E 4  97  ? -14.114 60.281  -105.490 1.00 67.87  ? 97  SER   F N     1 
ATOM   12052 C  CA    . SER   E 4  97  ? -15.001 59.634  -104.533 1.00 73.47  ? 97  SER   F CA    1 
ATOM   12053 C  C     . SER   E 4  97  ? -16.258 60.466  -104.335 1.00 70.01  ? 97  SER   F C     1 
ATOM   12054 O  O     . SER   E 4  97  ? -16.249 61.692  -104.476 1.00 65.85  ? 97  SER   F O     1 
ATOM   12055 C  CB    . SER   E 4  97  ? -14.313 59.412  -103.180 1.00 56.15  ? 97  SER   F CB    1 
ATOM   12056 O  OG    . SER   E 4  97  ? -12.997 58.944  -103.352 1.00 50.52  ? 97  SER   F OG    1 
ATOM   12057 N  N     . TYR   E 4  98  ? -17.333 59.777  -103.981 1.00 67.96  ? 98  TYR   F N     1 
ATOM   12058 C  CA    . TYR   E 4  98  ? -18.586 60.420  -103.641 1.00 68.52  ? 98  TYR   F CA    1 
ATOM   12059 C  C     . TYR   E 4  98  ? -19.241 59.610  -102.535 1.00 77.08  ? 98  TYR   F C     1 
ATOM   12060 O  O     . TYR   E 4  98  ? -19.093 58.384  -102.468 1.00 74.86  ? 98  TYR   F O     1 
ATOM   12061 C  CB    . TYR   E 4  98  ? -19.505 60.535  -104.872 1.00 75.71  ? 98  TYR   F CB    1 
ATOM   12062 C  CG    . TYR   E 4  98  ? -18.809 61.075  -106.108 1.00 74.36  ? 98  TYR   F CG    1 
ATOM   12063 C  CD1   . TYR   E 4  98  ? -18.102 60.228  -106.956 1.00 78.52  ? 98  TYR   F CD1   1 
ATOM   12064 C  CD2   . TYR   E 4  98  ? -18.848 62.431  -106.422 1.00 75.58  ? 98  TYR   F CD2   1 
ATOM   12065 C  CE1   . TYR   E 4  98  ? -17.459 60.713  -108.088 1.00 74.74  ? 98  TYR   F CE1   1 
ATOM   12066 C  CE2   . TYR   E 4  98  ? -18.205 62.924  -107.553 1.00 76.71  ? 98  TYR   F CE2   1 
ATOM   12067 C  CZ    . TYR   E 4  98  ? -17.516 62.057  -108.381 1.00 71.91  ? 98  TYR   F CZ    1 
ATOM   12068 O  OH    . TYR   E 4  98  ? -16.879 62.529  -109.504 1.00 79.72  ? 98  TYR   F OH    1 
ATOM   12069 N  N     . VAL   E 4  99  ? -19.937 60.302  -101.647 1.00 84.10  ? 99  VAL   F N     1 
ATOM   12070 C  CA    . VAL   E 4  99  ? -20.686 59.621  -100.599 1.00 82.09  ? 99  VAL   F CA    1 
ATOM   12071 C  C     . VAL   E 4  99  ? -22.036 59.224  -101.170 1.00 86.16  ? 99  VAL   F C     1 
ATOM   12072 O  O     . VAL   E 4  99  ? -22.636 59.966  -101.961 1.00 79.23  ? 99  VAL   F O     1 
ATOM   12073 C  CB    . VAL   E 4  99  ? -20.822 60.514  -99.355  1.00 72.75  ? 99  VAL   F CB    1 
ATOM   12074 C  CG1   . VAL   E 4  99  ? -19.447 60.960  -98.880  1.00 66.82  ? 99  VAL   F CG1   1 
ATOM   12075 C  CG2   . VAL   E 4  99  ? -21.701 61.717  -99.655  1.00 84.09  ? 99  VAL   F CG2   1 
ATOM   12076 N  N     . ILE   E 4  100 ? -22.504 58.033  -100.804 1.00 86.09  ? 100 ILE   F N     1 
ATOM   12077 C  CA    . ILE   E 4  100 ? -23.703 57.469  -101.406 1.00 88.56  ? 100 ILE   F CA    1 
ATOM   12078 C  C     . ILE   E 4  100 ? -24.556 56.815  -100.328 1.00 91.71  ? 100 ILE   F C     1 
ATOM   12079 O  O     . ILE   E 4  100 ? -24.048 56.254  -99.353  1.00 92.87  ? 100 ILE   F O     1 
ATOM   12080 C  CB    . ILE   E 4  100 ? -23.350 56.477  -102.535 1.00 81.13  ? 100 ILE   F CB    1 
ATOM   12081 C  CG1   . ILE   E 4  100 ? -23.076 57.244  -103.828 1.00 79.52  ? 100 ILE   F CG1   1 
ATOM   12082 C  CG2   . ILE   E 4  100 ? -24.463 55.484  -102.741 1.00 85.68  ? 100 ILE   F CG2   1 
ATOM   12083 C  CD1   . ILE   E 4  100 ? -22.681 56.365  -104.986 1.00 87.51  ? 100 ILE   F CD1   1 
ATOM   12084 N  N     . TYR   E 4  101 ? -25.872 56.890  -100.521 1.00 97.29  ? 101 TYR   F N     1 
ATOM   12085 C  CA    . TYR   E 4  101 ? -26.842 56.527  -99.495  1.00 102.02 ? 101 TYR   F CA    1 
ATOM   12086 C  C     . TYR   E 4  101 ? -27.832 55.503  -100.034 1.00 97.30  ? 101 TYR   F C     1 
ATOM   12087 O  O     . TYR   E 4  101 ? -28.543 55.792  -101.021 1.00 95.14  ? 101 TYR   F O     1 
ATOM   12088 C  CB    . TYR   E 4  101 ? -27.572 57.781  -99.008  1.00 94.85  ? 101 TYR   F CB    1 
ATOM   12089 C  CG    . TYR   E 4  101 ? -26.834 58.528  -97.930  1.00 97.04  ? 101 TYR   F CG    1 
ATOM   12090 C  CD1   . TYR   E 4  101 ? -26.640 57.953  -96.680  1.00 99.21  ? 101 TYR   F CD1   1 
ATOM   12091 C  CD2   . TYR   E 4  101 ? -26.339 59.807  -98.150  1.00 95.85  ? 101 TYR   F CD2   1 
ATOM   12092 C  CE1   . TYR   E 4  101 ? -25.972 58.623  -95.677  1.00 90.35  ? 101 TYR   F CE1   1 
ATOM   12093 C  CE2   . TYR   E 4  101 ? -25.666 60.489  -97.149  1.00 93.37  ? 101 TYR   F CE2   1 
ATOM   12094 C  CZ    . TYR   E 4  101 ? -25.489 59.886  -95.913  1.00 92.95  ? 101 TYR   F CZ    1 
ATOM   12095 O  OH    . TYR   E 4  101 ? -24.828 60.537  -94.900  1.00 100.95 ? 101 TYR   F OH    1 
ATOM   12096 N  N     . PRO   E 4  102 ? -27.932 54.309  -99.428  1.00 94.15  ? 102 PRO   F N     1 
ATOM   12097 C  CA    . PRO   E 4  102 ? -29.018 53.387  -99.793  1.00 96.88  ? 102 PRO   F CA    1 
ATOM   12098 C  C     . PRO   E 4  102 ? -30.387 53.991  -99.501  1.00 100.54 ? 102 PRO   F C     1 
ATOM   12099 O  O     . PRO   E 4  102 ? -30.854 53.982  -98.355  1.00 100.10 ? 102 PRO   F O     1 
ATOM   12100 C  CB    . PRO   E 4  102 ? -28.738 52.148  -98.928  1.00 90.50  ? 102 PRO   F CB    1 
ATOM   12101 C  CG    . PRO   E 4  102 ? -27.910 52.645  -97.798  1.00 96.90  ? 102 PRO   F CG    1 
ATOM   12102 C  CD    . PRO   E 4  102 ? -27.074 53.762  -98.363  1.00 96.19  ? 102 PRO   F CD    1 
ATOM   12103 N  N     . THR   E 4  103 ? -31.034 54.522  -100.535 1.00 96.79  ? 103 THR   F N     1 
ATOM   12104 C  CA    . THR   E 4  103 ? -32.273 55.268  -100.369 1.00 87.18  ? 103 THR   F CA    1 
ATOM   12105 C  C     . THR   E 4  103 ? -33.347 54.439  -99.675  1.00 89.37  ? 103 THR   F C     1 
ATOM   12106 O  O     . THR   E 4  103 ? -33.819 54.802  -98.595  1.00 84.76  ? 103 THR   F O     1 
ATOM   12107 C  CB    . THR   E 4  103 ? -32.812 55.778  -101.726 1.00 88.68  ? 103 THR   F CB    1 
ATOM   12108 O  OG1   . THR   E 4  103 ? -34.128 56.313  -101.544 1.00 91.58  ? 103 THR   F OG1   1 
ATOM   12109 C  CG2   . THR   E 4  103 ? -32.848 54.660  -102.769 1.00 83.00  ? 103 THR   F CG2   1 
ATOM   12110 N  N     . THR   E 4  125 ? -27.915 66.044  -99.819  1.00 114.22 ? 125 THR   F N     1 
ATOM   12111 C  CA    . THR   E 4  125 ? -26.769 66.010  -98.910  1.00 117.70 ? 125 THR   F CA    1 
ATOM   12112 C  C     . THR   E 4  125 ? -25.791 64.880  -99.265  1.00 112.80 ? 125 THR   F C     1 
ATOM   12113 O  O     . THR   E 4  125 ? -24.809 64.653  -98.553  1.00 101.10 ? 125 THR   F O     1 
ATOM   12114 C  CB    . THR   E 4  125 ? -27.219 65.856  -97.435  1.00 108.71 ? 125 THR   F CB    1 
ATOM   12115 O  OG1   . THR   E 4  125 ? -28.558 65.341  -97.385  1.00 100.05 ? 125 THR   F OG1   1 
ATOM   12116 C  CG2   . THR   E 4  125 ? -27.164 67.197  -96.713  1.00 99.94  ? 125 THR   F CG2   1 
ATOM   12117 N  N     . ASP   E 4  126 ? -26.070 64.179  -100.368 1.00 112.32 ? 126 ASP   F N     1 
ATOM   12118 C  CA    . ASP   E 4  126 ? -25.196 63.142  -100.908 1.00 104.09 ? 126 ASP   F CA    1 
ATOM   12119 C  C     . ASP   E 4  126 ? -24.905 63.465  -102.375 1.00 98.10  ? 126 ASP   F C     1 
ATOM   12120 O  O     . ASP   E 4  126 ? -25.415 64.446  -102.929 1.00 95.17  ? 126 ASP   F O     1 
ATOM   12121 C  CB    . ASP   E 4  126 ? -25.807 61.739  -100.710 1.00 100.62 ? 126 ASP   F CB    1 
ATOM   12122 C  CG    . ASP   E 4  126 ? -26.535 61.205  -101.944 1.00 97.64  ? 126 ASP   F CG    1 
ATOM   12123 O  OD1   . ASP   E 4  126 ? -27.098 61.996  -102.725 1.00 100.46 ? 126 ASP   F OD1   1 
ATOM   12124 O  OD2   . ASP   E 4  126 ? -26.559 59.967  -102.120 1.00 90.47  ? 126 ASP   F OD2   1 
ATOM   12125 N  N     . GLU   E 4  127 ? -24.065 62.647  -103.008 1.00 90.65  ? 127 GLU   F N     1 
ATOM   12126 C  CA    . GLU   E 4  127 ? -23.581 62.934  -104.355 1.00 90.61  ? 127 GLU   F CA    1 
ATOM   12127 C  C     . GLU   E 4  127 ? -23.744 61.730  -105.277 1.00 95.00  ? 127 GLU   F C     1 
ATOM   12128 O  O     . GLU   E 4  127 ? -22.855 61.400  -106.068 1.00 89.53  ? 127 GLU   F O     1 
ATOM   12129 C  CB    . GLU   E 4  127 ? -22.127 63.409  -104.334 1.00 84.51  ? 127 GLU   F CB    1 
ATOM   12130 C  CG    . GLU   E 4  127 ? -21.344 63.121  -103.050 1.00 80.06  ? 127 GLU   F CG    1 
ATOM   12131 C  CD    . GLU   E 4  127 ? -19.918 63.672  -103.090 1.00 73.46  ? 127 GLU   F CD    1 
ATOM   12132 O  OE1   . GLU   E 4  127 ? -19.688 64.736  -103.707 1.00 61.47  ? 127 GLU   F OE1   1 
ATOM   12133 O  OE2   . GLU   E 4  127 ? -19.018 63.030  -102.513 1.00 77.83  ? 127 GLU   F OE2   1 
ATOM   12134 N  N     . ARG   E 4  128 ? -24.896 61.061  -105.194 1.00 99.83  ? 128 ARG   F N     1 
ATOM   12135 C  CA    . ARG   E 4  128 ? -25.251 60.065  -106.202 1.00 102.44 ? 128 ARG   F CA    1 
ATOM   12136 C  C     . ARG   E 4  128 ? -25.678 60.730  -107.512 1.00 97.13  ? 128 ARG   F C     1 
ATOM   12137 O  O     . ARG   E 4  128 ? -25.468 60.168  -108.596 1.00 86.15  ? 128 ARG   F O     1 
ATOM   12138 C  CB    . ARG   E 4  128 ? -26.355 59.157  -105.651 1.00 98.65  ? 128 ARG   F CB    1 
ATOM   12139 C  CG    . ARG   E 4  128 ? -27.099 58.342  -106.684 1.00 96.94  ? 128 ARG   F CG    1 
ATOM   12140 C  CD    . ARG   E 4  128 ? -28.527 58.070  -106.230 1.00 94.16  ? 128 ARG   F CD    1 
ATOM   12141 N  NE    . ARG   E 4  128 ? -28.642 56.898  -105.373 1.00 86.33  ? 128 ARG   F NE    1 
ATOM   12142 C  CZ    . ARG   E 4  128 ? -28.419 56.898  -104.067 1.00 95.12  ? 128 ARG   F CZ    1 
ATOM   12143 N  NH1   . ARG   E 4  128 ? -28.010 57.986  -103.435 1.00 94.81  ? 128 ARG   F NH1   1 
ATOM   12144 N  NH2   . ARG   E 4  128 ? -28.613 55.777  -103.377 1.00 98.06  ? 128 ARG   F NH2   1 
ATOM   12145 N  N     . GLU   E 4  129 ? -26.277 61.921  -107.425 1.00 96.00  ? 129 GLU   F N     1 
ATOM   12146 C  CA    . GLU   E 4  129 ? -26.527 62.741  -108.605 1.00 94.55  ? 129 GLU   F CA    1 
ATOM   12147 C  C     . GLU   E 4  129 ? -25.221 63.279  -109.177 1.00 96.64  ? 129 GLU   F C     1 
ATOM   12148 O  O     . GLU   E 4  129 ? -24.869 62.999  -110.329 1.00 100.81 ? 129 GLU   F O     1 
ATOM   12149 C  CB    . GLU   E 4  129 ? -27.465 63.897  -108.248 1.00 101.56 ? 129 GLU   F CB    1 
ATOM   12150 C  CG    . GLU   E 4  129 ? -27.475 65.018  -109.287 1.00 109.72 ? 129 GLU   F CG    1 
ATOM   12151 C  CD    . GLU   E 4  129 ? -27.670 66.405  -108.681 1.00 100.87 ? 129 GLU   F CD    1 
ATOM   12152 O  OE1   . GLU   E 4  129 ? -27.245 66.619  -107.524 1.00 98.28  ? 129 GLU   F OE1   1 
ATOM   12153 O  OE2   . GLU   E 4  129 ? -28.247 67.278  -109.369 1.00 83.89  ? 129 GLU   F OE2   1 
ATOM   12154 N  N     . VAL   E 4  130 ? -24.482 64.050  -108.386 1.00 95.20  ? 130 VAL   F N     1 
ATOM   12155 C  CA    . VAL   E 4  130 ? -23.204 64.600  -108.822 1.00 91.57  ? 130 VAL   F CA    1 
ATOM   12156 C  C     . VAL   E 4  130 ? -22.253 63.508  -109.323 1.00 92.82  ? 130 VAL   F C     1 
ATOM   12157 O  O     . VAL   E 4  130 ? -21.334 63.795  -110.095 1.00 83.96  ? 130 VAL   F O     1 
ATOM   12158 C  CB    . VAL   E 4  130 ? -22.566 65.420  -107.688 1.00 81.20  ? 130 VAL   F CB    1 
ATOM   12159 C  CG1   . VAL   E 4  130 ? -21.313 66.128  -108.160 1.00 62.16  ? 130 VAL   F CG1   1 
ATOM   12160 C  CG2   . VAL   E 4  130 ? -23.580 66.422  -107.130 1.00 88.03  ? 130 VAL   F CG2   1 
ATOM   12161 N  N     . PHE   E 4  131 ? -22.480 62.252  -108.909 1.00 95.28  ? 131 PHE   F N     1 
ATOM   12162 C  CA    . PHE   E 4  131 ? -21.588 61.154  -109.294 1.00 95.85  ? 131 PHE   F CA    1 
ATOM   12163 C  C     . PHE   E 4  131 ? -21.755 60.772  -110.763 1.00 102.22 ? 131 PHE   F C     1 
ATOM   12164 O  O     . PHE   E 4  131 ? -20.778 60.710  -111.521 1.00 101.15 ? 131 PHE   F O     1 
ATOM   12165 C  CB    . PHE   E 4  131 ? -21.843 59.931  -108.412 1.00 91.75  ? 131 PHE   F CB    1 
ATOM   12166 C  CG    . PHE   E 4  131 ? -21.525 58.626  -109.094 1.00 99.21  ? 131 PHE   F CG    1 
ATOM   12167 C  CD1   . PHE   E 4  131 ? -20.209 58.243  -109.309 1.00 94.64  ? 131 PHE   F CD1   1 
ATOM   12168 C  CD2   . PHE   E 4  131 ? -22.537 57.792  -109.535 1.00 102.39 ? 131 PHE   F CD2   1 
ATOM   12169 C  CE1   . PHE   E 4  131 ? -19.909 57.056  -109.936 1.00 84.97  ? 131 PHE   F CE1   1 
ATOM   12170 C  CE2   . PHE   E 4  131 ? -22.239 56.601  -110.165 1.00 98.01  ? 131 PHE   F CE2   1 
ATOM   12171 C  CZ    . PHE   E 4  131 ? -20.922 56.236  -110.363 1.00 92.01  ? 131 PHE   F CZ    1 
ATOM   12172 N  N     . LEU   E 4  132 ? -22.987 60.457  -111.168 1.00 98.06  ? 132 LEU   F N     1 
ATOM   12173 C  CA    . LEU   E 4  132 ? -23.235 60.046  -112.543 1.00 96.17  ? 132 LEU   F CA    1 
ATOM   12174 C  C     . LEU   E 4  132 ? -22.553 60.982  -113.529 1.00 97.95  ? 132 LEU   F C     1 
ATOM   12175 O  O     . LEU   E 4  132 ? -21.949 60.532  -114.510 1.00 100.38 ? 132 LEU   F O     1 
ATOM   12176 C  CB    . LEU   E 4  132 ? -24.740 59.991  -112.787 1.00 94.50  ? 132 LEU   F CB    1 
ATOM   12177 C  CG    . LEU   E 4  132 ? -25.461 59.188  -111.700 1.00 97.24  ? 132 LEU   F CG    1 
ATOM   12178 C  CD1   . LEU   E 4  132 ? -26.970 59.259  -111.876 1.00 97.21  ? 132 LEU   F CD1   1 
ATOM   12179 C  CD2   . LEU   E 4  132 ? -24.977 57.741  -111.685 1.00 85.75  ? 132 LEU   F CD2   1 
ATOM   12180 N  N     . ALA   E 4  133 ? -22.620 62.289  -113.267 1.00 95.62  ? 133 ALA   F N     1 
ATOM   12181 C  CA    . ALA   E 4  133 ? -21.970 63.304  -114.090 1.00 97.51  ? 133 ALA   F CA    1 
ATOM   12182 C  C     . ALA   E 4  133 ? -20.531 62.925  -114.434 1.00 102.37 ? 133 ALA   F C     1 
ATOM   12183 O  O     . ALA   E 4  133 ? -20.233 62.559  -115.577 1.00 105.38 ? 133 ALA   F O     1 
ATOM   12184 C  CB    . ALA   E 4  133 ? -22.005 64.660  -113.379 1.00 92.43  ? 133 ALA   F CB    1 
ATOM   12185 N  N     . ALA   E 4  134 ? -19.630 63.011  -113.453 1.00 99.91  ? 134 ALA   F N     1 
ATOM   12186 C  CA    . ALA   E 4  134 ? -18.238 62.647  -113.681 1.00 96.49  ? 134 ALA   F CA    1 
ATOM   12187 C  C     . ALA   E 4  134 ? -18.074 61.205  -114.148 1.00 101.33 ? 134 ALA   F C     1 
ATOM   12188 O  O     . ALA   E 4  134 ? -16.980 60.843  -114.597 1.00 100.59 ? 134 ALA   F O     1 
ATOM   12189 C  CB    . ALA   E 4  134 ? -17.424 62.881  -112.404 1.00 79.91  ? 134 ALA   F CB    1 
ATOM   12190 N  N     . TYR   E 4  135 ? -19.125 60.382  -114.067 1.00 97.72  ? 135 TYR   F N     1 
ATOM   12191 C  CA    . TYR   E 4  135 ? -19.055 58.970  -114.432 1.00 100.97 ? 135 TYR   F CA    1 
ATOM   12192 C  C     . TYR   E 4  135 ? -18.713 58.763  -115.907 1.00 103.86 ? 135 TYR   F C     1 
ATOM   12193 O  O     . TYR   E 4  135 ? -17.580 58.400  -116.250 1.00 103.29 ? 135 TYR   F O     1 
ATOM   12194 C  CB    . TYR   E 4  135 ? -20.382 58.279  -114.092 1.00 98.71  ? 135 TYR   F CB    1 
ATOM   12195 C  CG    . TYR   E 4  135 ? -20.475 56.824  -114.520 1.00 96.54  ? 135 TYR   F CG    1 
ATOM   12196 C  CD1   . TYR   E 4  135 ? -19.535 55.892  -114.103 1.00 89.97  ? 135 TYR   F CD1   1 
ATOM   12197 C  CD2   . TYR   E 4  135 ? -21.519 56.382  -115.319 1.00 97.30  ? 135 TYR   F CD2   1 
ATOM   12198 C  CE1   . TYR   E 4  135 ? -19.621 54.568  -114.482 1.00 91.23  ? 135 TYR   F CE1   1 
ATOM   12199 C  CE2   . TYR   E 4  135 ? -21.617 55.057  -115.700 1.00 101.15 ? 135 TYR   F CE2   1 
ATOM   12200 C  CZ    . TYR   E 4  135 ? -20.666 54.153  -115.280 1.00 100.70 ? 135 TYR   F CZ    1 
ATOM   12201 O  OH    . TYR   E 4  135 ? -20.759 52.829  -115.658 1.00 94.33  ? 135 TYR   F OH    1 
ATOM   12202 N  N     . ASN   E 4  136 ? -19.686 58.984  -116.782 1.00 97.28  ? 136 ASN   F N     1 
ATOM   12203 C  CA    . ASN   E 4  136 ? -19.527 58.740  -118.212 1.00 98.35  ? 136 ASN   F CA    1 
ATOM   12204 C  C     . ASN   E 4  136 ? -18.210 59.288  -118.757 1.00 101.53 ? 136 ASN   F C     1 
ATOM   12205 O  O     . ASN   E 4  136 ? -17.978 60.500  -118.765 1.00 101.05 ? 136 ASN   F O     1 
ATOM   12206 C  CB    . ASN   E 4  136 ? -20.703 59.379  -118.950 1.00 107.92 ? 136 ASN   F CB    1 
ATOM   12207 C  CG    . ASN   E 4  136 ? -21.867 59.691  -118.029 1.00 105.97 ? 136 ASN   F CG    1 
ATOM   12208 O  OD1   . ASN   E 4  136 ? -22.059 59.034  -116.999 1.00 96.99  ? 136 ASN   F OD1   1 
ATOM   12209 N  ND2   . ASN   E 4  136 ? -22.648 60.703  -118.391 1.00 102.48 ? 136 ASN   F ND2   1 
ATOM   12210 N  N     . ARG   E 4  137 ? -17.347 58.387  -119.228 1.00 89.75  ? 137 ARG   F N     1 
ATOM   12211 C  CA    . ARG   E 4  137 ? -16.130 58.805  -119.911 1.00 88.97  ? 137 ARG   F CA    1 
ATOM   12212 C  C     . ARG   E 4  137 ? -16.038 58.147  -121.291 1.00 100.79 ? 137 ARG   F C     1 
ATOM   12213 O  O     . ARG   E 4  137 ? -16.586 58.650  -122.282 1.00 91.02  ? 137 ARG   F O     1 
ATOM   12214 C  CB    . ARG   E 4  137 ? -14.897 58.471  -119.071 1.00 89.95  ? 137 ARG   F CB    1 
ATOM   12215 C  CG    . ARG   E 4  137 ? -13.640 59.235  -119.488 1.00 99.05  ? 137 ARG   F CG    1 
ATOM   12216 C  CD    . ARG   E 4  137 ? -13.090 60.098  -118.347 1.00 107.39 ? 137 ARG   F CD    1 
ATOM   12217 N  NE    . ARG   E 4  137 ? -12.347 61.265  -118.820 1.00 114.16 ? 137 ARG   F NE    1 
ATOM   12218 C  CZ    . ARG   E 4  137 ? -11.708 62.125  -118.033 1.00 107.79 ? 137 ARG   F CZ    1 
ATOM   12219 N  NH1   . ARG   E 4  137 ? -11.655 61.959  -116.722 1.00 100.72 ? 137 ARG   F NH1   1 
ATOM   12220 N  NH2   . ARG   E 4  137 ? -11.106 63.181  -118.577 1.00 101.34 ? 137 ARG   F NH2   1 
ATOM   12221 N  N     . GLY   E 4  144 ? -13.116 55.392  -119.662 1.00 68.30  ? 144 GLY   F N     1 
ATOM   12222 C  CA    . GLY   E 4  144 ? -13.237 54.049  -119.118 1.00 76.50  ? 144 GLY   F CA    1 
ATOM   12223 C  C     . GLY   E 4  144 ? -13.316 54.000  -117.601 1.00 84.62  ? 144 GLY   F C     1 
ATOM   12224 O  O     . GLY   E 4  144 ? -12.309 54.177  -116.916 1.00 75.18  ? 144 GLY   F O     1 
ATOM   12225 N  N     . ASN   E 4  145 ? -14.510 53.727  -117.074 1.00 87.26  ? 145 ASN   F N     1 
ATOM   12226 C  CA    . ASN   E 4  145 ? -14.824 53.952  -115.666 1.00 88.42  ? 145 ASN   F CA    1 
ATOM   12227 C  C     . ASN   E 4  145 ? -14.842 52.635  -114.895 1.00 81.19  ? 145 ASN   F C     1 
ATOM   12228 O  O     . ASN   E 4  145 ? -15.704 51.786  -115.137 1.00 87.40  ? 145 ASN   F O     1 
ATOM   12229 C  CB    . ASN   E 4  145 ? -16.179 54.650  -115.517 1.00 93.28  ? 145 ASN   F CB    1 
ATOM   12230 C  CG    . ASN   E 4  145 ? -16.522 55.557  -116.697 1.00 92.66  ? 145 ASN   F CG    1 
ATOM   12231 O  OD1   . ASN   E 4  145 ? -15.642 56.168  -117.311 1.00 95.06  ? 145 ASN   F OD1   1 
ATOM   12232 N  ND2   . ASN   E 4  145 ? -17.816 55.657  -117.009 1.00 83.43  ? 145 ASN   F ND2   1 
ATOM   12233 N  N     . VAL   E 4  146 ? -13.928 52.483  -113.941 1.00 82.83  ? 146 VAL   F N     1 
ATOM   12234 C  CA    . VAL   E 4  146 ? -13.960 51.375  -112.987 1.00 84.21  ? 146 VAL   F CA    1 
ATOM   12235 C  C     . VAL   E 4  146 ? -13.980 51.951  -111.574 1.00 77.66  ? 146 VAL   F C     1 
ATOM   12236 O  O     . VAL   E 4  146 ? -13.075 52.705  -111.193 1.00 70.90  ? 146 VAL   F O     1 
ATOM   12237 C  CB    . VAL   E 4  146 ? -12.770 50.423  -113.168 1.00 79.14  ? 146 VAL   F CB    1 
ATOM   12238 C  CG1   . VAL   E 4  146 ? -12.767 49.371  -112.066 1.00 78.10  ? 146 VAL   F CG1   1 
ATOM   12239 C  CG2   . VAL   E 4  146 ? -12.836 49.772  -114.524 1.00 80.53  ? 146 VAL   F CG2   1 
ATOM   12240 N  N     . TRP   E 4  147 ? -14.996 51.581  -110.797 1.00 75.25  ? 147 TRP   F N     1 
ATOM   12241 C  CA    . TRP   E 4  147 ? -15.196 52.104  -109.450 1.00 81.68  ? 147 TRP   F CA    1 
ATOM   12242 C  C     . TRP   E 4  147 ? -15.205 50.943  -108.443 1.00 80.51  ? 147 TRP   F C     1 
ATOM   12243 O  O     . TRP   E 4  147 ? -14.820 49.814  -108.767 1.00 71.00  ? 147 TRP   F O     1 
ATOM   12244 C  CB    . TRP   E 4  147 ? -16.465 52.967  -109.418 1.00 84.93  ? 147 TRP   F CB    1 
ATOM   12245 C  CG    . TRP   E 4  147 ? -16.431 54.039  -110.496 1.00 86.04  ? 147 TRP   F CG    1 
ATOM   12246 C  CD1   . TRP   E 4  147 ? -16.810 53.900  -111.800 1.00 90.82  ? 147 TRP   F CD1   1 
ATOM   12247 C  CD2   . TRP   E 4  147 ? -15.954 55.386  -110.365 1.00 87.10  ? 147 TRP   F CD2   1 
ATOM   12248 N  NE1   . TRP   E 4  147 ? -16.613 55.075  -112.485 1.00 88.26  ? 147 TRP   F NE1   1 
ATOM   12249 C  CE2   . TRP   E 4  147 ? -16.088 56.003  -111.628 1.00 84.57  ? 147 TRP   F CE2   1 
ATOM   12250 C  CE3   . TRP   E 4  147 ? -15.435 56.133  -109.303 1.00 88.13  ? 147 TRP   F CE3   1 
ATOM   12251 C  CZ2   . TRP   E 4  147 ? -15.725 57.327  -111.856 1.00 82.17  ? 147 TRP   F CZ2   1 
ATOM   12252 C  CZ3   . TRP   E 4  147 ? -15.072 57.448  -109.531 1.00 86.92  ? 147 TRP   F CZ3   1 
ATOM   12253 C  CH2   . TRP   E 4  147 ? -15.222 58.033  -110.798 1.00 86.22  ? 147 TRP   F CH2   1 
ATOM   12254 N  N     . ILE   E 4  148 ? -15.616 51.235  -107.206 1.00 85.45  ? 148 ILE   F N     1 
ATOM   12255 C  CA    . ILE   E 4  148 ? -15.550 50.262  -106.117 1.00 80.60  ? 148 ILE   F CA    1 
ATOM   12256 C  C     . ILE   E 4  148 ? -16.436 50.739  -104.967 1.00 74.60  ? 148 ILE   F C     1 
ATOM   12257 O  O     . ILE   E 4  148 ? -16.728 51.931  -104.839 1.00 70.74  ? 148 ILE   F O     1 
ATOM   12258 C  CB    . ILE   E 4  148 ? -14.083 50.043  -105.662 1.00 68.22  ? 148 ILE   F CB    1 
ATOM   12259 C  CG1   . ILE   E 4  148 ? -13.996 48.869  -104.679 1.00 65.77  ? 148 ILE   F CG1   1 
ATOM   12260 C  CG2   . ILE   E 4  148 ? -13.519 51.329  -105.062 1.00 69.43  ? 148 ILE   F CG2   1 
ATOM   12261 C  CD1   . ILE   E 4  148 ? -12.601 48.546  -104.199 1.00 59.43  ? 148 ILE   F CD1   1 
ATOM   12262 N  N     . ALA   E 4  149 ? -16.851 49.797  -104.113 1.00 76.68  ? 149 ALA   F N     1 
ATOM   12263 C  CA    . ALA   E 4  149 ? -17.777 50.048  -102.999 1.00 69.91  ? 149 ALA   F CA    1 
ATOM   12264 C  C     . ALA   E 4  149 ? -17.086 50.581  -101.736 1.00 86.47  ? 149 ALA   F C     1 
ATOM   12265 O  O     . ALA   E 4  149 ? -17.727 51.140  -100.832 1.00 77.09  ? 149 ALA   F O     1 
ATOM   12266 C  CB    . ALA   E 4  149 ? -18.533 48.777  -102.670 1.00 79.60  ? 149 ALA   F CB    1 
ATOM   12267 N  N     . GLY   E 4  159 ? -17.368 41.870  -97.663  1.00 72.21  ? 159 GLY   F N     1 
ATOM   12268 C  CA    . GLY   E 4  159 ? -18.518 42.705  -97.965  1.00 85.22  ? 159 GLY   F CA    1 
ATOM   12269 C  C     . GLY   E 4  159 ? -18.170 44.007  -98.667  1.00 85.71  ? 159 GLY   F C     1 
ATOM   12270 O  O     . GLY   E 4  159 ? -18.428 45.094  -98.148  1.00 79.42  ? 159 GLY   F O     1 
ATOM   12271 N  N     . ILE   E 4  160 ? -17.578 43.882  -99.856  1.00 93.03  ? 160 ILE   F N     1 
ATOM   12272 C  CA    . ILE   E 4  160 ? -17.181 45.022  -100.678 1.00 92.86  ? 160 ILE   F CA    1 
ATOM   12273 C  C     . ILE   E 4  160 ? -17.354 44.634  -102.145 1.00 91.90  ? 160 ILE   F C     1 
ATOM   12274 O  O     . ILE   E 4  160 ? -17.149 43.476  -102.523 1.00 90.68  ? 160 ILE   F O     1 
ATOM   12275 C  CB    . ILE   E 4  160 ? -15.726 45.465  -100.374 1.00 89.64  ? 160 ILE   F CB    1 
ATOM   12276 C  CG1   . ILE   E 4  160 ? -14.900 44.307  -99.787  1.00 71.92  ? 160 ILE   F CG1   1 
ATOM   12277 C  CG2   . ILE   E 4  160 ? -15.715 46.689  -99.461  1.00 88.85  ? 160 ILE   F CG2   1 
ATOM   12278 C  CD1   . ILE   E 4  160 ? -15.056 44.102  -98.293  1.00 72.57  ? 160 ILE   F CD1   1 
ATOM   12279 N  N     . LEU   E 4  161 ? -17.735 45.607  -102.981 1.00 85.92  ? 161 LEU   F N     1 
ATOM   12280 C  CA    . LEU   E 4  161 ? -18.085 45.308  -104.368 1.00 84.45  ? 161 LEU   F CA    1 
ATOM   12281 C  C     . LEU   E 4  161 ? -17.499 46.328  -105.336 1.00 84.94  ? 161 LEU   F C     1 
ATOM   12282 O  O     . LEU   E 4  161 ? -17.741 47.531  -105.194 1.00 85.90  ? 161 LEU   F O     1 
ATOM   12283 C  CB    . LEU   E 4  161 ? -19.606 45.251  -104.543 1.00 87.94  ? 161 LEU   F CB    1 
ATOM   12284 C  CG    . LEU   E 4  161 ? -20.073 44.797  -105.928 1.00 80.36  ? 161 LEU   F CG    1 
ATOM   12285 C  CD1   . LEU   E 4  161 ? -20.193 45.973  -106.870 1.00 79.04  ? 161 LEU   F CD1   1 
ATOM   12286 C  CD2   . LEU   E 4  161 ? -19.113 43.762  -106.492 1.00 78.14  ? 161 LEU   F CD2   1 
ATOM   12287 N  N     . ILE   E 4  162 ? -16.769 45.830  -106.342 1.00 79.46  ? 162 ILE   F N     1 
ATOM   12288 C  CA    . ILE   E 4  162 ? -16.165 46.639  -107.398 1.00 74.64  ? 162 ILE   F CA    1 
ATOM   12289 C  C     . ILE   E 4  162 ? -16.700 46.172  -108.746 1.00 87.31  ? 162 ILE   F C     1 
ATOM   12290 O  O     . ILE   E 4  162 ? -16.884 44.968  -108.964 1.00 86.62  ? 162 ILE   F O     1 
ATOM   12291 C  CB    . ILE   E 4  162 ? -14.623 46.556  -107.379 1.00 72.35  ? 162 ILE   F CB    1 
ATOM   12292 C  CG1   . ILE   E 4  162 ? -14.058 46.763  -108.786 1.00 78.92  ? 162 ILE   F CG1   1 
ATOM   12293 C  CG2   . ILE   E 4  162 ? -14.143 45.233  -106.817 1.00 65.68  ? 162 ILE   F CG2   1 
ATOM   12294 C  CD1   . ILE   E 4  162 ? -12.663 46.201  -108.963 1.00 79.74  ? 162 ILE   F CD1   1 
ATOM   12295 N  N     . SER   E 4  163 ? -16.930 47.118  -109.652 1.00 88.28  ? 163 SER   F N     1 
ATOM   12296 C  CA    . SER   E 4  163 ? -17.482 46.814  -110.972 1.00 79.43  ? 163 SER   F CA    1 
ATOM   12297 C  C     . SER   E 4  163 ? -17.039 47.888  -111.962 1.00 85.06  ? 163 SER   F C     1 
ATOM   12298 O  O     . SER   E 4  163 ? -16.042 48.582  -111.742 1.00 91.30  ? 163 SER   F O     1 
ATOM   12299 C  CB    . SER   E 4  163 ? -19.013 46.696  -110.903 1.00 96.14  ? 163 SER   F CB    1 
ATOM   12300 O  OG    . SER   E 4  163 ? -19.591 46.905  -112.181 1.00 102.66 ? 163 SER   F OG    1 
ATOM   12301 N  N     . SER   E 4  164 ? -17.786 48.018  -113.061 1.00 96.41  ? 164 SER   F N     1 
ATOM   12302 C  CA    . SER   E 4  164 ? -17.452 48.926  -114.156 1.00 99.23  ? 164 SER   F CA    1 
ATOM   12303 C  C     . SER   E 4  164 ? -18.714 49.467  -114.821 1.00 95.92  ? 164 SER   F C     1 
ATOM   12304 O  O     . SER   E 4  164 ? -18.651 50.375  -115.659 1.00 80.93  ? 164 SER   F O     1 
ATOM   12305 C  CB    . SER   E 4  164 ? -16.577 48.218  -115.194 1.00 99.77  ? 164 SER   F CB    1 
ATOM   12306 O  OG    . SER   E 4  164 ? -16.509 48.966  -116.398 1.00 97.81  ? 164 SER   F OG    1 
ATOM   12307 N  N     . GLU   E 4  165 ? -19.861 48.898  -114.471 1.00 98.38  ? 165 GLU   F N     1 
ATOM   12308 C  CA    . GLU   E 4  165 ? -21.154 49.401  -114.909 1.00 103.25 ? 165 GLU   F CA    1 
ATOM   12309 C  C     . GLU   E 4  165 ? -21.856 49.987  -113.697 1.00 101.56 ? 165 GLU   F C     1 
ATOM   12310 O  O     . GLU   E 4  165 ? -21.994 49.312  -112.671 1.00 98.78  ? 165 GLU   F O     1 
ATOM   12311 C  CB    . GLU   E 4  165 ? -22.002 48.296  -115.545 1.00 104.60 ? 165 GLU   F CB    1 
ATOM   12312 C  CG    . GLU   E 4  165 ? -22.946 48.788  -116.640 1.00 107.03 ? 165 GLU   F CG    1 
ATOM   12313 C  CD    . GLU   E 4  165 ? -22.233 49.058  -117.958 1.00 104.13 ? 165 GLU   F CD    1 
ATOM   12314 O  OE1   . GLU   E 4  165 ? -21.180 48.430  -118.197 1.00 108.65 ? 165 GLU   F OE1   1 
ATOM   12315 O  OE2   . GLU   E 4  165 ? -22.725 49.892  -118.755 1.00 96.19  ? 165 GLU   F OE2   1 
ATOM   12316 N  N     . ALA   E 4  166 ? -22.278 51.247  -113.811 1.00 99.45  ? 166 ALA   F N     1 
ATOM   12317 C  CA    . ALA   E 4  166 ? -22.839 51.950  -112.663 1.00 104.57 ? 166 ALA   F CA    1 
ATOM   12318 C  C     . ALA   E 4  166 ? -23.940 51.132  -111.992 1.00 105.28 ? 166 ALA   F C     1 
ATOM   12319 O  O     . ALA   E 4  166 ? -23.822 50.749  -110.823 1.00 101.36 ? 166 ALA   F O     1 
ATOM   12320 C  CB    . ALA   E 4  166 ? -23.359 53.325  -113.096 1.00 94.36  ? 166 ALA   F CB    1 
ATOM   12321 N  N     . SER   E 4  167 ? -25.006 50.833  -112.736 1.00 105.88 ? 167 SER   F N     1 
ATOM   12322 C  CA    . SER   E 4  167 ? -26.215 50.199  -112.213 1.00 106.41 ? 167 SER   F CA    1 
ATOM   12323 C  C     . SER   E 4  167 ? -25.964 49.248  -111.042 1.00 101.82 ? 167 SER   F C     1 
ATOM   12324 O  O     . SER   E 4  167 ? -26.634 49.345  -110.006 1.00 92.58  ? 167 SER   F O     1 
ATOM   12325 C  CB    . SER   E 4  167 ? -26.928 49.457  -113.349 1.00 108.41 ? 167 SER   F CB    1 
ATOM   12326 O  OG    . SER   E 4  167 ? -27.141 50.316  -114.457 1.00 102.63 ? 167 SER   F OG    1 
ATOM   12327 N  N     . GLU   E 4  168 ? -25.000 48.331  -111.187 1.00 107.99 ? 168 GLU   F N     1 
ATOM   12328 C  CA    . GLU   E 4  168 ? -24.776 47.300  -110.176 1.00 104.56 ? 168 GLU   F CA    1 
ATOM   12329 C  C     . GLU   E 4  168 ? -24.012 47.809  -108.962 1.00 99.23  ? 168 GLU   F C     1 
ATOM   12330 O  O     . GLU   E 4  168 ? -23.989 47.129  -107.932 1.00 97.13  ? 168 GLU   F O     1 
ATOM   12331 C  CB    . GLU   E 4  168 ? -24.029 46.110  -110.783 1.00 108.79 ? 168 GLU   F CB    1 
ATOM   12332 C  CG    . GLU   E 4  168 ? -22.632 46.435  -111.289 1.00 108.05 ? 168 GLU   F CG    1 
ATOM   12333 C  CD    . GLU   E 4  168 ? -21.946 45.234  -111.921 1.00 112.20 ? 168 GLU   F CD    1 
ATOM   12334 O  OE1   . GLU   E 4  168 ? -22.372 44.088  -111.652 1.00 115.05 ? 168 GLU   F OE1   1 
ATOM   12335 O  OE2   . GLU   E 4  168 ? -20.982 45.436  -112.690 1.00 103.79 ? 168 GLU   F OE2   1 
ATOM   12336 N  N     . LEU   E 4  169 ? -23.371 48.973  -109.061 1.00 101.74 ? 169 LEU   F N     1 
ATOM   12337 C  CA    . LEU   E 4  169 ? -22.789 49.600  -107.880 1.00 92.19  ? 169 LEU   F CA    1 
ATOM   12338 C  C     . LEU   E 4  169 ? -23.857 50.368  -107.101 1.00 96.45  ? 169 LEU   F C     1 
ATOM   12339 O  O     . LEU   E 4  169 ? -24.173 50.027  -105.955 1.00 92.75  ? 169 LEU   F O     1 
ATOM   12340 C  CB    . LEU   E 4  169 ? -21.627 50.519  -108.285 1.00 93.59  ? 169 LEU   F CB    1 
ATOM   12341 C  CG    . LEU   E 4  169 ? -20.330 49.886  -108.813 1.00 86.91  ? 169 LEU   F CG    1 
ATOM   12342 C  CD1   . LEU   E 4  169 ? -19.294 50.945  -109.163 1.00 75.29  ? 169 LEU   F CD1   1 
ATOM   12343 C  CD2   . LEU   E 4  169 ? -19.753 48.900  -107.811 1.00 85.48  ? 169 LEU   F CD2   1 
ATOM   12344 N  N     . LEU   E 4  170 ? -24.442 51.399  -107.722 1.00 96.94  ? 170 LEU   F N     1 
ATOM   12345 C  CA    . LEU   E 4  170 ? -25.520 52.153  -107.089 1.00 88.16  ? 170 LEU   F CA    1 
ATOM   12346 C  C     . LEU   E 4  170 ? -26.637 51.257  -106.585 1.00 91.03  ? 170 LEU   F C     1 
ATOM   12347 O  O     . LEU   E 4  170 ? -27.368 51.657  -105.672 1.00 95.51  ? 170 LEU   F O     1 
ATOM   12348 C  CB    . LEU   E 4  170 ? -26.103 53.170  -108.068 1.00 88.89  ? 170 LEU   F CB    1 
ATOM   12349 C  CG    . LEU   E 4  170 ? -25.385 54.499  -108.267 1.00 86.45  ? 170 LEU   F CG    1 
ATOM   12350 C  CD1   . LEU   E 4  170 ? -25.820 55.110  -109.582 1.00 85.86  ? 170 LEU   F CD1   1 
ATOM   12351 C  CD2   . LEU   E 4  170 ? -25.697 55.437  -107.113 1.00 91.14  ? 170 LEU   F CD2   1 
ATOM   12352 N  N     . ASP   E 4  171 ? -26.804 50.066  -107.167 1.00 91.85  ? 171 ASP   F N     1 
ATOM   12353 C  CA    . ASP   E 4  171 ? -27.793 49.109  -106.688 1.00 95.13  ? 171 ASP   F CA    1 
ATOM   12354 C  C     . ASP   E 4  171 ? -27.279 48.243  -105.543 1.00 99.62  ? 171 ASP   F C     1 
ATOM   12355 O  O     . ASP   E 4  171 ? -28.088 47.678  -104.795 1.00 97.96  ? 171 ASP   F O     1 
ATOM   12356 C  CB    . ASP   E 4  171 ? -28.260 48.219  -107.844 1.00 94.41  ? 171 ASP   F CB    1 
ATOM   12357 C  CG    . ASP   E 4  171 ? -29.436 48.814  -108.601 1.00 91.74  ? 171 ASP   F CG    1 
ATOM   12358 O  OD1   . ASP   E 4  171 ? -30.374 49.303  -107.932 1.00 83.47  ? 171 ASP   F OD1   1 
ATOM   12359 O  OD2   . ASP   E 4  171 ? -29.425 48.790  -109.856 1.00 81.37  ? 171 ASP   F OD2   1 
ATOM   12360 N  N     . PHE   E 4  172 ? -25.954 48.133  -105.387 1.00 97.64  ? 172 PHE   F N     1 
ATOM   12361 C  CA    . PHE   E 4  172 ? -25.364 47.336  -104.316 1.00 93.09  ? 172 PHE   F CA    1 
ATOM   12362 C  C     . PHE   E 4  172 ? -25.475 48.050  -102.976 1.00 91.87  ? 172 PHE   F C     1 
ATOM   12363 O  O     . PHE   E 4  172 ? -25.828 47.438  -101.963 1.00 89.27  ? 172 PHE   F O     1 
ATOM   12364 C  CB    . PHE   E 4  172 ? -23.900 47.029  -104.651 1.00 89.97  ? 172 PHE   F CB    1 
ATOM   12365 C  CG    . PHE   E 4  172 ? -23.207 46.160  -103.641 1.00 87.71  ? 172 PHE   F CG    1 
ATOM   12366 C  CD1   . PHE   E 4  172 ? -23.365 44.784  -103.665 1.00 90.62  ? 172 PHE   F CD1   1 
ATOM   12367 C  CD2   . PHE   E 4  172 ? -22.378 46.717  -102.680 1.00 89.65  ? 172 PHE   F CD2   1 
ATOM   12368 C  CE1   . PHE   E 4  172 ? -22.720 43.979  -102.740 1.00 94.28  ? 172 PHE   F CE1   1 
ATOM   12369 C  CE2   . PHE   E 4  172 ? -21.732 45.921  -101.752 1.00 93.56  ? 172 PHE   F CE2   1 
ATOM   12370 C  CZ    . PHE   E 4  172 ? -21.902 44.548  -101.781 1.00 95.40  ? 172 PHE   F CZ    1 
ATOM   12371 N  N     . ILE   E 4  173 ? -25.161 49.345  -102.947 1.00 94.63  ? 173 ILE   F N     1 
ATOM   12372 C  CA    . ILE   E 4  173 ? -25.373 50.128  -101.733 1.00 94.30  ? 173 ILE   F CA    1 
ATOM   12373 C  C     . ILE   E 4  173 ? -26.841 50.077  -101.334 1.00 100.45 ? 173 ILE   F C     1 
ATOM   12374 O  O     . ILE   E 4  173 ? -27.185 49.762  -100.187 1.00 102.20 ? 173 ILE   F O     1 
ATOM   12375 C  CB    . ILE   E 4  173 ? -24.892 51.575  -101.936 1.00 85.53  ? 173 ILE   F CB    1 
ATOM   12376 C  CG1   . ILE   E 4  173 ? -23.372 51.642  -101.829 1.00 85.48  ? 173 ILE   F CG1   1 
ATOM   12377 C  CG2   . ILE   E 4  173 ? -25.560 52.503  -100.936 1.00 90.32  ? 173 ILE   F CG2   1 
ATOM   12378 C  CD1   . ILE   E 4  173 ? -22.791 52.976  -102.242 1.00 90.63  ? 173 ILE   F CD1   1 
ATOM   12379 N  N     . ASP   E 4  174 ? -27.731 50.371  -102.286 1.00 98.88  ? 174 ASP   F N     1 
ATOM   12380 C  CA    . ASP   E 4  174 ? -29.159 50.245  -102.033 1.00 95.06  ? 174 ASP   F CA    1 
ATOM   12381 C  C     . ASP   E 4  174 ? -29.516 48.876  -101.464 1.00 96.15  ? 174 ASP   F C     1 
ATOM   12382 O  O     . ASP   E 4  174 ? -30.578 48.727  -100.855 1.00 97.44  ? 174 ASP   F O     1 
ATOM   12383 C  CB    . ASP   E 4  174 ? -29.930 50.541  -103.323 1.00 95.51  ? 174 ASP   F CB    1 
ATOM   12384 C  CG    . ASP   E 4  174 ? -29.932 52.030  -103.676 1.00 96.44  ? 174 ASP   F CG    1 
ATOM   12385 O  OD1   . ASP   E 4  174 ? -30.278 52.852  -102.803 1.00 97.36  ? 174 ASP   F OD1   1 
ATOM   12386 O  OD2   . ASP   E 4  174 ? -29.581 52.385  -104.820 1.00 88.67  ? 174 ASP   F OD2   1 
ATOM   12387 N  N     . GLU   E 4  175 ? -28.647 47.877  -101.630 1.00 99.45  ? 175 GLU   F N     1 
ATOM   12388 C  CA    . GLU   E 4  175 ? -28.782 46.625  -100.895 1.00 95.09  ? 175 GLU   F CA    1 
ATOM   12389 C  C     . GLU   E 4  175 ? -28.773 46.893  -99.396  1.00 92.82  ? 175 GLU   F C     1 
ATOM   12390 O  O     . GLU   E 4  175 ? -29.828 47.125  -98.799  1.00 97.35  ? 175 GLU   F O     1 
ATOM   12391 C  CB    . GLU   E 4  175 ? -27.662 45.643  -101.257 1.00 99.50  ? 175 GLU   F CB    1 
ATOM   12392 C  CG    . GLU   E 4  175 ? -27.864 44.879  -102.563 1.00 99.55  ? 175 GLU   F CG    1 
ATOM   12393 C  CD    . GLU   E 4  175 ? -28.595 43.567  -102.353 1.00 102.80 ? 175 GLU   F CD    1 
ATOM   12394 O  OE1   . GLU   E 4  175 ? -28.302 42.887  -101.346 1.00 101.28 ? 175 GLU   F OE1   1 
ATOM   12395 O  OE2   . GLU   E 4  175 ? -29.465 43.224  -103.184 1.00 100.35 ? 175 GLU   F OE2   1 
ATOM   12396 N  N     . GLN   E 4  176 ? -27.590 46.876  -98.782  1.00 99.80  ? 176 GLN   F N     1 
ATOM   12397 C  CA    . GLN   E 4  176 ? -27.505 46.969  -97.331  1.00 104.34 ? 176 GLN   F CA    1 
ATOM   12398 C  C     . GLN   E 4  176 ? -27.810 48.389  -96.856  1.00 102.75 ? 176 GLN   F C     1 
ATOM   12399 O  O     . GLN   E 4  176 ? -27.935 49.335  -97.643  1.00 93.02  ? 176 GLN   F O     1 
ATOM   12400 C  CB    . GLN   E 4  176 ? -26.125 46.540  -96.830  1.00 95.64  ? 176 GLN   F CB    1 
ATOM   12401 C  CG    . GLN   E 4  176 ? -25.508 45.389  -97.590  1.00 89.84  ? 176 GLN   F CG    1 
ATOM   12402 C  CD    . GLN   E 4  176 ? -24.709 45.857  -98.786  1.00 85.18  ? 176 GLN   F CD    1 
ATOM   12403 O  OE1   . GLN   E 4  176 ? -24.066 46.902  -98.744  1.00 81.89  ? 176 GLN   F OE1   1 
ATOM   12404 N  NE2   . GLN   E 4  176 ? -24.749 45.085  -99.862  1.00 90.03  ? 176 GLN   F NE2   1 
ATOM   12405 N  N     . GLY   E 4  177 ? -27.921 48.527  -95.537  1.00 107.89 ? 177 GLY   F N     1 
ATOM   12406 C  CA    . GLY   E 4  177 ? -28.296 49.787  -94.928  1.00 112.75 ? 177 GLY   F CA    1 
ATOM   12407 C  C     . GLY   E 4  177 ? -27.187 50.440  -94.130  1.00 110.71 ? 177 GLY   F C     1 
ATOM   12408 O  O     . GLY   E 4  177 ? -27.340 50.693  -92.930  1.00 108.47 ? 177 GLY   F O     1 
ATOM   12409 N  N     . GLN   E 4  178 ? -26.058 50.701  -94.784  1.00 106.28 ? 178 GLN   F N     1 
ATOM   12410 C  CA    . GLN   E 4  178 ? -24.964 51.467  -94.204  1.00 110.55 ? 178 GLN   F CA    1 
ATOM   12411 C  C     . GLN   E 4  178 ? -24.484 52.481  -95.235  1.00 109.06 ? 178 GLN   F C     1 
ATOM   12412 O  O     . GLN   E 4  178 ? -24.506 52.206  -96.439  1.00 104.01 ? 178 GLN   F O     1 
ATOM   12413 C  CB    . GLN   E 4  178 ? -23.805 50.555  -93.760  1.00 105.45 ? 178 GLN   F CB    1 
ATOM   12414 C  CG    . GLN   E 4  178 ? -24.102 49.701  -92.529  1.00 111.72 ? 178 GLN   F CG    1 
ATOM   12415 C  CD    . GLN   E 4  178 ? -25.091 48.577  -92.801  1.00 114.02 ? 178 GLN   F CD    1 
ATOM   12416 O  OE1   . GLN   E 4  178 ? -25.417 48.282  -93.952  1.00 110.17 ? 178 GLN   F OE1   1 
ATOM   12417 N  NE2   . GLN   E 4  178 ? -25.577 47.944  -91.734  1.00 111.72 ? 178 GLN   F NE2   1 
ATOM   12418 N  N     . VAL   E 4  179 ? -24.072 53.664  -94.765  1.00 104.19 ? 179 VAL   F N     1 
ATOM   12419 C  CA    . VAL   E 4  179 ? -23.607 54.696  -95.685  1.00 94.59  ? 179 VAL   F CA    1 
ATOM   12420 C  C     . VAL   E 4  179 ? -22.371 54.195  -96.406  1.00 93.71  ? 179 VAL   F C     1 
ATOM   12421 O  O     . VAL   E 4  179 ? -21.457 53.632  -95.791  1.00 97.97  ? 179 VAL   F O     1 
ATOM   12422 C  CB    . VAL   E 4  179 ? -23.315 56.011  -94.948  1.00 102.20 ? 179 VAL   F CB    1 
ATOM   12423 C  CG1   . VAL   E 4  179 ? -22.110 55.847  -94.024  1.00 104.98 ? 179 VAL   F CG1   1 
ATOM   12424 C  CG2   . VAL   E 4  179 ? -23.072 57.128  -95.956  1.00 88.42  ? 179 VAL   F CG2   1 
ATOM   12425 N  N     . HIS   E 4  180 ? -22.332 54.404  -97.717  1.00 97.00  ? 180 HIS   F N     1 
ATOM   12426 C  CA    . HIS   E 4  180 ? -21.263 53.863  -98.536  1.00 93.32  ? 180 HIS   F CA    1 
ATOM   12427 C  C     . HIS   E 4  180 ? -20.666 54.938  -99.437  1.00 89.03  ? 180 HIS   F C     1 
ATOM   12428 O  O     . HIS   E 4  180 ? -21.252 56.002  -99.672  1.00 79.52  ? 180 HIS   F O     1 
ATOM   12429 C  CB    . HIS   E 4  180 ? -21.752 52.673  -99.371  1.00 89.56  ? 180 HIS   F CB    1 
ATOM   12430 C  CG    . HIS   E 4  180 ? -21.196 51.361  -98.919  1.00 93.93  ? 180 HIS   F CG    1 
ATOM   12431 N  ND1   . HIS   E 4  180 ? -21.806 50.156  -99.196  1.00 96.08  ? 180 HIS   F ND1   1 
ATOM   12432 C  CD2   . HIS   E 4  180 ? -20.080 51.064  -98.209  1.00 101.54 ? 180 HIS   F CD2   1 
ATOM   12433 C  CE1   . HIS   E 4  180 ? -21.092 49.174  -98.673  1.00 98.22  ? 180 HIS   F CE1   1 
ATOM   12434 N  NE2   . HIS   E 4  180 ? -20.039 49.699  -98.070  1.00 101.20 ? 180 HIS   F NE2   1 
ATOM   12435 N  N     . VAL   E 4  181 ? -19.471 54.633  -99.930  1.00 83.32  ? 181 VAL   F N     1 
ATOM   12436 C  CA    . VAL   E 4  181 ? -18.686 55.544  -100.743 1.00 78.84  ? 181 VAL   F CA    1 
ATOM   12437 C  C     . VAL   E 4  181 ? -18.238 54.791  -101.987 1.00 77.06  ? 181 VAL   F C     1 
ATOM   12438 O  O     . VAL   E 4  181 ? -17.893 53.606  -101.912 1.00 72.84  ? 181 VAL   F O     1 
ATOM   12439 C  CB    . VAL   E 4  181 ? -17.484 56.090  -99.944  1.00 65.49  ? 181 VAL   F CB    1 
ATOM   12440 C  CG1   . VAL   E 4  181 ? -16.622 54.945  -99.469  1.00 70.54  ? 181 VAL   F CG1   1 
ATOM   12441 C  CG2   . VAL   E 4  181 ? -16.683 57.064  -100.772 1.00 67.97  ? 181 VAL   F CG2   1 
ATOM   12442 N  N     . ILE   E 4  182 ? -18.276 55.473  -103.134 1.00 74.75  ? 182 ILE   F N     1 
ATOM   12443 C  CA    . ILE   E 4  182 ? -17.879 54.919  -104.429 1.00 71.63  ? 182 ILE   F CA    1 
ATOM   12444 C  C     . ILE   E 4  182 ? -16.656 55.692  -104.898 1.00 72.31  ? 182 ILE   F C     1 
ATOM   12445 O  O     . ILE   E 4  182 ? -16.760 56.882  -105.222 1.00 71.08  ? 182 ILE   F O     1 
ATOM   12446 C  CB    . ILE   E 4  182 ? -19.002 55.017  -105.473 1.00 81.99  ? 182 ILE   F CB    1 
ATOM   12447 C  CG1   . ILE   E 4  182 ? -20.189 54.116  -105.105 1.00 85.51  ? 182 ILE   F CG1   1 
ATOM   12448 C  CG2   . ILE   E 4  182 ? -18.458 54.705  -106.872 1.00 86.96  ? 182 ILE   F CG2   1 
ATOM   12449 C  CD1   . ILE   E 4  182 ? -21.188 53.903  -106.240 1.00 79.54  ? 182 ILE   F CD1   1 
ATOM   12450 N  N     . GLN   E 4  183 ? -15.502 55.033  -104.942 1.00 72.53  ? 183 GLN   F N     1 
ATOM   12451 C  CA    . GLN   E 4  183 ? -14.282 55.674  -105.412 1.00 74.29  ? 183 GLN   F CA    1 
ATOM   12452 C  C     . GLN   E 4  183 ? -13.709 54.929  -106.611 1.00 79.11  ? 183 GLN   F C     1 
ATOM   12453 O  O     . GLN   E 4  183 ? -13.849 53.706  -106.737 1.00 73.82  ? 183 GLN   F O     1 
ATOM   12454 C  CB    . GLN   E 4  183 ? -13.214 55.758  -104.321 1.00 58.37  ? 183 GLN   F CB    1 
ATOM   12455 C  CG    . GLN   E 4  183 ? -12.354 54.522  -104.210 1.00 63.83  ? 183 GLN   F CG    1 
ATOM   12456 C  CD    . GLN   E 4  183 ? -11.089 54.779  -103.425 1.00 57.89  ? 183 GLN   F CD    1 
ATOM   12457 O  OE1   . GLN   E 4  183 ? -10.976 55.791  -102.732 1.00 52.26  ? 183 GLN   F OE1   1 
ATOM   12458 N  NE2   . GLN   E 4  183 ? -10.119 53.874  -103.544 1.00 55.86  ? 183 GLN   F NE2   1 
ATOM   12459 N  N     . LYS   E 4  184 ? -13.053 55.689  -107.486 1.00 75.60  ? 184 LYS   F N     1 
ATOM   12460 C  CA    . LYS   E 4  184 ? -12.420 55.118  -108.662 1.00 70.08  ? 184 LYS   F CA    1 
ATOM   12461 C  C     . LYS   E 4  184 ? -11.452 54.023  -108.252 1.00 67.78  ? 184 LYS   F C     1 
ATOM   12462 O  O     . LYS   E 4  184 ? -10.563 54.242  -107.422 1.00 67.94  ? 184 LYS   F O     1 
ATOM   12463 C  CB    . LYS   E 4  184 ? -11.694 56.204  -109.455 1.00 71.54  ? 184 LYS   F CB    1 
ATOM   12464 C  CG    . LYS   E 4  184 ? -10.833 55.667  -110.593 1.00 80.30  ? 184 LYS   F CG    1 
ATOM   12465 C  CD    . LYS   E 4  184 ? -11.676 55.055  -111.715 1.00 79.14  ? 184 LYS   F CD    1 
ATOM   12466 C  CE    . LYS   E 4  184 ? -10.887 54.032  -112.528 1.00 64.16  ? 184 LYS   F CE    1 
ATOM   12467 N  NZ    . LYS   E 4  184 ? -9.538  54.543  -112.942 1.00 69.05  ? 184 LYS   F NZ    1 
ATOM   12468 N  N     . TYR   E 4  185 ? -11.648 52.835  -108.815 1.00 70.64  ? 185 TYR   F N     1 
ATOM   12469 C  CA    . TYR   E 4  185 ? -10.683 51.764  -108.641 1.00 65.99  ? 185 TYR   F CA    1 
ATOM   12470 C  C     . TYR   E 4  185 ? -9.453  52.088  -109.479 1.00 68.91  ? 185 TYR   F C     1 
ATOM   12471 O  O     . TYR   E 4  185 ? -9.571  52.514  -110.633 1.00 66.01  ? 185 TYR   F O     1 
ATOM   12472 C  CB    . TYR   E 4  185 ? -11.295 50.425  -109.047 1.00 58.69  ? 185 TYR   F CB    1 
ATOM   12473 C  CG    . TYR   E 4  185 ? -10.460 49.237  -108.649 1.00 60.90  ? 185 TYR   F CG    1 
ATOM   12474 C  CD1   . TYR   E 4  185 ? -9.358  48.859  -109.396 1.00 67.75  ? 185 TYR   F CD1   1 
ATOM   12475 C  CD2   . TYR   E 4  185 ? -10.771 48.492  -107.528 1.00 62.98  ? 185 TYR   F CD2   1 
ATOM   12476 C  CE1   . TYR   E 4  185 ? -8.584  47.772  -109.037 1.00 71.54  ? 185 TYR   F CE1   1 
ATOM   12477 C  CE2   . TYR   E 4  185 ? -10.003 47.400  -107.160 1.00 68.45  ? 185 TYR   F CE2   1 
ATOM   12478 C  CZ    . TYR   E 4  185 ? -8.912  47.045  -107.918 1.00 71.12  ? 185 TYR   F CZ    1 
ATOM   12479 O  OH    . TYR   E 4  185 ? -8.139  45.966  -107.555 1.00 76.69  ? 185 TYR   F OH    1 
ATOM   12480 N  N     . LEU   E 4  186 ? -8.274  51.945  -108.887 1.00 62.64  ? 186 LEU   F N     1 
ATOM   12481 C  CA    . LEU   E 4  186 ? -7.044  52.233  -109.619 1.00 68.58  ? 186 LEU   F CA    1 
ATOM   12482 C  C     . LEU   E 4  186 ? -6.826  51.125  -110.642 1.00 69.45  ? 186 LEU   F C     1 
ATOM   12483 O  O     . LEU   E 4  186 ? -6.332  50.040  -110.316 1.00 58.65  ? 186 LEU   F O     1 
ATOM   12484 C  CB    . LEU   E 4  186 ? -5.860  52.368  -108.670 1.00 62.74  ? 186 LEU   F CB    1 
ATOM   12485 C  CG    . LEU   E 4  186 ? -5.623  53.782  -108.117 1.00 74.71  ? 186 LEU   F CG    1 
ATOM   12486 C  CD1   . LEU   E 4  186 ? -6.240  54.848  -109.036 1.00 68.64  ? 186 LEU   F CD1   1 
ATOM   12487 C  CD2   . LEU   E 4  186 ? -6.100  53.941  -106.654 1.00 62.44  ? 186 LEU   F CD2   1 
ATOM   12488 N  N     . GLU   E 4  187 ? -7.202  51.402  -111.895 1.00 61.10  ? 187 GLU   F N     1 
ATOM   12489 C  CA    . GLU   E 4  187 ? -7.159  50.368  -112.917 1.00 67.29  ? 187 GLU   F CA    1 
ATOM   12490 C  C     . GLU   E 4  187 ? -5.741  49.925  -113.230 1.00 65.41  ? 187 GLU   F C     1 
ATOM   12491 O  O     . GLU   E 4  187 ? -5.549  48.793  -113.688 1.00 62.75  ? 187 GLU   F O     1 
ATOM   12492 C  CB    . GLU   E 4  187 ? -7.851  50.849  -114.194 1.00 62.57  ? 187 GLU   F CB    1 
ATOM   12493 C  CG    . GLU   E 4  187 ? -9.333  51.136  -113.999 1.00 74.53  ? 187 GLU   F CG    1 
ATOM   12494 C  CD    . GLU   E 4  187 ? -10.146 51.013  -115.278 1.00 77.04  ? 187 GLU   F CD    1 
ATOM   12495 O  OE1   . GLU   E 4  187 ? -9.800  50.153  -116.118 1.00 70.72  ? 187 GLU   F OE1   1 
ATOM   12496 O  OE2   . GLU   E 4  187 ? -11.142 51.763  -115.428 1.00 74.94  ? 187 GLU   F OE2   1 
ATOM   12497 N  N     . LYS   E 4  188 ? -4.746  50.767  -112.966 1.00 55.66  ? 188 LYS   F N     1 
ATOM   12498 C  CA    . LYS   E 4  188 ? -3.385  50.552  -113.449 1.00 60.02  ? 188 LYS   F CA    1 
ATOM   12499 C  C     . LYS   E 4  188 ? -2.425  50.609  -112.269 1.00 60.07  ? 188 LYS   F C     1 
ATOM   12500 O  O     . LYS   E 4  188 ? -1.599  51.521  -112.150 1.00 60.35  ? 188 LYS   F O     1 
ATOM   12501 C  CB    . LYS   E 4  188 ? -3.045  51.569  -114.541 1.00 69.65  ? 188 LYS   F CB    1 
ATOM   12502 C  CG    . LYS   E 4  188 ? -4.234  51.785  -115.498 1.00 67.86  ? 188 LYS   F CG    1 
ATOM   12503 C  CD    . LYS   E 4  188 ? -3.954  52.698  -116.674 1.00 68.11  ? 188 LYS   F CD    1 
ATOM   12504 C  CE    . LYS   E 4  188 ? -5.230  52.856  -117.511 1.00 82.52  ? 188 LYS   F CE    1 
ATOM   12505 N  NZ    . LYS   E 4  188 ? -5.113  53.783  -118.683 1.00 75.61  ? 188 LYS   F NZ    1 
ATOM   12506 N  N     . PRO   E 4  189 ? -2.499  49.624  -111.388 1.00 58.24  ? 189 PRO   F N     1 
ATOM   12507 C  CA    . PRO   E 4  189 ? -1.672  49.628  -110.179 1.00 51.93  ? 189 PRO   F CA    1 
ATOM   12508 C  C     . PRO   E 4  189 ? -0.328  48.937  -110.344 1.00 60.88  ? 189 PRO   F C     1 
ATOM   12509 O  O     . PRO   E 4  189 ? -0.267  47.802  -110.823 1.00 60.28  ? 189 PRO   F O     1 
ATOM   12510 C  CB    . PRO   E 4  189 ? -2.539  48.849  -109.194 1.00 65.73  ? 189 PRO   F CB    1 
ATOM   12511 C  CG    . PRO   E 4  189 ? -3.150  47.778  -110.101 1.00 66.88  ? 189 PRO   F CG    1 
ATOM   12512 C  CD    . PRO   E 4  189 ? -3.403  48.460  -111.432 1.00 54.51  ? 189 PRO   F CD    1 
ATOM   12513 N  N     . LEU   E 4  190 ? 0.744   49.596  -109.907 1.00 65.70  ? 190 LEU   F N     1 
ATOM   12514 C  CA    . LEU   E 4  190 ? 2.059   48.970  -109.795 1.00 63.34  ? 190 LEU   F CA    1 
ATOM   12515 C  C     . LEU   E 4  190 ? 1.943   47.519  -109.362 1.00 60.69  ? 190 LEU   F C     1 
ATOM   12516 O  O     . LEU   E 4  190 ? 1.337   47.210  -108.335 1.00 66.92  ? 190 LEU   F O     1 
ATOM   12517 C  CB    . LEU   E 4  190 ? 2.921   49.728  -108.781 1.00 58.95  ? 190 LEU   F CB    1 
ATOM   12518 C  CG    . LEU   E 4  190 ? 4.423   49.610  -109.034 1.00 55.29  ? 190 LEU   F CG    1 
ATOM   12519 C  CD1   . LEU   E 4  190 ? 4.901   50.895  -109.690 1.00 58.98  ? 190 LEU   F CD1   1 
ATOM   12520 C  CD2   . LEU   E 4  190 ? 5.207   49.298  -107.776 1.00 48.55  ? 190 LEU   F CD2   1 
ATOM   12521 N  N     . LEU   E 4  191 ? 2.547   46.632  -110.144 1.00 69.29  ? 191 LEU   F N     1 
ATOM   12522 C  CA    . LEU   E 4  191 ? 2.539   45.207  -109.859 1.00 71.60  ? 191 LEU   F CA    1 
ATOM   12523 C  C     . LEU   E 4  191 ? 3.949   44.752  -109.511 1.00 66.50  ? 191 LEU   F C     1 
ATOM   12524 O  O     . LEU   E 4  191 ? 4.917   45.176  -110.149 1.00 59.99  ? 191 LEU   F O     1 
ATOM   12525 C  CB    . LEU   E 4  191 ? 1.987   44.426  -111.053 1.00 67.06  ? 191 LEU   F CB    1 
ATOM   12526 C  CG    . LEU   E 4  191 ? 0.589   44.906  -111.457 1.00 69.86  ? 191 LEU   F CG    1 
ATOM   12527 C  CD1   . LEU   E 4  191 ? 0.173   44.340  -112.812 1.00 71.70  ? 191 LEU   F CD1   1 
ATOM   12528 C  CD2   . LEU   E 4  191 ? -0.451  44.573  -110.382 1.00 59.93  ? 191 LEU   F CD2   1 
ATOM   12529 N  N     . LEU   E 4  192 ? 4.054   43.918  -108.474 1.00 65.24  ? 192 LEU   F N     1 
ATOM   12530 C  CA    . LEU   E 4  192 ? 5.332   43.378  -108.026 1.00 65.14  ? 192 LEU   F CA    1 
ATOM   12531 C  C     . LEU   E 4  192 ? 5.746   42.183  -108.872 1.00 72.46  ? 192 LEU   F C     1 
ATOM   12532 O  O     . LEU   E 4  192 ? 4.906   41.473  -109.432 1.00 75.82  ? 192 LEU   F O     1 
ATOM   12533 C  CB    . LEU   E 4  192 ? 5.255   42.930  -106.570 1.00 63.49  ? 192 LEU   F CB    1 
ATOM   12534 C  CG    . LEU   E 4  192 ? 4.936   43.933  -105.469 1.00 60.14  ? 192 LEU   F CG    1 
ATOM   12535 C  CD1   . LEU   E 4  192 ? 4.749   43.164  -104.180 1.00 49.03  ? 192 LEU   F CD1   1 
ATOM   12536 C  CD2   . LEU   E 4  192 ? 6.059   44.941  -105.334 1.00 59.86  ? 192 LEU   F CD2   1 
ATOM   12537 N  N     . GLU   E 4  193 ? 7.062   41.950  -108.941 1.00 72.78  ? 193 GLU   F N     1 
ATOM   12538 C  CA    . GLU   E 4  193 ? 7.634   40.827  -109.680 1.00 72.00  ? 193 GLU   F CA    1 
ATOM   12539 C  C     . GLU   E 4  193 ? 8.710   40.168  -108.829 1.00 75.51  ? 193 GLU   F C     1 
ATOM   12540 O  O     . GLU   E 4  193 ? 9.490   40.869  -108.166 1.00 71.94  ? 193 GLU   F O     1 
ATOM   12541 C  CB    . GLU   E 4  193 ? 8.230   41.269  -111.022 1.00 62.67  ? 193 GLU   F CB    1 
ATOM   12542 C  CG    . GLU   E 4  193 ? 7.222   41.902  -111.971 1.00 61.69  ? 193 GLU   F CG    1 
ATOM   12543 C  CD    . GLU   E 4  193 ? 6.126   40.945  -112.401 1.00 64.16  ? 193 GLU   F CD    1 
ATOM   12544 O  OE1   . GLU   E 4  193 ? 6.202   39.749  -112.045 1.00 63.51  ? 193 GLU   F OE1   1 
ATOM   12545 O  OE2   . GLU   E 4  193 ? 5.188   41.392  -113.100 1.00 65.23  ? 193 GLU   F OE2   1 
ATOM   12546 N  N     . PRO   E 4  194 ? 8.797   38.826  -108.837 1.00 82.61  ? 194 PRO   F N     1 
ATOM   12547 C  CA    . PRO   E 4  194 ? 8.092   37.862  -109.703 1.00 80.36  ? 194 PRO   F CA    1 
ATOM   12548 C  C     . PRO   E 4  194 ? 6.651   37.553  -109.285 1.00 73.74  ? 194 PRO   F C     1 
ATOM   12549 O  O     . PRO   E 4  194 ? 6.454   36.951  -108.238 1.00 76.24  ? 194 PRO   F O     1 
ATOM   12550 C  CB    . PRO   E 4  194 ? 8.967   36.612  -109.563 1.00 84.65  ? 194 PRO   F CB    1 
ATOM   12551 C  CG    . PRO   E 4  194 ? 9.394   36.661  -108.105 1.00 74.02  ? 194 PRO   F CG    1 
ATOM   12552 C  CD    . PRO   E 4  194 ? 9.591   38.134  -107.799 1.00 76.45  ? 194 PRO   F CD    1 
ATOM   12553 N  N     . GLY   E 4  195 ? 5.631   37.909  -110.064 1.00 71.04  ? 195 GLY   F N     1 
ATOM   12554 C  CA    . GLY   E 4  195 ? 4.270   37.586  -109.675 1.00 70.37  ? 195 GLY   F CA    1 
ATOM   12555 C  C     . GLY   E 4  195 ? 3.170   38.348  -110.391 1.00 74.15  ? 195 GLY   F C     1 
ATOM   12556 O  O     . GLY   E 4  195 ? 2.055   37.839  -110.537 1.00 77.48  ? 195 GLY   F O     1 
ATOM   12557 N  N     . HIS   E 4  196 ? 3.452   39.570  -110.833 1.00 71.76  ? 196 HIS   F N     1 
ATOM   12558 C  CA    . HIS   E 4  196 ? 2.448   40.401  -111.491 1.00 73.55  ? 196 HIS   F CA    1 
ATOM   12559 C  C     . HIS   E 4  196 ? 1.235   40.608  -110.585 1.00 74.82  ? 196 HIS   F C     1 
ATOM   12560 O  O     . HIS   E 4  196 ? 0.088   40.431  -110.996 1.00 78.05  ? 196 HIS   F O     1 
ATOM   12561 C  CB    . HIS   E 4  196 ? 2.033   39.786  -112.827 1.00 76.87  ? 196 HIS   F CB    1 
ATOM   12562 C  CG    . HIS   E 4  196 ? 1.609   40.792  -113.855 1.00 79.36  ? 196 HIS   F CG    1 
ATOM   12563 N  ND1   . HIS   E 4  196 ? 2.512   41.565  -114.554 1.00 69.03  ? 196 HIS   F ND1   1 
ATOM   12564 C  CD2   . HIS   E 4  196 ? 0.380   41.142  -114.308 1.00 75.19  ? 196 HIS   F CD2   1 
ATOM   12565 C  CE1   . HIS   E 4  196 ? 1.856   42.354  -115.388 1.00 80.97  ? 196 HIS   F CE1   1 
ATOM   12566 N  NE2   . HIS   E 4  196 ? 0.561   42.117  -115.259 1.00 76.27  ? 196 HIS   F NE2   1 
ATOM   12567 N  N     . ARG   E 4  197 ? 1.502   40.998  -109.337 1.00 77.40  ? 197 ARG   F N     1 
ATOM   12568 C  CA    . ARG   E 4  197 ? 0.489   41.059  -108.288 1.00 79.31  ? 197 ARG   F CA    1 
ATOM   12569 C  C     . ARG   E 4  197 ? 0.447   42.441  -107.633 1.00 76.42  ? 197 ARG   F C     1 
ATOM   12570 O  O     . ARG   E 4  197 ? 1.467   43.132  -107.510 1.00 64.39  ? 197 ARG   F O     1 
ATOM   12571 C  CB    . ARG   E 4  197 ? 0.755   39.980  -107.221 1.00 76.19  ? 197 ARG   F CB    1 
ATOM   12572 C  CG    . ARG   E 4  197 ? 2.133   40.080  -106.598 1.00 66.77  ? 197 ARG   F CG    1 
ATOM   12573 C  CD    . ARG   E 4  197 ? 2.683   38.733  -106.202 1.00 66.15  ? 197 ARG   F CD    1 
ATOM   12574 N  NE    . ARG   E 4  197 ? 4.136   38.783  -106.141 1.00 65.92  ? 197 ARG   F NE    1 
ATOM   12575 C  CZ    . ARG   E 4  197 ? 4.838   38.896  -105.022 1.00 69.29  ? 197 ARG   F CZ    1 
ATOM   12576 N  NH1   . ARG   E 4  197 ? 4.246   38.937  -103.838 1.00 67.97  ? 197 ARG   F NH1   1 
ATOM   12577 N  NH2   . ARG   E 4  197 ? 6.169   38.966  -105.094 1.00 66.16  ? 197 ARG   F NH2   1 
ATOM   12578 N  N     . LYS   E 4  198 ? -0.747  42.830  -107.191 1.00 78.76  ? 198 LYS   F N     1 
ATOM   12579 C  CA    . LYS   E 4  198 ? -0.946  44.137  -106.586 1.00 71.33  ? 198 LYS   F CA    1 
ATOM   12580 C  C     . LYS   E 4  198 ? -0.617  44.097  -105.093 1.00 72.65  ? 198 LYS   F C     1 
ATOM   12581 O  O     . LYS   E 4  198 ? -0.366  43.041  -104.506 1.00 76.07  ? 198 LYS   F O     1 
ATOM   12582 C  CB    . LYS   E 4  198 ? -2.377  44.620  -106.815 1.00 67.60  ? 198 LYS   F CB    1 
ATOM   12583 C  CG    . LYS   E 4  198 ? -3.334  44.264  -105.699 1.00 76.23  ? 198 LYS   F CG    1 
ATOM   12584 C  CD    . LYS   E 4  198 ? -4.721  44.815  -105.986 1.00 81.10  ? 198 LYS   F CD    1 
ATOM   12585 C  CE    . LYS   E 4  198 ? -4.689  46.308  -106.276 1.00 75.31  ? 198 LYS   F CE    1 
ATOM   12586 N  NZ    . LYS   E 4  198 ? -5.995  46.813  -106.813 1.00 73.69  ? 198 LYS   F NZ    1 
ATOM   12587 N  N     . PHE   E 4  199 ? -0.613  45.279  -104.481 1.00 67.18  ? 199 PHE   F N     1 
ATOM   12588 C  CA    . PHE   E 4  199 ? -0.226  45.423  -103.085 1.00 64.00  ? 199 PHE   F CA    1 
ATOM   12589 C  C     . PHE   E 4  199 ? -0.713  46.773  -102.585 1.00 61.92  ? 199 PHE   F C     1 
ATOM   12590 O  O     . PHE   E 4  199 ? -0.968  47.690  -103.370 1.00 61.50  ? 199 PHE   F O     1 
ATOM   12591 C  CB    . PHE   E 4  199 ? 1.286   45.323  -102.919 1.00 50.21  ? 199 PHE   F CB    1 
ATOM   12592 C  CG    . PHE   E 4  199 ? 2.008   46.503  -103.472 1.00 65.53  ? 199 PHE   F CG    1 
ATOM   12593 C  CD1   . PHE   E 4  199 ? 2.154   46.662  -104.844 1.00 68.54  ? 199 PHE   F CD1   1 
ATOM   12594 C  CD2   . PHE   E 4  199 ? 2.511   47.478  -102.634 1.00 60.51  ? 199 PHE   F CD2   1 
ATOM   12595 C  CE1   . PHE   E 4  199 ? 2.812   47.763  -105.362 1.00 70.61  ? 199 PHE   F CE1   1 
ATOM   12596 C  CE2   . PHE   E 4  199 ? 3.168   48.584  -103.147 1.00 64.56  ? 199 PHE   F CE2   1 
ATOM   12597 C  CZ    . PHE   E 4  199 ? 3.319   48.729  -104.509 1.00 67.43  ? 199 PHE   F CZ    1 
ATOM   12598 N  N     . ASP   E 4  200 ? -0.845  46.886  -101.268 1.00 65.31  ? 200 ASP   F N     1 
ATOM   12599 C  CA    . ASP   E 4  200 ? -0.997  48.188  -100.633 1.00 63.84  ? 200 ASP   F CA    1 
ATOM   12600 C  C     . ASP   E 4  200 ? 0.091   48.348  -99.579  1.00 61.77  ? 200 ASP   F C     1 
ATOM   12601 O  O     . ASP   E 4  200 ? 0.787   47.389  -99.219  1.00 66.60  ? 200 ASP   F O     1 
ATOM   12602 C  CB    . ASP   E 4  200 ? -2.407  48.396  -100.044 1.00 50.45  ? 200 ASP   F CB    1 
ATOM   12603 C  CG    . ASP   E 4  200 ? -2.709  47.513  -98.839  1.00 63.55  ? 200 ASP   F CG    1 
ATOM   12604 O  OD1   . ASP   E 4  200 ? -1.790  47.124  -98.079  1.00 53.74  ? 200 ASP   F OD1   1 
ATOM   12605 O  OD2   . ASP   E 4  200 ? -3.910  47.213  -98.654  1.00 69.89  ? 200 ASP   F OD2   1 
ATOM   12606 N  N     . ILE   E 4  201 ? 0.257   49.590  -99.118  1.00 61.53  ? 201 ILE   F N     1 
ATOM   12607 C  CA    . ILE   E 4  201 ? 1.295   49.962  -98.158  1.00 56.85  ? 201 ILE   F CA    1 
ATOM   12608 C  C     . ILE   E 4  201 ? 0.623   50.517  -96.911  1.00 53.58  ? 201 ILE   F C     1 
ATOM   12609 O  O     . ILE   E 4  201 ? -0.085  51.530  -96.984  1.00 52.40  ? 201 ILE   F O     1 
ATOM   12610 C  CB    . ILE   E 4  201 ? 2.276   50.995  -98.739  1.00 52.21  ? 201 ILE   F CB    1 
ATOM   12611 C  CG1   . ILE   E 4  201 ? 2.999   50.425  -99.963  1.00 46.59  ? 201 ILE   F CG1   1 
ATOM   12612 C  CG2   . ILE   E 4  201 ? 3.239   51.464  -97.647  1.00 49.10  ? 201 ILE   F CG2   1 
ATOM   12613 C  CD1   . ILE   E 4  201 ? 4.224   51.174  -100.361 1.00 44.91  ? 201 ILE   F CD1   1 
ATOM   12614 N  N     . ARG   E 4  202 ? 0.852   49.857  -95.773  1.00 50.52  ? 202 ARG   F N     1 
ATOM   12615 C  CA    . ARG   E 4  202 ? 0.448   50.355  -94.466  1.00 40.72  ? 202 ARG   F CA    1 
ATOM   12616 C  C     . ARG   E 4  202 ? 1.585   51.167  -93.863  1.00 50.65  ? 202 ARG   F C     1 
ATOM   12617 O  O     . ARG   E 4  202 ? 2.728   50.698  -93.809  1.00 50.95  ? 202 ARG   F O     1 
ATOM   12618 C  CB    . ARG   E 4  202 ? 0.089   49.199  -93.532  1.00 46.43  ? 202 ARG   F CB    1 
ATOM   12619 C  CG    . ARG   E 4  202 ? 0.064   49.549  -92.038  1.00 44.71  ? 202 ARG   F CG    1 
ATOM   12620 C  CD    . ARG   E 4  202 ? -0.960  50.641  -91.740  1.00 50.00  ? 202 ARG   F CD    1 
ATOM   12621 N  NE    . ARG   E 4  202 ? -2.315  50.235  -92.096  1.00 49.45  ? 202 ARG   F NE    1 
ATOM   12622 C  CZ    . ARG   E 4  202 ? -3.061  49.434  -91.347  1.00 49.56  ? 202 ARG   F CZ    1 
ATOM   12623 N  NH1   . ARG   E 4  202 ? -2.611  48.948  -90.204  1.00 50.89  ? 202 ARG   F NH1   1 
ATOM   12624 N  NH2   . ARG   E 4  202 ? -4.286  49.112  -91.755  1.00 50.12  ? 202 ARG   F NH2   1 
ATOM   12625 N  N     . SER   E 4  203 ? 1.272   52.390  -93.429  1.00 50.24  ? 203 SER   F N     1 
ATOM   12626 C  CA    . SER   E 4  203 ? 2.189   53.215  -92.649  1.00 49.52  ? 203 SER   F CA    1 
ATOM   12627 C  C     . SER   E 4  203 ? 1.555   53.495  -91.297  1.00 49.56  ? 203 SER   F C     1 
ATOM   12628 O  O     . SER   E 4  203 ? 0.370   53.834  -91.219  1.00 48.07  ? 203 SER   F O     1 
ATOM   12629 C  CB    . SER   E 4  203 ? 2.514   54.535  -93.347  1.00 43.21  ? 203 SER   F CB    1 
ATOM   12630 O  OG    . SER   E 4  203 ? 3.421   54.340  -94.409  1.00 49.68  ? 203 SER   F OG    1 
ATOM   12631 N  N     . TRP   E 4  204 ? 2.333   53.338  -90.239  1.00 52.01  ? 204 TRP   F N     1 
ATOM   12632 C  CA    . TRP   E 4  204 ? 1.873   53.650  -88.896  1.00 56.51  ? 204 TRP   F CA    1 
ATOM   12633 C  C     . TRP   E 4  204 ? 2.386   55.032  -88.528  1.00 53.29  ? 204 TRP   F C     1 
ATOM   12634 O  O     . TRP   E 4  204 ? 3.574   55.328  -88.695  1.00 44.77  ? 204 TRP   F O     1 
ATOM   12635 C  CB    . TRP   E 4  204 ? 2.339   52.597  -87.883  1.00 49.64  ? 204 TRP   F CB    1 
ATOM   12636 C  CG    . TRP   E 4  204 ? 1.755   51.257  -88.183  1.00 52.98  ? 204 TRP   F CG    1 
ATOM   12637 C  CD1   . TRP   E 4  204 ? 0.483   50.835  -87.907  1.00 59.57  ? 204 TRP   F CD1   1 
ATOM   12638 C  CD2   . TRP   E 4  204 ? 2.400   50.175  -88.861  1.00 53.46  ? 204 TRP   F CD2   1 
ATOM   12639 N  NE1   . TRP   E 4  204 ? 0.303   49.547  -88.359  1.00 60.59  ? 204 TRP   F NE1   1 
ATOM   12640 C  CE2   . TRP   E 4  204 ? 1.466   49.118  -88.946  1.00 65.01  ? 204 TRP   F CE2   1 
ATOM   12641 C  CE3   . TRP   E 4  204 ? 3.682   49.990  -89.395  1.00 55.16  ? 204 TRP   F CE3   1 
ATOM   12642 C  CZ2   . TRP   E 4  204 ? 1.776   47.891  -89.546  1.00 62.52  ? 204 TRP   F CZ2   1 
ATOM   12643 C  CZ3   . TRP   E 4  204 ? 3.988   48.775  -89.991  1.00 57.94  ? 204 TRP   F CZ3   1 
ATOM   12644 C  CH2   . TRP   E 4  204 ? 3.037   47.740  -90.063  1.00 56.87  ? 204 TRP   F CH2   1 
ATOM   12645 N  N     . VAL   E 4  205 ? 1.477   55.885  -88.071  1.00 48.64  ? 205 VAL   F N     1 
ATOM   12646 C  CA    . VAL   E 4  205 ? 1.804   57.238  -87.658  1.00 46.51  ? 205 VAL   F CA    1 
ATOM   12647 C  C     . VAL   E 4  205 ? 1.307   57.406  -86.228  1.00 37.49  ? 205 VAL   F C     1 
ATOM   12648 O  O     . VAL   E 4  205 ? 0.163   57.055  -85.923  1.00 44.79  ? 205 VAL   F O     1 
ATOM   12649 C  CB    . VAL   E 4  205 ? 1.180   58.280  -88.612  1.00 49.66  ? 205 VAL   F CB    1 
ATOM   12650 C  CG1   . VAL   E 4  205 ? 1.821   59.650  -88.428  1.00 47.09  ? 205 VAL   F CG1   1 
ATOM   12651 C  CG2   . VAL   E 4  205 ? 1.335   57.848  -90.055  1.00 42.24  ? 205 VAL   F CG2   1 
ATOM   12652 N  N     . LEU   E 4  206 ? 2.171   57.908  -85.351  1.00 36.83  ? 206 LEU   F N     1 
ATOM   12653 C  CA    . LEU   E 4  206 ? 1.813   58.264  -83.981  1.00 35.02  ? 206 LEU   F CA    1 
ATOM   12654 C  C     . LEU   E 4  206 ? 1.863   59.777  -83.827  1.00 37.53  ? 206 LEU   F C     1 
ATOM   12655 O  O     . LEU   E 4  206 ? 2.935   60.376  -83.958  1.00 40.21  ? 206 LEU   F O     1 
ATOM   12656 C  CB    . LEU   E 4  206 ? 2.765   57.614  -82.976  1.00 42.77  ? 206 LEU   F CB    1 
ATOM   12657 C  CG    . LEU   E 4  206 ? 2.630   58.110  -81.521  1.00 44.44  ? 206 LEU   F CG    1 
ATOM   12658 C  CD1   . LEU   E 4  206 ? 1.501   57.396  -80.802  1.00 41.00  ? 206 LEU   F CD1   1 
ATOM   12659 C  CD2   . LEU   E 4  206 ? 3.942   57.997  -80.734  1.00 39.65  ? 206 LEU   F CD2   1 
ATOM   12660 N  N     . VAL   E 4  207 ? 0.717   60.387  -83.525  1.00 42.19  ? 207 VAL   F N     1 
ATOM   12661 C  CA    . VAL   E 4  207 ? 0.631   61.806  -83.172  1.00 38.13  ? 207 VAL   F CA    1 
ATOM   12662 C  C     . VAL   E 4  207 ? 0.548   61.916  -81.652  1.00 40.47  ? 207 VAL   F C     1 
ATOM   12663 O  O     . VAL   E 4  207 ? -0.398  61.397  -81.048  1.00 42.18  ? 207 VAL   F O     1 
ATOM   12664 C  CB    . VAL   E 4  207 ? -0.581  62.473  -83.835  1.00 37.93  ? 207 VAL   F CB    1 
ATOM   12665 C  CG1   . VAL   E 4  207 ? -0.624  63.952  -83.486  1.00 41.23  ? 207 VAL   F CG1   1 
ATOM   12666 C  CG2   . VAL   E 4  207 ? -0.539  62.273  -85.347  1.00 39.18  ? 207 VAL   F CG2   1 
ATOM   12667 N  N     . ASP   E 4  208 ? 1.537   62.592  -81.028  1.00 42.32  ? 208 ASP   F N     1 
ATOM   12668 C  CA    . ASP   E 4  208 ? 1.614   62.749  -79.572  1.00 46.74  ? 208 ASP   F CA    1 
ATOM   12669 C  C     . ASP   E 4  208 ? 0.844   63.996  -79.111  1.00 45.03  ? 208 ASP   F C     1 
ATOM   12670 O  O     . ASP   E 4  208 ? 0.143   64.650  -79.890  1.00 40.29  ? 208 ASP   F O     1 
ATOM   12671 C  CB    . ASP   E 4  208 ? 3.076   62.778  -79.089  1.00 35.18  ? 208 ASP   F CB    1 
ATOM   12672 C  CG    . ASP   E 4  208 ? 3.830   64.072  -79.463  1.00 43.55  ? 208 ASP   F CG    1 
ATOM   12673 O  OD1   . ASP   E 4  208 ? 3.226   65.030  -79.999  1.00 38.94  ? 208 ASP   F OD1   1 
ATOM   12674 O  OD2   . ASP   E 4  208 ? 5.063   64.118  -79.228  1.00 45.76  ? 208 ASP   F OD2   1 
ATOM   12675 N  N     . HIS   E 4  209 ? 0.979   64.340  -77.824  1.00 43.89  ? 209 HIS   F N     1 
ATOM   12676 C  CA    . HIS   E 4  209 ? 0.179   65.399  -77.212  1.00 40.94  ? 209 HIS   F CA    1 
ATOM   12677 C  C     . HIS   E 4  209 ? 0.628   66.810  -77.591  1.00 47.39  ? 209 HIS   F C     1 
ATOM   12678 O  O     . HIS   E 4  209 ? -0.131  67.761  -77.374  1.00 51.31  ? 209 HIS   F O     1 
ATOM   12679 C  CB    . HIS   E 4  209 ? 0.208   65.266  -75.693  1.00 43.10  ? 209 HIS   F CB    1 
ATOM   12680 C  CG    . HIS   E 4  209 ? 1.580   65.392  -75.118  1.00 41.61  ? 209 HIS   F CG    1 
ATOM   12681 N  ND1   . HIS   E 4  209 ? 2.534   64.410  -75.263  1.00 44.34  ? 209 HIS   F ND1   1 
ATOM   12682 C  CD2   . HIS   E 4  209 ? 2.170   66.398  -74.431  1.00 45.19  ? 209 HIS   F CD2   1 
ATOM   12683 C  CE1   . HIS   E 4  209 ? 3.653   64.803  -74.678  1.00 46.89  ? 209 HIS   F CE1   1 
ATOM   12684 N  NE2   . HIS   E 4  209 ? 3.457   66.002  -74.160  1.00 41.64  ? 209 HIS   F NE2   1 
ATOM   12685 N  N     . LEU   E 4  210 ? 1.829   66.981  -78.134  1.00 45.08  ? 210 LEU   F N     1 
ATOM   12686 C  CA    . LEU   E 4  210 ? 2.226   68.273  -78.680  1.00 41.57  ? 210 LEU   F CA    1 
ATOM   12687 C  C     . LEU   E 4  210 ? 1.813   68.448  -80.136  1.00 43.96  ? 210 LEU   F C     1 
ATOM   12688 O  O     . LEU   E 4  210 ? 2.018   69.530  -80.698  1.00 46.00  ? 210 LEU   F O     1 
ATOM   12689 C  CB    . LEU   E 4  210 ? 3.736   68.466  -78.533  1.00 37.61  ? 210 LEU   F CB    1 
ATOM   12690 C  CG    . LEU   E 4  210 ? 4.301   68.331  -77.107  1.00 39.06  ? 210 LEU   F CG    1 
ATOM   12691 C  CD1   . LEU   E 4  210 ? 5.787   68.380  -77.153  1.00 34.17  ? 210 LEU   F CD1   1 
ATOM   12692 C  CD2   . LEU   E 4  210 ? 3.785   69.394  -76.148  1.00 32.98  ? 210 LEU   F CD2   1 
ATOM   12693 N  N     . TYR   E 4  211 ? 1.195   67.424  -80.732  1.00 43.41  ? 211 TYR   F N     1 
ATOM   12694 C  CA    . TYR   E 4  211 ? 0.903   67.329  -82.167  1.00 35.65  ? 211 TYR   F CA    1 
ATOM   12695 C  C     . TYR   E 4  211 ? 2.154   67.171  -83.019  1.00 37.58  ? 211 TYR   F C     1 
ATOM   12696 O  O     . TYR   E 4  211 ? 2.200   67.666  -84.144  1.00 39.57  ? 211 TYR   F O     1 
ATOM   12697 C  CB    . TYR   E 4  211 ? 0.091   68.504  -82.692  1.00 33.47  ? 211 TYR   F CB    1 
ATOM   12698 C  CG    . TYR   E 4  211 ? -0.997  68.041  -83.630  1.00 38.26  ? 211 TYR   F CG    1 
ATOM   12699 C  CD1   . TYR   E 4  211 ? -2.221  67.647  -83.123  1.00 40.84  ? 211 TYR   F CD1   1 
ATOM   12700 C  CD2   . TYR   E 4  211 ? -0.801  67.958  -85.010  1.00 35.83  ? 211 TYR   F CD2   1 
ATOM   12701 C  CE1   . TYR   E 4  211 ? -3.235  67.204  -83.946  1.00 41.89  ? 211 TYR   F CE1   1 
ATOM   12702 C  CE2   . TYR   E 4  211 ? -1.835  67.506  -85.853  1.00 37.95  ? 211 TYR   F CE2   1 
ATOM   12703 C  CZ    . TYR   E 4  211 ? -3.049  67.132  -85.294  1.00 32.88  ? 211 TYR   F CZ    1 
ATOM   12704 O  OH    . TYR   E 4  211 ? -4.115  66.683  -86.029  1.00 32.29  ? 211 TYR   F OH    1 
ATOM   12705 N  N     . ASN   E 4  212 ? 3.175   66.506  -82.491  1.00 36.67  ? 212 ASN   F N     1 
ATOM   12706 C  CA    . ASN   E 4  212 ? 4.238   65.985  -83.335  1.00 43.63  ? 212 ASN   F CA    1 
ATOM   12707 C  C     . ASN   E 4  212 ? 3.701   64.824  -84.169  1.00 48.81  ? 212 ASN   F C     1 
ATOM   12708 O  O     . ASN   E 4  212 ? 3.117   63.879  -83.626  1.00 45.11  ? 212 ASN   F O     1 
ATOM   12709 C  CB    . ASN   E 4  212 ? 5.406   65.513  -82.478  1.00 46.06  ? 212 ASN   F CB    1 
ATOM   12710 C  CG    . ASN   E 4  212 ? 6.198   66.649  -81.935  1.00 45.52  ? 212 ASN   F CG    1 
ATOM   12711 O  OD1   . ASN   E 4  212 ? 6.358   67.653  -82.611  1.00 43.36  ? 212 ASN   F OD1   1 
ATOM   12712 N  ND2   . ASN   E 4  212 ? 6.681   66.521  -80.698  1.00 44.18  ? 212 ASN   F ND2   1 
ATOM   12713 N  N     . ILE   E 4  213 ? 3.898   64.884  -85.486  1.00 39.41  ? 213 ILE   F N     1 
ATOM   12714 C  CA    . ILE   E 4  213 ? 3.483   63.801  -86.373  1.00 41.33  ? 213 ILE   F CA    1 
ATOM   12715 C  C     . ILE   E 4  213 ? 4.688   62.897  -86.607  1.00 43.21  ? 213 ILE   F C     1 
ATOM   12716 O  O     . ILE   E 4  213 ? 5.624   63.268  -87.321  1.00 48.02  ? 213 ILE   F O     1 
ATOM   12717 C  CB    . ILE   E 4  213 ? 2.906   64.333  -87.685  1.00 37.19  ? 213 ILE   F CB    1 
ATOM   12718 C  CG1   . ILE   E 4  213 ? 1.706   65.231  -87.384  1.00 31.51  ? 213 ILE   F CG1   1 
ATOM   12719 C  CG2   . ILE   E 4  213 ? 2.512   63.179  -88.580  1.00 40.61  ? 213 ILE   F CG2   1 
ATOM   12720 C  CD1   . ILE   E 4  213 ? 1.189   65.981  -88.576  1.00 36.90  ? 213 ILE   F CD1   1 
ATOM   12721 N  N     . TYR   E 4  214 ? 4.669   61.714  -85.982  1.00 46.48  ? 214 TYR   F N     1 
ATOM   12722 C  CA    . TYR   E 4  214 ? 5.746   60.733  -86.046  1.00 41.05  ? 214 TYR   F CA    1 
ATOM   12723 C  C     . TYR   E 4  214 ? 5.396   59.637  -87.046  1.00 47.65  ? 214 TYR   F C     1 
ATOM   12724 O  O     . TYR   E 4  214 ? 4.240   59.215  -87.150  1.00 46.54  ? 214 TYR   F O     1 
ATOM   12725 C  CB    . TYR   E 4  214 ? 6.012   60.125  -84.660  1.00 43.92  ? 214 TYR   F CB    1 
ATOM   12726 C  CG    . TYR   E 4  214 ? 6.661   61.108  -83.709  1.00 42.52  ? 214 TYR   F CG    1 
ATOM   12727 C  CD1   . TYR   E 4  214 ? 7.963   61.514  -83.911  1.00 45.68  ? 214 TYR   F CD1   1 
ATOM   12728 C  CD2   . TYR   E 4  214 ? 5.965   61.661  -82.647  1.00 46.14  ? 214 TYR   F CD2   1 
ATOM   12729 C  CE1   . TYR   E 4  214 ? 8.571   62.421  -83.094  1.00 41.28  ? 214 TYR   F CE1   1 
ATOM   12730 C  CE2   . TYR   E 4  214 ? 6.574   62.584  -81.808  1.00 52.66  ? 214 TYR   F CE2   1 
ATOM   12731 C  CZ    . TYR   E 4  214 ? 7.889   62.956  -82.049  1.00 50.10  ? 214 TYR   F CZ    1 
ATOM   12732 O  OH    . TYR   E 4  214 ? 8.549   63.867  -81.258  1.00 57.12  ? 214 TYR   F OH    1 
ATOM   12733 N  N     . LEU   E 4  215 ? 6.396   59.194  -87.798  1.00 55.01  ? 215 LEU   F N     1 
ATOM   12734 C  CA    . LEU   E 4  215 ? 6.241   58.138  -88.795  1.00 49.08  ? 215 LEU   F CA    1 
ATOM   12735 C  C     . LEU   E 4  215 ? 7.239   57.034  -88.468  1.00 48.78  ? 215 LEU   F C     1 
ATOM   12736 O  O     . LEU   E 4  215 ? 8.456   57.242  -88.537  1.00 49.33  ? 215 LEU   F O     1 
ATOM   12737 C  CB    . LEU   E 4  215 ? 6.456   58.686  -90.201  1.00 44.21  ? 215 LEU   F CB    1 
ATOM   12738 C  CG    . LEU   E 4  215 ? 6.563   57.695  -91.357  1.00 46.79  ? 215 LEU   F CG    1 
ATOM   12739 C  CD1   . LEU   E 4  215 ? 5.270   56.874  -91.539  1.00 43.20  ? 215 LEU   F CD1   1 
ATOM   12740 C  CD2   . LEU   E 4  215 ? 6.957   58.415  -92.660  1.00 33.97  ? 215 LEU   F CD2   1 
ATOM   12741 N  N     . TYR   E 4  216 ? 6.721   55.883  -88.067  1.00 40.76  ? 216 TYR   F N     1 
ATOM   12742 C  CA    . TYR   E 4  216 ? 7.540   54.700  -87.862  1.00 51.05  ? 216 TYR   F CA    1 
ATOM   12743 C  C     . TYR   E 4  216 ? 8.333   54.385  -89.125  1.00 57.05  ? 216 TYR   F C     1 
ATOM   12744 O  O     . TYR   E 4  216 ? 7.771   54.346  -90.224  1.00 53.69  ? 216 TYR   F O     1 
ATOM   12745 C  CB    . TYR   E 4  216 ? 6.621   53.538  -87.497  1.00 46.67  ? 216 TYR   F CB    1 
ATOM   12746 C  CG    . TYR   E 4  216 ? 7.298   52.260  -87.136  1.00 54.85  ? 216 TYR   F CG    1 
