data_8YEU
# 
_entry.id   8YEU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YEU         pdb_00008yeu 10.2210/pdb8yeu/pdb 
WWPDB D_1300045525 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YEU 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-23 
_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         Yuxi 
_pdbx_contact_author.name_last          Wang 
_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 ? 
# 
_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                     'Tubulin-RB3_SLD-TTL in complex with compound 2NH2' 
_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 ? 
# 
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'                                        48966.324 2 ?        ? ? ? 
2  polymer     man 'Tubulin beta chain'                                                          48391.410 2 ?        ? ? ? 
3  polymer     man Stathmin-4                                                                    16844.162 1 ?        ? ? ? 
4  polymer     man 'Tubulin--tyrosine ligase'                                                    43825.914 1 6.3.2.25 ? ? ? 
5  non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                                                   523.180   2 ?        ? ? ? 
6  non-polymer syn 'CALCIUM ION'                                                                 40.078    2 ?        ? ? ? 
7  non-polymer syn 'MAGNESIUM ION'                                                               24.305    3 ?        ? ? ? 
8  non-polymer syn '6-fluoranyl-4-(6-methoxy-3,4-dihydro-2~{H}-quinolin-1-yl)quinazolin-2-amine' 324.352   2 ?        ? ? ? 
9  non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                                                    443.201   2 ?        ? ? ? 
10 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                        195.237   2 ?        ? ? ? 
11 non-polymer syn 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                505.208   1 ?        ? ? ? 
# 
_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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
A,C ? 
2 'polypeptide(L)' no no 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
B,D ? 
3 'polypeptide(L)' no no 
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
E   ? 
4 'polypeptide(L)' no no 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHH
;
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHH
;
F   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5  "GUANOSINE-5'-TRIPHOSPHATE"                                                   GTP   
6  'CALCIUM ION'                                                                 CA    
7  'MAGNESIUM ION'                                                               MG    
8  '6-fluoranyl-4-(6-methoxy-3,4-dihydro-2~{H}-quinolin-1-yl)quinazolin-2-amine' A1D6L 
9  "GUANOSINE-5'-DIPHOSPHATE"                                                    GDP   
10 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                        MES   
11 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                ACP   
# 
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 