ATOM   12747 C  CD1   . TYR   E 4  216 ? 8.650   52.232  -86.798  1.00 56.40  ? 216 TYR   F CD1   1 
ATOM   12748 C  CD2   . TYR   E 4  216 ? 6.577   51.061  -87.126  1.00 54.21  ? 216 TYR   F CD2   1 
ATOM   12749 C  CE1   . TYR   E 4  216 ? 9.267   51.046  -86.456  1.00 60.82  ? 216 TYR   F CE1   1 
ATOM   12750 C  CE2   . TYR   E 4  216 ? 7.185   49.870  -86.789  1.00 56.53  ? 216 TYR   F CE2   1 
ATOM   12751 C  CZ    . TYR   E 4  216 ? 8.528   49.866  -86.454  1.00 58.22  ? 216 TYR   F CZ    1 
ATOM   12752 O  OH    . TYR   E 4  216 ? 9.133   48.684  -86.125  1.00 53.67  ? 216 TYR   F OH    1 
ATOM   12753 N  N     . ARG   E 4  217 ? 9.648   54.160  -88.971  1.00 55.85  ? 217 ARG   F N     1 
ATOM   12754 C  CA    . ARG   E 4  217 ? 10.493  53.913  -90.145  1.00 55.75  ? 217 ARG   F CA    1 
ATOM   12755 C  C     . ARG   E 4  217 ? 10.193  52.583  -90.828  1.00 53.88  ? 217 ARG   F C     1 
ATOM   12756 O  O     . ARG   E 4  217 ? 10.455  52.453  -92.027  1.00 52.34  ? 217 ARG   F O     1 
ATOM   12757 C  CB    . ARG   E 4  217 ? 11.983  53.981  -89.784  1.00 55.27  ? 217 ARG   F CB    1 
ATOM   12758 C  CG    . ARG   E 4  217 ? 12.432  53.156  -88.581  1.00 65.70  ? 217 ARG   F CG    1 
ATOM   12759 C  CD    . ARG   E 4  217 ? 13.957  53.249  -88.472  1.00 71.33  ? 217 ARG   F CD    1 
ATOM   12760 N  NE    . ARG   E 4  217 ? 14.521  52.892  -87.171  1.00 75.08  ? 217 ARG   F NE    1 
ATOM   12761 C  CZ    . ARG   E 4  217 ? 14.476  51.682  -86.625  1.00 71.33  ? 217 ARG   F CZ    1 
ATOM   12762 N  NH1   . ARG   E 4  217 ? 13.765  50.702  -87.166  1.00 76.46  ? 217 ARG   F NH1   1 
ATOM   12763 N  NH2   . ARG   E 4  217 ? 15.163  51.449  -85.508  1.00 57.20  ? 217 ARG   F NH2   1 
ATOM   12764 N  N     . GLU   E 4  218 ? 9.618   51.613  -90.117  1.00 53.11  ? 218 GLU   F N     1 
ATOM   12765 C  CA    . GLU   E 4  218 ? 9.213   50.343  -90.712  1.00 54.85  ? 218 GLU   F CA    1 
ATOM   12766 C  C     . GLU   E 4  218 ? 7.754   50.412  -91.156  1.00 52.52  ? 218 GLU   F C     1 
ATOM   12767 O  O     . GLU   E 4  218 ? 6.853   50.512  -90.321  1.00 57.87  ? 218 GLU   F O     1 
ATOM   12768 C  CB    . GLU   E 4  218 ? 9.411   49.198  -89.721  1.00 57.77  ? 218 GLU   F CB    1 
ATOM   12769 C  CG    . GLU   E 4  218 ? 10.865  48.842  -89.443  1.00 67.55  ? 218 GLU   F CG    1 
ATOM   12770 C  CD    . GLU   E 4  218 ? 11.590  48.348  -90.682  1.00 61.80  ? 218 GLU   F CD    1 
ATOM   12771 O  OE1   . GLU   E 4  218 ? 10.909  47.849  -91.610  1.00 70.22  ? 218 GLU   F OE1   1 
ATOM   12772 O  OE2   . GLU   E 4  218 ? 12.833  48.470  -90.726  1.00 59.91  ? 218 GLU   F OE2   1 
ATOM   12773 N  N     . GLY   E 4  219 ? 7.521   50.340  -92.468  1.00 52.22  ? 219 GLY   F N     1 
ATOM   12774 C  CA    . GLY   E 4  219 ? 6.205   50.088  -93.016  1.00 47.03  ? 219 GLY   F CA    1 
ATOM   12775 C  C     . GLY   E 4  219 ? 6.073   48.658  -93.512  1.00 51.42  ? 219 GLY   F C     1 
ATOM   12776 O  O     . GLY   E 4  219 ? 6.961   47.821  -93.327  1.00 63.78  ? 219 GLY   F O     1 
ATOM   12777 N  N     . VAL   E 4  220 ? 4.937   48.371  -94.151  1.00 49.02  ? 220 VAL   F N     1 
ATOM   12778 C  CA    . VAL   E 4  220 ? 4.720   47.037  -94.726  1.00 61.49  ? 220 VAL   F CA    1 
ATOM   12779 C  C     . VAL   E 4  220 ? 3.872   47.145  -95.983  1.00 59.04  ? 220 VAL   F C     1 
ATOM   12780 O  O     . VAL   E 4  220 ? 2.937   47.950  -96.057  1.00 57.10  ? 220 VAL   F O     1 
ATOM   12781 C  CB    . VAL   E 4  220 ? 4.050   46.033  -93.751  1.00 54.36  ? 220 VAL   F CB    1 
ATOM   12782 C  CG1   . VAL   E 4  220 ? 4.788   45.971  -92.431  1.00 62.68  ? 220 VAL   F CG1   1 
ATOM   12783 C  CG2   . VAL   E 4  220 ? 2.569   46.343  -93.564  1.00 49.18  ? 220 VAL   F CG2   1 
ATOM   12784 N  N     . LEU   E 4  221 ? 4.202   46.306  -96.966  1.00 63.99  ? 221 LEU   F N     1 
ATOM   12785 C  CA    . LEU   E 4  221 ? 3.322   46.022  -98.092  1.00 66.01  ? 221 LEU   F CA    1 
ATOM   12786 C  C     . LEU   E 4  221 ? 2.563   44.741  -97.784  1.00 70.15  ? 221 LEU   F C     1 
ATOM   12787 O  O     . LEU   E 4  221 ? 3.177   43.715  -97.469  1.00 66.37  ? 221 LEU   F O     1 
ATOM   12788 C  CB    . LEU   E 4  221 ? 4.102   45.852  -99.399  1.00 65.04  ? 221 LEU   F CB    1 
ATOM   12789 C  CG    . LEU   E 4  221 ? 4.948   46.965  -100.021 1.00 62.14  ? 221 LEU   F CG    1 
ATOM   12790 C  CD1   . LEU   E 4  221 ? 6.234   47.192  -99.242  1.00 60.93  ? 221 LEU   F CD1   1 
ATOM   12791 C  CD2   . LEU   E 4  221 ? 5.272   46.598  -101.463 1.00 61.13  ? 221 LEU   F CD2   1 
ATOM   12792 N  N     . ARG   E 4  222 ? 1.234   44.805  -97.846  1.00 71.91  ? 222 ARG   F N     1 
ATOM   12793 C  CA    . ARG   E 4  222 ? 0.405   43.599  -97.843  1.00 72.05  ? 222 ARG   F CA    1 
ATOM   12794 C  C     . ARG   E 4  222 ? 0.218   43.198  -99.301  1.00 68.04  ? 222 ARG   F C     1 
ATOM   12795 O  O     . ARG   E 4  222 ? -0.598  43.786  -100.017 1.00 66.76  ? 222 ARG   F O     1 
ATOM   12796 C  CB    . ARG   E 4  222 ? -0.934  43.838  -97.148  1.00 67.73  ? 222 ARG   F CB    1 
ATOM   12797 C  CG    . ARG   E 4  222 ? -0.876  43.882  -95.628  1.00 64.99  ? 222 ARG   F CG    1 
ATOM   12798 C  CD    . ARG   E 4  222 ? -0.638  45.295  -95.110  1.00 73.22  ? 222 ARG   F CD    1 
ATOM   12799 N  NE    . ARG   E 4  222 ? -1.747  46.204  -95.396  1.00 68.74  ? 222 ARG   F NE    1 
ATOM   12800 C  CZ    . ARG   E 4  222 ? -2.647  46.603  -94.504  1.00 57.27  ? 222 ARG   F CZ    1 
ATOM   12801 N  NH1   . ARG   E 4  222 ? -2.619  46.174  -93.248  1.00 57.52  ? 222 ARG   F NH1   1 
ATOM   12802 N  NH2   . ARG   E 4  222 ? -3.594  47.458  -94.877  1.00 44.90  ? 222 ARG   F NH2   1 
ATOM   12803 N  N     . THR   E 4  223 ? 0.980   42.201  -99.748  1.00 67.99  ? 223 THR   F N     1 
ATOM   12804 C  CA    . THR   E 4  223 ? 1.020   41.851  -101.163 1.00 72.02  ? 223 THR   F CA    1 
ATOM   12805 C  C     . THR   E 4  223 ? -0.234  41.067  -101.543 1.00 71.31  ? 223 THR   F C     1 
ATOM   12806 O  O     . THR   E 4  223 ? -1.178  40.932  -100.760 1.00 71.80  ? 223 THR   F O     1 
ATOM   12807 C  CB    . THR   E 4  223 ? 2.294   41.073  -101.488 1.00 62.00  ? 223 THR   F CB    1 
ATOM   12808 O  OG1   . THR   E 4  223 ? 2.213   39.757  -100.934 1.00 66.94  ? 223 THR   F OG1   1 
ATOM   12809 C  CG2   . THR   E 4  223 ? 3.509   41.782  -100.915 1.00 65.15  ? 223 THR   F CG2   1 
ATOM   12810 N  N     . SER   E 4  224 ? -0.266  40.567  -102.776 1.00 83.81  ? 224 SER   F N     1 
ATOM   12811 C  CA    . SER   E 4  224 ? -1.277  39.623  -103.229 1.00 80.41  ? 224 SER   F CA    1 
ATOM   12812 C  C     . SER   E 4  224 ? -0.579  38.329  -103.618 1.00 83.48  ? 224 SER   F C     1 
ATOM   12813 O  O     . SER   E 4  224 ? 0.544   38.353  -104.133 1.00 85.69  ? 224 SER   F O     1 
ATOM   12814 C  CB    . SER   E 4  224 ? -2.078  40.174  -104.412 1.00 78.12  ? 224 SER   F CB    1 
ATOM   12815 O  OG    . SER   E 4  224 ? -3.188  39.346  -104.696 1.00 72.82  ? 224 SER   F OG    1 
ATOM   12816 N  N     . SER   E 4  225 ? -1.237  37.197  -103.348 1.00 91.31  ? 225 SER   F N     1 
ATOM   12817 C  CA    . SER   E 4  225 ? -0.638  35.889  -103.608 1.00 90.21  ? 225 SER   F CA    1 
ATOM   12818 C  C     . SER   E 4  225 ? -0.818  35.432  -105.052 1.00 87.65  ? 225 SER   F C     1 
ATOM   12819 O  O     . SER   E 4  225 ? -0.020  34.616  -105.525 1.00 92.22  ? 225 SER   F O     1 
ATOM   12820 C  CB    . SER   E 4  225 ? -1.222  34.833  -102.655 1.00 92.19  ? 225 SER   F CB    1 
ATOM   12821 O  OG    . SER   E 4  225 ? -0.207  34.146  -101.924 1.00 85.48  ? 225 SER   F OG    1 
ATOM   12822 N  N     . GLU   E 4  226 ? -1.836  35.928  -105.761 1.00 91.09  ? 226 GLU   F N     1 
ATOM   12823 C  CA    . GLU   E 4  226 ? -2.067  35.540  -107.147 1.00 96.33  ? 226 GLU   F CA    1 
ATOM   12824 C  C     . GLU   E 4  226 ? -2.076  36.767  -108.054 1.00 92.60  ? 226 GLU   F C     1 
ATOM   12825 O  O     . GLU   E 4  226 ? -2.402  37.871  -107.609 1.00 90.42  ? 226 GLU   F O     1 
ATOM   12826 C  CB    . GLU   E 4  226 ? -3.385  34.769  -107.317 1.00 102.66 ? 226 GLU   F CB    1 
ATOM   12827 C  CG    . GLU   E 4  226 ? -3.212  33.246  -107.439 1.00 94.04  ? 226 GLU   F CG    1 
ATOM   12828 C  CD    . GLU   E 4  226 ? -2.806  32.586  -106.126 1.00 99.00  ? 226 GLU   F CD    1 
ATOM   12829 O  OE1   . GLU   E 4  226 ? -3.285  33.041  -105.061 1.00 99.17  ? 226 GLU   F OE1   1 
ATOM   12830 O  OE2   . GLU   E 4  226 ? -2.007  31.617  -106.158 1.00 94.95  ? 226 GLU   F OE2   1 
ATOM   12831 N  N     . PRO   E 4  227 ? -1.750  36.595  -109.338 1.00 99.77  ? 227 PRO   F N     1 
ATOM   12832 C  CA    . PRO   E 4  227 ? -1.431  37.753  -110.184 1.00 88.79  ? 227 PRO   F CA    1 
ATOM   12833 C  C     . PRO   E 4  227 ? -2.651  38.601  -110.497 1.00 84.25  ? 227 PRO   F C     1 
ATOM   12834 O  O     . PRO   E 4  227 ? -3.756  38.093  -110.697 1.00 83.36  ? 227 PRO   F O     1 
ATOM   12835 C  CB    . PRO   E 4  227 ? -0.863  37.113  -111.455 1.00 91.66  ? 227 PRO   F CB    1 
ATOM   12836 C  CG    . PRO   E 4  227 ? -1.548  35.788  -111.525 1.00 90.42  ? 227 PRO   F CG    1 
ATOM   12837 C  CD    . PRO   E 4  227 ? -1.706  35.329  -110.095 1.00 94.00  ? 227 PRO   F CD    1 
ATOM   12838 N  N     . TYR   E 4  228 ? -2.428  39.912  -110.558 1.00 86.51  ? 228 TYR   F N     1 
ATOM   12839 C  CA    . TYR   E 4  228 ? -3.496  40.852  -110.866 1.00 89.39  ? 228 TYR   F CA    1 
ATOM   12840 C  C     . TYR   E 4  228 ? -4.225  40.429  -112.141 1.00 88.28  ? 228 TYR   F C     1 
ATOM   12841 O  O     . TYR   E 4  228 ? -3.654  39.782  -113.023 1.00 88.89  ? 228 TYR   F O     1 
ATOM   12842 C  CB    . TYR   E 4  228 ? -2.917  42.265  -110.999 1.00 71.73  ? 228 TYR   F CB    1 
ATOM   12843 C  CG    . TYR   E 4  228 ? -3.951  43.343  -111.146 1.00 65.20  ? 228 TYR   F CG    1 
ATOM   12844 C  CD1   . TYR   E 4  228 ? -4.832  43.634  -110.115 1.00 69.97  ? 228 TYR   F CD1   1 
ATOM   12845 C  CD2   . TYR   E 4  228 ? -4.045  44.077  -112.315 1.00 71.15  ? 228 TYR   F CD2   1 
ATOM   12846 C  CE1   . TYR   E 4  228 ? -5.784  44.620  -110.252 1.00 69.40  ? 228 TYR   F CE1   1 
ATOM   12847 C  CE2   . TYR   E 4  228 ? -4.994  45.069  -112.460 1.00 71.90  ? 228 TYR   F CE2   1 
ATOM   12848 C  CZ    . TYR   E 4  228 ? -5.856  45.336  -111.427 1.00 63.68  ? 228 TYR   F CZ    1 
ATOM   12849 O  OH    . TYR   E 4  228 ? -6.784  46.325  -111.580 1.00 58.93  ? 228 TYR   F OH    1 
ATOM   12850 N  N     . ASN   E 4  229 ? -5.506  40.789  -112.230 1.00 87.69  ? 229 ASN   F N     1 
ATOM   12851 C  CA    . ASN   E 4  229 ? -6.391  40.342  -113.304 1.00 89.05  ? 229 ASN   F CA    1 
ATOM   12852 C  C     . ASN   E 4  229 ? -6.764  41.543  -114.171 1.00 89.40  ? 229 ASN   F C     1 
ATOM   12853 O  O     . ASN   E 4  229 ? -7.661  42.313  -113.820 1.00 91.45  ? 229 ASN   F O     1 
ATOM   12854 C  CB    . ASN   E 4  229 ? -7.628  39.661  -112.723 1.00 92.50  ? 229 ASN   F CB    1 
ATOM   12855 C  CG    . ASN   E 4  229 ? -7.969  38.364  -113.432 1.00 90.00  ? 229 ASN   F CG    1 
ATOM   12856 O  OD1   . ASN   E 4  229 ? -8.928  38.291  -114.205 1.00 86.37  ? 229 ASN   F OD1   1 
ATOM   12857 N  ND2   . ASN   E 4  229 ? -7.177  37.331  -113.174 1.00 74.11  ? 229 ASN   F ND2   1 
ATOM   12858 N  N     . SER   E 4  230 ? -6.080  41.689  -115.310 1.00 98.00  ? 230 SER   F N     1 
ATOM   12859 C  CA    . SER   E 4  230 ? -6.291  42.799  -116.238 1.00 101.57 ? 230 SER   F CA    1 
ATOM   12860 C  C     . SER   E 4  230 ? -7.769  42.993  -116.559 1.00 105.52 ? 230 SER   F C     1 
ATOM   12861 O  O     . SER   E 4  230 ? -8.531  43.494  -115.725 1.00 98.60  ? 230 SER   F O     1 
ATOM   12862 C  CB    . SER   E 4  230 ? -5.494  42.568  -117.527 1.00 98.20  ? 230 SER   F CB    1 
ATOM   12863 O  OG    . SER   E 4  230 ? -4.814  43.745  -117.929 1.00 90.79  ? 230 SER   F OG    1 
ATOM   12864 N  N     . ALA   E 4  231 ? -8.186  42.615  -117.767 1.00 114.90 ? 231 ALA   F N     1 
ATOM   12865 C  CA    . ALA   E 4  231 ? -9.602  42.684  -118.109 1.00 118.51 ? 231 ALA   F CA    1 
ATOM   12866 C  C     . ALA   E 4  231 ? -10.413 41.818  -117.151 1.00 112.83 ? 231 ALA   F C     1 
ATOM   12867 O  O     . ALA   E 4  231 ? -9.970  40.747  -116.724 1.00 106.06 ? 231 ALA   F O     1 
ATOM   12868 C  CB    . ALA   E 4  231 ? -9.833  42.244  -119.557 1.00 112.36 ? 231 ALA   F CB    1 
ATOM   12869 N  N     . ASN   E 4  232 ? -11.607 42.296  -116.804 1.00 115.39 ? 232 ASN   F N     1 
ATOM   12870 C  CA    . ASN   E 4  232 ? -12.424 41.646  -115.786 1.00 115.40 ? 232 ASN   F CA    1 
ATOM   12871 C  C     . ASN   E 4  232 ? -11.828 41.848  -114.397 1.00 117.31 ? 232 ASN   F C     1 
ATOM   12872 O  O     . ASN   E 4  232 ? -10.620 41.672  -114.200 1.00 114.24 ? 232 ASN   F O     1 
ATOM   12873 C  CB    . ASN   E 4  232 ? -12.572 40.153  -116.080 1.00 112.56 ? 232 ASN   F CB    1 
ATOM   12874 C  CG    . ASN   E 4  232 ? -12.748 39.334  -114.821 1.00 113.96 ? 232 ASN   F CG    1 
ATOM   12875 O  OD1   . ASN   E 4  232 ? -11.769 38.928  -114.190 1.00 110.92 ? 232 ASN   F OD1   1 
ATOM   12876 N  ND2   . ASN   E 4  232 ? -13.999 39.093  -114.441 1.00 112.49 ? 232 ASN   F ND2   1 
ATOM   12877 N  N     . PHE   E 4  233 ? -12.676 42.220  -113.429 1.00 117.65 ? 233 PHE   F N     1 
ATOM   12878 C  CA    . PHE   E 4  233 ? -12.238 42.438  -112.049 1.00 107.60 ? 233 PHE   F CA    1 
ATOM   12879 C  C     . PHE   E 4  233 ? -13.458 42.254  -111.146 1.00 104.78 ? 233 PHE   F C     1 
ATOM   12880 O  O     . PHE   E 4  233 ? -14.266 43.175  -111.002 1.00 100.34 ? 233 PHE   F O     1 
ATOM   12881 C  CB    . PHE   E 4  233 ? -11.615 43.817  -111.861 1.00 98.63  ? 233 PHE   F CB    1 
ATOM   12882 C  CG    . PHE   E 4  233 ? -12.002 44.816  -112.914 1.00 105.02 ? 233 PHE   F CG    1 
ATOM   12883 C  CD1   . PHE   E 4  233 ? -13.300 45.285  -113.003 1.00 102.53 ? 233 PHE   F CD1   1 
ATOM   12884 C  CD2   . PHE   E 4  233 ? -11.060 45.300  -113.807 1.00 106.42 ? 233 PHE   F CD2   1 
ATOM   12885 C  CE1   . PHE   E 4  233 ? -13.656 46.206  -113.972 1.00 105.11 ? 233 PHE   F CE1   1 
ATOM   12886 C  CE2   . PHE   E 4  233 ? -11.412 46.221  -114.775 1.00 107.60 ? 233 PHE   F CE2   1 
ATOM   12887 C  CZ    . PHE   E 4  233 ? -12.712 46.671  -114.859 1.00 103.34 ? 233 PHE   F CZ    1 
ATOM   12888 N  N     . GLN   E 4  234 ? -13.577 41.071  -110.548 1.00 105.33 ? 234 GLN   F N     1 
ATOM   12889 C  CA    . GLN   E 4  234 ? -14.630 40.819  -109.571 1.00 110.34 ? 234 GLN   F CA    1 
ATOM   12890 C  C     . GLN   E 4  234 ? -14.293 39.571  -108.764 1.00 115.08 ? 234 GLN   F C     1 
ATOM   12891 O  O     . GLN   E 4  234 ? -14.947 39.262  -107.760 1.00 105.76 ? 234 GLN   F O     1 
ATOM   12892 C  CB    . GLN   E 4  234 ? -15.983 40.677  -110.268 1.00 104.57 ? 234 GLN   F CB    1 
ATOM   12893 C  CG    . GLN   E 4  234 ? -17.148 41.219  -109.465 1.00 103.41 ? 234 GLN   F CG    1 
ATOM   12894 C  CD    . GLN   E 4  234 ? -18.438 41.229  -110.264 1.00 115.50 ? 234 GLN   F CD    1 
ATOM   12895 O  OE1   . GLN   E 4  234 ? -19.138 42.240  -110.315 1.00 119.44 ? 234 GLN   F OE1   1 
ATOM   12896 N  NE2   . GLN   E 4  234 ? -18.757 40.102  -110.895 1.00 105.39 ? 234 GLN   F NE2   1 
ATOM   12897 N  N     . ASP   E 4  235 ? -13.259 38.851  -109.211 1.00 117.07 ? 235 ASP   F N     1 
ATOM   12898 C  CA    . ASP   E 4  235 ? -12.773 37.683  -108.485 1.00 112.25 ? 235 ASP   F CA    1 
ATOM   12899 C  C     . ASP   E 4  235 ? -12.377 38.025  -107.055 1.00 118.49 ? 235 ASP   F C     1 
ATOM   12900 O  O     . ASP   E 4  235 ? -12.531 37.193  -106.151 1.00 116.82 ? 235 ASP   F O     1 
ATOM   12901 C  CB    . ASP   E 4  235 ? -11.581 37.084  -109.231 1.00 109.18 ? 235 ASP   F CB    1 
ATOM   12902 C  CG    . ASP   E 4  235 ? -10.923 38.087  -110.172 1.00 109.26 ? 235 ASP   F CG    1 
ATOM   12903 O  OD1   . ASP   E 4  235 ? -11.621 38.636  -111.054 1.00 108.03 ? 235 ASP   F OD1   1 
ATOM   12904 O  OD2   . ASP   E 4  235 ? -9.711  38.339  -110.022 1.00 105.05 ? 235 ASP   F OD2   1 
ATOM   12905 N  N     . LYS   E 4  236 ? -11.869 39.239  -106.829 1.00 114.84 ? 236 LYS   F N     1 
ATOM   12906 C  CA    . LYS   E 4  236 ? -11.328 39.613  -105.530 1.00 97.89  ? 236 LYS   F CA    1 
ATOM   12907 C  C     . LYS   E 4  236 ? -10.129 38.724  -105.223 1.00 101.81 ? 236 LYS   F C     1 
ATOM   12908 O  O     . LYS   E 4  236 ? -9.630  38.027  -106.114 1.00 96.86  ? 236 LYS   F O     1 
ATOM   12909 C  CB    . LYS   E 4  236 ? -12.404 39.511  -104.447 1.00 89.39  ? 236 LYS   F CB    1 
ATOM   12910 C  CG    . LYS   E 4  236 ? -13.592 40.437  -104.698 1.00 94.27  ? 236 LYS   F CG    1 
ATOM   12911 C  CD    . LYS   E 4  236 ? -14.699 40.231  -103.674 1.00 91.09  ? 236 LYS   F CD    1 
ATOM   12912 C  CE    . LYS   E 4  236 ? -15.891 41.136  -103.939 1.00 79.58  ? 236 LYS   F CE    1 
ATOM   12913 N  NZ    . LYS   E 4  236 ? -17.045 40.780  -103.067 1.00 82.87  ? 236 LYS   F NZ    1 
ATOM   12914 N  N     . THR   E 4  237 ? -9.659  38.734  -103.976 1.00 103.21 ? 237 THR   F N     1 
ATOM   12915 C  CA    . THR   E 4  237 ? -8.423  38.042  -103.625 1.00 95.48  ? 237 THR   F CA    1 
ATOM   12916 C  C     . THR   E 4  237 ? -7.235  38.681  -104.337 1.00 92.62  ? 237 THR   F C     1 
ATOM   12917 O  O     . THR   E 4  237 ? -6.328  39.204  -103.683 1.00 90.42  ? 237 THR   F O     1 
ATOM   12918 C  CB    . THR   E 4  237 ? -8.505  36.556  -103.971 1.00 85.23  ? 237 THR   F CB    1 
ATOM   12919 O  OG1   . THR   E 4  237 ? -8.683  36.411  -105.382 1.00 92.35  ? 237 THR   F OG1   1 
ATOM   12920 C  CG2   . THR   E 4  237 ? -9.674  35.912  -103.258 1.00 96.97  ? 237 THR   F CG2   1 
ATOM   12921 N  N     . CYS   E 4  238 ? -7.226  38.642  -105.674 1.00 96.42  ? 238 CYS   F N     1 
ATOM   12922 C  CA    . CYS   E 4  238 ? -6.176  39.294  -106.454 1.00 97.21  ? 238 CYS   F CA    1 
ATOM   12923 C  C     . CYS   E 4  238 ? -6.436  40.780  -106.674 1.00 90.25  ? 238 CYS   F C     1 
ATOM   12924 O  O     . CYS   E 4  238 ? -5.539  41.484  -107.156 1.00 83.55  ? 238 CYS   F O     1 
ATOM   12925 C  CB    . CYS   E 4  238 ? -6.006  38.606  -107.813 1.00 92.87  ? 238 CYS   F CB    1 
ATOM   12926 S  SG    . CYS   E 4  238 ? -6.845  39.439  -109.190 1.00 94.31  ? 238 CYS   F SG    1 
ATOM   12927 N  N     . HIS   E 4  239 ? -7.636  41.265  -106.345 1.00 93.57  ? 239 HIS   F N     1 
ATOM   12928 C  CA    . HIS   E 4  239 ? -7.949  42.689  -106.366 1.00 90.54  ? 239 HIS   F CA    1 
ATOM   12929 C  C     . HIS   E 4  239 ? -7.997  43.314  -104.980 1.00 90.20  ? 239 HIS   F C     1 
ATOM   12930 O  O     . HIS   E 4  239 ? -7.734  44.514  -104.851 1.00 87.48  ? 239 HIS   F O     1 
ATOM   12931 C  CB    . HIS   E 4  239 ? -9.292  42.940  -107.061 1.00 90.99  ? 239 HIS   F CB    1 
ATOM   12932 C  CG    . HIS   E 4  239 ? -9.198  43.002  -108.554 1.00 98.30  ? 239 HIS   F CG    1 
ATOM   12933 N  ND1   . HIS   E 4  239 ? -9.397  41.900  -109.359 1.00 102.40 ? 239 HIS   F ND1   1 
ATOM   12934 C  CD2   . HIS   E 4  239 ? -8.930  44.033  -109.389 1.00 89.08  ? 239 HIS   F CD2   1 
ATOM   12935 C  CE1   . HIS   E 4  239 ? -9.255  42.250  -110.625 1.00 96.30  ? 239 HIS   F CE1   1 
ATOM   12936 N  NE2   . HIS   E 4  239 ? -8.973  43.540  -110.670 1.00 92.69  ? 239 HIS   F NE2   1 
ATOM   12937 N  N     . LEU   E 4  240 ? -8.326  42.543  -103.943 1.00 84.84  ? 240 LEU   F N     1 
ATOM   12938 C  CA    . LEU   E 4  240 ? -8.367  43.052  -102.573 1.00 79.56  ? 240 LEU   F CA    1 
ATOM   12939 C  C     . LEU   E 4  240 ? -7.102  42.587  -101.867 1.00 78.40  ? 240 LEU   F C     1 
ATOM   12940 O  O     . LEU   E 4  240 ? -7.016  41.446  -101.409 1.00 78.94  ? 240 LEU   F O     1 
ATOM   12941 C  CB    . LEU   E 4  240 ? -9.615  42.577  -101.836 1.00 77.57  ? 240 LEU   F CB    1 
ATOM   12942 C  CG    . LEU   E 4  240 ? -10.980 42.721  -102.517 1.00 84.78  ? 240 LEU   F CG    1 
ATOM   12943 C  CD1   . LEU   E 4  240 ? -12.081 42.254  -101.566 1.00 81.79  ? 240 LEU   F CD1   1 
ATOM   12944 C  CD2   . LEU   E 4  240 ? -11.248 44.142  -103.043 1.00 65.78  ? 240 LEU   F CD2   1 
ATOM   12945 N  N     . THR   E 4  241 ? -6.115  43.474  -101.784 1.00 77.04  ? 241 THR   F N     1 
ATOM   12946 C  CA    . THR   E 4  241 ? -4.918  43.152  -101.021 1.00 78.30  ? 241 THR   F CA    1 
ATOM   12947 C  C     . THR   E 4  241 ? -5.197  43.054  -99.531  1.00 85.74  ? 241 THR   F C     1 
ATOM   12948 O  O     . THR   E 4  241 ? -4.326  42.584  -98.787  1.00 86.31  ? 241 THR   F O     1 
ATOM   12949 C  CB    . THR   E 4  241 ? -3.832  44.201  -101.262 1.00 75.07  ? 241 THR   F CB    1 
ATOM   12950 O  OG1   . THR   E 4  241 ? -3.807  45.124  -100.165 1.00 80.28  ? 241 THR   F OG1   1 
ATOM   12951 C  CG2   . THR   E 4  241 ? -4.106  44.964  -102.554 1.00 73.19  ? 241 THR   F CG2   1 
ATOM   12952 N  N     . ASN   E 4  242 ? -6.379  43.491  -99.088  1.00 87.31  ? 242 ASN   F N     1 
ATOM   12953 C  CA    . ASN   E 4  242 ? -6.693  43.534  -97.666  1.00 97.70  ? 242 ASN   F CA    1 
ATOM   12954 C  C     . ASN   E 4  242 ? -6.415  42.171  -97.035  1.00 89.62  ? 242 ASN   F C     1 
ATOM   12955 O  O     . ASN   E 4  242 ? -6.920  41.143  -97.492  1.00 83.39  ? 242 ASN   F O     1 
ATOM   12956 C  CB    . ASN   E 4  242 ? -8.153  43.976  -97.459  1.00 95.83  ? 242 ASN   F CB    1 
ATOM   12957 C  CG    . ASN   E 4  242 ? -8.365  45.498  -97.701  1.00 100.96 ? 242 ASN   F CG    1 
ATOM   12958 O  OD1   . ASN   E 4  242 ? -8.229  45.996  -98.827  1.00 100.52 ? 242 ASN   F OD1   1 
ATOM   12959 N  ND2   . ASN   E 4  242 ? -8.724  46.225  -96.640  1.00 105.34 ? 242 ASN   F ND2   1 
ATOM   12960 N  N     . HIS   E 4  243 ? -5.591  42.182  -95.986  1.00 86.12  ? 243 HIS   F N     1 
ATOM   12961 C  CA    . HIS   E 4  243 ? -4.889  41.006  -95.475  1.00 93.57  ? 243 HIS   F CA    1 
ATOM   12962 C  C     . HIS   E 4  243 ? -5.745  39.756  -95.289  1.00 96.61  ? 243 HIS   F C     1 
ATOM   12963 O  O     . HIS   E 4  243 ? -5.526  38.748  -95.969  1.00 96.98  ? 243 HIS   F O     1 
ATOM   12964 C  CB    . HIS   E 4  243 ? -4.224  41.349  -94.141  1.00 88.59  ? 243 HIS   F CB    1 
ATOM   12965 C  CG    . HIS   E 4  243 ? -3.231  40.330  -93.683  1.00 83.60  ? 243 HIS   F CG    1 
ATOM   12966 N  ND1   . HIS   E 4  243 ? -3.582  39.031  -93.379  1.00 90.29  ? 243 HIS   F ND1   1 
ATOM   12967 C  CD2   . HIS   E 4  243 ? -1.896  40.420  -93.468  1.00 82.43  ? 243 HIS   F CD2   1 
ATOM   12968 C  CE1   . HIS   E 4  243 ? -2.506  38.366  -92.997  1.00 92.70  ? 243 HIS   F CE1   1 
ATOM   12969 N  NE2   . HIS   E 4  243 ? -1.470  39.186  -93.040  1.00 84.53  ? 243 HIS   F NE2   1 
ATOM   12970 N  N     . CYS   E 4  244 ? -6.690  39.794  -94.345  1.00 92.36  ? 244 CYS   F N     1 
ATOM   12971 C  CA    . CYS   E 4  244 ? -7.419  38.585  -93.968  1.00 93.53  ? 244 CYS   F CA    1 
ATOM   12972 C  C     . CYS   E 4  244 ? -7.965  37.850  -95.189  1.00 95.88  ? 244 CYS   F C     1 
ATOM   12973 O  O     . CYS   E 4  244 ? -7.744  36.644  -95.348  1.00 100.29 ? 244 CYS   F O     1 
ATOM   12974 C  CB    . CYS   E 4  244 ? -8.548  38.940  -93.001  1.00 106.02 ? 244 CYS   F CB    1 
ATOM   12975 S  SG    . CYS   E 4  244 ? -9.857  39.925  -93.753  1.00 117.75 ? 244 CYS   F SG    1 
ATOM   12976 N  N     . ILE   E 4  245 ? -8.678  38.561  -96.068  1.00 100.39 ? 245 ILE   F N     1 
ATOM   12977 C  CA    . ILE   E 4  245 ? -9.196  37.968  -97.300  1.00 103.21 ? 245 ILE   F CA    1 
ATOM   12978 C  C     . ILE   E 4  245 ? -8.087  37.417  -98.194  1.00 97.55  ? 245 ILE   F C     1 
ATOM   12979 O  O     . ILE   E 4  245 ? -8.371  36.720  -99.174  1.00 97.66  ? 245 ILE   F O     1 
ATOM   12980 C  CB    . ILE   E 4  245 ? -10.080 38.996  -98.054  1.00 97.45  ? 245 ILE   F CB    1 
ATOM   12981 C  CG1   . ILE   E 4  245 ? -11.516 38.973  -97.508  1.00 102.95 ? 245 ILE   F CG1   1 
ATOM   12982 C  CG2   . ILE   E 4  245 ? -10.071 38.764  -99.568  1.00 87.02  ? 245 ILE   F CG2   1 
ATOM   12983 C  CD1   . ILE   E 4  245 ? -12.198 37.608  -97.565  1.00 83.86  ? 245 ILE   F CD1   1 
ATOM   12984 N  N     . GLN   E 4  246 ? -6.827  37.699  -97.874  1.00 95.47  ? 246 GLN   F N     1 
ATOM   12985 C  CA    . GLN   E 4  246 ? -5.711  37.030  -98.526  1.00 92.68  ? 246 GLN   F CA    1 
ATOM   12986 C  C     . GLN   E 4  246 ? -5.268  35.785  -97.776  1.00 96.67  ? 246 GLN   F C     1 
ATOM   12987 O  O     . GLN   E 4  246 ? -4.759  34.844  -98.397  1.00 98.33  ? 246 GLN   F O     1 
ATOM   12988 C  CB    . GLN   E 4  246 ? -4.536  37.993  -98.668  1.00 88.81  ? 246 GLN   F CB    1 
ATOM   12989 C  CG    . GLN   E 4  246 ? -4.678  38.936  -99.838  1.00 86.49  ? 246 GLN   F CG    1 
ATOM   12990 C  CD    . GLN   E 4  246 ? -4.079  38.364  -101.098 1.00 80.92  ? 246 GLN   F CD    1 
ATOM   12991 O  OE1   . GLN   E 4  246 ? -2.963  37.841  -101.084 1.00 83.01  ? 246 GLN   F OE1   1 
ATOM   12992 N  NE2   . GLN   E 4  246 ? -4.816  38.450  -102.196 1.00 78.59  ? 246 GLN   F NE2   1 
ATOM   12993 N  N     . LYS   E 4  247 ? -5.449  35.758  -96.457  1.00 98.33  ? 247 LYS   F N     1 
ATOM   12994 C  CA    . LYS   E 4  247 ? -5.185  34.560  -95.671  1.00 102.11 ? 247 LYS   F CA    1 
ATOM   12995 C  C     . LYS   E 4  247 ? -6.277  33.531  -95.936  1.00 105.96 ? 247 LYS   F C     1 
ATOM   12996 O  O     . LYS   E 4  247 ? -6.975  33.104  -95.009  1.00 106.15 ? 247 LYS   F O     1 
ATOM   12997 C  CB    . LYS   E 4  247 ? -5.112  34.902  -94.180  1.00 89.55  ? 247 LYS   F CB    1 
ATOM   12998 C  CG    . LYS   E 4  247 ? -4.487  33.818  -93.325  1.00 96.45  ? 247 LYS   F CG    1 
ATOM   12999 C  CD    . LYS   E 4  247 ? -3.987  34.403  -92.014  1.00 102.70 ? 247 LYS   F CD    1 
ATOM   13000 C  CE    . LYS   E 4  247 ? -3.039  33.458  -91.295  1.00 84.59  ? 247 LYS   F CE    1 
ATOM   13001 N  NZ    . LYS   E 4  247 ? -2.468  34.106  -90.090  1.00 71.21  ? 247 LYS   F NZ    1 
ATOM   13002 N  N     . GLU   E 4  248 ? -6.435  33.123  -97.197  1.00 96.70  ? 248 GLU   F N     1 
ATOM   13003 C  CA    . GLU   E 4  248 ? -7.615  32.354  -97.557  1.00 95.06  ? 248 GLU   F CA    1 
ATOM   13004 C  C     . GLU   E 4  248 ? -7.671  31.993  -99.040  1.00 96.24  ? 248 GLU   F C     1 
ATOM   13005 O  O     . GLU   E 4  248 ? -8.641  31.371  -99.480  1.00 103.62 ? 248 GLU   F O     1 
ATOM   13006 C  CB    . GLU   E 4  248 ? -8.859  33.147  -97.144  1.00 94.79  ? 248 GLU   F CB    1 
ATOM   13007 C  CG    . GLU   E 4  248 ? -10.183 32.588  -97.598  1.00 92.81  ? 248 GLU   F CG    1 
ATOM   13008 C  CD    . GLU   E 4  248 ? -11.306 33.567  -97.359  1.00 96.39  ? 248 GLU   F CD    1 
ATOM   13009 O  OE1   . GLU   E 4  248 ? -11.081 34.540  -96.608  1.00 95.89  ? 248 GLU   F OE1   1 
ATOM   13010 O  OE2   . GLU   E 4  248 ? -12.405 33.375  -97.922  1.00 97.92  ? 248 GLU   F OE2   1 
ATOM   13011 N  N     . TYR   E 4  249 ? -6.651  32.367  -99.831  1.00 96.41  ? 249 TYR   F N     1 
ATOM   13012 C  CA    . TYR   E 4  249 ? -6.621  31.965  -101.237 1.00 94.04  ? 249 TYR   F CA    1 
ATOM   13013 C  C     . TYR   E 4  249 ? -5.220  31.797  -101.817 1.00 89.47  ? 249 TYR   F C     1 
ATOM   13014 O  O     . TYR   E 4  249 ? -5.118  31.510  -103.012 1.00 85.09  ? 249 TYR   F O     1 
ATOM   13015 C  CB    . TYR   E 4  249 ? -7.401  32.970  -102.123 1.00 93.69  ? 249 TYR   F CB    1 
ATOM   13016 C  CG    . TYR   E 4  249 ? -8.912  33.023  -101.933 1.00 97.58  ? 249 TYR   F CG    1 
ATOM   13017 C  CD1   . TYR   E 4  249 ? -9.475  33.681  -100.839 1.00 103.43 ? 249 TYR   F CD1   1 
ATOM   13018 C  CD2   . TYR   E 4  249 ? -9.777  32.463  -102.872 1.00 94.91  ? 249 TYR   F CD2   1 
ATOM   13019 C  CE1   . TYR   E 4  249 ? -10.855 33.749  -100.659 1.00 107.54 ? 249 TYR   F CE1   1 
ATOM   13020 C  CE2   . TYR   E 4  249 ? -11.167 32.533  -102.706 1.00 106.34 ? 249 TYR   F CE2   1 
ATOM   13021 C  CZ    . TYR   E 4  249 ? -11.700 33.180  -101.593 1.00 108.11 ? 249 TYR   F CZ    1 
ATOM   13022 O  OH    . TYR   E 4  249 ? -13.069 33.262  -101.396 1.00 87.94  ? 249 TYR   F OH    1 
ATOM   13023 N  N     . SER   E 4  250 ? -4.147  31.954  -101.039 1.00 97.07  ? 250 SER   F N     1 
ATOM   13024 C  CA    . SER   E 4  250 ? -2.773  31.972  -101.572 1.00 93.83  ? 250 SER   F CA    1 
ATOM   13025 C  C     . SER   E 4  250 ? -2.465  30.791  -102.493 1.00 87.03  ? 250 SER   F C     1 
ATOM   13026 O  O     . SER   E 4  250 ? -1.407  30.751  -103.127 1.00 84.56  ? 250 SER   F O     1 
ATOM   13027 C  CB    . SER   E 4  250 ? -1.749  32.004  -100.427 1.00 84.64  ? 250 SER   F CB    1 
ATOM   13028 O  OG    . SER   E 4  250 ? -0.421  32.137  -100.918 1.00 76.87  ? 250 SER   F OG    1 
ATOM   13029 N  N     . ARG   E 4  255 ? 3.115   32.585  -100.796 1.00 78.02  ? 255 ARG   F N     1 
ATOM   13030 C  CA    . ARG   E 4  255 ? 3.990   31.871  -101.728 1.00 82.65  ? 255 ARG   F CA    1 
ATOM   13031 C  C     . ARG   E 4  255 ? 5.301   32.606  -101.955 1.00 85.16  ? 255 ARG   F C     1 
ATOM   13032 O  O     . ARG   E 4  255 ? 6.345   31.984  -102.161 1.00 85.14  ? 255 ARG   F O     1 
ATOM   13033 C  CB    . ARG   E 4  255 ? 3.296   31.651  -103.074 1.00 85.40  ? 255 ARG   F CB    1 
ATOM   13034 C  CG    . ARG   E 4  255 ? 4.254   31.301  -104.217 1.00 79.60  ? 255 ARG   F CG    1 
ATOM   13035 C  CD    . ARG   E 4  255 ? 3.491   31.009  -105.513 1.00 84.06  ? 255 ARG   F CD    1 
ATOM   13036 N  NE    . ARG   E 4  255 ? 4.374   30.848  -106.665 1.00 89.69  ? 255 ARG   F NE    1 
ATOM   13037 C  CZ    . ARG   E 4  255 ? 3.961   30.604  -107.904 1.00 80.60  ? 255 ARG   F CZ    1 
ATOM   13038 N  NH1   . ARG   E 4  255 ? 2.678   30.467  -108.192 1.00 66.12  ? 255 ARG   F NH1   1 
ATOM   13039 N  NH2   . ARG   E 4  255 ? 4.861   30.500  -108.879 1.00 79.82  ? 255 ARG   F NH2   1 
ATOM   13040 N  N     . TYR   E 4  256 ? 5.235   33.938  -101.925 1.00 87.24  ? 256 TYR   F N     1 
ATOM   13041 C  CA    . TYR   E 4  256 ? 6.406   34.784  -102.122 1.00 82.12  ? 256 TYR   F CA    1 
ATOM   13042 C  C     . TYR   E 4  256 ? 6.888   35.474  -100.852 1.00 83.31  ? 256 TYR   F C     1 
ATOM   13043 O  O     . TYR   E 4  256 ? 8.097   35.670  -100.690 1.00 83.93  ? 256 TYR   F O     1 
ATOM   13044 C  CB    . TYR   E 4  256 ? 6.117   35.859  -103.175 1.00 68.48  ? 256 TYR   F CB    1 
ATOM   13045 C  CG    . TYR   E 4  256 ? 5.379   35.393  -104.412 1.00 74.55  ? 256 TYR   F CG    1 
ATOM   13046 C  CD1   . TYR   E 4  256 ? 6.068   34.902  -105.516 1.00 80.36  ? 256 TYR   F CD1   1 
ATOM   13047 C  CD2   . TYR   E 4  256 ? 3.997   35.486  -104.497 1.00 76.79  ? 256 TYR   F CD2   1 
ATOM   13048 C  CE1   . TYR   E 4  256 ? 5.398   34.503  -106.664 1.00 76.83  ? 256 TYR   F CE1   1 
ATOM   13049 C  CE2   . TYR   E 4  256 ? 3.320   35.089  -105.638 1.00 77.22  ? 256 TYR   F CE2   1 
ATOM   13050 C  CZ    . TYR   E 4  256 ? 4.025   34.601  -106.721 1.00 78.27  ? 256 TYR   F CZ    1 
ATOM   13051 O  OH    . TYR   E 4  256 ? 3.357   34.204  -107.860 1.00 79.28  ? 256 TYR   F OH    1 
ATOM   13052 N  N     . GLU   E 4  257 ? 5.976   35.857  -99.955  1.00 69.29  ? 257 GLU   F N     1 
ATOM   13053 C  CA    . GLU   E 4  257 ? 6.324   36.520  -98.706  1.00 80.41  ? 257 GLU   F CA    1 
ATOM   13054 C  C     . GLU   E 4  257 ? 5.604   35.837  -97.555  1.00 78.19  ? 257 GLU   F C     1 
ATOM   13055 O  O     . GLU   E 4  257 ? 4.412   35.535  -97.659  1.00 75.13  ? 257 GLU   F O     1 
ATOM   13056 C  CB    . GLU   E 4  257 ? 5.949   38.021  -98.724  1.00 72.72  ? 257 GLU   F CB    1 
ATOM   13057 C  CG    . GLU   E 4  257 ? 6.798   38.871  -99.633  1.00 67.05  ? 257 GLU   F CG    1 
ATOM   13058 C  CD    . GLU   E 4  257 ? 6.375   38.761  -101.084 1.00 81.27  ? 257 GLU   F CD    1 
ATOM   13059 O  OE1   . GLU   E 4  257 ? 5.145   38.795  -101.332 1.00 77.33  ? 257 GLU   F OE1   1 
ATOM   13060 O  OE2   . GLU   E 4  257 ? 7.268   38.639  -101.966 1.00 74.32  ? 257 GLU   F OE2   1 
ATOM   13061 N  N     . GLU   E 4  258 ? 6.332   35.611  -96.455  1.00 73.22  ? 258 GLU   F N     1 
ATOM   13062 C  CA    . GLU   E 4  258 ? 5.747   35.097  -95.219  1.00 74.93  ? 258 GLU   F CA    1 
ATOM   13063 C  C     . GLU   E 4  258 ? 4.458   35.836  -94.865  1.00 74.72  ? 258 GLU   F C     1 
ATOM   13064 O  O     . GLU   E 4  258 ? 4.501   36.977  -94.395  1.00 75.78  ? 258 GLU   F O     1 
ATOM   13065 C  CB    . GLU   E 4  258 ? 6.755   35.204  -94.067  1.00 65.07  ? 258 GLU   F CB    1 
ATOM   13066 C  CG    . GLU   E 4  258 ? 6.222   34.682  -92.727  1.00 72.12  ? 258 GLU   F CG    1 
ATOM   13067 C  CD    . GLU   E 4  258 ? 7.309   34.509  -91.670  1.00 78.11  ? 258 GLU   F CD    1 
ATOM   13068 O  OE1   . GLU   E 4  258 ? 8.421   35.048  -91.858  1.00 89.68  ? 258 GLU   F OE1   1 
ATOM   13069 O  OE2   . GLU   E 4  258 ? 7.055   33.826  -90.651  1.00 62.66  ? 258 GLU   F OE2   1 
ATOM   13070 N  N     . GLY   E 4  259 ? 3.308   35.197  -95.086  1.00 72.03  ? 259 GLY   F N     1 
ATOM   13071 C  CA    . GLY   E 4  259 ? 2.025   35.816  -94.809  1.00 60.45  ? 259 GLY   F CA    1 
ATOM   13072 C  C     . GLY   E 4  259 ? 1.666   36.969  -95.719  1.00 71.94  ? 259 GLY   F C     1 
ATOM   13073 O  O     . GLY   E 4  259 ? 0.880   37.838  -95.330  1.00 73.27  ? 259 GLY   F O     1 
ATOM   13074 N  N     . ASN   E 4  260 ? 2.220   37.005  -96.929  1.00 73.94  ? 260 ASN   F N     1 
ATOM   13075 C  CA    . ASN   E 4  260 ? 2.004   38.116  -97.855  1.00 72.35  ? 260 ASN   F CA    1 
ATOM   13076 C  C     . ASN   E 4  260 ? 2.447   39.445  -97.248  1.00 70.66  ? 260 ASN   F C     1 
ATOM   13077 O  O     . ASN   E 4  260 ? 1.760   40.461  -97.367  1.00 70.26  ? 260 ASN   F O     1 
ATOM   13078 C  CB    . ASN   E 4  260 ? 0.545   38.185  -98.304  1.00 65.25  ? 260 ASN   F CB    1 
ATOM   13079 C  CG    . ASN   E 4  260 ? 0.191   37.086  -99.281  1.00 75.66  ? 260 ASN   F CG    1 
ATOM   13080 O  OD1   . ASN   E 4  260 ? 0.807   36.016  -99.272  1.00 76.66  ? 260 ASN   F OD1   1 
ATOM   13081 N  ND2   . ASN   E 4  260 ? -0.795  37.344  -100.141 1.00 69.24  ? 260 ASN   F ND2   1 
ATOM   13082 N  N     . GLU   E 4  261 ? 3.621   39.442  -96.609  1.00 71.32  ? 261 GLU   F N     1 
ATOM   13083 C  CA    . GLU   E 4  261 ? 4.157   40.617  -95.923  1.00 68.63  ? 261 GLU   F CA    1 
ATOM   13084 C  C     . GLU   E 4  261 ? 5.554   40.932  -96.438  1.00 65.43  ? 261 GLU   F C     1 
ATOM   13085 O  O     . GLU   E 4  261 ? 6.516   40.225  -96.112  1.00 73.22  ? 261 GLU   F O     1 
ATOM   13086 C  CB    . GLU   E 4  261 ? 4.187   40.411  -94.406  1.00 66.83  ? 261 GLU   F CB    1 
ATOM   13087 C  CG    . GLU   E 4  261 ? 2.835   40.578  -93.738  1.00 62.43  ? 261 GLU   F CG    1 
ATOM   13088 C  CD    . GLU   E 4  261 ? 2.936   40.639  -92.234  1.00 61.69  ? 261 GLU   F CD    1 
ATOM   13089 O  OE1   . GLU   E 4  261 ? 3.999   40.275  -91.682  1.00 72.71  ? 261 GLU   F OE1   1 
ATOM   13090 O  OE2   . GLU   E 4  261 ? 1.948   41.060  -91.605  1.00 60.69  ? 261 GLU   F OE2   1 
ATOM   13091 N  N     . MET   E 4  262 ? 5.672   42.007  -97.210  1.00 61.71  ? 262 MET   F N     1 
ATOM   13092 C  CA    . MET   E 4  262 ? 6.963   42.534  -97.624  1.00 65.12  ? 262 MET   F CA    1 
ATOM   13093 C  C     . MET   E 4  262 ? 7.277   43.808  -96.844  1.00 68.40  ? 262 MET   F C     1 
ATOM   13094 O  O     . MET   E 4  262 ? 6.478   44.755  -96.833  1.00 60.28  ? 262 MET   F O     1 
ATOM   13095 C  CB    . MET   E 4  262 ? 6.998   42.816  -99.126  1.00 64.95  ? 262 MET   F CB    1 
ATOM   13096 C  CG    . MET   E 4  262 ? 8.411   43.080  -99.610  1.00 64.79  ? 262 MET   F CG    1 
ATOM   13097 S  SD    . MET   E 4  262 ? 8.523   43.664  -101.300 1.00 60.74  ? 262 MET   F SD    1 
ATOM   13098 C  CE    . MET   E 4  262 ? 7.756   42.325  -102.217 1.00 46.53  ? 262 MET   F CE    1 
ATOM   13099 N  N     . PHE   E 4  263 ? 8.445   43.825  -96.203  1.00 69.74  ? 263 PHE   F N     1 
ATOM   13100 C  CA    . PHE   E 4  263 ? 8.908   44.972  -95.442  1.00 72.07  ? 263 PHE   F CA    1 
ATOM   13101 C  C     . PHE   E 4  263 ? 9.752   45.889  -96.329  1.00 66.54  ? 263 PHE   F C     1 
ATOM   13102 O  O     . PHE   E 4  263 ? 9.918   45.656  -97.530  1.00 63.31  ? 263 PHE   F O     1 
ATOM   13103 C  CB    . PHE   E 4  263 ? 9.654   44.501  -94.193  1.00 61.62  ? 263 PHE   F CB    1 
ATOM   13104 C  CG    . PHE   E 4  263 ? 8.799   43.682  -93.281  1.00 61.30  ? 263 PHE   F CG    1 
ATOM   13105 C  CD1   . PHE   E 4  263 ? 7.646   44.226  -92.727  1.00 66.78  ? 263 PHE   F CD1   1 
ATOM   13106 C  CD2   . PHE   E 4  263 ? 9.111   42.367  -93.005  1.00 63.91  ? 263 PHE   F CD2   1 
ATOM   13107 C  CE1   . PHE   E 4  263 ? 6.818   43.475  -91.899  1.00 59.91  ? 263 PHE   F CE1   1 
ATOM   13108 C  CE2   . PHE   E 4  263 ? 8.297   41.617  -92.177  1.00 72.12  ? 263 PHE   F CE2   1 
ATOM   13109 C  CZ    . PHE   E 4  263 ? 7.142   42.176  -91.623  1.00 62.39  ? 263 PHE   F CZ    1 
ATOM   13110 N  N     . PHE   E 4  264 ? 10.296  46.951  -95.729  1.00 66.37  ? 264 PHE   F N     1 
ATOM   13111 C  CA    . PHE   E 4  264 ? 10.770  48.076  -96.525  1.00 52.75  ? 264 PHE   F CA    1 
ATOM   13112 C  C     . PHE   E 4  264 ? 12.180  47.882  -97.055  1.00 56.55  ? 264 PHE   F C     1 
ATOM   13113 O  O     . PHE   E 4  264 ? 12.519  48.467  -98.085  1.00 60.52  ? 264 PHE   F O     1 
ATOM   13114 C  CB    . PHE   E 4  264 ? 10.690  49.367  -95.712  1.00 54.37  ? 264 PHE   F CB    1 
ATOM   13115 C  CG    . PHE   E 4  264 ? 9.392   50.108  -95.881  1.00 55.49  ? 264 PHE   F CG    1 
ATOM   13116 C  CD1   . PHE   E 4  264 ? 8.300   49.495  -96.490  1.00 51.64  ? 264 PHE   F CD1   1 
ATOM   13117 C  CD2   . PHE   E 4  264 ? 9.268   51.426  -95.463  1.00 47.02  ? 264 PHE   F CD2   1 
ATOM   13118 C  CE1   . PHE   E 4  264 ? 7.110   50.174  -96.664  1.00 46.86  ? 264 PHE   F CE1   1 
ATOM   13119 C  CE2   . PHE   E 4  264 ? 8.080   52.106  -95.630  1.00 47.53  ? 264 PHE   F CE2   1 
ATOM   13120 C  CZ    . PHE   E 4  264 ? 6.998   51.482  -96.226  1.00 46.35  ? 264 PHE   F CZ    1 
ATOM   13121 N  N     . GLU   E 4  265 ? 13.017  47.091  -96.377  1.00 61.49  ? 265 GLU   F N     1 
ATOM   13122 C  CA    . GLU   E 4  265 ? 14.368  46.836  -96.884  1.00 57.58  ? 265 GLU   F CA    1 
ATOM   13123 C  C     . GLU   E 4  265 ? 14.334  45.995  -98.155  1.00 66.74  ? 265 GLU   F C     1 
ATOM   13124 O  O     . GLU   E 4  265 ? 15.128  46.218  -99.078  1.00 62.33  ? 265 GLU   F O     1 
ATOM   13125 C  CB    . GLU   E 4  265 ? 15.211  46.151  -95.809  1.00 65.20  ? 265 GLU   F CB    1 
ATOM   13126 C  CG    . GLU   E 4  265 ? 16.156  45.081  -96.314  1.00 66.33  ? 265 GLU   F CG    1 
ATOM   13127 C  CD    . GLU   E 4  265 ? 16.912  44.403  -95.177  1.00 73.76  ? 265 GLU   F CD    1 
ATOM   13128 O  OE1   . GLU   E 4  265 ? 17.706  45.087  -94.497  1.00 75.57  ? 265 GLU   F OE1   1 
ATOM   13129 O  OE2   . GLU   E 4  265 ? 16.699  43.191  -94.952  1.00 72.44  ? 265 GLU   F OE2   1 
ATOM   13130 N  N     . GLU   E 4  266 ? 13.416  45.028  -98.220  1.00 66.71  ? 266 GLU   F N     1 
ATOM   13131 C  CA    . GLU   E 4  266 ? 13.248  44.238  -99.432  1.00 58.15  ? 266 GLU   F CA    1 
ATOM   13132 C  C     . GLU   E 4  266 ? 12.596  45.060  -100.538 1.00 67.56  ? 266 GLU   F C     1 
ATOM   13133 O  O     . GLU   E 4  266 ? 13.080  45.080  -101.679 1.00 64.76  ? 266 GLU   F O     1 
ATOM   13134 C  CB    . GLU   E 4  266 ? 12.424  42.988  -99.123  1.00 60.66  ? 266 GLU   F CB    1 
ATOM   13135 C  CG    . GLU   E 4  266 ? 12.174  42.094  -100.332 1.00 64.32  ? 266 GLU   F CG    1 
ATOM   13136 C  CD    . GLU   E 4  266 ? 11.504  40.778  -99.968  1.00 70.37  ? 266 GLU   F CD    1 
ATOM   13137 O  OE1   . GLU   E 4  266 ? 10.252  40.704  -99.972  1.00 63.33  ? 266 GLU   F OE1   1 
ATOM   13138 O  OE2   . GLU   E 4  266 ? 12.239  39.814  -99.675  1.00 75.43  ? 266 GLU   F OE2   1 
ATOM   13139 N  N     . PHE   E 4  267 ? 11.492  45.749  -100.219 1.00 64.94  ? 267 PHE   F N     1 
ATOM   13140 C  CA    . PHE   E 4  267 ? 10.770  46.500  -101.241 1.00 57.42  ? 267 PHE   F CA    1 
ATOM   13141 C  C     . PHE   E 4  267 ? 11.613  47.625  -101.812 1.00 58.59  ? 267 PHE   F C     1 
ATOM   13142 O  O     . PHE   E 4  267 ? 11.406  48.036  -102.958 1.00 61.20  ? 267 PHE   F O     1 
ATOM   13143 C  CB    . PHE   E 4  267 ? 9.479   47.070  -100.673 1.00 54.52  ? 267 PHE   F CB    1 
ATOM   13144 C  CG    . PHE   E 4  267 ? 8.694   47.856  -101.669 1.00 57.14  ? 267 PHE   F CG    1 
ATOM   13145 C  CD1   . PHE   E 4  267 ? 8.401   47.320  -102.910 1.00 54.57  ? 267 PHE   F CD1   1 
ATOM   13146 C  CD2   . PHE   E 4  267 ? 8.246   49.126  -101.373 1.00 54.59  ? 267 PHE   F CD2   1 
ATOM   13147 C  CE1   . PHE   E 4  267 ? 7.667   48.028  -103.838 1.00 46.77  ? 267 PHE   F CE1   1 
ATOM   13148 C  CE2   . PHE   E 4  267 ? 7.515   49.837  -102.293 1.00 52.99  ? 267 PHE   F CE2   1 
ATOM   13149 C  CZ    . PHE   E 4  267 ? 7.222   49.282  -103.526 1.00 57.68  ? 267 PHE   F CZ    1 
ATOM   13150 N  N     . ASN   E 4  268 ? 12.540  48.158  -101.014 1.00 58.98  ? 268 ASN   F N     1 
ATOM   13151 C  CA    . ASN   E 4  268 ? 13.490  49.147  -101.511 1.00 59.62  ? 268 ASN   F CA    1 
ATOM   13152 C  C     . ASN   E 4  268 ? 14.499  48.489  -102.444 1.00 65.61  ? 268 ASN   F C     1 
ATOM   13153 O  O     . ASN   E 4  268 ? 14.780  49.002  -103.537 1.00 59.73  ? 268 ASN   F O     1 
ATOM   13154 C  CB    . ASN   E 4  268 ? 14.178  49.827  -100.320 1.00 56.56  ? 268 ASN   F CB    1 
ATOM   13155 C  CG    . ASN   E 4  268 ? 15.283  50.777  -100.726 1.00 52.01  ? 268 ASN   F CG    1 
ATOM   13156 O  OD1   . ASN   E 4  268 ? 15.036  51.876  -101.230 1.00 57.13  ? 268 ASN   F OD1   1 
ATOM   13157 N  ND2   . ASN   E 4  268 ? 16.514  50.374  -100.469 1.00 54.75  ? 268 ASN   F ND2   1 
ATOM   13158 N  N     . GLN   E 4  269 ? 15.016  47.326  -102.041 1.00 63.81  ? 269 GLN   F N     1 
ATOM   13159 C  CA    . GLN   E 4  269 ? 15.932  46.571  -102.888 1.00 63.28  ? 269 GLN   F CA    1 
ATOM   13160 C  C     . GLN   E 4  269 ? 15.285  46.209  -104.229 1.00 63.62  ? 269 GLN   F C     1 
ATOM   13161 O  O     . GLN   E 4  269 ? 15.894  46.387  -105.290 1.00 57.73  ? 269 GLN   F O     1 
ATOM   13162 C  CB    . GLN   E 4  269 ? 16.407  45.325  -102.137 1.00 62.63  ? 269 GLN   F CB    1 
ATOM   13163 C  CG    . GLN   E 4  269 ? 17.472  44.526  -102.837 1.00 49.81  ? 269 GLN   F CG    1 
ATOM   13164 C  CD    . GLN   E 4  269 ? 18.641  45.373  -103.258 1.00 61.38  ? 269 GLN   F CD    1 
ATOM   13165 O  OE1   . GLN   E 4  269 ? 18.652  45.932  -104.357 1.00 59.92  ? 269 GLN   F OE1   1 
ATOM   13166 N  NE2   . GLN   E 4  269 ? 19.642  45.469  -102.391 1.00 54.47  ? 269 GLN   F NE2   1 
ATOM   13167 N  N     . TYR   E 4  270 ? 14.047  45.700  -104.206 1.00 63.62  ? 270 TYR   F N     1 
ATOM   13168 C  CA    . TYR   E 4  270 ? 13.351  45.436  -105.463 1.00 54.46  ? 270 TYR   F CA    1 
ATOM   13169 C  C     . TYR   E 4  270 ? 13.233  46.703  -106.286 1.00 59.50  ? 270 TYR   F C     1 
ATOM   13170 O  O     . TYR   E 4  270 ? 13.480  46.698  -107.497 1.00 59.83  ? 270 TYR   F O     1 
ATOM   13171 C  CB    . TYR   E 4  270 ? 11.963  44.863  -105.210 1.00 55.54  ? 270 TYR   F CB    1 
ATOM   13172 C  CG    . TYR   E 4  270 ? 11.041  44.925  -106.416 1.00 55.37  ? 270 TYR   F CG    1 
ATOM   13173 C  CD1   . TYR   E 4  270 ? 11.029  43.905  -107.357 1.00 52.72  ? 270 TYR   F CD1   1 
ATOM   13174 C  CD2   . TYR   E 4  270 ? 10.162  45.986  -106.600 1.00 58.56  ? 270 TYR   F CD2   1 
ATOM   13175 C  CE1   . TYR   E 4  270 ? 10.178  43.943  -108.460 1.00 54.08  ? 270 TYR   F CE1   1 
ATOM   13176 C  CE2   . TYR   E 4  270 ? 9.302   46.031  -107.707 1.00 51.63  ? 270 TYR   F CE2   1 
ATOM   13177 C  CZ    . TYR   E 4  270 ? 9.323   45.005  -108.630 1.00 56.41  ? 270 TYR   F CZ    1 
ATOM   13178 O  OH    . TYR   E 4  270 ? 8.482   45.023  -109.720 1.00 53.77  ? 270 TYR   F OH    1 
ATOM   13179 N  N     . LEU   E 4  271 ? 12.835  47.803  -105.644 1.00 66.39  ? 271 LEU   F N     1 
ATOM   13180 C  CA    . LEU   E 4  271 ? 12.678  49.057  -106.370 1.00 59.93  ? 271 LEU   F CA    1 
ATOM   13181 C  C     . LEU   E 4  271 ? 13.988  49.474  -107.020 1.00 56.87  ? 271 LEU   F C     1 
ATOM   13182 O  O     . LEU   E 4  271 ? 14.002  49.922  -108.174 1.00 54.04  ? 271 LEU   F O     1 
ATOM   13183 C  CB    . LEU   E 4  271 ? 12.166  50.139  -105.428 1.00 49.30  ? 271 LEU   F CB    1 
ATOM   13184 C  CG    . LEU   E 4  271 ? 10.662  50.110  -105.230 1.00 54.16  ? 271 LEU   F CG    1 
ATOM   13185 C  CD1   . LEU   E 4  271 ? 10.301  51.010  -104.059 1.00 56.05  ? 271 LEU   F CD1   1 
ATOM   13186 C  CD2   . LEU   E 4  271 ? 9.917   50.526  -106.520 1.00 44.38  ? 271 LEU   F CD2   1 
ATOM   13187 N  N     . MET   E 4  272 ? 15.097  49.328  -106.300 1.00 47.15  ? 272 MET   F N     1 
ATOM   13188 C  CA    . MET   E 4  272 ? 16.390  49.618  -106.890 1.00 54.94  ? 272 MET   F CA    1 
ATOM   13189 C  C     . MET   E 4  272 ? 16.583  48.749  -108.119 1.00 60.86  ? 272 MET   F C     1 
ATOM   13190 O  O     . MET   E 4  272 ? 16.456  49.231  -109.249 1.00 62.17  ? 272 MET   F O     1 
ATOM   13191 C  CB    . MET   E 4  272 ? 17.515  49.377  -105.889 1.00 54.31  ? 272 MET   F CB    1 
ATOM   13192 C  CG    . MET   E 4  272 ? 17.713  50.491  -104.892 1.00 55.42  ? 272 MET   F CG    1 
ATOM   13193 S  SD    . MET   E 4  272 ? 18.834  49.954  -103.595 1.00 73.20  ? 272 MET   F SD    1 
ATOM   13194 C  CE    . MET   E 4  272 ? 20.273  49.454  -104.555 1.00 75.08  ? 272 MET   F CE    1 
ATOM   13195 N  N     . ASP   E 4  273 ? 16.857  47.460  -107.889 1.00 60.80  ? 273 ASP   F N     1 
ATOM   13196 C  CA    . ASP   E 4  273 ? 17.162  46.526  -108.968 1.00 54.60  ? 273 ASP   F CA    1 
ATOM   13197 C  C     . ASP   E 4  273 ? 16.084  46.531  -110.042 1.00 54.85  ? 273 ASP   F C     1 
ATOM   13198 O  O     . ASP   E 4  273 ? 16.382  46.431  -111.238 1.00 53.66  ? 273 ASP   F O     1 
ATOM   13199 C  CB    . ASP   E 4  273 ? 17.329  45.114  -108.403 1.00 61.50  ? 273 ASP   F CB    1 
ATOM   13200 C  CG    . ASP   E 4  273 ? 18.419  45.025  -107.345 1.00 65.91  ? 273 ASP   F CG    1 
ATOM   13201 O  OD1   . ASP   E 4  273 ? 19.432  45.752  -107.471 1.00 69.03  ? 273 ASP   F OD1   1 
ATOM   13202 O  OD2   . ASP   E 4  273 ? 18.259  44.222  -106.394 1.00 58.93  ? 273 ASP   F OD2   1 
ATOM   13203 N  N     . ALA   E 4  274 ? 14.828  46.651  -109.646 1.00 54.04  ? 274 ALA   F N     1 
ATOM   13204 C  CA    . ALA   E 4  274 ? 13.784  46.540  -110.653 1.00 52.77  ? 274 ALA   F CA    1 
ATOM   13205 C  C     . ALA   E 4  274 ? 13.503  47.854  -111.360 1.00 51.06  ? 274 ALA   F C     1 
ATOM   13206 O  O     . ALA   E 4  274 ? 13.324  47.860  -112.579 1.00 52.57  ? 274 ALA   F O     1 
ATOM   13207 C  CB    . ALA   E 4  274 ? 12.492  46.008  -110.027 1.00 65.62  ? 274 ALA   F CB    1 
ATOM   13208 N  N     . LEU   E 4  275 ? 13.460  48.973  -110.628 1.00 58.08  ? 275 LEU   F N     1 
ATOM   13209 C  CA    A LEU   E 4  275 ? 13.053  50.251  -111.200 1.00 56.31  ? 275 LEU   F CA    1 
ATOM   13210 C  CA    B LEU   E 4  275 ? 13.051  50.255  -111.192 0.00 56.25  ? 275 LEU   F CA    1 
ATOM   13211 C  C     . LEU   E 4  275 ? 14.146  51.315  -111.191 1.00 56.50  ? 275 LEU   F C     1 
ATOM   13212 O  O     . LEU   E 4  275 ? 13.926  52.413  -111.726 1.00 47.67  ? 275 LEU   F O     1 
ATOM   13213 C  CB    A LEU   E 4  275 ? 11.814  50.778  -110.467 1.00 55.17  ? 275 LEU   F CB    1 
ATOM   13214 C  CB    B LEU   E 4  275 ? 11.827  50.799  -110.441 0.00 55.13  ? 275 LEU   F CB    1 
ATOM   13215 C  CG    A LEU   E 4  275 ? 10.508  50.443  -111.179 1.00 52.94  ? 275 LEU   F CG    1 
ATOM   13216 C  CG    B LEU   E 4  275 ? 10.501  50.073  -110.675 0.00 53.48  ? 275 LEU   F CG    1 
ATOM   13217 C  CD1   A LEU   E 4  275 ? 10.649  49.106  -111.884 1.00 49.80  ? 275 LEU   F CD1   1 
ATOM   13218 C  CD1   B LEU   E 4  275 ? 9.396   50.694  -109.834 0.00 52.98  ? 275 LEU   F CD1   1 
ATOM   13219 C  CD2   A LEU   E 4  275 ? 9.347   50.435  -110.192 1.00 51.78  ? 275 LEU   F CD2   1 
ATOM   13220 C  CD2   B LEU   E 4  275 ? 10.133  50.098  -112.150 0.00 53.18  ? 275 LEU   F CD2   1 
ATOM   13221 N  N     . ASN   E 4  276 ? 15.315  51.032  -110.611 1.00 56.83  ? 276 ASN   F N     1 
ATOM   13222 C  CA    . ASN   E 4  276 ? 16.424  51.986  -110.641 1.00 59.78  ? 276 ASN   F CA    1 
ATOM   13223 C  C     . ASN   E 4  276 ? 16.076  53.248  -109.843 1.00 62.62  ? 276 ASN   F C     1 
ATOM   13224 O  O     . ASN   E 4  276 ? 16.200  54.374  -110.326 1.00 57.13  ? 276 ASN   F O     1 
ATOM   13225 C  CB    . ASN   E 4  276 ? 16.792  52.326  -112.087 1.00 57.08  ? 276 ASN   F CB    1 
ATOM   13226 C  CG    . ASN   E 4  276 ? 18.069  53.123  -112.199 1.00 59.53  ? 276 ASN   F CG    1 
ATOM   13227 O  OD1   . ASN   E 4  276 ? 18.987  52.982  -111.382 1.00 45.70  ? 276 ASN   F OD1   1 
ATOM   13228 N  ND2   . ASN   E 4  276 ? 18.139  53.970  -113.228 1.00 60.22  ? 276 ASN   F ND2   1 
ATOM   13229 N  N     . THR   E 4  277 ? 15.618  53.045  -108.613 1.00 62.07  ? 277 THR   F N     1 
ATOM   13230 C  CA    A THR   E 4  277 ? 15.257  54.152  -107.739 1.00 61.47  ? 277 THR   F CA    1 
ATOM   13231 C  CA    B THR   E 4  277 ? 15.260  54.154  -107.740 0.00 61.20  ? 277 THR   F CA    1 
ATOM   13232 C  C     . THR   E 4  277 ? 15.292  53.648  -106.300 1.00 62.34  ? 277 THR   F C     1 
ATOM   13233 O  O     . THR   E 4  277 ? 15.927  52.627  -106.006 1.00 59.28  ? 277 THR   F O     1 
ATOM   13234 C  CB    A THR   E 4  277 ? 13.887  54.728  -108.119 1.00 55.55  ? 277 THR   F CB    1 
ATOM   13235 C  CB    B THR   E 4  277 ? 13.891  54.733  -108.135 0.00 55.85  ? 277 THR   F CB    1 
ATOM   13236 O  OG1   A THR   E 4  277 ? 13.560  55.772  -107.203 1.00 57.61  ? 277 THR   F OG1   1 
ATOM   13237 O  OG1   B THR   E 4  277 ? 13.567  55.832  -107.274 0.00 57.59  ? 277 THR   F OG1   1 
ATOM   13238 C  CG2   A THR   E 4  277 ? 12.829  53.656  -108.033 1.00 58.31  ? 277 THR   F CG2   1 
ATOM   13239 C  CG2   B THR   E 4  277 ? 12.810  53.669  -108.018 0.00 58.20  ? 277 THR   F CG2   1 
ATOM   13240 N  N     . THR   E 4  278 ? 14.618  54.366  -105.403 1.00 61.27  ? 278 THR   F N     1 
ATOM   13241 C  CA    . THR   E 4  278 ? 14.537  53.950  -104.011 1.00 61.36  ? 278 THR   F CA    1 
ATOM   13242 C  C     . THR   E 4  278 ? 13.117  54.122  -103.515 1.00 54.20  ? 278 THR   F C     1 
ATOM   13243 O  O     . THR   E 4  278 ? 12.316  54.867  -104.088 1.00 49.80  ? 278 THR   F O     1 
ATOM   13244 C  CB    . THR   E 4  278 ? 15.470  54.741  -103.083 1.00 56.40  ? 278 THR   F CB    1 
ATOM   13245 O  OG1   . THR   E 4  278 ? 15.341  56.144  -103.357 1.00 60.85  ? 278 THR   F OG1   1 
ATOM   13246 C  CG2   . THR   E 4  278 ? 16.920  54.282  -103.223 1.00 46.56  ? 278 THR   F CG2   1 
ATOM   13247 N  N     . LEU   E 4  279 ? 12.827  53.408  -102.426 1.00 48.17  ? 279 LEU   F N     1 
ATOM   13248 C  CA    . LEU   E 4  279 ? 11.599  53.643  -101.680 1.00 55.56  ? 279 LEU   F CA    1 
ATOM   13249 C  C     . LEU   E 4  279 ? 11.469  55.118  -101.309 1.00 55.86  ? 279 LEU   F C     1 
ATOM   13250 O  O     . LEU   E 4  279 ? 10.457  55.765  -101.611 1.00 51.83  ? 279 LEU   F O     1 
ATOM   13251 C  CB    . LEU   E 4  279 ? 11.590  52.750  -100.436 1.00 47.14  ? 279 LEU   F CB    1 
ATOM   13252 C  CG    . LEU   E 4  279 ? 10.345  52.699  -99.561  1.00 46.63  ? 279 LEU   F CG    1 
ATOM   13253 C  CD1   . LEU   E 4  279 ? 9.095   52.715  -100.418 1.00 48.28  ? 279 LEU   F CD1   1 
ATOM   13254 C  CD2   . LEU   E 4  279 ? 10.399  51.450  -98.711  1.00 46.22  ? 279 LEU   F CD2   1 
ATOM   13255 N  N     . GLU   E 4  280 ? 12.514  55.672  -100.688 1.00 50.22  ? 280 GLU   F N     1 
ATOM   13256 C  CA    . GLU   E 4  280 ? 12.510  57.066  -100.260 1.00 55.16  ? 280 GLU   F CA    1 
ATOM   13257 C  C     . GLU   E 4  280 ? 12.054  58.015  -101.368 1.00 59.82  ? 280 GLU   F C     1 
ATOM   13258 O  O     . GLU   E 4  280 ? 11.064  58.745  -101.218 1.00 57.22  ? 280 GLU   F O     1 
ATOM   13259 C  CB    . GLU   E 4  280 ? 13.902  57.457  -99.778  1.00 58.01  ? 280 GLU   F CB    1 
ATOM   13260 C  CG    . GLU   E 4  280 ? 13.893  58.747  -99.005  1.00 64.49  ? 280 GLU   F CG    1 
ATOM   13261 C  CD    . GLU   E 4  280 ? 12.992  58.663  -97.794  1.00 64.07  ? 280 GLU   F CD    1 
ATOM   13262 O  OE1   . GLU   E 4  280 ? 13.096  57.660  -97.047  1.00 55.29  ? 280 GLU   F OE1   1 
ATOM   13263 O  OE2   . GLU   E 4  280 ? 12.175  59.594  -97.607  1.00 62.98  ? 280 GLU   F OE2   1 
ATOM   13264 N  N     . ASN   E 4  281 ? 12.788  58.044  -102.482 1.00 52.87  ? 281 ASN   F N     1 
ATOM   13265 C  CA    . ASN   E 4  281 ? 12.511  59.057  -103.492 1.00 46.02  ? 281 ASN   F CA    1 
ATOM   13266 C  C     . ASN   E 4  281 ? 11.205  58.790  -104.214 1.00 49.22  ? 281 ASN   F C     1 
ATOM   13267 O  O     . ASN   E 4  281 ? 10.550  59.728  -104.681 1.00 51.95  ? 281 ASN   F O     1 
ATOM   13268 C  CB    . ASN   E 4  281 ? 13.646  59.118  -104.504 1.00 48.39  ? 281 ASN   F CB    1 
ATOM   13269 C  CG    . ASN   E 4  281 ? 14.944  59.582  -103.901 1.00 48.78  ? 281 ASN   F CG    1 
ATOM   13270 O  OD1   . ASN   E 4  281 ? 15.139  59.562  -102.680 1.00 43.38  ? 281 ASN   F OD1   1 
ATOM   13271 N  ND2   . ASN   E 4  281 ? 15.854  60.005  -104.764 1.00 50.87  ? 281 ASN   F ND2   1 
ATOM   13272 N  N     . SER   E 4  282 ? 10.818  57.525  -104.334 1.00 61.25  ? 282 SER   F N     1 
ATOM   13273 C  CA    . SER   E 4  282 ? 9.713   57.171  -105.214 1.00 55.29  ? 282 SER   F CA    1 
ATOM   13274 C  C     . SER   E 4  282 ? 8.378   57.117  -104.487 1.00 52.06  ? 282 SER   F C     1 
ATOM   13275 O  O     . SER   E 4  282 ? 7.373   57.603  -105.018 1.00 49.61  ? 282 SER   F O     1 
ATOM   13276 C  CB    . SER   E 4  282 ? 9.998   55.833  -105.902 1.00 49.66  ? 282 SER   F CB    1 
ATOM   13277 O  OG    . SER   E 4  282 ? 10.527  54.893  -104.984 1.00 58.30  ? 282 SER   F OG    1 
ATOM   13278 N  N     . ILE   E 4  283 ? 8.334   56.549  -103.284 1.00 46.68  ? 283 ILE   F N     1 
ATOM   13279 C  CA    . ILE   E 4  283 ? 7.084   56.393  -102.545 1.00 55.79  ? 283 ILE   F CA    1 
ATOM   13280 C  C     . ILE   E 4  283 ? 7.059   57.253  -101.282 1.00 52.79  ? 283 ILE   F C     1 
ATOM   13281 O  O     . ILE   E 4  283 ? 6.176   58.095  -101.118 1.00 44.70  ? 283 ILE   F O     1 
ATOM   13282 C  CB    . ILE   E 4  283 ? 6.811   54.911  -102.211 1.00 61.22  ? 283 ILE   F CB    1 
ATOM   13283 C  CG1   . ILE   E 4  283 ? 7.087   54.014  -103.423 1.00 64.14  ? 283 ILE   F CG1   1 
ATOM   13284 C  CG2   . ILE   E 4  283 ? 5.376   54.756  -101.770 1.00 62.62  ? 283 ILE   F CG2   1 
ATOM   13285 C  CD1   . ILE   E 4  283 ? 6.082   54.165  -104.543 1.00 60.47  ? 283 ILE   F CD1   1 
ATOM   13286 N  N     . LEU   E 4  284 ? 8.054   57.079  -100.395 1.00 53.03  ? 284 LEU   F N     1 
ATOM   13287 C  CA    A LEU   E 4  284 ? 7.958   57.630  -99.043  0.65 52.71  ? 284 LEU   F CA    1 
ATOM   13288 C  CA    B LEU   E 4  284 ? 7.961   57.631  -99.044  0.35 52.68  ? 284 LEU   F CA    1 
ATOM   13289 C  C     . LEU   E 4  284 ? 7.790   59.146  -99.056  1.00 52.11  ? 284 LEU   F C     1 
ATOM   13290 O  O     . LEU   E 4  284 ? 7.053   59.699  -98.233  1.00 49.44  ? 284 LEU   F O     1 
ATOM   13291 C  CB    A LEU   E 4  284 ? 9.185   57.225  -98.223  0.65 52.96  ? 284 LEU   F CB    1 
ATOM   13292 C  CB    B LEU   E 4  284 ? 9.193   57.235  -98.227  0.35 52.96  ? 284 LEU   F CB    1 
ATOM   13293 C  CG    A LEU   E 4  284 ? 8.961   56.483  -96.894  0.65 50.86  ? 284 LEU   F CG    1 
ATOM   13294 C  CG    B LEU   E 4  284 ? 9.278   55.777  -97.757  0.35 50.46  ? 284 LEU   F CG    1 
ATOM   13295 C  CD1   A LEU   E 4  284 ? 7.999   55.327  -97.051  0.65 46.85  ? 284 LEU   F CD1   1 
ATOM   13296 C  CD1   B LEU   E 4  284 ? 10.607  55.505  -97.064  0.35 50.39  ? 284 LEU   F CD1   1 
ATOM   13297 C  CD2   A LEU   E 4  284 ? 10.282  55.976  -96.332  0.65 49.73  ? 284 LEU   F CD2   1 
ATOM   13298 C  CD2   B LEU   E 4  284 ? 8.122   55.437  -96.832  0.35 47.11  ? 284 LEU   F CD2   1 
ATOM   13299 N  N     . LEU   E 4  285 ? 8.460   59.841  -99.979  1.00 63.46  ? 285 LEU   F N     1 
ATOM   13300 C  CA    . LEU   E 4  285 ? 8.323   61.296  -100.030 1.00 50.42  ? 285 LEU   F CA    1 
ATOM   13301 C  C     . LEU   E 4  285 ? 6.863   61.703  -100.180 1.00 44.78  ? 285 LEU   F C     1 
ATOM   13302 O  O     . LEU   E 4  285 ? 6.362   62.540  -99.425  1.00 54.97  ? 285 LEU   F O     1 
ATOM   13303 C  CB    . LEU   E 4  285 ? 9.166   61.869  -101.160 1.00 50.49  ? 285 LEU   F CB    1 
ATOM   13304 C  CG    . LEU   E 4  285 ? 10.112  63.011  -100.791 1.00 48.58  ? 285 LEU   F CG    1 
ATOM   13305 C  CD1   . LEU   E 4  285 ? 10.855  63.454  -102.034 1.00 54.55  ? 285 LEU   F CD1   1 
ATOM   13306 C  CD2   . LEU   E 4  285 ? 9.358   64.178  -100.185 1.00 53.43  ? 285 LEU   F CD2   1 
ATOM   13307 N  N     . GLN   E 4  286 ? 6.149   61.103  -101.128 1.00 43.55  ? 286 GLN   F N     1 
ATOM   13308 C  CA    . GLN   E 4  286 ? 4.721   61.397  -101.244 1.00 50.86  ? 286 GLN   F CA    1 
ATOM   13309 C  C     . GLN   E 4  286 ? 3.939   60.940  -100.012 1.00 47.68  ? 286 GLN   F C     1 
ATOM   13310 O  O     . GLN   E 4  286 ? 2.974   61.598  -99.608  1.00 47.19  ? 286 GLN   F O     1 
ATOM   13311 C  CB    . GLN   E 4  286 ? 4.139   60.741  -102.493 1.00 43.72  ? 286 GLN   F CB    1 
ATOM   13312 C  CG    . GLN   E 4  286 ? 4.665   61.268  -103.795 1.00 42.88  ? 286 GLN   F CG    1 
ATOM   13313 C  CD    . GLN   E 4  286 ? 4.459   60.271  -104.907 1.00 50.09  ? 286 GLN   F CD    1 
ATOM   13314 O  OE1   . GLN   E 4  286 ? 3.408   60.240  -105.556 1.00 49.58  ? 286 GLN   F OE1   1 
ATOM   13315 N  NE2   . GLN   E 4  286 ? 5.455   59.429  -105.119 1.00 45.76  ? 286 GLN   F NE2   1 
ATOM   13316 N  N     . ILE   E 4  287 ? 4.305   59.793  -99.428  1.00 43.41  ? 287 ILE   F N     1 
ATOM   13317 C  CA    . ILE   E 4  287 ? 3.608   59.322  -98.234  1.00 42.03  ? 287 ILE   F CA    1 
ATOM   13318 C  C     . ILE   E 4  287 ? 3.763   60.333  -97.107  1.00 45.65  ? 287 ILE   F C     1 
ATOM   13319 O  O     . ILE   E 4  287 ? 2.778   60.768  -96.501  1.00 47.68  ? 287 ILE   F O     1 
ATOM   13320 C  CB    . ILE   E 4  287 ? 4.111   57.929  -97.809  1.00 50.71  ? 287 ILE   F CB    1 
ATOM   13321 C  CG1   . ILE   E 4  287 ? 3.461   56.826  -98.650  1.00 49.29  ? 287 ILE   F CG1   1 
ATOM   13322 C  CG2   . ILE   E 4  287 ? 3.823   57.688  -96.318  1.00 43.42  ? 287 ILE   F CG2   1 
ATOM   13323 C  CD1   . ILE   E 4  287 ? 3.922   55.438  -98.282  1.00 43.23  ? 287 ILE   F CD1   1 
ATOM   13324 N  N     . LYS   E 4  288 ? 5.003   60.738  -96.823  1.00 46.58  ? 288 LYS   F N     1 
ATOM   13325 C  CA    . LYS   E 4  288 ? 5.238   61.680  -95.735  1.00 43.06  ? 288 LYS   F CA    1 
ATOM   13326 C  C     . LYS   E 4  288 ? 4.424   62.951  -95.934  1.00 44.72  ? 288 LYS   F C     1 
ATOM   13327 O  O     . LYS   E 4  288 ? 3.737   63.414  -95.016  1.00 53.09  ? 288 LYS   F O     1 
ATOM   13328 C  CB    . LYS   E 4  288 ? 6.735   61.968  -95.610  1.00 39.97  ? 288 LYS   F CB    1 
ATOM   13329 C  CG    . LYS   E 4  288 ? 7.513   60.725  -95.168  1.00 45.22  ? 288 LYS   F CG    1 
ATOM   13330 C  CD    . LYS   E 4  288 ? 8.927   60.995  -94.682  1.00 27.75  ? 288 LYS   F CD    1 
ATOM   13331 C  CE    . LYS   E 4  288 ? 9.937   61.046  -95.814  1.00 49.12  ? 288 LYS   F CE    1 
ATOM   13332 N  NZ    . LYS   E 4  288 ? 11.324  60.738  -95.302  1.00 57.66  ? 288 LYS   F NZ    1 
ATOM   13333 N  N     . HIS   E 4  289 ? 4.453   63.504  -97.142  1.00 39.00  ? 289 HIS   F N     1 
ATOM   13334 C  CA    . HIS   E 4  289 ? 3.618   64.658  -97.454  1.00 35.74  ? 289 HIS   F CA    1 
ATOM   13335 C  C     . HIS   E 4  289 ? 2.138   64.371  -97.208  1.00 42.94  ? 289 HIS   F C     1 
ATOM   13336 O  O     . HIS   E 4  289 ? 1.431   65.210  -96.635  1.00 47.71  ? 289 HIS   F O     1 
ATOM   13337 C  CB    . HIS   E 4  289 ? 3.868   65.088  -98.906  1.00 42.67  ? 289 HIS   F CB    1 
ATOM   13338 C  CG    . HIS   E 4  289 ? 2.808   65.979  -99.483  1.00 42.48  ? 289 HIS   F CG    1 
ATOM   13339 N  ND1   . HIS   E 4  289 ? 2.734   67.331  -99.210  1.00 39.14  ? 289 HIS   F ND1   1 
ATOM   13340 C  CD2   . HIS   E 4  289 ? 1.793   65.711  -100.339 1.00 37.77  ? 289 HIS   F CD2   1 
ATOM   13341 C  CE1   . HIS   E 4  289 ? 1.716   67.852  -99.869  1.00 37.17  ? 289 HIS   F CE1   1 
ATOM   13342 N  NE2   . HIS   E 4  289 ? 1.129   66.891  -100.564 1.00 36.45  ? 289 HIS   F NE2   1 
ATOM   13343 N  N     . ILE   E 4  290 ? 1.643   63.196  -97.629  1.00 45.10  ? 290 ILE   F N     1 
ATOM   13344 C  CA    . ILE   E 4  290 ? 0.206   62.919  -97.517  1.00 46.28  ? 290 ILE   F CA    1 
ATOM   13345 C  C     . ILE   E 4  290 ? -0.228  62.840  -96.054  1.00 40.77  ? 290 ILE   F C     1 
ATOM   13346 O  O     . ILE   E 4  290 ? -1.275  63.372  -95.682  1.00 35.06  ? 290 ILE   F O     1 
ATOM   13347 C  CB    . ILE   E 4  290 ? -0.177  61.645  -98.293  1.00 53.21  ? 290 ILE   F CB    1 
ATOM   13348 C  CG1   . ILE   E 4  290 ? -0.346  61.957  -99.789  1.00 48.78  ? 290 ILE   F CG1   1 
ATOM   13349 C  CG2   . ILE   E 4  290 ? -1.474  61.058  -97.751  1.00 43.05  ? 290 ILE   F CG2   1 
ATOM   13350 C  CD1   . ILE   E 4  290 ? -0.345  60.732  -100.692 1.00 45.72  ? 290 ILE   F CD1   1 
ATOM   13351 N  N     . ILE   E 4  291 ? 0.576   62.209  -95.198  1.00 33.55  ? 291 ILE   F N     1 
ATOM   13352 C  CA    . ILE   E 4  291 ? 0.255   62.156  -93.774  1.00 34.30  ? 291 ILE   F CA    1 
ATOM   13353 C  C     . ILE   E 4  291 ? 0.230   63.561  -93.171  1.00 44.60  ? 291 ILE   F C     1 
ATOM   13354 O  O     . ILE   E 4  291 ? -0.716  63.938  -92.472  1.00 37.13  ? 291 ILE   F O     1 
ATOM   13355 C  CB    . ILE   E 4  291 ? 1.251   61.246  -93.038  1.00 36.14  ? 291 ILE   F CB    1 
ATOM   13356 C  CG1   . ILE   E 4  291 ? 1.226   59.837  -93.636  1.00 38.48  ? 291 ILE   F CG1   1 
ATOM   13357 C  CG2   . ILE   E 4  291 ? 0.924   61.193  -91.563  1.00 41.92  ? 291 ILE   F CG2   1 
ATOM   13358 C  CD1   . ILE   E 4  291 ? 2.546   59.085  -93.542  1.00 30.14  ? 291 ILE   F CD1   1 
ATOM   13359 N  N     . ARG   E 4  292 ? 1.267   64.364  -93.434  1.00 49.32  ? 292 ARG   F N     1 
ATOM   13360 C  CA    . ARG   E 4  292 ? 1.327   65.692  -92.827  1.00 49.49  ? 292 ARG   F CA    1 
ATOM   13361 C  C     . ARG   E 4  292 ? 0.130   66.543  -93.249  1.00 48.36  ? 292 ARG   F C     1 
ATOM   13362 O  O     . ARG   E 4  292 ? -0.509  67.198  -92.414  1.00 45.86  ? 292 ARG   F O     1 
ATOM   13363 C  CB    . ARG   E 4  292 ? 2.646   66.386  -93.180  1.00 47.08  ? 292 ARG   F CB    1 
ATOM   13364 C  CG    . ARG   E 4  292 ? 3.351   67.049  -91.995  1.00 55.56  ? 292 ARG   F CG    1 
ATOM   13365 C  CD    . ARG   E 4  292 ? 4.085   68.356  -92.370  1.00 62.88  ? 292 ARG   F CD    1 
ATOM   13366 N  NE    . ARG   E 4  292 ? 4.629   68.316  -93.719  1.00 57.16  ? 292 ARG   F NE    1 
ATOM   13367 C  CZ    . ARG   E 4  292 ? 5.561   67.460  -94.115  1.00 69.76  ? 292 ARG   F CZ    1 
ATOM   13368 N  NH1   . ARG   E 4  292 ? 6.121   66.613  -93.270  1.00 79.24  ? 292 ARG   F NH1   1 
ATOM   13369 N  NH2   . ARG   E 4  292 ? 5.929   67.438  -95.395  1.00 64.90  ? 292 ARG   F NH2   1 
ATOM   13370 N  N     . SER   E 4  293 ? -0.202  66.540  -94.541  1.00 40.57  ? 293 SER   F N     1 
ATOM   13371 C  CA    . SER   E 4  293 ? -1.341  67.337  -94.998  1.00 48.28  ? 293 SER   F CA    1 
ATOM   13372 C  C     . SER   E 4  293 ? -2.644  66.897  -94.330  1.00 47.28  ? 293 SER   F C     1 
ATOM   13373 O  O     . SER   E 4  293 ? -3.471  67.738  -93.953  1.00 40.96  ? 293 SER   F O     1 
ATOM   13374 C  CB    . SER   E 4  293 ? -1.483  67.255  -96.523  1.00 46.79  ? 293 SER   F CB    1 
ATOM   13375 O  OG    . SER   E 4  293 ? -0.263  67.523  -97.182  1.00 46.83  ? 293 SER   F OG    1 
ATOM   13376 N  N     . CYS   E 4  294 ? -2.858  65.582  -94.200  1.00 48.67  ? 294 CYS   F N     1 
ATOM   13377 C  CA    . CYS   E 4  294 ? -4.118  65.083  -93.656  1.00 41.87  ? 294 CYS   F CA    1 
ATOM   13378 C  C     . CYS   E 4  294 ? -4.282  65.496  -92.207  1.00 42.02  ? 294 CYS   F C     1 
ATOM   13379 O  O     . CYS   E 4  294 ? -5.334  66.007  -91.813  1.00 40.62  ? 294 CYS   F O     1 
ATOM   13380 C  CB    . CYS   E 4  294 ? -4.192  63.562  -93.781  1.00 37.59  ? 294 CYS   F CB    1 
ATOM   13381 S  SG    . CYS   E 4  294 ? -4.650  62.968  -95.423  1.00 50.66  ? 294 CYS   F SG    1 
ATOM   13382 N  N     . LEU   E 4  295 ? -3.240  65.288  -91.403  1.00 40.83  ? 295 LEU   F N     1 
ATOM   13383 C  CA    . LEU   E 4  295 ? -3.316  65.585  -89.976  1.00 43.56  ? 295 LEU   F CA    1 
ATOM   13384 C  C     . LEU   E 4  295 ? -3.252  67.088  -89.699  1.00 44.63  ? 295 LEU   F C     1 
ATOM   13385 O  O     . LEU   E 4  295 ? -4.009  67.597  -88.868  1.00 50.49  ? 295 LEU   F O     1 
ATOM   13386 C  CB    . LEU   E 4  295 ? -2.206  64.833  -89.235  1.00 41.79  ? 295 LEU   F CB    1 
ATOM   13387 C  CG    . LEU   E 4  295 ? -2.474  63.321  -89.248  1.00 41.87  ? 295 LEU   F CG    1 
ATOM   13388 C  CD1   . LEU   E 4  295 ? -1.343  62.508  -88.629  1.00 37.06  ? 295 LEU   F CD1   1 
ATOM   13389 C  CD2   . LEU   E 4  295 ? -3.801  63.047  -88.555  1.00 42.69  ? 295 LEU   F CD2   1 
ATOM   13390 N  N     . MET   E 4  296 ? -2.367  67.822  -90.374  1.00 44.52  ? 296 MET   F N     1 
ATOM   13391 C  CA    . MET   E 4  296 ? -2.359  69.267  -90.173  1.00 49.75  ? 296 MET   F CA    1 
ATOM   13392 C  C     . MET   E 4  296 ? -3.707  69.886  -90.517  1.00 42.83  ? 296 MET   F C     1 
ATOM   13393 O  O     . MET   E 4  296 ? -4.113  70.882  -89.912  1.00 42.79  ? 296 MET   F O     1 
ATOM   13394 C  CB    . MET   E 4  296 ? -1.257  69.913  -91.001  1.00 52.34  ? 296 MET   F CB    1 
ATOM   13395 C  CG    . MET   E 4  296 ? 0.122   69.796  -90.398  1.00 60.02  ? 296 MET   F CG    1 
ATOM   13396 S  SD    . MET   E 4  296 ? 1.323   70.310  -91.646  1.00 78.34  ? 296 MET   F SD    1 
ATOM   13397 C  CE    . MET   E 4  296 ? 0.808   72.018  -91.928  1.00 71.27  ? 296 MET   F CE    1 
ATOM   13398 N  N     . CYS   E 4  297 ? -4.425  69.306  -91.466  1.00 37.06  ? 297 CYS   F N     1 
ATOM   13399 C  CA    . CYS   E 4  297 ? -5.721  69.855  -91.830  1.00 40.68  ? 297 CYS   F CA    1 
ATOM   13400 C  C     . CYS   E 4  297 ? -6.668  69.907  -90.628  1.00 47.45  ? 297 CYS   F C     1 
ATOM   13401 O  O     . CYS   E 4  297 ? -7.319  70.927  -90.375  1.00 46.66  ? 297 CYS   F O     1 
ATOM   13402 C  CB    . CYS   E 4  297 ? -6.309  69.019  -92.951  1.00 37.19  ? 297 CYS   F CB    1 
ATOM   13403 S  SG    . CYS   E 4  297 ? -7.945  69.467  -93.318  1.00 55.38  ? 297 CYS   F SG    1 
ATOM   13404 N  N     . ILE   E 4  298 ? -6.754  68.807  -89.872  1.00 46.39  ? 298 ILE   F N     1 
ATOM   13405 C  CA    . ILE   E 4  298 ? -7.696  68.696  -88.763  1.00 41.85  ? 298 ILE   F CA    1 
ATOM   13406 C  C     . ILE   E 4  298 ? -7.098  69.069  -87.421  1.00 44.97  ? 298 ILE   F C     1 
ATOM   13407 O  O     . ILE   E 4  298 ? -7.777  68.919  -86.395  1.00 46.42  ? 298 ILE   F O     1 
ATOM   13408 C  CB    . ILE   E 4  298 ? -8.216  67.262  -88.605  1.00 35.20  ? 298 ILE   F CB    1 
ATOM   13409 C  CG1   . ILE   E 4  298 ? -7.016  66.362  -88.317  1.00 32.10  ? 298 ILE   F CG1   1 
ATOM   13410 C  CG2   . ILE   E 4  298 ? -9.025  66.857  -89.840  1.00 48.95  ? 298 ILE   F CG2   1 
ATOM   13411 C  CD1   . ILE   E 4  298 ? -7.360  65.074  -87.689  1.00 34.11  ? 298 ILE   F CD1   1 
ATOM   13412 N  N     . GLU   E 4  299 ? -5.843  69.509  -87.380  1.00 44.21  ? 299 GLU   F N     1 
ATOM   13413 C  CA    . GLU   E 4  299 ? -5.241  69.850  -86.093  1.00 42.27  ? 299 GLU   F CA    1 
ATOM   13414 C  C     . GLU   E 4  299 ? -6.081  70.826  -85.283  1.00 41.44  ? 299 GLU   F C     1 
ATOM   13415 O  O     . GLU   E 4  299 ? -6.283  70.574  -84.084  1.00 46.19  ? 299 GLU   F O     1 
ATOM   13416 C  CB    . GLU   E 4  299 ? -3.829  70.402  -86.304  1.00 42.79  ? 299 GLU   F CB    1 
ATOM   13417 C  CG    . GLU   E 4  299 ? -3.396  71.319  -85.192  1.00 44.10  ? 299 GLU   F CG    1 
ATOM   13418 C  CD    . GLU   E 4  299 ? -1.898  71.433  -85.094  1.00 51.99  ? 299 GLU   F CD    1 
ATOM   13419 O  OE1   . GLU   E 4  299 ? -1.229  71.498  -86.152  1.00 51.94  ? 299 GLU   F OE1   1 
ATOM   13420 O  OE2   . GLU   E 4  299 ? -1.386  71.439  -83.952  1.00 58.34  ? 299 GLU   F OE2   1 
ATOM   13421 N  N     . PRO   E 4  300 ? -6.585  71.935  -85.843  1.00 40.66  ? 300 PRO   F N     1 
ATOM   13422 C  CA    . PRO   E 4  300 ? -7.431  72.840  -85.042  1.00 42.27  ? 300 PRO   F CA    1 
ATOM   13423 C  C     . PRO   E 4  300 ? -8.683  72.181  -84.475  1.00 43.12  ? 300 PRO   F C     1 
ATOM   13424 O  O     . PRO   E 4  300 ? -9.159  72.589  -83.407  1.00 42.95  ? 300 PRO   F O     1 
ATOM   13425 C  CB    . PRO   E 4  300 ? -7.769  73.977  -86.025  1.00 26.70  ? 300 PRO   F CB    1 
ATOM   13426 C  CG    . PRO   E 4  300 ? -7.297  73.543  -87.330  1.00 34.49  ? 300 PRO   F CG    1 
ATOM   13427 C  CD    . PRO   E 4  300 ? -6.214  72.549  -87.123  1.00 37.02  ? 300 PRO   F CD    1 
ATOM   13428 N  N     . ALA   E 4  301 ? -9.215  71.150  -85.121  1.00 34.96  ? 301 ALA   F N     1 
ATOM   13429 C  CA    . ALA   E 4  301 ? -10.392 70.514  -84.552  1.00 37.63  ? 301 ALA   F CA    1 
ATOM   13430 C  C     . ALA   E 4  301 ? -10.064 69.537  -83.417  1.00 40.42  ? 301 ALA   F C     1 
ATOM   13431 O  O     . ALA   E 4  301 ? -10.906 69.334  -82.538  1.00 44.49  ? 301 ALA   F O     1 
ATOM   13432 C  CB    . ALA   E 4  301 ? -11.174 69.809  -85.654  1.00 35.34  ? 301 ALA   F CB    1 
ATOM   13433 N  N     . ILE   E 4  302 ? -8.880  68.921  -83.395  1.00 36.72  ? 302 ILE   F N     1 
ATOM   13434 C  CA    . ILE   E 4  302 ? -8.603  67.847  -82.440  1.00 40.47  ? 302 ILE   F CA    1 
ATOM   13435 C  C     . ILE   E 4  302 ? -7.416  68.123  -81.525  1.00 44.52  ? 302 ILE   F C     1 
ATOM   13436 O  O     . ILE   E 4  302 ? -7.227  67.378  -80.547  1.00 47.02  ? 302 ILE   F O     1 
ATOM   13437 C  CB    . ILE   E 4  302 ? -8.409  66.473  -83.137  1.00 35.89  ? 302 ILE   F CB    1 
ATOM   13438 C  CG1   . ILE   E 4  302 ? -7.186  66.455  -84.049  1.00 30.76  ? 302 ILE   F CG1   1 
ATOM   13439 C  CG2   . ILE   E 4  302 ? -9.629  66.094  -83.940  1.00 37.14  ? 302 ILE   F CG2   1 
ATOM   13440 C  CD1   . ILE   E 4  302 ? -6.854  65.081  -84.544  1.00 26.60  ? 302 ILE   F CD1   1 
ATOM   13441 N  N     . SER   E 4  303 ? -6.605  69.147  -81.784  1.00 40.81  ? 303 SER   F N     1 
ATOM   13442 C  CA    . SER   E 4  303 ? -5.483  69.418  -80.890  1.00 40.28  ? 303 SER   F CA    1 
ATOM   13443 C  C     . SER   E 4  303 ? -5.939  69.521  -79.435  1.00 39.44  ? 303 SER   F C     1 
ATOM   13444 O  O     . SER   E 4  303 ? -7.064  69.927  -79.131  1.00 38.43  ? 303 SER   F O     1 
ATOM   13445 C  CB    . SER   E 4  303 ? -4.772  70.706  -81.282  1.00 40.62  ? 303 SER   F CB    1 
ATOM   13446 O  OG    . SER   E 4  303 ? -3.642  70.883  -80.454  1.00 39.42  ? 303 SER   F OG    1 
ATOM   13447 N  N     . THR   E 4  304 ? -5.045  69.162  -78.521  1.00 41.32  ? 304 THR   F N     1 
ATOM   13448 C  CA    . THR   E 4  304 ? -5.311  69.345  -77.102  1.00 37.35  ? 304 THR   F CA    1 
ATOM   13449 C  C     . THR   E 4  304 ? -4.291  70.256  -76.432  1.00 45.72  ? 304 THR   F C     1 
ATOM   13450 O  O     . THR   E 4  304 ? -4.133  70.204  -75.211  1.00 51.82  ? 304 THR   F O     1 
ATOM   13451 C  CB    . THR   E 4  304 ? -5.357  67.999  -76.397  1.00 40.59  ? 304 THR   F CB    1 
ATOM   13452 O  OG1   . THR   E 4  304 ? -4.066  67.382  -76.487  1.00 45.13  ? 304 THR   F OG1   1 
ATOM   13453 C  CG2   . THR   E 4  304 ? -6.427  67.124  -77.036  1.00 34.44  ? 304 THR   F CG2   1 
ATOM   13454 N  N     . LYS   E 4  305 ? -3.622  71.114  -77.208  1.00 50.67  ? 305 LYS   F N     1 
ATOM   13455 C  CA    . LYS   E 4  305 ? -2.581  71.977  -76.669  1.00 51.28  ? 305 LYS   F CA    1 
ATOM   13456 C  C     . LYS   E 4  305 ? -3.048  72.745  -75.431  1.00 49.83  ? 305 LYS   F C     1 
ATOM   13457 O  O     . LYS   E 4  305 ? -2.298  72.884  -74.460  1.00 51.72  ? 305 LYS   F O     1 
ATOM   13458 C  CB    . LYS   E 4  305 ? -2.102  72.946  -77.753  1.00 55.34  ? 305 LYS   F CB    1 
ATOM   13459 C  CG    . LYS   E 4  305 ? -0.922  73.812  -77.319  1.00 72.91  ? 305 LYS   F CG    1 
ATOM   13460 C  CD    . LYS   E 4  305 ? -0.683  75.007  -78.236  1.00 79.64  ? 305 LYS   F CD    1 
ATOM   13461 C  CE    . LYS   E 4  305 ? 0.414   75.919  -77.669  1.00 88.63  ? 305 LYS   F CE    1 
ATOM   13462 N  NZ    . LYS   E 4  305 ? 0.770   77.037  -78.596  1.00 82.88  ? 305 LYS   F NZ    1 
ATOM   13463 N  N     . HIS   E 4  306 ? -4.268  73.263  -75.441  1.00 52.12  ? 306 HIS   F N     1 
ATOM   13464 C  CA    . HIS   E 4  306 ? -4.741  74.079  -74.324  1.00 54.76  ? 306 HIS   F CA    1 
ATOM   13465 C  C     . HIS   E 4  306 ? -5.964  73.454  -73.681  1.00 51.09  ? 306 HIS   F C     1 
ATOM   13466 O  O     . HIS   E 4  306 ? -6.885  74.146  -73.241  1.00 51.99  ? 306 HIS   F O     1 
ATOM   13467 C  CB    . HIS   E 4  306 ? -5.043  75.506  -74.773  1.00 57.56  ? 306 HIS   F CB    1 
ATOM   13468 C  CG    . HIS   E 4  306 ? -3.869  76.192  -75.397  1.00 66.41  ? 306 HIS   F CG    1 
ATOM   13469 N  ND1   . HIS   E 4  306 ? -3.925  76.782  -76.643  1.00 67.48  ? 306 HIS   F ND1   1 
ATOM   13470 C  CD2   . HIS   E 4  306 ? -2.597  76.353  -74.958  1.00 69.73  ? 306 HIS   F CD2   1 
ATOM   13471 C  CE1   . HIS   E 4  306 ? -2.740  77.285  -76.941  1.00 76.57  ? 306 HIS   F CE1   1 
ATOM   13472 N  NE2   . HIS   E 4  306 ? -1.916  77.039  -75.936  1.00 84.82  ? 306 HIS   F NE2   1 
ATOM   13473 N  N     . LEU   E 4  307 ? -5.986  72.130  -73.632  1.00 41.05  ? 307 LEU   F N     1 
ATOM   13474 C  CA    . LEU   E 4  307 ? -7.143  71.400  -73.159  1.00 35.34  ? 307 LEU   F CA    1 
ATOM   13475 C  C     . LEU   E 4  307 ? -6.825  70.780  -71.803  1.00 36.73  ? 307 LEU   F C     1 
ATOM   13476 O  O     . LEU   E 4  307 ? -5.663  70.558  -71.451  1.00 29.34  ? 307 LEU   F O     1 
ATOM   13477 C  CB    . LEU   E 4  307 ? -7.551  70.336  -74.178  1.00 31.71  ? 307 LEU   F CB    1 
ATOM   13478 C  CG    . LEU   E 4  307 ? -8.991  69.852  -74.099  1.00 37.44  ? 307 LEU   F CG    1 
ATOM   13479 C  CD1   . LEU   E 4  307 ? -9.932  71.009  -74.300  1.00 30.70  ? 307 LEU   F CD1   1 
ATOM   13480 C  CD2   . LEU   E 4  307 ? -9.265  68.718  -75.113  1.00 34.22  ? 307 LEU   F CD2   1 
ATOM   13481 N  N     . HIS   E 4  308 ? -7.881  70.503  -71.037  1.00 35.35  ? 308 HIS   F N     1 
ATOM   13482 C  CA    . HIS   E 4  308 ? -7.728  70.018  -69.673  1.00 26.18  ? 308 HIS   F CA    1 
ATOM   13483 C  C     . HIS   E 4  308 ? -7.353  68.541  -69.601  1.00 27.20  ? 308 HIS   F C     1 
ATOM   13484 O  O     . HIS   E 4  308 ? -6.996  68.061  -68.518  1.00 29.41  ? 308 HIS   F O     1 
ATOM   13485 C  CB    . HIS   E 4  308 ? -9.010  70.297  -68.898  1.00 26.79  ? 308 HIS   F CB    1 
ATOM   13486 C  CG    . HIS   E 4  308 ? -10.240 70.003  -69.683  1.00 31.29  ? 308 HIS   F CG    1 
ATOM   13487 N  ND1   . HIS   E 4  308 ? -10.818 70.928  -70.525  1.00 33.24  ? 308 HIS   F ND1   1 
ATOM   13488 C  CD2   . HIS   E 4  308 ? -10.982 68.878  -69.789  1.00 27.72  ? 308 HIS   F CD2   1 
ATOM   13489 C  CE1   . HIS   E 4  308 ? -11.866 70.387  -71.118  1.00 26.65  ? 308 HIS   F CE1   1 
ATOM   13490 N  NE2   . HIS   E 4  308 ? -11.984 69.142  -70.691  1.00 36.50  ? 308 HIS   F NE2   1 
ATOM   13491 N  N     . TYR   E 4  309 ? -7.405  67.815  -70.713  1.00 28.03  ? 309 TYR   F N     1 
ATOM   13492 C  CA    . TYR   E 4  309 ? -6.743  66.522  -70.842  1.00 31.08  ? 309 TYR   F CA    1 
ATOM   13493 C  C     . TYR   E 4  309 ? -5.919  66.540  -72.127  1.00 34.42  ? 309 TYR   F C     1 
ATOM   13494 O  O     . TYR   E 4  309 ? -6.113  67.400  -72.986  1.00 34.37  ? 309 TYR   F O     1 
ATOM   13495 C  CB    . TYR   E 4  309 ? -7.746  65.351  -70.852  1.00 27.70  ? 309 TYR   F CB    1 
ATOM   13496 C  CG    . TYR   E 4  309 ? -8.610  65.325  -72.095  1.00 38.97  ? 309 TYR   F CG    1 
ATOM   13497 C  CD1   . TYR   E 4  309 ? -8.144  64.756  -73.280  1.00 29.62  ? 309 TYR   F CD1   1 
ATOM   13498 C  CD2   . TYR   E 4  309 ? -9.885  65.881  -72.089  1.00 32.76  ? 309 TYR   F CD2   1 
ATOM   13499 C  CE1   . TYR   E 4  309 ? -8.913  64.750  -74.397  1.00 31.86  ? 309 TYR   F CE1   1 
ATOM   13500 C  CE2   . TYR   E 4  309 ? -10.658 65.875  -73.209  1.00 28.10  ? 309 TYR   F CE2   1 
ATOM   13501 C  CZ    . TYR   E 4  309 ? -10.171 65.319  -74.361  1.00 32.95  ? 309 TYR   F CZ    1 
ATOM   13502 O  OH    . TYR   E 4  309 ? -10.945 65.325  -75.492  1.00 35.79  ? 309 TYR   F OH    1 
ATOM   13503 N  N     . GLN   E 4  310 ? -4.998  65.584  -72.245  1.00 35.95  ? 310 GLN   F N     1 
ATOM   13504 C  CA    . GLN   E 4  310 ? -4.117  65.440  -73.399  1.00 39.33  ? 310 GLN   F CA    1 
ATOM   13505 C  C     . GLN   E 4  310 ? -4.416  64.144  -74.144  1.00 35.12  ? 310 GLN   F C     1 
ATOM   13506 O  O     . GLN   E 4  310 ? -4.693  63.115  -73.525  1.00 33.85  ? 310 GLN   F O     1 
ATOM   13507 C  CB    . GLN   E 4  310 ? -2.637  65.427  -72.990  1.00 35.82  ? 310 GLN   F CB    1 
ATOM   13508 C  CG    . GLN   E 4  310 ? -2.117  66.697  -72.367  1.00 35.53  ? 310 GLN   F CG    1 
ATOM   13509 C  CD    . GLN   E 4  310 ? -2.258  67.875  -73.273  1.00 52.49  ? 310 GLN   F CD    1 
ATOM   13510 O  OE1   . GLN   E 4  310 ? -1.739  67.886  -74.405  1.00 58.63  ? 310 GLN   F OE1   1 
ATOM   13511 N  NE2   . GLN   E 4  310 ? -2.985  68.886  -72.800  1.00 52.48  ? 310 GLN   F NE2   1 
ATOM   13512 N  N     . SER   E 4  311 ? -4.326  64.194  -75.474  1.00 40.86  ? 311 SER   F N     1 
ATOM   13513 C  CA    . SER   E 4  311 ? -4.513  63.033  -76.341  1.00 39.51  ? 311 SER   F CA    1 
ATOM   13514 C  C     . SER   E 4  311 ? -3.213  62.663  -77.059  1.00 39.30  ? 311 SER   F C     1 
ATOM   13515 O  O     . SER   E 4  311 ? -2.375  63.521  -77.353  1.00 42.88  ? 311 SER   F O     1 
ATOM   13516 C  CB    . SER   E 4  311 ? -5.600  63.286  -77.400  1.00 32.69  ? 311 SER   F CB    1 
ATOM   13517 O  OG    . SER   E 4  311 ? -6.889  63.553  -76.855  1.00 36.10  ? 311 SER   F OG    1 
ATOM   13518 N  N     . PHE   E 4  312 ? -3.051  61.372  -77.336  1.00 35.21  ? 312 PHE   F N     1 
ATOM   13519 C  CA    . PHE   E 4  312 ? -2.181  60.900  -78.409  1.00 41.74  ? 312 PHE   F CA    1 
ATOM   13520 C  C     . PHE   E 4  312 ? -2.954  59.837  -79.183  1.00 35.13  ? 312 PHE   F C     1 
ATOM   13521 O  O     . PHE   E 4  312 ? -4.012  59.392  -78.746  1.00 36.27  ? 312 PHE   F O     1 
ATOM   13522 C  CB    . PHE   E 4  312 ? -0.823  60.372  -77.883  1.00 40.10  ? 312 PHE   F CB    1 
ATOM   13523 C  CG    . PHE   E 4  312 ? -0.900  59.042  -77.159  1.00 40.28  ? 312 PHE   F CG    1 
ATOM   13524 C  CD1   . PHE   E 4  312 ? -0.922  57.843  -77.870  1.00 39.18  ? 312 PHE   F CD1   1 
ATOM   13525 C  CD2   . PHE   E 4  312 ? -0.909  58.989  -75.770  1.00 40.49  ? 312 PHE   F CD2   1 
ATOM   13526 C  CE1   . PHE   E 4  312 ? -0.985  56.618  -77.211  1.00 40.98  ? 312 PHE   F CE1   1 
ATOM   13527 C  CE2   . PHE   E 4  312 ? -0.970  57.767  -75.103  1.00 44.97  ? 312 PHE   F CE2   1 
ATOM   13528 C  CZ    . PHE   E 4  312 ? -1.005  56.579  -75.823  1.00 41.94  ? 312 PHE   F CZ    1 
ATOM   13529 N  N     . GLN   E 4  313 ? -2.451  59.432  -80.351  1.00 45.13  ? 313 GLN   F N     1 
ATOM   13530 C  CA    . GLN   E 4  313 ? -3.152  58.388  -81.096  1.00 44.51  ? 313 GLN   F CA    1 
ATOM   13531 C  C     . GLN   E 4  313 ? -2.255  57.787  -82.169  1.00 44.68  ? 313 GLN   F C     1 
ATOM   13532 O  O     . GLN   E 4  313 ? -1.454  58.485  -82.798  1.00 38.43  ? 313 GLN   F O     1 
ATOM   13533 C  CB    . GLN   E 4  313 ? -4.440  58.920  -81.739  1.00 38.34  ? 313 GLN   F CB    1 
ATOM   13534 C  CG    . GLN   E 4  313 ? -5.259  57.848  -82.453  1.00 34.74  ? 313 GLN   F CG    1 
ATOM   13535 C  CD    . GLN   E 4  313 ? -6.641  58.345  -82.833  1.00 39.93  ? 313 GLN   F CD    1 
ATOM   13536 O  OE1   . GLN   E 4  313 ? -7.050  59.442  -82.417  1.00 38.63  ? 313 GLN   F OE1   1 
ATOM   13537 N  NE2   . GLN   E 4  313 ? -7.371  57.555  -83.633  1.00 35.13  ? 313 GLN   F NE2   1 
ATOM   13538 N  N     . LEU   E 4  314 ? -2.434  56.483  -82.386  1.00 46.70  ? 314 LEU   F N     1 
ATOM   13539 C  CA    . LEU   E 4  314 ? -1.750  55.744  -83.440  1.00 42.74  ? 314 LEU   F CA    1 
ATOM   13540 C  C     . LEU   E 4  314 ? -2.699  55.544  -84.614  1.00 43.68  ? 314 LEU   F C     1 
ATOM   13541 O  O     . LEU   E 4  314 ? -3.825  55.060  -84.433  1.00 37.58  ? 314 LEU   F O     1 
ATOM   13542 C  CB    . LEU   E 4  314 ? -1.252  54.391  -82.935  1.00 38.29  ? 314 LEU   F CB    1 
ATOM   13543 C  CG    . LEU   E 4  314 ? -0.495  53.544  -83.955  1.00 39.43  ? 314 LEU   F CG    1 
ATOM   13544 C  CD1   . LEU   E 4  314 ? 0.922   54.098  -84.197  1.00 34.83  ? 314 LEU   F CD1   1 
ATOM   13545 C  CD2   . LEU   E 4  314 ? -0.433  52.124  -83.460  1.00 44.60  ? 314 LEU   F CD2   1 
ATOM   13546 N  N     . PHE   E 4  315 ? -2.240  55.923  -85.809  1.00 36.56  ? 315 PHE   F N     1 
ATOM   13547 C  CA    . PHE   E 4  315 ? -3.044  55.892  -87.021  1.00 38.05  ? 315 PHE   F CA    1 
ATOM   13548 C  C     . PHE   E 4  315 ? -2.458  54.887  -88.008  1.00 46.14  ? 315 PHE   F C     1 
ATOM   13549 O  O     . PHE   E 4  315 ? -1.240  54.666  -88.056  1.00 48.46  ? 315 PHE   F O     1 
ATOM   13550 C  CB    . PHE   E 4  315 ? -3.127  57.283  -87.676  1.00 37.37  ? 315 PHE   F CB    1 
ATOM   13551 C  CG    . PHE   E 4  315 ? -3.943  58.285  -86.897  1.00 34.19  ? 315 PHE   F CG    1 
ATOM   13552 C  CD1   . PHE   E 4  315 ? -5.319  58.408  -87.117  1.00 40.62  ? 315 PHE   F CD1   1 
ATOM   13553 C  CD2   . PHE   E 4  315 ? -3.342  59.113  -85.951  1.00 32.75  ? 315 PHE   F CD2   1 
ATOM   13554 C  CE1   . PHE   E 4  315 ? -6.089  59.342  -86.388  1.00 37.97  ? 315 PHE   F CE1   1 
ATOM   13555 C  CE2   . PHE   E 4  315 ? -4.087  60.046  -85.224  1.00 32.31  ? 315 PHE   F CE2   1 
ATOM   13556 C  CZ    . PHE   E 4  315 ? -5.467  60.164  -85.440  1.00 34.80  ? 315 PHE   F CZ    1 
ATOM   13557 N  N     . GLY   E 4  316 ? -3.335  54.270  -88.793  1.00 42.60  ? 316 GLY   F N     1 
ATOM   13558 C  CA    . GLY   E 4  316 ? -2.880  53.346  -89.813  1.00 43.13  ? 316 GLY   F CA    1 
ATOM   13559 C  C     . GLY   E 4  316 ? -3.190  53.865  -91.195  1.00 43.74  ? 316 GLY   F C     1 
ATOM   13560 O  O     . GLY   E 4  316 ? -4.353  53.852  -91.604  1.00 58.63  ? 316 GLY   F O     1 
ATOM   13561 N  N     . PHE   E 4  317 ? -2.182  54.345  -91.920  1.00 41.27  ? 317 PHE   F N     1 
ATOM   13562 C  CA    . PHE   E 4  317 ? -2.397  54.934  -93.237  1.00 45.46  ? 317 PHE   F CA    1 
ATOM   13563 C  C     . PHE   E 4  317 ? -2.188  53.898  -94.338  1.00 45.65  ? 317 PHE   F C     1 
ATOM   13564 O  O     . PHE   E 4  317 ? -1.219  53.128  -94.314  1.00 42.39  ? 317 PHE   F O     1 
ATOM   13565 C  CB    . PHE   E 4  317 ? -1.468  56.130  -93.451  1.00 44.05  ? 317 PHE   F CB    1 
ATOM   13566 C  CG    . PHE   E 4  317 ? -1.997  57.429  -92.890  1.00 45.16  ? 317 PHE   F CG    1 
ATOM   13567 C  CD1   . PHE   E 4  317 ? -1.730  57.799  -91.572  1.00 43.34  ? 317 PHE   F CD1   1 
ATOM   13568 C  CD2   . PHE   E 4  317 ? -2.739  58.294  -93.687  1.00 41.71  ? 317 PHE   F CD2   1 
ATOM   13569 C  CE1   . PHE   E 4  317 ? -2.206  58.992  -91.054  1.00 36.67  ? 317 PHE   F CE1   1 
ATOM   13570 C  CE2   . PHE   E 4  317 ? -3.211  59.492  -93.173  1.00 36.38  ? 317 PHE   F CE2   1 
ATOM   13571 C  CZ    . PHE   E 4  317 ? -2.940  59.840  -91.853  1.00 30.93  ? 317 PHE   F CZ    1 
ATOM   13572 N  N     . ASP   E 4  318 ? -3.104  53.885  -95.305  1.00 46.46  ? 318 ASP   F N     1 
ATOM   13573 C  CA    . ASP   E 4  318 ? -3.129  52.857  -96.344  1.00 49.11  ? 318 ASP   F CA    1 
ATOM   13574 C  C     . ASP   E 4  318 ? -3.001  53.502  -97.719  1.00 48.09  ? 318 ASP   F C     1 
ATOM   13575 O  O     . ASP   E 4  318 ? -3.874  54.275  -98.133  1.00 46.64  ? 318 ASP   F O     1 
ATOM   13576 C  CB    . ASP   E 4  318 ? -4.411  52.023  -96.259  1.00 50.44  ? 318 ASP   F CB    1 
ATOM   13577 C  CG    . ASP   E 4  318 ? -4.398  51.023  -95.102  1.00 57.03  ? 318 ASP   F CG    1 
ATOM   13578 O  OD1   . ASP   E 4  318 ? -3.468  51.069  -94.253  1.00 52.88  ? 318 ASP   F OD1   1 
ATOM   13579 O  OD2   . ASP   E 4  318 ? -5.329  50.184  -95.053  1.00 58.56  ? 318 ASP   F OD2   1 
ATOM   13580 N  N     . PHE   E 4  319 ? -1.929  53.159  -98.437  1.00 48.11  ? 319 PHE   F N     1 
ATOM   13581 C  CA    . PHE   E 4  319 ? -1.602  53.786  -99.707  1.00 44.77  ? 319 PHE   F CA    1 
ATOM   13582 C  C     . PHE   E 4  319 ? -1.564  52.770  -100.840 1.00 50.25  ? 319 PHE   F C     1 
ATOM   13583 O  O     . PHE   E 4  319 ? -1.176  51.606  -100.658 1.00 38.00  ? 319 PHE   F O     1 
ATOM   13584 C  CB    . PHE   E 4  319 ? -0.246  54.499  -99.649  1.00 51.11  ? 319 PHE   F CB    1 
ATOM   13585 C  CG    . PHE   E 4  319 ? -0.159  55.547  -98.592  1.00 48.44  ? 319 PHE   F CG    1 
ATOM   13586 C  CD1   . PHE   E 4  319 ? -0.646  56.818  -98.823  1.00 49.63  ? 319 PHE   F CD1   1 
ATOM   13587 C  CD2   . PHE   E 4  319 ? 0.406   55.260  -97.365  1.00 48.21  ? 319 PHE   F CD2   1 
ATOM   13588 C  CE1   . PHE   E 4  319 ? -0.567  57.781  -97.852  1.00 48.51  ? 319 PHE   F CE1   1 
ATOM   13589 C  CE2   . PHE   E 4  319 ? 0.483   56.220  -96.389  1.00 44.87  ? 319 PHE   F CE2   1 
ATOM   13590 C  CZ    . PHE   E 4  319 ? -0.000  57.479  -96.631  1.00 45.04  ? 319 PHE   F CZ    1 
ATOM   13591 N  N     . MET   E 4  320 ? -1.976  53.250  -102.016 1.00 56.17  ? 320 MET   F N     1 
ATOM   13592 C  CA    . MET   E 4  320 ? -1.776  52.589  -103.299 1.00 56.42  ? 320 MET   F CA    1 
ATOM   13593 C  C     . MET   E 4  320 ? -0.591  53.216  -104.020 1.00 57.01  ? 320 MET   F C     1 
ATOM   13594 O  O     . MET   E 4  320 ? -0.438  54.441  -104.026 1.00 54.53  ? 320 MET   F O     1 
ATOM   13595 C  CB    . MET   E 4  320 ? -3.020  52.711  -104.181 1.00 50.28  ? 320 MET   F CB    1 
ATOM   13596 C  CG    . MET   E 4  320 ? -4.065  51.670  -103.905 1.00 54.42  ? 320 MET   F CG    1 
ATOM   13597 S  SD    . MET   E 4  320 ? -3.323  50.050  -103.594 1.00 69.09  ? 320 MET   F SD    1 
ATOM   13598 C  CE    . MET   E 4  320 ? -2.062  49.964  -104.888 1.00 64.70  ? 320 MET   F CE    1 
ATOM   13599 N  N     . VAL   E 4  321 ? 0.248   52.378  -104.623 1.00 54.88  ? 321 VAL   F N     1 
ATOM   13600 C  CA    . VAL   E 4  321 ? 1.311   52.831  -105.516 1.00 56.23  ? 321 VAL   F CA    1 
ATOM   13601 C  C     . VAL   E 4  321 ? 0.915   52.429  -106.925 1.00 51.57  ? 321 VAL   F C     1 
ATOM   13602 O  O     . VAL   E 4  321 ? 0.619   51.258  -107.171 1.00 62.97  ? 321 VAL   F O     1 
ATOM   13603 C  CB    . VAL   E 4  321 ? 2.674   52.226  -105.138 1.00 62.14  ? 321 VAL   F CB    1 
ATOM   13604 C  CG1   . VAL   E 4  321 ? 3.746   52.725  -106.086 1.00 62.95  ? 321 VAL   F CG1   1 
ATOM   13605 C  CG2   . VAL   E 4  321 ? 3.033   52.560  -103.699 1.00 53.80  ? 321 VAL   F CG2   1 
ATOM   13606 N  N     . ASP   E 4  322 ? 0.894   53.379  -107.848 1.00 55.47  ? 322 ASP   F N     1 
ATOM   13607 C  CA    . ASP   E 4  322 ? 0.346   53.077  -109.166 1.00 53.48  ? 322 ASP   F CA    1 
ATOM   13608 C  C     . ASP   E 4  322 ? 1.457   52.971  -110.215 1.00 54.66  ? 322 ASP   F C     1 
ATOM   13609 O  O     . ASP   E 4  322 ? 2.644   53.143  -109.922 1.00 57.65  ? 322 ASP   F O     1 
ATOM   13610 C  CB    . ASP   E 4  322 ? -0.767  54.089  -109.518 1.00 46.62  ? 322 ASP   F CB    1 
ATOM   13611 C  CG    . ASP   E 4  322 ? -0.370  55.141  -110.543 1.00 59.24  ? 322 ASP   F CG    1 
ATOM   13612 O  OD1   . ASP   E 4  322 ? 0.808   55.565  -110.577 1.00 52.62  ? 322 ASP   F OD1   1 
ATOM   13613 O  OD2   . ASP   E 4  322 ? -1.292  55.575  -111.293 1.00 54.72  ? 322 ASP   F OD2   1 
ATOM   13614 N  N     . GLU   E 4  323 ? 1.058   52.588  -111.434 1.00 63.18  ? 323 GLU   F N     1 
ATOM   13615 C  CA    . GLU   E 4  323 ? 1.998   52.328  -112.528 1.00 57.32  ? 323 GLU   F CA    1 
ATOM   13616 C  C     . GLU   E 4  323 ? 3.134   53.349  -112.578 1.00 61.74  ? 323 GLU   F C     1 
ATOM   13617 O  O     . GLU   E 4  323 ? 4.311   52.977  -112.599 1.00 61.30  ? 323 GLU   F O     1 
ATOM   13618 C  CB    . GLU   E 4  323 ? 1.230   52.322  -113.854 1.00 60.62  ? 323 GLU   F CB    1 
ATOM   13619 C  CG    . GLU   E 4  323 ? 1.668   51.293  -114.895 1.00 69.76  ? 323 GLU   F CG    1 
ATOM   13620 C  CD    . GLU   E 4  323 ? 0.684   51.204  -116.068 1.00 70.67  ? 323 GLU   F CD    1 
ATOM   13621 O  OE1   . GLU   E 4  323 ? 0.303   52.263  -116.624 1.00 68.09  ? 323 GLU   F OE1   1 
ATOM   13622 O  OE2   . GLU   E 4  323 ? 0.275   50.075  -116.420 1.00 63.43  ? 323 GLU   F OE2   1 
ATOM   13623 N  N     . GLU   E 4  324 ? 2.790   54.652  -112.580 1.00 55.77  ? 324 GLU   F N     1 
ATOM   13624 C  CA    . GLU   E 4  324 ? 3.739   55.752  -112.733 1.00 53.46  ? 324 GLU   F CA    1 
ATOM   13625 C  C     . GLU   E 4  324 ? 4.492   56.092  -111.455 1.00 54.95  ? 324 GLU   F C     1 
ATOM   13626 O  O     . GLU   E 4  324 ? 5.069   57.178  -111.364 1.00 58.97  ? 324 GLU   F O     1 
ATOM   13627 C  CB    . GLU   E 4  324 ? 3.022   57.012  -113.223 1.00 54.61  ? 324 GLU   F CB    1 
ATOM   13628 C  CG    . GLU   E 4  324 ? 2.011   56.780  -114.329 1.00 60.70  ? 324 GLU   F CG    1 
ATOM   13629 C  CD    . GLU   E 4  324 ? 2.651   56.355  -115.629 1.00 61.87  ? 324 GLU   F CD    1 
ATOM   13630 O  OE1   . GLU   E 4  324 ? 3.796   56.782  -115.913 1.00 58.28  ? 324 GLU   F OE1   1 
ATOM   13631 O  OE2   . GLU   E 4  324 ? 2.002   55.584  -116.367 1.00 71.19  ? 324 GLU   F OE2   1 
ATOM   13632 N  N     . LEU   E 4  325 ? 4.507   55.219  -110.461 1.00 54.63  ? 325 LEU   F N     1 
ATOM   13633 C  CA    . LEU   E 4  325 ? 5.107   55.529  -109.171 1.00 58.05  ? 325 LEU   F CA    1 
ATOM   13634 C  C     . LEU   E 4  325 ? 4.444   56.734  -108.491 1.00 59.71  ? 325 LEU   F C     1 
ATOM   13635 O  O     . LEU   E 4  325 ? 5.070   57.388  -107.648 1.00 55.65  ? 325 LEU   F O     1 
ATOM   13636 C  CB    . LEU   E 4  325 ? 6.620   55.744  -109.304 1.00 58.02  ? 325 LEU   F CB    1 
ATOM   13637 C  CG    . LEU   E 4  325 ? 7.384   54.430  -109.521 1.00 66.28  ? 325 LEU   F CG    1 
ATOM   13638 C  CD1   . LEU   E 4  325 ? 8.897   54.553  -109.280 1.00 48.74  ? 325 LEU   F CD1   1 
ATOM   13639 C  CD2   . LEU   E 4  325 ? 6.780   53.337  -108.630 1.00 65.15  ? 325 LEU   F CD2   1 
ATOM   13640 N  N     . LYS   E 4  326 ? 3.182   57.032  -108.832 1.00 43.48  ? 326 LYS   F N     1 
ATOM   13641 C  CA    . LYS   E 4  326 ? 2.371   57.973  -108.067 1.00 48.80  ? 326 LYS   F CA    1 
ATOM   13642 C  C     . LYS   E 4  326 ? 1.658   57.279  -106.903 1.00 57.89  ? 326 LYS   F C     1 
ATOM   13643 O  O     . LYS   E 4  326 ? 1.050   56.214  -107.074 1.00 54.62  ? 326 LYS   F O     1 
ATOM   13644 C  CB    . LYS   E 4  326 ? 1.343   58.650  -108.960 1.00 49.78  ? 326 LYS   F CB    1 
ATOM   13645 C  CG    . LYS   E 4  326 ? 0.364   59.491  -108.179 1.00 47.08  ? 326 LYS   F CG    1 
ATOM   13646 C  CD    . LYS   E 4  326 ? -0.672  60.083  -109.117 1.00 57.85  ? 326 LYS   F CD    1 
ATOM   13647 C  CE    . LYS   E 4  326 ? -1.489  61.192  -108.467 1.00 50.31  ? 326 LYS   F CE    1 
ATOM   13648 N  NZ    . LYS   E 4  326 ? -2.345  61.873  -109.481 1.00 59.87  ? 326 LYS   F NZ    1 
ATOM   13649 N  N     . VAL   E 4  327 ? 1.717   57.900  -105.718 1.00 59.87  ? 327 VAL   F N     1 
ATOM   13650 C  CA    . VAL   E 4  327 ? 1.122   57.350  -104.504 1.00 49.69  ? 327 VAL   F CA    1 
ATOM   13651 C  C     . VAL   E 4  327 ? -0.294  57.893  -104.330 1.00 50.29  ? 327 VAL   F C     1 
ATOM   13652 O  O     . VAL   E 4  327 ? -0.573  59.067  -104.593 1.00 51.45  ? 327 VAL   F O     1 
ATOM   13653 C  CB    . VAL   E 4  327 ? 2.003   57.661  -103.279 1.00 53.14  ? 327 VAL   F CB    1 
ATOM   13654 C  CG1   . VAL   E 4  327 ? 1.302   57.270  -101.993 1.00 52.23  ? 327 VAL   F CG1   1 
ATOM   13655 C  CG2   . VAL   E 4  327 ? 3.339   56.933  -103.382 1.00 57.56  ? 327 VAL   F CG2   1 
ATOM   13656 N  N     . TRP   E 4  328 ? -1.200  57.023  -103.893 1.00 57.43  ? 328 TRP   F N     1 
ATOM   13657 C  CA    . TRP   E 4  328 ? -2.588  57.372  -103.631 1.00 47.79  ? 328 TRP   F CA    1 
ATOM   13658 C  C     . TRP   E 4  328 ? -2.960  56.943  -102.219 1.00 47.84  ? 328 TRP   F C     1 
ATOM   13659 O  O     . TRP   E 4  328 ? -2.450  55.946  -101.707 1.00 51.04  ? 328 TRP   F O     1 
ATOM   13660 C  CB    . TRP   E 4  328 ? -3.518  56.702  -104.633 1.00 53.53  ? 328 TRP   F CB    1 
ATOM   13661 C  CG    . TRP   E 4  328 ? -3.264  57.096  -106.039 1.00 47.41  ? 328 TRP   F CG    1 
ATOM   13662 C  CD1   . TRP   E 4  328 ? -2.326  56.575  -106.889 1.00 46.91  ? 328 TRP   F CD1   1 
ATOM   13663 C  CD2   . TRP   E 4  328 ? -3.968  58.095  -106.776 1.00 45.95  ? 328 TRP   F CD2   1 
ATOM   13664 N  NE1   . TRP   E 4  328 ? -2.409  57.192  -108.117 1.00 49.87  ? 328 TRP   F NE1   1 
ATOM   13665 C  CE2   . TRP   E 4  328 ? -3.404  58.135  -108.070 1.00 50.39  ? 328 TRP   F CE2   1 
ATOM   13666 C  CE3   . TRP   E 4  328 ? -5.017  58.968  -106.466 1.00 41.20  ? 328 TRP   F CE3   1 
ATOM   13667 C  CZ2   . TRP   E 4  328 ? -3.855  59.010  -109.050 1.00 46.59  ? 328 TRP   F CZ2   1 
ATOM   13668 C  CZ3   . TRP   E 4  328 ? -5.461  59.838  -107.431 1.00 46.63  ? 328 TRP   F CZ3   1 
ATOM   13669 C  CH2   . TRP   E 4  328 ? -4.886  59.847  -108.717 1.00 51.75  ? 328 TRP   F CH2   1 
ATOM   13670 N  N     . LEU   E 4  329 ? -3.847  57.711  -101.589 1.00 58.19  ? 329 LEU   F N     1 
ATOM   13671 C  CA    . LEU   E 4  329 ? -4.352  57.403  -100.254 1.00 55.14  ? 329 LEU   F CA    1 
ATOM   13672 C  C     . LEU   E 4  329 ? -5.677  56.659  -100.367 1.00 46.12  ? 329 LEU   F C     1 
ATOM   13673 O  O     . LEU   E 4  329 ? -6.514  56.991  -101.210 1.00 50.24  ? 329 LEU   F O     1 
ATOM   13674 C  CB    . LEU   E 4  329 ? -4.531  58.681  -99.426  1.00 54.39  ? 329 LEU   F CB    1 
ATOM   13675 C  CG    . LEU   E 4  329 ? -5.120  58.574  -98.005  1.00 48.74  ? 329 LEU   F CG    1 
ATOM   13676 C  CD1   . LEU   E 4  329 ? -4.143  57.953  -97.008  1.00 41.78  ? 329 LEU   F CD1   1 
ATOM   13677 C  CD2   . LEU   E 4  329 ? -5.609  59.934  -97.517  1.00 44.26  ? 329 LEU   F CD2   1 
ATOM   13678 N  N     . ILE   E 4  330 ? -5.868  55.653  -99.512  1.00 59.36  ? 330 ILE   F N     1 
ATOM   13679 C  CA    . ILE   E 4  330 ? -7.044  54.785  -99.595  1.00 62.31  ? 330 ILE   F CA    1 
ATOM   13680 C  C     . ILE   E 4  330 ? -7.956  54.953  -98.383  1.00 58.23  ? 330 ILE   F C     1 
ATOM   13681 O  O     . ILE   E 4  330 ? -9.027  55.561  -98.484  1.00 61.67  ? 330 ILE   F O     1 
ATOM   13682 C  CB    . ILE   E 4  330 ? -6.623  53.314  -99.757  1.00 59.24  ? 330 ILE   F CB    1 
ATOM   13683 C  CG1   . ILE   E 4  330 ? -5.951  53.122  -101.116 1.00 51.87  ? 330 ILE   F CG1   1 
ATOM   13684 C  CG2   . ILE   E 4  330 ? -7.826  52.408  -99.602  1.00 52.06  ? 330 ILE   F CG2   1 
ATOM   13685 C  CD1   . ILE   E 4  330 ? -6.726  53.754  -102.253 1.00 50.32  ? 330 ILE   F CD1   1 
ATOM   13686 N  N     . GLU   E 4  331 ? -7.562  54.375  -97.247  1.00 57.95  ? 331 GLU   F N     1 
ATOM   13687 C  CA    . GLU   E 4  331 ? -8.265  54.550  -95.982  1.00 60.11  ? 331 GLU   F CA    1 
ATOM   13688 C  C     . GLU   E 4  331 ? -7.247  54.980  -94.933  1.00 59.39  ? 331 GLU   F C     1 
ATOM   13689 O  O     . GLU   E 4  331 ? -6.032  54.819  -95.115  1.00 54.23  ? 331 GLU   F O     1 
ATOM   13690 C  CB    . GLU   E 4  331 ? -9.044  53.261  -95.532  1.00 61.05  ? 331 GLU   F CB    1 
ATOM   13691 C  CG    . GLU   E 4  331 ? -8.215  52.021  -95.055  1.00 62.85  ? 331 GLU   F CG    1 
ATOM   13692 C  CD    . GLU   E 4  331 ? -9.089  50.804  -94.597  1.00 90.20  ? 331 GLU   F CD    1 
ATOM   13693 O  OE1   . GLU   E 4  331 ? -9.890  50.938  -93.634  1.00 75.57  ? 331 GLU   F OE1   1 
ATOM   13694 O  OE2   . GLU   E 4  331 ? -8.970  49.702  -95.198  1.00 102.20 ? 331 GLU   F OE2   1 
ATOM   13695 N  N     . VAL   E 4  332 ? -7.752  55.583  -93.854  1.00 56.59  ? 332 VAL   F N     1 
ATOM   13696 C  CA    . VAL   E 4  332 ? -6.968  55.857  -92.648  1.00 54.27  ? 332 VAL   F CA    1 
ATOM   13697 C  C     . VAL   E 4  332 ? -7.722  55.243  -91.479  1.00 47.34  ? 332 VAL   F C     1 
ATOM   13698 O  O     . VAL   E 4  332 ? -8.876  55.601  -91.229  1.00 48.06  ? 332 VAL   F O     1 
ATOM   13699 C  CB    . VAL   E 4  332 ? -6.735  57.361  -92.414  1.00 42.71  ? 332 VAL   F CB    1 
ATOM   13700 C  CG1   . VAL   E 4  332 ? -5.827  57.567  -91.245  1.00 41.88  ? 332 VAL   F CG1   1 
ATOM   13701 C  CG2   . VAL   E 4  332 ? -6.125  57.994  -93.635  1.00 52.82  ? 332 VAL   F CG2   1 
ATOM   13702 N  N     . ASN   E 4  333 ? -7.081  54.320  -90.773  1.00 47.15  ? 333 ASN   F N     1 
ATOM   13703 C  CA    . ASN   E 4  333 ? -7.734  53.560  -89.720  1.00 52.05  ? 333 ASN   F CA    1 
ATOM   13704 C  C     . ASN   E 4  333 ? -7.276  54.085  -88.371  1.00 49.02  ? 333 ASN   F C     1 
ATOM   13705 O  O     . ASN   E 4  333 ? -6.070  54.186  -88.123  1.00 47.70  ? 333 ASN   F O     1 
ATOM   13706 C  CB    . ASN   E 4  333 ? -7.420  52.065  -89.842  1.00 64.76  ? 333 ASN   F CB    1 
ATOM   13707 C  CG    . ASN   E 4  333 ? -7.687  51.522  -91.238  1.00 69.68  ? 333 ASN   F CG    1 
ATOM   13708 O  OD1   . ASN   E 4  333 ? -6.893  51.747  -92.156  1.00 64.17  ? 333 ASN   F OD1   1 
ATOM   13709 N  ND2   . ASN   E 4  333 ? -8.805  50.797  -91.405  1.00 72.64  ? 333 ASN   F ND2   1 
ATOM   13710 N  N     . GLY   E 4  334 ? -8.240  54.400  -87.497  1.00 44.64  ? 334 GLY   F N     1 
ATOM   13711 C  CA    . GLY   E 4  334 ? -7.942  54.981  -86.204  1.00 36.12  ? 334 GLY   F CA    1 
ATOM   13712 C  C     . GLY   E 4  334 ? -7.514  53.996  -85.146  1.00 41.43  ? 334 GLY   F C     1 
ATOM   13713 O  O     . GLY   E 4  334 ? -6.984  54.402  -84.104  1.00 44.58  ? 334 GLY   F O     1 
ATOM   13714 N  N     . ALA   E 4  335 ? -7.731  52.702  -85.384  1.00 43.55  ? 335 ALA   F N     1 
ATOM   13715 C  CA    . ALA   E 4  335 ? -7.390  51.664  -84.410  1.00 45.99  ? 335 ALA   F CA    1 
ATOM   13716 C  C     . ALA   E 4  335 ? -6.521  50.600  -85.068  1.00 42.12  ? 335 ALA   F C     1 
ATOM   13717 O  O     . ALA   E 4  335 ? -6.808  49.407  -84.988  1.00 45.00  ? 335 ALA   F O     1 
ATOM   13718 C  CB    . ALA   E 4  335 ? -8.649  51.049  -83.798  1.00 38.22  ? 335 ALA   F CB    1 
ATOM   13719 N  N     . PRO   E 4  336 ? -5.435  51.001  -85.720  1.00 51.54  ? 336 PRO   F N     1 
ATOM   13720 C  CA    . PRO   E 4  336 ? -4.630  50.028  -86.468  1.00 56.70  ? 336 PRO   F CA    1 
ATOM   13721 C  C     . PRO   E 4  336 ? -4.119  48.922  -85.562  1.00 51.30  ? 336 PRO   F C     1 
ATOM   13722 O  O     . PRO   E 4  336 ? -3.875  49.131  -84.373  1.00 49.88  ? 336 PRO   F O     1 
ATOM   13723 C  CB    . PRO   E 4  336 ? -3.472  50.870  -87.009  1.00 51.03  ? 336 PRO   F CB    1 
ATOM   13724 C  CG    . PRO   E 4  336 ? -3.329  51.974  -85.975  1.00 48.79  ? 336 PRO   F CG    1 
ATOM   13725 C  CD    . PRO   E 4  336 ? -4.756  52.304  -85.606  1.00 49.44  ? 336 PRO   F CD    1 
ATOM   13726 N  N     . ALA   E 4  337 ? -3.982  47.732  -86.136  1.00 58.35  ? 337 ALA   F N     1 
ATOM   13727 C  CA    . ALA   E 4  337 ? -3.178  46.663  -85.561  1.00 57.59  ? 337 ALA   F CA    1 
ATOM   13728 C  C     . ALA   E 4  337 ? -1.822  46.669  -86.248  1.00 60.37  ? 337 ALA   F C     1 
ATOM   13729 O  O     . ALA   E 4  337 ? -1.670  47.201  -87.353  1.00 61.68  ? 337 ALA   F O     1 
ATOM   13730 C  CB    . ALA   E 4  337 ? -3.854  45.300  -85.728  1.00 42.21  ? 337 ALA   F CB    1 
ATOM   13731 N  N     . CYS   E 4  338 ? -0.830  46.079  -85.590  1.00 50.92  ? 338 CYS   F N     1 
ATOM   13732 C  CA    . CYS   E 4  338 ? 0.510   46.077  -86.155  1.00 53.95  ? 338 CYS   F CA    1 
ATOM   13733 C  C     . CYS   E 4  338 ? 0.814   44.729  -86.808  1.00 61.22  ? 338 CYS   F C     1 
ATOM   13734 O  O     . CYS   E 4  338 ? 0.014   43.791  -86.773  1.00 67.37  ? 338 CYS   F O     1 
ATOM   13735 C  CB    . CYS   E 4  338 ? 1.539   46.422  -85.085  1.00 51.66  ? 338 CYS   F CB    1 
ATOM   13736 S  SG    . CYS   E 4  338 ? 3.112   46.893  -85.767  1.00 58.66  ? 338 CYS   F SG    1 
ATOM   13737 N  N     . ALA   E 4  339 ? 1.985   44.636  -87.431  1.00 57.18  ? 339 ALA   F N     1 
ATOM   13738 C  CA    . ALA   E 4  339 ? 2.459   43.371  -87.964  1.00 52.70  ? 339 ALA   F CA    1 
ATOM   13739 C  C     . ALA   E 4  339 ? 3.250   42.649  -86.888  1.00 62.94  ? 339 ALA   F C     1 
ATOM   13740 O  O     . ALA   E 4  339 ? 3.939   43.284  -86.085  1.00 70.47  ? 339 ALA   F O     1 
ATOM   13741 C  CB    . ALA   E 4  339 ? 3.323   43.590  -89.202  1.00 57.10  ? 339 ALA   F CB    1 
ATOM   13742 N  N     . GLN   E 4  340 ? 3.148   41.317  -86.869  1.00 60.41  ? 340 GLN   F N     1 
ATOM   13743 C  CA    . GLN   E 4  340 ? 3.770   40.560  -85.789  1.00 63.45  ? 340 GLN   F CA    1 
ATOM   13744 C  C     . GLN   E 4  340 ? 5.244   40.919  -85.649  1.00 64.35  ? 340 GLN   F C     1 
ATOM   13745 O  O     . GLN   E 4  340 ? 5.725   41.205  -84.547  1.00 63.01  ? 340 GLN   F O     1 
ATOM   13746 C  CB    . GLN   E 4  340 ? 3.593   39.057  -86.011  1.00 60.54  ? 340 GLN   F CB    1 
ATOM   13747 C  CG    . GLN   E 4  340 ? 3.451   38.247  -84.709  1.00 60.78  ? 340 GLN   F CG    1 
ATOM   13748 C  CD    . GLN   E 4  340 ? 4.748   38.189  -83.895  1.00 83.39  ? 340 GLN   F CD    1 
ATOM   13749 O  OE1   . GLN   E 4  340 ? 5.826   37.920  -84.438  1.00 85.87  ? 340 GLN   F OE1   1 
ATOM   13750 N  NE2   . GLN   E 4  340 ? 4.647   38.445  -82.587  1.00 78.75  ? 340 GLN   F NE2   1 
ATOM   13751 N  N     . LYS   E 4  341 ? 5.972   40.940  -86.768  1.00 65.63  ? 341 LYS   F N     1 
ATOM   13752 C  CA    . LYS   E 4  341 ? 7.402   41.222  -86.706  1.00 67.29  ? 341 LYS   F CA    1 
ATOM   13753 C  C     . LYS   E 4  341 ? 7.697   42.525  -85.970  1.00 65.29  ? 341 LYS   F C     1 
ATOM   13754 O  O     . LYS   E 4  341 ? 8.765   42.661  -85.354  1.00 51.38  ? 341 LYS   F O     1 
ATOM   13755 C  CB    . LYS   E 4  341 ? 7.996   41.266  -88.124  1.00 67.32  ? 341 LYS   F CB    1 
ATOM   13756 C  CG    . LYS   E 4  341 ? 9.539   41.248  -88.161  1.00 68.69  ? 341 LYS   F CG    1 
ATOM   13757 C  CD    . LYS   E 4  341 ? 10.129  41.830  -89.457  1.00 66.63  ? 341 LYS   F CD    1 
ATOM   13758 C  CE    . LYS   E 4  341 ? 11.665  41.864  -89.397  1.00 73.64  ? 341 LYS   F CE    1 
ATOM   13759 N  NZ    . LYS   E 4  341 ? 12.272  43.018  -90.128  1.00 58.78  ? 341 LYS   F NZ    1 
ATOM   13760 N  N     . LEU   E 4  342 ? 6.760   43.486  -86.002  1.00 64.93  ? 342 LEU   F N     1 
ATOM   13761 C  CA    . LEU   E 4  342 ? 7.050   44.868  -85.627  1.00 71.16  ? 342 LEU   F CA    1 
ATOM   13762 C  C     . LEU   E 4  342 ? 6.431   45.319  -84.306  1.00 65.74  ? 342 LEU   F C     1 
ATOM   13763 O  O     . LEU   E 4  342 ? 6.783   46.405  -83.831  1.00 66.27  ? 342 LEU   F O     1 
ATOM   13764 C  CB    . LEU   E 4  342 ? 6.610   45.822  -86.757  1.00 65.59  ? 342 LEU   F CB    1 
ATOM   13765 C  CG    . LEU   E 4  342 ? 7.426   45.692  -88.064  1.00 68.29  ? 342 LEU   F CG    1 
ATOM   13766 C  CD1   . LEU   E 4  342 ? 6.904   46.537  -89.233  1.00 42.14  ? 342 LEU   F CD1   1 
ATOM   13767 C  CD2   . LEU   E 4  342 ? 8.889   46.011  -87.804  1.00 65.73  ? 342 LEU   F CD2   1 
ATOM   13768 N  N     . TYR   E 4  343 ? 5.555   44.516  -83.688  1.00 70.93  ? 343 TYR   F N     1 
ATOM   13769 C  CA    . TYR   E 4  343 ? 4.888   44.902  -82.438  1.00 64.34  ? 343 TYR   F CA    1 
ATOM   13770 C  C     . TYR   E 4  343 ? 5.880   45.372  -81.378  1.00 50.92  ? 343 TYR   F C     1 
ATOM   13771 O  O     . TYR   E 4  343 ? 5.759   46.474  -80.837  1.00 58.69  ? 343 TYR   F O     1 
ATOM   13772 C  CB    . TYR   E 4  343 ? 4.060   43.731  -81.887  1.00 50.39  ? 343 TYR   F CB    1 
ATOM   13773 C  CG    . TYR   E 4  343 ? 2.636   43.706  -82.378  1.00 59.97  ? 343 TYR   F CG    1 
ATOM   13774 C  CD1   . TYR   E 4  343 ? 1.649   44.440  -81.742  1.00 62.41  ? 343 TYR   F CD1   1 
ATOM   13775 C  CD2   . TYR   E 4  343 ? 2.273   42.952  -83.486  1.00 63.09  ? 343 TYR   F CD2   1 
ATOM   13776 C  CE1   . TYR   E 4  343 ? 0.329   44.422  -82.197  1.00 59.37  ? 343 TYR   F CE1   1 
ATOM   13777 C  CE2   . TYR   E 4  343 ? 0.960   42.920  -83.942  1.00 60.61  ? 343 TYR   F CE2   1 
ATOM   13778 C  CZ    . TYR   E 4  343 ? -0.013  43.656  -83.296  1.00 57.80  ? 343 TYR   F CZ    1 
ATOM   13779 O  OH    . TYR   E 4  343 ? -1.325  43.629  -83.754  1.00 61.49  ? 343 TYR   F OH    1 
ATOM   13780 N  N     . ALA   E 4  344 ? 6.835   44.515  -81.028  1.00 50.33  ? 344 ALA   F N     1 
ATOM   13781 C  CA    . ALA   E 4  344 ? 7.846   44.863  -80.039  1.00 51.64  ? 344 ALA   F CA    1 
ATOM   13782 C  C     . ALA   E 4  344 ? 8.354   46.286  -80.215  1.00 57.14  ? 344 ALA   F C     1 
ATOM   13783 O  O     . ALA   E 4  344 ? 8.326   47.089  -79.275  1.00 49.96  ? 344 ALA   F O     1 
ATOM   13784 C  CB    . ALA   E 4  344 ? 9.012   43.876  -80.128  1.00 37.23  ? 344 ALA   F CB    1 
ATOM   13785 N  N     . GLU   E 4  345 ? 8.818   46.620  -81.423  1.00 58.28  ? 345 GLU   F N     1 
ATOM   13786 C  CA    . GLU   E 4  345 ? 9.488   47.901  -81.609  1.00 62.96  ? 345 GLU   F CA    1 
ATOM   13787 C  C     . GLU   E 4  345 ? 8.491   49.052  -81.564  1.00 61.32  ? 345 GLU   F C     1 
ATOM   13788 O  O     . GLU   E 4  345 ? 8.707   50.041  -80.853  1.00 56.56  ? 345 GLU   F O     1 
ATOM   13789 C  CB    . GLU   E 4  345 ? 10.281  47.914  -82.920  1.00 62.96  ? 345 GLU   F CB    1 
ATOM   13790 C  CG    . GLU   E 4  345 ? 11.561  48.750  -82.842  1.00 62.68  ? 345 GLU   F CG    1 
ATOM   13791 C  CD    . GLU   E 4  345 ? 12.215  48.994  -84.194  1.00 64.59  ? 345 GLU   F CD    1 
ATOM   13792 O  OE1   . GLU   E 4  345 ? 11.598  48.701  -85.235  1.00 63.24  ? 345 GLU   F OE1   1 
ATOM   13793 O  OE2   . GLU   E 4  345 ? 13.353  49.496  -84.216  1.00 63.91  ? 345 GLU   F OE2   1 
ATOM   13794 N  N     . LEU   E 4  346 ? 7.387   48.939  -82.313  1.00 57.23  ? 346 LEU   F N     1 
ATOM   13795 C  CA    . LEU   E 4  346 ? 6.411   50.024  -82.351  1.00 56.22  ? 346 LEU   F CA    1 
ATOM   13796 C  C     . LEU   E 4  346 ? 5.845   50.295  -80.966  1.00 57.47  ? 346 LEU   F C     1 
ATOM   13797 O  O     . LEU   E 4  346 ? 5.797   51.444  -80.513  1.00 56.67  ? 346 LEU   F O     1 
ATOM   13798 C  CB    . LEU   E 4  346 ? 5.280   49.706  -83.324  1.00 53.23  ? 346 LEU   F CB    1 
ATOM   13799 C  CG    . LEU   E 4  346 ? 4.307   50.886  -83.427  1.00 55.64  ? 346 LEU   F CG    1 
ATOM   13800 C  CD1   . LEU   E 4  346 ? 5.078   52.165  -83.690  1.00 48.22  ? 346 LEU   F CD1   1 
ATOM   13801 C  CD2   . LEU   E 4  346 ? 3.249   50.675  -84.507  1.00 55.89  ? 346 LEU   F CD2   1 
ATOM   13802 N  N     . CYS   E 4  347 ? 5.411   49.243  -80.275  1.00 56.00  ? 347 CYS   F N     1 
ATOM   13803 C  CA    . CYS   E 4  347 ? 4.775   49.436  -78.983  1.00 47.99  ? 347 CYS   F CA    1 
ATOM   13804 C  C     . CYS   E 4  347 ? 5.755   49.991  -77.959  1.00 54.56  ? 347 CYS   F C     1 
ATOM   13805 O  O     . CYS   E 4  347 ? 5.348   50.728  -77.053  1.00 61.33  ? 347 CYS   F O     1 
ATOM   13806 C  CB    . CYS   E 4  347 ? 4.155   48.118  -78.515  1.00 60.56  ? 347 CYS   F CB    1 
ATOM   13807 S  SG    . CYS   E 4  347 ? 2.867   47.434  -79.649  1.00 55.32  ? 347 CYS   F SG    1 
ATOM   13808 N  N     . GLN   E 4  348 ? 7.046   49.675  -78.088  1.00 55.79  ? 348 GLN   F N     1 
ATOM   13809 C  CA    . GLN   E 4  348 ? 8.030   50.335  -77.236  1.00 54.50  ? 348 GLN   F CA    1 
ATOM   13810 C  C     . GLN   E 4  348 ? 8.209   51.790  -77.627  1.00 55.32  ? 348 GLN   F C     1 
ATOM   13811 O  O     . GLN   E 4  348 ? 8.500   52.629  -76.768  1.00 56.52  ? 348 GLN   F O     1 
ATOM   13812 C  CB    . GLN   E 4  348 ? 9.385   49.638  -77.296  1.00 53.96  ? 348 GLN   F CB    1 
ATOM   13813 C  CG    . GLN   E 4  348 ? 10.400  50.308  -76.380  1.00 52.71  ? 348 GLN   F CG    1 
ATOM   13814 C  CD    . GLN   E 4  348 ? 10.003  50.177  -74.916  1.00 63.92  ? 348 GLN   F CD    1 
ATOM   13815 O  OE1   . GLN   E 4  348 ? 9.205   49.309  -74.564  1.00 70.46  ? 348 GLN   F OE1   1 
ATOM   13816 N  NE2   . GLN   E 4  348 ? 10.548  51.036  -74.061  1.00 56.07  ? 348 GLN   F NE2   1 
ATOM   13817 N  N     . GLY   E 4  349 ? 8.063   52.102  -78.917  1.00 55.84  ? 349 GLY   F N     1 
ATOM   13818 C  CA    . GLY   E 4  349 ? 8.137   53.489  -79.349  1.00 52.61  ? 349 GLY   F CA    1 
ATOM   13819 C  C     . GLY   E 4  349 ? 6.941   54.298  -78.886  1.00 58.68  ? 349 GLY   F C     1 
ATOM   13820 O  O     . GLY   E 4  349 ? 7.086   55.450  -78.465  1.00 56.02  ? 349 GLY   F O     1 
ATOM   13821 N  N     . ILE   E 4  350 ? 5.739   53.711  -78.963  1.00 58.40  ? 350 ILE   F N     1 
ATOM   13822 C  CA    . ILE   E 4  350 ? 4.558   54.340  -78.371  1.00 61.68  ? 350 ILE   F CA    1 
ATOM   13823 C  C     . ILE   E 4  350 ? 4.845   54.729  -76.925  1.00 53.35  ? 350 ILE   F C     1 
ATOM   13824 O  O     . ILE   E 4  350 ? 4.545   55.847  -76.487  1.00 42.18  ? 350 ILE   F O     1 
ATOM   13825 C  CB    . ILE   E 4  350 ? 3.342   53.399  -78.472  1.00 57.13  ? 350 ILE   F CB    1 
ATOM   13826 C  CG1   . ILE   E 4  350 ? 3.028   53.091  -79.934  1.00 46.11  ? 350 ILE   F CG1   1 
ATOM   13827 C  CG2   . ILE   E 4  350 ? 2.129   53.989  -77.735  1.00 51.30  ? 350 ILE   F CG2   1 
ATOM   13828 C  CD1   . ILE   E 4  350 ? 2.033   51.964  -80.122  1.00 49.93  ? 350 ILE   F CD1   1 
ATOM   13829 N  N     . VAL   E 4  351 ? 5.452   53.810  -76.171  1.00 56.15  ? 351 VAL   F N     1 
ATOM   13830 C  CA    . VAL   E 4  351 ? 5.667   54.031  -74.747  1.00 51.63  ? 351 VAL   F CA    1 
ATOM   13831 C  C     . VAL   E 4  351 ? 6.653   55.159  -74.519  1.00 56.27  ? 351 VAL   F C     1 
ATOM   13832 O  O     . VAL   E 4  351 ? 6.517   55.941  -73.570  1.00 60.38  ? 351 VAL   F O     1 
ATOM   13833 C  CB    . VAL   E 4  351 ? 6.150   52.740  -74.079  1.00 47.57  ? 351 VAL   F CB    1 
ATOM   13834 C  CG1   . VAL   E 4  351 ? 6.809   53.090  -72.766  1.00 51.02  ? 351 VAL   F CG1   1 
ATOM   13835 C  CG2   . VAL   E 4  351 ? 4.977   51.782  -73.886  1.00 52.75  ? 351 VAL   F CG2   1 
ATOM   13836 N  N     . ASP   E 4  352 ? 7.667   55.256  -75.374  1.00 55.15  ? 352 ASP   F N     1 
ATOM   13837 C  CA    . ASP   E 4  352 ? 8.746   56.209  -75.171  1.00 55.66  ? 352 ASP   F CA    1 
ATOM   13838 C  C     . ASP   E 4  352 ? 8.441   57.582  -75.750  1.00 54.59  ? 352 ASP   F C     1 
ATOM   13839 O  O     . ASP   E 4  352 ? 8.857   58.595  -75.173  1.00 62.82  ? 352 ASP   F O     1 
ATOM   13840 C  CB    . ASP   E 4  352 ? 10.045  55.655  -75.771  1.00 56.04  ? 352 ASP   F CB    1 
ATOM   13841 C  CG    . ASP   E 4  352 ? 10.500  54.366  -75.086  1.00 66.15  ? 352 ASP   F CG    1 
ATOM   13842 O  OD1   . ASP   E 4  352 ? 10.413  54.307  -73.835  1.00 72.76  ? 352 ASP   F OD1   1 
ATOM   13843 O  OD2   . ASP   E 4  352 ? 10.917  53.411  -75.790  1.00 60.25  ? 352 ASP   F OD2   1 
ATOM   13844 N  N     . VAL   E 4  353 ? 7.721   57.653  -76.859  1.00 49.34  ? 353 VAL   F N     1 
ATOM   13845 C  CA    A VAL   E 4  353 ? 7.422   58.932  -77.488  0.82 48.58  ? 353 VAL   F CA    1 
ATOM   13846 C  CA    B VAL   E 4  353 ? 7.422   58.935  -77.486  0.18 48.63  ? 353 VAL   F CA    1 
ATOM   13847 C  C     . VAL   E 4  353 ? 6.188   59.585  -76.872  1.00 52.50  ? 353 VAL   F C     1 
ATOM   13848 O  O     . VAL   E 4  353 ? 6.213   60.770  -76.511  1.00 45.60  ? 353 VAL   F O     1 
ATOM   13849 C  CB    A VAL   E 4  353 ? 7.255   58.742  -79.011  0.82 46.90  ? 353 VAL   F CB    1 
ATOM   13850 C  CB    B VAL   E 4  353 ? 7.260   58.750  -79.009  0.18 47.01  ? 353 VAL   F CB    1 
ATOM   13851 C  CG1   A VAL   E 4  353 ? 7.025   60.076  -79.684  0.82 49.24  ? 353 VAL   F CG1   1 
ATOM   13852 C  CG1   B VAL   E 4  353 ? 6.984   60.086  -79.674  0.18 49.16  ? 353 VAL   F CG1   1 
ATOM   13853 C  CG2   A VAL   E 4  353 ? 8.463   58.045  -79.594  0.82 47.75  ? 353 VAL   F CG2   1 
ATOM   13854 C  CG2   B VAL   E 4  353 ? 8.499   58.099  -79.596  0.18 47.81  ? 353 VAL   F CG2   1 
ATOM   13855 N  N     . ALA   E 4  354 ? 5.103   58.807  -76.723  1.00 40.92  ? 354 ALA   F N     1 
ATOM   13856 C  CA    . ALA   E 4  354 ? 3.785   59.327  -76.386  1.00 38.91  ? 354 ALA   F CA    1 
ATOM   13857 C  C     . ALA   E 4  354 ? 3.320   59.093  -74.950  1.00 48.21  ? 354 ALA   F C     1 
ATOM   13858 O  O     . ALA   E 4  354 ? 2.307   59.675  -74.551  1.00 42.38  ? 354 ALA   F O     1 
ATOM   13859 C  CB    . ALA   E 4  354 ? 2.739   58.734  -77.337  1.00 39.22  ? 354 ALA   F CB    1 
ATOM   13860 N  N     . ILE   E 4  355 ? 4.002   58.270  -74.155  1.00 47.03  ? 355 ILE   F N     1 
ATOM   13861 C  CA    . ILE   E 4  355 ? 3.597   58.038  -72.776  1.00 48.90  ? 355 ILE   F CA    1 
ATOM   13862 C  C     . ILE   E 4  355 ? 4.665   58.482  -71.780  1.00 53.57  ? 355 ILE   F C     1 
ATOM   13863 O  O     . ILE   E 4  355 ? 4.347   59.086  -70.744  1.00 42.12  ? 355 ILE   F O     1 
ATOM   13864 C  CB    . ILE   E 4  355 ? 3.214   56.560  -72.552  1.00 46.12  ? 355 ILE   F CB    1 
ATOM   13865 C  CG1   . ILE   E 4  355 ? 2.029   56.198  -73.443  1.00 40.63  ? 355 ILE   F CG1   1 
ATOM   13866 C  CG2   . ILE   E 4  355 ? 2.887   56.303  -71.081  1.00 44.78  ? 355 ILE   F CG2   1 
ATOM   13867 C  CD1   . ILE   E 4  355 ? 1.734   54.720  -73.507  1.00 45.82  ? 355 ILE   F CD1   1 
ATOM   13868 N  N     . SER   E 4  356 ? 5.938   58.213  -72.071  1.00 58.58  ? 356 SER   F N     1 
ATOM   13869 C  CA    . SER   E 4  356 ? 6.993   58.666  -71.173  1.00 59.26  ? 356 SER   F CA    1 
ATOM   13870 C  C     . SER   E 4  356 ? 7.392   60.109  -71.428  1.00 50.65  ? 356 SER   F C     1 
ATOM   13871 O  O     . SER   E 4  356 ? 8.083   60.702  -70.592  1.00 46.74  ? 356 SER   F O     1 
ATOM   13872 C  CB    . SER   E 4  356 ? 8.214   57.753  -71.281  1.00 55.95  ? 356 SER   F CB    1 
ATOM   13873 O  OG    . SER   E 4  356 ? 7.987   56.549  -70.579  1.00 48.07  ? 356 SER   F OG    1 
ATOM   13874 N  N     . SER   E 4  357 ? 6.971   60.684  -72.557  1.00 52.06  ? 357 SER   F N     1 
ATOM   13875 C  CA    . SER   E 4  357 ? 7.139   62.117  -72.764  1.00 42.59  ? 357 SER   F CA    1 
ATOM   13876 C  C     . SER   E 4  357 ? 6.342   62.903  -71.737  1.00 44.00  ? 357 SER   F C     1 
ATOM   13877 O  O     . SER   E 4  357 ? 6.813   63.921  -71.221  1.00 42.34  ? 357 SER   F O     1 
ATOM   13878 C  CB    . SER   E 4  357 ? 6.711   62.490  -74.184  1.00 48.38  ? 357 SER   F CB    1 
ATOM   13879 O  OG    . SER   E 4  357 ? 5.373   62.084  -74.442  1.00 49.93  ? 357 SER   F OG    1 
ATOM   13880 N  N     . VAL   E 4  358 ? 5.130   62.438  -71.431  1.00 46.52  ? 358 VAL   F N     1 
ATOM   13881 C  CA    . VAL   E 4  358 ? 4.270   63.082  -70.445  1.00 42.86  ? 358 VAL   F CA    1 
ATOM   13882 C  C     . VAL   E 4  358 ? 4.509   62.539  -69.040  1.00 44.62  ? 358 VAL   F C     1 
ATOM   13883 O  O     . VAL   E 4  358 ? 4.369   63.275  -68.059  1.00 43.01  ? 358 VAL   F O     1 
ATOM   13884 C  CB    . VAL   E 4  358 ? 2.791   62.922  -70.856  1.00 39.40  ? 358 VAL   F CB    1 
ATOM   13885 C  CG1   . VAL   E 4  358 ? 1.862   63.121  -69.669  1.00 27.64  ? 358 VAL   F CG1   1 
ATOM   13886 C  CG2   . VAL   E 4  358 ? 2.451   63.896  -71.944  1.00 40.35  ? 358 VAL   F CG2   1 
ATOM   13887 N  N     . PHE   E 4  359 ? 4.845   61.256  -68.910  1.00 53.94  ? 359 PHE   F N     1 
ATOM   13888 C  CA    . PHE   E 4  359 ? 5.051   60.620  -67.613  1.00 50.37  ? 359 PHE   F CA    1 
ATOM   13889 C  C     . PHE   E 4  359 ? 6.472   60.075  -67.613  1.00 57.36  ? 359 PHE   F C     1 
ATOM   13890 O  O     . PHE   E 4  359 ? 6.701   58.900  -67.952  1.00 64.05  ? 359 PHE   F O     1 
ATOM   13891 C  CB    . PHE   E 4  359 ? 3.997   59.548  -67.356  1.00 45.96  ? 359 PHE   F CB    1 
ATOM   13892 C  CG    . PHE   E 4  359 ? 2.605   60.036  -67.592  1.00 43.83  ? 359 PHE   F CG    1 
ATOM   13893 C  CD1   . PHE   E 4  359 ? 2.068   61.021  -66.794  1.00 43.33  ? 359 PHE   F CD1   1 
ATOM   13894 C  CD2   . PHE   E 4  359 ? 1.847   59.543  -68.636  1.00 49.64  ? 359 PHE   F CD2   1 
ATOM   13895 C  CE1   . PHE   E 4  359 ? 0.783   61.494  -67.013  1.00 39.42  ? 359 PHE   F CE1   1 
ATOM   13896 C  CE2   . PHE   E 4  359 ? 0.558   60.008  -68.856  1.00 50.83  ? 359 PHE   F CE2   1 
ATOM   13897 C  CZ    . PHE   E 4  359 ? 0.030   60.988  -68.036  1.00 37.44  ? 359 PHE   F CZ    1 
ATOM   13898 N  N     . PRO   E 4  360 ? 7.456   60.916  -67.271  1.00 54.44  ? 360 PRO   F N     1 
ATOM   13899 C  CA    . PRO   E 4  360 ? 8.857   60.483  -67.310  1.00 52.03  ? 360 PRO   F CA    1 
ATOM   13900 C  C     . PRO   E 4  360 ? 9.174   59.483  -66.209  1.00 55.11  ? 360 PRO   F C     1 
ATOM   13901 O  O     . PRO   E 4  360 ? 8.812   59.677  -65.047  1.00 59.72  ? 360 PRO   F O     1 
ATOM   13902 C  CB    . PRO   E 4  360 ? 9.639   61.790  -67.134  1.00 51.25  ? 360 PRO   F CB    1 
ATOM   13903 C  CG    . PRO   E 4  360 ? 8.680   62.735  -66.573  1.00 56.58  ? 360 PRO   F CG    1 
ATOM   13904 C  CD    . PRO   E 4  360 ? 7.354   62.375  -67.134  1.00 48.91  ? 360 PRO   F CD    1 
ATOM   13905 N  N     . LEU   E 4  361 ? 9.851   58.405  -66.602  1.00 56.77  ? 361 LEU   F N     1 
ATOM   13906 C  CA    . LEU   E 4  361 ? 10.324  57.380  -65.690  1.00 59.20  ? 361 LEU   F CA    1 
ATOM   13907 C  C     . LEU   E 4  361 ? 11.451  57.931  -64.815  1.00 60.75  ? 361 LEU   F C     1 
ATOM   13908 O  O     . LEU   E 4  361 ? 11.856  59.093  -64.926  1.00 56.74  ? 361 LEU   F O     1 
ATOM   13909 C  CB    . LEU   E 4  361 ? 10.778  56.153  -66.482  1.00 50.89  ? 361 LEU   F CB    1 
ATOM   13910 C  CG    . LEU   E 4  361 ? 9.642   55.388  -67.163  1.00 56.95  ? 361 LEU   F CG    1 
ATOM   13911 C  CD1   . LEU   E 4  361 ? 10.127  54.096  -67.754  1.00 58.98  ? 361 LEU   F CD1   1 
ATOM   13912 C  CD2   . LEU   E 4  361 ? 8.524   55.111  -66.164  1.00 70.10  ? 361 LEU   F CD2   1 
ATOM   13913 N  N     . ALA   E 4  362 ? 11.966  57.069  -63.938  1.00 73.64  ? 362 ALA   F N     1 
ATOM   13914 C  CA    . ALA   E 4  362 ? 13.001  57.431  -62.960  1.00 74.41  ? 362 ALA   F CA    1 
ATOM   13915 C  C     . ALA   E 4  362 ? 14.315  57.873  -63.627  1.00 73.57  ? 362 ALA   F C     1 
ATOM   13916 O  O     . ALA   E 4  362 ? 15.174  58.514  -63.002  1.00 67.01  ? 362 ALA   F O     1 
ATOM   13917 C  CB    . ALA   E 4  362 ? 13.252  56.253  -62.013  1.00 47.92  ? 362 ALA   F CB    1 
ATOM   13918 N  N     . THR   E 4  372 ? 18.532  57.892  -82.606  1.00 97.64  ? 372 THR   F N     1 
ATOM   13919 C  CA    . THR   E 4  372 ? 18.232  56.512  -82.244  1.00 93.82  ? 372 THR   F CA    1 
ATOM   13920 C  C     . THR   E 4  372 ? 16.723  56.255  -82.242  1.00 103.08 ? 372 THR   F C     1 
ATOM   13921 O  O     . THR   E 4  372 ? 16.259  55.271  -81.658  1.00 104.04 ? 372 THR   F O     1 
ATOM   13922 C  CB    . THR   E 4  372 ? 18.804  56.156  -80.855  1.00 89.19  ? 372 THR   F CB    1 
ATOM   13923 O  OG1   . THR   E 4  372 ? 19.611  57.240  -80.370  1.00 93.50  ? 372 THR   F OG1   1 
ATOM   13924 C  CG2   . THR   E 4  372 ? 19.640  54.884  -80.930  1.00 77.99  ? 372 THR   F CG2   1 
ATOM   13925 N  N     . SER   E 4  373 ? 15.964  57.141  -82.892  1.00 95.90  ? 373 SER   F N     1 
ATOM   13926 C  CA    . SER   E 4  373 ? 14.511  57.022  -82.939  1.00 74.70  ? 373 SER   F CA    1 
ATOM   13927 C  C     . SER   E 4  373 ? 14.080  55.989  -83.966  1.00 71.33  ? 373 SER   F C     1 
ATOM   13928 O  O     . SER   E 4  373 ? 14.696  55.850  -85.026  1.00 77.92  ? 373 SER   F O     1 
ATOM   13929 C  CB    . SER   E 4  373 ? 13.865  58.361  -83.288  1.00 63.86  ? 373 SER   F CB    1 
ATOM   13930 O  OG    . SER   E 4  373 ? 14.226  59.353  -82.350  1.00 91.50  ? 373 SER   F OG    1 
ATOM   13931 N  N     . ILE   E 4  374 ? 13.003  55.268  -83.648  1.00 63.73  ? 374 ILE   F N     1 
ATOM   13932 C  CA    . ILE   E 4  374 ? 12.347  54.416  -84.637  1.00 59.03  ? 374 ILE   F CA    1 
ATOM   13933 C  C     . ILE   E 4  374 ? 11.409  55.197  -85.544  1.00 57.32  ? 374 ILE   F C     1 
ATOM   13934 O  O     . ILE   E 4  374 ? 10.894  54.636  -86.524  1.00 51.86  ? 374 ILE   F O     1 
ATOM   13935 C  CB    . ILE   E 4  374 ? 11.565  53.291  -83.937  1.00 57.63  ? 374 ILE   F CB    1 
ATOM   13936 C  CG1   . ILE   E 4  374 ? 10.577  53.887  -82.932  1.00 54.78  ? 374 ILE   F CG1   1 
ATOM   13937 C  CG2   . ILE   E 4  374 ? 12.518  52.339  -83.239  1.00 62.27  ? 374 ILE   F CG2   1 
ATOM   13938 C  CD1   . ILE   E 4  374 ? 9.324   53.052  -82.721  1.00 56.48  ? 374 ILE   F CD1   1 
ATOM   13939 N  N     . PHE   E 4  375 ? 11.178  56.475  -85.242  1.00 60.24  ? 375 PHE   F N     1 
ATOM   13940 C  CA    . PHE   E 4  375 ? 10.195  57.315  -85.907  1.00 55.12  ? 375 PHE   F CA    1 
ATOM   13941 C  C     . PHE   E 4  375 ? 10.891  58.426  -86.676  1.00 56.53  ? 375 PHE   F C     1 
ATOM   13942 O  O     . PHE   E 4  375 ? 11.946  58.912  -86.255  1.00 61.86  ? 375 PHE   F O     1 
ATOM   13943 C  CB    . PHE   E 4  375 ? 9.231   57.953  -84.894  1.00 51.21  ? 375 PHE   F CB    1 
ATOM   13944 C  CG    . PHE   E 4  375 ? 8.366   56.977  -84.168  1.00 38.27  ? 375 PHE   F CG    1 
ATOM   13945 C  CD1   . PHE   E 4  375 ? 7.345   56.331  -84.818  1.00 46.28  ? 375 PHE   F CD1   1 
ATOM   13946 C  CD2   . PHE   E 4  375 ? 8.564   56.720  -82.834  1.00 48.32  ? 375 PHE   F CD2   1 
ATOM   13947 C  CE1   . PHE   E 4  375 ? 6.545   55.433  -84.151  1.00 45.77  ? 375 PHE   F CE1   1 
ATOM   13948 C  CE2   . PHE   E 4  375 ? 7.759   55.825  -82.154  1.00 50.07  ? 375 PHE   F CE2   1 
ATOM   13949 C  CZ    . PHE   E 4  375 ? 6.750   55.179  -82.818  1.00 45.52  ? 375 PHE   F CZ    1 
ATOM   13950 N  N     . ILE   E 4  376 ? 10.283  58.830  -87.798  1.00 52.94  ? 376 ILE   F N     1 
ATOM   13951 C  CA    . ILE   E 4  376 ? 10.658  60.042  -88.528  1.00 49.73  ? 376 ILE   F CA    1 
ATOM   13952 C  C     . ILE   E 4  376 ? 9.649   61.128  -88.168  1.00 55.84  ? 376 ILE   F C     1 
ATOM   13953 O  O     . ILE   E 4  376 ? 8.458   60.993  -88.475  1.00 53.35  ? 376 ILE   F O     1 
ATOM   13954 C  CB    . ILE   E 4  376 ? 10.659  59.820  -90.052  1.00 48.67  ? 376 ILE   F CB    1 
ATOM   13955 C  CG1   . ILE   E 4  376 ? 11.090  58.393  -90.449  1.00 53.83  ? 376 ILE   F CG1   1 
ATOM   13956 C  CG2   . ILE   E 4  376 ? 11.438  60.916  -90.749  1.00 33.10  ? 376 ILE   F CG2   1 
ATOM   13957 C  CD1   . ILE   E 4  376 ? 12.352  57.868  -89.774  1.00 62.72  ? 376 ILE   F CD1   1 
ATOM   13958 N  N     . LYS   E 4  377 ? 10.101  62.217  -87.541  1.00 54.50  ? 377 LYS   F N     1 
ATOM   13959 C  CA    . LYS   E 4  377 ? 9.186   63.320  -87.249  1.00 52.32  ? 377 LYS   F CA    1 
ATOM   13960 C  C     . LYS   E 4  377 ? 8.908   64.098  -88.537  1.00 47.23  ? 377 LYS   F C     1 
ATOM   13961 O  O     . LYS   E 4  377 ? 9.836   64.614  -89.172  1.00 50.46  ? 377 LYS   F O     1 
ATOM   13962 C  CB    . LYS   E 4  377 ? 9.745   64.241  -86.154  1.00 45.23  ? 377 LYS   F CB    1 
ATOM   13963 C  CG    . LYS   E 4  377 ? 8.827   65.460  -85.855  1.00 50.21  ? 377 LYS   F CG    1 
ATOM   13964 C  CD    . LYS   E 4  377 ? 9.431   66.527  -84.919  1.00 49.74  ? 377 LYS   F CD    1 
ATOM   13965 C  CE    . LYS   E 4  377 ? 9.230   66.186  -83.431  1.00 57.12  ? 377 LYS   F CE    1 
ATOM   13966 N  NZ    . LYS   E 4  377 ? 9.692   67.256  -82.482  1.00 60.44  ? 377 LYS   F NZ    1 
ATOM   13967 N  N     . LEU   E 4  378 ? 7.637   64.198  -88.920  1.00 41.67  ? 378 LEU   F N     1 
ATOM   13968 C  CA    . LEU   E 4  378 ? 7.257   64.933  -90.125  1.00 50.11  ? 378 LEU   F CA    1 
ATOM   13969 C  C     . LEU   E 4  378 ? 7.092   66.415  -89.779  1.00 62.78  ? 378 LEU   F C     1 
ATOM   13970 O  O     . LEU   E 4  378 ? 6.196   66.785  -89.004  1.00 63.42  ? 378 LEU   F O     1 
ATOM   13971 C  CB    . LEU   E 4  378 ? 5.984   64.349  -90.743  1.00 37.06  ? 378 LEU   F CB    1 
ATOM   13972 C  CG    . LEU   E 4  378 ? 5.950   62.847  -91.067  1.00 42.16  ? 378 LEU   F CG    1 
ATOM   13973 C  CD1   . LEU   E 4  378 ? 5.301   62.544  -92.429  1.00 45.44  ? 378 LEU   F CD1   1 
ATOM   13974 C  CD2   . LEU   E 4  378 ? 7.328   62.241  -91.007  1.00 41.96  ? 378 LEU   F CD2   1 
ATOM   13975 N  N     . HIS   E 4  379 ? 7.948   67.259  -90.372  1.00 68.02  ? 379 HIS   F N     1 
ATOM   13976 C  CA    . HIS   E 4  379 ? 8.239   68.604  -89.865  1.00 71.20  ? 379 HIS   F CA    1 
ATOM   13977 C  C     . HIS   E 4  379 ? 7.327   69.659  -90.486  1.00 85.42  ? 379 HIS   F C     1 
ATOM   13978 O  O     . HIS   E 4  379 ? 7.532   70.068  -91.638  1.00 78.69  ? 379 HIS   F O     1 
ATOM   13979 C  CB    . HIS   E 4  379 ? 9.698   68.967  -90.127  1.00 66.44  ? 379 HIS   F CB    1 
ATOM   13980 C  CG    . HIS   E 4  379 ? 10.635  68.487  -89.066  1.00 65.37  ? 379 HIS   F CG    1 
ATOM   13981 N  ND1   . HIS   E 4  379 ? 12.005  68.510  -89.216  1.00 71.58  ? 379 HIS   F ND1   1 
ATOM   13982 C  CD2   . HIS   E 4  379 ? 10.399  67.968  -87.838  1.00 62.69  ? 379 HIS   F CD2   1 
ATOM   13983 C  CE1   . HIS   E 4  379 ? 12.574  68.029  -88.125  1.00 75.98  ? 379 HIS   F CE1   1 
ATOM   13984 N  NE2   . HIS   E 4  379 ? 11.621  67.691  -87.273  1.00 74.85  ? 379 HIS   F NE2   1 
ATOM   13985 N  N     . HIS   E 4  380 ? 6.370   70.150  -89.692  1.00 92.04  ? 380 HIS   F N     1 
ATOM   13986 C  CA    . HIS   E 4  380 ? 5.508   71.277  -90.064  1.00 85.65  ? 380 HIS   F CA    1 
ATOM   13987 C  C     . HIS   E 4  380 ? 5.621   72.437  -89.068  1.00 85.78  ? 380 HIS   F C     1 
ATOM   13988 O  O     . HIS   E 4  380 ? 5.348   73.595  -89.402  1.00 81.45  ? 380 HIS   F O     1 
ATOM   13989 C  CB    . HIS   E 4  380 ? 4.054   70.822  -90.167  1.00 77.14  ? 380 HIS   F CB    1 
ATOM   13990 C  CG    . HIS   E 4  380 ? 3.462   70.361  -88.869  1.00 86.96  ? 380 HIS   F CG    1 
ATOM   13991 N  ND1   . HIS   E 4  380 ? 4.084   69.444  -88.047  1.00 85.43  ? 380 HIS   F ND1   1 
ATOM   13992 C  CD2   . HIS   E 4  380 ? 2.289   70.676  -88.263  1.00 85.57  ? 380 HIS   F CD2   1 
ATOM   13993 C  CE1   . HIS   E 4  380 ? 3.326   69.225  -86.985  1.00 82.05  ? 380 HIS   F CE1   1 
ATOM   13994 N  NE2   . HIS   E 4  380 ? 2.230   69.959  -87.094  1.00 74.06  ? 380 HIS   F NE2   1 
ATOM   13995 N  N     . MET   F 2  1   ? -28.744 77.383  -31.821  1.00 65.21  ? 1   MET   B N     1 
ATOM   13996 C  CA    . MET   F 2  1   ? -27.319 77.384  -31.502  1.00 69.52  ? 1   MET   B CA    1 
ATOM   13997 C  C     . MET   F 2  1   ? -26.690 75.983  -31.542  1.00 56.97  ? 1   MET   B C     1 
ATOM   13998 O  O     . MET   F 2  1   ? -25.630 75.760  -30.947  1.00 56.57  ? 1   MET   B O     1 
ATOM   13999 C  CB    . MET   F 2  1   ? -27.092 78.015  -30.125  1.00 71.83  ? 1   MET   B CB    1 
ATOM   14000 C  CG    . MET   F 2  1   ? -27.115 79.534  -30.130  1.00 82.23  ? 1   MET   B CG    1 
ATOM   14001 S  SD    . MET   F 2  1   ? -25.683 80.238  -30.976  1.00 95.52  ? 1   MET   B SD    1 
ATOM   14002 C  CE    . MET   F 2  1   ? -26.107 79.924  -32.695  1.00 101.15 ? 1   MET   B CE    1 
ATOM   14003 N  N     . ARG   F 2  2   ? -27.345 75.056  -32.247  1.00 51.80  ? 2   ARG   B N     1 
ATOM   14004 C  CA    . ARG   F 2  2   ? -26.874 73.682  -32.402  1.00 41.14  ? 2   ARG   B CA    1 
ATOM   14005 C  C     . ARG   F 2  2   ? -26.095 73.212  -31.167  1.00 44.38  ? 2   ARG   B C     1 
ATOM   14006 O  O     . ARG   F 2  2   ? -24.859 73.171  -31.171  1.00 35.71  ? 2   ARG   B O     1 
ATOM   14007 C  CB    . ARG   F 2  2   ? -26.053 73.577  -33.686  1.00 40.58  ? 2   ARG   B CB    1 
ATOM   14008 C  CG    . ARG   F 2  2   ? -26.907 73.644  -34.957  1.00 45.17  ? 2   ARG   B CG    1 
ATOM   14009 C  CD    . ARG   F 2  2   ? -27.113 72.250  -35.572  1.00 49.11  ? 2   ARG   B CD    1 
ATOM   14010 N  NE    . ARG   F 2  2   ? -28.524 71.917  -35.756  1.00 51.27  ? 2   ARG   B NE    1 
ATOM   14011 C  CZ    . ARG   F 2  2   ? -29.000 70.682  -35.902  1.00 52.04  ? 2   ARG   B CZ    1 
ATOM   14012 N  NH1   . ARG   F 2  2   ? -28.204 69.627  -35.950  1.00 37.80  ? 2   ARG   B NH1   1 
ATOM   14013 N  NH2   . ARG   F 2  2   ? -30.317 70.497  -35.975  1.00 64.35  ? 2   ARG   B NH2   1 
ATOM   14014 N  N     . GLU   F 2  3   ? -26.834 72.906  -30.091  1.00 42.86  ? 3   GLU   B N     1 
ATOM   14015 C  CA    . GLU   F 2  3   ? -26.329 72.364  -28.839  1.00 40.29  ? 3   GLU   B CA    1 
ATOM   14016 C  C     . GLU   F 2  3   ? -26.135 70.845  -28.932  1.00 39.91  ? 3   GLU   B C     1 
ATOM   14017 O  O     . GLU   F 2  3   ? -26.729 70.153  -29.773  1.00 37.99  ? 3   GLU   B O     1 
ATOM   14018 C  CB    . GLU   F 2  3   ? -27.279 72.683  -27.672  1.00 38.71  ? 3   GLU   B CB    1 
ATOM   14019 C  CG    . GLU   F 2  3   ? -27.299 74.138  -27.199  1.00 40.44  ? 3   GLU   B CG    1 
ATOM   14020 C  CD    . GLU   F 2  3   ? -28.419 74.988  -27.828  1.00 43.48  ? 3   GLU   B CD    1 
ATOM   14021 O  OE1   . GLU   F 2  3   ? -29.237 74.480  -28.622  1.00 41.93  ? 3   GLU   B OE1   1 
ATOM   14022 O  OE2   . GLU   F 2  3   ? -28.486 76.184  -27.512  1.00 47.22  ? 3   GLU   B OE2   1 
ATOM   14023 N  N     . ILE   F 2  4   ? -25.267 70.337  -28.058  1.00 38.25  ? 4   ILE   B N     1 
ATOM   14024 C  CA    . ILE   F 2  4   ? -24.991 68.911  -27.923  1.00 41.69  ? 4   ILE   B CA    1 
ATOM   14025 C  C     . ILE   F 2  4   ? -24.999 68.587  -26.440  1.00 35.63  ? 4   ILE   B C     1 
ATOM   14026 O  O     . ILE   F 2  4   ? -24.296 69.241  -25.662  1.00 29.21  ? 4   ILE   B O     1 
ATOM   14027 C  CB    . ILE   F 2  4   ? -23.636 68.500  -28.547  1.00 34.47  ? 4   ILE   B CB    1 
ATOM   14028 C  CG1   . ILE   F 2  4   ? -23.672 68.593  -30.070  1.00 33.14  ? 4   ILE   B CG1   1 
ATOM   14029 C  CG2   . ILE   F 2  4   ? -23.269 67.081  -28.127  1.00 27.54  ? 4   ILE   B CG2   1 
ATOM   14030 C  CD1   . ILE   F 2  4   ? -22.304 68.457  -30.719  1.00 26.27  ? 4   ILE   B CD1   1 
ATOM   14031 N  N     . VAL   F 2  5   ? -25.788 67.587  -26.055  1.00 35.87  ? 5   VAL   B N     1 
ATOM   14032 C  CA    . VAL   F 2  5   ? -25.845 67.112  -24.675  1.00 30.08  ? 5   VAL   B CA    1 
ATOM   14033 C  C     . VAL   F 2  5   ? -24.853 65.958  -24.518  1.00 32.58  ? 5   VAL   B C     1 
ATOM   14034 O  O     . VAL   F 2  5   ? -24.947 64.947  -25.224  1.00 33.02  ? 5   VAL   B O     1 
ATOM   14035 C  CB    . VAL   F 2  5   ? -27.271 66.675  -24.296  1.00 30.96  ? 5   VAL   B CB    1 
ATOM   14036 C  CG1   . VAL   F 2  5   ? -27.344 66.325  -22.833  1.00 32.30  ? 5   VAL   B CG1   1 
ATOM   14037 C  CG2   . VAL   F 2  5   ? -28.292 67.755  -24.632  1.00 29.94  ? 5   VAL   B CG2   1 
ATOM   14038 N  N     . HIS   F 2  6   ? -23.914 66.103  -23.583  1.00 32.23  ? 6   HIS   B N     1 
ATOM   14039 C  CA    . HIS   F 2  6   ? -22.886 65.101  -23.327  1.00 34.73  ? 6   HIS   B CA    1 
ATOM   14040 C  C     . HIS   F 2  6   ? -23.312 64.226  -22.151  1.00 38.53  ? 6   HIS   B C     1 
ATOM   14041 O  O     . HIS   F 2  6   ? -23.738 64.734  -21.110  1.00 40.41  ? 6   HIS   B O     1 
ATOM   14042 C  CB    . HIS   F 2  6   ? -21.526 65.769  -23.051  1.00 31.29  ? 6   HIS   B CB    1 
ATOM   14043 C  CG    . HIS   F 2  6   ? -20.442 64.822  -22.599  1.00 40.22  ? 6   HIS   B CG    1 
ATOM   14044 N  ND1   . HIS   F 2  6   ? -19.574 64.202  -23.473  1.00 38.67  ? 6   HIS   B ND1   1 
ATOM   14045 C  CD2   . HIS   F 2  6   ? -20.067 64.415  -21.358  1.00 40.86  ? 6   HIS   B CD2   1 
ATOM   14046 C  CE1   . HIS   F 2  6   ? -18.720 63.452  -22.796  1.00 34.35  ? 6   HIS   B CE1   1 
ATOM   14047 N  NE2   . HIS   F 2  6   ? -18.996 63.565  -21.510  1.00 35.31  ? 6   HIS   B NE2   1 
ATOM   14048 N  N     . ILE   F 2  7   ? -23.194 62.914  -22.317  1.00 37.72  ? 7   ILE   B N     1 
ATOM   14049 C  CA    . ILE   F 2  7   ? -23.503 61.956  -21.267  1.00 30.63  ? 7   ILE   B CA    1 
ATOM   14050 C  C     . ILE   F 2  7   ? -22.292 61.042  -21.112  1.00 31.53  ? 7   ILE   B C     1 
ATOM   14051 O  O     . ILE   F 2  7   ? -21.847 60.430  -22.090  1.00 34.05  ? 7   ILE   B O     1 
ATOM   14052 C  CB    . ILE   F 2  7   ? -24.767 61.145  -21.599  1.00 29.83  ? 7   ILE   B CB    1 
ATOM   14053 C  CG1   . ILE   F 2  7   ? -25.890 62.073  -22.043  1.00 32.18  ? 7   ILE   B CG1   1 
ATOM   14054 C  CG2   . ILE   F 2  7   ? -25.227 60.363  -20.410  1.00 29.64  ? 7   ILE   B CG2   1 
ATOM   14055 C  CD1   . ILE   F 2  7   ? -27.077 61.366  -22.628  1.00 23.98  ? 7   ILE   B CD1   1 
ATOM   14056 N  N     . GLN   F 2  8   ? -21.749 60.960  -19.899  1.00 34.16  ? 8   GLN   B N     1 
ATOM   14057 C  CA    . GLN   F 2  8   ? -20.705 59.992  -19.571  1.00 32.39  ? 8   GLN   B CA    1 
ATOM   14058 C  C     . GLN   F 2  8   ? -21.199 59.060  -18.477  1.00 30.28  ? 8   GLN   B C     1 
ATOM   14059 O  O     . GLN   F 2  8   ? -21.709 59.523  -17.453  1.00 34.47  ? 8   GLN   B O     1 
ATOM   14060 C  CB    . GLN   F 2  8   ? -19.426 60.683  -19.131  1.00 30.09  ? 8   GLN   B CB    1 
ATOM   14061 C  CG    . GLN   F 2  8   ? -19.611 61.730  -18.083  1.00 30.82  ? 8   GLN   B CG    1 
ATOM   14062 C  CD    . GLN   F 2  8   ? -18.414 62.640  -18.014  1.00 32.46  ? 8   GLN   B CD    1 
ATOM   14063 O  OE1   . GLN   F 2  8   ? -18.167 63.424  -18.943  1.00 31.32  ? 8   GLN   B OE1   1 
ATOM   14064 N  NE2   . GLN   F 2  8   ? -17.627 62.511  -16.947  1.00 29.28  ? 8   GLN   B NE2   1 
ATOM   14065 N  N     . ALA   F 2  9   ? -21.044 57.753  -18.690  1.00 27.12  ? 9   ALA   B N     1 
ATOM   14066 C  CA    . ALA   F 2  9   ? -21.625 56.745  -17.806  1.00 30.85  ? 9   ALA   B CA    1 
ATOM   14067 C  C     . ALA   F 2  9   ? -20.608 55.655  -17.487  1.00 27.81  ? 9   ALA   B C     1 
ATOM   14068 O  O     . ALA   F 2  9   ? -19.987 55.090  -18.392  1.00 29.11  ? 9   ALA   B O     1 
ATOM   14069 C  CB    . ALA   F 2  9   ? -22.873 56.131  -18.435  1.00 21.62  ? 9   ALA   B CB    1 
ATOM   14070 N  N     . GLY   F 2  10  ? -20.449 55.358  -16.203  1.00 27.68  ? 10  GLY   B N     1 
ATOM   14071 C  CA    . GLY   F 2  10  ? -19.539 54.324  -15.762  1.00 21.58  ? 10  GLY   B CA    1 
ATOM   14072 C  C     . GLY   F 2  10  ? -18.119 54.812  -15.543  1.00 24.19  ? 10  GLY   B C     1 
ATOM   14073 O  O     . GLY   F 2  10  ? -17.773 55.976  -15.761  1.00 24.03  ? 10  GLY   B O     1 
ATOM   14074 N  N     . GLN   F 2  11  ? -17.261 53.874  -15.120  1.00 26.26  ? 11  GLN   B N     1 
ATOM   14075 C  CA    . GLN   F 2  11  ? -15.872 54.223  -14.831  1.00 33.67  ? 11  GLN   B CA    1 
ATOM   14076 C  C     . GLN   F 2  11  ? -15.174 54.767  -16.067  1.00 21.65  ? 11  GLN   B C     1 
ATOM   14077 O  O     . GLN   F 2  11  ? -14.866 55.950  -16.129  1.00 32.79  ? 11  GLN   B O     1 
ATOM   14078 C  CB    . GLN   F 2  11  ? -15.092 53.030  -14.272  1.00 29.19  ? 11  GLN   B CB    1 
ATOM   14079 C  CG    . GLN   F 2  11  ? -13.735 53.453  -13.681  1.00 44.21  ? 11  GLN   B CG    1 
ATOM   14080 C  CD    . GLN   F 2  11  ? -12.883 52.283  -13.181  1.00 54.74  ? 11  GLN   B CD    1 
ATOM   14081 O  OE1   . GLN   F 2  11  ? -13.272 51.546  -12.261  1.00 65.58  ? 11  GLN   B OE1   1 
ATOM   14082 N  NE2   . GLN   F 2  11  ? -11.705 52.116  -13.787  1.00 45.98  ? 11  GLN   B NE2   1 
ATOM   14083 N  N     . CYS   F 2  12  ? -14.942 53.923  -17.063  1.00 25.18  ? 12  CYS   B N     1 
ATOM   14084 C  CA    . CYS   F 2  12  ? -14.286 54.365  -18.289  1.00 23.42  ? 12  CYS   B CA    1 
ATOM   14085 C  C     . CYS   F 2  12  ? -14.963 55.608  -18.861  1.00 31.83  ? 12  CYS   B C     1 
ATOM   14086 O  O     . CYS   F 2  12  ? -14.324 56.645  -19.070  1.00 32.26  ? 12  CYS   B O     1 
ATOM   14087 C  CB    . CYS   F 2  12  ? -14.284 53.223  -19.314  1.00 11.27  ? 12  CYS   B CB    1 
ATOM   14088 S  SG    . CYS   F 2  12  ? -13.584 53.685  -20.866  1.00 24.07  ? 12  CYS   B SG    1 
ATOM   14089 N  N     . GLY   F 2  13  ? -16.267 55.512  -19.127  1.00 27.27  ? 13  GLY   B N     1 
ATOM   14090 C  CA    . GLY   F 2  13  ? -16.967 56.625  -19.733  1.00 26.64  ? 13  GLY   B CA    1 
ATOM   14091 C  C     . GLY   F 2  13  ? -16.805 57.924  -18.978  1.00 29.17  ? 13  GLY   B C     1 
ATOM   14092 O  O     . GLY   F 2  13  ? -16.753 58.994  -19.594  1.00 30.74  ? 13  GLY   B O     1 
ATOM   14093 N  N     . ASN   F 2  14  ? -16.720 57.857  -17.638  1.00 29.74  ? 14  ASN   B N     1 
ATOM   14094 C  CA    . ASN   F 2  14  ? -16.537 59.060  -16.818  1.00 33.57  ? 14  ASN   B CA    1 
ATOM   14095 C  C     . ASN   F 2  14  ? -15.084 59.528  -16.789  1.00 33.15  ? 14  ASN   B C     1 
ATOM   14096 O  O     . ASN   F 2  14  ? -14.819 60.722  -16.598  1.00 31.55  ? 14  ASN   B O     1 
ATOM   14097 C  CB    . ASN   F 2  14  ? -17.021 58.816  -15.376  1.00 32.38  ? 14  ASN   B CB    1 
ATOM   14098 C  CG    . ASN   F 2  14  ? -18.479 59.226  -15.162  1.00 36.85  ? 14  ASN   B CG    1 
ATOM   14099 O  OD1   . ASN   F 2  14  ? -18.800 60.417  -15.063  1.00 32.02  ? 14  ASN   B OD1   1 
ATOM   14100 N  ND2   . ASN   F 2  14  ? -19.366 58.237  -15.084  1.00 29.41  ? 14  ASN   B ND2   1 
ATOM   14101 N  N     . GLN   F 2  15  ? -14.135 58.615  -16.959  1.00 25.84  ? 15  GLN   B N     1 
ATOM   14102 C  CA    . GLN   F 2  15  ? -12.742 59.022  -16.869  1.00 38.77  ? 15  GLN   B CA    1 
ATOM   14103 C  C     . GLN   F 2  15  ? -12.246 59.631  -18.175  1.00 34.75  ? 15  GLN   B C     1 
ATOM   14104 O  O     . GLN   F 2  15  ? -11.493 60.616  -18.156  1.00 29.23  ? 15  GLN   B O     1 
ATOM   14105 C  CB    . GLN   F 2  15  ? -11.869 57.839  -16.452  1.00 36.49  ? 15  GLN   B CB    1 
ATOM   14106 C  CG    . GLN   F 2  15  ? -10.807 58.252  -15.449  1.00 54.05  ? 15  GLN   B CG    1 
ATOM   14107 C  CD    . GLN   F 2  15  ? -10.811 57.385  -14.210  1.00 64.28  ? 15  GLN   B CD    1 
ATOM   14108 O  OE1   . GLN   F 2  15  ? -11.248 56.224  -14.244  1.00 55.34  ? 15  GLN   B OE1   1 
ATOM   14109 N  NE2   . GLN   F 2  15  ? -10.317 57.939  -13.104  1.00 65.70  ? 15  GLN   B NE2   1 
ATOM   14110 N  N     . ILE   F 2  16  ? -12.646 59.057  -19.315  1.00 30.47  ? 16  ILE   B N     1 
ATOM   14111 C  CA    . ILE   F 2  16  ? -12.355 59.712  -20.587  1.00 31.86  ? 16  ILE   B CA    1 
ATOM   14112 C  C     . ILE   F 2  16  ? -13.282 60.906  -20.814  1.00 33.71  ? 16  ILE   B C     1 
ATOM   14113 O  O     . ILE   F 2  16  ? -12.913 61.846  -21.535  1.00 28.47  ? 16  ILE   B O     1 
ATOM   14114 C  CB    . ILE   F 2  16  ? -12.415 58.706  -21.753  1.00 25.77  ? 16  ILE   B CB    1 
ATOM   14115 C  CG1   . ILE   F 2  16  ? -13.857 58.387  -22.140  1.00 28.67  ? 16  ILE   B CG1   1 
ATOM   14116 C  CG2   . ILE   F 2  16  ? -11.618 57.417  -21.400  1.00 25.88  ? 16  ILE   B CG2   1 
ATOM   14117 C  CD1   . ILE   F 2  16  ? -13.980 57.546  -23.441  1.00 25.93  ? 16  ILE   B CD1   1 
ATOM   14118 N  N     . GLY   F 2  17  ? -14.455 60.919  -20.172  1.00 30.81  ? 17  GLY   B N     1 
ATOM   14119 C  CA    . GLY   F 2  17  ? -15.329 62.078  -20.273  1.00 32.32  ? 17  GLY   B CA    1 
ATOM   14120 C  C     . GLY   F 2  17  ? -14.763 63.308  -19.586  1.00 29.36  ? 17  GLY   B C     1 
ATOM   14121 O  O     . GLY   F 2  17  ? -14.697 64.395  -20.168  1.00 35.71  ? 17  GLY   B O     1 
ATOM   14122 N  N     . ALA   F 2  18  ? -14.348 63.161  -18.339  1.00 31.59  ? 18  ALA   B N     1 
ATOM   14123 C  CA    . ALA   F 2  18  ? -13.747 64.298  -17.658  1.00 34.70  ? 18  ALA   B CA    1 
ATOM   14124 C  C     . ALA   F 2  18  ? -12.512 64.789  -18.398  1.00 31.65  ? 18  ALA   B C     1 
ATOM   14125 O  O     . ALA   F 2  18  ? -12.229 65.986  -18.409  1.00 39.30  ? 18  ALA   B O     1 
ATOM   14126 C  CB    . ALA   F 2  18  ? -13.412 63.920  -16.216  1.00 29.12  ? 18  ALA   B CB    1 
ATOM   14127 N  N     . LYS   F 2  19  ? -11.778 63.886  -19.035  1.00 28.02  ? 19  LYS   B N     1 
ATOM   14128 C  CA    . LYS   F 2  19  ? -10.578 64.281  -19.761  1.00 35.25  ? 19  LYS   B CA    1 
ATOM   14129 C  C     . LYS   F 2  19  ? -10.939 65.083  -21.019  1.00 37.18  ? 19  LYS   B C     1 
ATOM   14130 O  O     . LYS   F 2  19  ? -10.401 66.171  -21.256  1.00 36.01  ? 19  LYS   B O     1 
ATOM   14131 C  CB    . LYS   F 2  19  ? -9.770  63.023  -20.083  1.00 32.43  ? 19  LYS   B CB    1 
ATOM   14132 C  CG    . LYS   F 2  19  ? -8.307  63.060  -19.680  1.00 42.87  ? 19  LYS   B CG    1 
ATOM   14133 C  CD    . LYS   F 2  19  ? -7.446  63.137  -20.969  1.00 46.33  ? 19  LYS   B CD    1 
ATOM   14134 C  CE    . LYS   F 2  19  ? -5.927  63.136  -20.713  1.00 49.86  ? 19  LYS   B CE    1 
ATOM   14135 N  NZ    . LYS   F 2  19  ? -5.164  64.022  -21.669  1.00 47.92  ? 19  LYS   B NZ    1 
ATOM   14136 N  N     . PHE   F 2  20  ? -11.875 64.577  -21.823  1.00 33.14  ? 20  PHE   B N     1 
ATOM   14137 C  CA    . PHE   F 2  20  ? -12.391 65.365  -22.932  1.00 28.95  ? 20  PHE   B CA    1 