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 
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 
# 
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' 1 440 pig          ? TUBA1B ? ? ? ? ? ? 'Sus scrofa'        9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 431 pig          ? TUBB2B ? ? ? ? ? ? 'Sus scrofa'        9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 143 'Norway rat' ? Stmn4  ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 380 chicken      ? ?      ? ? ? ? ? ? '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 
A1D6L non-polymer         . '6-fluoranyl-4-(6-methoxy-3,4-dihydro-2~{H}-quinolin-1-yl)quinazolin-2-amine' ? 'C18 H17 F N4 O'    
324.352 
ACP   non-polymer         . 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                
;ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
;
'C11 H18 N5 O12 P3' 505.208 
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 
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 
MES   non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                        ? 'C6 H13 N O4 S'     
195.237 
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 ?   ?   ?   A . n 
A 1 439 SER 439 439 ?   ?   ?   A . n 
A 1 440 VAL 440 440 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ARG 2   2   2   ARG ARG B . n 
B 2 3   GLU 3   3   3   GLU GLU B . n 
B 2 4   ILE 4   4   4   ILE ILE B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   HIS 6   6   6   HIS HIS B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   GLN 8   8   8   GLN GLN B . n 
B 2 9   ALA 9   9   9   ALA ALA B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLN 11  11  11  GLN GLN B . n 
B 2 12  CYS 12  12  12  CYS CYS B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  ASN 14  14  14  ASN ASN B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  GLY 17  17  17  GLY GLY B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  PHE 20  20  20  PHE PHE B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  ILE 24  24  24  ILE ILE B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  ASP 26  26  26  ASP ASP B . n 
B 2 27  GLU 27  27  27  GLU GLU B . n 
B 2 28  HIS 28  28  28  HIS HIS B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ILE 30  30  30  ILE ILE B . n 
B 2 31  ASP 31  31  31  ASP ASP B . n 
B 2 32  PRO 32  32  32  PRO PRO B . n 
B 2 33  THR 33  33  33  THR THR B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  SER 35  35  35  SER SER B . n 
B 2 36  TYR 36  36  36  TYR TYR B . n 
B 2 37  HIS 37  37  37  HIS HIS B . n 
B 2 38  GLY 38  38  38  GLY GLY B . n 
B 2 39  ASP 39  39  39  ASP ASP B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  LEU 42  42  42  LEU LEU B . n 
B 2 43  GLN 43  43  43  GLN GLN B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  GLU 45  45  45  GLU GLU B . n 
B 2 46  ARG 46  46  46  ARG ARG B . n 
B 2 47  ILE 47  47  47  ILE ILE B . n 
B 2 48  ASN 48  48  48  ASN ASN B . n 
B 2 49  VAL 49  49  49  VAL VAL B . n 
B 2 50  TYR 50  50  50  TYR TYR B . n 
B 2 51  TYR 51  51  51  TYR TYR B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  GLU 53  53  53  GLU GLU B . n 
B 2 54  ALA 54  54  54  ALA ALA B . n 