ATOM   14138 C  C     . PHE   F 2  20  ? -12.717 66.792  -22.488  1.00 40.47  ? 20  PHE   B C     1 
ATOM   14139 O  O     . PHE   F 2  20  ? -12.298 67.768  -23.126  1.00 39.03  ? 20  PHE   B O     1 
ATOM   14140 C  CB    . PHE   F 2  20  ? -13.620 64.669  -23.525  1.00 30.29  ? 20  PHE   B CB    1 
ATOM   14141 C  CG    . PHE   F 2  20  ? -14.435 65.537  -24.463  1.00 34.96  ? 20  PHE   B CG    1 
ATOM   14142 C  CD1   . PHE   F 2  20  ? -14.022 65.753  -25.777  1.00 32.25  ? 20  PHE   B CD1   1 
ATOM   14143 C  CD2   . PHE   F 2  20  ? -15.619 66.134  -24.030  1.00 29.36  ? 20  PHE   B CD2   1 
ATOM   14144 C  CE1   . PHE   F 2  20  ? -14.770 66.551  -26.643  1.00 31.28  ? 20  PHE   B CE1   1 
ATOM   14145 C  CE2   . PHE   F 2  20  ? -16.380 66.923  -24.899  1.00 33.87  ? 20  PHE   B CE2   1 
ATOM   14146 C  CZ    . PHE   F 2  20  ? -15.955 67.133  -26.211  1.00 28.48  ? 20  PHE   B CZ    1 
ATOM   14147 N  N     . TRP   F 2  21  ? -13.470 66.935  -21.393  1.00 35.66  ? 21  TRP   B N     1 
ATOM   14148 C  CA    . TRP   F 2  21  ? -13.845 68.270  -20.938  1.00 38.85  ? 21  TRP   B CA    1 
ATOM   14149 C  C     . TRP   F 2  21  ? -12.613 69.070  -20.547  1.00 34.81  ? 21  TRP   B C     1 
ATOM   14150 O  O     . TRP   F 2  21  ? -12.446 70.228  -20.940  1.00 38.74  ? 21  TRP   B O     1 
ATOM   14151 C  CB    . TRP   F 2  21  ? -14.832 68.174  -19.770  1.00 34.51  ? 21  TRP   B CB    1 
ATOM   14152 C  CG    . TRP   F 2  21  ? -16.217 67.816  -20.236  1.00 41.32  ? 21  TRP   B CG    1 
ATOM   14153 C  CD1   . TRP   F 2  21  ? -16.857 66.621  -20.076  1.00 30.08  ? 21  TRP   B CD1   1 
ATOM   14154 C  CD2   . TRP   F 2  21  ? -17.110 68.656  -20.981  1.00 31.61  ? 21  TRP   B CD2   1 
ATOM   14155 N  NE1   . TRP   F 2  21  ? -18.093 66.669  -20.676  1.00 34.17  ? 21  TRP   B NE1   1 
ATOM   14156 C  CE2   . TRP   F 2  21  ? -18.268 67.901  -21.247  1.00 26.79  ? 21  TRP   B CE2   1 
ATOM   14157 C  CE3   . TRP   F 2  21  ? -17.036 69.968  -21.454  1.00 35.90  ? 21  TRP   B CE3   1 
ATOM   14158 C  CZ2   . TRP   F 2  21  ? -19.356 68.421  -21.934  1.00 31.01  ? 21  TRP   B CZ2   1 
ATOM   14159 C  CZ3   . TRP   F 2  21  ? -18.122 70.490  -22.152  1.00 33.87  ? 21  TRP   B CZ3   1 
ATOM   14160 C  CH2   . TRP   F 2  21  ? -19.264 69.716  -22.384  1.00 32.49  ? 21  TRP   B CH2   1 
ATOM   14161 N  N     . GLU   F 2  22  ? -11.743 68.463  -19.765  1.00 35.38  ? 22  GLU   B N     1 
ATOM   14162 C  CA    . GLU   F 2  22  ? -10.521 69.129  -19.364  1.00 41.57  ? 22  GLU   B CA    1 
ATOM   14163 C  C     . GLU   F 2  22  ? -9.790  69.708  -20.572  1.00 43.01  ? 22  GLU   B C     1 
ATOM   14164 O  O     . GLU   F 2  22  ? -9.329  70.854  -20.537  1.00 37.93  ? 22  GLU   B O     1 
ATOM   14165 C  CB    . GLU   F 2  22  ? -9.670  68.119  -18.608  1.00 31.11  ? 22  GLU   B CB    1 
ATOM   14166 C  CG    . GLU   F 2  22  ? -8.261  68.507  -18.371  1.00 46.19  ? 22  GLU   B CG    1 
ATOM   14167 C  CD    . GLU   F 2  22  ? -7.470  67.338  -17.833  1.00 63.68  ? 22  GLU   B CD    1 
ATOM   14168 O  OE1   . GLU   F 2  22  ? -8.040  66.537  -17.024  1.00 42.48  ? 22  GLU   B OE1   1 
ATOM   14169 O  OE2   . GLU   F 2  22  ? -6.291  67.214  -18.251  1.00 72.17  ? 22  GLU   B OE2   1 
ATOM   14170 N  N     . VAL   F 2  23  ? -9.727  68.942  -21.667  1.00 38.34  ? 23  VAL   B N     1 
ATOM   14171 C  CA    . VAL   F 2  23  ? -8.911  69.305  -22.820  1.00 37.20  ? 23  VAL   B CA    1 
ATOM   14172 C  C     . VAL   F 2  23  ? -9.587  70.382  -23.665  1.00 40.35  ? 23  VAL   B C     1 
ATOM   14173 O  O     . VAL   F 2  23  ? -8.950  71.372  -24.052  1.00 42.09  ? 23  VAL   B O     1 
ATOM   14174 C  CB    . VAL   F 2  23  ? -8.599  68.058  -23.663  1.00 34.13  ? 23  VAL   B CB    1 
ATOM   14175 C  CG1   . VAL   F 2  23  ? -7.969  68.484  -24.948  1.00 30.59  ? 23  VAL   B CG1   1 
ATOM   14176 C  CG2   . VAL   F 2  23  ? -7.683  67.118  -22.909  1.00 34.73  ? 23  VAL   B CG2   1 
ATOM   14177 N  N     . ILE   F 2  24  ? -10.868 70.196  -24.003  1.00 36.16  ? 24  ILE   B N     1 
ATOM   14178 C  CA    . ILE   F 2  24  ? -11.543 71.221  -24.794  1.00 41.94  ? 24  ILE   B CA    1 
ATOM   14179 C  C     . ILE   F 2  24  ? -11.825 72.452  -23.954  1.00 42.20  ? 24  ILE   B C     1 
ATOM   14180 O  O     . ILE   F 2  24  ? -11.959 73.550  -24.507  1.00 42.07  ? 24  ILE   B O     1 
ATOM   14181 C  CB    . ILE   F 2  24  ? -12.861 70.746  -25.448  1.00 30.43  ? 24  ILE   B CB    1 
ATOM   14182 C  CG1   . ILE   F 2  24  ? -13.887 70.386  -24.389  1.00 32.95  ? 24  ILE   B CG1   1 
ATOM   14183 C  CG2   . ILE   F 2  24  ? -12.622 69.591  -26.431  1.00 28.59  ? 24  ILE   B CG2   1 
ATOM   14184 C  CD1   . ILE   F 2  24  ? -15.298 70.330  -24.913  1.00 25.98  ? 24  ILE   B CD1   1 
ATOM   14185 N  N     . SER   F 2  25  ? -11.919 72.304  -22.629  1.00 40.97  ? 25  SER   B N     1 
ATOM   14186 C  CA    . SER   F 2  25  ? -12.084 73.476  -21.772  1.00 39.01  ? 25  SER   B CA    1 
ATOM   14187 C  C     . SER   F 2  25  ? -10.877 74.395  -21.894  1.00 44.08  ? 25  SER   B C     1 
ATOM   14188 O  O     . SER   F 2  25  ? -11.019 75.606  -22.089  1.00 46.67  ? 25  SER   B O     1 
ATOM   14189 C  CB    . SER   F 2  25  ? -12.305 73.053  -20.317  1.00 39.58  ? 25  SER   B CB    1 
ATOM   14190 O  OG    . SER   F 2  25  ? -13.637 72.609  -20.117  1.00 38.29  ? 25  SER   B OG    1 
ATOM   14191 N  N     . ASP   F 2  26  ? -9.675  73.826  -21.812  1.00 38.85  ? 26  ASP   B N     1 
ATOM   14192 C  CA    . ASP   F 2  26  ? -8.477  74.590  -22.131  1.00 38.93  ? 26  ASP   B CA    1 
ATOM   14193 C  C     . ASP   F 2  26  ? -8.528  75.141  -23.563  1.00 49.01  ? 26  ASP   B C     1 
ATOM   14194 O  O     . ASP   F 2  26  ? -8.324  76.340  -23.781  1.00 42.34  ? 26  ASP   B O     1 
ATOM   14195 C  CB    . ASP   F 2  26  ? -7.241  73.722  -21.904  1.00 38.29  ? 26  ASP   B CB    1 
ATOM   14196 C  CG    . ASP   F 2  26  ? -5.949  74.457  -22.202  1.00 61.91  ? 26  ASP   B CG    1 
ATOM   14197 O  OD1   . ASP   F 2  26  ? -5.650  75.449  -21.502  1.00 71.45  ? 26  ASP   B OD1   1 
ATOM   14198 O  OD2   . ASP   F 2  26  ? -5.227  74.042  -23.139  1.00 67.93  ? 26  ASP   B OD2   1 
ATOM   14199 N  N     . GLU   F 2  27  ? -8.806  74.286  -24.560  1.00 52.15  ? 27  GLU   B N     1 
ATOM   14200 C  CA    . GLU   F 2  27  ? -8.818  74.775  -25.942  1.00 45.14  ? 27  GLU   B CA    1 
ATOM   14201 C  C     . GLU   F 2  27  ? -9.680  76.024  -26.083  1.00 46.12  ? 27  GLU   B C     1 
ATOM   14202 O  O     . GLU   F 2  27  ? -9.340  76.932  -26.851  1.00 47.01  ? 27  GLU   B O     1 
ATOM   14203 C  CB    . GLU   F 2  27  ? -9.314  73.695  -26.912  1.00 38.22  ? 27  GLU   B CB    1 
ATOM   14204 C  CG    . GLU   F 2  27  ? -8.416  72.483  -27.009  1.00 35.18  ? 27  GLU   B CG    1 
ATOM   14205 C  CD    . GLU   F 2  27  ? -8.653  71.654  -28.260  1.00 38.22  ? 27  GLU   B CD    1 
ATOM   14206 O  OE1   . GLU   F 2  27  ? -9.609  71.938  -29.033  1.00 35.31  ? 27  GLU   B OE1   1 
ATOM   14207 O  OE2   . GLU   F 2  27  ? -7.849  70.725  -28.484  1.00 38.79  ? 27  GLU   B OE2   1 
ATOM   14208 N  N     . HIS   F 2  28  ? -10.804 76.081  -25.359  1.00 42.08  ? 28  HIS   B N     1 
ATOM   14209 C  CA    . HIS   F 2  28  ? -11.755 77.178  -25.448  1.00 38.02  ? 28  HIS   B CA    1 
ATOM   14210 C  C     . HIS   F 2  28  ? -11.489 78.266  -24.423  1.00 45.21  ? 28  HIS   B C     1 
ATOM   14211 O  O     . HIS   F 2  28  ? -12.236 79.243  -24.373  1.00 45.58  ? 28  HIS   B O     1 
ATOM   14212 C  CB    . HIS   F 2  28  ? -13.189 76.666  -25.276  1.00 39.90  ? 28  HIS   B CB    1 
ATOM   14213 C  CG    . HIS   F 2  28  ? -13.704 75.895  -26.451  1.00 43.28  ? 28  HIS   B CG    1 
ATOM   14214 N  ND1   . HIS   F 2  28  ? -14.308 76.501  -27.534  1.00 43.28  ? 28  HIS   B ND1   1 
ATOM   14215 C  CD2   . HIS   F 2  28  ? -13.705 74.568  -26.714  1.00 40.78  ? 28  HIS   B CD2   1 
ATOM   14216 C  CE1   . HIS   F 2  28  ? -14.653 75.580  -28.416  1.00 43.25  ? 28  HIS   B CE1   1 
ATOM   14217 N  NE2   . HIS   F 2  28  ? -14.295 74.399  -27.945  1.00 44.41  ? 28  HIS   B NE2   1 
ATOM   14218 N  N     . GLY   F 2  29  ? -10.454 78.124  -23.603  1.00 45.21  ? 29  GLY   B N     1 
ATOM   14219 C  CA    . GLY   F 2  29  ? -10.111 79.171  -22.663  1.00 50.30  ? 29  GLY   B CA    1 
ATOM   14220 C  C     . GLY   F 2  29  ? -10.941 79.233  -21.398  1.00 52.60  ? 29  GLY   B C     1 
ATOM   14221 O  O     . GLY   F 2  29  ? -10.973 80.284  -20.746  1.00 56.58  ? 29  GLY   B O     1 
ATOM   14222 N  N     . ILE   F 2  30  ? -11.601 78.143  -21.016  1.00 41.23  ? 30  ILE   B N     1 
ATOM   14223 C  CA    . ILE   F 2  30  ? -12.373 78.082  -19.781  1.00 48.37  ? 30  ILE   B CA    1 
ATOM   14224 C  C     . ILE   F 2  30  ? -11.535 77.400  -18.706  1.00 52.74  ? 30  ILE   B C     1 
ATOM   14225 O  O     . ILE   F 2  30  ? -11.000 76.303  -18.924  1.00 41.04  ? 30  ILE   B O     1 
ATOM   14226 C  CB    . ILE   F 2  30  ? -13.704 77.342  -19.991  1.00 49.09  ? 30  ILE   B CB    1 
ATOM   14227 C  CG1   . ILE   F 2  30  ? -14.644 78.173  -20.864  1.00 55.91  ? 30  ILE   B CG1   1 
ATOM   14228 C  CG2   . ILE   F 2  30  ? -14.356 77.050  -18.662  1.00 49.34  ? 30  ILE   B CG2   1 
ATOM   14229 C  CD1   . ILE   F 2  30  ? -14.157 78.338  -22.278  1.00 56.03  ? 30  ILE   B CD1   1 
ATOM   14230 N  N     . ASP   F 2  31  ? -11.416 78.047  -17.546  1.00 49.56  ? 31  ASP   B N     1 
ATOM   14231 C  CA    . ASP   F 2  31  ? -10.671 77.479  -16.430  1.00 53.47  ? 31  ASP   B CA    1 
ATOM   14232 C  C     . ASP   F 2  31  ? -11.592 76.680  -15.523  1.00 54.39  ? 31  ASP   B C     1 
ATOM   14233 O  O     . ASP   F 2  31  ? -12.821 76.706  -15.670  1.00 46.47  ? 31  ASP   B O     1 
ATOM   14234 C  CB    . ASP   F 2  31  ? -9.945  78.583  -15.656  1.00 53.48  ? 31  ASP   B CB    1 
ATOM   14235 C  CG    . ASP   F 2  31  ? -10.886 79.561  -14.925  1.00 53.76  ? 31  ASP   B CG    1 
ATOM   14236 O  OD1   . ASP   F 2  31  ? -12.073 79.268  -14.634  1.00 53.69  ? 31  ASP   B OD1   1 
ATOM   14237 O  OD2   . ASP   F 2  31  ? -10.393 80.659  -14.622  1.00 50.75  ? 31  ASP   B OD2   1 
ATOM   14238 N  N     . PRO   F 2  32  ? -11.012 75.952  -14.561  1.00 47.86  ? 32  PRO   B N     1 
ATOM   14239 C  CA    . PRO   F 2  32  ? -11.836 75.125  -13.665  1.00 48.01  ? 32  PRO   B CA    1 
ATOM   14240 C  C     . PRO   F 2  32  ? -13.058 75.834  -13.112  1.00 55.31  ? 32  PRO   B C     1 
ATOM   14241 O  O     . PRO   F 2  32  ? -14.160 75.280  -13.179  1.00 62.02  ? 32  PRO   B O     1 
ATOM   14242 C  CB    . PRO   F 2  32  ? -10.845 74.732  -12.568  1.00 47.48  ? 32  PRO   B CB    1 
ATOM   14243 C  CG    . PRO   F 2  32  ? -9.529  74.721  -13.248  1.00 46.94  ? 32  PRO   B CG    1 
ATOM   14244 C  CD    . PRO   F 2  32  ? -9.574  75.812  -14.284  1.00 47.06  ? 32  PRO   B CD    1 
ATOM   14245 N  N     . THR   F 2  33  ? -12.904 77.048  -12.576  1.00 64.30  ? 33  THR   B N     1 
ATOM   14246 C  CA    . THR   F 2  33  ? -14.052 77.807  -12.081  1.00 58.72  ? 33  THR   B CA    1 
ATOM   14247 C  C     . THR   F 2  33  ? -15.034 78.187  -13.185  1.00 56.98  ? 33  THR   B C     1 
ATOM   14248 O  O     . THR   F 2  33  ? -16.101 78.737  -12.876  1.00 50.36  ? 33  THR   B O     1 
ATOM   14249 C  CB    . THR   F 2  33  ? -13.592 79.080  -11.371  1.00 53.99  ? 33  THR   B CB    1 
ATOM   14250 O  OG1   . THR   F 2  33  ? -13.973 80.223  -12.155  1.00 53.07  ? 33  THR   B OG1   1 
ATOM   14251 C  CG2   . THR   F 2  33  ? -12.084 79.068  -11.189  1.00 45.47  ? 33  THR   B CG2   1 
ATOM   14252 N  N     . GLY   F 2  34  ? -14.688 77.946  -14.450  1.00 54.67  ? 34  GLY   B N     1 
ATOM   14253 C  CA    . GLY   F 2  34  ? -15.642 78.064  -15.536  1.00 55.18  ? 34  GLY   B CA    1 
ATOM   14254 C  C     . GLY   F 2  34  ? -15.739 79.418  -16.199  1.00 57.81  ? 34  GLY   B C     1 
ATOM   14255 O  O     . GLY   F 2  34  ? -16.798 79.753  -16.746  1.00 61.23  ? 34  GLY   B O     1 
ATOM   14256 N  N     . SER   F 2  35  ? -14.669 80.209  -16.183  1.00 53.59  ? 35  SER   B N     1 
ATOM   14257 C  CA    . SER   F 2  35  ? -14.706 81.562  -16.713  1.00 58.23  ? 35  SER   B CA    1 
ATOM   14258 C  C     . SER   F 2  35  ? -13.760 81.673  -17.898  1.00 65.26  ? 35  SER   B C     1 
ATOM   14259 O  O     . SER   F 2  35  ? -12.702 81.035  -17.923  1.00 69.00  ? 35  SER   B O     1 
ATOM   14260 C  CB    . SER   F 2  35  ? -14.343 82.582  -15.630  1.00 59.27  ? 35  SER   B CB    1 
ATOM   14261 O  OG    . SER   F 2  35  ? -15.391 82.679  -14.673  1.00 66.82  ? 35  SER   B OG    1 
ATOM   14262 N  N     . TYR   F 2  36  ? -14.147 82.473  -18.886  1.00 60.61  ? 36  TYR   B N     1 
ATOM   14263 C  CA    . TYR   F 2  36  ? -13.339 82.597  -20.087  1.00 56.50  ? 36  TYR   B CA    1 
ATOM   14264 C  C     . TYR   F 2  36  ? -12.140 83.488  -19.812  1.00 51.69  ? 36  TYR   B C     1 
ATOM   14265 O  O     . TYR   F 2  36  ? -12.292 84.597  -19.300  1.00 56.41  ? 36  TYR   B O     1 
ATOM   14266 C  CB    . TYR   F 2  36  ? -14.160 83.160  -21.254  1.00 60.87  ? 36  TYR   B CB    1 
ATOM   14267 C  CG    . TYR   F 2  36  ? -13.315 83.367  -22.496  1.00 56.08  ? 36  TYR   B CG    1 
ATOM   14268 C  CD1   . TYR   F 2  36  ? -12.641 82.302  -23.078  1.00 55.04  ? 36  TYR   B CD1   1 
ATOM   14269 C  CD2   . TYR   F 2  36  ? -13.167 84.624  -23.062  1.00 47.32  ? 36  TYR   B CD2   1 
ATOM   14270 C  CE1   . TYR   F 2  36  ? -11.849 82.483  -24.186  1.00 58.65  ? 36  TYR   B CE1   1 
ATOM   14271 C  CE2   . TYR   F 2  36  ? -12.379 84.815  -24.170  1.00 48.24  ? 36  TYR   B CE2   1 
ATOM   14272 C  CZ    . TYR   F 2  36  ? -11.717 83.743  -24.732  1.00 60.55  ? 36  TYR   B CZ    1 
ATOM   14273 O  OH    . TYR   F 2  36  ? -10.920 83.921  -25.849  1.00 62.91  ? 36  TYR   B OH    1 
ATOM   14274 N  N     . HIS   F 2  37  ? -10.951 83.007  -20.165  1.00 55.76  ? 37  HIS   B N     1 
ATOM   14275 C  CA    . HIS   F 2  37  ? -9.731  83.792  -20.074  1.00 52.93  ? 37  HIS   B CA    1 
ATOM   14276 C  C     . HIS   F 2  37  ? -8.829  83.489  -21.271  1.00 60.50  ? 37  HIS   B C     1 
ATOM   14277 O  O     . HIS   F 2  37  ? -7.700  83.040  -21.124  1.00 71.17  ? 37  HIS   B O     1 
ATOM   14278 C  CB    . HIS   F 2  37  ? -9.005  83.514  -18.762  1.00 54.49  ? 37  HIS   B CB    1 
ATOM   14279 C  CG    . HIS   F 2  37  ? -9.602  84.227  -17.590  1.00 71.23  ? 37  HIS   B CG    1 
ATOM   14280 N  ND1   . HIS   F 2  37  ? -10.872 83.960  -17.123  1.00 74.31  ? 37  HIS   B ND1   1 
ATOM   14281 C  CD2   . HIS   F 2  37  ? -9.112  85.214  -16.804  1.00 67.40  ? 37  HIS   B CD2   1 
ATOM   14282 C  CE1   . HIS   F 2  37  ? -11.137 84.746  -16.095  1.00 64.56  ? 37  HIS   B CE1   1 
ATOM   14283 N  NE2   . HIS   F 2  37  ? -10.084 85.515  -15.879  1.00 74.48  ? 37  HIS   B NE2   1 
ATOM   14284 N  N     . GLY   F 2  38  ? -9.329  83.751  -22.485  1.00 56.30  ? 38  GLY   B N     1 
ATOM   14285 C  CA    . GLY   F 2  38  ? -8.630  83.403  -23.701  1.00 58.88  ? 38  GLY   B CA    1 
ATOM   14286 C  C     . GLY   F 2  38  ? -8.390  84.598  -24.614  1.00 57.16  ? 38  GLY   B C     1 
ATOM   14287 O  O     . GLY   F 2  38  ? -8.953  85.681  -24.425  1.00 50.74  ? 38  GLY   B O     1 
ATOM   14288 N  N     . ASP   F 2  39  ? -7.550  84.369  -25.632  1.00 64.07  ? 39  ASP   B N     1 
ATOM   14289 C  CA    . ASP   F 2  39  ? -7.067  85.420  -26.527  1.00 60.17  ? 39  ASP   B CA    1 
ATOM   14290 C  C     . ASP   F 2  39  ? -7.434  85.165  -27.983  1.00 61.86  ? 39  ASP   B C     1 
ATOM   14291 O  O     . ASP   F 2  39  ? -6.559  85.119  -28.855  1.00 63.78  ? 39  ASP   B O     1 
ATOM   14292 C  CB    . ASP   F 2  39  ? -5.548  85.576  -26.404  1.00 68.86  ? 39  ASP   B CB    1 
ATOM   14293 C  CG    . ASP   F 2  39  ? -4.819  84.243  -26.338  1.00 72.70  ? 39  ASP   B CG    1 
ATOM   14294 O  OD1   . ASP   F 2  39  ? -5.329  83.241  -26.897  1.00 73.56  ? 39  ASP   B OD1   1 
ATOM   14295 O  OD2   . ASP   F 2  39  ? -3.735  84.204  -25.709  1.00 65.55  ? 39  ASP   B OD2   1 
ATOM   14296 N  N     . SER   F 2  40  ? -8.730  85.018  -28.248  1.00 56.87  ? 40  SER   B N     1 
ATOM   14297 C  CA    . SER   F 2  40  ? -9.250  84.799  -29.589  1.00 53.06  ? 40  SER   B CA    1 
ATOM   14298 C  C     . SER   F 2  40  ? -10.759 84.686  -29.509  1.00 65.42  ? 40  SER   B C     1 
ATOM   14299 O  O     . SER   F 2  40  ? -11.289 83.909  -28.705  1.00 64.63  ? 40  SER   B O     1 
ATOM   14300 C  CB    . SER   F 2  40  ? -8.662  83.539  -30.228  1.00 63.74  ? 40  SER   B CB    1 
ATOM   14301 O  OG    . SER   F 2  40  ? -9.335  83.206  -31.440  1.00 59.74  ? 40  SER   B OG    1 
ATOM   14302 N  N     . ASP   F 2  41  ? -11.464 85.475  -30.318  1.00 71.79  ? 41  ASP   B N     1 
ATOM   14303 C  CA    . ASP   F 2  41  ? -12.912 85.340  -30.386  1.00 69.73  ? 41  ASP   B CA    1 
ATOM   14304 C  C     . ASP   F 2  41  ? -13.321 84.007  -31.007  1.00 66.88  ? 41  ASP   B C     1 
ATOM   14305 O  O     . ASP   F 2  41  ? -14.457 83.554  -30.802  1.00 59.34  ? 41  ASP   B O     1 
ATOM   14306 C  CB    . ASP   F 2  41  ? -13.490 86.533  -31.147  1.00 63.73  ? 41  ASP   B CB    1 
ATOM   14307 C  CG    . ASP   F 2  41  ? -13.264 87.852  -30.409  1.00 86.95  ? 41  ASP   B CG    1 
ATOM   14308 O  OD1   . ASP   F 2  41  ? -13.439 87.888  -29.166  1.00 81.76  ? 41  ASP   B OD1   1 
ATOM   14309 O  OD2   . ASP   F 2  41  ? -12.896 88.850  -31.066  1.00 93.97  ? 41  ASP   B OD2   1 
ATOM   14310 N  N     . LEU   F 2  42  ? -12.401 83.362  -31.736  1.00 67.72  ? 42  LEU   B N     1 
ATOM   14311 C  CA    . LEU   F 2  42  ? -12.644 82.025  -32.268  1.00 60.37  ? 42  LEU   B CA    1 
ATOM   14312 C  C     . LEU   F 2  42  ? -12.932 81.025  -31.153  1.00 50.78  ? 42  LEU   B C     1 
ATOM   14313 O  O     . LEU   F 2  42  ? -13.805 80.158  -31.289  1.00 46.18  ? 42  LEU   B O     1 
ATOM   14314 C  CB    . LEU   F 2  42  ? -11.438 81.585  -33.099  1.00 54.17  ? 42  LEU   B CB    1 
ATOM   14315 C  CG    . LEU   F 2  42  ? -11.788 81.383  -34.576  1.00 66.51  ? 42  LEU   B CG    1 
ATOM   14316 C  CD1   . LEU   F 2  42  ? -12.412 82.667  -35.205  1.00 49.62  ? 42  LEU   B CD1   1 
ATOM   14317 C  CD2   . LEU   F 2  42  ? -10.581 80.856  -35.364  1.00 53.07  ? 42  LEU   B CD2   1 
ATOM   14318 N  N     . GLN   F 2  43  ? -12.203 81.133  -30.044  1.00 51.62  ? 45  GLN   B N     1 
ATOM   14319 C  CA    . GLN   F 2  43  ? -12.431 80.246  -28.914  1.00 49.40  ? 45  GLN   B CA    1 
ATOM   14320 C  C     . GLN   F 2  43  ? -13.865 80.326  -28.404  1.00 49.28  ? 45  GLN   B C     1 
ATOM   14321 O  O     . GLN   F 2  43  ? -14.425 79.312  -27.973  1.00 52.83  ? 45  GLN   B O     1 
ATOM   14322 C  CB    . GLN   F 2  43  ? -11.450 80.571  -27.795  1.00 52.19  ? 45  GLN   B CB    1 
ATOM   14323 C  CG    . GLN   F 2  43  ? -10.106 79.919  -27.972  1.00 55.32  ? 45  GLN   B CG    1 
ATOM   14324 C  CD    . GLN   F 2  43  ? -9.036  80.595  -27.164  1.00 58.12  ? 45  GLN   B CD    1 
ATOM   14325 O  OE1   . GLN   F 2  43  ? -9.317  81.178  -26.121  1.00 52.78  ? 45  GLN   B OE1   1 
ATOM   14326 N  NE2   . GLN   F 2  43  ? -7.794  80.551  -27.657  1.00 70.62  ? 45  GLN   B NE2   1 
ATOM   14327 N  N     . LEU   F 2  44  ? -14.482 81.510  -28.438  1.00 49.98  ? 46  LEU   B N     1 
ATOM   14328 C  CA    . LEU   F 2  44  ? -15.840 81.663  -27.911  1.00 49.31  ? 46  LEU   B CA    1 
ATOM   14329 C  C     . LEU   F 2  44  ? -16.930 81.546  -28.963  1.00 40.50  ? 46  LEU   B C     1 
ATOM   14330 O  O     . LEU   F 2  44  ? -18.097 81.388  -28.593  1.00 41.36  ? 46  LEU   B O     1 
ATOM   14331 C  CB    . LEU   F 2  44  ? -16.013 83.015  -27.194  1.00 39.28  ? 46  LEU   B CB    1 
ATOM   14332 C  CG    . LEU   F 2  44  ? -15.580 83.047  -25.725  1.00 51.22  ? 46  LEU   B CG    1 
ATOM   14333 C  CD1   . LEU   F 2  44  ? -15.800 84.428  -25.109  1.00 41.03  ? 46  LEU   B CD1   1 
ATOM   14334 C  CD2   . LEU   F 2  44  ? -16.302 81.951  -24.925  1.00 49.22  ? 46  LEU   B CD2   1 
ATOM   14335 N  N     . GLU   F 2  45  ? -16.587 81.623  -30.249  1.00 39.65  ? 47  GLU   B N     1 
ATOM   14336 C  CA    . GLU   F 2  45  ? -17.608 81.812  -31.277  1.00 43.13  ? 47  GLU   B CA    1 
ATOM   14337 C  C     . GLU   F 2  45  ? -18.685 80.726  -31.244  1.00 47.05  ? 47  GLU   B C     1 
ATOM   14338 O  O     . GLU   F 2  45  ? -19.871 81.022  -31.433  1.00 46.29  ? 47  GLU   B O     1 
ATOM   14339 C  CB    . GLU   F 2  45  ? -16.955 81.881  -32.656  1.00 53.05  ? 47  GLU   B CB    1 
ATOM   14340 C  CG    . GLU   F 2  45  ? -17.938 82.164  -33.786  1.00 57.36  ? 47  GLU   B CG    1 
ATOM   14341 C  CD    . GLU   F 2  45  ? -17.239 82.469  -35.096  1.00 68.87  ? 47  GLU   B CD    1 
ATOM   14342 O  OE1   . GLU   F 2  45  ? -16.190 83.154  -35.056  1.00 77.48  ? 47  GLU   B OE1   1 
ATOM   14343 O  OE2   . GLU   F 2  45  ? -17.728 82.017  -36.162  1.00 72.08  ? 47  GLU   B OE2   1 
ATOM   14344 N  N     . ARG   F 2  46  ? -18.301 79.459  -31.029  1.00 46.44  ? 48  ARG   B N     1 
ATOM   14345 C  CA    . ARG   F 2  46  ? -19.261 78.354  -30.980  1.00 40.75  ? 48  ARG   B CA    1 
ATOM   14346 C  C     . ARG   F 2  46  ? -19.215 77.620  -29.637  1.00 54.57  ? 48  ARG   B C     1 
ATOM   14347 O  O     . ARG   F 2  46  ? -19.539 76.429  -29.554  1.00 47.55  ? 48  ARG   B O     1 
ATOM   14348 C  CB    . ARG   F 2  46  ? -19.030 77.368  -32.126  1.00 36.38  ? 48  ARG   B CB    1 
ATOM   14349 C  CG    . ARG   F 2  46  ? -19.137 77.959  -33.518  1.00 44.62  ? 48  ARG   B CG    1 
ATOM   14350 C  CD    . ARG   F 2  46  ? -19.895 77.017  -34.451  1.00 46.51  ? 48  ARG   B CD    1 
ATOM   14351 N  NE    . ARG   F 2  46  ? -19.020 76.009  -35.040  1.00 46.90  ? 48  ARG   B NE    1 
ATOM   14352 C  CZ    . ARG   F 2  46  ? -19.438 74.865  -35.572  1.00 49.08  ? 48  ARG   B CZ    1 
ATOM   14353 N  NH1   . ARG   F 2  46  ? -20.718 74.506  -35.546  1.00 44.34  ? 48  ARG   B NH1   1 
ATOM   14354 N  NH2   . ARG   F 2  46  ? -18.546 74.051  -36.135  1.00 42.92  ? 48  ARG   B NH2   1 
ATOM   14355 N  N     . ILE   F 2  47  ? -18.823 78.327  -28.571  1.00 52.03  ? 49  ILE   B N     1 
ATOM   14356 C  CA    . ILE   F 2  47  ? -18.774 77.743  -27.239  1.00 43.58  ? 49  ILE   B CA    1 
ATOM   14357 C  C     . ILE   F 2  47  ? -20.132 77.201  -26.823  1.00 45.07  ? 49  ILE   B C     1 
ATOM   14358 O  O     . ILE   F 2  47  ? -20.225 76.372  -25.910  1.00 49.89  ? 49  ILE   B O     1 
ATOM   14359 C  CB    . ILE   F 2  47  ? -18.239 78.785  -26.231  1.00 48.94  ? 49  ILE   B CB    1 
ATOM   14360 C  CG1   . ILE   F 2  47  ? -17.681 78.089  -24.993  1.00 41.37  ? 49  ILE   B CG1   1 
ATOM   14361 C  CG2   . ILE   F 2  47  ? -19.316 79.814  -25.859  1.00 37.65  ? 49  ILE   B CG2   1 
ATOM   14362 C  CD1   . ILE   F 2  47  ? -16.333 77.493  -25.231  1.00 46.93  ? 49  ILE   B CD1   1 
ATOM   14363 N  N     . ASN   F 2  48  ? -21.197 77.638  -27.482  1.00 48.21  ? 50  ASN   B N     1 
ATOM   14364 C  CA    . ASN   F 2  48  ? -22.537 77.184  -27.150  1.00 41.29  ? 50  ASN   B CA    1 
ATOM   14365 C  C     . ASN   F 2  48  ? -22.775 75.727  -27.497  1.00 43.76  ? 50  ASN   B C     1 
ATOM   14366 O  O     . ASN   F 2  48  ? -23.785 75.166  -27.066  1.00 45.29  ? 50  ASN   B O     1 
ATOM   14367 C  CB    . ASN   F 2  48  ? -23.562 78.045  -27.878  1.00 54.78  ? 50  ASN   B CB    1 
ATOM   14368 C  CG    . ASN   F 2  48  ? -24.515 78.726  -26.926  1.00 75.95  ? 50  ASN   B CG    1 
ATOM   14369 O  OD1   . ASN   F 2  48  ? -25.735 78.707  -27.129  1.00 74.11  ? 50  ASN   B OD1   1 
ATOM   14370 N  ND2   . ASN   F 2  48  ? -23.964 79.319  -25.857  1.00 71.46  ? 50  ASN   B ND2   1 
ATOM   14371 N  N     . VAL   F 2  49  ? -21.894 75.102  -28.274  1.00 41.94  ? 51  VAL   B N     1 
ATOM   14372 C  CA    . VAL   F 2  49  ? -22.157 73.727  -28.677  1.00 39.04  ? 51  VAL   B CA    1 
ATOM   14373 C  C     . VAL   F 2  49  ? -21.927 72.762  -27.517  1.00 45.03  ? 51  VAL   B C     1 
ATOM   14374 O  O     . VAL   F 2  49  ? -22.565 71.696  -27.447  1.00 42.34  ? 51  VAL   B O     1 
ATOM   14375 C  CB    . VAL   F 2  49  ? -21.304 73.371  -29.901  1.00 38.21  ? 51  VAL   B CB    1 
ATOM   14376 C  CG1   . VAL   F 2  49  ? -21.403 71.889  -30.211  1.00 39.73  ? 51  VAL   B CG1   1 
ATOM   14377 C  CG2   . VAL   F 2  49  ? -21.731 74.221  -31.099  1.00 38.50  ? 51  VAL   B CG2   1 
ATOM   14378 N  N     . TYR   F 2  50  ? -21.040 73.112  -26.580  1.00 30.19  ? 52  TYR   B N     1 
ATOM   14379 C  CA    . TYR   F 2  50  ? -20.747 72.232  -25.466  1.00 33.70  ? 52  TYR   B CA    1 
ATOM   14380 C  C     . TYR   F 2  50  ? -21.003 72.843  -24.083  1.00 43.38  ? 52  TYR   B C     1 
ATOM   14381 O  O     . TYR   F 2  50  ? -21.154 72.078  -23.124  1.00 39.09  ? 52  TYR   B O     1 
ATOM   14382 C  CB    . TYR   F 2  50  ? -19.293 71.718  -25.560  1.00 28.04  ? 52  TYR   B CB    1 
ATOM   14383 C  CG    . TYR   F 2  50  ? -19.148 70.562  -26.552  1.00 33.67  ? 52  TYR   B CG    1 
ATOM   14384 C  CD1   . TYR   F 2  50  ? -19.456 69.248  -26.194  1.00 29.90  ? 52  TYR   B CD1   1 
ATOM   14385 C  CD2   . TYR   F 2  50  ? -18.732 70.793  -27.856  1.00 39.27  ? 52  TYR   B CD2   1 
ATOM   14386 C  CE1   . TYR   F 2  50  ? -19.350 68.206  -27.113  1.00 32.33  ? 52  TYR   B CE1   1 
ATOM   14387 C  CE2   . TYR   F 2  50  ? -18.621 69.762  -28.784  1.00 34.76  ? 52  TYR   B CE2   1 
ATOM   14388 C  CZ    . TYR   F 2  50  ? -18.930 68.476  -28.419  1.00 36.54  ? 52  TYR   B CZ    1 
ATOM   14389 O  OH    . TYR   F 2  50  ? -18.807 67.484  -29.374  1.00 26.87  ? 52  TYR   B OH    1 
ATOM   14390 N  N     . TYR   F 2  51  ? -21.098 74.174  -23.952  1.00 39.88  ? 53  TYR   B N     1 
ATOM   14391 C  CA    . TYR   F 2  51  ? -21.288 74.834  -22.662  1.00 40.56  ? 53  TYR   B CA    1 
ATOM   14392 C  C     . TYR   F 2  51  ? -22.595 75.631  -22.615  1.00 45.94  ? 53  TYR   B C     1 
ATOM   14393 O  O     . TYR   F 2  51  ? -22.976 76.279  -23.597  1.00 55.30  ? 53  TYR   B O     1 
ATOM   14394 C  CB    . TYR   F 2  51  ? -20.116 75.768  -22.355  1.00 42.03  ? 53  TYR   B CB    1 
ATOM   14395 C  CG    . TYR   F 2  51  ? -18.754 75.091  -22.323  1.00 41.63  ? 53  TYR   B CG    1 
ATOM   14396 C  CD1   . TYR   F 2  51  ? -18.049 74.845  -23.497  1.00 34.56  ? 53  TYR   B CD1   1 
ATOM   14397 C  CD2   . TYR   F 2  51  ? -18.164 74.721  -21.116  1.00 38.65  ? 53  TYR   B CD2   1 
ATOM   14398 C  CE1   . TYR   F 2  51  ? -16.812 74.236  -23.476  1.00 37.29  ? 53  TYR   B CE1   1 
ATOM   14399 C  CE2   . TYR   F 2  51  ? -16.917 74.109  -21.083  1.00 40.54  ? 53  TYR   B CE2   1 
ATOM   14400 C  CZ    . TYR   F 2  51  ? -16.245 73.870  -22.266  1.00 43.11  ? 53  TYR   B CZ    1 
ATOM   14401 O  OH    . TYR   F 2  51  ? -15.003 73.274  -22.245  1.00 36.66  ? 53  TYR   B OH    1 
ATOM   14402 N  N     . ASN   F 2  52  ? -23.284 75.584  -21.471  1.00 50.17  ? 54  ASN   B N     1 
ATOM   14403 C  CA    . ASN   F 2  52  ? -24.415 76.476  -21.220  1.00 49.60  ? 54  ASN   B CA    1 
ATOM   14404 C  C     . ASN   F 2  52  ? -23.917 77.827  -20.734  1.00 53.70  ? 54  ASN   B C     1 
ATOM   14405 O  O     . ASN   F 2  52  ? -22.854 77.936  -20.112  1.00 43.95  ? 54  ASN   B O     1 
ATOM   14406 C  CB    . ASN   F 2  52  ? -25.371 75.911  -20.172  1.00 39.68  ? 54  ASN   B CB    1 
ATOM   14407 C  CG    . ASN   F 2  52  ? -26.245 74.790  -20.705  1.00 43.96  ? 54  ASN   B CG    1 
ATOM   14408 O  OD1   . ASN   F 2  52  ? -26.868 74.909  -21.762  1.00 51.90  ? 54  ASN   B OD1   1 
ATOM   14409 N  ND2   . ASN   F 2  52  ? -26.302 73.686  -19.962  1.00 43.44  ? 54  ASN   B ND2   1 
ATOM   14410 N  N     . GLU   F 2  53  ? -24.709 78.861  -21.017  1.00 64.80  ? 55  GLU   B N     1 
ATOM   14411 C  CA    . GLU   F 2  53  ? -24.384 80.227  -20.624  1.00 64.94  ? 55  GLU   B CA    1 
ATOM   14412 C  C     . GLU   F 2  53  ? -24.972 80.497  -19.242  1.00 67.11  ? 55  GLU   B C     1 
ATOM   14413 O  O     . GLU   F 2  53  ? -26.181 80.336  -19.037  1.00 76.61  ? 55  GLU   B O     1 
ATOM   14414 C  CB    . GLU   F 2  53  ? -24.923 81.221  -21.653  1.00 74.41  ? 55  GLU   B CB    1 
ATOM   14415 C  CG    . GLU   F 2  53  ? -24.382 82.642  -21.509  1.00 83.66  ? 55  GLU   B CG    1 
ATOM   14416 C  CD    . GLU   F 2  53  ? -23.080 82.864  -22.268  1.00 88.37  ? 55  GLU   B CD    1 
ATOM   14417 O  OE1   . GLU   F 2  53  ? -22.858 82.157  -23.284  1.00 77.62  ? 55  GLU   B OE1   1 
ATOM   14418 O  OE2   . GLU   F 2  53  ? -22.287 83.748  -21.847  1.00 87.53  ? 55  GLU   B OE2   1 
ATOM   14419 N  N     . ALA   F 2  54  ? -24.120 80.891  -18.296  1.00 62.61  ? 56  ALA   B N     1 
ATOM   14420 C  CA    . ALA   F 2  54  ? -24.540 81.205  -16.936  1.00 72.27  ? 56  ALA   B CA    1 
ATOM   14421 C  C     . ALA   F 2  54  ? -24.237 82.666  -16.615  1.00 79.93  ? 56  ALA   B C     1 
ATOM   14422 O  O     . ALA   F 2  54  ? -23.605 83.385  -17.398  1.00 81.12  ? 56  ALA   B O     1 
ATOM   14423 C  CB    . ALA   F 2  54  ? -23.860 80.280  -15.918  1.00 71.39  ? 56  ALA   B CB    1 
ATOM   14424 N  N     . THR   F 2  55  ? -24.699 83.105  -15.443  1.00 77.60  ? 57  THR   B N     1 
ATOM   14425 C  CA    . THR   F 2  55  ? -24.586 84.507  -15.055  1.00 81.32  ? 57  THR   B CA    1 
ATOM   14426 C  C     . THR   F 2  55  ? -23.227 84.779  -14.426  1.00 80.81  ? 57  THR   B C     1 
ATOM   14427 O  O     . THR   F 2  55  ? -22.766 84.023  -13.566  1.00 78.32  ? 57  THR   B O     1 
ATOM   14428 C  CB    . THR   F 2  55  ? -25.696 84.891  -14.078  1.00 84.97  ? 57  THR   B CB    1 
ATOM   14429 O  OG1   . THR   F 2  55  ? -26.965 84.491  -14.610  1.00 102.40 ? 57  THR   B OG1   1 
ATOM   14430 C  CG2   . THR   F 2  55  ? -25.703 86.399  -13.848  1.00 81.62  ? 57  THR   B CG2   1 
ATOM   14431 N  N     . GLY   F 2  56  ? -22.602 85.873  -14.838  1.00 79.26  ? 58  GLY   B N     1 
ATOM   14432 C  CA    . GLY   F 2  56  ? -21.240 86.167  -14.455  1.00 72.95  ? 58  GLY   B CA    1 
ATOM   14433 C  C     . GLY   F 2  56  ? -20.224 85.905  -15.539  1.00 76.06  ? 58  GLY   B C     1 
ATOM   14434 O  O     . GLY   F 2  56  ? -19.025 85.838  -15.237  1.00 81.38  ? 58  GLY   B O     1 
ATOM   14435 N  N     . ASN   F 2  57  ? -20.659 85.781  -16.791  1.00 75.86  ? 59  ASN   B N     1 
ATOM   14436 C  CA    . ASN   F 2  57  ? -19.837 85.216  -17.853  1.00 81.82  ? 59  ASN   B CA    1 
ATOM   14437 C  C     . ASN   F 2  57  ? -19.149 83.944  -17.349  1.00 73.17  ? 59  ASN   B C     1 
ATOM   14438 O  O     . ASN   F 2  57  ? -17.940 83.880  -17.125  1.00 78.80  ? 59  ASN   B O     1 
ATOM   14439 C  CB    . ASN   F 2  57  ? -18.835 86.247  -18.385  1.00 81.08  ? 59  ASN   B CB    1 
ATOM   14440 C  CG    . ASN   F 2  57  ? -19.426 87.121  -19.487  1.00 88.88  ? 59  ASN   B CG    1 
ATOM   14441 O  OD1   . ASN   F 2  57  ? -20.182 86.641  -20.340  1.00 93.27  ? 59  ASN   B OD1   1 
ATOM   14442 N  ND2   . ASN   F 2  57  ? -19.085 88.408  -19.473  1.00 78.70  ? 59  ASN   B ND2   1 
ATOM   14443 N  N     . LYS   F 2  58  ? -19.995 82.939  -17.133  1.00 69.32  ? 60  LYS   B N     1 
ATOM   14444 C  CA    . LYS   F 2  58  ? -19.574 81.607  -16.729  1.00 65.23  ? 60  LYS   B CA    1 
ATOM   14445 C  C     . LYS   F 2  58  ? -20.141 80.589  -17.709  1.00 60.21  ? 60  LYS   B C     1 
ATOM   14446 O  O     . LYS   F 2  58  ? -21.245 80.764  -18.242  1.00 56.25  ? 60  LYS   B O     1 
ATOM   14447 C  CB    . LYS   F 2  58  ? -20.016 81.288  -15.287  1.00 62.99  ? 60  LYS   B CB    1 
ATOM   14448 C  CG    . LYS   F 2  58  ? -19.108 81.915  -14.226  1.00 67.06  ? 60  LYS   B CG    1 
ATOM   14449 C  CD    . LYS   F 2  58  ? -19.307 81.286  -12.856  1.00 57.78  ? 60  LYS   B CD    1 
ATOM   14450 C  CE    . LYS   F 2  58  ? -17.968 80.988  -12.173  1.00 68.05  ? 60  LYS   B CE    1 
ATOM   14451 N  NZ    . LYS   F 2  58  ? -17.082 82.184  -12.032  1.00 60.37  ? 60  LYS   B NZ    1 
ATOM   14452 N  N     . TYR   F 2  59  ? -19.366 79.540  -17.964  1.00 52.11  ? 61  TYR   B N     1 
ATOM   14453 C  CA    . TYR   F 2  59  ? -19.733 78.498  -18.911  1.00 45.21  ? 61  TYR   B CA    1 
ATOM   14454 C  C     . TYR   F 2  59  ? -19.708 77.156  -18.196  1.00 49.89  ? 61  TYR   B C     1 
ATOM   14455 O  O     . TYR   F 2  59  ? -18.695 76.787  -17.589  1.00 51.56  ? 61  TYR   B O     1 
ATOM   14456 C  CB    . TYR   F 2  59  ? -18.788 78.507  -20.111  1.00 44.15  ? 61  TYR   B CB    1 
ATOM   14457 C  CG    . TYR   F 2  59  ? -18.775 79.838  -20.809  1.00 47.25  ? 61  TYR   B CG    1 
ATOM   14458 C  CD1   . TYR   F 2  59  ? -19.714 80.142  -21.787  1.00 46.42  ? 61  TYR   B CD1   1 
ATOM   14459 C  CD2   . TYR   F 2  59  ? -17.847 80.805  -20.472  1.00 53.65  ? 61  TYR   B CD2   1 
ATOM   14460 C  CE1   . TYR   F 2  59  ? -19.719 81.355  -22.419  1.00 48.04  ? 61  TYR   B CE1   1 
ATOM   14461 C  CE2   . TYR   F 2  59  ? -17.844 82.030  -21.104  1.00 55.16  ? 61  TYR   B CE2   1 
ATOM   14462 C  CZ    . TYR   F 2  59  ? -18.782 82.303  -22.075  1.00 52.30  ? 61  TYR   B CZ    1 
ATOM   14463 O  OH    . TYR   F 2  59  ? -18.780 83.536  -22.702  1.00 60.36  ? 61  TYR   B OH    1 
ATOM   14464 N  N     . VAL   F 2  60  ? -20.821 76.440  -18.253  1.00 45.99  ? 62  VAL   B N     1 
ATOM   14465 C  CA    . VAL   F 2  60  ? -20.967 75.144  -17.599  1.00 43.69  ? 62  VAL   B CA    1 
ATOM   14466 C  C     . VAL   F 2  60  ? -21.030 74.081  -18.692  1.00 51.58  ? 62  VAL   B C     1 
ATOM   14467 O  O     . VAL   F 2  60  ? -21.869 74.187  -19.602  1.00 44.76  ? 62  VAL   B O     1 
ATOM   14468 C  CB    . VAL   F 2  60  ? -22.222 75.089  -16.700  1.00 46.15  ? 62  VAL   B CB    1 
ATOM   14469 C  CG1   . VAL   F 2  60  ? -22.223 73.821  -15.824  1.00 38.50  ? 62  VAL   B CG1   1 
ATOM   14470 C  CG2   . VAL   F 2  60  ? -22.370 76.361  -15.826  1.00 34.71  ? 62  VAL   B CG2   1 
ATOM   14471 N  N     . PRO   F 2  61  ? -20.168 73.062  -18.662  1.00 51.85  ? 63  PRO   B N     1 
ATOM   14472 C  CA    . PRO   F 2  61  ? -20.351 71.917  -19.568  1.00 39.14  ? 63  PRO   B CA    1 
ATOM   14473 C  C     . PRO   F 2  61  ? -21.793 71.444  -19.551  1.00 43.29  ? 63  PRO   B C     1 
ATOM   14474 O  O     . PRO   F 2  61  ? -22.377 71.224  -18.482  1.00 41.20  ? 63  PRO   B O     1 
ATOM   14475 C  CB    . PRO   F 2  61  ? -19.409 70.852  -18.998  1.00 29.17  ? 63  PRO   B CB    1 
ATOM   14476 C  CG    . PRO   F 2  61  ? -18.323 71.647  -18.319  1.00 49.06  ? 63  PRO   B CG    1 
ATOM   14477 C  CD    . PRO   F 2  61  ? -18.937 72.962  -17.856  1.00 44.29  ? 63  PRO   B CD    1 
ATOM   14478 N  N     . ARG   F 2  62  ? -22.377 71.312  -20.751  1.00 40.44  ? 64  ARG   B N     1 
ATOM   14479 C  CA    . ARG   F 2  62  ? -23.691 70.692  -20.927  1.00 33.72  ? 64  ARG   B CA    1 
ATOM   14480 C  C     . ARG   F 2  62  ? -23.524 69.172  -20.858  1.00 37.44  ? 64  ARG   B C     1 
ATOM   14481 O  O     . ARG   F 2  62  ? -23.744 68.431  -21.825  1.00 35.61  ? 64  ARG   B O     1 
ATOM   14482 C  CB    . ARG   F 2  62  ? -24.330 71.135  -22.231  1.00 31.07  ? 64  ARG   B CB    1 
ATOM   14483 C  CG    . ARG   F 2  62  ? -25.828 70.840  -22.303  1.00 33.26  ? 64  ARG   B CG    1 
ATOM   14484 C  CD    . ARG   F 2  62  ? -26.463 71.372  -23.593  1.00 46.73  ? 64  ARG   B CD    1 
ATOM   14485 N  NE    . ARG   F 2  62  ? -26.321 72.816  -23.792  1.00 46.03  ? 64  ARG   B NE    1 
ATOM   14486 C  CZ    . ARG   F 2  62  ? -25.419 73.377  -24.586  1.00 40.74  ? 64  ARG   B CZ    1 
ATOM   14487 N  NH1   . ARG   F 2  62  ? -24.524 72.656  -25.242  1.00 38.14  ? 64  ARG   B NH1   1 
ATOM   14488 N  NH2   . ARG   F 2  62  ? -25.410 74.695  -24.722  1.00 42.22  ? 64  ARG   B NH2   1 
ATOM   14489 N  N     . ALA   F 2  63  ? -23.149 68.715  -19.656  1.00 32.58  ? 65  ALA   B N     1 
ATOM   14490 C  CA    . ALA   F 2  63  ? -22.674 67.359  -19.418  1.00 30.71  ? 65  ALA   B CA    1 
ATOM   14491 C  C     . ALA   F 2  63  ? -23.466 66.692  -18.298  1.00 34.41  ? 65  ALA   B C     1 
ATOM   14492 O  O     . ALA   F 2  63  ? -23.774 67.305  -17.273  1.00 36.10  ? 65  ALA   B O     1 
ATOM   14493 C  CB    . ALA   F 2  63  ? -21.175 67.360  -19.069  1.00 29.89  ? 65  ALA   B CB    1 
ATOM   14494 N  N     . ILE   F 2  64  ? -23.780 65.423  -18.488  1.00 33.59  ? 66  ILE   B N     1 
ATOM   14495 C  CA    . ILE   F 2  64  ? -24.460 64.637  -17.473  1.00 36.53  ? 66  ILE   B CA    1 
ATOM   14496 C  C     . ILE   F 2  64  ? -23.558 63.466  -17.122  1.00 33.89  ? 66  ILE   B C     1 
ATOM   14497 O  O     . ILE   F 2  64  ? -23.082 62.750  -18.015  1.00 37.32  ? 66  ILE   B O     1 
ATOM   14498 C  CB    . ILE   F 2  64  ? -25.846 64.181  -17.958  1.00 34.14  ? 66  ILE   B CB    1 
ATOM   14499 C  CG1   . ILE   F 2  64  ? -26.585 65.395  -18.539  1.00 35.28  ? 66  ILE   B CG1   1 
ATOM   14500 C  CG2   . ILE   F 2  64  ? -26.630 63.565  -16.804  1.00 28.38  ? 66  ILE   B CG2   1 
ATOM   14501 C  CD1   . ILE   F 2  64  ? -27.942 65.074  -19.172  1.00 37.68  ? 66  ILE   B CD1   1 
ATOM   14502 N  N     . LEU   F 2  65  ? -23.293 63.297  -15.832  1.00 30.63  ? 67  LEU   B N     1 
ATOM   14503 C  CA    . LEU   F 2  65  ? -22.387 62.271  -15.337  1.00 32.37  ? 67  LEU   B CA    1 
ATOM   14504 C  C     . LEU   F 2  65  ? -23.187 61.193  -14.614  1.00 38.10  ? 67  LEU   B C     1 
ATOM   14505 O  O     . LEU   F 2  65  ? -23.940 61.489  -13.677  1.00 37.61  ? 67  LEU   B O     1 
ATOM   14506 C  CB    . LEU   F 2  65  ? -21.338 62.881  -14.418  1.00 32.02  ? 67  LEU   B CB    1 
ATOM   14507 C  CG    . LEU   F 2  65  ? -20.539 64.017  -15.049  1.00 36.84  ? 67  LEU   B CG    1 
ATOM   14508 C  CD1   . LEU   F 2  65  ? -21.354 65.312  -14.995  1.00 42.82  ? 67  LEU   B CD1   1 
ATOM   14509 C  CD2   . LEU   F 2  65  ? -19.189 64.207  -14.354  1.00 30.86  ? 67  LEU   B CD2   1 
ATOM   14510 N  N     . VAL   F 2  66  ? -23.007 59.944  -15.040  1.00 36.82  ? 68  VAL   B N     1 
ATOM   14511 C  CA    . VAL   F 2  66  ? -23.870 58.838  -14.643  1.00 32.69  ? 68  VAL   B CA    1 
ATOM   14512 C  C     . VAL   F 2  66  ? -23.022 57.631  -14.286  1.00 32.18  ? 68  VAL   B C     1 
ATOM   14513 O  O     . VAL   F 2  66  ? -22.096 57.281  -15.026  1.00 31.21  ? 68  VAL   B O     1 
ATOM   14514 C  CB    . VAL   F 2  66  ? -24.846 58.479  -15.772  1.00 35.85  ? 68  VAL   B CB    1 
ATOM   14515 C  CG1   . VAL   F 2  66  ? -25.759 57.331  -15.349  1.00 34.25  ? 68  VAL   B CG1   1 
ATOM   14516 C  CG2   . VAL   F 2  66  ? -25.624 59.728  -16.190  1.00 39.46  ? 68  VAL   B CG2   1 
ATOM   14517 N  N     . ASP   F 2  67  ? -23.350 56.983  -13.165  1.00 39.49  ? 69  ASP   B N     1 
ATOM   14518 C  CA    . ASP   F 2  67  ? -22.711 55.747  -12.718  1.00 33.53  ? 69  ASP   B CA    1 
ATOM   14519 C  C     . ASP   F 2  67  ? -23.546 55.143  -11.599  1.00 36.88  ? 69  ASP   B C     1 
ATOM   14520 O  O     . ASP   F 2  67  ? -24.184 55.864  -10.829  1.00 39.26  ? 69  ASP   B O     1 
ATOM   14521 C  CB    . ASP   F 2  67  ? -21.275 55.991  -12.234  1.00 26.35  ? 69  ASP   B CB    1 
ATOM   14522 C  CG    . ASP   F 2  67  ? -20.393 54.752  -12.336  1.00 32.29  ? 69  ASP   B CG    1 
ATOM   14523 O  OD1   . ASP   F 2  67  ? -20.911 53.632  -12.588  1.00 37.42  ? 69  ASP   B OD1   1 
ATOM   14524 O  OD2   . ASP   F 2  67  ? -19.161 54.902  -12.153  1.00 44.40  ? 69  ASP   B OD2   1 
ATOM   14525 N  N     . LEU   F 2  68  ? -23.533 53.815  -11.521  1.00 34.97  ? 70  LEU   B N     1 
ATOM   14526 C  CA    . LEU   F 2  68  ? -24.316 53.082  -10.538  1.00 34.65  ? 70  LEU   B CA    1 
ATOM   14527 C  C     . LEU   F 2  68  ? -23.592 52.895  -9.217   1.00 38.75  ? 70  LEU   B C     1 
ATOM   14528 O  O     . LEU   F 2  68  ? -24.139 52.235  -8.324   1.00 33.96  ? 70  LEU   B O     1 
ATOM   14529 C  CB    . LEU   F 2  68  ? -24.708 51.710  -11.091  1.00 36.02  ? 70  LEU   B CB    1 
ATOM   14530 C  CG    . LEU   F 2  68  ? -25.864 51.743  -12.087  1.00 32.70  ? 70  LEU   B CG    1 
ATOM   14531 C  CD1   . LEU   F 2  68  ? -26.048 50.390  -12.737  1.00 29.17  ? 70  LEU   B CD1   1 
ATOM   14532 C  CD2   . LEU   F 2  68  ? -27.120 52.167  -11.382  1.00 24.91  ? 70  LEU   B CD2   1 
ATOM   14533 N  N     . GLU   F 2  69  ? -22.378 53.420  -9.083   1.00 48.56  ? 71  GLU   B N     1 
ATOM   14534 C  CA    . GLU   F 2  69  ? -21.646 53.431  -7.825   1.00 46.40  ? 71  GLU   B CA    1 
ATOM   14535 C  C     . GLU   F 2  69  ? -20.967 54.776  -7.652   1.00 43.84  ? 71  GLU   B C     1 
ATOM   14536 O  O     . GLU   F 2  69  ? -20.707 55.483  -8.633   1.00 42.49  ? 71  GLU   B O     1 
ATOM   14537 C  CB    . GLU   F 2  69  ? -20.601 52.317  -7.741   1.00 46.21  ? 71  GLU   B CB    1 
ATOM   14538 C  CG    . GLU   F 2  69  ? -19.661 52.241  -8.901   1.00 43.64  ? 71  GLU   B CG    1 
ATOM   14539 C  CD    . GLU   F 2  69  ? -18.566 51.259  -8.616   1.00 54.26  ? 71  GLU   B CD    1 
ATOM   14540 O  OE1   . GLU   F 2  69  ? -18.320 51.015  -7.416   1.00 60.17  ? 71  GLU   B OE1   1 
ATOM   14541 O  OE2   . GLU   F 2  69  ? -17.969 50.718  -9.570   1.00 54.55  ? 71  GLU   B OE2   1 
ATOM   14542 N  N     . PRO   F 2  70  ? -20.667 55.159  -6.410   1.00 50.83  ? 72  PRO   B N     1 
ATOM   14543 C  CA    . PRO   F 2  70  ? -20.345 56.567  -6.140   1.00 52.93  ? 72  PRO   B CA    1 
ATOM   14544 C  C     . PRO   F 2  70  ? -18.899 56.960  -6.403   1.00 59.73  ? 72  PRO   B C     1 
ATOM   14545 O  O     . PRO   F 2  70  ? -18.645 58.151  -6.636   1.00 55.21  ? 72  PRO   B O     1 
ATOM   14546 C  CB    . PRO   F 2  70  ? -20.708 56.724  -4.657   1.00 49.81  ? 72  PRO   B CB    1 
ATOM   14547 C  CG    . PRO   F 2  70  ? -20.545 55.383  -4.092   1.00 46.64  ? 72  PRO   B CG    1 
ATOM   14548 C  CD    . PRO   F 2  70  ? -20.945 54.412  -5.174   1.00 58.99  ? 72  PRO   B CD    1 
ATOM   14549 N  N     . GLY   F 2  71  ? -17.943 56.032  -6.391   1.00 55.62  ? 73  GLY   B N     1 
ATOM   14550 C  CA    . GLY   F 2  71  ? -16.600 56.432  -6.753   1.00 43.04  ? 73  GLY   B CA    1 
ATOM   14551 C  C     . GLY   F 2  71  ? -16.604 57.028  -8.147   1.00 65.77  ? 73  GLY   B C     1 
ATOM   14552 O  O     . GLY   F 2  71  ? -17.674 57.247  -8.732   1.00 72.34  ? 73  GLY   B O     1 
ATOM   14553 N  N     . THR   F 2  72  ? -15.429 57.259  -8.723   1.00 62.97  ? 74  THR   B N     1 
ATOM   14554 C  CA    . THR   F 2  72  ? -15.363 57.930  -10.018  1.00 55.57  ? 74  THR   B CA    1 
ATOM   14555 C  C     . THR   F 2  72  ? -15.996 59.313  -9.899   1.00 58.67  ? 74  THR   B C     1 
ATOM   14556 O  O     . THR   F 2  72  ? -15.282 60.323  -9.861   1.00 64.96  ? 74  THR   B O     1 
ATOM   14557 C  CB    . THR   F 2  72  ? -16.039 57.114  -11.135  1.00 54.32  ? 74  THR   B CB    1 
ATOM   14558 O  OG1   . THR   F 2  72  ? -17.358 56.672  -10.737  1.00 53.96  ? 74  THR   B OG1   1 
ATOM   14559 C  CG2   . THR   F 2  72  ? -15.163 55.940  -11.556  1.00 41.40  ? 74  THR   B CG2   1 
ATOM   14560 N  N     . MET   F 2  73  ? -17.329 59.378  -9.830   1.00 52.77  ? 75  MET   B N     1 
ATOM   14561 C  CA    . MET   F 2  73  ? -17.978 60.670  -9.626   1.00 60.23  ? 75  MET   B CA    1 
ATOM   14562 C  C     . MET   F 2  73  ? -17.287 61.449  -8.513   1.00 55.81  ? 75  MET   B C     1 
ATOM   14563 O  O     . MET   F 2  73  ? -17.037 62.651  -8.651   1.00 55.25  ? 75  MET   B O     1 
ATOM   14564 C  CB    . MET   F 2  73  ? -19.461 60.473  -9.307   1.00 72.73  ? 75  MET   B CB    1 
ATOM   14565 C  CG    . MET   F 2  73  ? -20.120 59.310  -10.055  1.00 71.15  ? 75  MET   B CG    1 
ATOM   14566 S  SD    . MET   F 2  73  ? -21.302 59.835  -11.301  1.00 63.38  ? 75  MET   B SD    1 
ATOM   14567 C  CE    . MET   F 2  73  ? -22.155 61.158  -10.438  1.00 43.21  ? 75  MET   B CE    1 
ATOM   14568 N  N     . ASP   F 2  74  ? -16.952 60.766  -7.414   1.00 50.37  ? 76  ASP   B N     1 
ATOM   14569 C  CA    . ASP   F 2  74  ? -16.145 61.358  -6.352   1.00 48.46  ? 76  ASP   B CA    1 
ATOM   14570 C  C     . ASP   F 2  74  ? -14.822 61.901  -6.879   1.00 58.34  ? 76  ASP   B C     1 
ATOM   14571 O  O     . ASP   F 2  74  ? -14.494 63.076  -6.681   1.00 58.40  ? 76  ASP   B O     1 
ATOM   14572 C  CB    . ASP   F 2  74  ? -15.882 60.322  -5.268   1.00 47.97  ? 76  ASP   B CB    1 
ATOM   14573 C  CG    . ASP   F 2  74  ? -17.030 60.185  -4.325   1.00 57.84  ? 76  ASP   B CG    1 
ATOM   14574 O  OD1   . ASP   F 2  74  ? -18.136 60.667  -4.675   1.00 46.94  ? 76  ASP   B OD1   1 
ATOM   14575 O  OD2   . ASP   F 2  74  ? -16.815 59.620  -3.229   1.00 66.61  ? 76  ASP   B OD2   1 
ATOM   14576 N  N     . SER   F 2  75  ? -14.022 61.045  -7.522   1.00 51.49  ? 77  SER   B N     1 
ATOM   14577 C  CA    . SER   F 2  75  ? -12.728 61.507  -8.011   1.00 54.97  ? 77  SER   B CA    1 
ATOM   14578 C  C     . SER   F 2  75  ? -12.895 62.540  -9.117   1.00 60.04  ? 77  SER   B C     1 
ATOM   14579 O  O     . SER   F 2  75  ? -12.139 63.516  -9.177   1.00 64.94  ? 77  SER   B O     1 
ATOM   14580 C  CB    . SER   F 2  75  ? -11.873 60.327  -8.486   1.00 56.51  ? 77  SER   B CB    1 
ATOM   14581 O  OG    . SER   F 2  75  ? -12.614 59.417  -9.284   1.00 66.66  ? 77  SER   B OG    1 
ATOM   14582 N  N     . VAL   F 2  76  ? -13.881 62.354  -9.995   1.00 46.99  ? 78  VAL   B N     1 
ATOM   14583 C  CA    . VAL   F 2  76  ? -14.179 63.386  -10.980  1.00 53.24  ? 78  VAL   B CA    1 
ATOM   14584 C  C     . VAL   F 2  76  ? -14.448 64.713  -10.285  1.00 51.81  ? 78  VAL   B C     1 
ATOM   14585 O  O     . VAL   F 2  76  ? -13.919 65.755  -10.684  1.00 57.63  ? 78  VAL   B O     1 
ATOM   14586 C  CB    . VAL   F 2  76  ? -15.360 62.964  -11.876  1.00 57.54  ? 78  VAL   B CB    1 
ATOM   14587 C  CG1   . VAL   F 2  76  ? -16.036 64.189  -12.482  1.00 49.69  ? 78  VAL   B CG1   1 
ATOM   14588 C  CG2   . VAL   F 2  76  ? -14.878 62.040  -12.979  1.00 46.19  ? 78  VAL   B CG2   1 
ATOM   14589 N  N     . ARG   F 2  77  ? -15.264 64.697  -9.221   1.00 58.26  ? 79  ARG   B N     1 
ATOM   14590 C  CA    . ARG   F 2  77  ? -15.623 65.944  -8.537   1.00 56.89  ? 79  ARG   B CA    1 
ATOM   14591 C  C     . ARG   F 2  77  ? -14.431 66.615  -7.877   1.00 62.94  ? 79  ARG   B C     1 
ATOM   14592 O  O     . ARG   F 2  77  ? -14.467 67.827  -7.644   1.00 71.48  ? 79  ARG   B O     1 
ATOM   14593 C  CB    . ARG   F 2  77  ? -16.690 65.699  -7.480   1.00 47.90  ? 79  ARG   B CB    1 
ATOM   14594 C  CG    . ARG   F 2  77  ? -17.464 66.941  -7.101   1.00 52.23  ? 79  ARG   B CG    1 
ATOM   14595 C  CD    . ARG   F 2  77  ? -18.463 66.616  -6.013   1.00 53.27  ? 79  ARG   B CD    1 
ATOM   14596 N  NE    . ARG   F 2  77  ? -19.119 65.330  -6.231   1.00 56.20  ? 79  ARG   B NE    1 
ATOM   14597 C  CZ    . ARG   F 2  77  ? -20.363 65.182  -6.671   1.00 58.48  ? 79  ARG   B CZ    1 
ATOM   14598 N  NH1   . ARG   F 2  77  ? -21.123 66.230  -6.973   1.00 47.77  ? 79  ARG   B NH1   1 
ATOM   14599 N  NH2   . ARG   F 2  77  ? -20.862 63.952  -6.803   1.00 59.83  ? 79  ARG   B NH2   1 
ATOM   14600 N  N     . SER   F 2  78  ? -13.389 65.853  -7.556   1.00 53.35  ? 80  SER   B N     1 
ATOM   14601 C  CA    . SER   F 2  78  ? -12.148 66.389  -7.026   1.00 61.27  ? 80  SER   B CA    1 
ATOM   14602 C  C     . SER   F 2  78  ? -11.037 66.367  -8.069   1.00 65.91  ? 80  SER   B C     1 
ATOM   14603 O  O     . SER   F 2  78  ? -9.856  66.345  -7.713   1.00 61.89  ? 80  SER   B O     1 
ATOM   14604 C  CB    . SER   F 2  78  ? -11.728 65.599  -5.793   1.00 63.98  ? 80  SER   B CB    1 
ATOM   14605 O  OG    . SER   F 2  78  ? -11.545 64.246  -6.167   1.00 68.12  ? 80  SER   B OG    1 
ATOM   14606 N  N     . GLY   F 2  79  ? -11.395 66.343  -9.350   1.00 65.24  ? 81  GLY   B N     1 
ATOM   14607 C  CA    . GLY   F 2  79  ? -10.433 66.456  -10.420  1.00 59.38  ? 81  GLY   B CA    1 
ATOM   14608 C  C     . GLY   F 2  79  ? -10.189 67.910  -10.755  1.00 61.13  ? 81  GLY   B C     1 
ATOM   14609 O  O     . GLY   F 2  79  ? -10.929 68.798  -10.318  1.00 65.07  ? 81  GLY   B O     1 
ATOM   14610 N  N     . PRO   F 2  80  ? -9.144  68.187  -11.539  1.00 66.40  ? 82  PRO   B N     1 
ATOM   14611 C  CA    . PRO   F 2  80  ? -8.779  69.589  -11.810  1.00 64.43  ? 82  PRO   B CA    1 
ATOM   14612 C  C     . PRO   F 2  80  ? -9.993  70.436  -12.158  1.00 65.12  ? 82  PRO   B C     1 
ATOM   14613 O  O     . PRO   F 2  80  ? -10.333 71.393  -11.446  1.00 56.07  ? 82  PRO   B O     1 
ATOM   14614 C  CB    . PRO   F 2  80  ? -7.806  69.485  -12.997  1.00 64.95  ? 82  PRO   B CB    1 
ATOM   14615 C  CG    . PRO   F 2  80  ? -7.972  68.074  -13.544  1.00 59.62  ? 82  PRO   B CG    1 
ATOM   14616 C  CD    . PRO   F 2  80  ? -8.376  67.237  -12.363  1.00 59.34  ? 82  PRO   B CD    1 
ATOM   14617 N  N     . PHE   F 2  81  ? -10.667 70.068  -13.252  1.00 61.85  ? 83  PHE   B N     1 
ATOM   14618 C  CA    . PHE   F 2  81  ? -11.866 70.762  -13.697  1.00 49.23  ? 83  PHE   B CA    1 
ATOM   14619 C  C     . PHE   F 2  81  ? -13.116 70.240  -13.012  1.00 54.47  ? 83  PHE   B C     1 
ATOM   14620 O  O     . PHE   F 2  81  ? -14.226 70.523  -13.478  1.00 52.07  ? 83  PHE   B O     1 
ATOM   14621 C  CB    . PHE   F 2  81  ? -12.001 70.659  -15.219  1.00 51.00  ? 83  PHE   B CB    1 
ATOM   14622 C  CG    . PHE   F 2  81  ? -11.090 71.577  -15.963  1.00 42.02  ? 83  PHE   B CG    1 
ATOM   14623 C  CD1   . PHE   F 2  81  ? -9.731  71.352  -15.981  1.00 41.97  ? 83  PHE   B CD1   1 
ATOM   14624 C  CD2   . PHE   F 2  81  ? -11.592 72.682  -16.628  1.00 50.61  ? 83  PHE   B CD2   1 
ATOM   14625 C  CE1   . PHE   F 2  81  ? -8.879  72.208  -16.654  1.00 50.50  ? 83  PHE   B CE1   1 
ATOM   14626 C  CE2   . PHE   F 2  81  ? -10.747 73.546  -17.309  1.00 54.04  ? 83  PHE   B CE2   1 
ATOM   14627 C  CZ    . PHE   F 2  81  ? -9.383  73.307  -17.320  1.00 49.09  ? 83  PHE   B CZ    1 
ATOM   14628 N  N     . GLY   F 2  82  ? -12.958 69.499  -11.908  1.00 48.14  ? 84  GLY   B N     1 
ATOM   14629 C  CA    . GLY   F 2  82  ? -14.105 68.891  -11.257  1.00 39.32  ? 84  GLY   B CA    1 
ATOM   14630 C  C     . GLY   F 2  82  ? -15.235 69.865  -10.996  1.00 51.78  ? 84  GLY   B C     1 
ATOM   14631 O  O     . GLY   F 2  82  ? -16.410 69.527  -11.168  1.00 49.21  ? 84  GLY   B O     1 
ATOM   14632 N  N     . GLN   F 2  83  ? -14.905 71.094  -10.595  1.00 50.85  ? 85  GLN   B N     1 
ATOM   14633 C  CA    . GLN   F 2  83  ? -15.961 71.996  -10.164  1.00 55.09  ? 85  GLN   B CA    1 
ATOM   14634 C  C     . GLN   F 2  83  ? -16.718 72.677  -11.309  1.00 53.50  ? 85  GLN   B C     1 
ATOM   14635 O  O     . GLN   F 2  83  ? -17.759 73.283  -11.031  1.00 53.96  ? 85  GLN   B O     1 
ATOM   14636 C  CB    . GLN   F 2  83  ? -15.404 73.054  -9.200   1.00 62.32  ? 85  GLN   B CB    1 
ATOM   14637 C  CG    . GLN   F 2  83  ? -14.260 73.909  -9.737   1.00 72.89  ? 85  GLN   B CG    1 
ATOM   14638 C  CD    . GLN   F 2  83  ? -13.998 75.161  -8.876   1.00 73.88  ? 85  GLN   B CD    1 
ATOM   14639 O  OE1   . GLN   F 2  83  ? -14.925 75.897  -8.537   1.00 72.67  ? 85  GLN   B OE1   1 
ATOM   14640 N  NE2   . GLN   F 2  83  ? -12.732 75.403  -8.536   1.00 65.36  ? 85  GLN   B NE2   1 
ATOM   14641 N  N     . ILE   F 2  84  ? -16.275 72.581  -12.574  1.00 47.42  ? 86  ILE   B N     1 
ATOM   14642 C  CA    . ILE   F 2  84  ? -17.043 73.223  -13.655  1.00 50.91  ? 86  ILE   B CA    1 
ATOM   14643 C  C     . ILE   F 2  84  ? -18.415 72.610  -13.865  1.00 51.51  ? 86  ILE   B C     1 
ATOM   14644 O  O     . ILE   F 2  84  ? -19.270 73.246  -14.495  1.00 49.54  ? 86  ILE   B O     1 
ATOM   14645 C  CB    . ILE   F 2  84  ? -16.414 73.201  -15.067  1.00 54.15  ? 86  ILE   B CB    1 
ATOM   14646 C  CG1   . ILE   F 2  84  ? -15.191 72.299  -15.173  1.00 58.88  ? 86  ILE   B CG1   1 
ATOM   14647 C  CG2   . ILE   F 2  84  ? -16.172 74.627  -15.592  1.00 57.56  ? 86  ILE   B CG2   1 
ATOM   14648 C  CD1   . ILE   F 2  84  ? -14.610 72.281  -16.577  1.00 49.03  ? 86  ILE   B CD1   1 
ATOM   14649 N  N     . PHE   F 2  85  ? -18.644 71.378  -13.419  1.00 42.14  ? 87  PHE   B N     1 
ATOM   14650 C  CA    . PHE   F 2  85  ? -19.878 70.702  -13.780  1.00 47.26  ? 87  PHE   B CA    1 
ATOM   14651 C  C     . PHE   F 2  85  ? -21.044 71.209  -12.929  1.00 47.42  ? 87  PHE   B C     1 
ATOM   14652 O  O     . PHE   F 2  85  ? -20.887 71.555  -11.754  1.00 46.83  ? 87  PHE   B O     1 
ATOM   14653 C  CB    . PHE   F 2  85  ? -19.715 69.185  -13.635  1.00 46.81  ? 87  PHE   B CB    1 
ATOM   14654 C  CG    . PHE   F 2  85  ? -18.637 68.597  -14.516  1.00 41.41  ? 87  PHE   B CG    1 
ATOM   14655 C  CD1   . PHE   F 2  85  ? -18.870 68.385  -15.879  1.00 33.77  ? 87  PHE   B CD1   1 
ATOM   14656 C  CD2   . PHE   F 2  85  ? -17.397 68.243  -13.985  1.00 40.15  ? 87  PHE   B CD2   1 
ATOM   14657 C  CE1   . PHE   F 2  85  ? -17.881 67.842  -16.700  1.00 37.08  ? 87  PHE   B CE1   1 
ATOM   14658 C  CE2   . PHE   F 2  85  ? -16.391 67.693  -14.799  1.00 40.67  ? 87  PHE   B CE2   1 
ATOM   14659 C  CZ    . PHE   F 2  85  ? -16.639 67.488  -16.163  1.00 30.24  ? 87  PHE   B CZ    1 
ATOM   14660 N  N     . ARG   F 2  86  ? -22.213 71.272  -13.543  1.00 44.98  ? 88  ARG   B N     1 
ATOM   14661 C  CA    . ARG   F 2  86  ? -23.447 71.507  -12.799  1.00 45.18  ? 88  ARG   B CA    1 
ATOM   14662 C  C     . ARG   F 2  86  ? -23.660 70.384  -11.777  1.00 50.63  ? 88  ARG   B C     1 
ATOM   14663 O  O     . ARG   F 2  86  ? -23.715 69.203  -12.166  1.00 48.76  ? 88  ARG   B O     1 
ATOM   14664 C  CB    . ARG   F 2  86  ? -24.615 71.594  -13.781  1.00 38.25  ? 88  ARG   B CB    1 
ATOM   14665 C  CG    . ARG   F 2  86  ? -25.970 71.651  -13.158  1.00 50.14  ? 88  ARG   B CG    1 
ATOM   14666 C  CD    . ARG   F 2  86  ? -27.042 72.073  -14.166  1.00 44.74  ? 88  ARG   B CD    1 
ATOM   14667 N  NE    . ARG   F 2  86  ? -28.327 72.277  -13.504  1.00 74.14  ? 88  ARG   B NE    1 
ATOM   14668 C  CZ    . ARG   F 2  86  ? -29.318 71.389  -13.467  1.00 78.52  ? 88  ARG   B CZ    1 
ATOM   14669 N  NH1   . ARG   F 2  86  ? -29.255 70.245  -14.143  1.00 58.14  ? 88  ARG   B NH1   1 
ATOM   14670 N  NH2   . ARG   F 2  86  ? -30.401 71.654  -12.732  1.00 70.80  ? 88  ARG   B NH2   1 
ATOM   14671 N  N     . PRO   F 2  87  ? -23.792 70.695  -10.481  1.00 53.68  ? 89  PRO   B N     1 
ATOM   14672 C  CA    . PRO   F 2  87  ? -23.810 69.619  -9.467   1.00 49.57  ? 89  PRO   B CA    1 
ATOM   14673 C  C     . PRO   F 2  87  ? -25.079 68.772  -9.456   1.00 44.06  ? 89  PRO   B C     1 
ATOM   14674 O  O     . PRO   F 2  87  ? -25.022 67.621  -9.017   1.00 41.83  ? 89  PRO   B O     1 
ATOM   14675 C  CB    . PRO   F 2  87  ? -23.629 70.381  -8.142   1.00 49.36  ? 89  PRO   B CB    1 
ATOM   14676 C  CG    . PRO   F 2  87  ? -23.166 71.763  -8.529   1.00 46.32  ? 89  PRO   B CG    1 
ATOM   14677 C  CD    . PRO   F 2  87  ? -23.779 72.031  -9.864   1.00 48.31  ? 89  PRO   B CD    1 
ATOM   14678 N  N     . ASP   F 2  88  ? -26.228 69.296  -9.900   1.00 55.46  ? 90  ASP   B N     1 
ATOM   14679 C  CA    . ASP   F 2  88  ? -27.393 68.439  -10.117  1.00 44.33  ? 90  ASP   B CA    1 
ATOM   14680 C  C     . ASP   F 2  88  ? -27.182 67.452  -11.253  1.00 51.63  ? 90  ASP   B C     1 
ATOM   14681 O  O     . ASP   F 2  88  ? -27.984 66.518  -11.405  1.00 52.99  ? 90  ASP   B O     1 
ATOM   14682 C  CB    . ASP   F 2  88  ? -28.643 69.259  -10.444  1.00 49.21  ? 90  ASP   B CB    1 
ATOM   14683 C  CG    . ASP   F 2  88  ? -29.038 70.204  -9.340   1.00 62.60  ? 90  ASP   B CG    1 
ATOM   14684 O  OD1   . ASP   F 2  88  ? -28.220 70.426  -8.421   1.00 63.79  ? 90  ASP   B OD1   1 
ATOM   14685 O  OD2   . ASP   F 2  88  ? -30.180 70.724  -9.397   1.00 61.79  ? 90  ASP   B OD2   1 
ATOM   14686 N  N     . ASN   F 2  89  ? -26.156 67.652  -12.075  1.00 45.51  ? 91  ASN   B N     1 
ATOM   14687 C  CA    . ASN   F 2  89  ? -25.916 66.779  -13.211  1.00 43.19  ? 91  ASN   B CA    1 
ATOM   14688 C  C     . ASN   F 2  89  ? -25.093 65.549  -12.843  1.00 47.60  ? 91  ASN   B C     1 
ATOM   14689 O  O     . ASN   F 2  89  ? -24.728 64.777  -13.737  1.00 48.98  ? 91  ASN   B O     1 
ATOM   14690 C  CB    . ASN   F 2  89  ? -25.243 67.557  -14.340  1.00 44.70  ? 91  ASN   B CB    1 
ATOM   14691 C  CG    . ASN   F 2  89  ? -26.212 68.474  -15.091  1.00 43.06  ? 91  ASN   B CG    1 
ATOM   14692 O  OD1   . ASN   F 2  89  ? -27.322 68.760  -14.643  1.00 42.23  ? 91  ASN   B OD1   1 
ATOM   14693 N  ND2   . ASN   F 2  89  ? -25.788 68.922  -16.249  1.00 39.83  ? 91  ASN   B ND2   1 
ATOM   14694 N  N     . PHE   F 2  90  ? -24.789 65.345  -11.556  1.00 42.61  ? 92  PHE   B N     1 
ATOM   14695 C  CA    . PHE   F 2  90  ? -24.219 64.085  -11.087  1.00 41.17  ? 92  PHE   B CA    1 
ATOM   14696 C  C     . PHE   F 2  90  ? -25.368 63.186  -10.643  1.00 37.88  ? 92  PHE   B C     1 
ATOM   14697 O  O     . PHE   F 2  90  ? -26.014 63.456  -9.629   1.00 44.47  ? 92  PHE   B O     1 
ATOM   14698 C  CB    . PHE   F 2  90  ? -23.246 64.300  -9.936   1.00 34.66  ? 92  PHE   B CB    1 
ATOM   14699 C  CG    . PHE   F 2  90  ? -22.004 65.060  -10.294  1.00 36.86  ? 92  PHE   B CG    1 
ATOM   14700 C  CD1   . PHE   F 2  90  ? -22.043 66.426  -10.518  1.00 38.53  ? 92  PHE   B CD1   1 
ATOM   14701 C  CD2   . PHE   F 2  90  ? -20.773 64.423  -10.317  1.00 41.21  ? 92  PHE   B CD2   1 
ATOM   14702 C  CE1   . PHE   F 2  90  ? -20.878 67.139  -10.824  1.00 38.24  ? 92  PHE   B CE1   1 
ATOM   14703 C  CE2   . PHE   F 2  90  ? -19.602 65.130  -10.613  1.00 44.50  ? 92  PHE   B CE2   1 
ATOM   14704 C  CZ    . PHE   F 2  90  ? -19.661 66.491  -10.866  1.00 41.29  ? 92  PHE   B CZ    1 
ATOM   14705 N  N     . VAL   F 2  91  ? -25.631 62.128  -11.399  1.00 37.71  ? 93  VAL   B N     1 
ATOM   14706 C  CA    . VAL   F 2  91  ? -26.676 61.156  -11.082  1.00 40.59  ? 93  VAL   B CA    1 
ATOM   14707 C  C     . VAL   F 2  91  ? -26.005 59.801  -10.870  1.00 45.20  ? 93  VAL   B C     1 
ATOM   14708 O  O     . VAL   F 2  91  ? -25.354 59.277  -11.786  1.00 44.90  ? 93  VAL   B O     1 
ATOM   14709 C  CB    . VAL   F 2  91  ? -27.732 61.099  -12.194  1.00 40.37  ? 93  VAL   B CB    1 
ATOM   14710 C  CG1   . VAL   F 2  91  ? -28.787 60.069  -11.903  1.00 33.70  ? 93  VAL   B CG1   1 
ATOM   14711 C  CG2   . VAL   F 2  91  ? -28.341 62.472  -12.376  1.00 35.91  ? 93  VAL   B CG2   1 
ATOM   14712 N  N     . PHE   F 2  92  ? -26.141 59.242  -9.664   1.00 46.25  ? 94  PHE   B N     1 
ATOM   14713 C  CA    . PHE   F 2  92  ? -25.385 58.039  -9.328   1.00 46.61  ? 94  PHE   B CA    1 
ATOM   14714 C  C     . PHE   F 2  92  ? -26.113 57.186  -8.293   1.00 45.27  ? 94  PHE   B C     1 
ATOM   14715 O  O     . PHE   F 2  92  ? -26.759 57.717  -7.384   1.00 45.48  ? 94  PHE   B O     1 
ATOM   14716 C  CB    . PHE   F 2  92  ? -23.972 58.400  -8.830   1.00 48.29  ? 94  PHE   B CB    1 
ATOM   14717 C  CG    . PHE   F 2  92  ? -23.940 59.334  -7.636   1.00 54.36  ? 94  PHE   B CG    1 
ATOM   14718 C  CD1   . PHE   F 2  92  ? -24.042 58.839  -6.336   1.00 55.81  ? 94  PHE   B CD1   1 
ATOM   14719 C  CD2   . PHE   F 2  92  ? -23.761 60.704  -7.809   1.00 54.21  ? 94  PHE   B CD2   1 
ATOM   14720 C  CE1   . PHE   F 2  92  ? -23.996 59.692  -5.238   1.00 51.53  ? 94  PHE   B CE1   1 
ATOM   14721 C  CE2   . PHE   F 2  92  ? -23.707 61.567  -6.714   1.00 52.75  ? 94  PHE   B CE2   1 
ATOM   14722 C  CZ    . PHE   F 2  92  ? -23.829 61.056  -5.426   1.00 60.04  ? 94  PHE   B CZ    1 
ATOM   14723 N  N     . GLY   F 2  93  ? -26.012 55.858  -8.455   1.00 38.08  ? 95  GLY   B N     1 
ATOM   14724 C  CA    . GLY   F 2  93  ? -26.480 54.897  -7.471   1.00 35.88  ? 95  GLY   B CA    1 
ATOM   14725 C  C     . GLY   F 2  93  ? -25.403 54.472  -6.479   1.00 42.97  ? 95  GLY   B C     1 
ATOM   14726 O  O     . GLY   F 2  93  ? -24.421 55.182  -6.237   1.00 37.34  ? 95  GLY   B O     1 
ATOM   14727 N  N     . GLN   F 2  94  ? -25.602 53.267  -5.886   1.00 46.27  ? 96  GLN   B N     1 
ATOM   14728 C  CA    . GLN   F 2  94  ? -24.703 52.736  -4.854   1.00 39.98  ? 96  GLN   B CA    1 
ATOM   14729 C  C     . GLN   F 2  94  ? -24.264 51.306  -5.115   1.00 44.11  ? 96  GLN   B C     1 
ATOM   14730 O  O     . GLN   F 2  94  ? -23.126 50.946  -4.805   1.00 44.27  ? 96  GLN   B O     1 
ATOM   14731 C  CB    . GLN   F 2  94  ? -25.365 52.786  -3.475   1.00 40.22  ? 96  GLN   B CB    1 
ATOM   14732 C  CG    . GLN   F 2  94  ? -25.623 54.181  -2.918   1.00 49.93  ? 96  GLN   B CG    1 
ATOM   14733 C  CD    . GLN   F 2  94  ? -24.344 54.924  -2.558   1.00 54.79  ? 96  GLN   B CD    1 
ATOM   14734 O  OE1   . GLN   F 2  94  ? -23.288 54.316  -2.353   1.00 56.40  ? 96  GLN   B OE1   1 
ATOM   14735 N  NE2   . GLN   F 2  94  ? -24.436 56.248  -2.484   1.00 44.94  ? 96  GLN   B NE2   1 
ATOM   14736 N  N     . SER   F 2  95  ? -25.141 50.475  -5.667   1.00 40.42  ? 97  SER   B N     1 
ATOM   14737 C  CA    . SER   F 2  95  ? -24.848 49.053  -5.710   1.00 45.69  ? 97  SER   B CA    1 
ATOM   14738 C  C     . SER   F 2  95  ? -23.698 48.738  -6.655   1.00 43.51  ? 97  SER   B C     1 
ATOM   14739 O  O     . SER   F 2  95  ? -22.977 47.756  -6.441   1.00 46.69  ? 97  SER   B O     1 
ATOM   14740 C  CB    . SER   F 2  95  ? -26.091 48.278  -6.132   1.00 42.86  ? 97  SER   B CB    1 
ATOM   14741 O  OG    . SER   F 2  95  ? -26.425 48.590  -7.482   1.00 46.83  ? 97  SER   B OG    1 
ATOM   14742 N  N     . GLY   F 2  96  ? -23.519 49.542  -7.702   1.00 38.84  ? 98  GLY   B N     1 
ATOM   14743 C  CA    . GLY   F 2  96  ? -22.670 49.163  -8.812   1.00 36.44  ? 98  GLY   B CA    1 
ATOM   14744 C  C     . GLY   F 2  96  ? -23.372 48.217  -9.779   1.00 33.11  ? 98  GLY   B C     1 
ATOM   14745 O  O     . GLY   F 2  96  ? -24.546 47.873  -9.645   1.00 34.07  ? 98  GLY   B O     1 
ATOM   14746 N  N     . ALA   F 2  97  ? -22.619 47.793  -10.787  1.00 24.99  ? 99  ALA   B N     1 
ATOM   14747 C  CA    . ALA   F 2  97  ? -23.118 46.872  -11.791  1.00 20.07  ? 99  ALA   B CA    1 
ATOM   14748 C  C     . ALA   F 2  97  ? -22.284 45.598  -11.893  1.00 19.52  ? 99  ALA   B C     1 
ATOM   14749 O  O     . ALA   F 2  97  ? -22.654 44.701  -12.664  1.00 22.10  ? 99  ALA   B O     1 
ATOM   14750 C  CB    . ALA   F 2  97  ? -23.187 47.573  -13.164  1.00 17.46  ? 99  ALA   B CB    1 
ATOM   14751 N  N     . GLY   F 2  98  ? -21.179 45.501  -11.149  1.00 17.43  ? 100 GLY   B N     1 
ATOM   14752 C  CA    . GLY   F 2  98  ? -20.362 44.295  -11.129  1.00 9.78   ? 100 GLY   B CA    1 
ATOM   14753 C  C     . GLY   F 2  98  ? -19.948 43.799  -12.497  1.00 25.43  ? 100 GLY   B C     1 
ATOM   14754 O  O     . GLY   F 2  98  ? -20.003 42.591  -12.758  1.00 21.61  ? 100 GLY   B O     1 
ATOM   14755 N  N     . ASN   F 2  99  ? -19.543 44.710  -13.392  1.00 26.46  ? 101 ASN   B N     1 
ATOM   14756 C  CA    . ASN   F 2  99  ? -19.148 44.332  -14.754  1.00 27.26  ? 101 ASN   B CA    1 
ATOM   14757 C  C     . ASN   F 2  99  ? -20.159 43.423  -15.429  1.00 22.69  ? 101 ASN   B C     1 
ATOM   14758 O  O     . ASN   F 2  99  ? -19.786 42.482  -16.129  1.00 22.80  ? 101 ASN   B O     1 
ATOM   14759 C  CB    . ASN   F 2  99  ? -17.797 43.643  -14.765  1.00 21.98  ? 101 ASN   B CB    1 
ATOM   14760 C  CG    . ASN   F 2  99  ? -16.678 44.593  -14.538  1.00 31.16  ? 101 ASN   B CG    1 
ATOM   14761 O  OD1   . ASN   F 2  99  ? -16.705 45.770  -14.985  1.00 18.67  ? 101 ASN   B OD1   1 
ATOM   14762 N  ND2   . ASN   F 2  99  ? -15.658 44.102  -13.841  1.00 26.28  ? 101 ASN   B ND2   1 
ATOM   14763 N  N     . ASN   F 2  100 ? -21.442 43.678  -15.204  1.00 24.76  ? 102 ASN   B N     1 
ATOM   14764 C  CA    . ASN   F 2  100 ? -22.490 42.804  -15.720  1.00 29.61  ? 102 ASN   B CA    1 
ATOM   14765 C  C     . ASN   F 2  100 ? -23.498 43.644  -16.494  1.00 28.96  ? 102 ASN   B C     1 
ATOM   14766 O  O     . ASN   F 2  100 ? -24.244 44.433  -15.904  1.00 27.90  ? 102 ASN   B O     1 
ATOM   14767 C  CB    . ASN   F 2  100 ? -23.176 42.018  -14.602  1.00 23.43  ? 102 ASN   B CB    1 
ATOM   14768 C  CG    . ASN   F 2  100 ? -24.300 41.110  -15.130  1.00 23.55  ? 102 ASN   B CG    1 
ATOM   14769 O  OD1   . ASN   F 2  100 ? -25.060 41.492  -16.007  1.00 30.10  ? 102 ASN   B OD1   1 
ATOM   14770 N  ND2   . ASN   F 2  100 ? -24.389 39.916  -14.607  1.00 21.56  ? 102 ASN   B ND2   1 
ATOM   14771 N  N     . TRP   F 2  101 ? -23.528 43.448  -17.813  1.00 29.91  ? 103 TRP   B N     1 
ATOM   14772 C  CA    . TRP   F 2  101 ? -24.425 44.222  -18.676  1.00 31.11  ? 103 TRP   B CA    1 
ATOM   14773 C  C     . TRP   F 2  101 ? -25.878 44.109  -18.221  1.00 27.99  ? 103 TRP   B C     1 
ATOM   14774 O  O     . TRP   F 2  101 ? -26.601 45.112  -18.179  1.00 34.13  ? 103 TRP   B O     1 
ATOM   14775 C  CB    . TRP   F 2  101 ? -24.262 43.743  -20.119  1.00 25.42  ? 103 TRP   B CB    1 
ATOM   14776 C  CG    . TRP   F 2  101 ? -24.896 44.541  -21.201  1.00 27.50  ? 103 TRP   B CG    1 
ATOM   14777 C  CD1   . TRP   F 2  101 ? -24.310 45.511  -21.934  1.00 25.66  ? 103 TRP   B CD1   1 
ATOM   14778 C  CD2   . TRP   F 2  101 ? -26.224 44.382  -21.726  1.00 29.51  ? 103 TRP   B CD2   1 
ATOM   14779 N  NE1   . TRP   F 2  101 ? -25.186 45.992  -22.869  1.00 30.63  ? 103 TRP   B NE1   1 
ATOM   14780 C  CE2   . TRP   F 2  101 ? -26.367 45.308  -22.772  1.00 27.58  ? 103 TRP   B CE2   1 
ATOM   14781 C  CE3   . TRP   F 2  101 ? -27.305 43.543  -21.411  1.00 31.94  ? 103 TRP   B CE3   1 
ATOM   14782 C  CZ2   . TRP   F 2  101 ? -27.554 45.441  -23.501  1.00 25.33  ? 103 TRP   B CZ2   1 
ATOM   14783 C  CZ3   . TRP   F 2  101 ? -28.484 43.658  -22.152  1.00 25.40  ? 103 TRP   B CZ3   1 
ATOM   14784 C  CH2   . TRP   F 2  101 ? -28.592 44.602  -23.183  1.00 23.71  ? 103 TRP   B CH2   1 
ATOM   14785 N  N     . ALA   F 2  102 ? -26.325 42.900  -17.876  1.00 24.83  ? 104 ALA   B N     1 
ATOM   14786 C  CA    . ALA   F 2  102 ? -27.708 42.721  -17.447  1.00 25.30  ? 104 ALA   B CA    1 
ATOM   14787 C  C     . ALA   F 2  102 ? -28.035 43.622  -16.254  1.00 26.32  ? 104 ALA   B C     1 
ATOM   14788 O  O     . ALA   F 2  102 ? -29.083 44.269  -16.224  1.00 29.28  ? 104 ALA   B O     1 
ATOM   14789 C  CB    . ALA   F 2  102 ? -27.955 41.248  -17.128  1.00 24.58  ? 104 ALA   B CB    1 
ATOM   14790 N  N     . LYS   F 2  103 ? -27.121 43.728  -15.294  1.00 27.76  ? 105 LYS   B N     1 
ATOM   14791 C  CA    . LYS   F 2  103 ? -27.323 44.634  -14.169  1.00 28.26  ? 105 LYS   B CA    1 
ATOM   14792 C  C     . LYS   F 2  103 ? -27.430 46.085  -14.627  1.00 35.23  ? 105 LYS   B C     1 
ATOM   14793 O  O     . LYS   F 2  103 ? -28.198 46.874  -14.044  1.00 34.76  ? 105 LYS   B O     1 
ATOM   14794 C  CB    . LYS   F 2  103 ? -26.194 44.463  -13.146  1.00 22.87  ? 105 LYS   B CB    1 
ATOM   14795 C  CG    . LYS   F 2  103 ? -26.144 43.055  -12.615  1.00 23.18  ? 105 LYS   B CG    1 
ATOM   14796 C  CD    . LYS   F 2  103 ? -25.355 42.901  -11.330  1.00 23.61  ? 105 LYS   B CD    1 
ATOM   14797 C  CE    . LYS   F 2  103 ? -25.402 41.425  -10.899  1.00 25.07  ? 105 LYS   B CE    1 
ATOM   14798 N  NZ    . LYS   F 2  103 ? -24.577 41.040  -9.716   1.00 21.71  ? 105 LYS   B NZ    1 
ATOM   14799 N  N     . GLY   F 2  104 ? -26.672 46.458  -15.668  1.00 30.52  ? 106 GLY   B N     1 
ATOM   14800 C  CA    . GLY   F 2  104 ? -26.692 47.818  -16.171  1.00 26.03  ? 106 GLY   B CA    1 
ATOM   14801 C  C     . GLY   F 2  104 ? -27.931 48.128  -16.986  1.00 31.04  ? 106 GLY   B C     1 
ATOM   14802 O  O     . GLY   F 2  104 ? -28.519 49.218  -16.879  1.00 25.67  ? 106 GLY   B O     1 
ATOM   14803 N  N     . HIS   F 2  105 ? -28.344 47.159  -17.801  1.00 26.23  ? 107 HIS   B N     1 
ATOM   14804 C  CA    . HIS   F 2  105 ? -29.423 47.380  -18.759  1.00 32.24  ? 107 HIS   B CA    1 
ATOM   14805 C  C     . HIS   F 2  105 ? -30.794 47.139  -18.153  1.00 31.93  ? 107 HIS   B C     1 
ATOM   14806 O  O     . HIS   F 2  105 ? -31.745 47.859  -18.480  1.00 33.18  ? 107 HIS   B O     1 
ATOM   14807 C  CB    . HIS   F 2  105 ? -29.248 46.455  -19.967  1.00 30.13  ? 107 HIS   B CB    1 
ATOM   14808 C  CG    . HIS   F 2  105 ? -29.954 46.908  -21.206  1.00 29.37  ? 107 HIS   B CG    1 
ATOM   14809 N  ND1   . HIS   F 2  105 ? -29.462 47.907  -22.018  1.00 33.85  ? 107 HIS   B ND1   1 
ATOM   14810 C  CD2   . HIS   F 2  105 ? -31.080 46.460  -21.808  1.00 33.93  ? 107 HIS   B CD2   1 
ATOM   14811 C  CE1   . HIS   F 2  105 ? -30.263 48.067  -23.058  1.00 31.53  ? 107 HIS   B CE1   1 
ATOM   14812 N  NE2   . HIS   F 2  105 ? -31.250 47.197  -22.958  1.00 32.64  ? 107 HIS   B NE2   1 
ATOM   14813 N  N     . TYR   F 2  106 ? -30.895 46.153  -17.252  1.00 30.93  ? 108 TYR   B N     1 
ATOM   14814 C  CA    . TYR   F 2  106 ? -32.152 45.538  -16.862  1.00 22.63  ? 108 TYR   B CA    1 
ATOM   14815 C  C     . TYR   F 2  106 ? -32.529 45.648  -15.397  1.00 27.25  ? 108 TYR   B C     1 
ATOM   14816 O  O     . TYR   F 2  106 ? -33.721 45.632  -15.101  1.00 34.01  ? 108 TYR   B O     1 
ATOM   14817 C  CB    . TYR   F 2  106 ? -32.121 44.060  -17.191  1.00 25.65  ? 108 TYR   B CB    1 
ATOM   14818 C  CG    . TYR   F 2  106 ? -32.353 43.804  -18.632  1.00 29.92  ? 108 TYR   B CG    1 
ATOM   14819 C  CD1   . TYR   F 2  106 ? -33.384 44.461  -19.327  1.00 27.79  ? 108 TYR   B CD1   1 
ATOM   14820 C  CD2   . TYR   F 2  106 ? -31.549 42.914  -19.306  1.00 24.88  ? 108 TYR   B CD2   1 
ATOM   14821 C  CE1   . TYR   F 2  106 ? -33.592 44.218  -20.660  1.00 33.71  ? 108 TYR   B CE1   1 
ATOM   14822 C  CE2   . TYR   F 2  106 ? -31.737 42.655  -20.617  1.00 35.55  ? 108 TYR   B CE2   1 
ATOM   14823 C  CZ    . TYR   F 2  106 ? -32.745 43.303  -21.307  1.00 40.80  ? 108 TYR   B CZ    1 
ATOM   14824 O  OH    . TYR   F 2  106 ? -32.869 42.997  -22.637  1.00 32.47  ? 108 TYR   B OH    1 
ATOM   14825 N  N     . THR   F 2  107 ? -31.576 45.686  -14.468  1.00 28.88  ? 109 THR   B N     1 
ATOM   14826 C  CA    . THR   F 2  107 ? -31.970 45.619  -13.063  1.00 28.89  ? 109 THR   B CA    1 
ATOM   14827 C  C     . THR   F 2  107 ? -31.527 46.854  -12.274  1.00 39.43  ? 109 THR   B C     1 
ATOM   14828 O  O     . THR   F 2  107 ? -32.316 47.799  -12.119  1.00 33.82  ? 109 THR   B O     1 
ATOM   14829 C  CB    . THR   F 2  107 ? -31.450 44.326  -12.456  1.00 28.23  ? 109 THR   B CB    1 
ATOM   14830 O  OG1   . THR   F 2  107 ? -30.051 44.216  -12.705  1.00 29.99  ? 109 THR   B OG1   1 
ATOM   14831 C  CG2   . THR   F 2  107 ? -32.134 43.133  -13.124  1.00 27.43  ? 109 THR   B CG2   1 
ATOM   14832 N  N     . GLU   F 2  108 ? -30.281 46.872  -11.781  1.00 36.94  ? 110 GLU   B N     1 
ATOM   14833 C  CA    . GLU   F 2  108 ? -29.789 48.047  -11.066  1.00 25.67  ? 110 GLU   B CA    1 
ATOM   14834 C  C     . GLU   F 2  108 ? -29.958 49.293  -11.907  1.00 36.93  ? 110 GLU   B C     1 
ATOM   14835 O  O     . GLU   F 2  108 ? -30.313 50.361  -11.390  1.00 41.82  ? 110 GLU   B O     1 
ATOM   14836 C  CB    . GLU   F 2  108 ? -28.309 47.886  -10.696  1.00 36.32  ? 110 GLU   B CB    1 
ATOM   14837 C  CG    . GLU   F 2  108 ? -27.886 46.485  -10.278  1.00 33.17  ? 110 GLU   B CG    1 
ATOM   14838 C  CD    . GLU   F 2  108 ? -28.599 46.052  -9.044   1.00 36.91  ? 110 GLU   B CD    1 
ATOM   14839 O  OE1   . GLU   F 2  108 ? -28.712 46.894  -8.136   1.00 22.69  ? 110 GLU   B OE1   1 
ATOM   14840 O  OE2   . GLU   F 2  108 ? -29.074 44.888  -8.999   1.00 57.05  ? 110 GLU   B OE2   1 
ATOM   14841 N  N     . GLY   F 2  109 ? -29.683 49.178  -13.211  1.00 33.59  ? 111 GLY   B N     1 
ATOM   14842 C  CA    . GLY   F 2  109 ? -29.703 50.349  -14.063  1.00 36.10  ? 111 GLY   B CA    1 
ATOM   14843 C  C     . GLY   F 2  109 ? -31.099 50.894  -14.267  1.00 41.16  ? 111 GLY   B C     1 
ATOM   14844 O  O     . GLY   F 2  109 ? -31.282 52.109  -14.398  1.00 42.32  ? 111 GLY   B O     1 
ATOM   14845 N  N     . ALA   F 2  110 ? -32.103 50.009  -14.299  1.00 42.59  ? 112 ALA   B N     1 
ATOM   14846 C  CA    . ALA   F 2  110 ? -33.489 50.455  -14.443  1.00 41.60  ? 112 ALA   B CA    1 
ATOM   14847 C  C     . ALA   F 2  110 ? -33.931 51.329  -13.268  1.00 31.35  ? 112 ALA   B C     1 
ATOM   14848 O  O     . ALA   F 2  110 ? -34.694 52.279  -13.456  1.00 41.97  ? 112 ALA   B O     1 
ATOM   14849 C  CB    . ALA   F 2  110 ? -34.409 49.238  -14.611  1.00 28.85  ? 112 ALA   B CB    1 
ATOM   14850 N  N     . GLU   F 2  111 ? -33.435 51.058  -12.060  1.00 37.70  ? 113 GLU   B N     1 
ATOM   14851 C  CA    . GLU   F 2  111 ? -33.796 51.885  -10.905  1.00 43.28  ? 113 GLU   B CA    1 
ATOM   14852 C  C     . GLU   F 2  111 ? -33.393 53.354  -11.114  1.00 43.34  ? 113 GLU   B C     1 
ATOM   14853 O  O     . GLU   F 2  111 ? -34.199 54.267  -10.905  1.00 42.68  ? 113 GLU   B O     1 
ATOM   14854 C  CB    . GLU   F 2  111 ? -33.166 51.289  -9.636   1.00 38.45  ? 113 GLU   B CB    1 
ATOM   14855 C  CG    . GLU   F 2  111 ? -33.767 51.783  -8.310   1.00 46.51  ? 113 GLU   B CG    1 
ATOM   14856 C  CD    . GLU   F 2  111 ? -33.296 50.988  -7.078   1.00 54.09  ? 113 GLU   B CD    1 
ATOM   14857 O  OE1   . GLU   F 2  111 ? -32.991 49.777  -7.201   1.00 59.32  ? 113 GLU   B OE1   1 
ATOM   14858 O  OE2   . GLU   F 2  111 ? -33.231 51.585  -5.977   1.00 60.12  ? 113 GLU   B OE2   1 
ATOM   14859 N  N     . LEU   F 2  112 ? -32.164 53.603  -11.574  1.00 42.37  ? 114 LEU   B N     1 
ATOM   14860 C  CA    . LEU   F 2  112 ? -31.604 54.952  -11.628  1.00 40.58  ? 114 LEU   B CA    1 
ATOM   14861 C  C     . LEU   F 2  112 ? -31.857 55.690  -12.957  1.00 41.19  ? 114 LEU   B C     1 
ATOM   14862 O  O     . LEU   F 2  112 ? -31.715 56.919  -13.001  1.00 36.06  ? 114 LEU   B O     1 
ATOM   14863 C  CB    . LEU   F 2  112 ? -30.090 54.870  -11.340  1.00 35.84  ? 114 LEU   B CB    1 
ATOM   14864 C  CG    . LEU   F 2  112 ? -29.165 56.084  -11.496  1.00 42.72  ? 114 LEU   B CG    1 
ATOM   14865 C  CD1   . LEU   F 2  112 ? -29.309 57.078  -10.362  1.00 32.54  ? 114 LEU   B CD1   1 
ATOM   14866 C  CD2   . LEU   F 2  112 ? -27.712 55.655  -11.640  1.00 42.67  ? 114 LEU   B CD2   1 
ATOM   14867 N  N     . VAL   F 2  113 ? -32.265 54.990  -14.019  1.00 25.98  ? 115 VAL   B N     1 
ATOM   14868 C  CA    . VAL   F 2  113 ? -32.321 55.583  -15.361  1.00 33.40  ? 115 VAL   B CA    1 
ATOM   14869 C  C     . VAL   F 2  113 ? -33.216 56.834  -15.403  1.00 40.17  ? 115 VAL   B C     1 
ATOM   14870 O  O     . VAL   F 2  113 ? -32.804 57.894  -15.901  1.00 36.16  ? 115 VAL   B O     1 
ATOM   14871 C  CB    . VAL   F 2  113 ? -32.786 54.522  -16.372  1.00 31.02  ? 115 VAL   B CB    1 
ATOM   14872 C  CG1   . VAL   F 2  113 ? -34.263 54.225  -16.193  1.00 30.10  ? 115 VAL   B CG1   1 
ATOM   14873 C  CG2   . VAL   F 2  113 ? -32.476 54.932  -17.785  1.00 36.41  ? 115 VAL   B CG2   1 
ATOM   14874 N  N     . ASP   F 2  114 ? -34.470 56.717  -14.931  1.00 31.71  ? 116 ASP   B N     1 
ATOM   14875 C  CA    . ASP   F 2  114 ? -35.404 57.841  -14.986  1.00 30.47  ? 116 ASP   B CA    1 
ATOM   14876 C  C     . ASP   F 2  114 ? -34.780 59.114  -14.452  1.00 38.45  ? 116 ASP   B C     1 
ATOM   14877 O  O     . ASP   F 2  114 ? -34.985 60.192  -15.010  1.00 43.98  ? 116 ASP   B O     1 
ATOM   14878 C  CB    . ASP   F 2  114 ? -36.669 57.555  -14.179  1.00 24.49  ? 116 ASP   B CB    1 
ATOM   14879 C  CG    . ASP   F 2  114 ? -37.674 56.779  -14.939  1.00 32.17  ? 116 ASP   B CG    1 
ATOM   14880 O  OD1   . ASP   F 2  114 ? -37.309 56.125  -15.949  1.00 46.86  ? 116 ASP   B OD1   1 
ATOM   14881 O  OD2   . ASP   F 2  114 ? -38.850 56.842  -14.531  1.00 55.87  ? 116 ASP   B OD2   1 
ATOM   14882 N  N     . SER   F 2  115 ? -34.053 59.021  -13.344  1.00 32.70  ? 117 SER   B N     1 
ATOM   14883 C  CA    . SER   F 2  115 ? -33.507 60.231  -12.773  1.00 31.05  ? 117 SER   B CA    1 
ATOM   14884 C  C     . SER   F 2  115 ? -32.404 60.800  -13.656  1.00 37.11  ? 117 SER   B C     1 
ATOM   14885 O  O     . SER   F 2  115 ? -32.278 62.027  -13.770  1.00 41.27  ? 117 SER   B O     1 
ATOM   14886 C  CB    . SER   F 2  115 ? -33.020 59.958  -11.359  1.00 27.01  ? 117 SER   B CB    1 
ATOM   14887 O  OG    . SER   F 2  115 ? -31.905 59.099  -11.421  1.00 51.87  ? 117 SER   B OG    1 
ATOM   14888 N  N     . VAL   F 2  116 ? -31.618 59.946  -14.312  1.00 31.60  ? 118 VAL   B N     1 
ATOM   14889 C  CA    . VAL   F 2  116 ? -30.735 60.444  -15.369  1.00 33.57  ? 118 VAL   B CA    1 
ATOM   14890 C  C     . VAL   F 2  116 ? -31.549 61.175  -16.438  1.00 37.52  ? 118 VAL   B C     1 
ATOM   14891 O  O     . VAL   F 2  116 ? -31.255 62.327  -16.787  1.00 34.61  ? 118 VAL   B O     1 
ATOM   14892 C  CB    . VAL   F 2  116 ? -29.920 59.298  -15.996  1.00 36.42  ? 118 VAL   B CB    1 
ATOM   14893 C  CG1   . VAL   F 2  116 ? -29.160 59.827  -17.233  1.00 29.01  ? 118 VAL   B CG1   1 
ATOM   14894 C  CG2   . VAL   F 2  116 ? -28.969 58.666  -14.973  1.00 33.84  ? 118 VAL   B CG2   1 
ATOM   14895 N  N     . LEU   F 2  117 ? -32.593 60.511  -16.963  1.00 27.04  ? 119 LEU   B N     1 
ATOM   14896 C  CA    . LEU   F 2  117 ? -33.409 61.084  -18.028  1.00 32.64  ? 119 LEU   B CA    1 
ATOM   14897 C  C     . LEU   F 2  117 ? -33.931 62.484  -17.684  1.00 42.33  ? 119 LEU   B C     1 
ATOM   14898 O  O     . LEU   F 2  117 ? -33.870 63.390  -18.526  1.00 40.81  ? 119 LEU   B O     1 
ATOM   14899 C  CB    . LEU   F 2  117 ? -34.557 60.134  -18.366  1.00 30.94  ? 119 LEU   B CB    1 
ATOM   14900 C  CG    . LEU   F 2  117 ? -34.108 58.890  -19.146  1.00 43.87  ? 119 LEU   B CG    1 
ATOM   14901 C  CD1   . LEU   F 2  117 ? -35.208 57.852  -19.168  1.00 37.53  ? 119 LEU   B CD1   1 
ATOM   14902 C  CD2   . LEU   F 2  117 ? -33.651 59.233  -20.583  1.00 28.26  ? 119 LEU   B CD2   1 
ATOM   14903 N  N     . ASP   F 2  118 ? -34.454 62.681  -16.455  1.00 34.56  ? 120 ASP   B N     1 
ATOM   14904 C  CA    . ASP   F 2  118 ? -34.971 63.994  -16.054  1.00 37.84  ? 120 ASP   B CA    1 
ATOM   14905 C  C     . ASP   F 2  118 ? -33.929 65.082  -16.247  1.00 34.66  ? 120 ASP   B C     1 
ATOM   14906 O  O     . ASP   F 2  118 ? -34.243 66.180  -16.725  1.00 38.55  ? 120 ASP   B O     1 
ATOM   14907 C  CB    . ASP   F 2  118 ? -35.425 64.013  -14.583  1.00 34.82  ? 120 ASP   B CB    1 
ATOM   14908 C  CG    . ASP   F 2  118 ? -36.523 63.026  -14.281  1.00 34.48  ? 120 ASP   B CG    1 
ATOM   14909 O  OD1   . ASP   F 2  118 ? -37.411 62.807  -15.131  1.00 36.87  ? 120 ASP   B OD1   1 
ATOM   14910 O  OD2   . ASP   F 2  118 ? -36.490 62.458  -13.165  1.00 41.59  ? 120 ASP   B OD2   1 
ATOM   14911 N  N     . VAL   F 2  119 ? -32.687 64.806  -15.851  1.00 31.50  ? 121 VAL   B N     1 
ATOM   14912 C  CA    . VAL   F 2  119 ? -31.609 65.762  -16.074  1.00 32.17  ? 121 VAL   B CA    1 
ATOM   14913 C  C     . VAL   F 2  119 ? -31.353 65.954  -17.565  1.00 39.47  ? 121 VAL   B C     1 
ATOM   14914 O  O     . VAL   F 2  119 ? -31.052 67.068  -18.018  1.00 40.36  ? 121 VAL   B O     1 
ATOM   14915 C  CB    . VAL   F 2  119 ? -30.339 65.306  -15.343  1.00 33.17  ? 121 VAL   B CB    1 
ATOM   14916 C  CG1   . VAL   F 2  119 ? -29.231 66.339  -15.509  1.00 37.43  ? 121 VAL   B CG1   1 
ATOM   14917 C  CG2   . VAL   F 2  119 ? -30.654 65.055  -13.894  1.00 39.28  ? 121 VAL   B CG2   1 
ATOM   14918 N  N     . VAL   F 2  120 ? -31.447 64.877  -18.352  1.00 34.67  ? 122 VAL   B N     1 
ATOM   14919 C  CA    . VAL   F 2  120 ? -31.290 65.020  -19.801  1.00 39.38  ? 122 VAL   B CA    1 
ATOM   14920 C  C     . VAL   F 2  120 ? -32.328 65.992  -20.344  1.00 39.30  ? 122 VAL   B C     1 
ATOM   14921 O  O     . VAL   F 2  120 ? -32.008 66.906  -21.111  1.00 42.52  ? 122 VAL   B O     1 
ATOM   14922 C  CB    . VAL   F 2  120 ? -31.385 63.653  -20.503  1.00 34.26  ? 122 VAL   B CB    1 
ATOM   14923 C  CG1   . VAL   F 2  120 ? -31.421 63.846  -22.016  1.00 33.37  ? 122 VAL   B CG1   1 
ATOM   14924 C  CG2   . VAL   F 2  120 ? -30.221 62.761  -20.098  1.00 25.73  ? 122 VAL   B CG2   1 
ATOM   14925 N  N     . ARG   F 2  121 ? -33.591 65.799  -19.953  1.00 45.56  ? 123 ARG   B N     1 
ATOM   14926 C  CA    . ARG   F 2  121 ? -34.667 66.720  -20.314  1.00 52.26  ? 123 ARG   B CA    1 
ATOM   14927 C  C     . ARG   F 2  121 ? -34.317 68.145  -19.912  1.00 50.83  ? 123 ARG   B C     1 
ATOM   14928 O  O     . ARG   F 2  121 ? -34.253 69.048  -20.757  1.00 52.58  ? 123 ARG   B O     1 
ATOM   14929 C  CB    . ARG   F 2  121 ? -35.971 66.287  -19.638  1.00 48.90  ? 123 ARG   B CB    1 
ATOM   14930 C  CG    . ARG   F 2  121 ? -37.238 66.485  -20.453  1.00 53.21  ? 123 ARG   B CG    1 
ATOM   14931 C  CD    . ARG   F 2  121 ? -38.028 65.181  -20.466  1.00 49.59  ? 123 ARG   B CD    1 
ATOM   14932 N  NE    . ARG   F 2  121 ? -37.908 64.530  -19.165  1.00 58.47  ? 123 ARG   B NE    1 
ATOM   14933 C  CZ    . ARG   F 2  121 ? -38.087 63.237  -18.935  1.00 45.25  ? 123 ARG   B CZ    1 
ATOM   14934 N  NH1   . ARG   F 2  121 ? -38.460 62.408  -19.894  1.00 44.14  ? 123 ARG   B NH1   1 
ATOM   14935 N  NH2   . ARG   F 2  121 ? -37.872 62.763  -17.713  1.00 50.62  ? 123 ARG   B NH2   1 
ATOM   14936 N  N     . LYS   F 2  122 ? -34.080 68.358  -18.611  1.00 39.81  ? 124 LYS   B N     1 
ATOM   14937 C  CA    . LYS   F 2  122 ? -33.768 69.696  -18.119  1.00 41.55  ? 124 LYS   B CA    1 
ATOM   14938 C  C     . LYS   F 2  122 ? -32.721 70.381  -18.990  1.00 46.40  ? 124 LYS   B C     1 
ATOM   14939 O  O     . LYS   F 2  122 ? -32.789 71.592  -19.222  1.00 49.28  ? 124 LYS   B O     1 
ATOM   14940 C  CB    . LYS   F 2  122 ? -33.286 69.607  -16.676  1.00 47.23  ? 124 LYS   B CB    1 
ATOM   14941 C  CG    . LYS   F 2  122 ? -33.429 70.859  -15.836  1.00 31.62  ? 124 LYS   B CG    1 
ATOM   14942 C  CD    . LYS   F 2  122 ? -32.999 70.497  -14.432  1.00 67.13  ? 124 LYS   B CD    1 
ATOM   14943 C  CE    . LYS   F 2  122 ? -33.487 69.070  -14.056  1.00 62.21  ? 124 LYS   B CE    1 
ATOM   14944 N  NZ    . LYS   F 2  122 ? -32.759 68.420  -12.903  1.00 52.42  ? 124 LYS   B NZ    1 
ATOM   14945 N  N     . GLU   F 2  123 ? -31.732 69.624  -19.462  1.00 46.91  ? 125 GLU   B N     1 
ATOM   14946 C  CA    . GLU   F 2  123 ? -30.718 70.182  -20.345  1.00 40.60  ? 125 GLU   B CA    1 
ATOM   14947 C  C     . GLU   F 2  123 ? -31.272 70.366  -21.747  1.00 39.66  ? 125 GLU   B C     1 
ATOM   14948 O  O     . GLU   F 2  123 ? -31.172 71.452  -22.321  1.00 43.24  ? 125 GLU   B O     1 
ATOM   14949 C  CB    . GLU   F 2  123 ? -29.483 69.278  -20.362  1.00 40.36  ? 125 GLU   B CB    1 
ATOM   14950 C  CG    . GLU   F 2  123 ? -28.585 69.463  -19.167  1.00 31.91  ? 125 GLU   B CG    1 
ATOM   14951 C  CD    . GLU   F 2  123 ? -27.921 70.828  -19.165  1.00 43.79  ? 125 GLU   B CD    1 
ATOM   14952 O  OE1   . GLU   F 2  123 ? -28.251 71.627  -20.077  1.00 43.52  ? 125 GLU   B OE1   1 
ATOM   14953 O  OE2   . GLU   F 2  123 ? -27.075 71.095  -18.268  1.00 39.08  ? 125 GLU   B OE2   1 
ATOM   14954 N  N     . SER   F 2  124 ? -31.870 69.318  -22.309  1.00 34.04  ? 126 SER   B N     1 
ATOM   14955 C  CA    . SER   F 2  124 ? -32.493 69.453  -23.616  1.00 38.79  ? 126 SER   B CA    1 
ATOM   14956 C  C     . SER   F 2  124 ? -33.497 70.601  -23.617  1.00 48.32  ? 126 SER   B C     1 
ATOM   14957 O  O     . SER   F 2  124 ? -33.383 71.540  -24.411  1.00 48.15  ? 126 SER   B O     1 
ATOM   14958 C  CB    . SER   F 2  124 ? -33.143 68.131  -24.023  1.00 44.12  ? 126 SER   B CB    1 
ATOM   14959 O  OG    . SER   F 2  124 ? -32.175 67.228  -24.566  1.00 47.39  ? 126 SER   B OG    1 
ATOM   14960 N  N     . GLU   F 2  125 ? -34.479 70.549  -22.709  1.00 56.56  ? 127 GLU   B N     1 
ATOM   14961 C  CA    . GLU   F 2  125 ? -35.435 71.639  -22.497  1.00 63.67  ? 127 GLU   B CA    1 
ATOM   14962 C  C     . GLU   F 2  125 ? -34.833 73.012  -22.789  1.00 57.62  ? 127 GLU   B C     1 
ATOM   14963 O  O     . GLU   F 2  125 ? -35.435 73.827  -23.492  1.00 59.78  ? 127 GLU   B O     1 
ATOM   14964 C  CB    . GLU   F 2  125 ? -35.955 71.636  -21.052  1.00 64.48  ? 127 GLU   B CB    1 
ATOM   14965 C  CG    . GLU   F 2  125 ? -36.650 70.367  -20.605  1.00 75.12  ? 127 GLU   B CG    1 
ATOM   14966 C  CD    . GLU   F 2  125 ? -37.897 70.075  -21.396  1.00 78.10  ? 127 GLU   B CD    1 
ATOM   14967 O  OE1   . GLU   F 2  125 ? -38.983 70.545  -20.975  1.00 77.91  ? 127 GLU   B OE1   1 
ATOM   14968 O  OE2   . GLU   F 2  125 ? -37.781 69.382  -22.437  1.00 75.96  ? 127 GLU   B OE2   1 
ATOM   14969 N  N     . SER   F 2  126 ? -33.644 73.263  -22.239  1.00 49.51  ? 128 SER   B N     1 
ATOM   14970 C  CA    . SER   F 2  126 ? -32.948 74.537  -22.321  1.00 47.49  ? 128 SER   B CA    1 
ATOM   14971 C  C     . SER   F 2  126 ? -32.458 74.887  -23.724  1.00 48.06  ? 128 SER   B C     1 
ATOM   14972 O  O     . SER   F 2  126 ? -31.977 76.008  -23.916  1.00 50.38  ? 128 SER   B O     1 
ATOM   14973 C  CB    . SER   F 2  126 ? -31.745 74.514  -21.370  1.00 39.90  ? 128 SER   B CB    1 
ATOM   14974 O  OG    . SER   F 2  126 ? -31.983 75.278  -20.204  1.00 59.31  ? 128 SER   B OG    1 
ATOM   14975 N  N     . CYS   F 2  127 ? -32.563 73.980  -24.700  1.00 41.89  ? 129 CYS   B N     1 
ATOM   14976 C  CA    . CYS   F 2  127 ? -31.758 74.066  -25.918  1.00 45.90  ? 129 CYS   B CA    1 
ATOM   14977 C  C     . CYS   F 2  127 ? -32.475 74.824  -27.034  1.00 43.33  ? 129 CYS   B C     1 
ATOM   14978 O  O     . CYS   F 2  127 ? -33.630 74.528  -27.361  1.00 40.56  ? 129 CYS   B O     1 
ATOM   14979 C  CB    . CYS   F 2  127 ? -31.359 72.665  -26.401  1.00 43.17  ? 129 CYS   B CB    1 
ATOM   14980 S  SG    . CYS   F 2  127 ? -29.924 71.944  -25.514  1.00 48.61  ? 129 CYS   B SG    1 
ATOM   14981 N  N     . ASP   F 2  128 ? -31.766 75.788  -27.631  1.00 40.07  ? 130 ASP   B N     1 
ATOM   14982 C  CA    . ASP   F 2  128 ? -32.304 76.527  -28.771  1.00 41.27  ? 130 ASP   B CA    1 
ATOM   14983 C  C     . ASP   F 2  128 ? -32.541 75.615  -29.967  1.00 42.68  ? 130 ASP   B C     1 
ATOM   14984 O  O     . ASP   F 2  128 ? -33.575 75.701  -30.630  1.00 39.47  ? 130 ASP   B O     1 
ATOM   14985 C  CB    . ASP   F 2  128 ? -31.340 77.653  -29.150  1.00 54.94  ? 130 ASP   B CB    1 
ATOM   14986 C  CG    . ASP   F 2  128 ? -31.980 78.701  -30.030  1.00 69.28  ? 130 ASP   B CG    1 
ATOM   14987 O  OD1   . ASP   F 2  128 ? -32.509 78.347  -31.109  1.00 65.26  ? 130 ASP   B OD1   1 
ATOM   14988 O  OD2   . ASP   F 2  128 ? -31.962 79.887  -29.630  1.00 86.16  ? 130 ASP   B OD2   1 
ATOM   14989 N  N     . CYS   F 2  129 ? -31.579 74.744  -30.269  1.00 55.57  ? 131 CYS   B N     1 
ATOM   14990 C  CA    . CYS   F 2  129 ? -31.630 73.902  -31.463  1.00 49.16  ? 131 CYS   B CA    1 
ATOM   14991 C  C     . CYS   F 2  129 ? -30.705 72.724  -31.153  1.00 45.90  ? 131 CYS   B C     1 
ATOM   14992 O  O     . CYS   F 2  129 ? -29.484 72.859  -31.238  1.00 42.35  ? 131 CYS   B O     1 
ATOM   14993 C  CB    . CYS   F 2  129 ? -31.196 74.688  -32.699  1.00 54.21  ? 131 CYS   B CB    1 
ATOM   14994 S  SG    . CYS   F 2  129 ? -30.902 73.783  -34.249  1.00 62.61  ? 131 CYS   B SG    1 
ATOM   14995 N  N     . LEU   F 2  130 ? -31.294 71.605  -30.737  1.00 47.73  ? 132 LEU   B N     1 
ATOM   14996 C  CA    . LEU   F 2  130 ? -30.539 70.475  -30.213  1.00 32.42  ? 132 LEU   B CA    1 
ATOM   14997 C  C     . LEU   F 2  130 ? -30.023 69.639  -31.373  1.00 42.25  ? 132 LEU   B C     1 
ATOM   14998 O  O     . LEU   F 2  130 ? -30.814 69.138  -32.182  1.00 47.25  ? 132 LEU   B O     1 
ATOM   14999 C  CB    . LEU   F 2  130 ? -31.429 69.641  -29.283  1.00 36.85  ? 132 LEU   B CB    1 
ATOM   15000 C  CG    . LEU   F 2  130 ? -30.912 68.397  -28.529  1.00 31.74  ? 132 LEU   B CG    1 
ATOM   15001 C  CD1   . LEU   F 2  130 ? -29.753 68.747  -27.609  1.00 35.25  ? 132 LEU   B CD1   1 
ATOM   15002 C  CD2   . LEU   F 2  130 ? -32.035 67.770  -27.733  1.00 25.70  ? 132 LEU   B CD2   1 
ATOM   15003 N  N     . GLN   F 2  131 ? -28.701 69.476  -31.475  1.00 39.75  ? 133 GLN   B N     1 
ATOM   15004 C  CA    . GLN   F 2  131 ? -28.212 68.579  -32.516  1.00 38.08  ? 133 GLN   B CA    1 
ATOM   15005 C  C     . GLN   F 2  131 ? -28.482 67.130  -32.148  1.00 34.23  ? 133 GLN   B C     1 
ATOM   15006 O  O     . GLN   F 2  131 ? -28.826 66.312  -33.006  1.00 35.62  ? 133 GLN   B O     1 
ATOM   15007 C  CB    . GLN   F 2  131 ? -26.724 68.754  -32.744  1.00 40.80  ? 133 GLN   B CB    1 
ATOM   15008 C  CG    . GLN   F 2  131 ? -26.210 70.125  -32.964  1.00 42.70  ? 133 GLN   B CG    1 
ATOM   15009 C  CD    . GLN   F 2  131 ? -24.761 70.025  -33.326  1.00 35.21  ? 133 GLN   B CD    1 
ATOM   15010 O  OE1   . GLN   F 2  131 ? -24.392 69.143  -34.097  1.00 32.29  ? 133 GLN   B OE1   1 
ATOM   15011 N  NE2   . GLN   F 2  131 ? -23.917 70.860  -32.718  1.00 31.20  ? 133 GLN   B NE2   1 
ATOM   15012 N  N     . GLY   F 2  132 ? -28.314 66.795  -30.889  1.00 31.25  ? 134 GLY   B N     1 
ATOM   15013 C  CA    . GLY   F 2  132 ? -28.356 65.422  -30.456  1.00 30.91  ? 134 GLY   B CA    1 
ATOM   15014 C  C     . GLY   F 2  132 ? -27.427 65.230  -29.270  1.00 33.49  ? 134 GLY   B C     1 
ATOM   15015 O  O     . GLY   F 2  132 ? -27.102 66.183  -28.548  1.00 29.84  ? 134 GLY   B O     1 
ATOM   15016 N  N     . PHE   F 2  133 ? -26.983 63.984  -29.117  1.00 30.53  ? 135 PHE   B N     1 
ATOM   15017 C  CA    . PHE   F 2  133 ? -26.329 63.523  -27.900  1.00 36.02  ? 135 PHE   B CA    1 
ATOM   15018 C  C     . PHE   F 2  133 ? -24.973 62.891  -28.214  1.00 37.67  ? 135 PHE   B C     1 
ATOM   15019 O  O     . PHE   F 2  133 ? -24.776 62.265  -29.272  1.00 30.27  ? 135 PHE   B O     1 
ATOM   15020 C  CB    . PHE   F 2  133 ? -27.259 62.538  -27.177  1.00 31.96  ? 135 PHE   B CB    1 
ATOM   15021 C  CG    . PHE   F 2  133 ? -28.660 63.053  -27.031  1.00 29.38  ? 135 PHE   B CG    1 
ATOM   15022 C  CD1   . PHE   F 2  133 ? -29.538 63.028  -28.099  1.00 37.04  ? 135 PHE   B CD1   1 
ATOM   15023 C  CD2   . PHE   F 2  133 ? -29.085 63.603  -25.841  1.00 31.90  ? 135 PHE   B CD2   1 
ATOM   15024 C  CE1   . PHE   F 2  133 ? -30.833 63.538  -27.975  1.00 32.73  ? 135 PHE   B CE1   1 
ATOM   15025 C  CE2   . PHE   F 2  133 ? -30.370 64.106  -25.705  1.00 37.63  ? 135 PHE   B CE2   1 
ATOM   15026 C  CZ    . PHE   F 2  133 ? -31.247 64.074  -26.781  1.00 35.99  ? 135 PHE   B CZ    1 
ATOM   15027 N  N     . GLN   F 2  134 ? -24.029 63.061  -27.291  1.00 28.24  ? 136 GLN   B N     1 
ATOM   15028 C  CA    . GLN   F 2  134 ? -22.775 62.334  -27.401  1.00 33.52  ? 136 GLN   B CA    1 
ATOM   15029 C  C     . GLN   F 2  134 ? -22.539 61.599  -26.090  1.00 35.89  ? 136 GLN   B C     1 
ATOM   15030 O  O     . GLN   F 2  134 ? -22.577 62.218  -25.022  1.00 32.70  ? 136 GLN   B O     1 
ATOM   15031 C  CB    . GLN   F 2  134 ? -21.602 63.266  -27.781  1.00 32.24  ? 136 GLN   B CB    1 
ATOM   15032 C  CG    . GLN   F 2  134 ? -20.873 63.953  -26.642  1.00 35.91  ? 136 GLN   B CG    1 
ATOM   15033 C  CD    . GLN   F 2  134 ? -19.473 64.503  -27.032  1.00 33.15  ? 136 GLN   B CD    1 
ATOM   15034 O  OE1   . GLN   F 2  134 ? -19.245 65.018  -28.129  1.00 28.80  ? 136 GLN   B OE1   1 
ATOM   15035 N  NE2   . GLN   F 2  134 ? -18.547 64.410  -26.099  1.00 34.46  ? 136 GLN   B NE2   1 
ATOM   15036 N  N     . LEU   F 2  135 ? -22.338 60.273  -26.176  1.00 30.94  ? 137 LEU   B N     1 
ATOM   15037 C  CA    . LEU   F 2  135 ? -22.141 59.402  -25.017  1.00 28.99  ? 137 LEU   B CA    1 
ATOM   15038 C  C     . LEU   F 2  135 ? -20.744 58.797  -25.014  1.00 32.09  ? 137 LEU   B C     1 
ATOM   15039 O  O     . LEU   F 2  135 ? -20.352 58.130  -25.981  1.00 28.07  ? 137 LEU   B O     1 
ATOM   15040 C  CB    . LEU   F 2  135 ? -23.151 58.246  -24.993  1.00 32.46  ? 137 LEU   B CB    1 
ATOM   15041 C  CG    . LEU   F 2  135 ? -22.931 57.216  -23.865  1.00 24.89  ? 137 LEU   B CG    1 
ATOM   15042 C  CD1   . LEU   F 2  135 ? -23.512 57.703  -22.600  1.00 21.14  ? 137 LEU   B CD1   1 
ATOM   15043 C  CD2   . LEU   F 2  135 ? -23.482 55.844  -24.187  1.00 28.22  ? 137 LEU   B CD2   1 
ATOM   15044 N  N     . THR   F 2  136 ? -20.018 58.991  -23.908  1.00 29.32  ? 138 THR   B N     1 
ATOM   15045 C  CA    . THR   F 2  136 ? -18.764 58.292  -23.642  1.00 28.72  ? 138 THR   B CA    1 
ATOM   15046 C  C     . THR   F 2  136 ? -19.034 57.131  -22.693  1.00 31.04  ? 138 THR   B C     1 
ATOM   15047 O  O     . THR   F 2  136 ? -19.771 57.273  -21.710  1.00 32.65  ? 138 THR   B O     1 
ATOM   15048 C  CB    . THR   F 2  136 ? -17.690 59.223  -23.038  1.00 24.99  ? 138 THR   B CB    1 
ATOM   15049 O  OG1   . THR   F 2  136 ? -18.248 60.024  -21.980  1.00 27.83  ? 138 THR   B OG1   1 
ATOM   15050 C  CG2   . THR   F 2  136 ? -17.113 60.152  -24.089  1.00 28.72  ? 138 THR   B CG2   1 
ATOM   15051 N  N     . HIS   F 2  137 ? -18.418 55.987  -22.978  1.00 25.18  ? 139 HIS   B N     1 
ATOM   15052 C  CA    . HIS   F 2  137 ? -18.639 54.796  -22.172  1.00 24.64  ? 139 HIS   B CA    1 
ATOM   15053 C  C     . HIS   F 2  137 ? -17.771 53.675  -22.725  1.00 30.85  ? 139 HIS   B C     1 
ATOM   15054 O  O     . HIS   F 2  137 ? -17.351 53.706  -23.895  1.00 25.76  ? 139 HIS   B O     1 
ATOM   15055 C  CB    . HIS   F 2  137 ? -20.120 54.355  -22.174  1.00 24.03  ? 139 HIS   B CB    1 
ATOM   15056 C  CG    . HIS   F 2  137 ? -20.602 53.878  -23.511  1.00 27.32  ? 139 HIS   B CG    1 
ATOM   15057 N  ND1   . HIS   F 2  137 ? -21.540 52.881  -23.653  1.00 23.74  ? 139 HIS   B ND1   1 
ATOM   15058 C  CD2   . HIS   F 2  137 ? -20.265 54.259  -24.770  1.00 31.42  ? 139 HIS   B CD2   1 
ATOM   15059 C  CE1   . HIS   F 2  137 ? -21.765 52.670  -24.939  1.00 28.68  ? 139 HIS   B CE1   1 
ATOM   15060 N  NE2   . HIS   F 2  137 ? -20.999 53.489  -25.639  1.00 26.93  ? 139 HIS   B NE2   1 
ATOM   15061 N  N     . SER   F 2  138 ? -17.538 52.664  -21.878  1.00 19.88  ? 140 SER   B N     1 
ATOM   15062 C  CA    . SER   F 2  138 ? -16.912 51.423  -22.299  1.00 22.95  ? 140 SER   B CA    1 
ATOM   15063 C  C     . SER   F 2  138 ? -17.968 50.377  -22.620  1.00 24.54  ? 140 SER   B C     1 
ATOM   15064 O  O     . SER   F 2  138 ? -19.089 50.414  -22.099  1.00 22.46  ? 140 SER   B O     1 
ATOM   15065 C  CB    . SER   F 2  138 ? -16.012 50.880  -21.212  1.00 26.06  ? 140 SER   B CB    1 
ATOM   15066 O  OG    . SER   F 2  138 ? -16.879 50.428  -20.206  1.00 29.62  ? 140 SER   B OG    1 
ATOM   15067 N  N     . LEU   F 2  139 ? -17.587 49.418  -23.477  1.00 22.70  ? 141 LEU   B N     1 
ATOM   15068 C  CA    . LEU   F 2  139 ? -18.484 48.319  -23.823  1.00 21.40  ? 141 LEU   B CA    1 
ATOM   15069 C  C     . LEU   F 2  139 ? -18.223 47.047  -23.035  1.00 25.08  ? 141 LEU   B C     1 
ATOM   15070 O  O     . LEU   F 2  139 ? -19.015 46.104  -23.150  1.00 22.22  ? 141 LEU   B O     1 
ATOM   15071 C  CB    . LEU   F 2  139 ? -18.405 47.994  -25.311  1.00 24.25  ? 141 LEU   B CB    1 
ATOM   15072 C  CG    . LEU   F 2  139 ? -18.688 49.207  -26.200  1.00 26.98  ? 141 LEU   B CG    1 
ATOM   15073 C  CD1   . LEU   F 2  139 ? -18.810 48.840  -27.708  1.00 22.29  ? 141 LEU   B CD1   1 
ATOM   15074 C  CD2   . LEU   F 2  139 ? -19.893 49.945  -25.669  1.00 15.67  ? 141 LEU   B CD2   1 
ATOM   15075 N  N     . GLY   F 2  140 ? -17.164 47.011  -22.221  1.00 22.88  ? 142 GLY   B N     1 
ATOM   15076 C  CA    . GLY   F 2  140 ? -16.752 45.789  -21.549  1.00 28.14  ? 142 GLY   B CA    1 
ATOM   15077 C  C     . GLY   F 2  140 ? -17.280 45.591  -20.140  1.00 24.14  ? 142 GLY   B C     1 
ATOM   15078 O  O     . GLY   F 2  140 ? -17.336 44.464  -19.645  1.00 21.85  ? 142 GLY   B O     1 
ATOM   15079 N  N     . GLY   F 2  141 ? -17.679 46.669  -19.493  1.00 20.95  ? 143 GLY   B N     1 
ATOM   15080 C  CA    . GLY   F 2  141 ? -18.225 46.618  -18.148  1.00 19.76  ? 143 GLY   B CA    1 
ATOM   15081 C  C     . GLY   F 2  141 ? -19.727 46.417  -18.091  1.00 23.54  ? 143 GLY   B C     1 
ATOM   15082 O  O     . GLY   F 2  141 ? -20.344 45.795  -18.972  1.00 25.36  ? 143 GLY   B O     1 
ATOM   15083 N  N     . GLY   F 2  142 ? -20.317 46.957  -17.031  1.00 16.87  ? 144 GLY   B N     1 
ATOM   15084 C  CA    . GLY   F 2  142 ? -21.722 46.805  -16.764  1.00 22.16  ? 144 GLY   B CA    1 
ATOM   15085 C  C     . GLY   F 2  142 ? -22.465 48.109  -16.913  1.00 21.62  ? 144 GLY   B C     1 
ATOM   15086 O  O     . GLY   F 2  142 ? -23.513 48.136  -17.559  1.00 26.43  ? 144 GLY   B O     1 
ATOM   15087 N  N     . THR   F 2  143 ? -21.947 49.194  -16.327  1.00 18.08  ? 145 THR   B N     1 
ATOM   15088 C  CA    . THR   F 2  143 ? -22.690 50.462  -16.345  1.00 22.31  ? 145 THR   B CA    1 
ATOM   15089 C  C     . THR   F 2  143 ? -22.653 51.152  -17.705  1.00 28.76  ? 145 THR   B C     1 
ATOM   15090 O  O     . THR   F 2  143 ? -23.688 51.283  -18.368  1.00 31.26  ? 145 THR   B O     1 
ATOM   15091 C  CB    . THR   F 2  143 ? -22.175 51.422  -15.279  1.00 18.66  ? 145 THR   B CB    1 
ATOM   15092 O  OG1   . THR   F 2  143 ? -22.175 50.772  -14.019  1.00 15.76  ? 145 THR   B OG1   1 
ATOM   15093 C  CG2   . THR   F 2  143 ? -23.085 52.627  -15.211  1.00 26.57  ? 145 THR   B CG2   1 
ATOM   15094 N  N     . GLY   F 2  144 ? -21.474 51.651  -18.118  1.00 23.79  ? 146 GLY   B N     1 
ATOM   15095 C  CA    . GLY   F 2  144 ? -21.384 52.272  -19.432  1.00 25.02  ? 146 GLY   B CA    1 
ATOM   15096 C  C     . GLY   F 2  144 ? -22.006 51.400  -20.494  1.00 23.35  ? 146 GLY   B C     1 
ATOM   15097 O  O     . GLY   F 2  144 ? -22.766 51.874  -21.345  1.00 27.55  ? 146 GLY   B O     1 
ATOM   15098 N  N     . SER   F 2  145 ? -21.755 50.101  -20.405  1.00 23.90  ? 147 SER   B N     1 
ATOM   15099 C  CA    . SER   F 2  145 ? -22.150 49.164  -21.442  1.00 21.65  ? 147 SER   B CA    1 
ATOM   15100 C  C     . SER   F 2  145 ? -23.657 48.911  -21.417  1.00 30.59  ? 147 SER   B C     1 
ATOM   15101 O  O     . SER   F 2  145 ? -24.357 49.129  -22.416  1.00 27.20  ? 147 SER   B O     1 
ATOM   15102 C  CB    . SER   F 2  145 ? -21.373 47.862  -21.248  1.00 22.79  ? 147 SER   B CB    1 
ATOM   15103 O  OG    . SER   F 2  145 ? -21.757 46.875  -22.183  1.00 31.36  ? 147 SER   B OG    1 
ATOM   15104 N  N     . GLY   F 2  146 ? -24.175 48.437  -20.279  1.00 29.40  ? 148 GLY   B N     1 
ATOM   15105 C  CA    . GLY   F 2  146 ? -25.553 48.000  -20.189  1.00 24.51  ? 148 GLY   B CA    1 
ATOM   15106 C  C     . GLY   F 2  146 ? -26.525 49.128  -19.905  1.00 32.38  ? 148 GLY   B C     1 
ATOM   15107 O  O     . GLY   F 2  146 ? -27.594 49.217  -20.526  1.00 27.46  ? 148 GLY   B O     1 
ATOM   15108 N  N     . MET   F 2  147 ? -26.167 49.998  -18.956  1.00 26.81  ? 149 MET   B N     1 
ATOM   15109 C  CA    . MET   F 2  147 ? -27.011 51.156  -18.697  1.00 33.28  ? 149 MET   B CA    1 
ATOM   15110 C  C     . MET   F 2  147 ? -26.767 52.259  -19.724  1.00 29.18  ? 149 MET   B C     1 
ATOM   15111 O  O     . MET   F 2  147 ? -27.672 53.047  -20.015  1.00 30.28  ? 149 MET   B O     1 
ATOM   15112 C  CB    . MET   F 2  147 ? -26.787 51.666  -17.261  1.00 25.37  ? 149 MET   B CB    1 
ATOM   15113 C  CG    . MET   F 2  147 ? -27.679 52.833  -16.878  1.00 26.03  ? 149 MET   B CG    1 
ATOM   15114 S  SD    . MET   F 2  147 ? -27.435 53.586  -15.249  1.00 31.85  ? 149 MET   B SD    1 
ATOM   15115 C  CE    . MET   F 2  147 ? -28.853 54.698  -15.179  1.00 29.73  ? 149 MET   B CE    1 
ATOM   15116 N  N     . GLY   F 2  148 ? -25.555 52.331  -20.275  1.00 33.83  ? 150 GLY   B N     1 
ATOM   15117 C  CA    . GLY   F 2  148 ? -25.288 53.297  -21.326  1.00 26.15  ? 150 GLY   B CA    1 
ATOM   15118 C  C     . GLY   F 2  148 ? -26.153 53.062  -22.546  1.00 27.30  ? 150 GLY   B C     1 
ATOM   15119 O  O     . GLY   F 2  148 ? -26.753 53.990  -23.084  1.00 28.02  ? 150 GLY   B O     1 
ATOM   15120 N  N     . THR   F 2  149 ? -26.243 51.808  -22.991  1.00 29.70  ? 151 THR   B N     1 
ATOM   15121 C  CA    . THR   F 2  149 ? -27.107 51.510  -24.123  1.00 27.99  ? 151 THR   B CA    1 
ATOM   15122 C  C     . THR   F 2  149 ? -28.584 51.462  -23.747  1.00 31.25  ? 151 THR   B C     1 
ATOM   15123 O  O     . THR   F 2  149 ? -29.436 51.661  -24.625  1.00 35.34  ? 151 THR   B O     1 
ATOM   15124 C  CB    . THR   F 2  149 ? -26.696 50.196  -24.777  1.00 22.24  ? 151 THR   B CB    1 
ATOM   15125 O  OG1   . THR   F 2  149 ? -26.898 49.140  -23.855  1.00 26.86  ? 151 THR   B OG1   1 
ATOM   15126 C  CG2   . THR   F 2  149 ? -25.245 50.251  -25.180  1.00 25.82  ? 151 THR   B CG2   1 
ATOM   15127 N  N     . LEU   F 2  150 ? -28.917 51.217  -22.477  1.00 31.53  ? 152 LEU   B N     1 
ATOM   15128 C  CA    . LEU   F 2  150 ? -30.287 51.449  -22.037  1.00 27.30  ? 152 LEU   B CA    1 
ATOM   15129 C  C     . LEU   F 2  150 ? -30.664 52.914  -22.222  1.00 30.61  ? 152 LEU   B C     1 
ATOM   15130 O  O     . LEU   F 2  150 ? -31.601 53.241  -22.963  1.00 33.02  ? 152 LEU   B O     1 
ATOM   15131 C  CB    . LEU   F 2  150 ? -30.463 51.025  -20.587  1.00 27.06  ? 152 LEU   B CB    1 
ATOM   15132 C  CG    . LEU   F 2  150 ? -31.897 51.294  -20.115  1.00 33.64  ? 152 LEU   B CG    1 
ATOM   15133 C  CD1   . LEU   F 2  150 ? -32.935 50.548  -20.962  1.00 23.96  ? 152 LEU   B CD1   1 
ATOM   15134 C  CD2   . LEU   F 2  150 ? -32.064 50.998  -18.645  1.00 28.10  ? 152 LEU   B CD2   1 
ATOM   15135 N  N     . LEU   F 2  151 ? -29.908 53.811  -21.580  1.00 30.56  ? 153 LEU   B N     1 
ATOM   15136 C  CA    . LEU   F 2  151 ? -30.039 55.261  -21.758  1.00 32.62  ? 153 LEU   B CA    1 
ATOM   15137 C  C     . LEU   F 2  151 ? -30.203 55.691  -23.213  1.00 32.05  ? 153 LEU   B C     1 
ATOM   15138 O  O     . LEU   F 2  151 ? -31.035 56.546  -23.529  1.00 35.66  ? 153 LEU   B O     1 
ATOM   15139 C  CB    . LEU   F 2  151 ? -28.813 55.955  -21.153  1.00 29.25  ? 153 LEU   B CB    1 
ATOM   15140 C  CG    . LEU   F 2  151 ? -28.993 56.381  -19.704  1.00 29.59  ? 153 LEU   B CG    1 
ATOM   15141 C  CD1   . LEU   F 2  151 ? -27.730 57.038  -19.164  1.00 29.71  ? 153 LEU   B CD1   1 
ATOM   15142 C  CD2   . LEU   F 2  151 ? -30.190 57.324  -19.641  1.00 30.30  ? 153 LEU   B CD2   1 
ATOM   15143 N  N     . ILE   F 2  152 ? -29.387 55.131  -24.110  1.00 35.57  ? 154 ILE   B N     1 
ATOM   15144 C  CA    . ILE   F 2  152 ? -29.482 55.470  -25.526  1.00 28.20  ? 154 ILE   B CA    1 
ATOM   15145 C  C     . ILE   F 2  152 ? -30.852 55.088  -26.073  1.00 31.89  ? 154 ILE   B C     1 
ATOM   15146 O  O     . ILE   F 2  152 ? -31.457 55.835  -26.845  1.00 33.05  ? 154 ILE   B O     1 
ATOM   15147 C  CB    . ILE   F 2  152 ? -28.337 54.792  -26.300  1.00 27.91  ? 154 ILE   B CB    1 
ATOM   15148 C  CG1   . ILE   F 2  152 ? -27.023 55.561  -26.093  1.00 23.62  ? 154 ILE   B CG1   1 
ATOM   15149 C  CG2   . ILE   F 2  152 ? -28.681 54.641  -27.770  1.00 24.98  ? 154 ILE   B CG2   1 
ATOM   15150 C  CD1   . ILE   F 2  152 ? -25.835 54.893  -26.717  1.00 19.79  ? 154 ILE   B CD1   1 
ATOM   15151 N  N     . SER   F 2  153 ? -31.375 53.929  -25.664  1.00 38.13  ? 155 SER   B N     1 
ATOM   15152 C  CA    . SER   F 2  153 ? -32.676 53.484  -26.162  1.00 35.24  ? 155 SER   B CA    1 
ATOM   15153 C  C     . SER   F 2  153 ? -33.795 54.397  -25.682  1.00 38.16  ? 155 SER   B C     1 
ATOM   15154 O  O     . SER   F 2  153 ? -34.687 54.756  -26.453  1.00 33.72  ? 155 SER   B O     1 
ATOM   15155 C  CB    . SER   F 2  153 ? -32.945 52.055  -25.709  1.00 37.89  ? 155 SER   B CB    1 
ATOM   15156 O  OG    . SER   F 2  153 ? -34.152 51.579  -26.255  1.00 41.77  ? 155 SER   B OG    1 
ATOM   15157 N  N     . LYS   F 2  154 ? -33.765 54.761  -24.399  1.00 42.54  ? 156 LYS   B N     1 
ATOM   15158 C  CA    . LYS   F 2  154 ? -34.696 55.735  -23.844  1.00 37.28  ? 156 LYS   B CA    1 
ATOM   15159 C  C     . LYS   F 2  154 ? -34.627 57.056  -24.600  1.00 38.40  ? 156 LYS   B C     1 
ATOM   15160 O  O     . LYS   F 2  154 ? -35.633 57.540  -25.129  1.00 37.63  ? 156 LYS   B O     1 
ATOM   15161 C  CB    . LYS   F 2  154 ? -34.380 55.955  -22.360  1.00 32.88  ? 156 LYS   B CB    1 
ATOM   15162 C  CG    . LYS   F 2  154 ? -34.378 54.688  -21.518  1.00 33.61  ? 156 LYS   B CG    1 
ATOM   15163 C  CD    . LYS   F 2  154 ? -35.716 53.963  -21.551  1.00 29.18  ? 156 LYS   B CD    1 
ATOM   15164 C  CE    . LYS   F 2  154 ? -36.182 53.656  -20.139  1.00 40.87  ? 156 LYS   B CE    1 
ATOM   15165 N  NZ    . LYS   F 2  154 ? -36.842 52.324  -20.017  1.00 49.10  ? 156 LYS   B NZ    1 
ATOM   15166 N  N     . ILE   F 2  155 ? -33.435 57.659  -24.643  1.00 40.50  ? 157 ILE   B N     1 
ATOM   15167 C  CA    . ILE   F 2  155 ? -33.259 58.974  -25.258  1.00 36.34  ? 157 ILE   B CA    1 
ATOM   15168 C  C     . ILE   F 2  155 ? -33.793 58.988  -26.686  1.00 36.42  ? 157 ILE   B C     1 
ATOM   15169 O  O     . ILE   F 2  155 ? -34.472 59.934  -27.106  1.00 40.22  ? 157 ILE   B O     1 
ATOM   15170 C  CB    . ILE   F 2  155 ? -31.777 59.372  -25.184  1.00 26.49  ? 157 ILE   B CB    1 
ATOM   15171 C  CG1   . ILE   F 2  155 ? -31.369 59.398  -23.716  1.00 22.01  ? 157 ILE   B CG1   1 
ATOM   15172 C  CG2   . ILE   F 2  155 ? -31.511 60.686  -25.891  1.00 24.67  ? 157 ILE   B CG2   1 
ATOM   15173 C  CD1   . ILE   F 2  155 ? -30.087 60.115  -23.401  1.00 28.71  ? 157 ILE   B CD1   1 
ATOM   15174 N  N     . ARG   F 2  156 ? -33.531 57.930  -27.443  1.00 27.98  ? 158 ARG   B N     1 
ATOM   15175 C  CA    . ARG   F 2  156 ? -34.053 57.890  -28.801  1.00 35.76  ? 158 ARG   B CA    1 
ATOM   15176 C  C     . ARG   F 2  156 ? -35.573 57.820  -28.813  1.00 40.61  ? 158 ARG   B C     1 
ATOM   15177 O  O     . ARG   F 2  156 ? -36.206 58.258  -29.788  1.00 40.44  ? 158 ARG   B O     1 
ATOM   15178 C  CB    . ARG   F 2  156 ? -33.458 56.711  -29.584  1.00 26.86  ? 158 ARG   B CB    1 
ATOM   15179 C  CG    . ARG   F 2  156 ? -33.812 56.747  -31.064  1.00 29.18  ? 158 ARG   B CG    1 
ATOM   15180 C  CD    . ARG   F 2  156 ? -32.885 55.854  -31.840  1.00 33.29  ? 158 ARG   B CD    1 
ATOM   15181 N  NE    . ARG   F 2  156 ? -33.272 55.703  -33.231  1.00 31.83  ? 158 ARG   B NE    1 
ATOM   15182 C  CZ    . ARG   F 2  156 ? -33.162 54.566  -33.909  1.00 42.03  ? 158 ARG   B CZ    1 
ATOM   15183 N  NH1   . ARG   F 2  156 ? -32.751 53.451  -33.325  1.00 39.99  ? 158 ARG   B NH1   1 
ATOM   15184 N  NH2   . ARG   F 2  156 ? -33.468 54.543  -35.206  1.00 33.37  ? 158 ARG   B NH2   1 
ATOM   15185 N  N     . GLU   F 2  157 ? -36.180 57.257  -27.760  1.00 40.10  ? 159 GLU   B N     1 
ATOM   15186 C  CA    . GLU   F 2  157 ? -37.637 57.224  -27.709  1.00 39.66  ? 159 GLU   B CA    1 
ATOM   15187 C  C     . GLU   F 2  157 ? -38.201 58.634  -27.573  1.00 39.94  ? 159 GLU   B C     1 
ATOM   15188 O  O     . GLU   F 2  157 ? -39.242 58.955  -28.164  1.00 39.32  ? 159 GLU   B O     1 
ATOM   15189 C  CB    . GLU   F 2  157 ? -38.101 56.335  -26.564  1.00 38.74  ? 159 GLU   B CB    1 
ATOM   15190 C  CG    . GLU   F 2  157 ? -39.607 56.271  -26.378  1.00 37.59  ? 159 GLU   B CG    1 
ATOM   15191 C  CD    . GLU   F 2  157 ? -40.086 54.911  -25.859  1.00 52.37  ? 159 GLU   B CD    1 
ATOM   15192 O  OE1   . GLU   F 2  157 ? -39.744 54.548  -24.709  1.00 48.50  ? 159 GLU   B OE1   1 
ATOM   15193 O  OE2   . GLU   F 2  157 ? -40.796 54.201  -26.613  1.00 53.77  ? 159 GLU   B OE2   1 
ATOM   15194 N  N     . GLU   F 2  158 ? -37.509 59.494  -26.825  1.00 22.82  ? 160 GLU   B N     1 
ATOM   15195 C  CA    . GLU   F 2  158 ? -37.961 60.855  -26.596  1.00 34.82  ? 160 GLU   B CA    1 
ATOM   15196 C  C     . GLU   F 2  158 ? -37.537 61.805  -27.706  1.00 44.94  ? 160 GLU   B C     1 
ATOM   15197 O  O     . GLU   F 2  158 ? -38.294 62.716  -28.055  1.00 48.63  ? 160 GLU   B O     1 
ATOM   15198 C  CB    . GLU   F 2  158 ? -37.427 61.377  -25.257  1.00 37.01  ? 160 GLU   B CB    1 
ATOM   15199 C  CG    . GLU   F 2  158 ? -38.326 61.125  -24.081  1.00 36.83  ? 160 GLU   B CG    1 
ATOM   15200 C  CD    . GLU   F 2  158 ? -38.046 62.064  -22.924  1.00 46.49  ? 160 GLU   B CD    1 
ATOM   15201 O  OE1   . GLU   F 2  158 ? -38.315 63.281  -23.056  1.00 48.60  ? 160 GLU   B OE1   1 
ATOM   15202 O  OE2   . GLU   F 2  158 ? -37.559 61.579  -21.879  1.00 55.00  ? 160 GLU   B OE2   1 
ATOM   15203 N  N     . TYR   F 2  159 ? -36.340 61.627  -28.258  1.00 38.01  ? 161 TYR   B N     1 
ATOM   15204 C  CA    . TYR   F 2  159 ? -35.810 62.508  -29.295  1.00 35.73  ? 161 TYR   B CA    1 
ATOM   15205 C  C     . TYR   F 2  159 ? -35.532 61.700  -30.551  1.00 34.80  ? 161 TYR   B C     1 
ATOM   15206 O  O     . TYR   F 2  159 ? -34.392 61.636  -31.027  1.00 32.00  ? 161 TYR   B O     1 
ATOM   15207 C  CB    . TYR   F 2  159 ? -34.553 63.222  -28.811  1.00 35.81  ? 161 TYR   B CB    1 
ATOM   15208 C  CG    . TYR   F 2  159 ? -34.776 63.916  -27.492  1.00 44.43  ? 161 TYR   B CG    1 
ATOM   15209 C  CD1   . TYR   F 2  159 ? -34.584 63.239  -26.291  1.00 44.36  ? 161 TYR   B CD1   1 
ATOM   15210 C  CD2   . TYR   F 2  159 ? -35.194 65.244  -27.439  1.00 34.17  ? 161 TYR   B CD2   1 
ATOM   15211 C  CE1   . TYR   F 2  159 ? -34.790 63.873  -25.072  1.00 38.13  ? 161 TYR   B CE1   1 
ATOM   15212 C  CE2   . TYR   F 2  159 ? -35.395 65.881  -26.232  1.00 40.24  ? 161 TYR   B CE2   1 
ATOM   15213 C  CZ    . TYR   F 2  159 ? -35.191 65.183  -25.050  1.00 42.12  ? 161 TYR   B CZ    1 
ATOM   15214 O  OH    . TYR   F 2  159 ? -35.383 65.797  -23.837  1.00 56.51  ? 161 TYR   B OH    1 
ATOM   15215 N  N     . PRO   F 2  160 ? -36.567 61.079  -31.119  1.00 36.43  ? 162 PRO   B N     1 
ATOM   15216 C  CA    . PRO   F 2  160 ? -36.347 60.156  -32.244  1.00 29.60  ? 162 PRO   B CA    1 
ATOM   15217 C  C     . PRO   F 2  160 ? -35.654 60.801  -33.421  1.00 35.07  ? 162 PRO   B C     1 
ATOM   15218 O  O     . PRO   F 2  160 ? -35.058 60.089  -34.239  1.00 33.96  ? 162 PRO   B O     1 
ATOM   15219 C  CB    . PRO   F 2  160 ? -37.770 59.700  -32.614  1.00 28.38  ? 162 PRO   B CB    1 
ATOM   15220 C  CG    . PRO   F 2  160 ? -38.694 60.642  -31.962  1.00 25.02  ? 162 PRO   B CG    1 
ATOM   15221 C  CD    . PRO   F 2  160 ? -37.992 61.252  -30.785  1.00 28.29  ? 162 PRO   B CD    1 
ATOM   15222 N  N     . ASP   F 2  161 ? -35.690 62.129  -33.511  1.00 32.73  ? 163 ASP   B N     1 
ATOM   15223 C  CA    . ASP   F 2  161 ? -35.181 62.885  -34.643  1.00 37.08  ? 163 ASP   B CA    1 
ATOM   15224 C  C     . ASP   F 2  161 ? -33.953 63.718  -34.306  1.00 43.35  ? 163 ASP   B C     1 
ATOM   15225 O  O     . ASP   F 2  161 ? -33.681 64.697  -35.008  1.00 43.03  ? 163 ASP   B O     1 
ATOM   15226 C  CB    . ASP   F 2  161 ? -36.253 63.832  -35.144  1.00 41.41  ? 163 ASP   B CB    1 
ATOM   15227 C  CG    . ASP   F 2  161 ? -36.473 64.944  -34.173  1.00 39.24  ? 163 ASP   B CG    1 
ATOM   15228 O  OD1   . ASP   F 2  161 ? -36.359 64.666  -32.961  1.00 35.75  ? 163 ASP   B OD1   1 
ATOM   15229 O  OD2   . ASP   F 2  161 ? -36.732 66.074  -34.604  1.00 47.34  ? 163 ASP   B OD2   1 
ATOM   15230 N  N     . ARG   F 2  162 ? -33.247 63.405  -33.221  1.00 39.35  ? 164 ARG   B N     1 
ATOM   15231 C  CA    . ARG   F 2  162 ? -31.966 64.036  -32.934  1.00 35.80  ? 164 ARG   B CA    1 
ATOM   15232 C  C     . ARG   F 2  162 ? -30.850 63.027  -33.185  1.00 32.54  ? 164 ARG   B C     1 
ATOM   15233 O  O     . ARG   F 2  162 ? -31.095 61.835  -33.365  1.00 35.97  ? 164 ARG   B O     1 
ATOM   15234 C  CB    . ARG   F 2  162 ? -31.926 64.592  -31.503  1.00 39.43  ? 164 ARG   B CB    1 
ATOM   15235 C  CG    . ARG   F 2  162 ? -32.967 65.689  -31.195  1.00 38.94  ? 164 ARG   B CG    1 
ATOM   15236 C  CD    . ARG   F 2  162 ? -32.747 66.987  -31.984  1.00 43.95  ? 164 ARG   B CD    1 
ATOM   15237 N  NE    . ARG   F 2  162 ? -33.665 67.179  -33.117  1.00 59.69  ? 164 ARG   B NE    1 
ATOM   15238 C  CZ    . ARG   F 2  162 ? -33.363 67.851  -34.234  1.00 69.96  ? 164 ARG   B CZ    1 
ATOM   15239 N  NH1   . ARG   F 2  162 ? -32.144 68.343  -34.443  1.00 62.53  ? 164 ARG   B NH1   1 
ATOM   15240 N  NH2   . ARG   F 2  162 ? -34.302 68.029  -35.173  1.00 46.08  ? 164 ARG   B NH2   1 
ATOM   15241 N  N     . ILE   F 2  163 ? -29.614 63.504  -33.230  1.00 37.07  ? 165 ILE   B N     1 
ATOM   15242 C  CA    . ILE   F 2  163 ? -28.500 62.624  -33.571  1.00 29.76  ? 165 ILE   B CA    1 
ATOM   15243 C  C     . ILE   F 2  163 ? -27.986 61.965  -32.302  1.00 27.28  ? 165 ILE   B C     1 
ATOM   15244 O  O     . ILE   F 2  163 ? -27.912 62.585  -31.240  1.00 33.17  ? 165 ILE   B O     1 
ATOM   15245 C  CB    . ILE   F 2  163 ? -27.377 63.382  -34.315  1.00 31.28  ? 165 ILE   B CB    1 
ATOM   15246 C  CG1   . ILE   F 2  163 ? -27.856 63.873  -35.690  1.00 32.60  ? 165 ILE   B CG1   1 
ATOM   15247 C  CG2   . ILE   F 2  163 ? -26.171 62.469  -34.538  1.00 33.00  ? 165 ILE   B CG2   1 
ATOM   15248 C  CD1   . ILE   F 2  163 ? -28.225 62.756  -36.683  1.00 22.44  ? 165 ILE   B CD1   1 
ATOM   15249 N  N     . MET   F 2  164 ? -27.657 60.692  -32.407  1.00 28.07  ? 166 MET   B N     1 
ATOM   15250 C  CA    . MET   F 2  164 ? -27.102 59.926  -31.303  1.00 30.78  ? 166 MET   B CA    1 
ATOM   15251 C  C     . MET   F 2  164 ? -25.665 59.544  -31.657  1.00 34.98  ? 166 MET   B C     1 
ATOM   15252 O  O     . MET   F 2  164 ? -25.431 58.840  -32.649  1.00 32.63  ? 166 MET   B O     1 
ATOM   15253 C  CB    . MET   F 2  164 ? -27.964 58.693  -31.026  1.00 28.66  ? 166 MET   B CB    1 
ATOM   15254 C  CG    . MET   F 2  164 ? -27.527 57.847  -29.845  1.00 31.08  ? 166 MET   B CG    1 
ATOM   15255 S  SD    . MET   F 2  164 ? -27.445 58.782  -28.327  1.00 38.22  ? 166 MET   B SD    1 
ATOM   15256 C  CE    . MET   F 2  164 ? -25.816 58.304  -27.830  1.00 36.59  ? 166 MET   B CE    1 
ATOM   15257 N  N     . ASN   F 2  165 ? -24.712 60.000  -30.840  1.00 34.25  ? 167 ASN   B N     1 
ATOM   15258 C  CA    . ASN   F 2  165 ? -23.289 59.818  -31.103  1.00 31.95  ? 167 ASN   B CA    1 
ATOM   15259 C  C     . ASN   F 2  165 ? -22.597 59.217  -29.885  1.00 29.44  ? 167 ASN   B C     1 
ATOM   15260 O  O     . ASN   F 2  165 ? -22.780 59.701  -28.760  1.00 29.50  ? 167 ASN   B O     1 
ATOM   15261 C  CB    . ASN   F 2  165 ? -22.645 61.157  -31.470  1.00 33.66  ? 167 ASN   B CB    1 
ATOM   15262 C  CG    . ASN   F 2  165 ? -21.189 61.022  -31.810  1.00 35.12  ? 167 ASN   B CG    1 
ATOM   15263 O  OD1   . ASN   F 2  165 ? -20.832 60.474  -32.852  1.00 47.27  ? 167 ASN   B OD1   1 
ATOM   15264 N  ND2   . ASN   F 2  165 ? -20.336 61.520  -30.940  1.00 33.85  ? 167 ASN   B ND2   1 
ATOM   15265 N  N     . THR   F 2  166 ? -21.789 58.180  -30.102  1.00 23.15  ? 168 THR   B N     1 
ATOM   15266 C  CA    A THR   F 2  166 ? -21.095 57.539  -28.998  1.00 26.19  ? 168 THR   B CA    1 
ATOM   15267 C  CA    B THR   F 2  166 ? -21.098 57.511  -29.008  0.00 26.41  ? 168 THR   B CA    1 
ATOM   15268 C  C     . THR   F 2  166 ? -19.604 57.413  -29.282  1.00 28.08  ? 168 THR   B C     1 
ATOM   15269 O  O     . THR   F 2  166 ? -19.180 57.202  -30.428  1.00 27.52  ? 168 THR   B O     1 
ATOM   15270 C  CB    A THR   F 2  166 ? -21.684 56.160  -28.681  1.00 24.84  ? 168 THR   B CB    1 
ATOM   15271 C  CB    B THR   F 2  166 ? -21.667 56.105  -28.771  0.00 24.73  ? 168 THR   B CB    1 
ATOM   15272 O  OG1   A THR   F 2  166 ? -21.117 55.172  -29.535  1.00 26.15  ? 168 THR   B OG1   1 
ATOM   15273 O  OG1   B THR   F 2  166 ? -21.527 55.322  -29.963  0.00 25.94  ? 168 THR   B OG1   1 
ATOM   15274 C  CG2   A THR   F 2  166 ? -23.176 56.164  -28.852  1.00 23.81  ? 168 THR   B CG2   1 
ATOM   15275 C  CG2   B THR   F 2  166 ? -23.138 56.181  -28.389  0.00 25.21  ? 168 THR   B CG2   1 
ATOM   15276 N  N     . PHE   F 2  167 ? -18.815 57.591  -28.230  1.00 25.80  ? 169 PHE   B N     1 
ATOM   15277 C  CA    . PHE   F 2  167 ? -17.415 57.180  -28.194  1.00 27.77  ? 169 PHE   B CA    1 
ATOM   15278 C  C     . PHE   F 2  167 ? -17.422 55.938  -27.327  1.00 24.96  ? 169 PHE   B C     1 
ATOM   15279 O  O     . PHE   F 2  167 ? -17.663 56.039  -26.120  1.00 26.99  ? 169 PHE   B O     1 
ATOM   15280 C  CB    . PHE   F 2  167 ? -16.505 58.227  -27.563  1.00 26.76  ? 169 PHE   B CB    1 
ATOM   15281 C  CG    . PHE   F 2  167 ? -16.363 59.486  -28.349  1.00 30.54  ? 169 PHE   B CG    1 
ATOM   15282 C  CD1   . PHE   F 2  167 ? -17.294 60.496  -28.230  1.00 30.30  ? 169 PHE   B CD1   1 
ATOM   15283 C  CD2   . PHE   F 2  167 ? -15.258 59.687  -29.162  1.00 27.38  ? 169 PHE   B CD2   1 
ATOM   15284 C  CE1   . PHE   F 2  167 ? -17.146 61.682  -28.932  1.00 37.04  ? 169 PHE   B CE1   1 
ATOM   15285 C  CE2   . PHE   F 2  167 ? -15.099 60.867  -29.848  1.00 28.00  ? 169 PHE   B CE2   1 
ATOM   15286 C  CZ    . PHE   F 2  167 ? -16.054 61.861  -29.740  1.00 29.72  ? 169 PHE   B CZ    1 
ATOM   15287 N  N     . SER   F 2  168 ? -17.206 54.769  -27.933  1.00 23.99  ? 170 SER   B N     1 
ATOM   15288 C  CA    . SER   F 2  168 ? -17.409 53.487  -27.259  1.00 23.64  ? 170 SER   B CA    1 
ATOM   15289 C  C     . SER   F 2  168 ? -16.084 52.737  -27.171  1.00 24.28  ? 170 SER   B C     1 
ATOM   15290 O  O     . SER   F 2  168 ? -15.565 52.274  -28.191  1.00 24.02  ? 170 SER   B O     1 
ATOM   15291 C  CB    . SER   F 2  168 ? -18.468 52.664  -27.994  1.00 29.10  ? 170 SER   B CB    1 
ATOM   15292 O  OG    . SER   F 2  168 ? -19.638 53.439  -28.230  1.00 29.32  ? 170 SER   B OG    1 
ATOM   15293 N  N     . VAL   F 2  169 ? -15.555 52.596  -25.954  1.00 28.44  ? 171 VAL   B N     1 
ATOM   15294 C  CA    . VAL   F 2  169 ? -14.266 51.941  -25.729  1.00 25.16  ? 171 VAL   B CA    1 
ATOM   15295 C  C     . VAL   F 2  169 ? -14.432 50.426  -25.824  1.00 24.46  ? 171 VAL   B C     1 
ATOM   15296 O  O     . VAL   F 2  169 ? -15.200 49.821  -25.060  1.00 22.25  ? 171 VAL   B O     1 
ATOM   15297 C  CB    . VAL   F 2  169 ? -13.669 52.341  -24.371  1.00 29.50  ? 171 VAL   B CB    1 
ATOM   15298 C  CG1   . VAL   F 2  169 ? -12.244 51.788  -24.236  1.00 26.12  ? 171 VAL   B CG1   1 
ATOM   15299 C  CG2   . VAL   F 2  169 ? -13.667 53.842  -24.214  1.00 23.48  ? 171 VAL   B CG2   1 
ATOM   15300 N  N     . MET   F 2  170 ? -13.703 49.808  -26.764  1.00 22.30  ? 172 MET   B N     1 
ATOM   15301 C  CA    . MET   F 2  170 ? -13.897 48.373  -26.924  1.00 23.86  ? 172 MET   B CA    1 
ATOM   15302 C  C     . MET   F 2  170 ? -12.914 47.603  -26.050  1.00 29.99  ? 172 MET   B C     1 
ATOM   15303 O  O     . MET   F 2  170 ? -11.754 48.018  -25.891  1.00 27.80  ? 172 MET   B O     1 
ATOM   15304 C  CB    . MET   F 2  170 ? -13.703 47.949  -28.367  1.00 25.80  ? 172 MET   B CB    1 
ATOM   15305 C  CG    . MET   F 2  170 ? -14.209 48.949  -29.359  1.00 30.26  ? 172 MET   B CG    1 
ATOM   15306 S  SD    . MET   F 2  170 ? -15.990 48.891  -29.548  0.60 30.61  ? 172 MET   B SD    1 
ATOM   15307 C  CE    . MET   F 2  170 ? -16.260 47.129  -29.763  0.75 26.73  ? 172 MET   B CE    1 
ATOM   15308 N  N     . PRO   F 2  171 ? -13.376 46.493  -25.497  1.00 22.12  ? 173 PRO   B N     1 
ATOM   15309 C  CA    . PRO   F 2  171 ? -12.549 45.732  -24.567  1.00 20.71  ? 173 PRO   B CA    1 
ATOM   15310 C  C     . PRO   F 2  171 ? -11.499 44.902  -25.291  1.00 23.74  ? 173 PRO   B C     1 
ATOM   15311 O  O     . PRO   F 2  171 ? -11.684 44.476  -26.431  1.00 22.62  ? 173 PRO   B O     1 
ATOM   15312 C  CB    . PRO   F 2  171 ? -13.571 44.845  -23.858  1.00 17.96  ? 173 PRO   B CB    1 
ATOM   15313 C  CG    . PRO   F 2  171 ? -14.614 44.616  -24.906  1.00 22.29  ? 173 PRO   B CG    1 
ATOM   15314 C  CD    . PRO   F 2  171 ? -14.701 45.890  -25.692  1.00 23.07  ? 173 PRO   B CD    1 
ATOM   15315 N  N     . SER   F 2  172 ? -10.378 44.674  -24.600  1.00 25.16  ? 174 SER   B N     1 
ATOM   15316 C  CA    . SER   F 2  172 ? -9.251  43.922  -25.152  1.00 22.03  ? 174 SER   B CA    1 
ATOM   15317 C  C     . SER   F 2  172 ? -8.574  43.076  -24.077  1.00 22.72  ? 174 SER   B C     1 
ATOM   15318 O  O     . SER   F 2  172 ? -8.279  43.582  -22.980  1.00 24.17  ? 174 SER   B O     1 
ATOM   15319 C  CB    . SER   F 2  172 ? -8.236  44.869  -25.798  1.00 26.38  ? 174 SER   B CB    1 
ATOM   15320 O  OG    . SER   F 2  172 ? -7.011  44.198  -26.053  1.00 26.66  ? 174 SER   B OG    1 
ATOM   15321 N  N     . PRO   F 2  173 ? -8.305  41.797  -24.341  1.00 26.52  ? 175 PRO   B N     1 
ATOM   15322 C  CA    . PRO   F 2  173 ? -7.630  40.975  -23.318  1.00 25.75  ? 175 PRO   B CA    1 
ATOM   15323 C  C     . PRO   F 2  173 ? -6.219  41.437  -22.989  1.00 30.41  ? 175 PRO   B C     1 
ATOM   15324 O  O     . PRO   F 2  173 ? -5.647  40.942  -22.008  1.00 35.52  ? 175 PRO   B O     1 
ATOM   15325 C  CB    . PRO   F 2  173 ? -7.640  39.558  -23.921  1.00 21.01  ? 175 PRO   B CB    1 
ATOM   15326 C  CG    . PRO   F 2  173 ? -8.024  39.747  -25.378  1.00 41.54  ? 175 PRO   B CG    1 
ATOM   15327 C  CD    . PRO   F 2  173 ? -8.851  40.993  -25.447  1.00 28.96  ? 175 PRO   B CD    1 
ATOM   15328 N  N     . LYS   F 2  174 ? -5.635  42.367  -23.756  1.00 26.60  ? 176 LYS   B N     1 
ATOM   15329 C  CA    . LYS   F 2  174 ? -4.306  42.860  -23.411  1.00 28.86  ? 176 LYS   B CA    1 
ATOM   15330 C  C     . LYS   F 2  174 ? -4.347  43.816  -22.232  1.00 31.89  ? 176 LYS   B C     1 
ATOM   15331 O  O     . LYS   F 2  174 ? -3.303  44.093  -21.623  1.00 28.54  ? 176 LYS   B O     1 
ATOM   15332 C  CB    . LYS   F 2  174 ? -3.644  43.541  -24.625  1.00 23.81  ? 176 LYS   B CB    1 
ATOM   15333 C  CG    . LYS   F 2  174 ? -3.408  42.601  -25.836  1.00 29.70  ? 176 LYS   B CG    1 
ATOM   15334 C  CD    . LYS   F 2  174 ? -2.691  43.284  -27.015  1.00 35.31  ? 176 LYS   B CD    1 
ATOM   15335 C  CE    . LYS   F 2  174 ? -2.569  42.352  -28.227  1.00 38.79  ? 176 LYS   B CE    1 
ATOM   15336 N  NZ    . LYS   F 2  174 ? -1.754  42.920  -29.375  1.00 40.20  ? 176 LYS   B NZ    1 
ATOM   15337 N  N     . VAL   F 2  175 ? -5.530  44.318  -21.897  1.00 30.12  ? 177 VAL   B N     1 
ATOM   15338 C  CA    . VAL   F 2  175 ? -5.663  45.390  -20.926  1.00 23.33  ? 177 VAL   B CA    1 
ATOM   15339 C  C     . VAL   F 2  175 ? -6.506  44.993  -19.730  1.00 30.73  ? 177 VAL   B C     1 
ATOM   15340 O  O     . VAL   F 2  175 ? -6.375  45.605  -18.654  1.00 32.85  ? 177 VAL   B O     1 
ATOM   15341 C  CB    . VAL   F 2  175 ? -6.237  46.638  -21.613  1.00 24.72  ? 177 VAL   B CB    1 
ATOM   15342 C  CG1   . VAL   F 2  175 ? -6.663  47.699  -20.620  1.00 27.76  ? 177 VAL   B CG1   1 
ATOM   15343 C  CG2   . VAL   F 2  175 ? -5.185  47.172  -22.580  1.00 27.33  ? 177 VAL   B CG2   1 
ATOM   15344 N  N     . SER   F 2  176 ? -7.329  43.964  -19.845  1.00 28.11  ? 178 SER   B N     1 
ATOM   15345 C  CA    . SER   F 2  176 ? -8.214  43.612  -18.758  1.00 30.01  ? 178 SER   B CA    1 
ATOM   15346 C  C     . SER   F 2  176 ? -8.377  42.106  -18.784  1.00 27.68  ? 178 SER   B C     1 
ATOM   15347 O  O     . SER   F 2  176 ? -8.079  41.451  -19.783  1.00 28.98  ? 178 SER   B O     1 
ATOM   15348 C  CB    . SER   F 2  176 ? -9.558  44.341  -18.878  1.00 27.58  ? 178 SER   B CB    1 
ATOM   15349 O  OG    . SER   F 2  176 ? -10.222 43.934  -20.057  1.00 34.38  ? 178 SER   B OG    1 
ATOM   15350 N  N     . ASP   F 2  177 ? -8.838  41.563  -17.658  1.00 32.50  ? 179 ASP   B N     1 
ATOM   15351 C  CA    . ASP   F 2  177 ? -8.859  40.121  -17.454  1.00 27.83  ? 179 ASP   B CA    1 
ATOM   15352 C  C     . ASP   F 2  177 ? -10.205 39.617  -16.929  1.00 28.28  ? 179 ASP   B C     1 
ATOM   15353 O  O     . ASP   F 2  177 ? -10.284 38.486  -16.441  1.00 30.38  ? 179 ASP   B O     1 
ATOM   15354 C  CB    . ASP   F 2  177 ? -7.714  39.709  -16.517  1.00 24.70  ? 179 ASP   B CB    1 
ATOM   15355 C  CG    . ASP   F 2  177 ? -7.661  40.545  -15.239  1.00 34.38  ? 179 ASP   B CG    1 
ATOM   15356 O  OD1   . ASP   F 2  177 ? -8.702  41.104  -14.828  1.00 30.79  ? 179 ASP   B OD1   1 
ATOM   15357 O  OD2   . ASP   F 2  177 ? -6.567  40.644  -14.637  1.00 34.52  ? 179 ASP   B OD2   1 
ATOM   15358 N  N     . THR   F 2  178 ? -11.262 40.422  -17.019  1.00 21.05  ? 180 THR   B N     1 
ATOM   15359 C  CA    . THR   F 2  178 ? -12.615 39.946  -16.749  1.00 20.58  ? 180 THR   B CA    1 
ATOM   15360 C  C     . THR   F 2  178 ? -13.126 39.066  -17.899  1.00 23.77  ? 180 THR   B C     1 
ATOM   15361 O  O     . THR   F 2  178 ? -13.300 39.532  -19.032  1.00 23.58  ? 180 THR   B O     1 
ATOM   15362 C  CB    . THR   F 2  178 ? -13.549 41.127  -16.542  1.00 20.75  ? 180 THR   B CB    1 
ATOM   15363 O  OG1   . THR   F 2  178 ? -13.123 41.872  -15.406  1.00 28.52  ? 180 THR   B OG1   1 
ATOM   15364 C  CG2   . THR   F 2  178 ? -14.998 40.659  -16.366  1.00 19.17  ? 180 THR   B CG2   1 
ATOM   15365 N  N     . VAL   F 2  179 ? -13.427 37.806  -17.588  1.00 22.17  ? 181 VAL   B N     1 
ATOM   15366 C  CA    . VAL   F 2  179 ? -13.756 36.817  -18.602  1.00 19.92  ? 181 VAL   B CA    1 
ATOM   15367 C  C     . VAL   F 2  179 ? -15.058 37.097  -19.356  1.00 18.40  ? 181 VAL   B C     1 
ATOM   15368 O  O     . VAL   F 2  179 ? -15.217 36.589  -20.473  1.00 26.44  ? 181 VAL   B O     1 
ATOM   15369 C  CB    . VAL   F 2  179 ? -13.810 35.425  -17.941  1.00 18.95  ? 181 VAL   B CB    1 
ATOM   15370 C  CG1   . VAL   F 2  179 ? -15.084 35.295  -17.071  1.00 19.74  ? 181 VAL   B CG1   1 
ATOM   15371 C  CG2   . VAL   F 2  179 ? -13.713 34.323  -18.973  1.00 9.71   ? 181 VAL   B CG2   1 
ATOM   15372 N  N     . VAL   F 2  180 ? -15.998 37.874  -18.812  1.00 17.39  ? 182 VAL   B N     1 
ATOM   15373 C  CA    . VAL   F 2  180 ? -17.303 38.061  -19.468  1.00 17.83  ? 182 VAL   B CA    1 
ATOM   15374 C  C     . VAL   F 2  180 ? -17.354 39.315  -20.334  1.00 22.48  ? 182 VAL   B C     1 
ATOM   15375 O  O     . VAL   F 2  180 ? -18.425 39.643  -20.867  1.00 26.61  ? 182 VAL   B O     1 
ATOM   15376 C  CB    . VAL   F 2  180 ? -18.474 38.070  -18.474  1.00 15.63  ? 182 VAL   B CB    1 
ATOM   15377 C  CG1   . VAL   F 2  180 ? -18.548 36.759  -17.752  1.00 16.56  ? 182 VAL   B CG1   1 
ATOM   15378 C  CG2   . VAL   F 2  180 ? -18.421 39.292  -17.514  1.00 16.43  ? 182 VAL   B CG2   1 
ATOM   15379 N  N     . GLU   F 2  181 ? -16.247 40.014  -20.506  1.00 23.67  ? 183 GLU   B N     1 
ATOM   15380 C  CA    . GLU   F 2  181 ? -16.294 41.212  -21.339  1.00 23.39  ? 183 GLU   B CA    1 
ATOM   15381 C  C     . GLU   F 2  181 ? -16.793 40.955  -22.762  1.00 23.57  ? 183 GLU   B C     1 
ATOM   15382 O  O     . GLU   F 2  181 ? -17.483 41.837  -23.296  1.00 22.55  ? 183 GLU   B O     1 
ATOM   15383 C  CB    . GLU   F 2  181 ? -14.918 41.889  -21.366  1.00 22.17  ? 183 GLU   B CB    1 
ATOM   15384 C  CG    . GLU   F 2  181 ? -14.473 42.423  -20.006  1.00 21.72  ? 183 GLU   B CG    1 
ATOM   15385 C  CD    . GLU   F 2  181 ? -13.394 43.442  -20.125  1.00 21.80  ? 183 GLU   B CD    1 
ATOM   15386 O  OE1   . GLU   F 2  181 ? -12.540 43.332  -21.022  1.00 36.44  ? 183 GLU   B OE1   1 
ATOM   15387 O  OE2   . GLU   F 2  181 ? -13.385 44.372  -19.333  1.00 27.10  ? 183 GLU   B OE2   1 
ATOM   15388 N  N     . PRO   F 2  182 ? -16.469 39.841  -23.444  1.00 25.66  ? 184 PRO   B N     1 
ATOM   15389 C  CA    . PRO   F 2  182 ? -17.019 39.655  -24.798  1.00 23.88  ? 184 PRO   B CA    1 
ATOM   15390 C  C     . PRO   F 2  182 ? -18.537 39.565  -24.815  1.00 25.22  ? 184 PRO   B C     1 
ATOM   15391 O  O     . PRO   F 2  182 ? -19.164 40.060  -25.762  1.00 21.07  ? 184 PRO   B O     1 
ATOM   15392 C  CB    . PRO   F 2  182 ? -16.343 38.361  -25.277  1.00 25.84  ? 184 PRO   B CB    1 
ATOM   15393 C  CG    . PRO   F 2  182 ? -15.052 38.352  -24.569  1.00 15.83  ? 184 PRO   B CG    1 
ATOM   15394 C  CD    . PRO   F 2  182 ? -15.396 38.865  -23.183  1.00 21.76  ? 184 PRO   B CD    1 
ATOM   15395 N  N     . TYR   F 2  183 ? -19.153 38.998  -23.774  1.00 21.26  ? 185 TYR   B N     1 
ATOM   15396 C  CA    . TYR   F 2  183 ? -20.607 39.079  -23.639  1.00 23.28  ? 185 TYR   B CA    1 
ATOM   15397 C  C     . TYR   F 2  183 ? -21.086 40.530  -23.608  1.00 23.49  ? 185 TYR   B C     1 
ATOM   15398 O  O     . TYR   F 2  183 ? -21.947 40.938  -24.401  1.00 21.50  ? 185 TYR   B O     1 
ATOM   15399 C  CB    . TYR   F 2  183 ? -21.055 38.355  -22.373  1.00 24.77  ? 185 TYR   B CB    1 
ATOM   15400 C  CG    . TYR   F 2  183 ? -21.011 36.871  -22.477  1.00 25.38  ? 185 TYR   B CG    1 
ATOM   15401 C  CD1   . TYR   F 2  183 ? -20.945 36.251  -23.711  1.00 25.37  ? 185 TYR   B CD1   1 
ATOM   15402 C  CD2   . TYR   F 2  183 ? -21.041 36.083  -21.346  1.00 24.52  ? 185 TYR   B CD2   1 
ATOM   15403 C  CE1   . TYR   F 2  183 ? -20.914 34.886  -23.815  1.00 29.69  ? 185 TYR   B CE1   1 
ATOM   15404 C  CE2   . TYR   F 2  183 ? -21.023 34.691  -21.442  1.00 27.47  ? 185 TYR   B CE2   1 
ATOM   15405 C  CZ    . TYR   F 2  183 ? -20.945 34.098  -22.680  1.00 28.76  ? 185 TYR   B CZ    1 
ATOM   15406 O  OH    . TYR   F 2  183 ? -20.921 32.716  -22.798  1.00 26.99  ? 185 TYR   B OH    1 
ATOM   15407 N  N     . ASN   F 2  184 ? -20.551 41.319  -22.672  1.00 21.00  ? 186 ASN   B N     1 
ATOM   15408 C  CA    . ASN   F 2  184 ? -21.008 42.695  -22.500  1.00 25.27  ? 186 ASN   B CA    1 
ATOM   15409 C  C     . ASN   F 2  184 ? -20.791 43.526  -23.762  1.00 33.15  ? 186 ASN   B C     1 
ATOM   15410 O  O     . ASN   F 2  184 ? -21.589 44.435  -24.063  1.00 27.73  ? 186 ASN   B O     1 
ATOM   15411 C  CB    . ASN   F 2  184 ? -20.286 43.367  -21.327  1.00 27.38  ? 186 ASN   B CB    1 
ATOM   15412 C  CG    . ASN   F 2  184 ? -20.585 42.724  -19.998  1.00 26.06  ? 186 ASN   B CG    1 
ATOM   15413 O  OD1   . ASN   F 2  184 ? -21.577 42.025  -19.841  1.00 31.49  ? 186 ASN   B OD1   1 
ATOM   15414 N  ND2   . ASN   F 2  184 ? -19.711 42.945  -19.034  1.00 25.44  ? 186 ASN   B ND2   1 
ATOM   15415 N  N     . ALA   F 2  185 ? -19.708 43.252  -24.495  1.00 26.52  ? 187 ALA   B N     1 
ATOM   15416 C  CA    . ALA   F 2  185 ? -19.429 44.037  -25.684  1.00 21.20  ? 187 ALA   B CA    1 
ATOM   15417 C  C     . ALA   F 2  185 ? -20.375 43.656  -26.809  1.00 26.81  ? 187 ALA   B C     1 
ATOM   15418 O  O     . ALA   F 2  185 ? -20.848 44.530  -27.549  1.00 29.20  ? 187 ALA   B O     1 
ATOM   15419 C  CB    . ALA   F 2  185 ? -17.975 43.855  -26.113  1.00 23.87  ? 187 ALA   B CB    1 
ATOM   15420 N  N     . THR   F 2  186 ? -20.655 42.355  -26.956  1.00 23.35  ? 188 THR   B N     1 
ATOM   15421 C  CA    . THR   F 2  186 ? -21.551 41.908  -28.017  1.00 24.75  ? 188 THR   B CA    1 
ATOM   15422 C  C     . THR   F 2  186 ? -22.978 42.354  -27.735  1.00 27.79  ? 188 THR   B C     1 
ATOM   15423 O  O     . THR   F 2  186 ? -23.740 42.658  -28.660  1.00 33.96  ? 188 THR   B O     1 
ATOM   15424 C  CB    . THR   F 2  186 ? -21.501 40.382  -28.175  1.00 26.85  ? 188 THR   B CB    1 
ATOM   15425 O  OG1   . THR   F 2  186 ? -20.141 39.922  -28.241  1.00 28.61  ? 188 THR   B OG1   1 
ATOM   15426 C  CG2   . THR   F 2  186 ? -22.255 39.956  -29.410  1.00 19.42  ? 188 THR   B CG2   1 
ATOM   15427 N  N     . LEU   F 2  187 ? -23.372 42.375  -26.467  1.00 26.00  ? 189 LEU   B N     1 
ATOM   15428 C  CA    . LEU   F 2  187 ? -24.708 42.869  -26.168  1.00 30.24  ? 189 LEU   B CA    1 
ATOM   15429 C  C     . LEU   F 2  187 ? -24.808 44.360  -26.469  1.00 26.16  ? 189 LEU   B C     1 
ATOM   15430 O  O     . LEU   F 2  187 ? -25.861 44.838  -26.903  1.00 30.19  ? 189 LEU   B O     1 
ATOM   15431 C  CB    . LEU   F 2  187 ? -25.073 42.564  -24.702  1.00 23.85  ? 189 LEU   B CB    1 
ATOM   15432 C  CG    . LEU   F 2  187 ? -25.295 41.072  -24.370  1.00 28.65  ? 189 LEU   B CG    1 
ATOM   15433 C  CD1   . LEU   F 2  187 ? -25.239 40.790  -22.844  1.00 21.27  ? 189 LEU   B CD1   1 
ATOM   15434 C  CD2   . LEU   F 2  187 ? -26.614 40.535  -25.008  1.00 15.61  ? 189 LEU   B CD2   1 
ATOM   15435 N  N     . SER   F 2  188 ? -23.724 45.097  -26.249  1.00 20.42  ? 190 SER   B N     1 
ATOM   15436 C  CA    . SER   F 2  188 ? -23.730 46.533  -26.493  1.00 24.33  ? 190 SER   B CA    1 
ATOM   15437 C  C     . SER   F 2  188 ? -23.687 46.844  -27.978  1.00 22.57  ? 190 SER   B C     1 
ATOM   15438 O  O     . SER   F 2  188 ? -24.413 47.721  -28.442  1.00 23.95  ? 190 SER   B O     1 
ATOM   15439 C  CB    . SER   F 2  188 ? -22.552 47.203  -25.780  1.00 28.55  ? 190 SER   B CB    1 
ATOM   15440 O  OG    . SER   F 2  188 ? -22.762 47.218  -24.375  1.00 29.60  ? 190 SER   B OG    1 
ATOM   15441 N  N     . VAL   F 2  189 ? -22.849 46.139  -28.744  1.00 23.28  ? 191 VAL   B N     1 
ATOM   15442 C  CA    . VAL   F 2  189 ? -22.742 46.449  -30.161  1.00 23.75  ? 191 VAL   B CA    1 
ATOM   15443 C  C     . VAL   F 2  189 ? -24.091 46.237  -30.828  1.00 25.60  ? 191 VAL   B C     1 
ATOM   15444 O  O     . VAL   F 2  189 ? -24.493 46.998  -31.718  1.00 25.82  ? 191 VAL   B O     1 
ATOM   15445 C  CB    . VAL   F 2  189 ? -21.621 45.618  -30.825  1.00 22.42  ? 191 VAL   B CB    1 
ATOM   15446 C  CG1   . VAL   F 2  189 ? -21.765 45.620  -32.362  1.00 17.17  ? 191 VAL   B CG1   1 
ATOM   15447 C  CG2   . VAL   F 2  189 ? -20.231 46.127  -30.402  1.00 16.79  ? 191 VAL   B CG2   1 
ATOM   15448 N  N     . HIS   F 2  190 ? -24.825 45.222  -30.381  1.00 26.78  ? 192 HIS   B N     1 
ATOM   15449 C  CA    . HIS   F 2  190 ? -26.170 44.984  -30.893  1.00 26.72  ? 192 HIS   B CA    1 
ATOM   15450 C  C     . HIS   F 2  190 ? -27.028 46.236  -30.780  1.00 29.95  ? 192 HIS   B C     1 
ATOM   15451 O  O     . HIS   F 2  190 ? -27.691 46.650  -31.738  1.00 29.26  ? 192 HIS   B O     1 
ATOM   15452 C  CB    . HIS   F 2  190 ? -26.793 43.831  -30.122  1.00 31.92  ? 192 HIS   B CB    1 
ATOM   15453 C  CG    . HIS   F 2  190 ? -28.170 43.484  -30.575  1.00 39.31  ? 192 HIS   B CG    1 
ATOM   15454 N  ND1   . HIS   F 2  190 ? -28.538 43.505  -31.902  1.00 39.18  ? 192 HIS   B ND1   1 
ATOM   15455 C  CD2   . HIS   F 2  190 ? -29.268 43.108  -29.880  1.00 28.76  ? 192 HIS   B CD2   1 
ATOM   15456 C  CE1   . HIS   F 2  190 ? -29.809 43.163  -32.004  1.00 41.41  ? 192 HIS   B CE1   1 
ATOM   15457 N  NE2   . HIS   F 2  190 ? -30.274 42.916  -30.791  1.00 42.65  ? 192 HIS   B NE2   1 
ATOM   15458 N  N     . GLN   F 2  191 ? -27.004 46.865  -29.608  1.00 28.67  ? 193 GLN   B N     1 
ATOM   15459 C  CA    . GLN   F 2  191 ? -27.762 48.086  -29.393  1.00 27.96  ? 193 GLN   B CA    1 
ATOM   15460 C  C     . GLN   F 2  191 ? -27.223 49.225  -30.243  1.00 33.69  ? 193 GLN   B C     1 
ATOM   15461 O  O     . GLN   F 2  191 ? -27.995 50.024  -30.797  1.00 29.89  ? 193 GLN   B O     1 
ATOM   15462 C  CB    . GLN   F 2  191 ? -27.695 48.459  -27.920  1.00 19.33  ? 193 GLN   B CB    1 
ATOM   15463 C  CG    . GLN   F 2  191 ? -28.081 47.323  -27.020  1.00 25.72  ? 193 GLN   B CG    1 
ATOM   15464 C  CD    . GLN   F 2  191 ? -29.588 47.230  -26.889  1.00 29.78  ? 193 GLN   B CD    1 
ATOM   15465 O  OE1   . GLN   F 2  191 ? -30.255 48.244  -26.709  1.00 30.32  ? 193 GLN   B OE1   1 
ATOM   15466 N  NE2   . GLN   F 2  191 ? -30.132 46.022  -27.014  1.00 34.78  ? 193 GLN   B NE2   1 
ATOM   15467 N  N     . LEU   F 2  192 ? -25.893 49.330  -30.320  1.00 30.31  ? 194 LEU   B N     1 
ATOM   15468 C  CA    . LEU   F 2  192 ? -25.279 50.448  -31.018  1.00 31.42  ? 194 LEU   B CA    1 
ATOM   15469 C  C     . LEU   F 2  192 ? -25.596 50.384  -32.496  1.00 23.54  ? 194 LEU   B C     1 
ATOM   15470 O  O     . LEU   F 2  192 ? -25.916 51.407  -33.113  1.00 28.90  ? 194 LEU   B O     1 
ATOM   15471 C  CB    . LEU   F 2  192 ? -23.774 50.453  -30.776  1.00 24.32  ? 194 LEU   B CB    1 
ATOM   15472 C  CG    . LEU   F 2  192 ? -23.370 50.668  -29.320  1.00 19.59  ? 194 LEU   B CG    1 
ATOM   15473 C  CD1   . LEU   F 2  192 ? -21.879 50.356  -29.148  1.00 20.26  ? 194 LEU   B CD1   1 
ATOM   15474 C  CD2   . LEU   F 2  192 ? -23.681 52.091  -28.892  1.00 22.69  ? 194 LEU   B CD2   1 
ATOM   15475 N  N     . VAL   F 2  193 ? -25.553 49.185  -33.066  1.00 21.87  ? 195 VAL   B N     1 
ATOM   15476 C  CA    . VAL   F 2  193 ? -25.950 49.017  -34.458  1.00 27.55  ? 195 VAL   B CA    1 
ATOM   15477 C  C     . VAL   F 2  193 ? -27.354 49.561  -34.676  1.00 34.62  ? 195 VAL   B C     1 
ATOM   15478 O  O     . VAL   F 2  193 ? -27.636 50.197  -35.695  1.00 33.56  ? 195 VAL   B O     1 
ATOM   15479 C  CB    . VAL   F 2  193 ? -25.835 47.539  -34.871  1.00 25.33  ? 195 VAL   B CB    1 
ATOM   15480 C  CG1   . VAL   F 2  193 ? -26.760 47.232  -36.029  1.00 30.34  ? 195 VAL   B CG1   1 
ATOM   15481 C  CG2   . VAL   F 2  193 ? -24.403 47.234  -35.258  1.00 25.24  ? 195 VAL   B CG2   1 
ATOM   15482 N  N     . GLU   F 2  194 ? -28.245 49.362  -33.702  1.00 35.63  ? 196 GLU   B N     1 
ATOM   15483 C  CA    . GLU   F 2  194 ? -29.647 49.705  -33.901  1.00 30.32  ? 196 GLU   B CA    1 
ATOM   15484 C  C     . GLU   F 2  194 ? -29.954 51.171  -33.633  1.00 36.15  ? 196 GLU   B C     1 
ATOM   15485 O  O     . GLU   F 2  194 ? -30.800 51.745  -34.323  1.00 39.54  ? 196 GLU   B O     1 
ATOM   15486 C  CB    . GLU   F 2  194 ? -30.527 48.829  -33.014  1.00 32.78  ? 196 GLU   B CB    1 
ATOM   15487 C  CG    . GLU   F 2  194 ? -30.393 47.343  -33.267  1.00 35.41  ? 196 GLU   B CG    1 
ATOM   15488 C  CD    . GLU   F 2  194 ? -30.743 46.959  -34.677  1.00 44.22  ? 196 GLU   B CD    1 
ATOM   15489 O  OE1   . GLU   F 2  194 ? -31.553 47.686  -35.291  1.00 56.35  ? 196 GLU   B OE1   1 
ATOM   15490 O  OE2   . GLU   F 2  194 ? -30.201 45.945  -35.180  1.00 47.05  ? 196 GLU   B OE2   1 
ATOM   15491 N  N     . ASN   F 2  195 ? -29.277 51.801  -32.666  1.00 39.30  ? 197 ASN   B N     1 
ATOM   15492 C  CA    . ASN   F 2  195 ? -29.757 53.041  -32.068  1.00 32.76  ? 197 ASN   B CA    1 
ATOM   15493 C  C     . ASN   F 2  195 ? -28.756 54.197  -32.046  1.00 40.87  ? 197 ASN   B C     1 
ATOM   15494 O  O     . ASN   F 2  195 ? -29.051 55.231  -31.427  1.00 38.07  ? 197 ASN   B O     1 
ATOM   15495 C  CB    . ASN   F 2  195 ? -30.217 52.784  -30.630  1.00 31.61  ? 197 ASN   B CB    1 
ATOM   15496 C  CG    . ASN   F 2  195 ? -31.525 51.996  -30.552  1.00 41.84  ? 197 ASN   B CG    1 
ATOM   15497 O  OD1   . ASN   F 2  195 ? -32.479 52.236  -31.306  1.00 39.75  ? 197 ASN   B OD1   1 
ATOM   15498 N  ND2   . ASN   F 2  195 ? -31.575 51.060  -29.613  1.00 31.26  ? 197 ASN   B ND2   1 
ATOM   15499 N  N     . THR   F 2  196 ? -27.582 54.075  -32.660  1.00 31.88  ? 198 THR   B N     1 
ATOM   15500 C  CA    . THR   F 2  196 ? -26.734 55.256  -32.766  1.00 35.60  ? 198 THR   B CA    1 
ATOM   15501 C  C     . THR   F 2  196 ? -26.601 55.661  -34.230  1.00 36.22  ? 198 THR   B C     1 
ATOM   15502 O  O     . THR   F 2  196 ? -26.769 54.849  -35.147  1.00 30.29  ? 198 THR   B O     1 
ATOM   15503 C  CB    . THR   F 2  196 ? -25.326 55.058  -32.157  1.00 32.17  ? 198 THR   B CB    1 
ATOM   15504 O  OG1   . THR   F 2  196 ? -24.581 54.090  -32.917  1.00 35.39  ? 198 THR   B OG1   1 
ATOM   15505 C  CG2   . THR   F 2  196 ? -25.398 54.640  -30.703  1.00 18.21  ? 198 THR   B CG2   1 
ATOM   15506 N  N     . ASP   F 2  197 ? -26.276 56.939  -34.430  1.00 35.98  ? 199 ASP   B N     1 
ATOM   15507 C  CA    . ASP   F 2  197 ? -26.008 57.475  -35.754  1.00 33.76  ? 199 ASP   B CA    1 
ATOM   15508 C  C     . ASP   F 2  197 ? -24.530 57.407  -36.126  1.00 34.87  ? 199 ASP   B C     1 
ATOM   15509 O  O     . ASP   F 2  197 ? -24.186 57.127  -37.277  1.00 33.38  ? 199 ASP   B O     1 
ATOM   15510 C  CB    . ASP   F 2  197 ? -26.520 58.904  -35.806  1.00 39.57  ? 199 ASP   B CB    1 
ATOM   15511 C  CG    . ASP   F 2  197 ? -27.977 58.947  -35.639  1.00 30.55  ? 199 ASP   B CG    1 
ATOM   15512 O  OD1   . ASP   F 2  197 ? -28.613 58.284  -36.471  1.00 34.81  ? 199 ASP   B OD1   1 
ATOM   15513 O  OD2   . ASP   F 2  197 ? -28.475 59.559  -34.671  1.00 28.84  ? 199 ASP   B OD2   1 
ATOM   15514 N  N     . GLU   F 2  198 ? -23.647 57.627  -35.162  1.00 38.19  ? 200 GLU   B N     1 
ATOM   15515 C  CA    . GLU   F 2  198 ? -22.218 57.507  -35.394  1.00 42.94  ? 200 GLU   B CA    1 
ATOM   15516 C  C     . GLU   F 2  198 ? -21.610 56.946  -34.134  1.00 25.25  ? 200 GLU   B C     1 
ATOM   15517 O  O     . GLU   F 2  198 ? -21.883 57.464  -33.052  1.00 31.25  ? 200 GLU   B O     1 
ATOM   15518 C  CB    . GLU   F 2  198 ? -21.559 58.863  -35.714  1.00 39.49  ? 200 GLU   B CB    1 
ATOM   15519 C  CG    . GLU   F 2  198 ? -22.272 59.667  -36.758  1.00 38.50  ? 200 GLU   B CG    1 
ATOM   15520 C  CD    . GLU   F 2  198 ? -22.441 61.109  -36.344  1.00 34.27  ? 200 GLU   B CD    1 
ATOM   15521 O  OE1   . GLU   F 2  198 ? -22.299 61.430  -35.144  1.00 43.88  ? 200 GLU   B OE1   1 
ATOM   15522 O  OE2   . GLU   F 2  198 ? -22.728 61.923  -37.223  1.00 32.62  ? 200 GLU   B OE2   1 
ATOM   15523 N  N     . THR   F 2  199 ? -20.746 55.948  -34.278  1.00 26.20  ? 201 THR   B N     1 
ATOM   15524 C  CA    . THR   F 2  199 ? -19.970 55.416  -33.158  1.00 28.53  ? 201 THR   B CA    1 
ATOM   15525 C  C     . THR   F 2  199 ? -18.477 55.467  -33.474  1.00 26.83  ? 201 THR   B C     1 
ATOM   15526 O  O     . THR   F 2  199 ? -18.019 54.870  -34.457  1.00 30.35  ? 201 THR   B O     1 
ATOM   15527 C  CB    . THR   F 2  199 ? -20.382 53.979  -32.842  1.00 25.31  ? 201 THR   B CB    1 
ATOM   15528 O  OG1   . THR   F 2  199 ? -21.668 53.985  -32.216  1.00 23.36  ? 201 THR   B OG1   1 