B 2 55  THR 55  55  55  THR THR B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  ARG 62  62  62  ARG ARG B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  LEU 65  65  65  LEU LEU B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PRO 70  70  70  PRO PRO B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  THR 72  72  72  THR THR B . n 
B 2 73  MET 73  73  73  MET MET B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  SER 75  75  75  SER SER B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  ARG 77  77  77  ARG ARG B . n 
B 2 78  SER 78  78  78  SER SER B . n 
B 2 79  GLY 79  79  79  GLY GLY B . n 
B 2 80  PRO 80  80  80  PRO PRO B . n 
B 2 81  PHE 81  81  81  PHE PHE B . n 
B 2 82  GLY 82  82  82  GLY GLY B . n 
B 2 83  GLN 83  83  83  GLN GLN B . n 
B 2 84  ILE 84  84  84  ILE ILE B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  ASP 88  88  88  ASP ASP B . n 
B 2 89  ASN 89  89  89  ASN ASN B . n 
B 2 90  PHE 90  90  90  PHE PHE B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  PHE 92  92  92  PHE PHE B . n 
B 2 93  GLY 93  93  93  GLY GLY B . n 
B 2 94  GLN 94  94  94  GLN GLN B . n 
B 2 95  SER 95  95  95  SER SER B . n 
B 2 96  GLY 96  96  96  GLY GLY B . n 
B 2 97  ALA 97  97  97  ALA ALA B . n 
B 2 98  GLY 98  98  98  GLY GLY B . n 
B 2 99  ASN 99  99  99  ASN ASN B . n 
B 2 100 ASN 100 100 100 ASN ASN B . n 
B 2 101 TRP 101 101 101 TRP TRP B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 LYS 103 103 103 LYS LYS B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 HIS 105 105 105 HIS HIS B . n 
B 2 106 TYR 106 106 106 TYR TYR B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 GLU 108 108 108 GLU GLU B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 ALA 110 110 110 ALA ALA B . n 
B 2 111 GLU 111 111 111 GLU GLU B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 ASP 114 114 114 ASP ASP B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 LEU 117 117 117 LEU LEU B . n 
B 2 118 ASP 118 118 118 ASP ASP B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 VAL 120 120 120 VAL VAL B . n 
B 2 121 ARG 121 121 121 ARG ARG B . n 
B 2 122 LYS 122 122 122 LYS LYS B . n 
B 2 123 GLU 123 123 123 GLU GLU B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 GLU 125 125 125 GLU GLU B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 CYS 127 127 127 CYS CYS B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 CYS 129 129 129 CYS CYS B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 GLY 132 132 132 GLY GLY B . n 
B 2 133 PHE 133 133 133 PHE PHE B . n 
B 2 134 GLN 134 134 134 GLN GLN B . n 
B 2 135 LEU 135 135 135 LEU LEU B . n 
B 2 136 THR 136 136 136 THR THR B . n 
B 2 137 HIS 137 137 137 HIS HIS B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 LEU 139 139 139 LEU LEU B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 GLY 141 141 141 GLY GLY B . n 
B 2 142 GLY 142 142 142 GLY GLY B . n 
B 2 143 THR 143 143 143 THR THR B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 SER 145 145 145 SER SER B . n 
B 2 146 GLY 146 146 146 GLY GLY B . n 
B 2 147 MET 147 147 147 MET MET B . n 