ATOM   15529 C  CG2   . THR   F 2  199 ? -19.350 53.336  -31.916  1.00 25.76  ? 201 THR   B CG2   1 
ATOM   15530 N  N     . TYR   F 2  200 ? -17.718 56.167  -32.646  1.00 24.79  ? 202 TYR   B N     1 
ATOM   15531 C  CA    . TYR   F 2  200 ? -16.264 56.061  -32.678  1.00 18.38  ? 202 TYR   B CA    1 
ATOM   15532 C  C     . TYR   F 2  200 ? -15.847 54.801  -31.919  1.00 25.45  ? 202 TYR   B C     1 
ATOM   15533 O  O     . TYR   F 2  200 ? -16.009 54.718  -30.693  1.00 20.90  ? 202 TYR   B O     1 
ATOM   15534 C  CB    . TYR   F 2  200 ? -15.636 57.304  -32.064  1.00 19.86  ? 202 TYR   B CB    1 
ATOM   15535 C  CG    . TYR   F 2  200 ? -15.931 58.564  -32.824  1.00 22.60  ? 202 TYR   B CG    1 
ATOM   15536 C  CD1   . TYR   F 2  200 ? -15.282 58.846  -34.009  1.00 26.28  ? 202 TYR   B CD1   1 
ATOM   15537 C  CD2   . TYR   F 2  200 ? -16.836 59.481  -32.342  1.00 24.58  ? 202 TYR   B CD2   1 
ATOM   15538 C  CE1   . TYR   F 2  200 ? -15.547 60.002  -34.706  1.00 30.68  ? 202 TYR   B CE1   1 
ATOM   15539 C  CE2   . TYR   F 2  200 ? -17.110 60.627  -33.013  1.00 26.80  ? 202 TYR   B CE2   1 
ATOM   15540 C  CZ    . TYR   F 2  200 ? -16.463 60.894  -34.199  1.00 34.90  ? 202 TYR   B CZ    1 
ATOM   15541 O  OH    . TYR   F 2  200 ? -16.745 62.052  -34.874  1.00 28.15  ? 202 TYR   B OH    1 
ATOM   15542 N  N     . CYS   F 2  201 ? -15.306 53.821  -32.637  1.00 24.69  ? 203 CYS   B N     1 
ATOM   15543 C  CA    . CYS   F 2  201 ? -14.758 52.616  -32.015  1.00 25.93  ? 203 CYS   B CA    1 
ATOM   15544 C  C     . CYS   F 2  201 ? -13.378 52.913  -31.449  1.00 29.61  ? 203 CYS   B C     1 
ATOM   15545 O  O     . CYS   F 2  201 ? -12.369 52.815  -32.146  1.00 40.45  ? 203 CYS   B O     1 
ATOM   15546 C  CB    . CYS   F 2  201 ? -14.687 51.481  -33.023  1.00 28.87  ? 203 CYS   B CB    1 
ATOM   15547 S  SG    . CYS   F 2  201 ? -16.257 51.275  -33.864  1.00 39.64  ? 203 CYS   B SG    1 
ATOM   15548 N  N     . ILE   F 2  202 ? -13.330 53.254  -30.162  1.00 29.44  ? 204 ILE   B N     1 
ATOM   15549 C  CA    . ILE   F 2  202 ? -12.074 53.440  -29.436  1.00 32.89  ? 204 ILE   B CA    1 
ATOM   15550 C  C     . ILE   F 2  202 ? -11.677 52.101  -28.809  1.00 28.80  ? 204 ILE   B C     1 
ATOM   15551 O  O     . ILE   F 2  202 ? -12.214 51.693  -27.783  1.00 26.89  ? 204 ILE   B O     1 
ATOM   15552 C  CB    . ILE   F 2  202 ? -12.192 54.547  -28.394  1.00 25.75  ? 204 ILE   B CB    1 
ATOM   15553 C  CG1   . ILE   F 2  202 ? -12.268 55.874  -29.122  1.00 31.51  ? 204 ILE   B CG1   1 
ATOM   15554 C  CG2   . ILE   F 2  202 ? -10.979 54.546  -27.489  1.00 26.19  ? 204 ILE   B CG2   1 
ATOM   15555 C  CD1   . ILE   F 2  202 ? -13.354 56.742  -28.644  1.00 31.84  ? 204 ILE   B CD1   1 
ATOM   15556 N  N     . ASP   F 2  203 ? -10.691 51.443  -29.419  1.00 26.14  ? 205 ASP   B N     1 
ATOM   15557 C  CA    . ASP   F 2  203 ? -10.332 50.056  -29.139  1.00 23.19  ? 205 ASP   B CA    1 
ATOM   15558 C  C     . ASP   F 2  203 ? -9.148  50.001  -28.170  1.00 24.85  ? 205 ASP   B C     1 
ATOM   15559 O  O     . ASP   F 2  203 ? -8.022  50.363  -28.529  1.00 20.39  ? 205 ASP   B O     1 
ATOM   15560 C  CB    . ASP   F 2  203 ? -9.990  49.355  -30.455  1.00 22.05  ? 205 ASP   B CB    1 
ATOM   15561 C  CG    . ASP   F 2  203 ? -9.720  47.881  -30.292  1.00 23.11  ? 205 ASP   B CG    1 
ATOM   15562 O  OD1   . ASP   F 2  203 ? -9.879  47.331  -29.183  1.00 24.88  ? 205 ASP   B OD1   1 
ATOM   15563 O  OD2   . ASP   F 2  203 ? -9.357  47.254  -31.296  1.00 26.15  ? 205 ASP   B OD2   1 
ATOM   15564 N  N     . ASN   F 2  204 ? -9.391  49.516  -26.951  1.00 22.86  ? 206 ASN   B N     1 
ATOM   15565 C  CA    . ASN   F 2  204 ? -8.278  49.354  -26.021  1.00 27.23  ? 206 ASN   B CA    1 
ATOM   15566 C  C     . ASN   F 2  204 ? -7.155  48.476  -26.597  1.00 31.07  ? 206 ASN   B C     1 
ATOM   15567 O  O     . ASN   F 2  204 ? -5.986  48.622  -26.207  1.00 24.21  ? 206 ASN   B O     1 
ATOM   15568 C  CB    . ASN   F 2  204 ? -8.780  48.788  -24.700  1.00 23.01  ? 206 ASN   B CB    1 
ATOM   15569 C  CG    . ASN   F 2  204 ? -9.189  49.868  -23.743  1.00 26.21  ? 206 ASN   B CG    1 
ATOM   15570 O  OD1   . ASN   F 2  204 ? -9.185  51.050  -24.090  1.00 20.42  ? 206 ASN   B OD1   1 
ATOM   15571 N  ND2   . ASN   F 2  204 ? -9.550  49.474  -22.524  1.00 21.61  ? 206 ASN   B ND2   1 
ATOM   15572 N  N     . GLU   F 2  205 ? -7.469  47.555  -27.507  1.00 19.62  ? 207 GLU   B N     1 
ATOM   15573 C  CA    . GLU   F 2  205 ? -6.377  46.798  -28.111  1.00 26.91  ? 207 GLU   B CA    1 
ATOM   15574 C  C     . GLU   F 2  205 ? -5.421  47.718  -28.875  1.00 33.96  ? 207 GLU   B C     1 
ATOM   15575 O  O     . GLU   F 2  205 ? -4.194  47.578  -28.769  1.00 31.38  ? 207 GLU   B O     1 
ATOM   15576 C  CB    . GLU   F 2  205 ? -6.912  45.699  -29.029  1.00 24.76  ? 207 GLU   B CB    1 
ATOM   15577 C  CG    . GLU   F 2  205 ? -5.794  44.933  -29.714  1.00 29.42  ? 207 GLU   B CG    1 
ATOM   15578 C  CD    . GLU   F 2  205 ? -5.883  43.416  -29.558  1.00 38.82  ? 207 GLU   B CD    1 
ATOM   15579 O  OE1   . GLU   F 2  205 ? -6.375  42.923  -28.500  1.00 34.77  ? 207 GLU   B OE1   1 
ATOM   15580 O  OE2   . GLU   F 2  205 ? -5.470  42.724  -30.525  1.00 36.46  ? 207 GLU   B OE2   1 
ATOM   15581 N  N     . ALA   F 2  206 ? -5.960  48.662  -29.659  1.00 27.49  ? 208 ALA   B N     1 
ATOM   15582 C  CA    . ALA   F 2  206 ? -5.083  49.600  -30.353  1.00 27.75  ? 208 ALA   B CA    1 
ATOM   15583 C  C     . ALA   F 2  206 ? -4.409  50.557  -29.375  1.00 25.73  ? 208 ALA   B C     1 
ATOM   15584 O  O     . ALA   F 2  206 ? -3.212  50.830  -29.506  1.00 34.96  ? 208 ALA   B O     1 
ATOM   15585 C  CB    . ALA   F 2  206 ? -5.853  50.371  -31.434  1.00 23.44  ? 208 ALA   B CB    1 
ATOM   15586 N  N     . LEU   F 2  207 ? -5.147  51.082  -28.391  1.00 25.15  ? 209 LEU   B N     1 
ATOM   15587 C  CA    . LEU   F 2  207 ? -4.519  52.013  -27.455  1.00 30.61  ? 209 LEU   B CA    1 
ATOM   15588 C  C     . LEU   F 2  207 ? -3.339  51.345  -26.761  1.00 33.05  ? 209 LEU   B C     1 
ATOM   15589 O  O     . LEU   F 2  207 ? -2.281  51.961  -26.584  1.00 33.49  ? 209 LEU   B O     1 
ATOM   15590 C  CB    . LEU   F 2  207 ? -5.533  52.538  -26.435  1.00 23.83  ? 209 LEU   B CB    1 
ATOM   15591 C  CG    . LEU   F 2  207 ? -6.739  53.287  -27.022  1.00 28.84  ? 209 LEU   B CG    1 
ATOM   15592 C  CD1   . LEU   F 2  207 ? -7.694  53.781  -25.936  1.00 16.08  ? 209 LEU   B CD1   1 
ATOM   15593 C  CD2   . LEU   F 2  207 ? -6.281  54.458  -27.900  1.00 26.60  ? 209 LEU   B CD2   1 
ATOM   15594 N  N     . TYR   F 2  208 ? -3.487  50.064  -26.411  1.00 31.59  ? 210 TYR   B N     1 
ATOM   15595 C  CA    . TYR   F 2  208 ? -2.386  49.321  -25.811  1.00 34.45  ? 210 TYR   B CA    1 
ATOM   15596 C  C     . TYR   F 2  208 ? -1.230  49.190  -26.802  1.00 32.49  ? 210 TYR   B C     1 
ATOM   15597 O  O     . TYR   F 2  208 ? -0.100  49.603  -26.523  1.00 35.10  ? 210 TYR   B O     1 
ATOM   15598 C  CB    . TYR   F 2  208 ? -2.871  47.941  -25.319  1.00 31.40  ? 210 TYR   B CB    1 
ATOM   15599 C  CG    . TYR   F 2  208 ? -1.741  47.094  -24.795  1.00 30.96  ? 210 TYR   B CG    1 
ATOM   15600 C  CD1   . TYR   F 2  208 ? -1.326  47.185  -23.459  1.00 24.18  ? 210 TYR   B CD1   1 
ATOM   15601 C  CD2   . TYR   F 2  208 ? -1.051  46.241  -25.646  1.00 29.71  ? 210 TYR   B CD2   1 
ATOM   15602 C  CE1   . TYR   F 2  208 ? -0.267  46.422  -22.982  1.00 25.83  ? 210 TYR   B CE1   1 
ATOM   15603 C  CE2   . TYR   F 2  208 ? 0.017   45.469  -25.188  1.00 29.58  ? 210 TYR   B CE2   1 
ATOM   15604 C  CZ    . TYR   F 2  208 ? 0.418   45.564  -23.860  1.00 34.29  ? 210 TYR   B CZ    1 
ATOM   15605 O  OH    . TYR   F 2  208 ? 1.499   44.804  -23.445  1.00 22.07  ? 210 TYR   B OH    1 
ATOM   15606 N  N     . ASP   F 2  209 ? -1.499  48.642  -27.981  1.00 25.00  ? 211 ASP   B N     1 
ATOM   15607 C  CA    . ASP   F 2  209 ? -0.439  48.541  -28.978  1.00 32.68  ? 211 ASP   B CA    1 
ATOM   15608 C  C     . ASP   F 2  209 ? 0.320   49.855  -29.139  1.00 34.59  ? 211 ASP   B C     1 
ATOM   15609 O  O     . ASP   F 2  209 ? 1.551   49.876  -29.056  1.00 37.44  ? 211 ASP   B O     1 
ATOM   15610 C  CB    . ASP   F 2  209 ? -1.012  48.076  -30.308  1.00 35.06  ? 211 ASP   B CB    1 
ATOM   15611 C  CG    . ASP   F 2  209 ? -0.851  46.595  -30.499  1.00 50.29  ? 211 ASP   B CG    1 
ATOM   15612 O  OD1   . ASP   F 2  209 ? 0.246   46.201  -30.963  1.00 69.06  ? 211 ASP   B OD1   1 
ATOM   15613 O  OD2   . ASP   F 2  209 ? -1.789  45.830  -30.140  1.00 46.43  ? 211 ASP   B OD2   1 
ATOM   15614 N  N     . ILE   F 2  210 ? -0.392  50.966  -29.357  1.00 31.22  ? 212 ILE   B N     1 
ATOM   15615 C  CA    . ILE   F 2  210 ? 0.287   52.254  -29.534  1.00 30.26  ? 212 ILE   B CA    1 
ATOM   15616 C  C     . ILE   F 2  210 ? 1.182   52.559  -28.337  1.00 34.66  ? 212 ILE   B C     1 
ATOM   15617 O  O     . ILE   F 2  210 ? 2.363   52.887  -28.489  1.00 37.43  ? 212 ILE   B O     1 
ATOM   15618 C  CB    . ILE   F 2  210 ? -0.727  53.388  -29.761  1.00 21.36  ? 212 ILE   B CB    1 
ATOM   15619 C  CG1   . ILE   F 2  210 ? -1.473  53.223  -31.082  1.00 27.42  ? 212 ILE   B CG1   1 
ATOM   15620 C  CG2   . ILE   F 2  210 ? -0.015  54.678  -29.822  1.00 24.05  ? 212 ILE   B CG2   1 
ATOM   15621 C  CD1   . ILE   F 2  210 ? -2.387  54.371  -31.381  1.00 28.82  ? 212 ILE   B CD1   1 
ATOM   15622 N  N     . CYS   F 2  211 ? 0.628   52.465  -27.127  1.00 35.68  ? 213 CYS   B N     1 
ATOM   15623 C  CA    . CYS   F 2  211 ? 1.339   52.932  -25.945  1.00 31.54  ? 213 CYS   B CA    1 
ATOM   15624 C  C     . CYS   F 2  211 ? 2.576   52.087  -25.648  1.00 40.36  ? 213 CYS   B C     1 
ATOM   15625 O  O     . CYS   F 2  211 ? 3.605   52.621  -25.215  1.00 42.11  ? 213 CYS   B O     1 
ATOM   15626 C  CB    . CYS   F 2  211 ? 0.405   52.919  -24.741  1.00 28.42  ? 213 CYS   B CB    1 
ATOM   15627 S  SG    . CYS   F 2  211 ? -0.758  54.244  -24.717  1.00 32.66  ? 213 CYS   B SG    1 
ATOM   15628 N  N     . PHE   F 2  212 ? 2.493   50.770  -25.863  1.00 34.50  ? 214 PHE   B N     1 
ATOM   15629 C  CA    . PHE   F 2  212 ? 3.481   49.797  -25.409  1.00 38.46  ? 214 PHE   B CA    1 
ATOM   15630 C  C     . PHE   F 2  212 ? 4.554   49.549  -26.461  1.00 38.74  ? 214 PHE   B C     1 
ATOM   15631 O  O     . PHE   F 2  212 ? 5.748   49.548  -26.154  1.00 43.66  ? 214 PHE   B O     1 
ATOM   15632 C  CB    . PHE   F 2  212 ? 2.759   48.492  -25.038  1.00 33.43  ? 214 PHE   B CB    1 
ATOM   15633 C  CG    . PHE   F 2  212 ? 3.666   47.360  -24.689  1.00 30.28  ? 214 PHE   B CG    1 
ATOM   15634 C  CD1   . PHE   F 2  212 ? 4.371   47.358  -23.484  1.00 33.14  ? 214 PHE   B CD1   1 
ATOM   15635 C  CD2   . PHE   F 2  212 ? 3.789   46.266  -25.542  1.00 32.54  ? 214 PHE   B CD2   1 
ATOM   15636 C  CE1   . PHE   F 2  212 ? 5.214   46.286  -23.139  1.00 33.72  ? 214 PHE   B CE1   1 
ATOM   15637 C  CE2   . PHE   F 2  212 ? 4.621   45.179  -25.217  1.00 37.66  ? 214 PHE   B CE2   1 
ATOM   15638 C  CZ    . PHE   F 2  212 ? 5.344   45.184  -24.019  1.00 37.42  ? 214 PHE   B CZ    1 
ATOM   15639 N  N     . ARG   F 2  213 ? 4.129   49.323  -27.696  1.00 34.93  ? 215 ARG   B N     1 
ATOM   15640 C  CA    . ARG   F 2  213 ? 5.031   49.141  -28.826  1.00 37.93  ? 215 ARG   B CA    1 
ATOM   15641 C  C     . ARG   F 2  213 ? 5.563   50.486  -29.316  1.00 46.98  ? 215 ARG   B C     1 
ATOM   15642 O  O     . ARG   F 2  213 ? 6.773   50.710  -29.393  1.00 44.40  ? 215 ARG   B O     1 
ATOM   15643 C  CB    . ARG   F 2  213 ? 4.280   48.440  -29.958  1.00 36.30  ? 215 ARG   B CB    1 
ATOM   15644 C  CG    . ARG   F 2  213 ? 4.763   47.093  -30.361  1.00 55.25  ? 215 ARG   B CG    1 
ATOM   15645 C  CD    . ARG   F 2  213 ? 4.584   46.939  -31.875  1.00 60.83  ? 215 ARG   B CD    1 
ATOM   15646 N  NE    . ARG   F 2  213 ? 3.790   45.769  -32.231  1.00 87.14  ? 215 ARG   B NE    1 
ATOM   15647 C  CZ    . ARG   F 2  213 ? 4.286   44.548  -32.386  1.00 90.05  ? 215 ARG   B CZ    1 
ATOM   15648 N  NH1   . ARG   F 2  213 ? 5.571   44.296  -32.190  1.00 88.65  ? 215 ARG   B NH1   1 
ATOM   15649 N  NH2   . ARG   F 2  213 ? 3.472   43.554  -32.738  1.00 88.96  ? 215 ARG   B NH2   1 
ATOM   15650 N  N     . THR   F 2  214 ? 4.662   51.403  -29.647  1.00 45.68  ? 216 THR   B N     1 
ATOM   15651 C  CA    . THR   F 2  214 ? 5.078   52.595  -30.364  1.00 35.20  ? 216 THR   B CA    1 
ATOM   15652 C  C     . THR   F 2  214 ? 5.669   53.640  -29.430  1.00 38.91  ? 216 THR   B C     1 
ATOM   15653 O  O     . THR   F 2  214 ? 6.734   54.196  -29.718  1.00 41.75  ? 216 THR   B O     1 
ATOM   15654 C  CB    . THR   F 2  214 ? 3.896   53.156  -31.143  1.00 30.59  ? 216 THR   B CB    1 
ATOM   15655 O  OG1   . THR   F 2  214 ? 3.612   52.280  -32.241  1.00 43.85  ? 216 THR   B OG1   1 
ATOM   15656 C  CG2   . THR   F 2  214 ? 4.222   54.504  -31.656  1.00 24.44  ? 216 THR   B CG2   1 
ATOM   15657 N  N     . LEU   F 2  215 ? 4.994   53.931  -28.312  1.00 40.23  ? 217 LEU   B N     1 
ATOM   15658 C  CA    . LEU   F 2  215 ? 5.467   54.934  -27.363  1.00 34.22  ? 217 LEU   B CA    1 
ATOM   15659 C  C     . LEU   F 2  215 ? 6.423   54.364  -26.327  1.00 31.94  ? 217 LEU   B C     1 
ATOM   15660 O  O     . LEU   F 2  215 ? 6.915   55.116  -25.490  1.00 35.25  ? 217 LEU   B O     1 
ATOM   15661 C  CB    . LEU   F 2  215 ? 4.292   55.616  -26.656  1.00 36.56  ? 217 LEU   B CB    1 
ATOM   15662 C  CG    . LEU   F 2  215 ? 3.278   56.342  -27.553  1.00 43.13  ? 217 LEU   B CG    1 
ATOM   15663 C  CD1   . LEU   F 2  215 ? 2.116   56.951  -26.727  1.00 34.07  ? 217 LEU   B CD1   1 
ATOM   15664 C  CD2   . LEU   F 2  215 ? 3.963   57.407  -28.418  1.00 34.26  ? 217 LEU   B CD2   1 
ATOM   15665 N  N     . LYS   F 2  216 ? 6.724   53.070  -26.381  1.00 35.69  ? 218 LYS   B N     1 
ATOM   15666 C  CA    . LYS   F 2  216 ? 7.716   52.464  -25.491  1.00 41.54  ? 218 LYS   B CA    1 
ATOM   15667 C  C     . LYS   F 2  216 ? 7.368   52.727  -24.028  1.00 45.05  ? 218 LYS   B C     1 
ATOM   15668 O  O     . LYS   F 2  216 ? 8.228   53.076  -23.216  1.00 47.02  ? 218 LYS   B O     1 
ATOM   15669 C  CB    . LYS   F 2  216 ? 9.132   52.952  -25.817  1.00 36.39  ? 218 LYS   B CB    1 
ATOM   15670 C  CG    . LYS   F 2  216 ? 9.549   52.781  -27.294  1.00 46.57  ? 218 LYS   B CG    1 
ATOM   15671 C  CD    . LYS   F 2  216 ? 9.323   51.361  -27.881  1.00 35.74  ? 218 LYS   B CD    1 
ATOM   15672 C  CE    . LYS   F 2  216 ? 9.884   51.278  -29.329  1.00 48.50  ? 218 LYS   B CE    1 
ATOM   15673 N  NZ    . LYS   F 2  216 ? 9.526   50.031  -30.115  1.00 47.44  ? 218 LYS   B NZ    1 
ATOM   15674 N  N     . LEU   F 2  217 ? 6.081   52.588  -23.711  1.00 39.78  ? 219 LEU   B N     1 
ATOM   15675 C  CA    . LEU   F 2  217 ? 5.552   52.602  -22.354  1.00 31.35  ? 219 LEU   B CA    1 
ATOM   15676 C  C     . LEU   F 2  217 ? 5.411   51.149  -21.893  1.00 40.77  ? 219 LEU   B C     1 
ATOM   15677 O  O     . LEU   F 2  217 ? 4.471   50.455  -22.285  1.00 37.80  ? 219 LEU   B O     1 
ATOM   15678 C  CB    . LEU   F 2  217 ? 4.209   53.318  -22.324  1.00 35.92  ? 219 LEU   B CB    1 
ATOM   15679 C  CG    . LEU   F 2  217 ? 4.230   54.752  -22.835  1.00 41.61  ? 219 LEU   B CG    1 
ATOM   15680 C  CD1   . LEU   F 2  217 ? 2.888   55.425  -22.587  1.00 33.34  ? 219 LEU   B CD1   1 
ATOM   15681 C  CD2   . LEU   F 2  217 ? 5.358   55.517  -22.157  1.00 32.76  ? 219 LEU   B CD2   1 
ATOM   15682 N  N     . THR   F 2  218 ? 6.348   50.687  -21.060  1.00 42.89  ? 220 THR   B N     1 
ATOM   15683 C  CA    . THR   F 2  218 ? 6.440   49.266  -20.738  1.00 35.77  ? 220 THR   B CA    1 
ATOM   15684 C  C     . THR   F 2  218 ? 5.459   48.853  -19.649  1.00 30.98  ? 220 THR   B C     1 
ATOM   15685 O  O     . THR   F 2  218 ? 5.211   47.654  -19.485  1.00 34.74  ? 220 THR   B O     1 
ATOM   15686 C  CB    . THR   F 2  218 ? 7.883   48.893  -20.319  1.00 37.71  ? 220 THR   B CB    1 
ATOM   15687 O  OG1   . THR   F 2  218 ? 8.384   49.808  -19.329  0.87 27.06  ? 220 THR   B OG1   1 
ATOM   15688 C  CG2   . THR   F 2  218 ? 8.820   48.901  -21.512  1.00 33.82  ? 220 THR   B CG2   1 
ATOM   15689 N  N     . THR   F 2  219 ? 4.922   49.818  -18.906  1.00 28.98  ? 221 THR   B N     1 
ATOM   15690 C  CA    . THR   F 2  219 ? 3.885   49.608  -17.893  1.00 32.15  ? 221 THR   B CA    1 
ATOM   15691 C  C     . THR   F 2  219 ? 2.764   50.608  -18.163  1.00 34.53  ? 221 THR   B C     1 
ATOM   15692 O  O     . THR   F 2  219 ? 2.601   51.591  -17.431  1.00 30.29  ? 221 THR   B O     1 
ATOM   15693 C  CB    . THR   F 2  219 ? 4.423   49.811  -16.473  1.00 29.91  ? 221 THR   B CB    1 
ATOM   15694 O  OG1   . THR   F 2  219 ? 5.009   51.107  -16.393  1.00 29.39  ? 221 THR   B OG1   1 
ATOM   15695 C  CG2   . THR   F 2  219 ? 5.461   48.759  -16.065  1.00 28.07  ? 221 THR   B CG2   1 
ATOM   15696 N  N     . PRO   F 2  220 ? 1.988   50.407  -19.226  1.00 33.51  ? 222 PRO   B N     1 
ATOM   15697 C  CA    . PRO   F 2  220 ? 0.948   51.385  -19.560  1.00 35.52  ? 222 PRO   B CA    1 
ATOM   15698 C  C     . PRO   F 2  220 ? -0.142  51.474  -18.489  1.00 35.23  ? 222 PRO   B C     1 
ATOM   15699 O  O     . PRO   F 2  220 ? -0.510  50.482  -17.856  1.00 33.61  ? 222 PRO   B O     1 
ATOM   15700 C  CB    . PRO   F 2  220 ? 0.398   50.862  -20.891  1.00 33.25  ? 222 PRO   B CB    1 
ATOM   15701 C  CG    . PRO   F 2  220 ? 0.796   49.424  -20.931  1.00 25.84  ? 222 PRO   B CG    1 
ATOM   15702 C  CD    . PRO   F 2  220 ? 2.094   49.348  -20.242  1.00 30.71  ? 222 PRO   B CD    1 
ATOM   15703 N  N     . THR   F 2  221 ? -0.654  52.685  -18.294  1.00 31.85  ? 223 THR   B N     1 
ATOM   15704 C  CA    . THR   F 2  221 ? -1.779  52.973  -17.417  1.00 24.71  ? 223 THR   B CA    1 
ATOM   15705 C  C     . THR   F 2  221 ? -2.972  53.470  -18.227  1.00 28.01  ? 223 THR   B C     1 
ATOM   15706 O  O     . THR   F 2  221 ? -2.839  53.921  -19.370  1.00 28.34  ? 223 THR   B O     1 
ATOM   15707 C  CB    . THR   F 2  221 ? -1.416  54.048  -16.407  1.00 28.82  ? 223 THR   B CB    1 
ATOM   15708 O  OG1   . THR   F 2  221 ? -1.339  55.297  -17.113  1.00 29.31  ? 223 THR   B OG1   1 
ATOM   15709 C  CG2   . THR   F 2  221 ? -0.065  53.734  -15.741  1.00 20.91  ? 223 THR   B CG2   1 
ATOM   15710 N  N     . TYR   F 2  222 ? -4.154  53.408  -17.611  1.00 30.57  ? 224 TYR   B N     1 
ATOM   15711 C  CA    . TYR   F 2  222 ? -5.319  54.030  -18.241  1.00 31.49  ? 224 TYR   B CA    1 
ATOM   15712 C  C     . TYR   F 2  222 ? -5.086  55.510  -18.490  1.00 22.13  ? 224 TYR   B C     1 
ATOM   15713 O  O     . TYR   F 2  222 ? -5.663  56.078  -19.417  1.00 23.22  ? 224 TYR   B O     1 
ATOM   15714 C  CB    . TYR   F 2  222 ? -6.587  53.806  -17.396  1.00 29.41  ? 224 TYR   B CB    1 
ATOM   15715 C  CG    . TYR   F 2  222 ? -7.157  52.413  -17.591  1.00 33.01  ? 224 TYR   B CG    1 
ATOM   15716 C  CD1   . TYR   F 2  222 ? -7.519  51.976  -18.868  1.00 21.33  ? 224 TYR   B CD1   1 
ATOM   15717 C  CD2   . TYR   F 2  222 ? -7.290  51.517  -16.521  1.00 28.82  ? 224 TYR   B CD2   1 
ATOM   15718 C  CE1   . TYR   F 2  222 ? -8.010  50.699  -19.084  1.00 26.94  ? 224 TYR   B CE1   1 
ATOM   15719 C  CE2   . TYR   F 2  222 ? -7.801  50.222  -16.730  1.00 27.43  ? 224 TYR   B CE2   1 
ATOM   15720 C  CZ    . TYR   F 2  222 ? -8.161  49.824  -18.015  1.00 29.41  ? 224 TYR   B CZ    1 
ATOM   15721 O  OH    . TYR   F 2  222 ? -8.666  48.560  -18.267  1.00 33.85  ? 224 TYR   B OH    1 
ATOM   15722 N  N     . GLY   F 2  223 ? -4.236  56.150  -17.689  1.00 26.92  ? 225 GLY   B N     1 
ATOM   15723 C  CA    . GLY   F 2  223 ? -3.879  57.531  -17.978  1.00 23.08  ? 225 GLY   B CA    1 
ATOM   15724 C  C     . GLY   F 2  223 ? -3.235  57.680  -19.345  1.00 32.71  ? 225 GLY   B C     1 
ATOM   15725 O  O     . GLY   F 2  223 ? -3.537  58.626  -20.076  1.00 33.69  ? 225 GLY   B O     1 
ATOM   15726 N  N     . ASP   F 2  224 ? -2.345  56.739  -19.707  1.00 26.74  ? 226 ASP   B N     1 
ATOM   15727 C  CA    . ASP   F 2  224 ? -1.715  56.745  -21.026  1.00 23.79  ? 226 ASP   B CA    1 
ATOM   15728 C  C     . ASP   F 2  224 ? -2.745  56.542  -22.124  1.00 31.01  ? 226 ASP   B C     1 
ATOM   15729 O  O     . ASP   F 2  224 ? -2.796  57.300  -23.101  1.00 33.37  ? 226 ASP   B O     1 
ATOM   15730 C  CB    . ASP   F 2  224 ? -0.654  55.640  -21.133  1.00 26.27  ? 226 ASP   B CB    1 
ATOM   15731 C  CG    . ASP   F 2  224 ? 0.417   55.744  -20.086  1.00 33.73  ? 226 ASP   B CG    1 
ATOM   15732 O  OD1   . ASP   F 2  224 ? 0.798   56.870  -19.723  1.00 35.01  ? 226 ASP   B OD1   1 
ATOM   15733 O  OD2   . ASP   F 2  224 ? 0.872   54.687  -19.609  1.00 41.26  ? 226 ASP   B OD2   1 
ATOM   15734 N  N     . LEU   F 2  225 ? -3.530  55.472  -22.011  1.00 28.74  ? 227 LEU   B N     1 
ATOM   15735 C  CA    . LEU   F 2  225 ? -4.584  55.211  -22.980  1.00 23.32  ? 227 LEU   B CA    1 
ATOM   15736 C  C     . LEU   F 2  225 ? -5.487  56.427  -23.145  1.00 27.91  ? 227 LEU   B C     1 
ATOM   15737 O  O     . LEU   F 2  225 ? -5.790  56.836  -24.272  1.00 32.18  ? 227 LEU   B O     1 
ATOM   15738 C  CB    . LEU   F 2  225 ? -5.385  53.995  -22.528  1.00 22.89  ? 227 LEU   B CB    1 
ATOM   15739 C  CG    . LEU   F 2  225 ? -4.864  52.651  -23.027  1.00 22.98  ? 227 LEU   B CG    1 
ATOM   15740 C  CD1   . LEU   F 2  225 ? -3.350  52.455  -22.867  1.00 13.05  ? 227 LEU   B CD1   1 
ATOM   15741 C  CD2   . LEU   F 2  225 ? -5.642  51.581  -22.344  1.00 20.75  ? 227 LEU   B CD2   1 
ATOM   15742 N  N     . ASN   F 2  226 ? -5.873  57.054  -22.026  1.00 25.43  ? 228 ASN   B N     1 
ATOM   15743 C  CA    . ASN   F 2  226 ? -6.813  58.161  -22.071  1.00 25.79  ? 228 ASN   B CA    1 
ATOM   15744 C  C     . ASN   F 2  226 ? -6.170  59.416  -22.621  1.00 27.49  ? 228 ASN   B C     1 
ATOM   15745 O  O     . ASN   F 2  226 ? -6.879  60.294  -23.113  1.00 39.16  ? 228 ASN   B O     1 
ATOM   15746 C  CB    . ASN   F 2  226 ? -7.417  58.451  -20.681  1.00 26.07  ? 228 ASN   B CB    1 
ATOM   15747 C  CG    . ASN   F 2  226 ? -8.301  57.292  -20.132  1.00 21.70  ? 228 ASN   B CG    1 
ATOM   15748 O  OD1   . ASN   F 2  226 ? -8.599  56.326  -20.826  1.00 29.11  ? 228 ASN   B OD1   1 
ATOM   15749 N  ND2   . ASN   F 2  226 ? -8.706  57.407  -18.879  1.00 23.17  ? 228 ASN   B ND2   1 
ATOM   15750 N  N     . HIS   F 2  227 ? -4.850  59.518  -22.565  1.00 27.67  ? 229 HIS   B N     1 
ATOM   15751 C  CA    . HIS   F 2  227 ? -4.168  60.621  -23.233  1.00 28.82  ? 229 HIS   B CA    1 
ATOM   15752 C  C     . HIS   F 2  227 ? -4.400  60.552  -24.740  1.00 32.05  ? 229 HIS   B C     1 
ATOM   15753 O  O     . HIS   F 2  227 ? -4.825  61.533  -25.365  1.00 30.89  ? 229 HIS   B O     1 
ATOM   15754 C  CB    . HIS   F 2  227 ? -2.679  60.577  -22.880  1.00 29.37  ? 229 HIS   B CB    1 
ATOM   15755 C  CG    . HIS   F 2  227 ? -1.848  61.570  -23.615  1.00 34.70  ? 229 HIS   B CG    1 
ATOM   15756 N  ND1   . HIS   F 2  227 ? -1.779  62.897  -23.252  1.00 41.67  ? 229 HIS   B ND1   1 
ATOM   15757 C  CD2   . HIS   F 2  227 ? -1.034  61.430  -24.688  1.00 37.42  ? 229 HIS   B CD2   1 
ATOM   15758 C  CE1   . HIS   F 2  227 ? -0.960  63.533  -24.071  1.00 34.63  ? 229 HIS   B CE1   1 
ATOM   15759 N  NE2   . HIS   F 2  227 ? -0.502  62.668  -24.956  1.00 38.92  ? 229 HIS   B NE2   1 
ATOM   15760 N  N     . LEU   F 2  228 ? -4.175  59.374  -25.336  1.00 31.61  ? 230 LEU   B N     1 
ATOM   15761 C  CA    . LEU   F 2  228 ? -4.546  59.170  -26.734  1.00 24.90  ? 230 LEU   B CA    1 
ATOM   15762 C  C     . LEU   F 2  228 ? -6.062  59.306  -26.967  1.00 29.43  ? 230 LEU   B C     1 
ATOM   15763 O  O     . LEU   F 2  228 ? -6.490  59.767  -28.033  1.00 26.16  ? 230 LEU   B O     1 
ATOM   15764 C  CB    . LEU   F 2  228 ? -4.044  57.806  -27.203  1.00 22.34  ? 230 LEU   B CB    1 
ATOM   15765 C  CG    . LEU   F 2  228 ? -2.549  57.516  -27.050  1.00 20.55  ? 230 LEU   B CG    1 
ATOM   15766 C  CD1   . LEU   F 2  228 ? -2.228  56.050  -27.324  1.00 22.53  ? 230 LEU   B CD1   1 
ATOM   15767 C  CD2   . LEU   F 2  228 ? -1.683  58.419  -27.914  1.00 25.19  ? 230 LEU   B CD2   1 
ATOM   15768 N  N     . VAL   F 2  229 ? -6.900  58.922  -26.000  1.00 24.89  ? 231 VAL   B N     1 
ATOM   15769 C  CA    . VAL   F 2  229 ? -8.324  59.072  -26.260  1.00 22.33  ? 231 VAL   B CA    1 
ATOM   15770 C  C     . VAL   F 2  229 ? -8.775  60.533  -26.183  1.00 28.15  ? 231 VAL   B C     1 
ATOM   15771 O  O     . VAL   F 2  229 ? -9.740  60.922  -26.850  1.00 22.00  ? 231 VAL   B O     1 
ATOM   15772 C  CB    . VAL   F 2  229 ? -9.137  58.178  -25.323  1.00 26.02  ? 231 VAL   B CB    1 
ATOM   15773 C  CG1   . VAL   F 2  229 ? -10.637 58.436  -25.562  1.00 24.38  ? 231 VAL   B CG1   1 
ATOM   15774 C  CG2   . VAL   F 2  229 ? -8.784  56.722  -25.606  1.00 23.78  ? 231 VAL   B CG2   1 
ATOM   15775 N  N     . SER   F 2  230 ? -8.116  61.372  -25.382  1.00 27.88  ? 232 SER   B N     1 
ATOM   15776 C  CA    . SER   F 2  230 ? -8.579  62.749  -25.314  1.00 20.85  ? 232 SER   B CA    1 
ATOM   15777 C  C     . SER   F 2  230 ? -8.056  63.593  -26.470  1.00 30.82  ? 232 SER   B C     1 
ATOM   15778 O  O     . SER   F 2  230 ? -8.696  64.582  -26.825  1.00 33.21  ? 232 SER   B O     1 
ATOM   15779 C  CB    . SER   F 2  230 ? -8.193  63.390  -23.984  1.00 32.18  ? 232 SER   B CB    1 
ATOM   15780 O  OG    . SER   F 2  230 ? -6.809  63.668  -23.922  1.00 39.66  ? 232 SER   B OG    1 
ATOM   15781 N  N     . ALA   F 2  231 ? -6.906  63.242  -27.065  1.00 27.25  ? 233 ALA   B N     1 
ATOM   15782 C  CA    . ALA   F 2  231 ? -6.496  63.916  -28.293  1.00 23.38  ? 233 ALA   B CA    1 
ATOM   15783 C  C     . ALA   F 2  231 ? -7.419  63.547  -29.461  1.00 31.16  ? 233 ALA   B C     1 
ATOM   15784 O  O     . ALA   F 2  231 ? -7.853  64.421  -30.227  1.00 28.05  ? 233 ALA   B O     1 
ATOM   15785 C  CB    . ALA   F 2  231 ? -5.044  63.577  -28.615  1.00 31.48  ? 233 ALA   B CB    1 
ATOM   15786 N  N     . THR   F 2  232 ? -7.763  62.262  -29.589  1.00 23.10  ? 234 THR   B N     1 
ATOM   15787 C  CA    . THR   F 2  232 ? -8.723  61.845  -30.606  1.00 24.66  ? 234 THR   B CA    1 
ATOM   15788 C  C     . THR   F 2  232 ? -10.060 62.556  -30.446  1.00 29.75  ? 234 THR   B C     1 
ATOM   15789 O  O     . THR   F 2  232 ? -10.653 63.029  -31.426  1.00 25.93  ? 234 THR   B O     1 
ATOM   15790 C  CB    . THR   F 2  232 ? -8.925  60.342  -30.544  1.00 24.33  ? 234 THR   B CB    1 
ATOM   15791 O  OG1   . THR   F 2  232 ? -7.674  59.680  -30.819  1.00 29.56  ? 234 THR   B OG1   1 
ATOM   15792 C  CG2   . THR   F 2  232 ? -9.974  59.921  -31.558  1.00 25.23  ? 234 THR   B CG2   1 
ATOM   15793 N  N     . MET   F 2  233 ? -10.566 62.623  -29.215  1.00 31.67  ? 235 MET   B N     1 
ATOM   15794 C  CA    . MET   F 2  233 ? -11.895 63.186  -29.020  1.00 23.48  ? 235 MET   B CA    1 
ATOM   15795 C  C     . MET   F 2  233 ? -11.889 64.661  -29.349  1.00 27.30  ? 235 MET   B C     1 
ATOM   15796 O  O     . MET   F 2  233 ? -12.828 65.175  -29.969  1.00 28.12  ? 235 MET   B O     1 
ATOM   15797 C  CB    . MET   F 2  233 ? -12.374 62.940  -27.591  1.00 25.33  ? 235 MET   B CB    1 
ATOM   15798 C  CG    . MET   F 2  233 ? -12.710 61.464  -27.285  1.00 24.77  ? 235 MET   B CG    1 
ATOM   15799 S  SD    . MET   F 2  233 ? -13.370 61.284  -25.619  1.00 31.84  ? 235 MET   B SD    1 
ATOM   15800 C  CE    . MET   F 2  233 ? -14.962 62.125  -25.835  1.00 35.07  ? 235 MET   B CE    1 
ATOM   15801 N  N     . SER   F 2  234 ? -10.827 65.354  -28.945  1.00 33.33  ? 236 SER   B N     1 
ATOM   15802 C  CA    . SER   F 2  234 ? -10.614 66.716  -29.405  1.00 31.71  ? 236 SER   B CA    1 
ATOM   15803 C  C     . SER   F 2  234 ? -10.594 66.766  -30.930  1.00 36.98  ? 236 SER   B C     1 
ATOM   15804 O  O     . SER   F 2  234 ? -11.351 67.522  -31.560  1.00 32.47  ? 236 SER   B O     1 
ATOM   15805 C  CB    . SER   F 2  234 ? -9.311  67.239  -28.820  1.00 28.84  ? 236 SER   B CB    1 
ATOM   15806 O  OG    . SER   F 2  234 ? -9.125  68.574  -29.212  1.00 39.57  ? 236 SER   B OG    1 
ATOM   15807 N  N     . GLY   F 2  235 ? -9.771  65.919  -31.544  1.00 27.37  ? 237 GLY   B N     1 
ATOM   15808 C  CA    . GLY   F 2  235 ? -9.667  65.936  -32.980  1.00 29.70  ? 237 GLY   B CA    1 
ATOM   15809 C  C     . GLY   F 2  235 ? -11.011 65.823  -33.672  1.00 33.85  ? 237 GLY   B C     1 
ATOM   15810 O  O     . GLY   F 2  235 ? -11.407 66.713  -34.430  1.00 32.03  ? 237 GLY   B O     1 
ATOM   15811 N  N     . VAL   F 2  236 ? -11.732 64.737  -33.405  1.00 28.65  ? 238 VAL   B N     1 
ATOM   15812 C  CA    . VAL   F 2  236 ? -12.930 64.431  -34.174  1.00 26.18  ? 238 VAL   B CA    1 
ATOM   15813 C  C     . VAL   F 2  236 ? -14.067 65.407  -33.878  1.00 28.95  ? 238 VAL   B C     1 
ATOM   15814 O  O     . VAL   F 2  236 ? -15.133 65.303  -34.489  1.00 27.94  ? 238 VAL   B O     1 
ATOM   15815 C  CB    . VAL   F 2  236 ? -13.387 62.973  -33.934  1.00 32.09  ? 238 VAL   B CB    1 
ATOM   15816 C  CG1   . VAL   F 2  236 ? -12.205 61.989  -34.037  1.00 24.05  ? 238 VAL   B CG1   1 
ATOM   15817 C  CG2   . VAL   F 2  236 ? -14.119 62.816  -32.603  1.00 22.42  ? 238 VAL   B CG2   1 
ATOM   15818 N  N     . THR   F 2  237 ? -13.880 66.350  -32.936  1.00 29.52  ? 239 THR   B N     1 
ATOM   15819 C  CA    . THR   F 2  237 ? -14.914 67.348  -32.671  1.00 25.71  ? 239 THR   B CA    1 
ATOM   15820 C  C     . THR   F 2  237 ? -14.479 68.768  -33.009  1.00 36.22  ? 239 THR   B C     1 
ATOM   15821 O  O     . THR   F 2  237 ? -15.244 69.707  -32.749  1.00 38.45  ? 239 THR   B O     1 
ATOM   15822 C  CB    . THR   F 2  237 ? -15.412 67.300  -31.198  1.00 31.18  ? 239 THR   B CB    1 
ATOM   15823 O  OG1   . THR   F 2  237 ? -14.337 67.498  -30.274  1.00 23.45  ? 239 THR   B OG1   1 
ATOM   15824 C  CG2   . THR   F 2  237 ? -16.137 65.980  -30.878  1.00 26.60  ? 239 THR   B CG2   1 
ATOM   15825 N  N     . THR   F 2  238 ? -13.291 68.962  -33.594  1.00 32.93  ? 240 THR   B N     1 
ATOM   15826 C  CA    . THR   F 2  238 ? -12.872 70.311  -33.962  1.00 34.28  ? 240 THR   B CA    1 
ATOM   15827 C  C     . THR   F 2  238 ? -13.935 70.981  -34.823  1.00 32.50  ? 240 THR   B C     1 
ATOM   15828 O  O     . THR   F 2  238 ? -14.369 72.099  -34.534  1.00 30.52  ? 240 THR   B O     1 
ATOM   15829 C  CB    . THR   F 2  238 ? -11.521 70.291  -34.698  1.00 36.78  ? 240 THR   B CB    1 
ATOM   15830 O  OG1   . THR   F 2  238 ? -10.566 69.519  -33.966  1.00 37.37  ? 240 THR   B OG1   1 
ATOM   15831 C  CG2   . THR   F 2  238 ? -10.969 71.699  -34.829  1.00 35.09  ? 240 THR   B CG2   1 
ATOM   15832 N  N     . CYS   F 2  239 ? -14.393 70.279  -35.867  1.00 34.99  ? 241 CYS   B N     1 
ATOM   15833 C  CA    . CYS   F 2  239 ? -15.357 70.813  -36.826  1.00 28.80  ? 241 CYS   B CA    1 
ATOM   15834 C  C     . CYS   F 2  239 ? -16.688 71.218  -36.194  1.00 38.97  ? 241 CYS   B C     1 
ATOM   15835 O  O     . CYS   F 2  239 ? -17.412 72.027  -36.786  1.00 39.43  ? 241 CYS   B O     1 
ATOM   15836 C  CB    . CYS   F 2  239 ? -15.602 69.785  -37.931  1.00 28.66  ? 241 CYS   B CB    1 
ATOM   15837 S  SG    . CYS   F 2  239 ? -14.147 69.468  -39.000  1.00 40.08  ? 241 CYS   B SG    1 
ATOM   15838 N  N     . LEU   F 2  240 ? -17.037 70.677  -35.019  1.00 40.49  ? 242 LEU   B N     1 
ATOM   15839 C  CA    . LEU   F 2  240 ? -18.262 71.065  -34.321  1.00 40.61  ? 242 LEU   B CA    1 
ATOM   15840 C  C     . LEU   F 2  240 ? -18.080 72.253  -33.386  1.00 36.85  ? 242 LEU   B C     1 
ATOM   15841 O  O     . LEU   F 2  240 ? -19.076 72.888  -33.016  1.00 40.65  ? 242 LEU   B O     1 
ATOM   15842 C  CB    . LEU   F 2  240 ? -18.812 69.898  -33.486  1.00 32.20  ? 242 LEU   B CB    1 
ATOM   15843 C  CG    . LEU   F 2  240 ? -18.913 68.526  -34.118  1.00 28.07  ? 242 LEU   B CG    1 
ATOM   15844 C  CD1   . LEU   F 2  240 ? -19.022 67.511  -33.000  1.00 29.89  ? 242 LEU   B CD1   1 
ATOM   15845 C  CD2   . LEU   F 2  240 ? -20.103 68.423  -35.070  1.00 24.97  ? 242 LEU   B CD2   1 
ATOM   15846 N  N     . ARG   F 2  241 ? -16.843 72.556  -32.985  1.00 35.31  ? 243 ARG   B N     1 
ATOM   15847 C  CA    . ARG   F 2  241 ? -16.567 73.514  -31.924  1.00 35.78  ? 243 ARG   B CA    1 
ATOM   15848 C  C     . ARG   F 2  241 ? -15.929 74.804  -32.410  1.00 38.86  ? 243 ARG   B C     1 
ATOM   15849 O  O     . ARG   F 2  241 ? -15.744 75.727  -31.606  1.00 46.24  ? 243 ARG   B O     1 
ATOM   15850 C  CB    . ARG   F 2  241 ? -15.638 72.890  -30.864  1.00 35.69  ? 243 ARG   B CB    1 
ATOM   15851 C  CG    . ARG   F 2  241 ? -16.081 71.543  -30.350  1.00 34.53  ? 243 ARG   B CG    1 
ATOM   15852 C  CD    . ARG   F 2  241 ? -15.260 71.123  -29.126  1.00 39.76  ? 243 ARG   B CD    1 
ATOM   15853 N  NE    . ARG   F 2  241 ? -14.020 70.435  -29.455  1.00 29.34  ? 243 ARG   B NE    1 
ATOM   15854 C  CZ    . ARG   F 2  241 ? -12.810 70.982  -29.412  1.00 36.37  ? 243 ARG   B CZ    1 
ATOM   15855 N  NH1   . ARG   F 2  241 ? -12.631 72.248  -29.064  1.00 30.32  ? 243 ARG   B NH1   1 
ATOM   15856 N  NH2   . ARG   F 2  241 ? -11.751 70.236  -29.722  1.00 32.27  ? 243 ARG   B NH2   1 
ATOM   15857 N  N     . PHE   F 2  242 ? -15.557 74.888  -33.675  1.00 39.40  ? 244 PHE   B N     1 
ATOM   15858 C  CA    . PHE   F 2  242 ? -14.965 76.085  -34.252  1.00 47.72  ? 244 PHE   B CA    1 
ATOM   15859 C  C     . PHE   F 2  242 ? -15.678 76.414  -35.549  1.00 42.18  ? 244 PHE   B C     1 
ATOM   15860 O  O     . PHE   F 2  242 ? -16.498 75.632  -36.037  1.00 41.88  ? 244 PHE   B O     1 
ATOM   15861 C  CB    . PHE   F 2  242 ? -13.455 75.892  -34.475  1.00 45.68  ? 244 PHE   B CB    1 
ATOM   15862 C  CG    . PHE   F 2  242 ? -12.678 75.686  -33.196  1.00 46.75  ? 244 PHE   B CG    1 
ATOM   15863 C  CD1   . PHE   F 2  242 ? -12.427 76.751  -32.346  1.00 48.85  ? 244 PHE   B CD1   1 
ATOM   15864 C  CD2   . PHE   F 2  242 ? -12.203 74.429  -32.842  1.00 44.03  ? 244 PHE   B CD2   1 
ATOM   15865 C  CE1   . PHE   F 2  242 ? -11.720 76.562  -31.153  1.00 49.98  ? 244 PHE   B CE1   1 
ATOM   15866 C  CE2   . PHE   F 2  242 ? -11.482 74.241  -31.664  1.00 37.52  ? 244 PHE   B CE2   1 
ATOM   15867 C  CZ    . PHE   F 2  242 ? -11.245 75.310  -30.817  1.00 37.10  ? 244 PHE   B CZ    1 
ATOM   15868 N  N     . PRO   F 2  243 ? -15.429 77.594  -36.110  1.00 44.70  ? 245 PRO   B N     1 
ATOM   15869 C  CA    . PRO   F 2  243 ? -16.130 77.975  -37.340  1.00 41.97  ? 245 PRO   B CA    1 
ATOM   15870 C  C     . PRO   F 2  243 ? -15.577 77.213  -38.531  1.00 38.88  ? 245 PRO   B C     1 
ATOM   15871 O  O     . PRO   F 2  243 ? -14.368 77.040  -38.676  1.00 49.54  ? 245 PRO   B O     1 
ATOM   15872 C  CB    . PRO   F 2  243 ? -15.861 79.478  -37.446  1.00 35.69  ? 245 PRO   B CB    1 
ATOM   15873 C  CG    . PRO   F 2  243 ? -15.450 79.886  -36.052  1.00 42.80  ? 245 PRO   B CG    1 
ATOM   15874 C  CD    . PRO   F 2  243 ? -14.675 78.722  -35.546  1.00 44.38  ? 245 PRO   B CD    1 
ATOM   15875 N  N     . GLY   F 2  244 ? -16.471 76.717  -39.369  1.00 45.00  ? 246 GLY   B N     1 
ATOM   15876 C  CA    . GLY   F 2  244 ? -16.012 75.813  -40.400  1.00 33.35  ? 246 GLY   B CA    1 
ATOM   15877 C  C     . GLY   F 2  244 ? -17.123 75.472  -41.364  1.00 49.59  ? 246 GLY   B C     1 
ATOM   15878 O  O     . GLY   F 2  244 ? -18.312 75.702  -41.103  1.00 36.38  ? 246 GLY   B O     1 
ATOM   15879 N  N     . GLN   F 2  245 ? -16.692 74.901  -42.490  1.00 47.64  ? 247 GLN   B N     1 
ATOM   15880 C  CA    . GLN   F 2  245 ? -17.497 74.553  -43.650  1.00 43.67  ? 247 GLN   B CA    1 
ATOM   15881 C  C     . GLN   F 2  245 ? -17.865 73.090  -43.684  1.00 47.06  ? 247 GLN   B C     1 
ATOM   15882 O  O     . GLN   F 2  245 ? -18.975 72.744  -44.096  1.00 53.33  ? 247 GLN   B O     1 
ATOM   15883 C  CB    . GLN   F 2  245 ? -16.722 74.865  -44.937  1.00 42.85  ? 247 GLN   B CB    1 
ATOM   15884 C  CG    . GLN   F 2  245 ? -16.343 76.300  -45.106  1.00 40.91  ? 247 GLN   B CG    1 
ATOM   15885 C  CD    . GLN   F 2  245 ? -17.504 77.093  -45.631  1.00 54.64  ? 247 GLN   B CD    1 
ATOM   15886 O  OE1   . GLN   F 2  245 ? -18.639 76.598  -45.657  1.00 50.35  ? 247 GLN   B OE1   1 
ATOM   15887 N  NE2   . GLN   F 2  245 ? -17.236 78.326  -46.079  1.00 60.28  ? 247 GLN   B NE2   1 
ATOM   15888 N  N     . LEU   F 2  246 ? -16.922 72.228  -43.325  1.00 44.26  ? 248 LEU   B N     1 
ATOM   15889 C  CA    . LEU   F 2  246 ? -17.097 70.794  -43.432  1.00 38.35  ? 248 LEU   B CA    1 
ATOM   15890 C  C     . LEU   F 2  246 ? -17.506 70.209  -42.087  1.00 40.18  ? 248 LEU   B C     1 
ATOM   15891 O  O     . LEU   F 2  246 ? -17.138 70.712  -41.025  1.00 40.91  ? 248 LEU   B O     1 
ATOM   15892 C  CB    . LEU   F 2  246 ? -15.818 70.130  -43.923  1.00 38.61  ? 248 LEU   B CB    1 
ATOM   15893 C  CG    . LEU   F 2  246 ? -15.874 68.604  -43.937  1.00 41.52  ? 248 LEU   B CG    1 
ATOM   15894 C  CD1   . LEU   F 2  246 ? -16.862 68.087  -44.988  1.00 42.25  ? 248 LEU   B CD1   1 
ATOM   15895 C  CD2   . LEU   F 2  246 ? -14.475 68.048  -44.177  1.00 50.18  ? 248 LEU   B CD2   1 
ATOM   15896 N  N     . ASN   F 2  247 ? -18.300 69.150  -42.158  1.00 35.38  ? 249 ASN   B N     1 
ATOM   15897 C  CA    . ASN   F 2  247 ? -18.779 68.414  -41.006  1.00 29.79  ? 249 ASN   B CA    1 
ATOM   15898 C  C     . ASN   F 2  247 ? -18.877 69.262  -39.735  1.00 35.82  ? 249 ASN   B C     1 
ATOM   15899 O  O     . ASN   F 2  247 ? -18.256 68.931  -38.723  1.00 45.40  ? 249 ASN   B O     1 
ATOM   15900 C  CB    . ASN   F 2  247 ? -17.873 67.210  -40.832  1.00 29.17  ? 249 ASN   B CB    1 
ATOM   15901 C  CG    . ASN   F 2  247 ? -17.868 66.346  -42.056  1.00 41.09  ? 249 ASN   B CG    1 
ATOM   15902 O  OD1   . ASN   F 2  247 ? -18.911 66.192  -42.704  1.00 43.64  ? 249 ASN   B OD1   1 
ATOM   15903 N  ND2   . ASN   F 2  247 ? -16.704 65.796  -42.415  1.00 36.40  ? 249 ASN   B ND2   1 
ATOM   15904 N  N     . ALA   F 2  248 ? -19.677 70.335  -39.759  1.00 36.74  ? 250 ALA   B N     1 
ATOM   15905 C  CA    . ALA   F 2  248 ? -19.712 71.295  -38.658  1.00 42.69  ? 250 ALA   B CA    1 
ATOM   15906 C  C     . ALA   F 2  248 ? -20.865 71.082  -37.695  1.00 33.60  ? 250 ALA   B C     1 
ATOM   15907 O  O     . ALA   F 2  248 ? -20.997 71.852  -36.744  1.00 39.93  ? 250 ALA   B O     1 
ATOM   15908 C  CB    . ALA   F 2  248 ? -19.765 72.731  -39.188  1.00 33.32  ? 250 ALA   B CB    1 
ATOM   15909 N  N     . ASP   F 2  249 ? -21.718 70.091  -37.934  1.00 33.79  ? 251 ASP   B N     1 
ATOM   15910 C  CA    . ASP   F 2  249 ? -22.709 69.638  -36.961  1.00 32.28  ? 251 ASP   B CA    1 
ATOM   15911 C  C     . ASP   F 2  249 ? -22.843 68.124  -37.105  1.00 32.75  ? 251 ASP   B C     1 
ATOM   15912 O  O     . ASP   F 2  249 ? -22.252 67.516  -37.998  1.00 27.74  ? 251 ASP   B O     1 
ATOM   15913 C  CB    . ASP   F 2  249 ? -24.063 70.340  -37.137  1.00 25.65  ? 251 ASP   B CB    1 
ATOM   15914 C  CG    . ASP   F 2  249 ? -24.714 70.018  -38.462  1.00 33.40  ? 251 ASP   B CG    1 
ATOM   15915 O  OD1   . ASP   F 2  249 ? -25.167 68.868  -38.652  1.00 37.05  ? 251 ASP   B OD1   1 
ATOM   15916 O  OD2   . ASP   F 2  249 ? -24.766 70.919  -39.324  1.00 45.02  ? 251 ASP   B OD2   1 
ATOM   15917 N  N     . LEU   F 2  250 ? -23.630 67.506  -36.220  1.00 29.20  ? 252 LEU   B N     1 
ATOM   15918 C  CA    . LEU   F 2  250 ? -23.646 66.048  -36.170  1.00 24.30  ? 252 LEU   B CA    1 
ATOM   15919 C  C     . LEU   F 2  250 ? -24.384 65.457  -37.365  1.00 28.53  ? 252 LEU   B C     1 
ATOM   15920 O  O     . LEU   F 2  250 ? -23.992 64.403  -37.873  1.00 29.30  ? 252 LEU   B O     1 
ATOM   15921 C  CB    . LEU   F 2  250 ? -24.269 65.557  -34.858  1.00 29.60  ? 252 LEU   B CB    1 
ATOM   15922 C  CG    . LEU   F 2  250 ? -23.613 65.953  -33.532  1.00 35.57  ? 252 LEU   B CG    1 
ATOM   15923 C  CD1   . LEU   F 2  250 ? -24.453 65.482  -32.340  1.00 29.65  ? 252 LEU   B CD1   1 
ATOM   15924 C  CD2   . LEU   F 2  250 ? -22.197 65.417  -33.460  1.00 23.77  ? 252 LEU   B CD2   1 
ATOM   15925 N  N     . ARG   F 2  251 ? -25.464 66.101  -37.831  1.00 32.51  ? 253 ARG   B N     1 
ATOM   15926 C  CA    . ARG   F 2  251 ? -26.203 65.497  -38.933  1.00 23.75  ? 253 ARG   B CA    1 
ATOM   15927 C  C     . ARG   F 2  251 ? -25.388 65.571  -40.214  1.00 27.77  ? 253 ARG   B C     1 
ATOM   15928 O  O     . ARG   F 2  251 ? -25.269 64.581  -40.948  1.00 23.93  ? 253 ARG   B O     1 
ATOM   15929 C  CB    . ARG   F 2  251 ? -27.560 66.159  -39.110  1.00 21.18  ? 253 ARG   B CB    1 
ATOM   15930 C  CG    . ARG   F 2  251 ? -28.448 65.351  -40.030  1.00 25.69  ? 253 ARG   B CG    1 
ATOM   15931 C  CD    . ARG   F 2  251 ? -29.873 65.825  -40.065  1.00 26.51  ? 253 ARG   B CD    1 
ATOM   15932 N  NE    . ARG   F 2  251 ? -30.378 66.098  -38.731  1.00 27.55  ? 253 ARG   B NE    1 
ATOM   15933 C  CZ    . ARG   F 2  251 ? -30.841 65.176  -37.899  1.00 51.06  ? 253 ARG   B CZ    1 
ATOM   15934 N  NH1   . ARG   F 2  251 ? -30.960 63.908  -38.268  1.00 61.12  ? 253 ARG   B NH1   1 
ATOM   15935 N  NH2   . ARG   F 2  251 ? -31.182 65.532  -36.659  1.00 51.92  ? 253 ARG   B NH2   1 
ATOM   15936 N  N     . LYS   F 2  252 ? -24.773 66.727  -40.466  1.00 32.69  ? 254 LYS   B N     1 
ATOM   15937 C  CA    . LYS   F 2  252 ? -23.964 66.884  -41.667  1.00 34.25  ? 254 LYS   B CA    1 
ATOM   15938 C  C     . LYS   F 2  252 ? -22.779 65.928  -41.667  1.00 29.76  ? 254 LYS   B C     1 
ATOM   15939 O  O     . LYS   F 2  252 ? -22.391 65.405  -42.720  1.00 32.75  ? 254 LYS   B O     1 
ATOM   15940 C  CB    . LYS   F 2  252 ? -23.515 68.336  -41.800  1.00 34.74  ? 254 LYS   B CB    1 
ATOM   15941 C  CG    . LYS   F 2  252 ? -24.286 69.045  -42.893  1.00 38.16  ? 254 LYS   B CG    1 
ATOM   15942 C  CD    . LYS   F 2  252 ? -24.131 70.554  -42.847  1.00 36.38  ? 254 LYS   B CD    1 
ATOM   15943 C  CE    . LYS   F 2  252 ? -24.651 71.168  -44.157  1.00 39.67  ? 254 LYS   B CE    1 
ATOM   15944 N  NZ    . LYS   F 2  252 ? -24.719 72.655  -44.061  1.00 32.92  ? 254 LYS   B NZ    1 
ATOM   15945 N  N     . LEU   F 2  253 ? -22.192 65.676  -40.499  1.00 29.58  ? 255 LEU   B N     1 
ATOM   15946 C  CA    . LEU   F 2  253 ? -21.151 64.661  -40.439  1.00 26.92  ? 255 LEU   B CA    1 
ATOM   15947 C  C     . LEU   F 2  253 ? -21.728 63.298  -40.778  1.00 28.32  ? 255 LEU   B C     1 
ATOM   15948 O  O     . LEU   F 2  253 ? -21.113 62.519  -41.509  1.00 27.81  ? 255 LEU   B O     1 
ATOM   15949 C  CB    . LEU   F 2  253 ? -20.505 64.665  -39.060  1.00 31.96  ? 255 LEU   B CB    1 
ATOM   15950 C  CG    . LEU   F 2  253 ? -19.622 63.498  -38.613  1.00 33.21  ? 255 LEU   B CG    1 
ATOM   15951 C  CD1   . LEU   F 2  253 ? -18.247 63.520  -39.294  1.00 24.33  ? 255 LEU   B CD1   1 
ATOM   15952 C  CD2   . LEU   F 2  253 ? -19.510 63.525  -37.092  1.00 17.13  ? 255 LEU   B CD2   1 
ATOM   15953 N  N     . ALA   F 2  254 ? -22.942 63.015  -40.294  1.00 27.20  ? 256 ALA   B N     1 
ATOM   15954 C  CA    . ALA   F 2  254 ? -23.537 61.699  -40.512  1.00 31.26  ? 256 ALA   B CA    1 
ATOM   15955 C  C     . ALA   F 2  254 ? -23.848 61.473  -41.989  1.00 30.40  ? 256 ALA   B C     1 
ATOM   15956 O  O     . ALA   F 2  254 ? -23.711 60.345  -42.495  1.00 29.19  ? 256 ALA   B O     1 
ATOM   15957 C  CB    . ALA   F 2  254 ? -24.798 61.533  -39.645  1.00 25.66  ? 256 ALA   B CB    1 
ATOM   15958 N  N     . VAL   F 2  255 ? -24.256 62.539  -42.694  1.00 30.95  ? 257 VAL   B N     1 
ATOM   15959 C  CA    . VAL   F 2  255 ? -24.597 62.452  -44.120  1.00 27.24  ? 257 VAL   B CA    1 
ATOM   15960 C  C     . VAL   F 2  255 ? -23.348 62.239  -44.977  1.00 31.65  ? 257 VAL   B C     1 
ATOM   15961 O  O     . VAL   F 2  255 ? -23.430 61.679  -46.083  1.00 32.70  ? 257 VAL   B O     1 
ATOM   15962 C  CB    . VAL   F 2  255 ? -25.343 63.726  -44.564  1.00 27.55  ? 257 VAL   B CB    1 
ATOM   15963 C  CG1   . VAL   F 2  255 ? -25.391 63.800  -46.098  1.00 23.31  ? 257 VAL   B CG1   1 
ATOM   15964 C  CG2   . VAL   F 2  255 ? -26.721 63.792  -43.952  1.00 22.74  ? 257 VAL   B CG2   1 
ATOM   15965 N  N     . ASN   F 2  256 ? -22.187 62.711  -44.505  1.00 24.96  ? 258 ASN   B N     1 
ATOM   15966 C  CA    . ASN   F 2  256 ? -20.928 62.517  -45.218  1.00 27.52  ? 258 ASN   B CA    1 
ATOM   15967 C  C     . ASN   F 2  256 ? -20.261 61.206  -44.889  1.00 28.96  ? 258 ASN   B C     1 
ATOM   15968 O  O     . ASN   F 2  256 ? -19.567 60.656  -45.748  1.00 33.89  ? 258 ASN   B O     1 
ATOM   15969 C  CB    . ASN   F 2  256 ? -19.944 63.643  -44.908  1.00 26.42  ? 258 ASN   B CB    1 
ATOM   15970 C  CG    . ASN   F 2  256 ? -20.185 64.859  -45.755  1.00 32.40  ? 258 ASN   B CG    1 
ATOM   15971 O  OD1   . ASN   F 2  256 ? -20.753 64.756  -46.838  1.00 35.95  ? 258 ASN   B OD1   1 
ATOM   15972 N  ND2   . ASN   F 2  256 ? -19.749 66.025  -45.275  1.00 35.90  ? 258 ASN   B ND2   1 
ATOM   15973 N  N     . MET   F 2  257 ? -20.453 60.688  -43.671  1.00 30.40  ? 259 MET   B N     1 
ATOM   15974 C  CA    . MET   F 2  257 ? -19.774 59.467  -43.249  1.00 30.61  ? 259 MET   B CA    1 
ATOM   15975 C  C     . MET   F 2  257 ? -20.578 58.191  -43.476  1.00 34.43  ? 259 MET   B C     1 
ATOM   15976 O  O     . MET   F 2  257 ? -19.973 57.139  -43.730  1.00 33.75  ? 259 MET   B O     1 
ATOM   15977 C  CB    . MET   F 2  257 ? -19.402 59.558  -41.777  1.00 27.16  ? 259 MET   B CB    1 
ATOM   15978 C  CG    . MET   F 2  257 ? -18.335 60.631  -41.539  1.00 36.27  ? 259 MET   B CG    1 
ATOM   15979 S  SD    . MET   F 2  257 ? -16.936 60.461  -42.674  1.00 32.06  ? 259 MET   B SD    1 
ATOM   15980 C  CE    . MET   F 2  257 ? -16.068 59.067  -41.927  1.00 23.99  ? 259 MET   B CE    1 
ATOM   15981 N  N     . VAL   F 2  258 ? -21.909 58.240  -43.412  1.00 27.55  ? 260 VAL   B N     1 
ATOM   15982 C  CA    . VAL   F 2  258 ? -22.672 56.996  -43.282  1.00 30.60  ? 260 VAL   B CA    1 
ATOM   15983 C  C     . VAL   F 2  258 ? -23.466 56.685  -44.548  1.00 31.69  ? 260 VAL   B C     1 
ATOM   15984 O  O     . VAL   F 2  258 ? -24.572 57.212  -44.742  1.00 28.49  ? 260 VAL   B O     1 
ATOM   15985 C  CB    . VAL   F 2  258 ? -23.570 57.044  -42.033  1.00 28.27  ? 260 VAL   B CB    1 
ATOM   15986 C  CG1   . VAL   F 2  258 ? -24.301 55.703  -41.814  1.00 24.45  ? 260 VAL   B CG1   1 
ATOM   15987 C  CG2   . VAL   F 2  258 ? -22.718 57.385  -40.825  1.00 26.36  ? 260 VAL   B CG2   1 
ATOM   15988 N  N     . PRO   F 2  259 ? -22.946 55.819  -45.424  1.00 31.18  ? 261 PRO   B N     1 
ATOM   15989 C  CA    . PRO   F 2  259 ? -23.650 55.495  -46.672  1.00 25.13  ? 261 PRO   B CA    1 
ATOM   15990 C  C     . PRO   F 2  259 ? -24.747 54.446  -46.529  1.00 28.29  ? 261 PRO   B C     1 
ATOM   15991 O  O     . PRO   F 2  259 ? -25.548 54.271  -47.461  1.00 32.07  ? 261 PRO   B O     1 
ATOM   15992 C  CB    . PRO   F 2  259 ? -22.519 54.968  -47.563  1.00 26.93  ? 261 PRO   B CB    1 
ATOM   15993 C  CG    . PRO   F 2  259 ? -21.605 54.287  -46.594  1.00 26.09  ? 261 PRO   B CG    1 
ATOM   15994 C  CD    . PRO   F 2  259 ? -21.615 55.184  -45.366  1.00 29.00  ? 261 PRO   B CD    1 
ATOM   15995 N  N     . PHE   F 2  260 ? -24.783 53.713  -45.421  1.00 32.13  ? 262 PHE   B N     1 
ATOM   15996 C  CA    . PHE   F 2  260 ? -25.776 52.690  -45.168  1.00 29.15  ? 262 PHE   B CA    1 
ATOM   15997 C  C     . PHE   F 2  260 ? -26.015 52.720  -43.661  1.00 30.24  ? 262 PHE   B C     1 
ATOM   15998 O  O     . PHE   F 2  260 ? -25.027 52.739  -42.896  1.00 24.39  ? 262 PHE   B O     1 
ATOM   15999 C  CB    . PHE   F 2  260 ? -25.312 51.316  -45.622  1.00 21.37  ? 262 PHE   B CB    1 
ATOM   16000 C  CG    . PHE   F 2  260 ? -24.951 51.253  -47.071  1.00 31.19  ? 262 PHE   B CG    1 
ATOM   16001 C  CD1   . PHE   F 2  260 ? -25.935 51.170  -48.044  1.00 35.55  ? 262 PHE   B CD1   1 
ATOM   16002 C  CD2   . PHE   F 2  260 ? -23.629 51.242  -47.479  1.00 33.56  ? 262 PHE   B CD2   1 
ATOM   16003 C  CE1   . PHE   F 2  260 ? -25.606 51.097  -49.409  1.00 31.51  ? 262 PHE   B CE1   1 
ATOM   16004 C  CE2   . PHE   F 2  260 ? -23.306 51.164  -48.849  1.00 36.01  ? 262 PHE   B CE2   1 
ATOM   16005 C  CZ    . PHE   F 2  260 ? -24.311 51.090  -49.810  1.00 20.42  ? 262 PHE   B CZ    1 
ATOM   16006 N  N     . PRO   F 2  261 ? -27.283 52.742  -43.208  1.00 27.34  ? 263 PRO   B N     1 
ATOM   16007 C  CA    . PRO   F 2  261 ? -27.554 53.086  -41.794  1.00 27.50  ? 263 PRO   B CA    1 
ATOM   16008 C  C     . PRO   F 2  261 ? -26.783 52.261  -40.782  1.00 23.66  ? 263 PRO   B C     1 
ATOM   16009 O  O     . PRO   F 2  261 ? -26.380 52.807  -39.748  1.00 24.95  ? 263 PRO   B O     1 
ATOM   16010 C  CB    . PRO   F 2  261 ? -29.072 52.877  -41.654  1.00 16.95  ? 263 PRO   B CB    1 
ATOM   16011 C  CG    . PRO   F 2  261 ? -29.451 52.012  -42.824  1.00 18.76  ? 263 PRO   B CG    1 
ATOM   16012 C  CD    . PRO   F 2  261 ? -28.523 52.442  -43.938  1.00 26.21  ? 263 PRO   B CD    1 
ATOM   16013 N  N     . ARG   F 2  262 ? -26.535 50.978  -41.044  1.00 26.05  ? 264 ARG   B N     1 
ATOM   16014 C  CA    . ARG   F 2  262 ? -25.880 50.174  -40.009  1.00 25.31  ? 264 ARG   B CA    1 
ATOM   16015 C  C     . ARG   F 2  262 ? -24.360 50.348  -39.979  1.00 26.70  ? 264 ARG   B C     1 
ATOM   16016 O  O     . ARG   F 2  262 ? -23.750 50.160  -38.925  1.00 32.80  ? 264 ARG   B O     1 
ATOM   16017 C  CB    . ARG   F 2  262 ? -26.235 48.696  -40.181  1.00 24.78  ? 264 ARG   B CB    1 
ATOM   16018 C  CG    . ARG   F 2  262 ? -27.735 48.409  -40.304  1.00 27.30  ? 264 ARG   B CG    1 
ATOM   16019 C  CD    . ARG   F 2  262 ? -27.998 46.942  -40.667  1.00 25.72  ? 264 ARG   B CD    1 
ATOM   16020 N  NE    . ARG   F 2  262 ? -27.629 46.076  -39.552  1.00 39.60  ? 264 ARG   B NE    1 
ATOM   16021 C  CZ    . ARG   F 2  262 ? -27.042 44.893  -39.675  1.00 39.18  ? 264 ARG   B CZ    1 
ATOM   16022 N  NH1   . ARG   F 2  262 ? -26.739 44.385  -40.863  1.00 50.44  ? 264 ARG   B NH1   1 
ATOM   16023 N  NH2   . ARG   F 2  262 ? -26.749 44.202  -38.581  1.00 26.08  ? 264 ARG   B NH2   1 
ATOM   16024 N  N     . LEU   F 2  263 ? -23.719 50.705  -41.093  1.00 26.85  ? 265 LEU   B N     1 
ATOM   16025 C  CA    . LEU   F 2  263 ? -22.260 50.870  -41.107  1.00 24.29  ? 265 LEU   B CA    1 
ATOM   16026 C  C     . LEU   F 2  263 ? -21.901 52.296  -40.683  1.00 26.39  ? 265 LEU   B C     1 
ATOM   16027 O  O     . LEU   F 2  263 ? -21.518 53.160  -41.487  1.00 23.08  ? 265 LEU   B O     1 
ATOM   16028 C  CB    . LEU   F 2  263 ? -21.688 50.519  -42.476  1.00 27.53  ? 265 LEU   B CB    1 
ATOM   16029 C  CG    . LEU   F 2  263 ? -22.305 49.324  -43.221  1.00 30.72  ? 265 LEU   B CG    1 
ATOM   16030 C  CD1   . LEU   F 2  263 ? -21.501 48.984  -44.469  1.00 32.95  ? 265 LEU   B CD1   1 
ATOM   16031 C  CD2   . LEU   F 2  263 ? -22.432 48.110  -42.321  1.00 30.53  ? 265 LEU   B CD2   1 
ATOM   16032 N  N     . HIS   F 2  264 ? -22.002 52.531  -39.377  1.00 24.08  ? 266 HIS   B N     1 
ATOM   16033 C  CA    . HIS   F 2  264 ? -21.706 53.831  -38.785  1.00 28.90  ? 266 HIS   B CA    1 
ATOM   16034 C  C     . HIS   F 2  264 ? -20.630 53.727  -37.704  1.00 21.98  ? 266 HIS   B C     1 
ATOM   16035 O  O     . HIS   F 2  264 ? -20.585 54.540  -36.775  1.00 25.42  ? 266 HIS   B O     1 
ATOM   16036 C  CB    . HIS   F 2  264 ? -22.980 54.494  -38.232  1.00 27.04  ? 266 HIS   B CB    1 
ATOM   16037 C  CG    . HIS   F 2  264 ? -23.759 53.649  -37.257  1.00 29.46  ? 266 HIS   B CG    1 
ATOM   16038 N  ND1   . HIS   F 2  264 ? -24.744 52.761  -37.649  1.00 26.38  ? 266 HIS   B ND1   1 
ATOM   16039 C  CD2   . HIS   F 2  264 ? -23.713 53.584  -35.904  1.00 29.93  ? 266 HIS   B CD2   1 
ATOM   16040 C  CE1   . HIS   F 2  264 ? -25.267 52.191  -36.578  1.00 28.90  ? 266 HIS   B CE1   1 
ATOM   16041 N  NE2   . HIS   F 2  264 ? -24.657 52.670  -35.508  1.00 26.53  ? 266 HIS   B NE2   1 
ATOM   16042 N  N     . PHE   F 2  265 ? -19.738 52.756  -37.828  1.00 22.27  ? 267 PHE   B N     1 
ATOM   16043 C  CA    . PHE   F 2  265 ? -18.662 52.545  -36.861  1.00 22.89  ? 267 PHE   B CA    1 
ATOM   16044 C  C     . PHE   F 2  265 ? -17.340 53.047  -37.445  1.00 23.10  ? 267 PHE   B C     1 
ATOM   16045 O  O     . PHE   F 2  265 ? -16.792 52.437  -38.365  1.00 29.50  ? 267 PHE   B O     1 
ATOM   16046 C  CB    . PHE   F 2  265 ? -18.587 51.069  -36.477  1.00 23.20  ? 267 PHE   B CB    1 
ATOM   16047 C  CG    . PHE   F 2  265 ? -19.801 50.585  -35.759  1.00 23.08  ? 267 PHE   B CG    1 
ATOM   16048 C  CD1   . PHE   F 2  265 ? -20.882 50.103  -36.455  1.00 22.83  ? 267 PHE   B CD1   1 
ATOM   16049 C  CD2   . PHE   F 2  265 ? -19.881 50.660  -34.381  1.00 27.53  ? 267 PHE   B CD2   1 
ATOM   16050 C  CE1   . PHE   F 2  265 ? -22.008 49.681  -35.779  1.00 27.46  ? 267 PHE   B CE1   1 
ATOM   16051 C  CE2   . PHE   F 2  265 ? -21.005 50.234  -33.702  1.00 22.83  ? 267 PHE   B CE2   1 
ATOM   16052 C  CZ    . PHE   F 2  265 ? -22.067 49.749  -34.393  1.00 20.85  ? 267 PHE   B CZ    1 
ATOM   16053 N  N     . PHE   F 2  266 ? -16.818 54.139  -36.894  1.00 20.70  ? 268 PHE   B N     1 
ATOM   16054 C  CA    . PHE   F 2  266 ? -15.650 54.802  -37.448  1.00 21.42  ? 268 PHE   B CA    1 
ATOM   16055 C  C     . PHE   F 2  266 ? -14.370 54.346  -36.776  1.00 18.93  ? 268 PHE   B C     1 
ATOM   16056 O  O     . PHE   F 2  266 ? -14.371 53.931  -35.617  1.00 30.69  ? 268 PHE   B O     1 
ATOM   16057 C  CB    . PHE   F 2  266 ? -15.769 56.309  -37.301  1.00 25.36  ? 268 PHE   B CB    1 
ATOM   16058 C  CG    . PHE   F 2  266 ? -17.030 56.861  -37.854  1.00 22.84  ? 268 PHE   B CG    1 
ATOM   16059 C  CD1   . PHE   F 2  266 ? -17.665 56.235  -38.914  1.00 25.19  ? 268 PHE   B CD1   1 
ATOM   16060 C  CD2   . PHE   F 2  266 ? -17.599 57.991  -37.311  1.00 27.59  ? 268 PHE   B CD2   1 
ATOM   16061 C  CE1   . PHE   F 2  266 ? -18.826 56.726  -39.434  1.00 19.30  ? 268 PHE   B CE1   1 
ATOM   16062 C  CE2   . PHE   F 2  266 ? -18.787 58.483  -37.820  1.00 30.20  ? 268 PHE   B CE2   1 
ATOM   16063 C  CZ    . PHE   F 2  266 ? -19.393 57.844  -38.891  1.00 26.44  ? 268 PHE   B CZ    1 
ATOM   16064 N  N     . MET   F 2  267 ? -13.282 54.411  -37.532  1.00 20.06  ? 269 MET   B N     1 
ATOM   16065 C  CA    . MET   F 2  267 ? -11.913 54.239  -37.048  1.00 26.69  ? 269 MET   B CA    1 
ATOM   16066 C  C     . MET   F 2  267 ? -11.279 55.612  -36.906  1.00 20.48  ? 269 MET   B C     1 
ATOM   16067 O  O     . MET   F 2  267 ? -10.995 56.250  -37.931  1.00 27.26  ? 269 MET   B O     1 
ATOM   16068 C  CB    . MET   F 2  267 ? -11.079 53.415  -38.023  1.00 21.33  ? 269 MET   B CB    1 
ATOM   16069 C  CG    . MET   F 2  267 ? -11.545 52.055  -38.342  1.00 34.10  ? 269 MET   B CG    1 
ATOM   16070 S  SD    . MET   F 2  267 ? -10.274 51.335  -39.412  1.00 49.21  ? 269 MET   B SD    1 
ATOM   16071 C  CE    . MET   F 2  267 ? -8.797  51.813  -38.525  1.00 19.36  ? 269 MET   B CE    1 
ATOM   16072 N  N     . PRO   F 2  268 ? -11.022 56.105  -35.707  1.00 21.64  ? 270 PRO   B N     1 
ATOM   16073 C  CA    . PRO   F 2  268 ? -10.275 57.357  -35.583  1.00 20.18  ? 270 PRO   B CA    1 
ATOM   16074 C  C     . PRO   F 2  268 ? -8.792  57.076  -35.730  1.00 26.63  ? 270 PRO   B C     1 
ATOM   16075 O  O     . PRO   F 2  268 ? -8.329  55.935  -35.623  1.00 23.74  ? 270 PRO   B O     1 
ATOM   16076 C  CB    . PRO   F 2  268 ? -10.610 57.857  -34.169  1.00 23.23  ? 270 PRO   B CB    1 
ATOM   16077 C  CG    . PRO   F 2  268 ? -11.380 56.677  -33.489  1.00 25.56  ? 270 PRO   B CG    1 
ATOM   16078 C  CD    . PRO   F 2  268 ? -11.271 55.484  -34.390  1.00 25.55  ? 270 PRO   B CD    1 
ATOM   16079 N  N     . GLY   F 2  269 ? -8.062  58.145  -36.018  1.00 28.65  ? 271 GLY   B N     1 
ATOM   16080 C  CA    . GLY   F 2  269 ? -6.623  58.084  -36.164  1.00 32.87  ? 271 GLY   B CA    1 
ATOM   16081 C  C     . GLY   F 2  269 ? -6.071  59.452  -35.875  1.00 33.56  ? 271 GLY   B C     1 
ATOM   16082 O  O     . GLY   F 2  269 ? -6.731  60.461  -36.134  1.00 37.72  ? 271 GLY   B O     1 
ATOM   16083 N  N     . PHE   F 2  270 ? -4.870  59.493  -35.303  1.00 38.36  ? 272 PHE   B N     1 
ATOM   16084 C  CA    . PHE   F 2  270 ? -4.321  60.757  -34.830  1.00 35.32  ? 272 PHE   B CA    1 
ATOM   16085 C  C     . PHE   F 2  270 ? -2.828  60.805  -35.080  1.00 35.32  ? 272 PHE   B C     1 
ATOM   16086 O  O     . PHE   F 2  270 ? -2.139  59.802  -34.902  1.00 35.76  ? 272 PHE   B O     1 
ATOM   16087 C  CB    . PHE   F 2  270 ? -4.594  60.932  -33.346  1.00 27.00  ? 272 PHE   B CB    1 
ATOM   16088 C  CG    . PHE   F 2  270 ? -4.270  62.295  -32.823  1.00 36.31  ? 272 PHE   B CG    1 
ATOM   16089 C  CD1   . PHE   F 2  270 ? -2.974  62.617  -32.440  1.00 33.84  ? 272 PHE   B CD1   1 
ATOM   16090 C  CD2   . PHE   F 2  270 ? -5.277  63.253  -32.664  1.00 36.64  ? 272 PHE   B CD2   1 
ATOM   16091 C  CE1   . PHE   F 2  270 ? -2.672  63.892  -31.933  1.00 32.70  ? 272 PHE   B CE1   1 
ATOM   16092 C  CE2   . PHE   F 2  270 ? -4.990  64.514  -32.150  1.00 35.53  ? 272 PHE   B CE2   1 
ATOM   16093 C  CZ    . PHE   F 2  270 ? -3.683  64.831  -31.782  1.00 33.67  ? 272 PHE   B CZ    1 
ATOM   16094 N  N     . ALA   F 2  271 ? -2.324  61.966  -35.484  1.00 33.64  ? 273 ALA   B N     1 
ATOM   16095 C  CA    . ALA   F 2  271 ? -0.877  62.120  -35.560  1.00 37.45  ? 273 ALA   B CA    1 
ATOM   16096 C  C     . ALA   F 2  271 ? -0.505  63.546  -35.196  1.00 37.44  ? 273 ALA   B C     1 
ATOM   16097 O  O     . ALA   F 2  271 ? -1.293  64.470  -35.431  1.00 36.69  ? 273 ALA   B O     1 
ATOM   16098 C  CB    . ALA   F 2  271 ? -0.326  61.759  -36.946  1.00 30.42  ? 273 ALA   B CB    1 
ATOM   16099 N  N     . PRO   F 2  272 ? 0.672   63.754  -34.578  1.00 37.92  ? 274 PRO   B N     1 
ATOM   16100 C  CA    . PRO   F 2  272 ? 1.624   62.731  -34.112  1.00 37.41  ? 274 PRO   B CA    1 
ATOM   16101 C  C     . PRO   F 2  272 ? 1.145   62.047  -32.848  1.00 36.03  ? 274 PRO   B C     1 
ATOM   16102 O  O     . PRO   F 2  272 ? 0.500   62.683  -32.024  1.00 35.94  ? 274 PRO   B O     1 
ATOM   16103 C  CB    . PRO   F 2  272 ? 2.882   63.549  -33.813  1.00 35.31  ? 274 PRO   B CB    1 
ATOM   16104 C  CG    . PRO   F 2  272 ? 2.314   64.842  -33.292  1.00 31.80  ? 274 PRO   B CG    1 
ATOM   16105 C  CD    . PRO   F 2  272 ? 1.134   65.108  -34.219  1.00 31.74  ? 274 PRO   B CD    1 
ATOM   16106 N  N     . LEU   F 2  273 ? 1.472   60.774  -32.649  1.00 39.79  ? 275 LEU   B N     1 
ATOM   16107 C  CA    . LEU   F 2  273 ? 1.246   60.138  -31.358  1.00 33.64  ? 275 LEU   B CA    1 
ATOM   16108 C  C     . LEU   F 2  273 ? 2.263   60.647  -30.352  1.00 36.39  ? 275 LEU   B C     1 
ATOM   16109 O  O     . LEU   F 2  273 ? 3.431   60.862  -30.688  1.00 39.98  ? 275 LEU   B O     1 
ATOM   16110 C  CB    . LEU   F 2  273 ? 1.346   58.620  -31.487  1.00 28.24  ? 275 LEU   B CB    1 
ATOM   16111 C  CG    . LEU   F 2  273 ? 0.367   58.032  -32.514  1.00 37.18  ? 275 LEU   B CG    1 
ATOM   16112 C  CD1   . LEU   F 2  273 ? 0.759   56.602  -32.894  1.00 35.28  ? 275 LEU   B CD1   1 
ATOM   16113 C  CD2   . LEU   F 2  273 ? -1.067  58.081  -31.975  1.00 28.61  ? 275 LEU   B CD2   1 
ATOM   16114 N  N     . THR   F 2  274 ? 1.810   60.852  -29.116  1.00 37.95  ? 276 THR   B N     1 
ATOM   16115 C  CA    . THR   F 2  274 ? 2.672   61.344  -28.048  1.00 42.07  ? 276 THR   B CA    1 
ATOM   16116 C  C     . THR   F 2  274 ? 2.316   60.730  -26.698  1.00 49.08  ? 276 THR   B C     1 
ATOM   16117 O  O     . THR   F 2  274 ? 1.140   60.506  -26.389  1.00 47.96  ? 276 THR   B O     1 
ATOM   16118 C  CB    . THR   F 2  274 ? 2.594   62.859  -27.915  1.00 38.72  ? 276 THR   B CB    1 
ATOM   16119 O  OG1   . THR   F 2  274 ? 1.267   63.236  -27.511  1.00 34.71  ? 276 THR   B OG1   1 
ATOM   16120 C  CG2   . THR   F 2  274 ? 2.974   63.515  -29.235  1.00 35.26  ? 276 THR   B CG2   1 
ATOM   16121 N  N     . SER   F 2  275 ? 3.350   60.465  -25.901  1.00 46.02  ? 277 SER   B N     1 
ATOM   16122 C  CA    . SER   F 2  275 ? 3.173   60.173  -24.491  1.00 38.20  ? 277 SER   B CA    1 
ATOM   16123 C  C     . SER   F 2  275 ? 2.924   61.470  -23.751  1.00 43.78  ? 277 SER   B C     1 
ATOM   16124 O  O     . SER   F 2  275 ? 3.544   62.494  -24.043  1.00 58.16  ? 277 SER   B O     1 
ATOM   16125 C  CB    . SER   F 2  275 ? 4.407   59.487  -23.906  1.00 31.63  ? 277 SER   B CB    1 
ATOM   16126 N  N     . ARG   F 2  276 ? 1.984   61.435  -22.819  1.00 44.14  ? 278 ARG   B N     1 
ATOM   16127 C  CA    . ARG   F 2  276 ? 1.910   62.466  -21.806  1.00 44.72  ? 278 ARG   B CA    1 
ATOM   16128 C  C     . ARG   F 2  276 ? 3.322   62.799  -21.328  1.00 57.85  ? 278 ARG   B C     1 
ATOM   16129 O  O     . ARG   F 2  276 ? 4.097   61.907  -20.960  1.00 58.02  ? 278 ARG   B O     1 
ATOM   16130 C  CB    . ARG   F 2  276 ? 1.035   61.957  -20.657  1.00 51.78  ? 278 ARG   B CB    1 
ATOM   16131 C  CG    . ARG   F 2  276 ? 1.061   60.415  -20.541  1.00 55.04  ? 278 ARG   B CG    1 
ATOM   16132 C  CD    . ARG   F 2  276 ? -0.148  59.798  -19.779  1.00 56.46  ? 278 ARG   B CD    1 
ATOM   16133 N  NE    . ARG   F 2  276 ? -0.261  60.175  -18.373  1.00 48.98  ? 278 ARG   B NE    1 
ATOM   16134 C  CZ    . ARG   F 2  276 ? -0.885  61.268  -17.956  1.00 68.65  ? 278 ARG   B CZ    1 
ATOM   16135 N  NH1   . ARG   F 2  276 ? -1.446  62.110  -18.808  1.00 63.32  ? 278 ARG   B NH1   1 
ATOM   16136 N  NH2   . ARG   F 2  276 ? -0.950  61.525  -16.654  1.00 78.80  ? 278 ARG   B NH2   1 
ATOM   16137 N  N     . GLY   F 2  277 ? 3.672   64.082  -21.382  1.00 53.05  ? 279 GLY   B N     1 
ATOM   16138 C  CA    . GLY   F 2  277 ? 4.997   64.533  -20.990  1.00 56.08  ? 279 GLY   B CA    1 
ATOM   16139 C  C     . GLY   F 2  277 ? 6.064   64.468  -22.065  1.00 69.30  ? 279 GLY   B C     1 
ATOM   16140 O  O     . GLY   F 2  277 ? 7.252   64.601  -21.740  1.00 72.76  ? 279 GLY   B O     1 
ATOM   16141 N  N     . SER   F 2  278 ? 5.681   64.288  -23.335  1.00 67.27  ? 280 SER   B N     1 
ATOM   16142 C  CA    . SER   F 2  278 ? 6.607   64.083  -24.446  1.00 68.28  ? 280 SER   B CA    1 
ATOM   16143 C  C     . SER   F 2  278 ? 7.289   65.364  -24.919  1.00 70.15  ? 280 SER   B C     1 
ATOM   16144 O  O     . SER   F 2  278 ? 8.135   65.284  -25.815  1.00 78.92  ? 280 SER   B O     1 
ATOM   16145 C  CB    . SER   F 2  278 ? 5.873   63.432  -25.634  1.00 58.73  ? 280 SER   B CB    1 
ATOM   16146 N  N     . GLN   F 2  279 ? 6.940   66.524  -24.355  1.00 61.66  ? 281 GLN   B N     1 
ATOM   16147 C  CA    . GLN   F 2  279 ? 7.515   67.819  -24.722  1.00 73.11  ? 281 GLN   B CA    1 
ATOM   16148 C  C     . GLN   F 2  279 ? 8.042   67.834  -26.151  1.00 70.84  ? 281 GLN   B C     1 
ATOM   16149 O  O     . GLN   F 2  279 ? 9.226   67.560  -26.375  1.00 76.79  ? 281 GLN   B O     1 
ATOM   16150 C  CB    . GLN   F 2  279 ? 8.638   68.198  -23.751  1.00 80.93  ? 281 GLN   B CB    1 
ATOM   16151 N  N     . GLN   F 2  280 ? 7.181   68.162  -27.116  1.00 79.85  ? 282 GLN   B N     1 
ATOM   16152 C  CA    . GLN   F 2  280 ? 7.517   67.995  -28.529  1.00 75.49  ? 282 GLN   B CA    1 
ATOM   16153 C  C     . GLN   F 2  280 ? 8.541   69.031  -28.987  1.00 67.15  ? 282 GLN   B C     1 
ATOM   16154 O  O     . GLN   F 2  280 ? 8.415   70.227  -28.700  1.00 63.73  ? 282 GLN   B O     1 
ATOM   16155 C  CB    . GLN   F 2  280 ? 6.253   68.077  -29.387  1.00 72.23  ? 282 GLN   B CB    1 
ATOM   16156 C  CG    . GLN   F 2  280 ? 5.381   66.820  -29.331  1.00 62.81  ? 282 GLN   B CG    1 
ATOM   16157 C  CD    . GLN   F 2  280 ? 6.001   65.647  -30.086  1.00 75.62  ? 282 GLN   B CD    1 
ATOM   16158 O  OE1   . GLN   F 2  280 ? 6.647   64.782  -29.487  1.00 79.15  ? 282 GLN   B OE1   1 
ATOM   16159 N  NE2   . GLN   F 2  280 ? 5.809   65.615  -31.411  1.00 63.53  ? 282 GLN   B NE2   1 
ATOM   16160 N  N     . TYR   F 2  281 ? 9.547   68.565  -29.724  1.00 65.59  ? 283 TYR   B N     1 
ATOM   16161 C  CA    . TYR   F 2  281 ? 10.681  69.404  -30.096  1.00 67.38  ? 283 TYR   B CA    1 
ATOM   16162 C  C     . TYR   F 2  281 ? 10.521  70.061  -31.463  1.00 60.81  ? 283 TYR   B C     1 
ATOM   16163 O  O     . TYR   F 2  281 ? 10.821  71.250  -31.601  1.00 61.54  ? 283 TYR   B O     1 
ATOM   16164 C  CB    . TYR   F 2  281 ? 11.975  68.587  -30.019  1.00 60.90  ? 283 TYR   B CB    1 
ATOM   16165 C  CG    . TYR   F 2  281 ? 12.307  68.264  -28.577  1.00 63.12  ? 283 TYR   B CG    1 
ATOM   16166 C  CD1   . TYR   F 2  281 ? 11.831  69.079  -27.552  1.00 66.76  ? 283 TYR   B CD1   1 
ATOM   16167 C  CD2   . TYR   F 2  281 ? 13.054  67.143  -28.229  1.00 68.61  ? 283 TYR   B CD2   1 
ATOM   16168 C  CE1   . TYR   F 2  281 ? 12.098  68.806  -26.224  1.00 71.34  ? 283 TYR   B CE1   1 
ATOM   16169 C  CE2   . TYR   F 2  281 ? 13.337  66.856  -26.888  1.00 72.97  ? 283 TYR   B CE2   1 
ATOM   16170 C  CZ    . TYR   F 2  281 ? 12.854  67.696  -25.889  1.00 78.22  ? 283 TYR   B CZ    1 
ATOM   16171 O  OH    . TYR   F 2  281 ? 13.118  67.441  -24.554  1.00 70.14  ? 283 TYR   B OH    1 
ATOM   16172 N  N     . ARG   F 2  282 ? 10.036  69.349  -32.472  1.00 56.30  ? 284 ARG   B N     1 
ATOM   16173 C  CA    . ARG   F 2  282 ? 9.655   70.006  -33.717  1.00 66.60  ? 284 ARG   B CA    1 
ATOM   16174 C  C     . ARG   F 2  282 ? 8.261   69.559  -34.117  1.00 57.89  ? 284 ARG   B C     1 
ATOM   16175 O  O     . ARG   F 2  282 ? 7.774   68.512  -33.686  1.00 57.81  ? 284 ARG   B O     1 
ATOM   16176 C  CB    . ARG   F 2  282 ? 10.628  69.720  -34.873  1.00 53.08  ? 284 ARG   B CB    1 
ATOM   16177 C  CG    . ARG   F 2  282 ? 10.617  68.292  -35.320  1.00 47.91  ? 284 ARG   B CG    1 
ATOM   16178 C  CD    . ARG   F 2  282 ? 11.361  68.129  -36.605  1.00 47.34  ? 284 ARG   B CD    1 
ATOM   16179 N  NE    . ARG   F 2  282 ? 10.981  66.893  -37.281  1.00 57.99  ? 284 ARG   B NE    1 
ATOM   16180 C  CZ    . ARG   F 2  282 ? 9.863   66.724  -37.982  1.00 52.79  ? 284 ARG   B CZ    1 
ATOM   16181 N  NH1   . ARG   F 2  282 ? 8.959   67.683  -38.093  1.00 48.08  ? 284 ARG   B NH1   1 
ATOM   16182 N  NH2   . ARG   F 2  282 ? 9.641   65.556  -38.579  1.00 52.51  ? 284 ARG   B NH2   1 
ATOM   16183 N  N     . ALA   F 2  283 ? 7.627   70.373  -34.952  1.00 54.85  ? 285 ALA   B N     1 
ATOM   16184 C  CA    . ALA   F 2  283 ? 6.336   70.020  -35.512  1.00 52.30  ? 285 ALA   B CA    1 
ATOM   16185 C  C     . ALA   F 2  283 ? 6.504   69.122  -36.733  1.00 55.94  ? 285 ALA   B C     1 
ATOM   16186 O  O     . ALA   F 2  283 ? 7.506   69.188  -37.449  1.00 52.34  ? 285 ALA   B O     1 
ATOM   16187 C  CB    . ALA   F 2  283 ? 5.564   71.275  -35.901  1.00 53.99  ? 285 ALA   B CB    1 
ATOM   16188 N  N     . LEU   F 2  284 ? 5.508   68.277  -36.975  1.00 57.17  ? 286 LEU   B N     1 
ATOM   16189 C  CA    . LEU   F 2  284 ? 5.505   67.534  -38.225  1.00 50.43  ? 286 LEU   B CA    1 
ATOM   16190 C  C     . LEU   F 2  284 ? 5.256   68.483  -39.392  1.00 41.46  ? 286 LEU   B C     1 
ATOM   16191 O  O     . LEU   F 2  284 ? 4.600   69.516  -39.254  1.00 50.36  ? 286 LEU   B O     1 
ATOM   16192 C  CB    . LEU   F 2  284 ? 4.433   66.442  -38.216  1.00 44.59  ? 286 LEU   B CB    1 
ATOM   16193 C  CG    . LEU   F 2  284 ? 4.404   65.398  -37.109  1.00 43.86  ? 286 LEU   B CG    1 
ATOM   16194 C  CD1   . LEU   F 2  284 ? 4.015   64.043  -37.705  1.00 36.56  ? 286 LEU   B CD1   1 
ATOM   16195 C  CD2   . LEU   F 2  284 ? 5.737   65.343  -36.367  1.00 43.76  ? 286 LEU   B CD2   1 
ATOM   16196 N  N     . THR   F 2  285 ? 5.796   68.126  -40.546  1.00 41.78  ? 287 THR   B N     1 
ATOM   16197 C  CA    . THR   F 2  285 ? 5.403   68.765  -41.790  1.00 45.43  ? 287 THR   B CA    1 
ATOM   16198 C  C     . THR   F 2  285 ? 4.072   68.190  -42.275  1.00 47.21  ? 287 THR   B C     1 
ATOM   16199 O  O     . THR   F 2  285 ? 3.672   67.082  -41.875  1.00 36.59  ? 287 THR   B O     1 
ATOM   16200 C  CB    . THR   F 2  285 ? 6.472   68.558  -42.863  1.00 43.64  ? 287 THR   B CB    1 
ATOM   16201 O  OG1   . THR   F 2  285 ? 6.504   67.177  -43.257  1.00 44.84  ? 287 THR   B OG1   1 
ATOM   16202 C  CG2   . THR   F 2  285 ? 7.817   68.928  -42.320  1.00 36.63  ? 287 THR   B CG2   1 
ATOM   16203 N  N     . VAL   F 2  286 ? 3.400   68.935  -43.151  1.00 38.34  ? 288 VAL   B N     1 
ATOM   16204 C  CA    . VAL   F 2  286 ? 2.104   68.497  -43.663  1.00 38.90  ? 288 VAL   B CA    1 
ATOM   16205 C  C     . VAL   F 2  286 ? 2.218   67.098  -44.294  1.00 43.34  ? 288 VAL   B C     1 
ATOM   16206 O  O     . VAL   F 2  286 ? 1.288   66.293  -44.153  1.00 37.59  ? 288 VAL   B O     1 
ATOM   16207 C  CB    . VAL   F 2  286 ? 1.508   69.525  -44.637  1.00 34.98  ? 288 VAL   B CB    1 
ATOM   16208 C  CG1   . VAL   F 2  286 ? 0.487   68.876  -45.540  1.00 34.51  ? 288 VAL   B CG1   1 
ATOM   16209 C  CG2   . VAL   F 2  286 ? 0.863   70.656  -43.868  1.00 30.53  ? 288 VAL   B CG2   1 
ATOM   16210 N  N     . PRO   F 2  287 ? 3.323   66.754  -44.964  1.00 39.85  ? 289 PRO   B N     1 
ATOM   16211 C  CA    . PRO   F 2  287 ? 3.406   65.402  -45.529  1.00 33.86  ? 289 PRO   B CA    1 
ATOM   16212 C  C     . PRO   F 2  287 ? 3.616   64.330  -44.479  1.00 36.18  ? 289 PRO   B C     1 
ATOM   16213 O  O     . PRO   F 2  287 ? 3.189   63.187  -44.684  1.00 39.76  ? 289 PRO   B O     1 
ATOM   16214 C  CB    . PRO   F 2  287 ? 4.593   65.507  -46.499  1.00 32.41  ? 289 PRO   B CB    1 
ATOM   16215 C  CG    . PRO   F 2  287 ? 4.728   66.957  -46.773  1.00 23.35  ? 289 PRO   B CG    1 
ATOM   16216 C  CD    . PRO   F 2  287 ? 4.395   67.615  -45.478  1.00 32.28  ? 289 PRO   B CD    1 
ATOM   16217 N  N     . GLU   F 2  288 ? 4.262   64.655  -43.357  1.00 38.92  ? 290 GLU   B N     1 
ATOM   16218 C  CA    . GLU   F 2  288 ? 4.327   63.689  -42.265  1.00 40.41  ? 290 GLU   B CA    1 
ATOM   16219 C  C     . GLU   F 2  288 ? 2.956   63.494  -41.636  1.00 39.00  ? 290 GLU   B C     1 
ATOM   16220 O  O     . GLU   F 2  288 ? 2.573   62.367  -41.314  1.00 40.74  ? 290 GLU   B O     1 
ATOM   16221 C  CB    . GLU   F 2  288 ? 5.326   64.136  -41.205  1.00 38.28  ? 290 GLU   B CB    1 
ATOM   16222 C  CG    . GLU   F 2  288 ? 6.773   64.180  -41.651  1.00 46.89  ? 290 GLU   B CG    1 
ATOM   16223 C  CD    . GLU   F 2  288 ? 7.651   64.976  -40.690  1.00 49.94  ? 290 GLU   B CD    1 
ATOM   16224 O  OE1   . GLU   F 2  288 ? 7.430   66.205  -40.544  1.00 42.07  ? 290 GLU   B OE1   1 
ATOM   16225 O  OE2   . GLU   F 2  288 ? 8.548   64.359  -40.069  1.00 48.61  ? 290 GLU   B OE2   1 
ATOM   16226 N  N     . LEU   F 2  289 ? 2.222   64.587  -41.419  1.00 40.53  ? 291 LEU   B N     1 
ATOM   16227 C  CA    . LEU   F 2  289 ? 0.852   64.488  -40.930  1.00 42.36  ? 291 LEU   B CA    1 
ATOM   16228 C  C     . LEU   F 2  289 ? 0.066   63.442  -41.702  1.00 39.02  ? 291 LEU   B C     1 
ATOM   16229 O  O     . LEU   F 2  289 ? -0.595  62.579  -41.108  1.00 34.72  ? 291 LEU   B O     1 
ATOM   16230 C  CB    . LEU   F 2  289 ? 0.158   65.834  -41.061  1.00 38.13  ? 291 LEU   B CB    1 
ATOM   16231 C  CG    . LEU   F 2  289 ? 0.497   66.818  -39.984  1.00 36.72  ? 291 LEU   B CG    1 
ATOM   16232 C  CD1   . LEU   F 2  289 ? -0.575  67.877  -40.028  1.00 42.66  ? 291 LEU   B CD1   1 
ATOM   16233 C  CD2   . LEU   F 2  289 ? 0.478   66.055  -38.715  1.00 28.63  ? 291 LEU   B CD2   1 
ATOM   16234 N  N     . THR   F 2  290 ? 0.147   63.508  -43.039  1.00 34.33  ? 292 THR   B N     1 
ATOM   16235 C  CA    . THR   F 2  290 ? -0.726  62.747  -43.923  1.00 30.54  ? 292 THR   B CA    1 
ATOM   16236 C  C     . THR   F 2  290 ? -0.320  61.290  -43.992  1.00 41.01  ? 292 THR   B C     1 
ATOM   16237 O  O     . THR   F 2  290 ? -1.162  60.397  -43.823  1.00 47.27  ? 292 THR   B O     1 
ATOM   16238 C  CB    . THR   F 2  290 ? -0.725  63.340  -45.325  1.00 30.44  ? 292 THR   B CB    1 
ATOM   16239 O  OG1   . THR   F 2  290 ? -1.037  64.745  -45.271  1.00 29.00  ? 292 THR   B OG1   1 
ATOM   16240 C  CG2   . THR   F 2  290 ? -1.754  62.612  -46.161  1.00 27.32  ? 292 THR   B CG2   1 
ATOM   16241 N  N     . GLN   F 2  291 ? 0.959   61.025  -44.258  1.00 38.19  ? 293 GLN   B N     1 
ATOM   16242 C  CA    . GLN   F 2  291 ? 1.441   59.652  -44.168  1.00 42.72  ? 293 GLN   B CA    1 
ATOM   16243 C  C     . GLN   F 2  291 ? 1.006   59.019  -42.854  1.00 39.34  ? 293 GLN   B C     1 
ATOM   16244 O  O     . GLN   F 2  291 ? 0.562   57.863  -42.813  1.00 33.46  ? 293 GLN   B O     1 
ATOM   16245 C  CB    . GLN   F 2  291 ? 2.967   59.619  -44.303  1.00 47.44  ? 293 GLN   B CB    1 
ATOM   16246 C  CG    . GLN   F 2  291 ? 3.511   60.285  -45.592  1.00 57.75  ? 293 GLN   B CG    1 
ATOM   16247 C  CD    . GLN   F 2  291 ? 3.193   59.498  -46.873  1.00 73.23  ? 293 GLN   B CD    1 
ATOM   16248 O  OE1   . GLN   F 2  291 ? 2.030   59.423  -47.318  1.00 66.25  ? 293 GLN   B OE1   1 
ATOM   16249 N  NE2   . GLN   F 2  291 ? 4.233   58.911  -47.473  1.00 65.85  ? 293 GLN   B NE2   1 
ATOM   16250 N  N     . GLN   F 2  292 ? 1.092   59.785  -41.775  1.00 31.91  ? 294 GLN   B N     1 
ATOM   16251 C  CA    . GLN   F 2  292 ? 0.989   59.208  -40.450  1.00 36.01  ? 294 GLN   B CA    1 
ATOM   16252 C  C     . GLN   F 2  292 ? -0.461  58.939  -40.094  1.00 38.54  ? 294 GLN   B C     1 
ATOM   16253 O  O     . GLN   F 2  292 ? -0.794  57.859  -39.598  1.00 38.34  ? 294 GLN   B O     1 
ATOM   16254 C  CB    . GLN   F 2  292 ? 1.645   60.145  -39.433  1.00 39.48  ? 294 GLN   B CB    1 
ATOM   16255 C  CG    . GLN   F 2  292 ? 2.681   59.497  -38.544  1.00 41.87  ? 294 GLN   B CG    1 
ATOM   16256 C  CD    . GLN   F 2  292 ? 3.646   60.501  -37.969  1.00 44.08  ? 294 GLN   B CD    1 
ATOM   16257 O  OE1   . GLN   F 2  292 ? 3.516   60.905  -36.808  1.00 49.26  ? 294 GLN   B OE1   1 
ATOM   16258 N  NE2   . GLN   F 2  292 ? 4.620   60.927  -38.780  1.00 34.41  ? 294 GLN   B NE2   1 
ATOM   16259 N  N     . MET   F 2  293 ? -1.340  59.905  -40.356  1.00 37.96  ? 295 MET   B N     1 
ATOM   16260 C  CA    . MET   F 2  293 ? -2.721  59.757  -39.929  1.00 33.59  ? 295 MET   B CA    1 
ATOM   16261 C  C     . MET   F 2  293 ? -3.461  58.687  -40.713  1.00 33.91  ? 295 MET   B C     1 
ATOM   16262 O  O     . MET   F 2  293 ? -4.561  58.294  -40.305  1.00 36.80  ? 295 MET   B O     1 
ATOM   16263 C  CB    . MET   F 2  293 ? -3.453  61.087  -40.048  1.00 31.82  ? 295 MET   B CB    1 
ATOM   16264 C  CG    . MET   F 2  293 ? -3.751  61.475  -41.479  1.00 40.88  ? 295 MET   B CG    1 
ATOM   16265 S  SD    . MET   F 2  293 ? -4.681  63.012  -41.569  1.00 52.02  ? 295 MET   B SD    1 
ATOM   16266 C  CE    . MET   F 2  293 ? -5.847  62.559  -42.874  1.00 52.86  ? 295 MET   B CE    1 
ATOM   16267 N  N     . PHE   F 2  294 ? -2.903  58.221  -41.826  1.00 30.96  ? 296 PHE   B N     1 
ATOM   16268 C  CA    . PHE   F 2  294 ? -3.430  57.072  -42.549  1.00 27.85  ? 296 PHE   B CA    1 
ATOM   16269 C  C     . PHE   F 2  294 ? -2.648  55.823  -42.237  1.00 27.91  ? 296 PHE   B C     1 
ATOM   16270 O  O     . PHE   F 2  294 ? -2.989  54.749  -42.738  1.00 32.33  ? 296 PHE   B O     1 
ATOM   16271 C  CB    . PHE   F 2  294 ? -3.391  57.289  -44.063  1.00 33.69  ? 296 PHE   B CB    1 
ATOM   16272 C  CG    . PHE   F 2  294 ? -4.456  58.196  -44.605  1.00 30.19  ? 296 PHE   B CG    1 
ATOM   16273 C  CD1   . PHE   F 2  294 ? -4.276  59.557  -44.633  1.00 28.87  ? 296 PHE   B CD1   1 
ATOM   16274 C  CD2   . PHE   F 2  294 ? -5.602  57.667  -45.177  1.00 35.00  ? 296 PHE   B CD2   1 
ATOM   16275 C  CE1   . PHE   F 2  294 ? -5.243  60.383  -45.167  1.00 35.96  ? 296 PHE   B CE1   1 
ATOM   16276 C  CE2   . PHE   F 2  294 ? -6.583  58.487  -45.711  1.00 28.82  ? 296 PHE   B CE2   1 
ATOM   16277 C  CZ    . PHE   F 2  294 ? -6.402  59.849  -45.711  1.00 31.43  ? 296 PHE   B CZ    1 
ATOM   16278 N  N     . ASP   F 2  295 ? -1.584  55.946  -41.454  1.00 31.40  ? 297 ASP   B N     1 
ATOM   16279 C  CA    . ASP   F 2  295 ? -0.800  54.786  -41.049  1.00 34.51  ? 297 ASP   B CA    1 
ATOM   16280 C  C     . ASP   F 2  295 ? -1.626  53.888  -40.134  1.00 31.84  ? 297 ASP   B C     1 
ATOM   16281 O  O     . ASP   F 2  295 ? -2.379  54.364  -39.278  1.00 30.05  ? 297 ASP   B O     1 
ATOM   16282 C  CB    . ASP   F 2  295 ? 0.478   55.255  -40.331  1.00 41.85  ? 297 ASP   B CB    1 
ATOM   16283 C  CG    . ASP   F 2  295 ? 1.529   54.156  -40.177  1.00 32.93  ? 297 ASP   B CG    1 
ATOM   16284 O  OD1   . ASP   F 2  295 ? 1.205   52.951  -40.153  1.00 41.73  ? 297 ASP   B OD1   1 
ATOM   16285 O  OD2   . ASP   F 2  295 ? 2.704   54.518  -40.067  1.00 43.57  ? 297 ASP   B OD2   1 
ATOM   16286 N  N     . SER   F 2  296 ? -1.476  52.579  -40.300  1.00 34.08  ? 298 SER   B N     1 
ATOM   16287 C  CA    . SER   F 2  296 ? -2.209  51.688  -39.414  1.00 33.21  ? 298 SER   B CA    1 
ATOM   16288 C  C     . SER   F 2  296 ? -1.717  51.798  -37.973  1.00 35.66  ? 298 SER   B C     1 
ATOM   16289 O  O     . SER   F 2  296 ? -2.497  51.593  -37.042  1.00 37.33  ? 298 SER   B O     1 
ATOM   16290 C  CB    . SER   F 2  296 ? -2.107  50.253  -39.905  1.00 34.03  ? 298 SER   B CB    1 
ATOM   16291 O  OG    . SER   F 2  296 ? -0.914  49.659  -39.421  1.00 59.94  ? 298 SER   B OG    1 
ATOM   16292 N  N     . LYS   F 2  297 ? -0.438  52.123  -37.764  1.00 43.43  ? 299 LYS   B N     1 
ATOM   16293 C  CA    . LYS   F 2  297 ? 0.088   52.326  -36.410  1.00 43.46  ? 299 LYS   B CA    1 
ATOM   16294 C  C     . LYS   F 2  297 ? -0.597  53.459  -35.664  1.00 30.90  ? 299 LYS   B C     1 
ATOM   16295 O  O     . LYS   F 2  297 ? -0.398  53.584  -34.454  1.00 36.19  ? 299 LYS   B O     1 
ATOM   16296 C  CB    . LYS   F 2  297 ? 1.598   52.627  -36.452  1.00 46.59  ? 299 LYS   B CB    1 
ATOM   16297 C  CG    . LYS   F 2  297 ? 2.454   51.455  -36.856  1.00 47.44  ? 299 LYS   B CG    1 
ATOM   16298 C  CD    . LYS   F 2  297 ? 3.834   51.892  -37.311  1.00 58.86  ? 299 LYS   B CD    1 
ATOM   16299 C  CE    . LYS   F 2  297 ? 4.501   50.730  -38.031  1.00 71.91  ? 299 LYS   B CE    1 
ATOM   16300 N  NZ    . LYS   F 2  297 ? 3.996   49.424  -37.484  1.00 64.46  ? 299 LYS   B NZ    1 
ATOM   16301 N  N     . ASN   F 2  298 ? -1.352  54.307  -36.352  1.00 34.15  ? 300 ASN   B N     1 
ATOM   16302 C  CA    . ASN   F 2  298 ? -1.977  55.474  -35.747  1.00 33.59  ? 300 ASN   B CA    1 
ATOM   16303 C  C     . ASN   F 2  298 ? -3.474  55.308  -35.531  1.00 32.20  ? 300 ASN   B C     1 
ATOM   16304 O  O     . ASN   F 2  298 ? -4.119  56.236  -35.031  1.00 33.83  ? 300 ASN   B O     1 
ATOM   16305 C  CB    . ASN   F 2  298 ? -1.732  56.719  -36.614  1.00 30.94  ? 300 ASN   B CB    1 
ATOM   16306 C  CG    . ASN   F 2  298 ? -0.294  57.186  -36.575  1.00 34.59  ? 300 ASN   B CG    1 
ATOM   16307 O  OD1   . ASN   F 2  298 ? 0.612   56.496  -37.049  1.00 35.50  ? 300 ASN   B OD1   1 
ATOM   16308 N  ND2   . ASN   F 2  298 ? -0.079  58.376  -36.039  1.00 35.10  ? 300 ASN   B ND2   1 
ATOM   16309 N  N     . MET   F 2  299 ? -4.052  54.184  -35.935  1.00 28.47  ? 301 MET   B N     1 
ATOM   16310 C  CA    . MET   F 2  299 ? -5.481  53.979  -35.765  1.00 29.58  ? 301 MET   B CA    1 
ATOM   16311 C  C     . MET   F 2  299 ? -5.813  53.699  -34.297  1.00 29.02  ? 301 MET   B C     1 
ATOM   16312 O  O     . MET   F 2  299 ? -5.038  53.085  -33.571  1.00 35.29  ? 301 MET   B O     1 
ATOM   16313 C  CB    . MET   F 2  299 ? -5.950  52.820  -36.648  1.00 30.64  ? 301 MET   B CB    1 
ATOM   16314 C  CG    . MET   F 2  299 ? -5.679  53.008  -38.145  1.00 27.74  ? 301 MET   B CG    1 
ATOM   16315 S  SD    . MET   F 2  299 ? -6.573  54.423  -38.844  1.00 35.21  ? 301 MET   B SD    1 
ATOM   16316 C  CE    . MET   F 2  299 ? -5.525  54.744  -40.271  1.00 37.25  ? 301 MET   B CE    1 
ATOM   16317 N  N     . MET   F 2  300 ? -6.968  54.179  -33.853  1.00 27.05  ? 302 MET   B N     1 
ATOM   16318 C  CA    . MET   F 2  300 ? -7.453  53.856  -32.521  1.00 24.74  ? 302 MET   B CA    1 
ATOM   16319 C  C     . MET   F 2  300 ? -8.343  52.607  -32.536  1.00 29.33  ? 302 MET   B C     1 
ATOM   16320 O  O     . MET   F 2  300 ? -8.929  52.245  -31.509  1.00 28.00  ? 302 MET   B O     1 
ATOM   16321 C  CB    . MET   F 2  300 ? -8.186  55.071  -31.915  1.00 25.14  ? 302 MET   B CB    1 
ATOM   16322 C  CG    . MET   F 2  300 ? -7.406  56.394  -31.962  1.00 24.39  ? 302 MET   B CG    1 
ATOM   16323 S  SD    . MET   F 2  300 ? -5.978  56.363  -30.857  1.00 32.31  ? 302 MET   B SD    1 
ATOM   16324 C  CE    . MET   F 2  300 ? -4.903  57.573  -31.606  1.00 29.27  ? 302 MET   B CE    1 
ATOM   16325 N  N     . ALA   F 2  301 ? -8.437  51.937  -33.679  1.00 26.90  ? 303 ALA   B N     1 
ATOM   16326 C  CA    . ALA   F 2  301 ? -9.097  50.651  -33.794  1.00 25.98  ? 303 ALA   B CA    1 
ATOM   16327 C  C     . ALA   F 2  301 ? -8.093  49.649  -34.339  1.00 28.31  ? 303 ALA   B C     1 
ATOM   16328 O  O     . ALA   F 2  301 ? -7.481  49.892  -35.381  1.00 28.48  ? 303 ALA   B O     1 
ATOM   16329 C  CB    . ALA   F 2  301 ? -10.323 50.742  -34.714  1.00 27.68  ? 303 ALA   B CB    1 
ATOM   16330 N  N     . ALA   F 2  302 ? -7.931  48.517  -33.653  1.00 29.53  ? 304 ALA   B N     1 
ATOM   16331 C  CA    . ALA   F 2  302 ? -6.953  47.532  -34.098  1.00 24.08  ? 304 ALA   B CA    1 
ATOM   16332 C  C     . ALA   F 2  302 ? -7.423  46.802  -35.351  1.00 30.08  ? 304 ALA   B C     1 
ATOM   16333 O  O     . ALA   F 2  302 ? -7.781  45.620  -35.284  1.00 32.57  ? 304 ALA   B O     1 
ATOM   16334 C  CB    . ALA   F 2  302 ? -6.643  46.534  -32.990  1.00 19.30  ? 304 ALA   B CB    1 
ATOM   16335 N  N     . CYS   F 2  303 ? -7.403  47.498  -36.493  1.00 20.55  ? 305 CYS   B N     1 
ATOM   16336 C  CA    . CYS   F 2  303 ? -7.720  46.934  -37.800  1.00 27.40  ? 305 CYS   B CA    1 
ATOM   16337 C  C     . CYS   F 2  303 ? -6.687  47.367  -38.832  1.00 32.14  ? 305 CYS   B C     1 
ATOM   16338 O  O     . CYS   F 2  303 ? -6.157  48.482  -38.783  1.00 38.33  ? 305 CYS   B O     1 
ATOM   16339 C  CB    . CYS   F 2  303 ? -9.098  47.385  -38.274  1.00 33.14  ? 305 CYS   B CB    1 
ATOM   16340 S  SG    . CYS   F 2  303 ? -10.332 47.235  -36.969  1.00 37.12  ? 305 CYS   B SG    1 
ATOM   16341 N  N     . ASP   F 2  304 ? -6.422  46.487  -39.786  1.00 33.37  ? 306 ASP   B N     1 
ATOM   16342 C  CA    . ASP   F 2  304 ? -5.485  46.784  -40.862  1.00 38.14  ? 306 ASP   B CA    1 
ATOM   16343 C  C     . ASP   F 2  304 ? -6.256  47.465  -41.986  1.00 35.08  ? 306 ASP   B C     1 
ATOM   16344 O  O     . ASP   F 2  304 ? -7.006  46.785  -42.697  1.00 41.38  ? 306 ASP   B O     1 
ATOM   16345 C  CB    . ASP   F 2  304 ? -4.835  45.497  -41.363  1.00 40.66  ? 306 ASP   B CB    1 
ATOM   16346 C  CG    . ASP   F 2  304 ? -3.557  45.738  -42.158  1.00 50.76  ? 306 ASP   B CG    1 
ATOM   16347 O  OD1   . ASP   F 2  304 ? -3.354  46.892  -42.628  1.00 50.04  ? 306 ASP   B OD1   1 
ATOM   16348 O  OD2   . ASP   F 2  304 ? -2.762  44.761  -42.300  1.00 34.55  ? 306 ASP   B OD2   1 
ATOM   16349 N  N     . PRO   F 2  305 ? -6.121  48.776  -42.188  1.00 27.08  ? 307 PRO   B N     1 
ATOM   16350 C  CA    . PRO   F 2  305 ? -6.898  49.416  -43.261  1.00 33.67  ? 307 PRO   B CA    1 
ATOM   16351 C  C     . PRO   F 2  305 ? -6.633  48.817  -44.636  1.00 33.09  ? 307 PRO   B C     1 
ATOM   16352 O  O     . PRO   F 2  305 ? -7.538  48.796  -45.479  1.00 35.43  ? 307 PRO   B O     1 
ATOM   16353 C  CB    . PRO   F 2  305 ? -6.463  50.893  -43.189  1.00 34.60  ? 307 PRO   B CB    1 
ATOM   16354 C  CG    . PRO   F 2  305 ? -5.765  51.044  -41.884  1.00 28.77  ? 307 PRO   B CG    1 
ATOM   16355 C  CD    . PRO   F 2  305 ? -5.152  49.704  -41.591  1.00 31.11  ? 307 PRO   B CD    1 
ATOM   16356 N  N     . ARG   F 2  306 ? -5.424  48.316  -44.890  1.00 36.92  ? 308 ARG   B N     1 
ATOM   16357 C  CA    . ARG   F 2  306 ? -5.150  47.663  -46.168  1.00 39.21  ? 308 ARG   B CA    1 
ATOM   16358 C  C     . ARG   F 2  306 ? -5.885  46.341  -46.320  1.00 36.16  ? 308 ARG   B C     1 
ATOM   16359 O  O     . ARG   F 2  306 ? -5.835  45.753  -47.399  1.00 39.37  ? 308 ARG   B O     1 
ATOM   16360 C  CB    . ARG   F 2  306 ? -3.641  47.438  -46.355  1.00 42.37  ? 308 ARG   B CB    1 
ATOM   16361 C  CG    . ARG   F 2  306 ? -2.882  48.615  -46.988  1.00 50.41  ? 308 ARG   B CG    1 
ATOM   16362 C  CD    . ARG   F 2  306 ? -1.374  48.570  -46.690  1.00 53.87  ? 308 ARG   B CD    1 
ATOM   16363 N  NE    . ARG   F 2  306 ? -0.654  47.613  -47.524  1.00 74.68  ? 308 ARG   B NE    1 
ATOM   16364 C  CZ    . ARG   F 2  306 ? 0.568   47.156  -47.263  1.00 91.74  ? 308 ARG   B CZ    1 
ATOM   16365 N  NH1   . ARG   F 2  306 ? 1.237   47.531  -46.178  1.00 81.79  ? 308 ARG   B NH1   1 
ATOM   16366 N  NH2   . ARG   F 2  306 ? 1.133   46.290  -48.105  1.00 69.04  ? 308 ARG   B NH2   1 
ATOM   16367 N  N     . HIS   F 2  307 ? -6.553  45.850  -45.280  1.00 38.80  ? 309 HIS   B N     1 
ATOM   16368 C  CA    . HIS   F 2  307 ? -7.371  44.654  -45.419  1.00 39.45  ? 309 HIS   B CA    1 
ATOM   16369 C  C     . HIS   F 2  307 ? -8.794  44.960  -45.850  1.00 40.09  ? 309 HIS   B C     1 
ATOM   16370 O  O     . HIS   F 2  307 ? -9.548  44.026  -46.134  1.00 49.20  ? 309 HIS   B O     1 
ATOM   16371 C  CB    . HIS   F 2  307 ? -7.406  43.857  -44.114  1.00 40.54  ? 309 HIS   B CB    1 
ATOM   16372 C  CG    . HIS   F 2  307 ? -6.095  43.224  -43.759  1.00 48.70  ? 309 HIS   B CG    1 
ATOM   16373 N  ND1   . HIS   F 2  307 ? -5.708  42.993  -42.456  1.00 49.83  ? 309 HIS   B ND1   1 
ATOM   16374 C  CD2   . HIS   F 2  307 ? -5.085  42.768  -44.537  1.00 45.33  ? 309 HIS   B CD2   1 
ATOM   16375 C  CE1   . HIS   F 2  307 ? -4.512  42.429  -42.446  1.00 52.10  ? 309 HIS   B CE1   1 
ATOM   16376 N  NE2   . HIS   F 2  307 ? -4.111  42.281  -43.695  1.00 42.32  ? 309 HIS   B NE2   1 
ATOM   16377 N  N     . GLY   F 2  308 ? -9.180  46.231  -45.902  1.00 33.61  ? 310 GLY   B N     1 
ATOM   16378 C  CA    . GLY   F 2  308 ? -10.486 46.599  -46.416  1.00 30.83  ? 310 GLY   B CA    1 
ATOM   16379 C  C     . GLY   F 2  308 ? -10.426 47.771  -47.381  1.00 37.90  ? 310 GLY   B C     1 
ATOM   16380 O  O     . GLY   F 2  308 ? -9.379  48.021  -48.005  1.00 33.65  ? 310 GLY   B O     1 
ATOM   16381 N  N     . ARG   F 2  309 ? -11.551 48.492  -47.518  1.00 34.18  ? 311 ARG   B N     1 
ATOM   16382 C  CA    . ARG   F 2  309 ? -11.636 49.696  -48.339  1.00 24.38  ? 311 ARG   B CA    1 
ATOM   16383 C  C     . ARG   F 2  309 ? -12.365 50.785  -47.566  1.00 32.40  ? 311 ARG   B C     1 
ATOM   16384 O  O     . ARG   F 2  309 ? -13.286 50.513  -46.788  1.00 30.90  ? 311 ARG   B O     1 
ATOM   16385 C  CB    . ARG   F 2  309 ? -12.346 49.430  -49.663  1.00 32.33  ? 311 ARG   B CB    1 
ATOM   16386 C  CG    . ARG   F 2  309 ? -12.137 48.010  -50.175  1.00 38.72  ? 311 ARG   B CG    1 
ATOM   16387 C  CD    . ARG   F 2  309 ? -11.554 47.967  -51.558  1.00 33.02  ? 311 ARG   B CD    1 
ATOM   16388 N  NE    . ARG   F 2  309 ? -12.597 48.002  -52.569  1.00 41.83  ? 311 ARG   B NE    1 
ATOM   16389 C  CZ    . ARG   F 2  309 ? -12.661 48.900  -53.544  1.00 50.14  ? 311 ARG   B CZ    1 
ATOM   16390 N  NH1   . ARG   F 2  309 ? -11.709 49.810  -53.707  1.00 37.83  ? 311 ARG   B NH1   1 
ATOM   16391 N  NH2   . ARG   F 2  309 ? -13.706 48.882  -54.380  1.00 41.43  ? 311 ARG   B NH2   1 
ATOM   16392 N  N     . TYR   F 2  310 ? -11.908 52.014  -47.745  1.00 32.82  ? 312 TYR   B N     1 
ATOM   16393 C  CA    . TYR   F 2  310 ? -12.584 53.148  -47.150  1.00 29.77  ? 312 TYR   B CA    1 
ATOM   16394 C  C     . TYR   F 2  310 ? -13.881 53.426  -47.888  1.00 35.00  ? 312 TYR   B C     1 
ATOM   16395 O  O     . TYR   F 2  310 ? -13.884 53.594  -49.117  1.00 33.70  ? 312 TYR   B O     1 
ATOM   16396 C  CB    . TYR   F 2  310 ? -11.678 54.369  -47.195  1.00 28.91  ? 312 TYR   B CB    1 
ATOM   16397 C  CG    . TYR   F 2  310 ? -10.538 54.237  -46.238  1.00 32.12  ? 312 TYR   B CG    1 
ATOM   16398 C  CD1   . TYR   F 2  310 ? -10.777 54.056  -44.882  1.00 26.76  ? 312 TYR   B CD1   1 
ATOM   16399 C  CD2   . TYR   F 2  310 ? -9.231  54.295  -46.677  1.00 29.16  ? 312 TYR   B CD2   1 
ATOM   16400 C  CE1   . TYR   F 2  310 ? -9.736  53.919  -43.999  1.00 36.56  ? 312 TYR   B CE1   1 
ATOM   16401 C  CE2   . TYR   F 2  310 ? -8.181  54.170  -45.801  1.00 20.29  ? 312 TYR   B CE2   1 
ATOM   16402 C  CZ    . TYR   F 2  310 ? -8.429  53.981  -44.461  1.00 30.83  ? 312 TYR   B CZ    1 
ATOM   16403 O  OH    . TYR   F 2  310 ? -7.375  53.845  -43.569  1.00 40.82  ? 312 TYR   B OH    1 
ATOM   16404 N  N     . LEU   F 2  311 ? -14.985 53.456  -47.133  1.00 28.37  ? 313 LEU   B N     1 
ATOM   16405 C  CA    . LEU   F 2  311 ? -16.254 53.919  -47.676  1.00 28.80  ? 313 LEU   B CA    1 
ATOM   16406 C  C     . LEU   F 2  311 ? -16.288 55.441  -47.729  1.00 29.01  ? 313 LEU   B C     1 
ATOM   16407 O  O     . LEU   F 2  311 ? -16.565 56.024  -48.782  1.00 32.88  ? 313 LEU   B O     1 
ATOM   16408 C  CB    . LEU   F 2  311 ? -17.415 53.383  -46.841  1.00 26.55  ? 313 LEU   B CB    1 
ATOM   16409 C  CG    . LEU   F 2  311 ? -17.589 51.871  -46.781  1.00 39.60  ? 313 LEU   B CG    1 
ATOM   16410 C  CD1   . LEU   F 2  311 ? -18.708 51.545  -45.791  1.00 40.30  ? 313 LEU   B CD1   1 
ATOM   16411 C  CD2   . LEU   F 2  311 ? -17.891 51.274  -48.173  1.00 27.56  ? 313 LEU   B CD2   1 
ATOM   16412 N  N     . THR   F 2  312 ? -16.001 56.096  -46.606  1.00 22.87  ? 314 THR   B N     1 
ATOM   16413 C  CA    . THR   F 2  312 ? -15.874 57.546  -46.528  1.00 20.82  ? 314 THR   B CA    1 
ATOM   16414 C  C     . THR   F 2  312 ? -14.782 57.877  -45.523  1.00 21.40  ? 314 THR   B C     1 
ATOM   16415 O  O     . THR   F 2  312 ? -14.335 57.023  -44.752  1.00 25.17  ? 314 THR   B O     1 
ATOM   16416 C  CB    . THR   F 2  312 ? -17.179 58.216  -46.105  1.00 27.93  ? 314 THR   B CB    1 
ATOM   16417 O  OG1   . THR   F 2  312 ? -17.447 57.900  -44.725  1.00 31.88  ? 314 THR   B OG1   1 
ATOM   16418 C  CG2   . THR   F 2  312 ? -18.347 57.760  -47.000  1.00 18.11  ? 314 THR   B CG2   1 
ATOM   16419 N  N     . VAL   F 2  313 ? -14.345 59.130  -45.540  1.00 22.28  ? 315 VAL   B N     1 
ATOM   16420 C  CA    . VAL   F 2  313 ? -13.211 59.577  -44.739  1.00 18.49  ? 315 VAL   B CA    1 
ATOM   16421 C  C     . VAL   F 2  313 ? -13.364 61.075  -44.521  1.00 23.62  ? 315 VAL   B C     1 
ATOM   16422 O  O     . VAL   F 2  313 ? -13.611 61.818  -45.475  1.00 24.72  ? 315 VAL   B O     1 
ATOM   16423 C  CB    . VAL   F 2  313 ? -11.851 59.261  -45.412  1.00 22.82  ? 315 VAL   B CB    1 
ATOM   16424 C  CG1   . VAL   F 2  313 ? -10.697 59.892  -44.644  1.00 20.24  ? 315 VAL   B CG1   1 
ATOM   16425 C  CG2   . VAL   F 2  313 ? -11.610 57.774  -45.555  1.00 26.10  ? 315 VAL   B CG2   1 
ATOM   16426 N  N     . ALA   F 2  314 ? -13.215 61.523  -43.270  1.00 24.82  ? 316 ALA   B N     1 
ATOM   16427 C  CA    . ALA   F 2  314 ? -13.011 62.925  -42.924  1.00 27.83  ? 316 ALA   B CA    1 
ATOM   16428 C  C     . ALA   F 2  314 ? -11.576 63.089  -42.444  1.00 31.07  ? 316 ALA   B C     1 
ATOM   16429 O  O     . ALA   F 2  314 ? -11.035 62.202  -41.773  1.00 34.70  ? 316 ALA   B O     1 
ATOM   16430 C  CB    . ALA   F 2  314 ? -13.991 63.402  -41.825  1.00 15.88  ? 316 ALA   B CB    1 
ATOM   16431 N  N     . ALA   F 2  315 ? -10.960 64.221  -42.773  1.00 29.17  ? 317 ALA   B N     1 
ATOM   16432 C  CA    . ALA   F 2  315 ? -9.606  64.518  -42.326  1.00 25.04  ? 317 ALA   B CA    1 
ATOM   16433 C  C     . ALA   F 2  315 ? -9.585  65.936  -41.785  1.00 32.27  ? 317 ALA   B C     1 
ATOM   16434 O  O     . ALA   F 2  315 ? -10.076 66.860  -42.441  1.00 36.36  ? 317 ALA   B O     1 
ATOM   16435 C  CB    . ALA   F 2  315 ? -8.576  64.347  -43.454  1.00 28.86  ? 317 ALA   B CB    1 
ATOM   16436 N  N     . ILE   F 2  316 ? -9.040  66.102  -40.581  1.00 30.57  ? 318 ILE   B N     1 
ATOM   16437 C  CA    . ILE   F 2  316 ? -9.033  67.381  -39.890  1.00 32.83  ? 318 ILE   B CA    1 
ATOM   16438 C  C     . ILE   F 2  316 ? -7.588  67.705  -39.545  1.00 31.55  ? 318 ILE   B C     1 
ATOM   16439 O  O     . ILE   F 2  316 ? -6.914  66.909  -38.881  1.00 33.30  ? 318 ILE   B O     1 
ATOM   16440 C  CB    . ILE   F 2  316 ? -9.917  67.360  -38.632  1.00 32.87  ? 318 ILE   B CB    1 
ATOM   16441 C  CG1   . ILE   F 2  316 ? -11.172 66.495  -38.845  1.00 31.20  ? 318 ILE   B CG1   1 
ATOM   16442 C  CG2   . ILE   F 2  316 ? -10.335 68.777  -38.274  1.00 34.50  ? 318 ILE   B CG2   1 
ATOM   16443 C  CD1   . ILE   F 2  316 ? -10.950 65.013  -38.622  0.00 30.01  ? 318 ILE   B CD1   1 
ATOM   16444 N  N     . PHE   F 2  317 ? -7.103  68.843  -40.036  1.00 31.27  ? 319 PHE   B N     1 
ATOM   16445 C  CA    . PHE   F 2  317 ? -5.769  69.357  -39.751  1.00 32.61  ? 319 PHE   B CA    1 
ATOM   16446 C  C     . PHE   F 2  317 ? -5.895  70.528  -38.787  1.00 38.73  ? 319 PHE   B C     1 
ATOM   16447 O  O     . PHE   F 2  317 ? -6.823  71.338  -38.897  1.00 43.49  ? 319 PHE   B O     1 
ATOM   16448 C  CB    . PHE   F 2  317 ? -5.035  69.822  -41.030  1.00 26.16  ? 319 PHE   B CB    1 
ATOM   16449 C  CG    . PHE   F 2  317 ? -4.687  68.706  -41.974  1.00 29.86  ? 319 PHE   B CG    1 
ATOM   16450 C  CD1   . PHE   F 2  317 ? -5.663  68.109  -42.764  1.00 33.49  ? 319 PHE   B CD1   1 
ATOM   16451 C  CD2   . PHE   F 2  317 ? -3.391  68.240  -42.069  1.00 26.90  ? 319 PHE   B CD2   1 
ATOM   16452 C  CE1   . PHE   F 2  317 ? -5.344  67.054  -43.619  1.00 33.17  ? 319 PHE   B CE1   1 
ATOM   16453 C  CE2   . PHE   F 2  317 ? -3.073  67.203  -42.921  1.00 25.66  ? 319 PHE   B CE2   1 
ATOM   16454 C  CZ    . PHE   F 2  317 ? -4.046  66.609  -43.692  1.00 28.01  ? 319 PHE   B CZ    1 
ATOM   16455 N  N     . ARG   F 2  318 ? -4.964  70.622  -37.842  1.00 35.22  ? 320 ARG   B N     1 
ATOM   16456 C  CA    . ARG   F 2  318 ? -4.968  71.732  -36.906  1.00 40.57  ? 320 ARG   B CA    1 
ATOM   16457 C  C     . ARG   F 2  318 ? -3.574  72.338  -36.831  1.00 36.69  ? 320 ARG   B C     1 
ATOM   16458 O  O     . ARG   F 2  318 ? -2.566  71.638  -36.964  1.00 37.19  ? 320 ARG   B O     1 
ATOM   16459 C  CB    . ARG   F 2  318 ? -5.459  71.273  -35.525  1.00 39.82  ? 320 ARG   B CB    1 
ATOM   16460 C  CG    . ARG   F 2  318 ? -6.648  70.332  -35.595  1.00 41.18  ? 320 ARG   B CG    1 
ATOM   16461 C  CD    . ARG   F 2  318 ? -7.222  70.103  -34.235  1.00 43.04  ? 320 ARG   B CD    1 
ATOM   16462 N  NE    . ARG   F 2  318 ? -7.457  71.371  -33.560  1.00 44.74  ? 320 ARG   B NE    1 
ATOM   16463 C  CZ    . ARG   F 2  318 ? -7.722  71.487  -32.266  1.00 51.49  ? 320 ARG   B CZ    1 
ATOM   16464 N  NH1   . ARG   F 2  318 ? -7.853  70.423  -31.490  1.00 49.99  ? 320 ARG   B NH1   1 
ATOM   16465 N  NH2   . ARG   F 2  318 ? -7.840  72.701  -31.732  1.00 46.72  ? 320 ARG   B NH2   1 
ATOM   16466 N  N     . GLY   F 2  319 ? -3.531  73.642  -36.605  1.00 33.20  ? 321 GLY   B N     1 
ATOM   16467 C  CA    . GLY   F 2  319 ? -2.303  74.407  -36.642  1.00 43.59  ? 321 GLY   B CA    1 
ATOM   16468 C  C     . GLY   F 2  319 ? -2.260  75.361  -37.830  1.00 50.76  ? 321 GLY   B C     1 
ATOM   16469 O  O     . GLY   F 2  319 ? -3.114  75.357  -38.718  1.00 46.90  ? 321 GLY   B O     1 
ATOM   16470 N  N     . ARG   F 2  320 ? -1.242  76.209  -37.820  1.00 53.16  ? 322 ARG   B N     1 
ATOM   16471 C  CA    . ARG   F 2  320 ? -1.008  77.102  -38.946  1.00 51.64  ? 322 ARG   B CA    1 
ATOM   16472 C  C     . ARG   F 2  320 ? -0.206  76.352  -40.003  1.00 38.45  ? 322 ARG   B C     1 
ATOM   16473 O  O     . ARG   F 2  320 ? 0.914   75.914  -39.733  1.00 45.98  ? 322 ARG   B O     1 
ATOM   16474 C  CB    . ARG   F 2  320 ? -0.289  78.366  -38.475  1.00 55.71  ? 322 ARG   B CB    1 
ATOM   16475 C  CG    . ARG   F 2  320 ? -0.615  79.613  -39.303  1.00 75.16  ? 322 ARG   B CG    1 
ATOM   16476 C  CD    . ARG   F 2  320 ? -0.345  80.919  -38.542  1.00 79.71  ? 322 ARG   B CD    1 
ATOM   16477 N  NE    . ARG   F 2  320 ? -1.341  81.167  -37.504  1.00 79.08  ? 322 ARG   B NE    1 
ATOM   16478 C  CZ    . ARG   F 2  320 ? -2.572  81.606  -37.736  1.00 81.58  ? 322 ARG   B CZ    1 
ATOM   16479 N  NH1   . ARG   F 2  320 ? -3.012  81.828  -38.967  1.00 70.43  ? 322 ARG   B NH1   1 
ATOM   16480 N  NH2   . ARG   F 2  320 ? -3.385  81.831  -36.708  1.00 82.30  ? 322 ARG   B NH2   1 
ATOM   16481 N  N     . MET   F 2  321 ? -0.785  76.172  -41.190  1.00 40.58  ? 323 MET   B N     1 
ATOM   16482 C  CA    . MET   F 2  321 ? -0.119  75.450  -42.267  1.00 30.06  ? 323 MET   B CA    1 
ATOM   16483 C  C     . MET   F 2  321 ? -0.755  75.836  -43.603  1.00 33.29  ? 323 MET   B C     1 
ATOM   16484 O  O     . MET   F 2  321 ? -1.708  76.616  -43.663  1.00 29.88  ? 323 MET   B O     1 
ATOM   16485 C  CB    . MET   F 2  321 ? -0.181  73.941  -42.039  1.00 33.46  ? 323 MET   B CB    1 
ATOM   16486 C  CG    . MET   F 2  321 ? -1.473  73.286  -42.546  1.00 26.52  ? 323 MET   B CG    1 
ATOM   16487 S  SD    . MET   F 2  321 ? -1.880  71.777  -41.655  1.00 35.21  ? 323 MET   B SD    1 
ATOM   16488 C  CE    . MET   F 2  321 ? -2.589  72.484  -40.164  1.00 30.82  ? 323 MET   B CE    1 
ATOM   16489 N  N     . SER   F 2  322 ? -0.225  75.253  -44.679  1.00 32.34  ? 324 SER   B N     1 
ATOM   16490 C  CA    . SER   F 2  322 ? -0.565  75.637  -46.043  1.00 37.95  ? 324 SER   B CA    1 
ATOM   16491 C  C     . SER   F 2  322 ? -1.719  74.791  -46.567  1.00 40.37  ? 324 SER   B C     1 
ATOM   16492 O  O     . SER   F 2  322 ? -1.590  73.573  -46.724  1.00 42.32  ? 324 SER   B O     1 
ATOM   16493 C  CB    . SER   F 2  322 ? 0.655   75.488  -46.955  1.00 33.28  ? 324 SER   B CB    1 
ATOM   16494 O  OG    . SER   F 2  322 ? 0.316   75.632  -48.319  1.00 33.40  ? 324 SER   B OG    1 
ATOM   16495 N  N     . MET   F 2  323 ? -2.837  75.447  -46.859  1.00 43.21  ? 325 MET   B N     1 
ATOM   16496 C  CA    . MET   F 2  323 ? -3.949  74.779  -47.516  1.00 36.96  ? 325 MET   B CA    1 
ATOM   16497 C  C     . MET   F 2  323 ? -3.509  74.133  -48.824  1.00 48.79  ? 325 MET   B C     1 
ATOM   16498 O  O     . MET   F 2  323 ? -3.870  72.982  -49.115  1.00 46.71  ? 325 MET   B O     1 
ATOM   16499 C  CB    . MET   F 2  323 ? -5.061  75.789  -47.757  1.00 45.57  ? 325 MET   B CB    1 
ATOM   16500 C  CG    . MET   F 2  323 ? -5.762  76.213  -46.505  1.00 53.94  ? 325 MET   B CG    1 
ATOM   16501 S  SD    . MET   F 2  323 ? -7.141  75.089  -46.264  1.00 76.72  ? 325 MET   B SD    1 
ATOM   16502 C  CE    . MET   F 2  323 ? -8.146  75.509  -47.677  1.00 50.95  ? 325 MET   B CE    1 
ATOM   16503 N  N     . LYS   F 2  324 ? -2.743  74.865  -49.647  1.00 48.19  ? 326 LYS   B N     1 
ATOM   16504 C  CA    . LYS   F 2  324 ? -2.258  74.261  -50.886  1.00 43.57  ? 326 LYS   B CA    1 
ATOM   16505 C  C     . LYS   F 2  324 ? -1.547  72.945  -50.593  1.00 41.98  ? 326 LYS   B C     1 
ATOM   16506 O  O     . LYS   F 2  324 ? -1.775  71.936  -51.273  1.00 44.23  ? 326 LYS   B O     1 
ATOM   16507 C  CB    . LYS   F 2  324 ? -1.334  75.233  -51.639  1.00 46.86  ? 326 LYS   B CB    1 
ATOM   16508 C  CG    . LYS   F 2  324 ? -0.427  74.583  -52.724  1.00 41.02  ? 326 LYS   B CG    1 
ATOM   16509 C  CD    . LYS   F 2  324 ? -0.301  75.462  -53.978  1.00 55.17  ? 326 LYS   B CD    1 
ATOM   16510 C  CE    . LYS   F 2  324 ? 0.696   74.928  -55.036  1.00 45.43  ? 326 LYS   B CE    1 
ATOM   16511 N  NZ    . LYS   F 2  324 ? 2.095   75.468  -54.848  1.00 46.10  ? 326 LYS   B NZ    1 
ATOM   16512 N  N     . GLU   F 2  325 ? -0.708  72.931  -49.556  1.00 41.16  ? 327 GLU   B N     1 
ATOM   16513 C  CA    . GLU   F 2  325 ? 0.105   71.756  -49.274  1.00 42.01  ? 327 GLU   B CA    1 
ATOM   16514 C  C     . GLU   F 2  325 ? -0.753  70.637  -48.680  1.00 42.16  ? 327 GLU   B C     1 
ATOM   16515 O  O     . GLU   F 2  325 ? -0.651  69.476  -49.100  1.00 40.96  ? 327 GLU   B O     1 
ATOM   16516 C  CB    . GLU   F 2  325 ? 1.272   72.161  -48.358  1.00 31.60  ? 327 GLU   B CB    1 
ATOM   16517 C  CG    . GLU   F 2  325 ? 2.448   71.210  -48.343  1.00 41.94  ? 327 GLU   B CG    1 
ATOM   16518 C  CD    . GLU   F 2  325 ? 3.489   71.556  -47.268  1.00 52.16  ? 327 GLU   B CD    1 
ATOM   16519 O  OE1   . GLU   F 2  325 ? 3.578   72.736  -46.857  1.00 44.15  ? 327 GLU   B OE1   1 
ATOM   16520 O  OE2   . GLU   F 2  325 ? 4.223   70.638  -46.832  1.00 59.07  ? 327 GLU   B OE2   1 
ATOM   16521 N  N     . VAL   F 2  326 ? -1.634  70.972  -47.728  1.00 37.91  ? 328 VAL   B N     1 
ATOM   16522 C  CA    . VAL   F 2  326 ? -2.577  69.976  -47.217  1.00 39.20  ? 328 VAL   B CA    1 
ATOM   16523 C  C     . VAL   F 2  326 ? -3.350  69.361  -48.374  1.00 39.76  ? 328 VAL   B C     1 
ATOM   16524 O  O     . VAL   F 2  326 ? -3.517  68.137  -48.454  1.00 35.05  ? 328 VAL   B O     1 
ATOM   16525 C  CB    . VAL   F 2  326 ? -3.538  70.597  -46.181  1.00 37.10  ? 328 VAL   B CB    1 
ATOM   16526 C  CG1   . VAL   F 2  326 ? -4.715  69.628  -45.914  1.00 27.98  ? 328 VAL   B CG1   1 
ATOM   16527 C  CG2   . VAL   F 2  326 ? -2.827  70.930  -44.885  1.00 33.74  ? 328 VAL   B CG2   1 
ATOM   16528 N  N     . ASP   F 2  327 ? -3.849  70.209  -49.283  1.00 32.23  ? 329 ASP   B N     1 
ATOM   16529 C  CA    . ASP   F 2  327 ? -4.629  69.701  -50.406  1.00 33.90  ? 329 ASP   B CA    1 
ATOM   16530 C  C     . ASP   F 2  327 ? -3.783  68.792  -51.288  1.00 35.55  ? 329 ASP   B C     1 
ATOM   16531 O  O     . ASP   F 2  327 ? -4.209  67.683  -51.644  1.00 34.91  ? 329 ASP   B O     1 
ATOM   16532 C  CB    . ASP   F 2  327 ? -5.221  70.857  -51.217  1.00 30.23  ? 329 ASP   B CB    1 
ATOM   16533 C  CG    . ASP   F 2  327 ? -6.355  71.584  -50.490  1.00 38.41  ? 329 ASP   B CG    1 
ATOM   16534 O  OD1   . ASP   F 2  327 ? -6.994  70.998  -49.558  1.00 31.21  ? 329 ASP   B OD1   1 
ATOM   16535 O  OD2   . ASP   F 2  327 ? -6.611  72.756  -50.875  1.00 35.63  ? 329 ASP   B OD2   1 
ATOM   16536 N  N     . GLU   F 2  328 ? -2.565  69.233  -51.635  1.00 36.46  ? 330 GLU   B N     1 
ATOM   16537 C  CA    . GLU   F 2  328 ? -1.699  68.402  -52.472  1.00 44.71  ? 330 GLU   B CA    1 
ATOM   16538 C  C     . GLU   F 2  328 ? -1.457  67.038  -51.843  1.00 38.93  ? 330 GLU   B C     1 
ATOM   16539 O  O     . GLU   F 2  328 ? -1.505  66.014  -52.533  1.00 39.57  ? 330 GLU   B O     1 
ATOM   16540 C  CB    . GLU   F 2  328 ? -0.365  69.096  -52.725  1.00 44.05  ? 330 GLU   B CB    1 
ATOM   16541 C  CG    . GLU   F 2  328 ? -0.319  69.916  -53.981  1.00 42.56  ? 330 GLU   B CG    1 
ATOM   16542 C  CD    . GLU   F 2  328 ? 0.450   71.192  -53.786  1.00 51.35  ? 330 GLU   B CD    1 
ATOM   16543 O  OE1   . GLU   F 2  328 ? 1.455   71.159  -53.033  1.00 48.97  ? 330 GLU   B OE1   1 
ATOM   16544 O  OE2   . GLU   F 2  328 ? 0.044   72.222  -54.378  1.00 53.35  ? 330 GLU   B OE2   1 
ATOM   16545 N  N     . GLN   F 2  329 ? -1.186  67.008  -50.534  1.00 39.28  ? 331 GLN   B N     1 
ATOM   16546 C  CA    . GLN   F 2  329 ? -0.892  65.746  -49.867  1.00 36.97  ? 331 GLN   B CA    1 
ATOM   16547 C  C     . GLN   F 2  329 ? -2.129  64.851  -49.788  1.00 39.59  ? 331 GLN   B C     1 
ATOM   16548 O  O     . GLN   F 2  329 ? -2.035  63.632  -49.984  1.00 35.73  ? 331 GLN   B O     1 
ATOM   16549 C  CB    . GLN   F 2  329 ? -0.316  66.022  -48.473  1.00 34.54  ? 331 GLN   B CB    1 
ATOM   16550 C  CG    . GLN   F 2  329 ? 1.113   66.557  -48.481  1.00 34.96  ? 331 GLN   B CG    1 
ATOM   16551 C  CD    . GLN   F 2  329 ? 2.048   65.704  -49.334  1.00 39.50  ? 331 GLN   B CD    1 
ATOM   16552 O  OE1   . GLN   F 2  329 ? 2.137   64.488  -49.163  1.00 38.08  ? 331 GLN   B OE1   1 
ATOM   16553 N  NE2   . GLN   F 2  329 ? 2.729   66.338  -50.267  1.00 31.56  ? 331 GLN   B NE2   1 
ATOM   16554 N  N     . MET   F 2  330 ? -3.296  65.428  -49.482  1.00 35.63  ? 332 MET   B N     1 
ATOM   16555 C  CA    . MET   F 2  330 ? -4.506  64.611  -49.412  1.00 41.09  ? 332 MET   B CA    1 
ATOM   16556 C  C     . MET   F 2  330 ? -4.840  64.015  -50.777  1.00 37.95  ? 332 MET   B C     1 
ATOM   16557 O  O     . MET   F 2  330 ? -5.294  62.865  -50.870  1.00 37.13  ? 332 MET   B O     1 
ATOM   16558 C  CB    . MET   F 2  330 ? -5.684  65.427  -48.842  1.00 25.59  ? 332 MET   B CB    1 
ATOM   16559 C  CG    . MET   F 2  330 ? -5.539  65.739  -47.326  1.00 33.42  ? 332 MET   B CG    1 
ATOM   16560 S  SD    . MET   F 2  330 ? -5.426  64.250  -46.292  1.00 27.26  ? 332 MET   B SD    1 
ATOM   16561 C  CE    . MET   F 2  330 ? -6.926  63.405  -46.843  1.00 26.81  ? 332 MET   B CE    1 
ATOM   16562 N  N     . LEU   F 2  331 ? -4.604  64.770  -51.854  1.00 33.30  ? 333 LEU   B N     1 
ATOM   16563 C  CA    . LEU   F 2  331 ? -4.792  64.196  -53.184  1.00 33.07  ? 333 LEU   B CA    1 
ATOM   16564 C  C     . LEU   F 2  331 ? -3.765  63.103  -53.447  1.00 29.64  ? 333 LEU   B C     1 
ATOM   16565 O  O     . LEU   F 2  331 ? -4.105  62.011  -53.913  1.00 35.89  ? 333 LEU   B O     1 
ATOM   16566 C  CB    . LEU   F 2  331 ? -4.719  65.293  -54.250  1.00 31.85  ? 333 LEU   B CB    1 
ATOM   16567 C  CG    . LEU   F 2  331 ? -5.974  66.168  -54.302  1.00 32.74  ? 333 LEU   B CG    1 
ATOM   16568 C  CD1   . LEU   F 2  331 ? -5.772  67.408  -55.165  1.00 28.52  ? 333 LEU   B CD1   1 
ATOM   16569 C  CD2   . LEU   F 2  331 ? -7.159  65.337  -54.790  1.00 21.45  ? 333 LEU   B CD2   1 
ATOM   16570 N  N     . ASN   F 2  332 ? -2.502  63.367  -53.129  1.00 30.44  ? 334 ASN   B N     1 
ATOM   16571 C  CA    . ASN   F 2  332 ? -1.473  62.353  -53.314  1.00 31.50  ? 334 ASN   B CA    1 
ATOM   16572 C  C     . ASN   F 2  332 ? -1.886  61.038  -52.666  1.00 38.68  ? 334 ASN   B C     1 
ATOM   16573 O  O     . ASN   F 2  332 ? -1.879  59.982  -53.316  1.00 38.43  ? 334 ASN   B O     1 
ATOM   16574 C  CB    . ASN   F 2  332 ? -0.148  62.870  -52.752  1.00 33.43  ? 334 ASN   B CB    1 
ATOM   16575 C  CG    . ASN   F 2  332 ? 0.885   61.802  -52.644  0.00 41.94  ? 334 ASN   B CG    1 
ATOM   16576 O  OD1   . ASN   F 2  332 ? 1.340   61.267  -53.650  0.82 49.08  ? 334 ASN   B OD1   1 
ATOM   16577 N  ND2   . ASN   F 2  332 ? 1.277   61.486  -51.418  1.00 46.27  ? 334 ASN   B ND2   1 
ATOM   16578 N  N     . VAL   F 2  333 ? -2.298  61.099  -51.387  1.00 42.66  ? 335 VAL   B N     1 
ATOM   16579 C  CA    . VAL   F 2  333 ? -2.669  59.897  -50.640  1.00 36.11  ? 335 VAL   B CA    1 
ATOM   16580 C  C     . VAL   F 2  333 ? -3.652  59.052  -51.439  1.00 42.46  ? 335 VAL   B C     1 
ATOM   16581 O  O     . VAL   F 2  333 ? -3.459  57.841  -51.622  1.00 40.56  ? 335 VAL   B O     1 
ATOM   16582 C  CB    . VAL   F 2  333 ? -3.245  60.272  -49.262  1.00 41.39  ? 335 VAL   B CB    1 
ATOM   16583 C  CG1   . VAL   F 2  333 ? -4.214  59.192  -48.795  1.00 44.37  ? 335 VAL   B CG1   1 
ATOM   16584 C  CG2   . VAL   F 2  333 ? -2.151  60.397  -48.236  1.00 38.46  ? 335 VAL   B CG2   1 
ATOM   16585 N  N     . GLN   F 2  334 ? -4.733  59.676  -51.917  1.00 39.61  ? 336 GLN   B N     1 
ATOM   16586 C  CA    . GLN   F 2  334 ? -5.782  58.883  -52.541  1.00 39.53  ? 336 GLN   B CA    1 
ATOM   16587 C  C     . GLN   F 2  334 ? -5.353  58.390  -53.902  1.00 41.51  ? 336 GLN   B C     1 
ATOM   16588 O  O     . GLN   F 2  334 ? -5.725  57.286  -54.308  1.00 49.12  ? 336 GLN   B O     1 
ATOM   16589 C  CB    . GLN   F 2  334 ? -7.075  59.682  -52.657  1.00 33.84  ? 336 GLN   B CB    1 
ATOM   16590 C  CG    . GLN   F 2  334 ? -7.321  60.604  -51.505  1.00 30.87  ? 336 GLN   B CG    1 
ATOM   16591 C  CD    . GLN   F 2  334 ? -8.476  61.537  -51.787  1.00 40.72  ? 336 GLN   B CD    1 
ATOM   16592 O  OE1   . GLN   F 2  334 ? -9.537  61.074  -52.191  1.00 37.16  ? 336 GLN   B OE1   1 
ATOM   16593 N  NE2   . GLN   F 2  334 ? -8.280  62.861  -51.589  1.00 28.13  ? 336 GLN   B NE2   1 
ATOM   16594 N  N     . ASN   F 2  335 ? -4.567  59.176  -54.621  1.00 47.77  ? 337 ASN   B N     1 
ATOM   16595 C  CA    . ASN   F 2  335 ? -4.197  58.750  -55.958  1.00 53.45  ? 337 ASN   B CA    1 
ATOM   16596 C  C     . ASN   F 2  335 ? -3.090  57.697  -55.949  1.00 44.07  ? 337 ASN   B C     1 
ATOM   16597 O  O     . ASN   F 2  335 ? -3.007  56.905  -56.891  1.00 50.93  ? 337 ASN   B O     1 
ATOM   16598 C  CB    . ASN   F 2  335 ? -3.843  59.983  -56.794  1.00 44.13  ? 337 ASN   B CB    1 
ATOM   16599 C  CG    . ASN   F 2  335 ? -5.092  60.798  -57.178  0.50 44.94  ? 337 ASN   B CG    1 
ATOM   16600 O  OD1   . ASN   F 2  335 ? -6.176  60.229  -57.403  1.00 42.43  ? 337 ASN   B OD1   1 
ATOM   16601 N  ND2   . ASN   F 2  335 ? -4.950  62.128  -57.242  1.00 39.86  ? 337 ASN   B ND2   1 
ATOM   16602 N  N     . LYS   F 2  336 ? -2.301  57.613  -54.886  1.00 35.41  ? 338 LYS   B N     1 
ATOM   16603 C  CA    . LYS   F 2  336 ? -1.284  56.576  -54.770  1.00 44.30  ? 338 LYS   B CA    1 
ATOM   16604 C  C     . LYS   F 2  336 ? -1.774  55.322  -54.053  1.00 44.60  ? 338 LYS   B C     1 
ATOM   16605 O  O     . LYS   F 2  336 ? -1.049  54.323  -54.020  1.00 44.72  ? 338 LYS   B O     1 
ATOM   16606 C  CB    . LYS   F 2  336 ? -0.044  57.121  -54.038  1.00 49.31  ? 338 LYS   B CB    1 
ATOM   16607 C  CG    . LYS   F 2  336 ? 0.700   58.217  -54.805  1.00 46.77  ? 338 LYS   B CG    1 
ATOM   16608 C  CD    . LYS   F 2  336 ? 2.162   57.876  -55.017  1.00 59.50  ? 338 LYS   B CD    1 
ATOM   16609 C  CE    . LYS   F 2  336 ? 2.780   58.782  -56.063  1.00 51.65  ? 338 LYS   B CE    1 
ATOM   16610 N  NZ    . LYS   F 2  336 ? 2.018   58.674  -57.343  1.00 72.38  ? 338 LYS   B NZ    1 
ATOM   16611 N  N     . ASN   F 2  337 ? -2.971  55.344  -53.475  1.00 49.24  ? 339 ASN   B N     1 
ATOM   16612 C  CA    . ASN   F 2  337 ? -3.542  54.179  -52.801  1.00 38.16  ? 339 ASN   B CA    1 
ATOM   16613 C  C     . ASN   F 2  337 ? -5.011  54.040  -53.158  1.00 42.23  ? 339 ASN   B C     1 
ATOM   16614 O  O     . ASN   F 2  337 ? -5.843  53.688  -52.313  1.00 37.58  ? 339 ASN   B O     1 
ATOM   16615 C  CB    . ASN   F 2  337 ? -3.355  54.283  -51.297  1.00 43.38  ? 339 ASN   B CB    1 
ATOM   16616 C  CG    . ASN   F 2  337 ? -1.920  54.533  -50.934  1.00 47.41  ? 339 ASN   B CG    1 
ATOM   16617 O  OD1   . ASN   F 2  337 ? -1.106  53.594  -50.871  1.00 41.34  ? 339 ASN   B OD1   1 
ATOM   16618 N  ND2   . ASN   F 2  337 ? -1.575  55.812  -50.741  1.00 34.77  ? 339 ASN   B ND2   1 
ATOM   16619 N  N     . SER   F 2  338 ? -5.320  54.263  -54.449  1.00 42.07  ? 340 SER   B N     1 
ATOM   16620 C  CA    . SER   F 2  338 ? -6.679  54.535  -54.904  1.00 38.66  ? 340 SER   B CA    1 
ATOM   16621 C  C     . SER   F 2  338 ? -7.553  53.295  -54.897  1.00 38.47  ? 340 SER   B C     1 
ATOM   16622 O  O     . SER   F 2  338 ? -8.777  53.413  -54.772  1.00 46.14  ? 340 SER   B O     1 
ATOM   16623 C  CB    . SER   F 2  338 ? -6.652  55.158  -56.306  1.00 47.33  ? 340 SER   B CB    1 
ATOM   16624 O  OG    . SER   F 2  338 ? -6.452  54.183  -57.320  1.00 43.73  ? 340 SER   B OG    1 
ATOM   16625 N  N     . SER   F 2  339 ? -6.963  52.108  -55.031  1.00 43.51  ? 341 SER   B N     1 
ATOM   16626 C  CA    . SER   F 2  339 ? -7.755  50.892  -54.875  1.00 38.33  ? 341 SER   B CA    1 
ATOM   16627 C  C     . SER   F 2  339 ? -8.295  50.744  -53.465  1.00 44.07  ? 341 SER   B C     1 
ATOM   16628 O  O     . SER   F 2  339 ? -9.182  49.914  -53.244  1.00 48.76  ? 341 SER   B O     1 
ATOM   16629 C  CB    . SER   F 2  339 ? -6.933  49.651  -55.201  1.00 37.62  ? 341 SER   B CB    1 
ATOM   16630 O  OG    . SER   F 2  339 ? -6.218  49.220  -54.052  1.00 47.54  ? 341 SER   B OG    1 
ATOM   16631 N  N     . TYR   F 2  340 ? -7.762  51.493  -52.499  1.00 34.83  ? 342 TYR   B N     1 
ATOM   16632 C  CA    . TYR   F 2  340 ? -8.266  51.384  -51.142  1.00 38.36  ? 342 TYR   B CA    1 
ATOM   16633 C  C     . TYR   F 2  340 ? -9.498  52.251  -50.865  1.00 40.37  ? 342 TYR   B C     1 
ATOM   16634 O  O     . TYR   F 2  340 ? -10.044 52.159  -49.761  1.00 37.49  ? 342 TYR   B O     1 
ATOM   16635 C  CB    . TYR   F 2  340 ? -7.152  51.710  -50.155  1.00 38.94  ? 342 TYR   B CB    1 
ATOM   16636 C  CG    . TYR   F 2  340 ? -6.115  50.618  -50.117  1.00 43.69  ? 342 TYR   B CG    1 
ATOM   16637 C  CD1   . TYR   F 2  340 ? -6.448  49.335  -49.691  1.00 43.85  ? 342 TYR   B CD1   1 
ATOM   16638 C  CD2   . TYR   F 2  340 ? -4.816  50.856  -50.527  1.00 41.06  ? 342 TYR   B CD2   1 
ATOM   16639 C  CE1   . TYR   F 2  340 ? -5.507  48.321  -49.671  1.00 44.76  ? 342 TYR   B CE1   1 
ATOM   16640 C  CE2   . TYR   F 2  340 ? -3.867  49.854  -50.513  1.00 43.17  ? 342 TYR   B CE2   1 
ATOM   16641 C  CZ    . TYR   F 2  340 ? -4.214  48.595  -50.082  1.00 50.21  ? 342 TYR   B CZ    1 
ATOM   16642 O  OH    . TYR   F 2  340 ? -3.262  47.615  -50.064  1.00 52.80  ? 342 TYR   B OH    1 
ATOM   16643 N  N     . PHE   F 2  341 ? -9.967  53.059  -51.824  1.00 37.14  ? 343 PHE   B N     1 
ATOM   16644 C  CA    . PHE   F 2  341 ? -11.154 53.896  -51.652  1.00 38.12  ? 343 PHE   B CA    1 
ATOM   16645 C  C     . PHE   F 2  341 ? -12.208 53.435  -52.642  1.00 39.02  ? 343 PHE   B C     1 
ATOM   16646 O  O     . PHE   F 2  341 ? -11.989 53.521  -53.852  1.00 42.96  ? 343 PHE   B O     1 
ATOM   16647 C  CB    . PHE   F 2  341 ? -10.859 55.380  -51.893  1.00 33.12  ? 343 PHE   B CB    1 
ATOM   16648 C  CG    . PHE   F 2  341 ? -9.779  55.938  -51.031  1.00 31.51  ? 343 PHE   B CG    1 
ATOM   16649 C  CD1   . PHE   F 2  341 ? -8.439  55.773  -51.378  1.00 33.24  ? 343 PHE   B CD1   1 
ATOM   16650 C  CD2   . PHE   F 2  341 ? -10.095 56.659  -49.900  1.00 26.59  ? 343 PHE   B CD2   1 
ATOM   16651 C  CE1   . PHE   F 2  341 ? -7.432  56.297  -50.594  1.00 30.99  ? 343 PHE   B CE1   1 
ATOM   16652 C  CE2   . PHE   F 2  341 ? -9.108  57.181  -49.088  1.00 27.18  ? 343 PHE   B CE2   1 
ATOM   16653 C  CZ    . PHE   F 2  341 ? -7.763  57.009  -49.438  1.00 37.21  ? 343 PHE   B CZ    1 
ATOM   16654 N  N     . VAL   F 2  342 ? -13.349 52.959  -52.142  1.00 35.19  ? 344 VAL   B N     1 
ATOM   16655 C  CA    . VAL   F 2  342 ? -14.367 52.462  -53.061  1.00 39.42  ? 344 VAL   B CA    1 
ATOM   16656 C  C     . VAL   F 2  342 ? -14.628 53.508  -54.147  1.00 37.85  ? 344 VAL   B C     1 
ATOM   16657 O  O     . VAL   F 2  342 ? -14.820 54.696  -53.861  1.00 36.76  ? 344 VAL   B O     1 
ATOM   16658 C  CB    . VAL   F 2  342 ? -15.652 52.062  -52.300  1.00 31.76  ? 344 VAL   B CB    1 
ATOM   16659 C  CG1   . VAL   F 2  342 ? -15.372 50.957  -51.291  1.00 24.81  ? 344 VAL   B CG1   1 
ATOM   16660 C  CG2   . VAL   F 2  342 ? -16.291 53.240  -51.642  1.00 26.64  ? 344 VAL   B CG2   1 
ATOM   16661 N  N     . GLU   F 2  343 ? -14.599 53.062  -55.408  1.00 36.91  ? 345 GLU   B N     1 
ATOM   16662 C  CA    . GLU   F 2  343 ? -14.866 53.937  -56.543  1.00 41.13  ? 345 GLU   B CA    1 
ATOM   16663 C  C     . GLU   F 2  343 ? -16.338 54.246  -56.733  1.00 40.73  ? 345 GLU   B C     1 
ATOM   16664 O  O     . GLU   F 2  343 ? -16.660 55.150  -57.510  1.00 39.33  ? 345 GLU   B O     1 
ATOM   16665 C  CB    . GLU   F 2  343 ? -14.363 53.330  -57.856  1.00 45.87  ? 345 GLU   B CB    1 
ATOM   16666 C  CG    . GLU   F 2  343 ? -15.165 52.148  -58.337  1.00 34.20  ? 345 GLU   B CG    1 
ATOM   16667 C  CD    . GLU   F 2  343 ? -14.814 50.925  -57.556  1.00 43.34  ? 345 GLU   B CD    1 
ATOM   16668 O  OE1   . GLU   F 2  343 ? -14.181 51.104  -56.503  1.00 40.58  ? 345 GLU   B OE1   1 
ATOM   16669 O  OE2   . GLU   F 2  343 ? -15.135 49.794  -57.986  1.00 57.31  ? 345 GLU   B OE2   1 
ATOM   16670 N  N     . TRP   F 2  344 ? -17.236 53.497  -56.102  1.00 37.43  ? 346 TRP   B N     1 
ATOM   16671 C  CA    . TRP   F 2  344 ? -18.649 53.797  -56.231  1.00 32.87  ? 346 TRP   B CA    1 
ATOM   16672 C  C     . TRP   F 2  344 ? -19.104 54.826  -55.215  1.00 36.47  ? 346 TRP   B C     1 
ATOM   16673 O  O     . TRP   F 2  344 ? -20.313 55.013  -55.030  1.00 33.64  ? 346 TRP   B O     1 
ATOM   16674 C  CB    . TRP   F 2  344 ? -19.491 52.521  -56.134  1.00 34.19  ? 346 TRP   B CB    1 
ATOM   16675 C  CG    . TRP   F 2  344 ? -19.069 51.545  -55.101  1.00 39.21  ? 346 TRP   B CG    1 
ATOM   16676 C  CD1   . TRP   F 2  344 ? -18.152 50.539  -55.245  1.00 38.24  ? 346 TRP   B CD1   1 
ATOM   16677 C  CD2   . TRP   F 2  344 ? -19.571 51.443  -53.756  1.00 39.67  ? 346 TRP   B CD2   1 
ATOM   16678 N  NE1   . TRP   F 2  344 ? -18.051 49.821  -54.073  1.00 38.76  ? 346 TRP   B NE1   1 
ATOM   16679 C  CE2   . TRP   F 2  344 ? -18.910 50.355  -53.145  1.00 34.44  ? 346 TRP   B CE2   1 
ATOM   16680 C  CE3   . TRP   F 2  344 ? -20.508 52.166  -53.012  1.00 32.28  ? 346 TRP   B CE3   1 
ATOM   16681 C  CZ2   . TRP   F 2  344 ? -19.157 49.979  -51.830  1.00 30.38  ? 346 TRP   B CZ2   1 
ATOM   16682 C  CZ3   . TRP   F 2  344 ? -20.757 51.784  -51.705  1.00 33.08  ? 346 TRP   B CZ3   1 
ATOM   16683 C  CH2   . TRP   F 2  344 ? -20.082 50.705  -51.128  1.00 32.85  ? 346 TRP   B CH2   1 
ATOM   16684 N  N     . ILE   F 2  345 ? -18.164 55.480  -54.541  1.00 33.42  ? 347 ILE   B N     1 
ATOM   16685 C  CA    . ILE   F 2  345 ? -18.462 56.722  -53.843  1.00 30.02  ? 347 ILE   B CA    1 
ATOM   16686 C  C     . ILE   F 2  345 ? -17.417 57.731  -54.300  1.00 32.56  ? 347 ILE   B C     1 
ATOM   16687 O  O     . ILE   F 2  345 ? -16.373 57.886  -53.652  1.00 41.37  ? 347 ILE   B O     1 
ATOM   16688 C  CB    . ILE   F 2  345 ? -18.480 56.546  -52.319  1.00 33.45  ? 347 ILE   B CB    1 
ATOM   16689 C  CG1   . ILE   F 2  345 ? -19.454 55.427  -51.936  1.00 37.11  ? 347 ILE   B CG1   1 
ATOM   16690 C  CG2   . ILE   F 2  345 ? -18.859 57.871  -51.625  1.00 23.83  ? 347 ILE   B CG2   1 
ATOM   16691 C  CD1   . ILE   F 2  345 ? -19.731 55.330  -50.446  1.00 27.46  ? 347 ILE   B CD1   1 
ATOM   16692 N  N     . PRO   F 2  346 ? -17.647 58.421  -55.412  1.00 28.42  ? 348 PRO   B N     1 
ATOM   16693 C  CA    . PRO   F 2  346 ? -16.673 59.412  -55.868  1.00 24.66  ? 348 PRO   B CA    1 
ATOM   16694 C  C     . PRO   F 2  346 ? -16.369 60.420  -54.768  1.00 34.00  ? 348 PRO   B C     1 
ATOM   16695 O  O     . PRO   F 2  346 ? -17.263 60.880  -54.052  1.00 30.64  ? 348 PRO   B O     1 
ATOM   16696 C  CB    . PRO   F 2  346 ? -17.363 60.069  -57.073  1.00 30.06  ? 348 PRO   B CB    1 
ATOM   16697 C  CG    . PRO   F 2  346 ? -18.426 59.045  -57.525  1.00 32.15  ? 348 PRO   B CG    1 
ATOM   16698 C  CD    . PRO   F 2  346 ? -18.854 58.359  -56.268  1.00 32.55  ? 348 PRO   B CD    1 
ATOM   16699 N  N     . ASN   F 2  347 ? -15.079 60.727  -54.604  1.00 31.75  ? 349 ASN   B N     1 
ATOM   16700 C  CA    . ASN   F 2  347 ? -14.661 61.884  -53.835  1.00 26.15  ? 349 ASN   B CA    1 
ATOM   16701 C  C     . ASN   F 2  347 ? -15.038 61.767  -52.366  1.00 28.38  ? 349 ASN   B C     1 
ATOM   16702 O  O     . ASN   F 2  347 ? -15.521 62.729  -51.763  1.00 24.32  ? 349 ASN   B O     1 
ATOM   16703 C  CB    . ASN   F 2  347 ? -15.273 63.147  -54.430  1.00 23.36  ? 349 ASN   B CB    1 
ATOM   16704 C  CG    . ASN   F 2  347 ? -15.000 63.269  -55.901  1.00 29.21  ? 349 ASN   B CG    1 
ATOM   16705 O  OD1   . ASN   F 2  347 ? -15.918 63.300  -56.711  1.00 40.02  ? 349 ASN   B OD1   1 
ATOM   16706 N  ND2   . ASN   F 2  347 ? -13.723 63.330  -56.261  1.00 38.04  ? 349 ASN   B ND2   1 
ATOM   16707 N  N     . ASN   F 2  348 ? -14.786 60.588  -51.777  1.00 23.93  ? 350 ASN   B N     1 
ATOM   16708 C  CA    . ASN   F 2  348 ? -15.292 60.306  -50.438  1.00 25.77  ? 350 ASN   B CA    1 
ATOM   16709 C  C     . ASN   F 2  348 ? -14.374 60.780  -49.303  1.00 25.68  ? 350 ASN   B C     1 
ATOM   16710 O  O     . ASN   F 2  348 ? -14.709 60.568  -48.134  1.00 26.97  ? 350 ASN   B O     1 
ATOM   16711 C  CB    . ASN   F 2  348 ? -15.612 58.807  -50.295  1.00 27.37  ? 350 ASN   B CB    1 
ATOM   16712 C  CG    . ASN   F 2  348 ? -14.438 57.906  -50.608  1.00 30.42  ? 350 ASN   B CG    1 
ATOM   16713 O  OD1   . ASN   F 2  348 ? -13.298 58.341  -50.649  1.00 36.78  ? 350 ASN   B OD1   1 
ATOM   16714 N  ND2   . ASN   F 2  348 ? -14.717 56.637  -50.821  1.00 29.45  ? 350 ASN   B ND2   1 
ATOM   16715 N  N     . VAL   F 2  349 ? -13.262 61.446  -49.603  1.00 27.24  ? 351 VAL   B N     1 
ATOM   16716 C  CA    . VAL   F 2  349 ? -12.382 62.042  -48.597  1.00 25.80  ? 351 VAL   B CA    1 
ATOM   16717 C  C     . VAL   F 2  349 ? -12.654 63.540  -48.548  1.00 30.95  ? 351 VAL   B C     1 
ATOM   16718 O  O     . VAL   F 2  349 ? -12.501 64.229  -49.562  1.00 33.12  ? 351 VAL   B O     1 
ATOM   16719 C  CB    . VAL   F 2  349 ? -10.903 61.778  -48.917  1.00 24.03  ? 351 VAL   B CB    1 
ATOM   16720 C  CG1   . VAL   F 2  349 ? -10.075 62.037  -47.697  1.00 35.67  ? 351 VAL   B CG1   1 
ATOM   16721 C  CG2   . VAL   F 2  349 ? -10.699 60.348  -49.403  1.00 19.85  ? 351 VAL   B CG2   1 
ATOM   16722 N  N     . LYS   F 2  350 ? -13.070 64.046  -47.380  1.00 34.29  ? 352 LYS   B N     1 
ATOM   16723 C  CA    . LYS   F 2  350 ? -13.334 65.467  -47.160  1.00 29.45  ? 352 LYS   B CA    1 
ATOM   16724 C  C     . LYS   F 2  350 ? -12.358 66.009  -46.130  1.00 29.43  ? 352 LYS   B C     1 
ATOM   16725 O  O     . LYS   F 2  350 ? -12.061 65.343  -45.138  1.00 40.24  ? 352 LYS   B O     1 
ATOM   16726 C  CB    . LYS   F 2  350 ? -14.769 65.717  -46.695  1.00 25.17  ? 352 LYS   B CB    1 
ATOM   16727 C  CG    . LYS   F 2  350 ? -15.823 65.331  -47.724  1.00 29.33  ? 352 LYS   B CG    1 
ATOM   16728 C  CD    . LYS   F 2  350 ? -15.611 66.096  -49.033  1.00 33.82  ? 352 LYS   B CD    1 
ATOM   16729 C  CE    . LYS   F 2  350 ? -16.768 65.902  -50.009  1.00 35.74  ? 352 LYS   B CE    1 
ATOM   16730 N  NZ    . LYS   F 2  350 ? -16.347 65.295  -51.301  1.00 30.06  ? 352 LYS   B NZ    1 
ATOM   16731 N  N     . THR   F 2  351 ? -11.854 67.214  -46.363  1.00 31.65  ? 353 THR   B N     1 
ATOM   16732 C  CA    . THR   F 2  351 ? -10.729 67.738  -45.603  1.00 35.15  ? 353 THR   B CA    1 
ATOM   16733 C  C     . THR   F 2  351 ? -11.082 69.080  -44.994  1.00 33.02  ? 353 THR   B C     1 
ATOM   16734 O  O     . THR   F 2  351 ? -11.569 69.975  -45.688  1.00 41.30  ? 353 THR   B O     1 
ATOM   16735 C  CB    . THR   F 2  351 ? -9.489  67.890  -46.490  1.00 33.95  ? 353 THR   B CB    1 
ATOM   16736 O  OG1   . THR   F 2  351 ? -9.147  66.612  -47.028  1.00 36.13  ? 353 THR   B OG1   1 
ATOM   16737 C  CG2   . THR   F 2  351 ? -8.315  68.444  -45.690  1.00 26.23  ? 353 THR   B CG2   1 
ATOM   16738 N  N     . ALA   F 2  352 ? -10.812 69.223  -43.707  1.00 31.60  ? 354 ALA   B N     1 
ATOM   16739 C  CA    . ALA   F 2  352 ? -11.015 70.476  -43.000  1.00 36.29  ? 354 ALA   B CA    1 
ATOM   16740 C  C     . ALA   F 2  352 ? -9.712  70.885  -42.329  1.00 36.47  ? 354 ALA   B C     1 
ATOM   16741 O  O     . ALA   F 2  352 ? -8.839  70.060  -42.032  1.00 31.40  ? 354 ALA   B O     1 
ATOM   16742 C  CB    . ALA   F 2  352 ? -12.138 70.379  -41.949  1.00 39.72  ? 354 ALA   B CB    1 
ATOM   16743 N  N     . VAL   F 2  353 ? -9.590  72.178  -42.092  1.00 36.60  ? 355 VAL   B N     1 
ATOM   16744 C  CA    . VAL   F 2  353 ? -8.405  72.716  -41.453  1.00 38.32  ? 355 VAL   B CA    1 
ATOM   16745 C  C     . VAL   F 2  353 ? -8.830  73.729  -40.414  1.00 36.64  ? 355 VAL   B C     1 
ATOM   16746 O  O     . VAL   F 2  353 ? -9.701  74.565  -40.661  1.00 46.47  ? 355 VAL   B O     1 
ATOM   16747 C  CB    . VAL   F 2  353 ? -7.448  73.347  -42.468  1.00 34.77  ? 355 VAL   B CB    1 
ATOM   16748 C  CG1   . VAL   F 2  353 ? -6.222  73.890  -41.729  1.00 41.43  ? 355 VAL   B CG1   1 
ATOM   16749 C  CG2   . VAL   F 2  353 ? -7.061  72.316  -43.512  1.00 19.33  ? 355 VAL   B CG2   1 
ATOM   16750 N  N     . CYS   F 2  354 ? -8.215  73.648  -39.249  1.00 40.26  ? 356 CYS   B N     1 
ATOM   16751 C  CA    . CYS   F 2  354 ? -8.480  74.566  -38.158  1.00 40.71  ? 356 CYS   B CA    1 
ATOM   16752 C  C     . CYS   F 2  354 ? -7.163  75.252  -37.809  1.00 42.11  ? 356 CYS   B C     1 
ATOM   16753 O  O     . CYS   F 2  354 ? -6.162  74.582  -37.536  1.00 42.36  ? 356 CYS   B O     1 
ATOM   16754 C  CB    . CYS   F 2  354 ? -9.073  73.812  -36.970  1.00 37.38  ? 356 CYS   B CB    1 
ATOM   16755 S  SG    . CYS   F 2  354 ? -9.561  74.860  -35.601  1.00 45.85  ? 356 CYS   B SG    1 
ATOM   16756 N  N     . ASP   F 2  355 ? -7.157  76.586  -37.854  1.00 37.74  ? 357 ASP   B N     1 
ATOM   16757 C  CA    . ASP   F 2  355 ? -5.944  77.333  -37.542  1.00 43.71  ? 357 ASP   B CA    1 
ATOM   16758 C  C     . ASP   F 2  355 ? -5.441  77.022  -36.144  1.00 49.30  ? 357 ASP   B C     1 
ATOM   16759 O  O     . ASP   F 2  355 ? -4.231  76.874  -35.936  1.00 48.81  ? 357 ASP   B O     1 
ATOM   16760 C  CB    . ASP   F 2  355 ? -6.201  78.830  -37.666  1.00 50.78  ? 357 ASP   B CB    1 
ATOM   16761 C  CG    . ASP   F 2  355 ? -6.297  79.286  -39.088  1.00 49.29  ? 357 ASP   B CG    1 
ATOM   16762 O  OD1   . ASP   F 2  355 ? -6.258  78.437  -40.001  1.00 50.57  ? 357 ASP   B OD1   1 
ATOM   16763 O  OD2   . ASP   F 2  355 ? -6.399  80.507  -39.293  1.00 64.64  ? 357 ASP   B OD2   1 
ATOM   16764 N  N     . ILE   F 2  356 ? -6.354  76.938  -35.173  1.00 45.70  ? 358 ILE   B N     1 
ATOM   16765 C  CA    . ILE   F 2  356 ? -6.024  76.779  -33.755  1.00 49.52  ? 358 ILE   B CA    1 
ATOM   16766 C  C     . ILE   F 2  356 ? -5.597  75.349  -33.425  1.00 48.78  ? 358 ILE   B C     1 
ATOM   16767 O  O     . ILE   F 2  356 ? -6.429  74.430  -33.471  1.00 51.94  ? 358 ILE   B O     1 
ATOM   16768 C  CB    . ILE   F 2  356 ? -7.212  77.208  -32.884  1.00 50.24  ? 358 ILE   B CB    1 
ATOM   16769 C  CG1   . ILE   F 2  356 ? -7.490  78.705  -33.088  1.00 48.64  ? 358 ILE   B CG1   1 
ATOM   16770 C  CG2   . ILE   F 2  356 ? -6.932  76.861  -31.435  1.00 43.16  ? 358 ILE   B CG2   1 
ATOM   16771 C  CD1   . ILE   F 2  356 ? -8.686  79.257  -32.318  1.00 49.78  ? 358 ILE   B CD1   1 
ATOM   16772 N  N     . PRO   F 2  357 ? -4.332  75.104  -33.090  1.00 46.09  ? 359 PRO   B N     1 
ATOM   16773 C  CA    . PRO   F 2  357 ? -3.886  73.723  -32.837  1.00 45.44  ? 359 PRO   B CA    1 
ATOM   16774 C  C     . PRO   F 2  357 ? -4.245  73.277  -31.433  1.00 46.71  ? 359 PRO   B C     1 
ATOM   16775 O  O     . PRO   F 2  357 ? -4.685  74.083  -30.597  1.00 42.72  ? 359 PRO   B O     1 
ATOM   16776 C  CB    . PRO   F 2  357 ? -2.359  73.796  -33.017  1.00 45.88  ? 359 PRO   B CB    1 
ATOM   16777 C  CG    . PRO   F 2  357 ? -2.010  75.208  -32.726  1.00 36.68  ? 359 PRO   B CG    1 
ATOM   16778 C  CD    . PRO   F 2  357 ? -3.196  76.041  -33.177  1.00 39.00  ? 359 PRO   B CD    1 
ATOM   16779 N  N     . PRO   F 2  358 ? -4.064  71.998  -31.138  1.00 50.21  ? 360 PRO   B N     1 
ATOM   16780 C  CA    . PRO   F 2  358 ? -4.323  71.504  -29.787  1.00 47.45  ? 360 PRO   B CA    1 
ATOM   16781 C  C     . PRO   F 2  358 ? -3.190  71.911  -28.852  1.00 46.40  ? 360 PRO   B C     1 
ATOM   16782 O  O     . PRO   F 2  358 ? -2.168  72.451  -29.273  1.00 49.79  ? 360 PRO   B O     1 
ATOM   16783 C  CB    . PRO   F 2  358 ? -4.393  69.988  -29.990  1.00 42.61  ? 360 PRO   B CB    1 
ATOM   16784 C  CG    . PRO   F 2  358 ? -3.467  69.722  -31.118  1.00 33.26  ? 360 PRO   B CG    1 
ATOM   16785 C  CD    . PRO   F 2  358 ? -3.632  70.919  -32.046  1.00 45.52  ? 360 PRO   B CD    1 
ATOM   16786 N  N     . ARG   F 2  359 ? -3.404  71.664  -27.558  1.00 58.37  ? 369 ARG   B N     1 
ATOM   16787 C  CA    . ARG   F 2  359 ? -2.418  72.016  -26.539  1.00 51.92  ? 369 ARG   B CA    1 
ATOM   16788 C  C     . ARG   F 2  359 ? -1.175  71.153  -26.695  1.00 48.56  ? 369 ARG   B C     1 
ATOM   16789 O  O     . ARG   F 2  359 ? -1.266  69.929  -26.826  1.00 52.70  ? 369 ARG   B O     1 
ATOM   16790 C  CB    . ARG   F 2  359 ? -3.014  71.854  -25.134  1.00 59.12  ? 369 ARG   B CB    1 
ATOM   16791 C  CG    . ARG   F 2  359 ? -2.016  71.461  -24.041  1.00 56.86  ? 369 ARG   B CG    1 
ATOM   16792 C  CD    . ARG   F 2  359 ? -2.247  72.208  -22.728  1.00 50.15  ? 369 ARG   B CD    1 
ATOM   16793 N  NE    . ARG   F 2  359 ? -2.710  73.573  -22.963  1.00 78.48  ? 369 ARG   B NE    1 
ATOM   16794 C  CZ    . ARG   F 2  359 ? -2.457  74.614  -22.175  1.00 83.04  ? 369 ARG   B CZ    1 
ATOM   16795 N  NH1   . ARG   F 2  359 ? -1.689  74.500  -21.101  1.00 84.35  ? 369 ARG   B NH1   1 
ATOM   16796 N  NH2   . ARG   F 2  359 ? -2.983  75.802  -22.478  1.00 60.60  ? 369 ARG   B NH2   1 
ATOM   16797 N  N     . GLY   F 2  360 ? -0.013  71.790  -26.698  1.00 46.03  ? 370 GLY   B N     1 
ATOM   16798 C  CA    . GLY   F 2  360 ? 1.225   71.045  -26.797  1.00 49.28  ? 370 GLY   B CA    1 
ATOM   16799 C  C     . GLY   F 2  360 ? 1.812   71.030  -28.192  1.00 51.45  ? 370 GLY   B C     1 
ATOM   16800 O  O     . GLY   F 2  360 ? 3.026   71.186  -28.360  1.00 48.40  ? 370 GLY   B O     1 
ATOM   16801 N  N     . LEU   F 2  361 ? 0.955   70.875  -29.200  1.00 48.25  ? 371 LEU   B N     1 
ATOM   16802 C  CA    . LEU   F 2  361 ? 1.378   70.692  -30.579  1.00 47.30  ? 371 LEU   B CA    1 
ATOM   16803 C  C     . LEU   F 2  361 ? 1.223   71.975  -31.392  1.00 47.04  ? 371 LEU   B C     1 
ATOM   16804 O  O     . LEU   F 2  361 ? 0.325   72.783  -31.143  1.00 50.13  ? 371 LEU   B O     1 
ATOM   16805 C  CB    . LEU   F 2  361 ? 0.573   69.567  -31.230  1.00 47.11  ? 371 LEU   B CB    1 
ATOM   16806 C  CG    . LEU   F 2  361 ? 0.863   68.163  -30.700  1.00 43.54  ? 371 LEU   B CG    1 
ATOM   16807 C  CD1   . LEU   F 2  361 ? -0.164  67.166  -31.206  1.00 34.44  ? 371 LEU   B CD1   1 
ATOM   16808 C  CD2   . LEU   F 2  361 ? 2.273   67.739  -31.110  1.00 39.85  ? 371 LEU   B CD2   1 
ATOM   16809 N  N     . LYS   F 2  362 ? 2.130   72.156  -32.362  1.00 43.36  ? 372 LYS   B N     1 
ATOM   16810 C  CA    . LYS   F 2  362 ? 1.974   73.140  -33.435  1.00 43.09  ? 372 LYS   B CA    1 
ATOM   16811 C  C     . LYS   F 2  362 ? 1.176   72.592  -34.609  1.00 42.36  ? 372 LYS   B C     1 
ATOM   16812 O  O     . LYS   F 2  362 ? 0.395   73.328  -35.218  1.00 50.43  ? 372 LYS   B O     1 
ATOM   16813 C  CB    . LYS   F 2  362 ? 3.337   73.602  -33.959  1.00 50.87  ? 372 LYS   B CB    1 
ATOM   16814 C  CG    . LYS   F 2  362 ? 4.010   74.699  -33.161  1.00 54.74  ? 372 LYS   B CG    1 
ATOM   16815 C  CD    . LYS   F 2  362 ? 5.397   74.960  -33.719  1.00 63.23  ? 372 LYS   B CD    1 
ATOM   16816 C  CE    . LYS   F 2  362 ? 6.319   73.761  -33.490  1.00 56.25  ? 372 LYS   B CE    1 
ATOM   16817 N  NZ    . LYS   F 2  362 ? 6.751   73.650  -32.047  1.00 59.17  ? 372 LYS   B NZ    1 
ATOM   16818 N  N     . MET   F 2  363 ? 1.368   71.312  -34.936  1.00 44.92  ? 373 MET   B N     1 
ATOM   16819 C  CA    . MET   F 2  363 ? 0.711   70.639  -36.050  1.00 42.04  ? 373 MET   B CA    1 
ATOM   16820 C  C     . MET   F 2  363 ? 0.125   69.305  -35.599  1.00 44.67  ? 373 MET   B C     1 
ATOM   16821 O  O     . MET   F 2  363 ? 0.838   68.468  -35.041  1.00 40.53  ? 373 MET   B O     1 
ATOM   16822 C  CB    . MET   F 2  363 ? 1.703   70.375  -37.183  1.00 53.02  ? 373 MET   B CB    1 
ATOM   16823 C  CG    . MET   F 2  363 ? 2.483   71.579  -37.634  1.00 55.60  ? 373 MET   B CG    1 
ATOM   16824 S  SD    . MET   F 2  363 ? 1.790   72.293  -39.124  1.00 52.07  ? 373 MET   B SD    1 
ATOM   16825 C  CE    . MET   F 2  363 ? 2.590   73.899  -39.070  1.00 63.25  ? 373 MET   B CE    1 
ATOM   16826 N  N     . SER   F 2  364 ? -1.152  69.076  -35.892  1.00 45.38  ? 374 SER   B N     1 
ATOM   16827 C  CA    . SER   F 2  364 ? -1.749  67.772  -35.657  1.00 33.88  ? 374 SER   B CA    1 
ATOM   16828 C  C     . SER   F 2  364 ? -2.673  67.415  -36.815  1.00 32.22  ? 374 SER   B C     1 
ATOM   16829 O  O     . SER   F 2  364 ? -3.113  68.273  -37.575  1.00 33.67  ? 374 SER   B O     1 
ATOM   16830 C  CB    . SER   F 2  364 ? -2.506  67.749  -34.318  1.00 38.14  ? 374 SER   B CB    1 
ATOM   16831 O  OG    . SER   F 2  364 ? -3.658  68.565  -34.361  1.00 41.83  ? 374 SER   B OG    1 
ATOM   16832 N  N     . ALA   F 2  365 ? -2.965  66.131  -36.948  1.00 35.50  ? 375 ALA   B N     1 
ATOM   16833 C  CA    . ALA   F 2  365 ? -3.999  65.680  -37.870  1.00 33.95  ? 375 ALA   B CA    1 
ATOM   16834 C  C     . ALA   F 2  365 ? -4.847  64.615  -37.175  1.00 33.60  ? 375 ALA   B C     1 
ATOM   16835 O  O     . ALA   F 2  365 ? -4.338  63.834  -36.364  1.00 30.70  ? 375 ALA   B O     1 
ATOM   16836 C  CB    . ALA   F 2  365 ? -3.397  65.139  -39.178  1.00 22.82  ? 375 ALA   B CB    1 
ATOM   16837 N  N     . THR   F 2  366 ? -6.148  64.616  -37.471  1.00 30.93  ? 376 THR   B N     1 
ATOM   16838 C  CA    . THR   F 2  366 ? -7.105  63.649  -36.942  1.00 31.16  ? 376 THR   B CA    1 
ATOM   16839 C  C     . THR   F 2  366 ? -7.846  63.007  -38.110  1.00 30.14  ? 376 THR   B C     1 
ATOM   16840 O  O     . THR   F 2  366 ? -8.332  63.703  -39.006  1.00 24.31  ? 376 THR   B O     1 
ATOM   16841 C  CB    . THR   F 2  366 ? -8.118  64.292  -35.972  1.00 27.27  ? 376 THR   B CB    1 
ATOM   16842 O  OG1   . THR   F 2  366 ? -7.433  64.993  -34.933  1.00 29.66  ? 376 THR   B OG1   1 
ATOM   16843 C  CG2   . THR   F 2  366 ? -9.021  63.242  -35.346  1.00 25.15  ? 376 THR   B CG2   1 
ATOM   16844 N  N     . PHE   F 2  367 ? -7.934  61.685  -38.069  1.00 27.67  ? 377 PHE   B N     1 
ATOM   16845 C  CA    . PHE   F 2  367 ? -8.467  60.839  -39.122  1.00 33.75  ? 377 PHE   B CA    1 
ATOM   16846 C  C     . PHE   F 2  367 ? -9.760  60.170  -38.636  1.00 31.22  ? 377 PHE   B C     1 
ATOM   16847 O  O     . PHE   F 2  367 ? -9.841  59.706  -37.497  1.00 23.31  ? 377 PHE   B O     1 
ATOM   16848 C  CB    . PHE   F 2  367 ? -7.390  59.802  -39.510  1.00 28.81  ? 377 PHE   B CB    1 
ATOM   16849 C  CG    . PHE   F 2  367 ? -7.873  58.692  -40.407  1.00 29.82  ? 377 PHE   B CG    1 
ATOM   16850 C  CD1   . PHE   F 2  367 ? -8.369  57.512  -39.870  1.00 30.38  ? 377 PHE   B CD1   1 
ATOM   16851 C  CD2   . PHE   F 2  367 ? -7.816  58.820  -41.791  1.00 32.80  ? 377 PHE   B CD2   1 
ATOM   16852 C  CE1   . PHE   F 2  367 ? -8.827  56.489  -40.716  1.00 36.24  ? 377 PHE   B CE1   1 
ATOM   16853 C  CE2   . PHE   F 2  367 ? -8.251  57.805  -42.635  1.00 26.73  ? 377 PHE   B CE2   1 
ATOM   16854 C  CZ    . PHE   F 2  367 ? -8.756  56.643  -42.102  1.00 29.36  ? 377 PHE   B CZ    1 
ATOM   16855 N  N     . ILE   F 2  368 ? -10.791 60.153  -39.479  1.00 24.82  ? 378 ILE   B N     1 
ATOM   16856 C  CA    . ILE   F 2  368 ? -12.016 59.424  -39.180  1.00 23.00  ? 378 ILE   B CA    1 
ATOM   16857 C  C     . ILE   F 2  368 ? -12.363 58.632  -40.424  1.00 31.81  ? 378 ILE   B C     1 
ATOM   16858 O  O     . ILE   F 2  368 ? -12.799 59.205  -41.431  1.00 28.19  ? 378 ILE   B O     1 
ATOM   16859 C  CB    . ILE   F 2  368 ? -13.180 60.340  -38.776  1.00 25.26  ? 378 ILE   B CB    1 
ATOM   16860 C  CG1   . ILE   F 2  368 ? -12.698 61.487  -37.898  1.00 25.96  ? 378 ILE   B CG1   1 
ATOM   16861 C  CG2   . ILE   F 2  368 ? -14.192 59.559  -37.998  1.00 19.10  ? 378 ILE   B CG2   1 
ATOM   16862 C  CD1   . ILE   F 2  368 ? -13.776 62.440  -37.550  1.00 28.84  ? 378 ILE   B CD1   1 
ATOM   16863 N  N     . GLY   F 2  369 ? -12.181 57.322  -40.367  1.00 30.68  ? 379 GLY   B N     1 
ATOM   16864 C  CA    . GLY   F 2  369 ? -12.409 56.469  -41.516  1.00 28.38  ? 379 GLY   B CA    1 
ATOM   16865 C  C     . GLY   F 2  369 ? -13.608 55.567  -41.296  1.00 24.39  ? 379 GLY   B C     1 
ATOM   16866 O  O     . GLY   F 2  369 ? -13.805 55.048  -40.206  1.00 28.86  ? 379 GLY   B O     1 
ATOM   16867 N  N     . ASN   F 2  370 ? -14.406 55.390  -42.342  1.00 26.63  ? 380 ASN   B N     1 
ATOM   16868 C  CA    . ASN   F 2  370 ? -15.435 54.369  -42.369  1.00 20.45  ? 380 ASN   B CA    1 
ATOM   16869 C  C     . ASN   F 2  370 ? -14.896 53.296  -43.312  1.00 27.72  ? 380 ASN   B C     1 
ATOM   16870 O  O     . ASN   F 2  370 ? -15.212 53.259  -44.502  1.00 32.40  ? 380 ASN   B O     1 
ATOM   16871 C  CB    . ASN   F 2  370 ? -16.753 54.956  -42.808  1.00 19.61  ? 380 ASN   B CB    1 
ATOM   16872 C  CG    . ASN   F 2  370 ? -17.949 54.019  -42.567  1.00 27.97  ? 380 ASN   B CG    1 
ATOM   16873 O  OD1   . ASN   F 2  370 ? -17.803 52.800  -42.387  1.00 26.87  ? 380 ASN   B OD1   1 
ATOM   16874 N  ND2   . ASN   F 2  370 ? -19.151 54.598  -42.600  1.00 23.34  ? 380 ASN   B ND2   1 
ATOM   16875 N  N     . SER   F 2  371 ? -14.026 52.441  -42.768  1.00 31.36  ? 381 SER   B N     1 
ATOM   16876 C  CA    . SER   F 2  371 ? -13.417 51.329  -43.491  1.00 24.35  ? 381 SER   B CA    1 
ATOM   16877 C  C     . SER   F 2  371 ? -14.186 50.036  -43.247  1.00 25.48  ? 381 SER   B C     1 
ATOM   16878 O  O     . SER   F 2  371 ? -14.604 49.754  -42.121  1.00 30.29  ? 381 SER   B O     1 
ATOM   16879 C  CB    . SER   F 2  371 ? -11.960 51.134  -43.066  1.00 24.00  ? 381 SER   B CB    1 
ATOM   16880 O  OG    . SER   F 2  371 ? -11.371 49.992  -43.697  1.00 30.04  ? 381 SER   B OG    1 
ATOM   16881 N  N     . THR   F 2  372 ? -14.357 49.239  -44.302  1.00 27.69  ? 382 THR   B N     1 
ATOM   16882 C  CA    . THR   F 2  372 ? -14.865 47.894  -44.088  1.00 26.94  ? 382 THR   B CA    1 
ATOM   16883 C  C     . THR   F 2  372 ? -13.921 47.058  -43.233  1.00 29.37  ? 382 THR   B C     1 
ATOM   16884 O  O     . THR   F 2  372 ? -14.337 46.010  -42.727  1.00 36.35  ? 382 THR   B O     1 
ATOM   16885 C  CB    . THR   F 2  372 ? -15.133 47.183  -45.425  1.00 33.75  ? 382 THR   B CB    1 
ATOM   16886 O  OG1   . THR   F 2  372 ? -13.908 46.704  -45.983  1.00 39.64  ? 382 THR   B OG1   1 
ATOM   16887 C  CG2   . THR   F 2  372 ? -15.785 48.125  -46.402  1.00 31.31  ? 382 THR   B CG2   1 
ATOM   16888 N  N     . ALA   F 2  373 ? -12.677 47.499  -43.043  1.00 25.94  ? 383 ALA   B N     1 
ATOM   16889 C  CA    . ALA   F 2  373 ? -11.725 46.790  -42.201  1.00 23.13  ? 383 ALA   B CA    1 
ATOM   16890 C  C     . ALA   F 2  373 ? -12.113 46.803  -40.721  1.00 23.39  ? 383 ALA   B C     1 
ATOM   16891 O  O     . ALA   F 2  373 ? -11.542 46.053  -39.925  1.00 25.32  ? 383 ALA   B O     1 
ATOM   16892 C  CB    . ALA   F 2  373 ? -10.333 47.398  -42.413  1.00 26.81  ? 383 ALA   B CB    1 
ATOM   16893 N  N     . ILE   F 2  374 ? -13.084 47.619  -40.323  1.00 27.19  ? 384 ILE   B N     1 
ATOM   16894 C  CA    . ILE   F 2  374 ? -13.570 47.554  -38.954  1.00 27.58  ? 384 ILE   B CA    1 
ATOM   16895 C  C     . ILE   F 2  374 ? -14.139 46.179  -38.618  1.00 30.50  ? 384 ILE   B C     1 
ATOM   16896 O  O     . ILE   F 2  374 ? -14.182 45.793  -37.439  1.00 27.32  ? 384 ILE   B O     1 
ATOM   16897 C  CB    . ILE   F 2  374 ? -14.618 48.644  -38.734  1.00 25.75  ? 384 ILE   B CB    1 
ATOM   16898 C  CG1   . ILE   F 2  374 ? -14.674 48.981  -37.258  1.00 25.54  ? 384 ILE   B CG1   1 
ATOM   16899 C  CG2   . ILE   F 2  374 ? -15.951 48.195  -39.287  1.00 24.67  ? 384 ILE   B CG2   1 
ATOM   16900 C  CD1   . ILE   F 2  374 ? -13.512 49.803  -36.831  1.00 27.48  ? 384 ILE   B CD1   1 
ATOM   16901 N  N     . GLN   F 2  375 ? -14.582 45.424  -39.631  1.00 25.27  ? 385 GLN   B N     1 
ATOM   16902 C  CA    . GLN   F 2  375 ? -15.026 44.059  -39.393  1.00 29.84  ? 385 GLN   B CA    1 
ATOM   16903 C  C     . GLN   F 2  375 ? -13.994 43.233  -38.630  1.00 39.31  ? 385 GLN   B C     1 
ATOM   16904 O  O     . GLN   F 2  375 ? -14.362 42.237  -37.997  1.00 38.82  ? 385 GLN   B O     1 
ATOM   16905 C  CB    . GLN   F 2  375 ? -15.367 43.369  -40.711  1.00 33.32  ? 385 GLN   B CB    1 
ATOM   16906 C  CG    . GLN   F 2  375 ? -14.182 42.821  -41.484  1.00 35.33  ? 385 GLN   B CG    1 
ATOM   16907 C  CD    . GLN   F 2  375 ? -14.636 41.974  -42.674  1.00 41.02  ? 385 GLN   B CD    1 
ATOM   16908 O  OE1   . GLN   F 2  375 ? -15.054 40.827  -42.507  1.00 51.73  ? 385 GLN   B OE1   1 
ATOM   16909 N  NE2   . GLN   F 2  375 ? -14.578 42.544  -43.873  1.00 31.43  ? 385 GLN   B NE2   1 
ATOM   16910 N  N     . GLU   F 2  376 ? -12.714 43.621  -38.647  1.00 31.86  ? 386 GLU   B N     1 
ATOM   16911 C  CA    . GLU   F 2  376 ? -11.738 42.856  -37.881  1.00 30.03  ? 386 GLU   B CA    1 
ATOM   16912 C  C     . GLU   F 2  376 ? -12.001 42.974  -36.385  1.00 31.71  ? 386 GLU   B C     1 
ATOM   16913 O  O     . GLU   F 2  376 ? -11.844 41.994  -35.646  1.00 29.40  ? 386 GLU   B O     1 
ATOM   16914 C  CB    . GLU   F 2  376 ? -10.320 43.303  -38.232  1.00 27.89  ? 386 GLU   B CB    1 
ATOM   16915 C  CG    . GLU   F 2  376 ? -9.913  42.857  -39.635  1.00 23.04  ? 386 GLU   B CG    1 
ATOM   16916 C  CD    . GLU   F 2  376 ? -8.488  43.247  -40.002  1.00 36.72  ? 386 GLU   B CD    1 
ATOM   16917 O  OE1   . GLU   F 2  376 ? -7.894  44.096  -39.295  1.00 38.77  ? 386 GLU   B OE1   1 
ATOM   16918 O  OE2   . GLU   F 2  376 ? -7.961  42.699  -41.000  1.00 38.76  ? 386 GLU   B OE2   1 
ATOM   16919 N  N     . LEU   F 2  377 ? -12.401 44.166  -35.926  1.00 30.54  ? 387 LEU   B N     1 