B 2 148 GLY 148 148 148 GLY GLY B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 LEU 151 151 151 LEU LEU B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 SER 153 153 153 SER SER B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 ILE 155 155 155 ILE ILE B . n 
B 2 156 ARG 156 156 156 ARG ARG B . n 
B 2 157 GLU 157 157 157 GLU GLU B . n 
B 2 158 GLU 158 158 158 GLU GLU B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 ASP 161 161 161 ASP ASP B . n 
B 2 162 ARG 162 162 162 ARG ARG B . n 
B 2 163 ILE 163 163 163 ILE ILE B . n 
B 2 164 MET 164 164 164 MET MET B . n 
B 2 165 ASN 165 165 165 ASN ASN B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 PHE 167 167 167 PHE PHE B . n 
B 2 168 SER 168 168 168 SER SER B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 MET 170 170 170 MET MET B . n 
B 2 171 PRO 171 171 171 PRO PRO B . n 
B 2 172 SER 172 172 172 SER SER B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 LYS 174 174 174 LYS LYS B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 SER 176 176 176 SER SER B . n 
B 2 177 ASP 177 177 177 ASP ASP B . n 
B 2 178 THR 178 178 178 THR THR B . n 
B 2 179 VAL 179 179 179 VAL VAL B . n 
B 2 180 VAL 180 180 180 VAL VAL B . n 
B 2 181 GLU 181 181 181 GLU GLU B . n 
B 2 182 PRO 182 182 182 PRO PRO B . n 
B 2 183 TYR 183 183 183 TYR TYR B . n 
B 2 184 ASN 184 184 184 ASN ASN B . n 
B 2 185 ALA 185 185 185 ALA ALA B . n 
B 2 186 THR 186 186 186 THR THR B . n 
B 2 187 LEU 187 187 187 LEU LEU B . n 
B 2 188 SER 188 188 188 SER SER B . n 
B 2 189 VAL 189 189 189 VAL VAL B . n 
B 2 190 HIS 190 190 190 HIS HIS B . n 
B 2 191 GLN 191 191 191 GLN GLN B . n 
B 2 192 LEU 192 192 192 LEU LEU B . n 
B 2 193 VAL 193 193 193 VAL VAL B . n 
B 2 194 GLU 194 194 194 GLU GLU B . n 
B 2 195 ASN 195 195 195 ASN ASN B . n 
B 2 196 THR 196 196 196 THR THR B . n 
B 2 197 ASP 197 197 197 ASP ASP B . n 
B 2 198 GLU 198 198 198 GLU GLU B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 CYS 201 201 201 CYS CYS B . n 
B 2 202 ILE 202 202 202 ILE ILE B . n 
B 2 203 ASP 203 203 203 ASP ASP B . n 
B 2 204 ASN 204 204 204 ASN ASN B . n 
B 2 205 GLU 205 205 205 GLU GLU B . n 
B 2 206 ALA 206 206 206 ALA ALA B . n 
B 2 207 LEU 207 207 207 LEU LEU B . n 
B 2 208 TYR 208 208 208 TYR TYR B . n 
B 2 209 ASP 209 209 209 ASP ASP B . n 
B 2 210 ILE 210 210 210 ILE ILE B . n 
B 2 211 CYS 211 211 211 CYS CYS B . n 
B 2 212 PHE 212 212 212 PHE PHE B . n 
B 2 213 ARG 213 213 213 ARG ARG B . n 
B 2 214 THR 214 214 214 THR THR B . n 
B 2 215 LEU 215 215 215 LEU LEU B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 LEU 217 217 217 LEU LEU B . n 
B 2 218 THR 218 218 218 THR THR B . n 
B 2 219 THR 219 219 219 THR THR B . n 
B 2 220 PRO 220 220 220 PRO PRO B . n 
B 2 221 THR 221 221 221 THR THR B . n 
B 2 222 TYR 222 222 222 TYR TYR B . n 
B 2 223 GLY 223 223 223 GLY GLY B . n 
B 2 224 ASP 224 224 224 ASP ASP B . n 
B 2 225 LEU 225 225 225 LEU LEU B . n 
B 2 226 ASN 226 226 226 ASN ASN B . n 
B 2 227 HIS 227 227 227 HIS HIS B . n 
B 2 228 LEU 228 228 228 LEU LEU B . n 
B 2 229 VAL 229 229 229 VAL VAL B . n 
B 2 230 SER 230 230 230 SER SER B . n 
B 2 231 ALA 231 231 231 ALA ALA B . n 
B 2 232 THR 232 232 232 THR THR B . n 