ATOM   16920 C  CA    . LEU   F 2  377 ? -12.757 44.379  -34.525  1.00 25.26  ? 387 LEU   B CA    1 
ATOM   16921 C  C     . LEU   F 2  377 ? -13.917 43.474  -34.109  1.00 28.38  ? 387 LEU   B C     1 
ATOM   16922 O  O     . LEU   F 2  377 ? -13.815 42.689  -33.155  1.00 31.60  ? 387 LEU   B O     1 
ATOM   16923 C  CB    . LEU   F 2  377 ? -13.131 45.847  -34.316  1.00 25.57  ? 387 LEU   B CB    1 
ATOM   16924 C  CG    . LEU   F 2  377 ? -12.869 46.601  -33.010  1.00 27.52  ? 387 LEU   B CG    1 
ATOM   16925 C  CD1   . LEU   F 2  377 ? -13.942 47.637  -32.805  1.00 26.21  ? 387 LEU   B CD1   1 
ATOM   16926 C  CD2   . LEU   F 2  377 ? -12.758 45.693  -31.801  1.00 31.16  ? 387 LEU   B CD2   1 
ATOM   16927 N  N     . PHE   F 2  378 ? -15.031 43.564  -34.830  1.00 25.43  ? 388 PHE   B N     1 
ATOM   16928 C  CA    . PHE   F 2  378 ? -16.206 42.807  -34.451  1.00 25.18  ? 388 PHE   B CA    1 
ATOM   16929 C  C     . PHE   F 2  378 ? -15.937 41.310  -34.520  1.00 24.65  ? 388 PHE   B C     1 
ATOM   16930 O  O     . PHE   F 2  378 ? -16.403 40.547  -33.663  1.00 25.68  ? 388 PHE   B O     1 
ATOM   16931 C  CB    . PHE   F 2  378 ? -17.370 43.253  -35.331  1.00 24.18  ? 388 PHE   B CB    1 
ATOM   16932 C  CG    . PHE   F 2  378 ? -17.678 44.731  -35.191  1.00 24.44  ? 388 PHE   B CG    1 
ATOM   16933 C  CD1   . PHE   F 2  378 ? -18.095 45.253  -33.964  1.00 23.06  ? 388 PHE   B CD1   1 
ATOM   16934 C  CD2   . PHE   F 2  378 ? -17.538 45.606  -36.276  1.00 27.35  ? 388 PHE   B CD2   1 
ATOM   16935 C  CE1   . PHE   F 2  378 ? -18.381 46.630  -33.823  1.00 29.07  ? 388 PHE   B CE1   1 
ATOM   16936 C  CE2   . PHE   F 2  378 ? -17.815 46.986  -36.155  1.00 21.81  ? 388 PHE   B CE2   1 
ATOM   16937 C  CZ    . PHE   F 2  378 ? -18.241 47.498  -34.930  1.00 27.68  ? 388 PHE   B CZ    1 
ATOM   16938 N  N     . LYS   F 2  379 ? -15.145 40.877  -35.505  1.00 27.98  ? 389 LYS   B N     1 
ATOM   16939 C  CA    . LYS   F 2  379 ? -14.761 39.465  -35.596  1.00 28.02  ? 389 LYS   B CA    1 
ATOM   16940 C  C     . LYS   F 2  379 ? -13.964 39.032  -34.381  1.00 31.02  ? 389 LYS   B C     1 
ATOM   16941 O  O     . LYS   F 2  379 ? -14.139 37.916  -33.880  1.00 34.48  ? 389 LYS   B O     1 
ATOM   16942 C  CB    . LYS   F 2  379 ? -13.935 39.206  -36.855  1.00 28.30  ? 389 LYS   B CB    1 
ATOM   16943 C  CG    . LYS   F 2  379 ? -14.751 38.894  -38.095  1.00 35.53  ? 389 LYS   B CG    1 
ATOM   16944 C  CD    . LYS   F 2  379 ? -13.929 39.172  -39.355  1.00 35.81  ? 389 LYS   B CD    1 
ATOM   16945 C  CE    . LYS   F 2  379 ? -14.348 38.258  -40.494  1.00 43.80  ? 389 LYS   B CE    1 
ATOM   16946 N  NZ    . LYS   F 2  379 ? -13.704 38.636  -41.776  1.00 56.10  ? 389 LYS   B NZ    1 
ATOM   16947 N  N     . ARG   F 2  380 ? -13.050 39.888  -33.921  1.00 25.33  ? 390 ARG   B N     1 
ATOM   16948 C  CA    . ARG   F 2  380 ? -12.255 39.557  -32.753  1.00 26.50  ? 390 ARG   B CA    1 
ATOM   16949 C  C     . ARG   F 2  380 ? -13.156 39.336  -31.551  1.00 32.02  ? 390 ARG   B C     1 
ATOM   16950 O  O     . ARG   F 2  380 ? -12.984 38.366  -30.803  1.00 34.80  ? 390 ARG   B O     1 
ATOM   16951 C  CB    . ARG   F 2  380 ? -11.251 40.673  -32.475  1.00 24.46  ? 390 ARG   B CB    1 
ATOM   16952 C  CG    . ARG   F 2  380 ? -10.326 40.423  -31.313  1.00 19.94  ? 390 ARG   B CG    1 
ATOM   16953 C  CD    . ARG   F 2  380 ? -9.480  41.650  -31.083  1.00 23.10  ? 390 ARG   B CD    1 
ATOM   16954 N  NE    . ARG   F 2  380 ? -10.106 42.602  -30.172  1.00 35.19  ? 390 ARG   B NE    1 
ATOM   16955 C  CZ    . ARG   F 2  380 ? -10.016 43.925  -30.264  1.00 30.44  ? 390 ARG   B CZ    1 
ATOM   16956 N  NH1   . ARG   F 2  380 ? -9.440  44.516  -31.298  1.00 26.97  ? 390 ARG   B NH1   1 
ATOM   16957 N  NH2   . ARG   F 2  380 ? -10.517 44.673  -29.293  1.00 28.55  ? 390 ARG   B NH2   1 
ATOM   16958 N  N     . ILE   F 2  381 ? -14.135 40.220  -31.364  1.00 30.43  ? 391 ILE   B N     1 
ATOM   16959 C  CA    . ILE   F 2  381 ? -15.016 40.096  -30.218  1.00 26.11  ? 391 ILE   B CA    1 
ATOM   16960 C  C     . ILE   F 2  381 ? -15.932 38.911  -30.406  1.00 32.31  ? 391 ILE   B C     1 
ATOM   16961 O  O     . ILE   F 2  381 ? -16.192 38.156  -29.458  1.00 32.91  ? 391 ILE   B O     1 
ATOM   16962 C  CB    . ILE   F 2  381 ? -15.807 41.391  -30.008  1.00 23.85  ? 391 ILE   B CB    1 
ATOM   16963 C  CG1   . ILE   F 2  381 ? -14.886 42.468  -29.441  1.00 21.30  ? 391 ILE   B CG1   1 
ATOM   16964 C  CG2   . ILE   F 2  381 ? -17.044 41.130  -29.119  1.00 23.45  ? 391 ILE   B CG2   1 
ATOM   16965 C  CD1   . ILE   F 2  381 ? -15.370 43.841  -29.775  1.00 26.20  ? 391 ILE   B CD1   1 
ATOM   16966 N  N     . SER   F 2  382 ? -16.426 38.719  -31.637  1.00 27.53  ? 392 SER   B N     1 
ATOM   16967 C  CA    . SER   F 2  382 ? -17.349 37.619  -31.900  1.00 30.75  ? 392 SER   B CA    1 
ATOM   16968 C  C     . SER   F 2  382 ? -16.702 36.270  -31.593  1.00 34.73  ? 392 SER   B C     1 
ATOM   16969 O  O     . SER   F 2  382 ? -17.352 35.368  -31.047  1.00 33.90  ? 392 SER   B O     1 
ATOM   16970 C  CB    . SER   F 2  382 ? -17.827 37.670  -33.355  1.00 35.39  ? 392 SER   B CB    1 
ATOM   16971 O  OG    . SER   F 2  382 ? -18.653 36.552  -33.672  1.00 31.13  ? 392 SER   B OG    1 
ATOM   16972 N  N     . GLU   F 2  383 ? -15.424 36.108  -31.950  1.00 34.34  ? 393 GLU   B N     1 
ATOM   16973 C  CA    . GLU   F 2  383 ? -14.754 34.835  -31.720  1.00 37.82  ? 393 GLU   B CA    1 
ATOM   16974 C  C     . GLU   F 2  383 ? -14.590 34.552  -30.227  1.00 41.64  ? 393 GLU   B C     1 
ATOM   16975 O  O     . GLU   F 2  383 ? -14.781 33.409  -29.786  1.00 33.02  ? 393 GLU   B O     1 
ATOM   16976 C  CB    . GLU   F 2  383 ? -13.412 34.817  -32.440  1.00 42.72  ? 393 GLU   B CB    1 
ATOM   16977 C  CG    . GLU   F 2  383 ? -12.394 33.835  -31.853  1.00 67.03  ? 393 GLU   B CG    1 
ATOM   16978 C  CD    . GLU   F 2  383 ? -11.178 34.532  -31.210  1.00 80.77  ? 393 GLU   B CD    1 
ATOM   16979 O  OE1   . GLU   F 2  383 ? -10.854 35.699  -31.594  1.00 63.82  ? 393 GLU   B OE1   1 
ATOM   16980 O  OE2   . GLU   F 2  383 ? -10.551 33.898  -30.316  1.00 66.60  ? 393 GLU   B OE2   1 
ATOM   16981 N  N     . GLN   F 2  384 ? -14.267 35.577  -29.426  1.00 29.68  ? 394 GLN   B N     1 
ATOM   16982 C  CA    . GLN   F 2  384 ? -14.265 35.382  -27.977  1.00 34.38  ? 394 GLN   B CA    1 
ATOM   16983 C  C     . GLN   F 2  384 ? -15.654 35.011  -27.469  1.00 29.56  ? 394 GLN   B C     1 
ATOM   16984 O  O     . GLN   F 2  384 ? -15.813 34.070  -26.686  1.00 34.29  ? 394 GLN   B O     1 
ATOM   16985 C  CB    . GLN   F 2  384 ? -13.754 36.630  -27.268  1.00 32.53  ? 394 GLN   B CB    1 
ATOM   16986 C  CG    . GLN   F 2  384 ? -12.368 37.050  -27.686  1.00 28.29  ? 394 GLN   B CG    1 
ATOM   16987 C  CD    . GLN   F 2  384 ? -11.834 38.203  -26.865  1.00 38.59  ? 394 GLN   B CD    1 
ATOM   16988 O  OE1   . GLN   F 2  384 ? -11.287 38.002  -25.766  1.00 56.14  ? 394 GLN   B OE1   1 
ATOM   16989 N  NE2   . GLN   F 2  384 ? -11.985 39.419  -27.380  1.00 28.87  ? 394 GLN   B NE2   1 
ATOM   16990 N  N     . PHE   F 2  385 ? -16.672 35.748  -27.906  1.00 31.26  ? 395 PHE   B N     1 
ATOM   16991 C  CA    . PHE   F 2  385 ? -18.052 35.436  -27.554  1.00 29.87  ? 395 PHE   B CA    1 
ATOM   16992 C  C     . PHE   F 2  385 ? -18.387 33.972  -27.847  1.00 29.83  ? 395 PHE   B C     1 
ATOM   16993 O  O     . PHE   F 2  385 ? -18.791 33.212  -26.960  1.00 31.40  ? 395 PHE   B O     1 
ATOM   16994 C  CB    . PHE   F 2  385 ? -18.987 36.381  -28.322  1.00 27.14  ? 395 PHE   B CB    1 
ATOM   16995 C  CG    . PHE   F 2  385 ? -20.448 36.097  -28.119  1.00 30.17  ? 395 PHE   B CG    1 
ATOM   16996 C  CD1   . PHE   F 2  385 ? -21.088 35.114  -28.864  1.00 33.01  ? 395 PHE   B CD1   1 
ATOM   16997 C  CD2   . PHE   F 2  385 ? -21.190 36.827  -27.194  1.00 27.60  ? 395 PHE   B CD2   1 
ATOM   16998 C  CE1   . PHE   F 2  385 ? -22.433 34.861  -28.674  1.00 32.93  ? 395 PHE   B CE1   1 
ATOM   16999 C  CE2   . PHE   F 2  385 ? -22.534 36.574  -27.000  1.00 22.56  ? 395 PHE   B CE2   1 
ATOM   17000 C  CZ    . PHE   F 2  385 ? -23.156 35.595  -27.738  1.00 27.49  ? 395 PHE   B CZ    1 
ATOM   17001 N  N     . THR   F 2  386 ? -18.233 33.565  -29.103  1.00 30.26  ? 396 THR   B N     1 
ATOM   17002 C  CA    . THR   F 2  386 ? -18.588 32.207  -29.495  1.00 34.59  ? 396 THR   B CA    1 
ATOM   17003 C  C     . THR   F 2  386 ? -17.899 31.156  -28.631  1.00 30.17  ? 396 THR   B C     1 
ATOM   17004 O  O     . THR   F 2  386 ? -18.521 30.155  -28.261  1.00 33.70  ? 396 THR   B O     1 
ATOM   17005 C  CB    . THR   F 2  386 ? -18.243 31.979  -30.963  1.00 31.68  ? 396 THR   B CB    1 
ATOM   17006 O  OG1   . THR   F 2  386 ? -18.743 33.085  -31.732  1.00 45.06  ? 396 THR   B OG1   1 
ATOM   17007 C  CG2   . THR   F 2  386 ? -18.893 30.708  -31.435  1.00 20.45  ? 396 THR   B CG2   1 
ATOM   17008 N  N     . ALA   F 2  387 ? -16.609 31.351  -28.323  1.00 29.25  ? 397 ALA   B N     1 
ATOM   17009 C  CA    . ALA   F 2  387 ? -15.857 30.326  -27.604  1.00 24.43  ? 397 ALA   B CA    1 
ATOM   17010 C  C     . ALA   F 2  387 ? -16.518 29.999  -26.271  1.00 30.46  ? 397 ALA   B C     1 
ATOM   17011 O  O     . ALA   F 2  387 ? -16.539 28.842  -25.843  1.00 32.79  ? 397 ALA   B O     1 
ATOM   17012 C  CB    . ALA   F 2  387 ? -14.424 30.781  -27.390  1.00 29.11  ? 397 ALA   B CB    1 
ATOM   17013 N  N     . MET   F 2  388 ? -17.079 31.005  -25.620  1.00 20.42  ? 398 MET   B N     1 
ATOM   17014 C  CA    . MET   F 2  388 ? -17.792 30.839  -24.378  1.00 22.35  ? 398 MET   B CA    1 
ATOM   17015 C  C     . MET   F 2  388 ? -19.252 30.507  -24.625  1.00 27.98  ? 398 MET   B C     1 
ATOM   17016 O  O     . MET   F 2  388 ? -19.803 29.632  -23.941  1.00 23.71  ? 398 MET   B O     1 
ATOM   17017 C  CB    . MET   F 2  388 ? -17.717 32.114  -23.526  1.00 22.55  ? 398 MET   B CB    1 
ATOM   17018 C  CG    . MET   F 2  388 ? -16.352 32.667  -23.257  1.00 25.43  ? 398 MET   B CG    1 
ATOM   17019 S  SD    . MET   F 2  388 ? -16.445 33.905  -21.936  1.00 29.62  ? 398 MET   B SD    1 
ATOM   17020 C  CE    . MET   F 2  388 ? -17.380 35.182  -22.749  1.00 26.82  ? 398 MET   B CE    1 
ATOM   17021 N  N     . PHE   F 2  389 ? -19.889 31.189  -25.594  1.00 25.28  ? 399 PHE   B N     1 
ATOM   17022 C  CA    . PHE   F 2  389 ? -21.335 31.068  -25.702  1.00 24.01  ? 399 PHE   B CA    1 
ATOM   17023 C  C     . PHE   F 2  389 ? -21.759 29.696  -26.194  1.00 22.34  ? 399 PHE   B C     1 
ATOM   17024 O  O     . PHE   F 2  389 ? -22.840 29.231  -25.821  1.00 28.52  ? 399 PHE   B O     1 
ATOM   17025 C  CB    . PHE   F 2  389 ? -21.943 32.148  -26.595  1.00 27.57  ? 399 PHE   B CB    1 
ATOM   17026 C  CG    . PHE   F 2  389 ? -23.453 32.099  -26.634  1.00 24.90  ? 399 PHE   B CG    1 
ATOM   17027 C  CD1   . PHE   F 2  389 ? -24.195 32.211  -25.451  1.00 23.08  ? 399 PHE   B CD1   1 
ATOM   17028 C  CD2   . PHE   F 2  389 ? -24.138 31.914  -27.839  1.00 26.29  ? 399 PHE   B CD2   1 
ATOM   17029 C  CE1   . PHE   F 2  389 ? -25.604 32.147  -25.454  1.00 25.00  ? 399 PHE   B CE1   1 
ATOM   17030 C  CE2   . PHE   F 2  389 ? -25.558 31.856  -27.864  1.00 27.23  ? 399 PHE   B CE2   1 
ATOM   17031 C  CZ    . PHE   F 2  389 ? -26.289 31.970  -26.668  1.00 26.06  ? 399 PHE   B CZ    1 
ATOM   17032 N  N     . ARG   F 2  390 ? -20.929 29.014  -26.988  1.00 26.76  ? 400 ARG   B N     1 
ATOM   17033 C  CA    . ARG   F 2  390 ? -21.296 27.676  -27.451  1.00 23.73  ? 400 ARG   B CA    1 
ATOM   17034 C  C     . ARG   F 2  390 ? -21.280 26.624  -26.339  1.00 31.87  ? 400 ARG   B C     1 
ATOM   17035 O  O     . ARG   F 2  390 ? -21.791 25.521  -26.545  1.00 29.40  ? 400 ARG   B O     1 
ATOM   17036 C  CB    . ARG   F 2  390 ? -20.385 27.245  -28.594  1.00 30.28  ? 400 ARG   B CB    1 
ATOM   17037 C  CG    . ARG   F 2  390 ? -18.932 27.027  -28.210  1.00 46.92  ? 400 ARG   B CG    1 
ATOM   17038 C  CD    . ARG   F 2  390 ? -18.136 26.596  -29.447  1.00 53.35  ? 400 ARG   B CD    1 
ATOM   17039 N  NE    . ARG   F 2  390 ? -18.320 27.538  -30.551  1.00 62.02  ? 400 ARG   B NE    1 
ATOM   17040 C  CZ    . ARG   F 2  390 ? -18.400 27.201  -31.835  1.00 71.42  ? 400 ARG   B CZ    1 
ATOM   17041 N  NH1   . ARG   F 2  390 ? -18.362 25.932  -32.221  1.00 74.88  ? 400 ARG   B NH1   1 
ATOM   17042 N  NH2   . ARG   F 2  390 ? -18.527 28.159  -32.753  1.00 44.99  ? 400 ARG   B NH2   1 
ATOM   17043 N  N     . ARG   F 2  391 ? -20.727 26.930  -25.165  1.00 28.65  ? 401 ARG   B N     1 
ATOM   17044 C  CA    . ARG   F 2  391 ? -20.916 26.101  -23.984  1.00 24.97  ? 401 ARG   B CA    1 
ATOM   17045 C  C     . ARG   F 2  391 ? -21.692 26.840  -22.907  1.00 28.87  ? 401 ARG   B C     1 
ATOM   17046 O  O     . ARG   F 2  391 ? -21.681 26.419  -21.740  1.00 28.72  ? 401 ARG   B O     1 
ATOM   17047 C  CB    . ARG   F 2  391 ? -19.576 25.612  -23.439  1.00 27.76  ? 401 ARG   B CB    1 
ATOM   17048 C  CG    . ARG   F 2  391 ? -18.718 24.941  -24.480  1.00 29.67  ? 401 ARG   B CG    1 
ATOM   17049 C  CD    . ARG   F 2  391 ? -19.291 23.585  -24.834  1.00 29.95  ? 401 ARG   B CD    1 
ATOM   17050 N  NE    . ARG   F 2  391 ? -18.991 22.620  -23.790  1.00 28.75  ? 401 ARG   B NE    1 
ATOM   17051 C  CZ    . ARG   F 2  391 ? -17.845 21.959  -23.701  1.00 25.90  ? 401 ARG   B CZ    1 
ATOM   17052 N  NH1   . ARG   F 2  391 ? -16.869 22.147  -24.568  1.00 27.77  ? 401 ARG   B NH1   1 
ATOM   17053 N  NH2   . ARG   F 2  391 ? -17.680 21.080  -22.723  1.00 29.07  ? 401 ARG   B NH2   1 
ATOM   17054 N  N     . LYS   F 2  392 ? -22.386 27.920  -23.285  1.00 19.44  ? 402 LYS   B N     1 
ATOM   17055 C  CA    . LYS   F 2  392 ? -23.212 28.679  -22.352  1.00 24.10  ? 402 LYS   B CA    1 
ATOM   17056 C  C     . LYS   F 2  392 ? -22.441 29.007  -21.067  1.00 27.14  ? 402 LYS   B C     1 
ATOM   17057 O  O     . LYS   F 2  392 ? -23.024 29.155  -19.997  1.00 35.06  ? 402 LYS   B O     1 
ATOM   17058 C  CB    . LYS   F 2  392 ? -24.516 27.936  -22.052  1.00 21.20  ? 402 LYS   B CB    1 
ATOM   17059 C  CG    . LYS   F 2  392 ? -25.404 27.807  -23.301  1.00 43.23  ? 402 LYS   B CG    1 
ATOM   17060 C  CD    . LYS   F 2  392 ? -26.538 26.763  -23.151  1.00 54.64  ? 402 LYS   B CD    1 
ATOM   17061 C  CE    . LYS   F 2  392 ? -27.423 26.708  -24.413  1.00 66.44  ? 402 LYS   B CE    1 
ATOM   17062 N  NZ    . LYS   F 2  392 ? -28.654 25.861  -24.272  1.00 58.31  ? 402 LYS   B NZ    1 
ATOM   17063 N  N     . ALA   F 2  393 ? -21.122 29.145  -21.183  1.00 18.43  ? 403 ALA   B N     1 
ATOM   17064 C  CA    . ALA   F 2  393 ? -20.281 29.492  -20.052  1.00 25.50  ? 403 ALA   B CA    1 
ATOM   17065 C  C     . ALA   F 2  393 ? -20.615 30.877  -19.506  1.00 30.22  ? 403 ALA   B C     1 
ATOM   17066 O  O     . ALA   F 2  393 ? -20.814 31.835  -20.257  1.00 24.57  ? 403 ALA   B O     1 
ATOM   17067 C  CB    . ALA   F 2  393 ? -18.809 29.456  -20.466  1.00 23.68  ? 403 ALA   B CB    1 
ATOM   17068 N  N     . PHE   F 2  394 ? -20.606 30.988  -18.180  1.00 28.45  ? 404 PHE   B N     1 
ATOM   17069 C  CA    . PHE   F 2  394 ? -20.784 32.241  -17.458  1.00 26.52  ? 404 PHE   B CA    1 
ATOM   17070 C  C     . PHE   F 2  394 ? -22.137 32.875  -17.688  1.00 21.99  ? 404 PHE   B C     1 
ATOM   17071 O  O     . PHE   F 2  394 ? -22.355 34.012  -17.257  1.00 22.69  ? 404 PHE   B O     1 
ATOM   17072 C  CB    . PHE   F 2  394 ? -19.672 33.228  -17.799  1.00 29.20  ? 404 PHE   B CB    1 
ATOM   17073 C  CG    . PHE   F 2  394 ? -18.332 32.687  -17.496  1.00 24.99  ? 404 PHE   B CG    1 
ATOM   17074 C  CD1   . PHE   F 2  394 ? -17.888 32.625  -16.186  1.00 25.32  ? 404 PHE   B CD1   1 
ATOM   17075 C  CD2   . PHE   F 2  394 ? -17.527 32.190  -18.513  1.00 22.59  ? 404 PHE   B CD2   1 
ATOM   17076 C  CE1   . PHE   F 2  394 ? -16.637 32.066  -15.896  1.00 27.37  ? 404 PHE   B CE1   1 
ATOM   17077 C  CE2   . PHE   F 2  394 ? -16.288 31.646  -18.239  1.00 22.50  ? 404 PHE   B CE2   1 
ATOM   17078 C  CZ    . PHE   F 2  394 ? -15.835 31.573  -16.937  1.00 19.46  ? 404 PHE   B CZ    1 
ATOM   17079 N  N     . LEU   F 2  395 ? -23.061 32.148  -18.328  1.00 19.46  ? 405 LEU   B N     1 
ATOM   17080 C  CA    . LEU   F 2  395 ? -24.379 32.695  -18.626  1.00 21.01  ? 405 LEU   B CA    1 
ATOM   17081 C  C     . LEU   F 2  395 ? -25.210 32.935  -17.370  1.00 27.46  ? 405 LEU   B C     1 
ATOM   17082 O  O     . LEU   F 2  395 ? -26.057 33.842  -17.360  1.00 30.37  ? 405 LEU   B O     1 
ATOM   17083 C  CB    . LEU   F 2  395 ? -25.121 31.758  -19.570  1.00 22.46  ? 405 LEU   B CB    1 
ATOM   17084 C  CG    . LEU   F 2  395 ? -25.760 32.373  -20.811  1.00 33.42  ? 405 LEU   B CG    1 
ATOM   17085 C  CD1   . LEU   F 2  395 ? -24.809 33.346  -21.487  1.00 31.82  ? 405 LEU   B CD1   1 
ATOM   17086 C  CD2   . LEU   F 2  395 ? -26.124 31.259  -21.773  1.00 39.97  ? 405 LEU   B CD2   1 
ATOM   17087 N  N     . HIS   F 2  396 ? -24.993 32.152  -16.305  1.00 20.67  ? 406 HIS   B N     1 
ATOM   17088 C  CA    . HIS   F 2  396 ? -25.849 32.286  -15.127  1.00 29.81  ? 406 HIS   B CA    1 
ATOM   17089 C  C     . HIS   F 2  396 ? -25.768 33.689  -14.525  1.00 30.87  ? 406 HIS   B C     1 
ATOM   17090 O  O     . HIS   F 2  396 ? -26.724 34.145  -13.873  1.00 28.84  ? 406 HIS   B O     1 
ATOM   17091 C  CB    . HIS   F 2  396 ? -25.504 31.212  -14.076  1.00 30.27  ? 406 HIS   B CB    1 
ATOM   17092 C  CG    . HIS   F 2  396 ? -24.201 31.438  -13.372  1.00 27.76  ? 406 HIS   B CG    1 
ATOM   17093 N  ND1   . HIS   F 2  396 ? -24.129 31.849  -12.058  1.00 31.36  ? 406 HIS   B ND1   1 
ATOM   17094 C  CD2   . HIS   F 2  396 ? -22.922 31.311  -13.800  1.00 24.60  ? 406 HIS   B CD2   1 
ATOM   17095 C  CE1   . HIS   F 2  396 ? -22.859 31.966  -11.709  1.00 30.08  ? 406 HIS   B CE1   1 
ATOM   17096 N  NE2   . HIS   F 2  396 ? -22.110 31.633  -12.745  1.00 30.20  ? 406 HIS   B NE2   1 
ATOM   17097 N  N     . TRP   F 2  397 ? -24.651 34.393  -14.740  1.00 22.49  ? 407 TRP   B N     1 
ATOM   17098 C  CA    . TRP   F 2  397 ? -24.565 35.774  -14.280  1.00 20.54  ? 407 TRP   B CA    1 
ATOM   17099 C  C     . TRP   F 2  397 ? -25.539 36.678  -15.008  1.00 22.00  ? 407 TRP   B C     1 
ATOM   17100 O  O     . TRP   F 2  397 ? -25.858 37.751  -14.503  1.00 23.24  ? 407 TRP   B O     1 
ATOM   17101 C  CB    . TRP   F 2  397 ? -23.151 36.319  -14.462  1.00 20.76  ? 407 TRP   B CB    1 
ATOM   17102 C  CG    . TRP   F 2  397 ? -22.098 35.550  -13.693  1.00 25.83  ? 407 TRP   B CG    1 
ATOM   17103 C  CD1   . TRP   F 2  397 ? -21.049 34.852  -14.217  1.00 27.66  ? 407 TRP   B CD1   1 
ATOM   17104 C  CD2   . TRP   F 2  397 ? -22.009 35.408  -12.277  1.00 21.43  ? 407 TRP   B CD2   1 
ATOM   17105 N  NE1   . TRP   F 2  397 ? -20.306 34.288  -13.211  1.00 29.81  ? 407 TRP   B NE1   1 
ATOM   17106 C  CE2   . TRP   F 2  397 ? -20.863 34.627  -12.008  1.00 30.74  ? 407 TRP   B CE2   1 
ATOM   17107 C  CE3   . TRP   F 2  397 ? -22.766 35.893  -11.203  1.00 21.25  ? 407 TRP   B CE3   1 
ATOM   17108 C  CZ2   . TRP   F 2  397 ? -20.469 34.291  -10.708  1.00 23.61  ? 407 TRP   B CZ2   1 
ATOM   17109 C  CZ3   . TRP   F 2  397 ? -22.389 35.559  -9.926   1.00 23.09  ? 407 TRP   B CZ3   1 
ATOM   17110 C  CH2   . TRP   F 2  397 ? -21.255 34.741  -9.685   1.00 22.95  ? 407 TRP   B CH2   1 
ATOM   17111 N  N     . TYR   F 2  398 ? -26.025 36.266  -16.178  1.00 20.56  ? 408 TYR   B N     1 
ATOM   17112 C  CA    . TYR   F 2  398 ? -27.026 37.016  -16.921  1.00 22.81  ? 408 TYR   B CA    1 
ATOM   17113 C  C     . TYR   F 2  398 ? -28.435 36.451  -16.734  1.00 29.71  ? 408 TYR   B C     1 
ATOM   17114 O  O     . TYR   F 2  398 ? -29.372 37.208  -16.447  1.00 25.90  ? 408 TYR   B O     1 
ATOM   17115 C  CB    . TYR   F 2  398 ? -26.624 37.054  -18.405  1.00 20.35  ? 408 TYR   B CB    1 
ATOM   17116 C  CG    . TYR   F 2  398 ? -25.248 37.634  -18.568  1.00 24.76  ? 408 TYR   B CG    1 
ATOM   17117 C  CD1   . TYR   F 2  398 ? -24.108 36.859  -18.360  1.00 17.68  ? 408 TYR   B CD1   1 
ATOM   17118 C  CD2   . TYR   F 2  398 ? -25.085 38.979  -18.854  1.00 24.92  ? 408 TYR   B CD2   1 
ATOM   17119 C  CE1   . TYR   F 2  398 ? -22.854 37.412  -18.472  1.00 23.37  ? 408 TYR   B CE1   1 
ATOM   17120 C  CE2   . TYR   F 2  398 ? -23.845 39.536  -18.957  1.00 24.54  ? 408 TYR   B CE2   1 
ATOM   17121 C  CZ    . TYR   F 2  398 ? -22.728 38.758  -18.772  1.00 25.09  ? 408 TYR   B CZ    1 
ATOM   17122 O  OH    . TYR   F 2  398 ? -21.494 39.346  -18.907  1.00 20.18  ? 408 TYR   B OH    1 
ATOM   17123 N  N     . THR   F 2  399 ? -28.602 35.127  -16.842  1.00 25.34  ? 409 THR   B N     1 
ATOM   17124 C  CA    . THR   F 2  399 ? -29.935 34.571  -16.672  1.00 23.33  ? 409 THR   B CA    1 
ATOM   17125 C  C     . THR   F 2  399 ? -30.464 34.876  -15.280  1.00 22.57  ? 409 THR   B C     1 
ATOM   17126 O  O     . THR   F 2  399 ? -31.663 35.131  -15.117  1.00 27.48  ? 409 THR   B O     1 
ATOM   17127 C  CB    . THR   F 2  399 ? -29.946 33.066  -16.970  1.00 21.32  ? 409 THR   B CB    1 
ATOM   17128 O  OG1   . THR   F 2  399 ? -29.019 32.383  -16.125  1.00 28.28  ? 409 THR   B OG1   1 
ATOM   17129 C  CG2   . THR   F 2  399 ? -29.575 32.798  -18.429  1.00 14.53  ? 409 THR   B CG2   1 
ATOM   17130 N  N     . GLY   F 2  400 ? -29.579 34.956  -14.286  1.00 25.18  ? 410 GLY   B N     1 
ATOM   17131 C  CA    . GLY   F 2  400 ? -29.995 35.342  -12.947  1.00 19.41  ? 410 GLY   B CA    1 
ATOM   17132 C  C     . GLY   F 2  400 ? -30.476 36.777  -12.820  1.00 29.50  ? 410 GLY   B C     1 
ATOM   17133 O  O     . GLY   F 2  400 ? -31.152 37.110  -11.837  1.00 27.63  ? 410 GLY   B O     1 
ATOM   17134 N  N     . GLU   F 2  401 ? -30.136 37.641  -13.775  1.00 30.44  ? 411 GLU   B N     1 
ATOM   17135 C  CA    . GLU   F 2  401 ? -30.687 38.988  -13.805  1.00 30.78  ? 411 GLU   B CA    1 
ATOM   17136 C  C     . GLU   F 2  401 ? -31.980 39.072  -14.606  1.00 31.78  ? 411 GLU   B C     1 
ATOM   17137 O  O     . GLU   F 2  401 ? -32.519 40.165  -14.773  1.00 34.12  ? 411 GLU   B O     1 
ATOM   17138 C  CB    . GLU   F 2  401 ? -29.674 39.979  -14.394  1.00 32.73  ? 411 GLU   B CB    1 
ATOM   17139 C  CG    . GLU   F 2  401 ? -28.408 40.164  -13.586  1.00 29.46  ? 411 GLU   B CG    1 
ATOM   17140 C  CD    . GLU   F 2  401 ? -28.680 40.383  -12.101  1.00 35.18  ? 411 GLU   B CD    1 
ATOM   17141 O  OE1   . GLU   F 2  401 ? -29.378 41.363  -11.718  1.00 29.86  ? 411 GLU   B OE1   1 
ATOM   17142 O  OE2   . GLU   F 2  401 ? -28.176 39.555  -11.317  1.00 38.99  ? 411 GLU   B OE2   1 
ATOM   17143 N  N     . GLY   F 2  402 ? -32.474 37.961  -15.132  1.00 27.13  ? 412 GLY   B N     1 
ATOM   17144 C  CA    . GLY   F 2  402 ? -33.693 37.955  -15.910  1.00 32.90  ? 412 GLY   B CA    1 
ATOM   17145 C  C     . GLY   F 2  402 ? -33.513 37.607  -17.373  1.00 38.64  ? 412 GLY   B C     1 
ATOM   17146 O  O     . GLY   F 2  402 ? -34.496 37.227  -18.023  1.00 39.26  ? 412 GLY   B O     1 
ATOM   17147 N  N     . MET   F 2  403 ? -32.292 37.699  -17.910  1.00 31.78  ? 413 MET   B N     1 
ATOM   17148 C  CA    . MET   F 2  403 ? -32.121 37.510  -19.340  1.00 25.75  ? 413 MET   B CA    1 
ATOM   17149 C  C     . MET   F 2  403 ? -32.261 36.044  -19.742  1.00 29.42  ? 413 MET   B C     1 
ATOM   17150 O  O     . MET   F 2  403 ? -32.038 35.110  -18.959  1.00 28.85  ? 413 MET   B O     1 
ATOM   17151 C  CB    . MET   F 2  403 ? -30.765 38.025  -19.818  1.00 27.14  ? 413 MET   B CB    1 
ATOM   17152 C  CG    . MET   F 2  403 ? -30.515 39.467  -19.536  1.00 30.19  ? 413 MET   B CG    1 
ATOM   17153 S  SD    . MET   F 2  403 ? -29.035 39.995  -20.395  1.00 31.63  ? 413 MET   B SD    1 
ATOM   17154 C  CE    . MET   F 2  403 ? -29.494 39.673  -22.089  1.00 33.93  ? 413 MET   B CE    1 
ATOM   17155 N  N     . ASP   F 2  404 ? -32.576 35.873  -21.020  1.00 30.37  ? 414 ASP   B N     1 
ATOM   17156 C  CA    . ASP   F 2  404 ? -32.787 34.604  -21.687  1.00 28.72  ? 414 ASP   B CA    1 
ATOM   17157 C  C     . ASP   F 2  404 ? -31.702 34.415  -22.748  1.00 34.35  ? 414 ASP   B C     1 
ATOM   17158 O  O     . ASP   F 2  404 ? -31.282 35.389  -23.385  1.00 29.71  ? 414 ASP   B O     1 
ATOM   17159 C  CB    . ASP   F 2  404 ? -34.191 34.610  -22.321  1.00 30.40  ? 414 ASP   B CB    1 
ATOM   17160 C  CG    . ASP   F 2  404 ? -34.637 33.248  -22.803  1.00 46.09  ? 414 ASP   B CG    1 
ATOM   17161 O  OD1   . ASP   F 2  404 ? -34.169 32.789  -23.880  1.00 49.58  ? 414 ASP   B OD1   1 
ATOM   17162 O  OD2   . ASP   F 2  404 ? -35.470 32.640  -22.094  1.00 50.97  ? 414 ASP   B OD2   1 
ATOM   17163 N  N     . GLU   F 2  405 ? -31.248 33.164  -22.928  1.00 30.51  ? 415 GLU   B N     1 
ATOM   17164 C  CA    . GLU   F 2  405 ? -30.263 32.834  -23.956  1.00 31.70  ? 415 GLU   B CA    1 
ATOM   17165 C  C     . GLU   F 2  405 ? -30.561 33.548  -25.261  1.00 36.33  ? 415 GLU   B C     1 
ATOM   17166 O  O     . GLU   F 2  405 ? -29.664 34.108  -25.909  1.00 27.98  ? 415 GLU   B O     1 
ATOM   17167 C  CB    . GLU   F 2  405 ? -30.231 31.322  -24.206  1.00 26.82  ? 415 GLU   B CB    1 
ATOM   17168 C  CG    . GLU   F 2  405 ? -29.581 30.529  -23.105  1.00 49.93  ? 415 GLU   B CG    1 
ATOM   17169 C  CD    . GLU   F 2  405 ? -29.313 29.075  -23.491  1.00 64.16  ? 415 GLU   B CD    1 
ATOM   17170 O  OE1   . GLU   F 2  405 ? -29.500 28.686  -24.680  1.00 57.17  ? 415 GLU   B OE1   1 
ATOM   17171 O  OE2   . GLU   F 2  405 ? -28.905 28.321  -22.581  1.00 55.44  ? 415 GLU   B OE2   1 
ATOM   17172 N  N     . MET   F 2  406 ? -31.837 33.500  -25.660  1.00 43.15  ? 416 MET   B N     1 
ATOM   17173 C  CA    . MET   F 2  406 ? -32.296 34.068  -26.921  1.00 41.61  ? 416 MET   B CA    1 
ATOM   17174 C  C     . MET   F 2  406 ? -31.670 35.432  -27.172  1.00 34.95  ? 416 MET   B C     1 
ATOM   17175 O  O     . MET   F 2  406 ? -31.156 35.709  -28.261  1.00 34.26  ? 416 MET   B O     1 
ATOM   17176 C  CB    . MET   F 2  406 ? -33.821 34.174  -26.890  1.00 41.45  ? 416 MET   B CB    1 
ATOM   17177 C  CG    . MET   F 2  406 ? -34.486 34.103  -28.244  1.00 57.36  ? 416 MET   B CG    1 
ATOM   17178 S  SD    . MET   F 2  406 ? -34.736 32.389  -28.716  1.00 105.68 ? 416 MET   B SD    1 
ATOM   17179 C  CE    . MET   F 2  406 ? -35.925 31.884  -27.461  1.00 66.36  ? 416 MET   B CE    1 
ATOM   17180 N  N     . GLU   F 2  407 ? -31.712 36.293  -26.157  1.00 28.51  ? 417 GLU   B N     1 
ATOM   17181 C  CA    . GLU   F 2  407 ? -31.147 37.624  -26.280  1.00 29.99  ? 417 GLU   B CA    1 
ATOM   17182 C  C     . GLU   F 2  407 ? -29.681 37.580  -26.697  1.00 34.71  ? 417 GLU   B C     1 
ATOM   17183 O  O     . GLU   F 2  407 ? -29.227 38.467  -27.427  1.00 40.15  ? 417 GLU   B O     1 
ATOM   17184 C  CB    . GLU   F 2  407 ? -31.314 38.350  -24.961  1.00 30.15  ? 417 GLU   B CB    1 
ATOM   17185 C  CG    . GLU   F 2  407 ? -31.492 39.808  -25.080  1.00 31.87  ? 417 GLU   B CG    1 
ATOM   17186 C  CD    . GLU   F 2  407 ? -32.103 40.410  -23.831  1.00 41.50  ? 417 GLU   B CD    1 
ATOM   17187 O  OE1   . GLU   F 2  407 ? -32.814 39.698  -23.070  1.00 37.55  ? 417 GLU   B OE1   1 
ATOM   17188 O  OE2   . GLU   F 2  407 ? -31.861 41.613  -23.620  1.00 39.65  ? 417 GLU   B OE2   1 
ATOM   17189 N  N     . PHE   F 2  408 ? -28.928 36.557  -26.264  1.00 29.12  ? 418 PHE   B N     1 
ATOM   17190 C  CA    . PHE   F 2  408 ? -27.538 36.425  -26.693  1.00 27.58  ? 418 PHE   B CA    1 
ATOM   17191 C  C     . PHE   F 2  408 ? -27.453 35.968  -28.142  1.00 31.21  ? 418 PHE   B C     1 
ATOM   17192 O  O     . PHE   F 2  408 ? -26.750 36.580  -28.954  1.00 36.11  ? 418 PHE   B O     1 
ATOM   17193 C  CB    . PHE   F 2  408 ? -26.773 35.446  -25.801  1.00 28.68  ? 418 PHE   B CB    1 
ATOM   17194 C  CG    . PHE   F 2  408 ? -26.424 35.981  -24.446  1.00 25.28  ? 418 PHE   B CG    1 
ATOM   17195 C  CD1   . PHE   F 2  408 ? -27.405 36.161  -23.481  1.00 24.53  ? 418 PHE   B CD1   1 
ATOM   17196 C  CD2   . PHE   F 2  408 ? -25.098 36.244  -24.109  1.00 27.68  ? 418 PHE   B CD2   1 
ATOM   17197 C  CE1   . PHE   F 2  408 ? -27.083 36.629  -22.222  1.00 23.37  ? 418 PHE   B CE1   1 
ATOM   17198 C  CE2   . PHE   F 2  408 ? -24.765 36.715  -22.837  1.00 25.86  ? 418 PHE   B CE2   1 
ATOM   17199 C  CZ    . PHE   F 2  408 ? -25.762 36.902  -21.894  1.00 23.37  ? 418 PHE   B CZ    1 
ATOM   17200 N  N     . THR   F 2  409 ? -28.132 34.869  -28.476  1.00 37.58  ? 419 THR   B N     1 
ATOM   17201 C  CA    . THR   F 2  409 ? -28.225 34.393  -29.855  1.00 31.84  ? 419 THR   B CA    1 
ATOM   17202 C  C     . THR   F 2  409 ? -28.514 35.551  -30.813  1.00 25.64  ? 419 THR   B C     1 
ATOM   17203 O  O     . THR   F 2  409 ? -27.913 35.640  -31.876  1.00 32.06  ? 419 THR   B O     1 
ATOM   17204 C  CB    . THR   F 2  409 ? -29.298 33.292  -29.958  1.00 32.94  ? 419 THR   B CB    1 
ATOM   17205 O  OG1   . THR   F 2  409 ? -28.861 32.119  -29.250  1.00 37.12  ? 419 THR   B OG1   1 
ATOM   17206 C  CG2   . THR   F 2  409 ? -29.570 32.902  -31.394  1.00 19.75  ? 419 THR   B CG2   1 
ATOM   17207 N  N     . GLU   F 2  410 ? -29.390 36.474  -30.429  1.00 30.75  ? 420 GLU   B N     1 
ATOM   17208 C  CA    . GLU   F 2  410 ? -29.719 37.593  -31.305  1.00 33.34  ? 420 GLU   B CA    1 
ATOM   17209 C  C     . GLU   F 2  410 ? -28.572 38.594  -31.423  1.00 36.17  ? 420 GLU   B C     1 
ATOM   17210 O  O     . GLU   F 2  410 ? -28.267 39.062  -32.528  1.00 30.59  ? 420 GLU   B O     1 
ATOM   17211 C  CB    . GLU   F 2  410 ? -30.964 38.305  -30.802  1.00 39.65  ? 420 GLU   B CB    1 
ATOM   17212 C  CG    . GLU   F 2  410 ? -32.264 37.690  -31.217  1.00 39.90  ? 420 GLU   B CG    1 
ATOM   17213 C  CD    . GLU   F 2  410 ? -33.385 38.247  -30.367  1.00 64.23  ? 420 GLU   B CD    1 
ATOM   17214 O  OE1   . GLU   F 2  410 ? -33.289 39.455  -29.999  1.00 66.16  ? 420 GLU   B OE1   1 
ATOM   17215 O  OE2   . GLU   F 2  410 ? -34.323 37.476  -30.040  1.00 41.71  ? 420 GLU   B OE2   1 
ATOM   17216 N  N     . ALA   F 2  411 ? -27.978 39.000  -30.288  1.00 35.58  ? 421 ALA   B N     1 
ATOM   17217 C  CA    . ALA   F 2  411 ? -26.822 39.892  -30.335  1.00 28.22  ? 421 ALA   B CA    1 
ATOM   17218 C  C     . ALA   F 2  411 ? -25.714 39.291  -31.191  1.00 34.40  ? 421 ALA   B C     1 
ATOM   17219 O  O     . ALA   F 2  411 ? -25.159 39.953  -32.074  1.00 31.05  ? 421 ALA   B O     1 
ATOM   17220 C  CB    . ALA   F 2  411 ? -26.309 40.164  -28.934  1.00 21.31  ? 421 ALA   B CB    1 
ATOM   17221 N  N     . GLU   F 2  412 ? -25.375 38.030  -30.932  1.00 32.56  ? 422 GLU   B N     1 
ATOM   17222 C  CA    . GLU   F 2  412 ? -24.404 37.341  -31.759  1.00 31.04  ? 422 GLU   B CA    1 
ATOM   17223 C  C     . GLU   F 2  412 ? -24.790 37.426  -33.225  1.00 33.54  ? 422 GLU   B C     1 
ATOM   17224 O  O     . GLU   F 2  412 ? -23.940 37.672  -34.097  1.00 26.69  ? 422 GLU   B O     1 
ATOM   17225 C  CB    . GLU   F 2  412 ? -24.300 35.876  -31.316  1.00 35.27  ? 422 GLU   B CB    1 
ATOM   17226 C  CG    . GLU   F 2  412 ? -23.181 35.096  -31.990  1.00 31.90  ? 422 GLU   B CG    1 
ATOM   17227 C  CD    . GLU   F 2  412 ? -23.208 33.629  -31.660  1.00 34.95  ? 422 GLU   B CD    1 
ATOM   17228 O  OE1   . GLU   F 2  412 ? -24.305 33.027  -31.646  1.00 44.00  ? 422 GLU   B OE1   1 
ATOM   17229 O  OE2   . GLU   F 2  412 ? -22.131 33.068  -31.424  1.00 34.15  ? 422 GLU   B OE2   1 
ATOM   17230 N  N     . SER   F 2  413 ? -26.080 37.231  -33.517  1.00 33.52  ? 423 SER   B N     1 
ATOM   17231 C  CA    A SER   F 2  413 ? -26.525 37.228  -34.908  0.85 30.97  ? 423 SER   B CA    1 
ATOM   17232 C  CA    B SER   F 2  413 ? -26.522 37.226  -34.908  0.15 30.83  ? 423 SER   B CA    1 
ATOM   17233 C  C     . SER   F 2  413 ? -26.411 38.611  -35.534  1.00 27.43  ? 423 SER   B C     1 
ATOM   17234 O  O     . SER   F 2  413 ? -25.943 38.745  -36.672  1.00 30.25  ? 423 SER   B O     1 
ATOM   17235 C  CB    A SER   F 2  413 ? -27.961 36.720  -35.005  0.85 27.47  ? 423 SER   B CB    1 
ATOM   17236 C  CB    B SER   F 2  413 ? -27.957 36.707  -35.003  0.15 27.81  ? 423 SER   B CB    1 
ATOM   17237 O  OG    A SER   F 2  413 ? -27.987 35.443  -35.584  0.85 27.10  ? 423 SER   B OG    1 
ATOM   17238 O  OG    B SER   F 2  413 ? -28.043 35.371  -34.545  0.15 28.24  ? 423 SER   B OG    1 
ATOM   17239 N  N     . ASN   F 2  414 ? -26.832 39.649  -34.809  1.00 21.87  ? 424 ASN   B N     1 
ATOM   17240 C  CA    . ASN   F 2  414 ? -26.803 40.984  -35.386  1.00 29.83  ? 424 ASN   B CA    1 
ATOM   17241 C  C     . ASN   F 2  414 ? -25.382 41.452  -35.671  1.00 34.86  ? 424 ASN   B C     1 
ATOM   17242 O  O     . ASN   F 2  414 ? -25.161 42.194  -36.636  1.00 30.45  ? 424 ASN   B O     1 
ATOM   17243 C  CB    . ASN   F 2  414 ? -27.492 41.985  -34.476  1.00 28.92  ? 424 ASN   B CB    1 
ATOM   17244 C  CG    . ASN   F 2  414 ? -28.015 43.160  -35.247  1.00 36.53  ? 424 ASN   B CG    1 
ATOM   17245 O  OD1   . ASN   F 2  414 ? -28.117 43.092  -36.475  1.00 40.02  ? 424 ASN   B OD1   1 
ATOM   17246 N  ND2   . ASN   F 2  414 ? -28.369 44.235  -34.550  1.00 33.59  ? 424 ASN   B ND2   1 
ATOM   17247 N  N     . MET   F 2  415 ? -24.412 41.038  -34.850  1.00 26.11  ? 425 MET   B N     1 
ATOM   17248 C  CA    . MET   F 2  415 ? -23.030 41.436  -35.077  1.00 23.63  ? 425 MET   B CA    1 
ATOM   17249 C  C     . MET   F 2  415 ? -22.392 40.610  -36.189  1.00 29.96  ? 425 MET   B C     1 
ATOM   17250 O  O     . MET   F 2  415 ? -21.604 41.145  -36.979  1.00 31.69  ? 425 MET   B O     1 
ATOM   17251 C  CB    . MET   F 2  415 ? -22.233 41.318  -33.776  1.00 24.28  ? 425 MET   B CB    1 
ATOM   17252 C  CG    . MET   F 2  415 ? -20.825 41.871  -33.820  1.00 20.81  ? 425 MET   B CG    1 
ATOM   17253 S  SD    . MET   F 2  415 ? -20.061 41.634  -32.199  1.00 36.35  ? 425 MET   B SD    1 
ATOM   17254 C  CE    . MET   F 2  415 ? -19.905 43.328  -31.747  1.00 21.73  ? 425 MET   B CE    1 
ATOM   17255 N  N     . ASN   F 2  416 ? -22.729 39.316  -36.290  1.00 21.34  ? 426 ASN   B N     1 
ATOM   17256 C  CA    . ASN   F 2  416 ? -22.196 38.533  -37.401  1.00 29.00  ? 426 ASN   B CA    1 
ATOM   17257 C  C     . ASN   F 2  416 ? -22.768 38.999  -38.732  1.00 29.22  ? 426 ASN   B C     1 
ATOM   17258 O  O     . ASN   F 2  416 ? -22.085 38.918  -39.769  1.00 29.22  ? 426 ASN   B O     1 
ATOM   17259 C  CB    . ASN   F 2  416 ? -22.458 37.034  -37.206  1.00 23.80  ? 426 ASN   B CB    1 
ATOM   17260 C  CG    . ASN   F 2  416 ? -21.678 36.461  -36.047  1.00 36.11  ? 426 ASN   B CG    1 
ATOM   17261 O  OD1   . ASN   F 2  416 ? -20.565 36.901  -35.751  1.00 38.80  ? 426 ASN   B OD1   1 
ATOM   17262 N  ND2   . ASN   F 2  416 ? -22.264 35.483  -35.368  1.00 45.16  ? 426 ASN   B ND2   1 
ATOM   17263 N  N     . ASP   F 2  417 ? -24.011 39.486  -38.719  1.00 28.08  ? 427 ASP   B N     1 
ATOM   17264 C  CA    . ASP   F 2  417 ? -24.547 40.164  -39.890  1.00 31.81  ? 427 ASP   B CA    1 
ATOM   17265 C  C     . ASP   F 2  417 ? -23.766 41.434  -40.184  1.00 29.12  ? 427 ASP   B C     1 
ATOM   17266 O  O     . ASP   F 2  417 ? -23.417 41.710  -41.337  1.00 34.97  ? 427 ASP   B O     1 
ATOM   17267 C  CB    . ASP   F 2  417 ? -26.017 40.498  -39.676  1.00 32.66  ? 427 ASP   B CB    1 
ATOM   17268 C  CG    . ASP   F 2  417 ? -26.916 39.296  -39.801  1.00 32.18  ? 427 ASP   B CG    1 
ATOM   17269 O  OD1   . ASP   F 2  417 ? -26.466 38.211  -40.235  1.00 38.63  ? 427 ASP   B OD1   1 
ATOM   17270 O  OD2   . ASP   F 2  417 ? -28.094 39.452  -39.447  1.00 37.28  ? 427 ASP   B OD2   1 
ATOM   17271 N  N     . LEU   F 2  418 ? -23.497 42.230  -39.150  1.00 23.61  ? 428 LEU   B N     1 
ATOM   17272 C  CA    . LEU   F 2  418 ? -22.771 43.472  -39.348  1.00 29.03  ? 428 LEU   B CA    1 
ATOM   17273 C  C     . LEU   F 2  418 ? -21.474 43.203  -40.094  1.00 32.12  ? 428 LEU   B C     1 
ATOM   17274 O  O     . LEU   F 2  418 ? -21.133 43.900  -41.053  1.00 34.31  ? 428 LEU   B O     1 
ATOM   17275 C  CB    . LEU   F 2  418 ? -22.498 44.151  -38.003  1.00 32.66  ? 428 LEU   B CB    1 
ATOM   17276 C  CG    . LEU   F 2  418 ? -21.743 45.481  -38.118  1.00 27.62  ? 428 LEU   B CG    1 
ATOM   17277 C  CD1   . LEU   F 2  418 ? -22.611 46.504  -38.801  1.00 22.27  ? 428 LEU   B CD1   1 
ATOM   17278 C  CD2   . LEU   F 2  418 ? -21.270 45.997  -36.782  1.00 24.10  ? 428 LEU   B CD2   1 
ATOM   17279 N  N     . VAL   F 2  419 ? -20.749 42.173  -39.674  1.00 29.64  ? 429 VAL   B N     1 
ATOM   17280 C  CA    . VAL   F 2  419 ? -19.493 41.846  -40.327  1.00 28.03  ? 429 VAL   B CA    1 
ATOM   17281 C  C     . VAL   F 2  419 ? -19.740 41.458  -41.778  1.00 31.13  ? 429 VAL   B C     1 
ATOM   17282 O  O     . VAL   F 2  419 ? -19.044 41.915  -42.691  1.00 30.76  ? 429 VAL   B O     1 
ATOM   17283 C  CB    . VAL   F 2  419 ? -18.770 40.728  -39.563  1.00 28.95  ? 429 VAL   B CB    1 
ATOM   17284 C  CG1   . VAL   F 2  419 ? -17.650 40.153  -40.438  1.00 28.34  ? 429 VAL   B CG1   1 
ATOM   17285 C  CG2   . VAL   F 2  419 ? -18.234 41.258  -38.244  1.00 26.10  ? 429 VAL   B CG2   1 
ATOM   17286 N  N     . SER   F 2  420 ? -20.731 40.602  -42.016  1.00 31.22  ? 430 SER   B N     1 
ATOM   17287 C  CA    . SER   F 2  420 ? -21.000 40.189  -43.389  1.00 39.85  ? 430 SER   B CA    1 
ATOM   17288 C  C     . SER   F 2  420 ? -21.397 41.381  -44.255  1.00 39.16  ? 430 SER   B C     1 
ATOM   17289 O  O     . SER   F 2  420 ? -21.011 41.463  -45.428  1.00 39.20  ? 430 SER   B O     1 
ATOM   17290 C  CB    . SER   F 2  420 ? -22.073 39.111  -43.404  1.00 29.25  ? 430 SER   B CB    1 
ATOM   17291 O  OG    . SER   F 2  420 ? -22.725 39.112  -42.148  1.00 51.67  ? 430 SER   B OG    1 
ATOM   17292 N  N     . GLU   F 2  421 ? -22.133 42.335  -43.682  1.00 35.45  ? 431 GLU   B N     1 
ATOM   17293 C  CA    . GLU   F 2  421 ? -22.471 43.553  -44.415  1.00 34.59  ? 431 GLU   B CA    1 
ATOM   17294 C  C     . GLU   F 2  421 ? -21.222 44.355  -44.775  1.00 30.85  ? 431 GLU   B C     1 
ATOM   17295 O  O     . GLU   F 2  421 ? -21.113 44.884  -45.881  1.00 38.53  ? 431 GLU   B O     1 
ATOM   17296 C  CB    . GLU   F 2  421 ? -23.441 44.374  -43.580  1.00 36.81  ? 431 GLU   B CB    1 
ATOM   17297 C  CG    . GLU   F 2  421 ? -24.064 45.548  -44.262  1.00 45.17  ? 431 GLU   B CG    1 
ATOM   17298 C  CD    . GLU   F 2  421 ? -25.189 46.107  -43.414  1.00 48.37  ? 431 GLU   B CD    1 
ATOM   17299 O  OE1   . GLU   F 2  421 ? -25.573 45.383  -42.442  1.00 33.70  ? 431 GLU   B OE1   1 
ATOM   17300 O  OE2   . GLU   F 2  421 ? -25.662 47.243  -43.719  1.00 33.18  ? 431 GLU   B OE2   1 
ATOM   17301 N  N     . TYR   F 2  422 ? -20.257 44.434  -43.867  1.00 29.97  ? 432 TYR   B N     1 
ATOM   17302 C  CA    . TYR   F 2  422 ? -19.001 45.100  -44.191  1.00 32.89  ? 432 TYR   B CA    1 
ATOM   17303 C  C     . TYR   F 2  422 ? -18.220 44.352  -45.274  1.00 35.75  ? 432 TYR   B C     1 
ATOM   17304 O  O     . TYR   F 2  422 ? -17.564 44.990  -46.109  1.00 38.00  ? 432 TYR   B O     1 
ATOM   17305 C  CB    . TYR   F 2  422 ? -18.161 45.268  -42.923  1.00 31.48  ? 432 TYR   B CB    1 
ATOM   17306 C  CG    . TYR   F 2  422 ? -18.429 46.545  -42.151  1.00 27.51  ? 432 TYR   B CG    1 
ATOM   17307 C  CD1   . TYR   F 2  422 ? -18.179 47.775  -42.745  1.00 24.07  ? 432 TYR   B CD1   1 
ATOM   17308 C  CD2   . TYR   F 2  422 ? -18.900 46.529  -40.819  1.00 26.34  ? 432 TYR   B CD2   1 
ATOM   17309 C  CE1   . TYR   F 2  422 ? -18.379 48.972  -42.065  1.00 28.16  ? 432 TYR   B CE1   1 
ATOM   17310 C  CE2   . TYR   F 2  422 ? -19.119 47.762  -40.099  1.00 22.97  ? 432 TYR   B CE2   1 
ATOM   17311 C  CZ    . TYR   F 2  422 ? -18.850 48.979  -40.754  1.00 32.31  ? 432 TYR   B CZ    1 
ATOM   17312 O  OH    . TYR   F 2  422 ? -19.021 50.234  -40.162  1.00 34.00  ? 432 TYR   B OH    1 
ATOM   17313 N  N     . GLN   F 2  423 ? -18.298 43.016  -45.298  1.00 36.10  ? 433 GLN   B N     1 
ATOM   17314 C  CA    . GLN   F 2  423 ? -17.579 42.238  -46.309  1.00 39.03  ? 433 GLN   B CA    1 
ATOM   17315 C  C     . GLN   F 2  423 ? -18.237 42.355  -47.687  1.00 40.89  ? 433 GLN   B C     1 
ATOM   17316 O  O     . GLN   F 2  423 ? -17.538 42.437  -48.708  1.00 44.62  ? 433 GLN   B O     1 
ATOM   17317 C  CB    . GLN   F 2  423 ? -17.473 40.771  -45.855  1.00 36.14  ? 433 GLN   B CB    1 
ATOM   17318 C  CG    . GLN   F 2  423 ? -16.700 39.784  -46.789  1.00 33.19  ? 433 GLN   B CG    1 
ATOM   17319 C  CD    . GLN   F 2  423 ? -15.250 40.212  -47.126  1.00 45.05  ? 433 GLN   B CD    1 
ATOM   17320 O  OE1   . GLN   F 2  423 ? -14.601 40.944  -46.370  1.00 38.41  ? 433 GLN   B OE1   1 
ATOM   17321 N  NE2   . GLN   F 2  423 ? -14.755 39.759  -48.281  1.00 43.54  ? 433 GLN   B NE2   1 
ATOM   17322 N  N     . GLN   F 2  424 ? -19.575 42.376  -47.737  1.00 40.44  ? 434 GLN   B N     1 
ATOM   17323 C  CA    . GLN   F 2  424 ? -20.285 42.535  -49.008  1.00 37.84  ? 434 GLN   B CA    1 
ATOM   17324 C  C     . GLN   F 2  424 ? -19.822 43.781  -49.751  1.00 40.53  ? 434 GLN   B C     1 
ATOM   17325 O  O     . GLN   F 2  424 ? -19.688 43.779  -50.982  1.00 41.05  ? 434 GLN   B O     1 
ATOM   17326 C  CB    . GLN   F 2  424 ? -21.799 42.613  -48.765  1.00 37.53  ? 434 GLN   B CB    1 
ATOM   17327 C  CG    . GLN   F 2  424 ? -22.504 43.732  -49.553  1.00 40.43  ? 434 GLN   B CG    1 
ATOM   17328 C  CD    . GLN   F 2  424 ? -23.986 43.913  -49.195  1.00 53.26  ? 434 GLN   B CD    1 
ATOM   17329 O  OE1   . GLN   F 2  424 ? -24.421 43.577  -48.089  1.00 53.19  ? 434 GLN   B OE1   1 
ATOM   17330 N  NE2   . GLN   F 2  424 ? -24.765 44.453  -50.141  1.00 57.88  ? 434 GLN   B NE2   1 
ATOM   17331 N  N     . TYR   F 2  425 ? -19.599 44.863  -49.015  1.00 43.62  ? 435 TYR   B N     1 
ATOM   17332 C  CA    . TYR   F 2  425 ? -19.315 46.147  -49.615  1.00 39.95  ? 435 TYR   B CA    1 
ATOM   17333 C  C     . TYR   F 2  425 ? -17.849 46.325  -49.926  1.00 42.03  ? 435 TYR   B C     1 
ATOM   17334 O  O     . TYR   F 2  425 ? -17.523 47.129  -50.805  1.00 47.05  ? 435 TYR   B O     1 
ATOM   17335 C  CB    . TYR   F 2  425 ? -19.804 47.271  -48.702  1.00 32.69  ? 435 TYR   B CB    1 
ATOM   17336 C  CG    . TYR   F 2  425 ? -21.295 47.448  -48.759  1.00 34.89  ? 435 TYR   B CG    1 
ATOM   17337 C  CD1   . TYR   F 2  425 ? -21.913 47.970  -49.896  1.00 42.13  ? 435 TYR   B CD1   1 
ATOM   17338 C  CD2   . TYR   F 2  425 ? -22.097 47.088  -47.689  1.00 35.71  ? 435 TYR   B CD2   1 
ATOM   17339 C  CE1   . TYR   F 2  425 ? -23.303 48.122  -49.960  1.00 39.02  ? 435 TYR   B CE1   1 
ATOM   17340 C  CE2   . TYR   F 2  425 ? -23.479 47.249  -47.732  1.00 35.44  ? 435 TYR   B CE2   1 
ATOM   17341 C  CZ    . TYR   F 2  425 ? -24.076 47.765  -48.867  1.00 37.05  ? 435 TYR   B CZ    1 
ATOM   17342 O  OH    . TYR   F 2  425 ? -25.445 47.922  -48.897  1.00 41.74  ? 435 TYR   B OH    1 
ATOM   17343 N  N     . GLN   F 2  426 ? -16.968 45.601  -49.231  1.00 40.26  ? 436 GLN   B N     1 
ATOM   17344 C  CA    . GLN   F 2  426 ? -15.552 45.580  -49.577  1.00 39.05  ? 436 GLN   B CA    1 
ATOM   17345 C  C     . GLN   F 2  426 ? -15.287 44.652  -50.746  1.00 44.04  ? 436 GLN   B C     1 
ATOM   17346 O  O     . GLN   F 2  426 ? -14.199 44.699  -51.328  1.00 47.71  ? 436 GLN   B O     1 
ATOM   17347 C  CB    . GLN   F 2  426 ? -14.698 45.205  -48.344  1.00 39.37  ? 436 GLN   B CB    1 
ATOM   17348 C  CG    . GLN   F 2  426 ? -13.851 43.923  -48.406  1.00 38.81  ? 436 GLN   B CG    1 
ATOM   17349 C  CD    . GLN   F 2  426 ? -12.999 43.696  -47.131  1.00 44.22  ? 436 GLN   B CD    1 
ATOM   17350 O  OE1   . GLN   F 2  426 ? -13.095 44.449  -46.148  1.00 38.99  ? 436 GLN   B OE1   1 
ATOM   17351 N  NE2   . GLN   F 2  426 ? -12.158 42.664  -47.158  1.00 35.96  ? 436 GLN   B NE2   1 
ATOM   17352 N  N     . ASP   F 2  427 ? -16.279 43.853  -51.138  1.00 48.89  ? 437 ASP   B N     1 
ATOM   17353 C  CA    . ASP   F 2  427 ? -16.222 43.072  -52.366  1.00 50.04  ? 437 ASP   B CA    1 
ATOM   17354 C  C     . ASP   F 2  427 ? -17.081 43.670  -53.485  1.00 45.61  ? 437 ASP   B C     1 
ATOM   17355 O  O     . ASP   F 2  427 ? -17.584 42.927  -54.331  1.00 60.27  ? 437 ASP   B O     1 
ATOM   17356 C  CB    . ASP   F 2  427 ? -16.633 41.623  -52.087  1.00 48.09  ? 437 ASP   B CB    1 
ATOM   17357 C  CG    . ASP   F 2  427 ? -15.546 40.830  -51.358  1.00 57.79  ? 437 ASP   B CG    1 
ATOM   17358 O  OD1   . ASP   F 2  427 ? -14.435 41.367  -51.149  1.00 58.57  ? 437 ASP   B OD1   1 
ATOM   17359 O  OD2   . ASP   F 2  427 ? -15.798 39.660  -50.994  1.00 70.35  ? 437 ASP   B OD2   1 
ATOM   17360 N  N     . ALA   F 2  428 ? -17.254 44.993  -53.521  1.00 54.91  ? 438 ALA   B N     1 
ATOM   17361 C  CA    . ALA   F 2  428 ? -18.091 45.633  -54.557  1.00 55.60  ? 438 ALA   B CA    1 
ATOM   17362 C  C     . ALA   F 2  428 ? -17.306 46.573  -55.482  1.00 45.23  ? 438 ALA   B C     1 
ATOM   17363 O  O     . ALA   F 2  428 ? -17.462 46.522  -56.713  1.00 56.08  ? 438 ALA   B O     1 
ATOM   17364 C  CB    . ALA   F 2  428 ? -19.265 46.392  -53.909  1.00 39.19  ? 438 ALA   B CB    1 
HETATM 17365 P  PG    . GTP   G 5  .   ? -27.408 74.153  -46.912  0.00 32.11  ? 501 GTP   A PG    1 
HETATM 17366 O  O1G   . GTP   G 5  .   ? -28.075 73.370  -48.017  0.00 31.94  ? 501 GTP   A O1G   1 
HETATM 17367 O  O2G   . GTP   G 5  .   ? -28.214 74.007  -45.643  0.00 32.01  ? 501 GTP   A O2G   1 
HETATM 17368 O  O3G   . GTP   G 5  .   ? -26.008 73.628  -46.696  0.00 32.53  ? 501 GTP   A O3G   1 
HETATM 17369 O  O3B   . GTP   G 5  .   ? -27.350 75.704  -47.348  0.00 32.25  ? 501 GTP   A O3B   1 
HETATM 17370 P  PB    . GTP   G 5  .   ? -26.026 76.285  -48.058  0.00 31.75  ? 501 GTP   A PB    1 
HETATM 17371 O  O1B   . GTP   G 5  .   ? -24.866 76.165  -47.099  0.00 31.84  ? 501 GTP   A O1B   1 
HETATM 17372 O  O2B   . GTP   G 5  .   ? -26.219 77.723  -48.509  0.00 30.89  ? 501 GTP   A O2B   1 
HETATM 17373 O  O3A   . GTP   G 5  .   ? -25.788 75.290  -49.303  0.00 31.34  ? 501 GTP   A O3A   1 
HETATM 17374 P  PA    . GTP   G 5  .   ? -24.421 75.374  -50.150  0.00 31.05  ? 501 GTP   A PA    1 
HETATM 17375 O  O1A   . GTP   G 5  .   ? -23.390 76.144  -49.361  0.00 31.06  ? 501 GTP   A O1A   1 
HETATM 17376 O  O2A   . GTP   G 5  .   ? -24.676 76.025  -51.485  0.00 30.92  ? 501 GTP   A O2A   1 
HETATM 17377 O  "O5'" . GTP   G 5  .   ? -23.930 73.847  -50.324  0.00 31.63  ? 501 GTP   A "O5'" 1 
HETATM 17378 C  "C5'" . GTP   G 5  .   ? -22.560 73.521  -50.456  0.00 32.73  ? 501 GTP   A "C5'" 1 
HETATM 17379 C  "C4'" . GTP   G 5  .   ? -22.061 73.771  -51.876  0.00 32.78  ? 501 GTP   A "C4'" 1 
HETATM 17380 O  "O4'" . GTP   G 5  .   ? -22.358 75.099  -52.251  0.00 31.37  ? 501 GTP   A "O4'" 1 
HETATM 17381 C  "C3'" . GTP   G 5  .   ? -20.553 73.618  -51.984  0.00 34.52  ? 501 GTP   A "C3'" 1 
HETATM 17382 O  "O3'" . GTP   G 5  .   ? -20.218 72.390  -52.588  0.00 37.01  ? 501 GTP   A "O3'" 1 
HETATM 17383 C  "C2'" . GTP   G 5  .   ? -20.097 74.771  -52.855  0.00 31.50  ? 501 GTP   A "C2'" 1 
HETATM 17384 O  "O2'" . GTP   G 5  .   ? -19.724 74.302  -54.130  0.00 30.90  ? 501 GTP   A "O2'" 1 
HETATM 17385 C  "C1'" . GTP   G 5  .   ? -21.296 75.700  -52.965  0.00 30.70  ? 501 GTP   A "C1'" 1 
HETATM 17386 N  N9    . GTP   G 5  .   ? -20.984 76.993  -52.329  0.00 29.72  ? 501 GTP   A N9    1 
HETATM 17387 C  C8    . GTP   G 5  .   ? -21.374 77.378  -51.073  0.00 29.75  ? 501 GTP   A C8    1 
HETATM 17388 N  N7    . GTP   G 5  .   ? -20.913 78.627  -50.841  0.00 29.12  ? 501 GTP   A N7    1 
HETATM 17389 C  C5    . GTP   G 5  .   ? -20.241 79.049  -51.933  0.00 28.71  ? 501 GTP   A C5    1 
HETATM 17390 C  C6    . GTP   G 5  .   ? -19.582 80.238  -52.218  0.00 28.21  ? 501 GTP   A C6    1 
HETATM 17391 O  O6    . GTP   G 5  .   ? -19.545 81.140  -51.383  0.00 28.52  ? 501 GTP   A O6    1 
HETATM 17392 N  N1    . GTP   G 5  .   ? -18.969 80.399  -53.443  0.00 28.00  ? 501 GTP   A N1    1 
HETATM 17393 C  C2    . GTP   G 5  .   ? -19.016 79.380  -54.373  0.00 27.77  ? 501 GTP   A C2    1 
HETATM 17394 N  N2    . GTP   G 5  .   ? -18.424 79.535  -55.555  0.00 27.69  ? 501 GTP   A N2    1 
HETATM 17395 N  N3    . GTP   G 5  .   ? -19.674 78.201  -54.082  0.00 28.03  ? 501 GTP   A N3    1 
HETATM 17396 C  C4    . GTP   G 5  .   ? -20.279 78.035  -52.880  0.00 28.75  ? 501 GTP   A C4    1 
HETATM 17397 MG MG    . MG    H 6  .   ? -25.947 76.274  -45.229  0.00 33.77  ? 502 MG    A MG    1 
HETATM 17398 CA CA    . CA    I 7  .   ? -34.068 107.235 -60.301  0.00 61.60  ? 503 CA    A CA    1 
HETATM 17399 P  PG    . GTP   J 5  .   ? -19.431 17.877  16.339   0.00 26.47  ? 501 GTP   C PG    1 
HETATM 17400 O  O1G   . GTP   J 5  .   ? -18.223 17.579  17.193   0.00 27.43  ? 501 GTP   C O1G   1 
HETATM 17401 O  O2G   . GTP   J 5  .   ? -20.211 16.606  16.102   0.00 26.86  ? 501 GTP   C O2G   1 
HETATM 17402 O  O3G   . GTP   J 5  .   ? -20.307 18.894  17.031   0.00 26.47  ? 501 GTP   C O3G   1 
HETATM 17403 O  O3B   . GTP   J 5  .   ? -18.923 18.467  14.930   0.00 26.43  ? 501 GTP   C O3B   1 
HETATM 17404 P  PB    . GTP   J 5  .   ? -18.209 19.908  14.849   0.00 26.18  ? 501 GTP   C PB    1 
HETATM 17405 O  O1B   . GTP   J 5  .   ? -19.071 20.938  15.536   0.00 26.13  ? 501 GTP   C O1B   1 
HETATM 17406 O  O2B   . GTP   J 5  .   ? -17.940 20.299  13.415   0.00 26.01  ? 501 GTP   C O2B   1 
HETATM 17407 O  O3A   . GTP   J 5  .   ? -16.831 19.738  15.665   0.00 26.94  ? 501 GTP   C O3A   1 
HETATM 17408 P  PA    . GTP   J 5  .   ? -15.452 19.353  14.926   0.00 27.40  ? 501 GTP   C PA    1 
HETATM 17409 O  O1A   . GTP   J 5  .   ? -14.413 18.952  15.945   0.00 28.62  ? 501 GTP   C O1A   1 
HETATM 17410 O  O2A   . GTP   J 5  .   ? -14.984 20.530  14.105   0.00 26.60  ? 501 GTP   C O2A   1 
HETATM 17411 O  "O5'" . GTP   J 5  .   ? -15.787 18.103  13.967   0.00 28.55  ? 501 GTP   C "O5'" 1 
HETATM 17412 C  "C5'" . GTP   J 5  .   ? -14.788 17.145  13.682   0.00 29.74  ? 501 GTP   C "C5'" 1 
HETATM 17413 C  "C4'" . GTP   J 5  .   ? -13.961 17.556  12.468   0.00 30.22  ? 501 GTP   C "C4'" 1 
HETATM 17414 O  "O4'" . GTP   J 5  .   ? -13.740 18.950  12.470   0.00 28.22  ? 501 GTP   C "O4'" 1 
HETATM 17415 C  "C3'" . GTP   J 5  .   ? -12.580 16.923  12.472   0.00 32.34  ? 501 GTP   C "C3'" 1 
HETATM 17416 O  "O3'" . GTP   J 5  .   ? -12.556 15.754  11.687   0.00 35.13  ? 501 GTP   C "O3'" 1 
HETATM 17417 C  "C2'" . GTP   J 5  .   ? -11.675 17.978  11.870   0.00 30.02  ? 501 GTP   C "C2'" 1 
HETATM 17418 O  "O2'" . GTP   J 5  .   ? -11.354 17.643  10.540   0.00 30.74  ? 501 GTP   C "O2'" 1 
HETATM 17419 C  "C1'" . GTP   J 5  .   ? -12.480 19.268  11.907   0.00 28.05  ? 501 GTP   C "C1'" 1 
HETATM 17420 N  N9    . GTP   J 5  .   ? -11.795 20.257  12.759   0.00 27.16  ? 501 GTP   C N9    1 
HETATM 17421 C  C8    . GTP   J 5  .   ? -12.150 20.608  14.035   0.00 27.03  ? 501 GTP   C C8    1 
HETATM 17422 N  N7    . GTP   J 5  .   ? -11.292 21.552  14.480   0.00 26.73  ? 501 GTP   C N7    1 
HETATM 17423 C  C5    . GTP   J 5  .   ? -10.398 21.817  13.504   0.00 26.75  ? 501 GTP   C C5    1 
HETATM 17424 C  C6    . GTP   J 5  .   ? -9.323  22.693  13.438   0.00 27.28  ? 501 GTP   C C6    1 
HETATM 17425 O  O6    . GTP   J 5  .   ? -9.047  23.406  14.401   0.00 27.90  ? 501 GTP   C O6    1 
HETATM 17426 N  N1    . GTP   J 5  .   ? -8.565  22.755  12.287   0.00 27.98  ? 501 GTP   C N1    1 
HETATM 17427 C  C2    . GTP   J 5  .   ? -8.882  21.950  11.212   0.00 27.55  ? 501 GTP   C C2    1 
HETATM 17428 N  N2    . GTP   J 5  .   ? -8.152  22.010  10.101   0.00 28.30  ? 501 GTP   C N2    1 
HETATM 17429 N  N3    . GTP   J 5  .   ? -9.954  21.082  11.285   0.00 27.02  ? 501 GTP   C N3    1 
HETATM 17430 C  C4    . GTP   J 5  .   ? -10.703 21.014  12.413   0.00 26.76  ? 501 GTP   C C4    1 
HETATM 17431 MG MG    . MG    K 6  .   ? -17.980 19.991  18.779   0.00 28.46  ? 502 MG    C MG    1 
HETATM 17432 CA CA    . CA    L 7  .   ? -12.983 53.385  10.489   0.00 44.88  ? 503 CA    C CA    1 
HETATM 17433 P  PB    . GDP   M 8  .   ? -24.555 -11.105 42.463   0.00 57.39  ? 501 GDP   D PB    1 
HETATM 17434 O  O1B   . GDP   M 8  .   ? -23.524 -10.081 42.880   0.00 56.75  ? 501 GDP   D O1B   1 
HETATM 17435 O  O2B   . GDP   M 8  .   ? -25.698 -10.414 41.761   0.00 56.09  ? 501 GDP   D O2B   1 
HETATM 17436 O  O3B   . GDP   M 8  .   ? -25.077 -11.823 43.684   0.00 57.77  ? 501 GDP   D O3B   1 
HETATM 17437 O  O3A   . GDP   M 8  .   ? -23.902 -12.173 41.450   0.00 58.88  ? 501 GDP   D O3A   1 
HETATM 17438 P  PA    . GDP   M 8  .   ? -22.692 -13.128 41.913   0.00 60.46  ? 501 GDP   D PA    1 
HETATM 17439 O  O1A   . GDP   M 8  .   ? -23.086 -13.956 43.113   0.00 61.44  ? 501 GDP   D O1A   1 
HETATM 17440 O  O2A   . GDP   M 8  .   ? -21.455 -12.314 42.201   0.00 60.67  ? 501 GDP   D O2A   1 
HETATM 17441 O  "O5'" . GDP   M 8  .   ? -22.438 -14.061 40.628   0.00 61.43  ? 501 GDP   D "O5'" 1 
HETATM 17442 C  "C5'" . GDP   M 8  .   ? -21.426 -15.063 40.661   0.00 62.73  ? 501 GDP   D "C5'" 1 
HETATM 17443 C  "C4'" . GDP   M 8  .   ? -20.447 -14.782 39.530   0.00 62.76  ? 501 GDP   D "C4'" 1 
HETATM 17444 O  "O4'" . GDP   M 8  .   ? -19.946 -13.454 39.695   0.00 61.75  ? 501 GDP   D "O4'" 1 
HETATM 17445 C  "C3'" . GDP   M 8  .   ? -19.256 -15.725 39.567   0.00 64.85  ? 501 GDP   D "C3'" 1 
HETATM 17446 O  "O3'" . GDP   M 8  .   ? -19.275 -16.585 38.424   0.00 66.73  ? 501 GDP   D "O3'" 1 
HETATM 17447 C  "C2'" . GDP   M 8  .   ? -18.024 -14.843 39.532   0.00 63.45  ? 501 GDP   D "C2'" 1 
HETATM 17448 O  "O2'" . GDP   M 8  .   ? -17.252 -15.119 38.359   0.00 64.01  ? 501 GDP   D "O2'" 1 
HETATM 17449 C  "C1'" . GDP   M 8  .   ? -18.533 -13.412 39.495   0.00 62.14  ? 501 GDP   D "C1'" 1 
HETATM 17450 N  N9    . GDP   M 8  .   ? -17.888 -12.623 40.573   0.00 61.80  ? 501 GDP   D N9    1 
HETATM 17451 C  C8    . GDP   M 8  .   ? -18.318 -12.513 41.844   0.00 61.92  ? 501 GDP   D C8    1 
HETATM 17452 N  N7    . GDP   M 8  .   ? -17.495 -11.716 42.573   0.00 61.97  ? 501 GDP   D N7    1 
HETATM 17453 C  C5    . GDP   M 8  .   ? -16.510 -11.301 41.755   0.00 61.69  ? 501 GDP   D C5    1 
HETATM 17454 C  C6    . GDP   M 8  .   ? -15.311 -10.440 41.875   0.00 62.09  ? 501 GDP   D C6    1 
HETATM 17455 O  O6    . GDP   M 8  .   ? -15.014 -9.892  42.959   0.00 63.26  ? 501 GDP   D O6    1 
HETATM 17456 N  N1    . GDP   M 8  .   ? -14.554 -10.269 40.785   0.00 61.62  ? 501 GDP   D N1    1 
HETATM 17457 C  C2    . GDP   M 8  .   ? -14.844 -10.845 39.603   0.00 60.87  ? 501 GDP   D C2    1 
HETATM 17458 N  N2    . GDP   M 8  .   ? -14.020 -10.615 38.551   0.00 59.97  ? 501 GDP   D N2    1 
HETATM 17459 N  N3    . GDP   M 8  .   ? -15.924 -11.644 39.421   0.00 61.03  ? 501 GDP   D N3    1 
HETATM 17460 C  C4    . GDP   M 8  .   ? -16.775 -11.902 40.440   0.00 61.57  ? 501 GDP   D C4    1 
HETATM 17461 P  PB    . GDP   N 8  .   ? -19.344 49.779  -16.008  0.00 22.37  ? 501 GDP   B PB    1 
HETATM 17462 O  O1B   . GDP   N 8  .   ? -19.176 48.945  -14.761  0.00 21.89  ? 501 GDP   B O1B   1 
HETATM 17463 O  O2B   . GDP   N 8  .   ? -20.730 49.566  -16.571  0.00 21.84  ? 501 GDP   B O2B   1 
HETATM 17464 O  O3B   . GDP   N 8  .   ? -19.160 51.238  -15.663  0.00 23.65  ? 501 GDP   B O3B   1 
HETATM 17465 O  O3A   . GDP   N 8  .   ? -18.237 49.343  -17.094  0.00 22.94  ? 501 GDP   B O3A   1 
HETATM 17466 P  PA    . GDP   N 8  .   ? -16.685 49.243  -16.673  0.00 23.79  ? 501 GDP   B PA    1 
HETATM 17467 O  O1A   . GDP   N 8  .   ? -16.513 48.308  -15.501  0.00 23.43  ? 501 GDP   B O1A   1 
HETATM 17468 O  O2A   . GDP   N 8  .   ? -16.141 50.612  -16.341  0.00 25.24  ? 501 GDP   B O2A   1 
HETATM 17469 O  "O5'" . GDP   N 8  .   ? -15.952 48.652  -17.980  0.00 24.20  ? 501 GDP   B "O5'" 1 
HETATM 17470 C  "C5'" . GDP   N 8  .   ? -14.672 48.032  -17.863  0.00 24.89  ? 501 GDP   B "C5'" 1 
HETATM 17471 C  "C4'" . GDP   N 8  .   ? -13.940 48.084  -19.198  0.00 25.22  ? 501 GDP   B "C4'" 1 
HETATM 17472 O  "O4'" . GDP   N 8  .   ? -13.729 49.450  -19.558  0.00 25.12  ? 501 GDP   B "O4'" 1 
HETATM 17473 C  "C3'" . GDP   N 8  .   ? -12.573 47.423  -19.108  0.00 26.42  ? 501 GDP   B "C3'" 1 
HETATM 17474 O  "O3'" . GDP   N 8  .   ? -12.532 46.265  -19.945  0.00 26.32  ? 501 GDP   B "O3'" 1 
HETATM 17475 C  "C2'" . GDP   N 8  .   ? -11.571 48.451  -19.597  0.00 26.34  ? 501 GDP   B "C2'" 1 
HETATM 17476 O  "O2'" . GDP   N 8  .   ? -10.862 47.945  -20.731  0.00 26.30  ? 501 GDP   B "O2'" 1 
HETATM 17477 C  "C1'" . GDP   N 8  .   ? -12.385 49.672  -19.992  0.00 25.57  ? 501 GDP   B "C1'" 1 
HETATM 17478 N  N9    . GDP   N 8  .   ? -11.851 50.887  -19.328  0.00 25.46  ? 501 GDP   B N9    1 
HETATM 17479 C  C8    . GDP   N 8  .   ? -12.063 51.230  -18.043  0.00 25.86  ? 501 GDP   B C8    1 
HETATM 17480 N  N7    . GDP   N 8  .   ? -11.447 52.401  -17.740  0.00 26.76  ? 501 GDP   B N7    1 
HETATM 17481 C  C5    . GDP   N 8  .   ? -10.823 52.828  -18.853  0.00 25.95  ? 501 GDP   B C5    1 
HETATM 17482 C  C6    . GDP   N 8  .   ? -9.991  53.995  -19.228  0.00 25.88  ? 501 GDP   B C6    1 
HETATM 17483 O  O6    . GDP   N 8  .   ? -9.716  54.885  -18.394  0.00 27.31  ? 501 GDP   B O6    1 
HETATM 17484 N  N1    . GDP   N 8  .   ? -9.537  54.064  -20.486  0.00 25.39  ? 501 GDP   B N1    1 
HETATM 17485 C  C2    . GDP   N 8  .   ? -9.816  53.119  -21.405  0.00 25.01  ? 501 GDP   B C2    1 
HETATM 17486 N  N2    . GDP   N 8  .   ? -9.318  53.267  -22.657  0.00 24.47  ? 501 GDP   B N2    1 
HETATM 17487 N  N3    . GDP   N 8  .   ? -10.573 52.025  -21.132  0.00 25.33  ? 501 GDP   B N3    1 
HETATM 17488 C  C4    . GDP   N 8  .   ? -11.093 51.828  -19.897  0.00 25.45  ? 501 GDP   B C4    1 
HETATM 17489 C  C10   . A1EPS O 9  .   ? -4.506  40.975  -18.542  1.00 29.12  ? 502 A1EPS B C10   1 
HETATM 17490 C  C13   . A1EPS O 9  .   ? -1.288  42.605  -19.012  1.00 25.38  ? 502 A1EPS B C13   1 
HETATM 17491 C  C15   . A1EPS O 9  .   ? -0.023  44.818  -18.054  1.00 26.02  ? 502 A1EPS B C15   1 
HETATM 17492 C  C17   . A1EPS O 9  .   ? 0.628   43.904  -20.473  1.00 24.44  ? 502 A1EPS B C17   1 
HETATM 17493 C  C20   . A1EPS O 9  .   ? -0.079  40.006  -17.092  1.00 25.35  ? 502 A1EPS B C20   1 
HETATM 17494 C  C21   . A1EPS O 9  .   ? -0.491  39.829  -15.599  1.00 35.04  ? 502 A1EPS B C21   1 
HETATM 17495 C  C22   . A1EPS O 9  .   ? -0.818  42.070  -22.699  1.00 31.40  ? 502 A1EPS B C22   1 
HETATM 17496 C  C26   . A1EPS O 9  .   ? -2.348  38.963  -23.561  1.00 46.77  ? 502 A1EPS B C26   1 
HETATM 17497 C  C02   . A1EPS O 9  .   ? -1.706  40.803  -20.744  1.00 28.77  ? 502 A1EPS B C02   1 
HETATM 17498 C  C03   . A1EPS O 9  .   ? -1.201  39.343  -20.564  1.00 28.23  ? 502 A1EPS B C03   1 
HETATM 17499 C  C04   . A1EPS O 9  .   ? -0.434  39.257  -19.383  1.00 29.85  ? 502 A1EPS B C04   1 
HETATM 17500 C  C05   . A1EPS O 9  .   ? -1.105  39.437  -18.103  1.00 27.12  ? 502 A1EPS B C05   1 
HETATM 17501 C  C06   . A1EPS O 9  .   ? -1.538  38.010  -17.428  1.00 27.79  ? 502 A1EPS B C06   1 
HETATM 17502 C  C07   . A1EPS O 9  .   ? -2.832  38.076  -16.579  1.00 27.75  ? 502 A1EPS B C07   1 
HETATM 17503 C  C08   . A1EPS O 9  .   ? -4.046  38.934  -17.202  1.00 31.96  ? 502 A1EPS B C08   1 
HETATM 17504 C  C11   . A1EPS O 9  .   ? -3.432  42.224  -18.925  1.00 27.33  ? 502 A1EPS B C11   1 
HETATM 17505 C  C12   . A1EPS O 9  .   ? -2.151  41.444  -19.236  1.00 23.78  ? 502 A1EPS B C12   1 
HETATM 17506 C  C14   . A1EPS O 9  .   ? -1.071  43.660  -17.891  1.00 24.74  ? 502 A1EPS B C14   1 
HETATM 17507 C  C16   . A1EPS O 9  .   ? 0.826   44.958  -19.348  1.00 20.83  ? 502 A1EPS B C16   1 
HETATM 17508 C  C18   . A1EPS O 9  .   ? -0.394  42.767  -20.266  1.00 18.00  ? 502 A1EPS B C18   1 
HETATM 17509 C  C19   . A1EPS O 9  .   ? -2.211  40.344  -18.103  1.00 31.60  ? 502 A1EPS B C19   1 
HETATM 17510 C  C23   . A1EPS O 9  .   ? -0.488  38.970  -21.989  1.00 27.88  ? 502 A1EPS B C23   1 
HETATM 17511 C  C29   . A1EPS O 9  .   ? 1.585   37.865  -19.496  1.00 37.67  ? 502 A1EPS B C29   1 
HETATM 17512 C  C30   . A1EPS O 9  .   ? 2.268   36.479  -19.653  1.00 37.35  ? 502 A1EPS B C30   1 
HETATM 17513 C  C33   . A1EPS O 9  .   ? 2.739   45.970  -20.438  1.00 31.71  ? 502 A1EPS B C33   1 
HETATM 17514 C  C34   . A1EPS O 9  .   ? -0.866  46.931  -17.601  1.00 28.18  ? 502 A1EPS B C34   1 
HETATM 17515 C  C35   . A1EPS O 9  .   ? -2.335  46.486  -17.978  1.00 28.60  ? 502 A1EPS B C35   1 
HETATM 17516 C  C36   . A1EPS O 9  .   ? -2.964  47.746  -18.670  1.00 24.04  ? 502 A1EPS B C36   1 
HETATM 17517 C  C37   . A1EPS O 9  .   ? -3.587  48.668  -17.583  1.00 31.99  ? 502 A1EPS B C37   1 
HETATM 17518 C  C38   . A1EPS O 9  .   ? -4.591  47.931  -16.647  1.00 36.61  ? 502 A1EPS B C38   1 
HETATM 17519 C  C40   . A1EPS O 9  .   ? -3.265  46.817  -14.625  1.00 28.39  ? 502 A1EPS B C40   1 
HETATM 17520 C  C41   . A1EPS O 9  .   ? -1.779  47.168  -14.634  1.00 26.61  ? 502 A1EPS B C41   1 
HETATM 17521 C  C42   . A1EPS O 9  .   ? -0.976  45.831  -14.615  1.00 35.15  ? 502 A1EPS B C42   1 
HETATM 17522 C  C43   . A1EPS O 9  .   ? -0.963  44.938  -13.556  1.00 28.83  ? 502 A1EPS B C43   1 
HETATM 17523 C  C44   . A1EPS O 9  .   ? -1.676  45.034  -12.172  1.00 30.84  ? 502 A1EPS B C44   1 
HETATM 17524 C  C45   . A1EPS O 9  .   ? -1.482  43.923  -11.199  1.00 31.37  ? 502 A1EPS B C45   1 
HETATM 17525 C  C46   . A1EPS O 9  .   ? -0.605  42.814  -11.614  1.00 32.45  ? 502 A1EPS B C46   1 
HETATM 17526 C  C47   . A1EPS O 9  .   ? 0.093   42.711  -12.923  1.00 32.05  ? 502 A1EPS B C47   1 
HETATM 17527 C  C48   . A1EPS O 9  .   ? -0.136  43.878  -13.909  1.00 28.63  ? 502 A1EPS B C48   1 
HETATM 17528 C  C50   . A1EPS O 9  .   ? -0.168  45.274  -15.642  1.00 25.22  ? 502 A1EPS B C50   1 
HETATM 17529 C  C51   . A1EPS O 9  .   ? 0.116   45.911  -16.983  1.00 23.92  ? 502 A1EPS B C51   1 
HETATM 17530 C  C52   . A1EPS O 9  .   ? -3.260  45.933  -16.894  1.00 27.08  ? 502 A1EPS B C52   1 
HETATM 17531 C  C53   . A1EPS O 9  .   ? -3.617  50.191  -17.755  1.00 37.13  ? 502 A1EPS B C53   1 
HETATM 17532 C  C54   . A1EPS O 9  .   ? -3.823  50.697  -19.220  1.00 25.23  ? 502 A1EPS B C54   1 
HETATM 17533 C  C56   . A1EPS O 9  .   ? 1.585   46.420  -16.815  1.00 31.91  ? 502 A1EPS B C56   1 
HETATM 17534 C  C59   . A1EPS O 9  .   ? 1.147   48.639  -15.662  1.00 33.49  ? 502 A1EPS B C59   1 
HETATM 17535 N  N01   . A1EPS O 9  .   ? -0.733  41.645  -21.303  1.00 23.88  ? 502 A1EPS B N01   1 
HETATM 17536 N  N09   . A1EPS O 9  .   ? -3.647  39.766  -18.318  1.00 31.61  ? 502 A1EPS B N09   1 
HETATM 17537 N  N39   . A1EPS O 9  .   ? -3.857  46.860  -15.952  1.00 32.64  ? 502 A1EPS B N39   1 
HETATM 17538 N  N49   . A1EPS O 9  .   ? 0.355   44.074  -15.183  1.00 26.33  ? 502 A1EPS B N49   1 
HETATM 17539 O  O24   . A1EPS O 9  .   ? 0.641   39.245  -22.264  1.00 31.80  ? 502 A1EPS B O24   1 
HETATM 17540 O  O25   . A1EPS O 9  .   ? -1.259  38.269  -22.963  1.00 35.41  ? 502 A1EPS B O25   1 
HETATM 17541 O  O27   . A1EPS O 9  .   ? -2.286  38.471  -20.456  1.00 33.06  ? 502 A1EPS B O27   1 
HETATM 17542 O  O28   . A1EPS O 9  .   ? 0.191   37.858  -19.301  1.00 28.59  ? 502 A1EPS B O28   1 
HETATM 17543 O  O31   . A1EPS O 9  .   ? 2.186   38.901  -19.551  1.00 34.85  ? 502 A1EPS B O31   1 
HETATM 17544 O  O32   . A1EPS O 9  .   ? 1.734   46.025  -19.441  1.00 29.51  ? 502 A1EPS B O32   1 
HETATM 17545 O  O55   . A1EPS O 9  .   ? -4.730  48.800  -18.414  1.00 48.80  ? 502 A1EPS B O55   1 
HETATM 17546 O  O57   . A1EPS O 9  .   ? 2.502   45.616  -16.832  1.00 28.92  ? 502 A1EPS B O57   1 
HETATM 17547 O  O58   . A1EPS O 9  .   ? 1.823   47.835  -16.667  1.00 47.40  ? 502 A1EPS B O58   1 
HETATM 17548 BR BR60  . A1EPS O 9  .   ? -0.291  41.370  -10.453  1.00 39.88  ? 502 A1EPS B BR60  1 
HETATM 17549 H  H102  . A1EPS O 9  .   ? -5.190  40.800  -19.371  1.00 34.76  ? 502 A1EPS B H102  1 
HETATM 17550 H  H101  . A1EPS O 9  .   ? -5.057  41.217  -17.635  1.00 34.76  ? 502 A1EPS B H101  1 
HETATM 17551 H  H171  . A1EPS O 9  .   ? 1.202   43.968  -21.396  1.00 29.14  ? 502 A1EPS B H171  1 
HETATM 17552 H  H202  . A1EPS O 9  .   ? 0.870   39.499  -17.246  1.00 30.24  ? 502 A1EPS B H202  1 
HETATM 17553 H  H201  . A1EPS O 9  .   ? 0.042   41.068  -17.289  1.00 30.24  ? 502 A1EPS B H201  1 
HETATM 17554 H  H211  . A1EPS O 9  .   ? -0.259  38.814  -15.275  1.00 41.86  ? 502 A1EPS B H211  1 
HETATM 17555 H  H213  . A1EPS O 9  .   ? -1.561  40.007  -15.494  1.00 41.86  ? 502 A1EPS B H213  1 
HETATM 17556 H  H212  . A1EPS O 9  .   ? 0.058   40.541  -14.983  1.00 41.86  ? 502 A1EPS B H212  1 
HETATM 17557 H  H223  . A1EPS O 9  .   ? -1.659  41.575  -23.178  1.00 37.49  ? 502 A1EPS B H223  1 
HETATM 17558 H  H222  . A1EPS O 9  .   ? 0.100   41.805  -23.215  1.00 37.49  ? 502 A1EPS B H222  1 
HETATM 17559 H  H221  . A1EPS O 9  .   ? -0.959  43.147  -22.742  1.00 37.49  ? 502 A1EPS B H221  1 
HETATM 17560 H  H262  . A1EPS O 9  .   ? -2.975  38.255  -24.103  1.00 55.94  ? 502 A1EPS B H262  1 
HETATM 17561 H  H261  . A1EPS O 9  .   ? -1.964  39.712  -24.253  1.00 55.94  ? 502 A1EPS B H261  1 
HETATM 17562 H  H263  . A1EPS O 9  .   ? -2.938  39.451  -22.786  1.00 55.94  ? 502 A1EPS B H263  1 
HETATM 17563 H  H1    . A1EPS O 9  .   ? -2.540  40.836  -21.449  1.00 34.34  ? 502 A1EPS B H1    1 
HETATM 17564 H  H041  . A1EPS O 9  .   ? 0.294   40.064  -19.494  1.00 35.64  ? 502 A1EPS B H041  1 
HETATM 17565 H  H061  . A1EPS O 9  .   ? -0.822  37.196  -17.311  1.00 33.16  ? 502 A1EPS B H061  1 
HETATM 17566 H  H071  . A1EPS O 9  .   ? -2.916  37.572  -15.616  1.00 33.12  ? 502 A1EPS B H071  1 
HETATM 17567 H  H082  . A1EPS O 9  .   ? -4.457  39.575  -16.419  1.00 38.17  ? 502 A1EPS B H082  1 
HETATM 17568 H  H081  . A1EPS O 9  .   ? -4.821  38.244  -17.542  1.00 38.17  ? 502 A1EPS B H081  1 
HETATM 17569 H  H112  . A1EPS O 9  .   ? -3.282  42.875  -18.061  1.00 32.61  ? 502 A1EPS B H112  1 
HETATM 17570 H  H111  . A1EPS O 9  .   ? -3.775  42.763  -19.810  1.00 32.61  ? 502 A1EPS B H111  1 
HETATM 17571 H  H141  . A1EPS O 9  .   ? -1.656  43.595  -16.977  1.00 29.50  ? 502 A1EPS B H141  1 
HETATM 17572 H  H191  . A1EPS O 9  .   ? -2.170  40.766  -17.097  1.00 37.73  ? 502 A1EPS B H191  1 
HETATM 17573 H  H301  . A1EPS O 9  .   ? 1.797   35.765  -18.980  1.00 44.63  ? 502 A1EPS B H301  1 
HETATM 17574 H  H303  . A1EPS O 9  .   ? 3.325   36.566  -19.407  1.00 44.63  ? 502 A1EPS B H303  1 
HETATM 17575 H  H302  . A1EPS O 9  .   ? 2.160   36.136  -20.680  1.00 44.63  ? 502 A1EPS B H302  1 
HETATM 17576 H  H333  . A1EPS O 9  .   ? 3.302   46.903  -20.438  1.00 37.87  ? 502 A1EPS B H333  1 
HETATM 17577 H  H331  . A1EPS O 9  .   ? 2.275   45.825  -21.413  1.00 37.87  ? 502 A1EPS B H331  1 
HETATM 17578 H  H332  . A1EPS O 9  .   ? 3.413   45.139  -20.229  1.00 37.87  ? 502 A1EPS B H332  1 
HETATM 17579 H  H342  . A1EPS O 9  .   ? -0.957  47.752  -16.890  1.00 33.63  ? 502 A1EPS B H342  1 
HETATM 17580 H  H341  . A1EPS O 9  .   ? -0.403  47.301  -18.516  1.00 33.63  ? 502 A1EPS B H341  1 
HETATM 17581 H  H351  . A1EPS O 9  .   ? -2.266  45.624  -18.646  1.00 34.13  ? 502 A1EPS B H351  1 
HETATM 17582 H  H362  . A1EPS O 9  .   ? -3.739  47.430  -19.365  1.00 28.67  ? 502 A1EPS B H362  1 
HETATM 17583 H  H361  . A1EPS O 9  .   ? -2.189  48.290  -19.207  1.00 28.67  ? 502 A1EPS B H361  1 
HETATM 17584 H  H382  . A1EPS O 9  .   ? -5.400  47.502  -17.238  1.00 43.74  ? 502 A1EPS B H382  1 
HETATM 17585 H  H381  . A1EPS O 9  .   ? -5.000  48.631  -15.918  1.00 43.74  ? 502 A1EPS B H381  1 
HETATM 17586 H  H401  . A1EPS O 9  .   ? -3.791  47.528  -13.983  1.00 33.89  ? 502 A1EPS B H401  1 
HETATM 17587 H  H402  . A1EPS O 9  .   ? -3.387  45.811  -14.218  1.00 33.89  ? 502 A1EPS B H402  1 
HETATM 17588 H  H412  . A1EPS O 9  .   ? -1.535  47.755  -13.762  1.00 31.75  ? 502 A1EPS B H412  1 
HETATM 17589 H  H411  . A1EPS O 9  .   ? -1.539  47.728  -15.524  1.00 31.75  ? 502 A1EPS B H411  1 
HETATM 17590 H  H441  . A1EPS O 9  .   ? -2.299  45.891  -11.924  1.00 36.82  ? 502 A1EPS B H441  1 
HETATM 17591 H  H451  . A1EPS O 9  .   ? -1.966  43.931  -10.224  1.00 37.46  ? 502 A1EPS B H451  1 
HETATM 17592 H  H471  . A1EPS O 9  .   ? 0.728   41.863  -13.173  1.00 38.27  ? 502 A1EPS B H471  1 
HETATM 17593 H  H522  . A1EPS O 9  .   ? -2.684  45.207  -16.314  1.00 32.31  ? 502 A1EPS B H522  1 
HETATM 17594 H  H521  . A1EPS O 9  .   ? -4.077  45.411  -17.398  1.00 32.31  ? 502 A1EPS B H521  1 
HETATM 17595 H  H531  . A1EPS O 9  .   ? -2.669  50.589  -17.392  1.00 44.37  ? 502 A1EPS B H531  1 
HETATM 17596 H  H532  . A1EPS O 9  .   ? -4.432  50.582  -17.147  1.00 44.37  ? 502 A1EPS B H532  1 
HETATM 17597 H  H543  . A1EPS O 9  .   ? -2.979  51.324  -19.510  1.00 30.09  ? 502 A1EPS B H543  1 
HETATM 17598 H  H541  . A1EPS O 9  .   ? -4.744  51.277  -19.278  1.00 30.09  ? 502 A1EPS B H541  1 
HETATM 17599 H  H542  . A1EPS O 9  .   ? -3.888  49.843  -19.894  1.00 30.09  ? 502 A1EPS B H542  1 
HETATM 17600 H  H592  . A1EPS O 9  .   ? 1.871   49.287  -15.169  1.00 40.01  ? 502 A1EPS B H592  1 
HETATM 17601 H  H593  . A1EPS O 9  .   ? 0.684   47.985  -14.926  1.00 40.01  ? 502 A1EPS B H593  1 
HETATM 17602 H  H591  . A1EPS O 9  .   ? 0.382   49.249  -16.140  1.00 40.01  ? 502 A1EPS B H591  1 
HETATM 17603 H  H491  . A1EPS O 9  .   ? 0.977   43.461  -15.686  1.00 31.41  ? 502 A1EPS B H491  1 
HETATM 17604 H  H271  . A1EPS O 9  .   ? -2.997  38.768  -21.003  1.00 39.49  ? 502 A1EPS B H271  1 
HETATM 17605 H  H551  . A1EPS O 9  .   ? -5.427  49.267  -17.972  1.00 58.38  ? 502 A1EPS B H551  1 
HETATM 17606 H  H091  . A1EPS O 9  .   ? -3.650  39.185  -19.139  1.00 37.74  ? 502 A1EPS B H091  1 
HETATM 17607 O  O     . HOH   P 10 .   ? -14.114 38.723  -13.703  1.00 35.47  ? 601 HOH   C O     1 
HETATM 17608 O  O     . HOH   P 10 .   ? -7.950  41.591  -12.043  1.00 40.48  ? 602 HOH   C O     1 
HETATM 17609 O  O     . HOH   P 10 .   ? 4.347   41.662  -20.986  1.00 36.43  ? 603 HOH   C O     1 
HETATM 17610 O  O     . HOH   P 10 .   ? -5.932  35.828  -19.727  1.00 32.51  ? 604 HOH   C O     1 
HETATM 17611 O  O     . HOH   Q 10 .   ? 2.191   43.286  -25.182  1.00 37.84  ? 601 HOH   B O     1 
HETATM 17612 O  O     . HOH   Q 10 .   ? -8.509  47.144  -16.232  1.00 25.67  ? 602 HOH   B O     1 
HETATM 17613 O  O     . HOH   Q 10 .   ? -11.028 41.840  -27.390  1.00 26.66  ? 603 HOH   B O     1 
HETATM 17614 O  O     . HOH   Q 10 .   ? -14.418 47.684  -22.929  1.00 21.08  ? 604 HOH   B O     1 
HETATM 17615 O  O     . HOH   Q 10 .   ? -6.138  44.677  -15.869  1.00 29.84  ? 605 HOH   B O     1 
# 