B 2 233 MET 233 233 233 MET MET B . n 
B 2 234 SER 234 234 234 SER SER B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 VAL 236 236 236 VAL VAL B . n 
B 2 237 THR 237 237 237 THR THR B . n 
B 2 238 THR 238 238 238 THR THR B . n 
B 2 239 CYS 239 239 239 CYS CYS B . n 
B 2 240 LEU 240 240 240 LEU LEU B . n 
B 2 241 ARG 241 241 241 ARG ARG B . n 
B 2 242 PHE 242 242 242 PHE PHE B . n 
B 2 243 PRO 243 243 243 PRO PRO B . n 
B 2 244 GLY 244 244 244 GLY GLY B . n 
B 2 245 GLN 245 245 245 GLN GLN B . n 
B 2 246 LEU 246 246 246 LEU LEU B . n 
B 2 247 ASN 247 247 247 ASN ASN B . n 
B 2 248 ALA 248 248 248 ALA ALA B . n 
B 2 249 ASP 249 249 249 ASP ASP B . n 
B 2 250 LEU 250 250 250 LEU LEU B . n 
B 2 251 ARG 251 251 251 ARG ARG B . n 
B 2 252 LYS 252 252 252 LYS LYS B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 ALA 254 254 254 ALA ALA B . n 
B 2 255 VAL 255 255 255 VAL VAL B . n 
B 2 256 ASN 256 256 256 ASN ASN B . n 
B 2 257 MET 257 257 257 MET MET B . n 
B 2 258 VAL 258 258 258 VAL VAL B . n 
B 2 259 PRO 259 259 259 PRO PRO B . n 
B 2 260 PHE 260 260 260 PHE PHE B . n 
B 2 261 PRO 261 261 261 PRO PRO B . n 
B 2 262 ARG 262 262 262 ARG ARG B . n 
B 2 263 LEU 263 263 263 LEU LEU B . n 
B 2 264 HIS 264 264 264 HIS HIS B . n 
B 2 265 PHE 265 265 265 PHE PHE B . n 
B 2 266 PHE 266 266 266 PHE PHE B . n 
B 2 267 MET 267 267 267 MET MET B . n 
B 2 268 PRO 268 268 268 PRO PRO B . n 
B 2 269 GLY 269 269 269 GLY GLY B . n 
B 2 270 PHE 270 270 270 PHE PHE B . n 
B 2 271 ALA 271 271 271 ALA ALA B . n 
B 2 272 PRO 272 272 272 PRO PRO B . n 
B 2 273 LEU 273 273 273 LEU LEU B . n 
B 2 274 THR 274 274 274 THR THR B . n 
B 2 275 SER 275 275 275 SER SER B . n 
B 2 276 ARG 276 276 276 ARG ARG B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 SER 278 278 278 SER SER B . n 
B 2 279 GLN 279 279 279 GLN GLN B . n 
B 2 280 GLN 280 280 280 GLN GLN B . n 
B 2 281 TYR 281 281 281 TYR TYR B . n 
B 2 282 ARG 282 282 282 ARG ARG B . n 
B 2 283 ALA 283 283 283 ALA ALA B . n 
B 2 284 LEU 284 284 284 LEU LEU B . n 
B 2 285 THR 285 285 285 THR THR B . n 
B 2 286 VAL 286 286 286 VAL VAL B . n 
B 2 287 PRO 287 287 287 PRO PRO B . n 
B 2 288 GLU 288 288 288 GLU GLU B . n 
B 2 289 LEU 289 289 289 LEU LEU B . n 
B 2 290 THR 290 290 290 THR THR B . n 
B 2 291 GLN 291 291 291 GLN GLN B . n 
B 2 292 GLN 292 292 292 GLN GLN B . n 
B 2 293 MET 293 293 293 MET MET B . n 
B 2 294 PHE 294 294 294 PHE PHE B . n 
B 2 295 ASP 295 295 295 ASP ASP B . n 
B 2 296 SER 296 296 296 SER SER B . n 
B 2 297 LYS 297 297 297 LYS LYS B . n 
B 2 298 ASN 298 298 298 ASN ASN B . n 
B 2 299 MET 299 299 299 MET MET B . n 
B 2 300 MET 300 300 300 MET MET B . n 
B 2 301 ALA 301 301 301 ALA ALA B . n 
B 2 302 ALA 302 302 302 ALA ALA B . n 
B 2 303 CYS 303 303 303 CYS CYS B . n 
B 2 304 ASP 304 304 304 ASP ASP B . n 
B 2 305 PRO 305 305 305 PRO PRO B . n 
B 2 306 ARG 306 306 306 ARG ARG B . n 
B 2 307 HIS 307 307 307 HIS HIS B . n 
B 2 308 GLY 308 308 308 GLY GLY B . n 
B 2 309 ARG 309 309 309 ARG ARG B . n 
B 2 310 TYR 310 310 310 TYR TYR B . n 
B 2 311 LEU 311 311 311 LEU LEU B . n 
B 2 312 THR 312 312 312 THR THR B . n 
B 2 313 VAL 313 313 313 VAL VAL B . n 
B 2 314 ALA 314 314 314 ALA ALA B . n 
B 2 315 ALA 315 315 315 ALA ALA B . n 
B 2 316 ILE 316 316 316 ILE ILE B . n 
B 2 317 PHE 317 317 317 PHE PHE B . n 
B 2 318 ARG 318 318 318 ARG ARG B . n 
B 2 319 GLY 319 319 319 GLY GLY B . n 
B 2 320 ARG 320 320 320 ARG ARG B . n 
B 2 321 MET 321 321 321 MET MET B . n 
B 2 322 SER 322 322 322 SER SER B . n 
B 2 323 MET 323 323 323 MET MET B . n 
B 2 324 LYS 324 324 324 LYS LYS B . n 
B 2 325 GLU 325 325 325 GLU GLU B . n 
B 2 326 VAL 326 326 326 VAL VAL B . n 
B 2 327 ASP 327 327 327 ASP ASP B . n 
B 2 328 GLU 328 328 328 GLU GLU B . n 
B 2 329 GLN 329 329 329 GLN GLN B . n 
B 2 330 MET 330 330 330 MET MET B . n 
B 2 331 LEU 331 331 331 LEU LEU B . n 
B 2 332 ASN 332 332 332 ASN ASN B . n 
B 2 333 VAL 333 333 333 VAL VAL B . n 
B 2 334 GLN 334 334 334 GLN GLN B . n 
B 2 335 ASN 335 335 335 ASN ASN B . n 
B 2 336 LYS 336 336 336 LYS LYS B . n 
B 2 337 ASN 337 337 337 ASN ASN B . n 
B 2 338 SER 338 338 338 SER SER B . n 
B 2 339 SER 339 339 339 SER SER B . n 
B 2 340 TYR 340 340 340 TYR TYR B . n 
B 2 341 PHE 341 341 341 PHE PHE B . n 
B 2 342 VAL 342 342 342 VAL VAL B . n 
B 2 343 GLU 343 343 343 GLU GLU B . n 
B 2 344 TRP 344 344 344 TRP TRP B . n 
B 2 345 ILE 345 345 345 ILE ILE B . n 
B 2 346 PRO 346 346 346 PRO PRO B . n 
B 2 347 ASN 347 347 347 ASN ASN B . n 
B 2 348 ASN 348 348 348 ASN ASN B . n 
B 2 349 VAL 349 349 349 VAL VAL B . n 
B 2 350 LYS 350 350 350 LYS LYS B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 ALA 352 352 352 ALA ALA B . n 
B 2 353 VAL 353 353 353 VAL VAL B . n 
B 2 354 CYS 354 354 354 CYS CYS B . n 
B 2 355 ASP 355 355 355 ASP ASP B . n 
B 2 356 ILE 356 356 356 ILE ILE B . n 
B 2 357 PRO 357 357 357 PRO PRO B . n 
B 2 358 PRO 358 358 358 PRO PRO B . n 
B 2 359 ARG 359 359 359 ARG ARG B . n 
B 2 360 GLY 360 360 360 GLY GLY B . n 
B 2 361 LEU 361 361 361 LEU LEU B . n 
B 2 362 LYS 362 362 362 LYS LYS B . n 
B 2 363 MET 363 363 363 MET MET B . n 
B 2 364 SER 364 364 364 SER SER B . n 
B 2 365 ALA 365 365 365 ALA ALA B . n 
B 2 366 THR 366 366 366 THR THR B . n 
B 2 367 PHE 367 367 367 PHE PHE B . n 
B 2 368 ILE 368 368 368 ILE ILE B . n 
B 2 369 GLY 369 369 369 GLY GLY B . n 
B 2 370 ASN 370 370 370 ASN ASN B . n 
B 2 371 SER 371 371 371 SER SER B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 ALA 373 373 373 ALA ALA B . n 
B 2 374 ILE 374 374 374 ILE ILE B . n 
B 2 375 GLN 375 375 375 GLN GLN B . n 
B 2 376 GLU 376 376 376 GLU GLU B . n 
B 2 377 LEU 377 377 377 LEU LEU B . n 
B 2 378 PHE 378 378 378 PHE PHE B . n 
B 2 379 LYS 379 379 379 LYS LYS B . n 
B 2 380 ARG 380 380 380 ARG ARG B . n 
B 2 381 ILE 381 381 381 ILE ILE B . n 
B 2 382 SER 382 382 382 SER SER B . n 
B 2 383 GLU 383 383 383 GLU GLU B . n 
B 2 384 GLN 384 384 384 GLN GLN B . n 
B 2 385 PHE 385 385 385 PHE PHE B . n 
B 2 386 THR 386 386 386 THR THR B . n 
B 2 387 ALA 387 387 387 ALA ALA B . n 
B 2 388 MET 388 388 388 MET MET B . n 
B 2 389 PHE 389 389 389 PHE PHE B . n 
B 2 390 ARG 390 390 390 ARG ARG B . n 
B 2 391 ARG 391 391 391 ARG ARG B . n 
B 2 392 LYS 392 392 392 LYS LYS B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 PHE 394 394 394 PHE PHE B . n 
B 2 395 LEU 395 395 395 LEU LEU B . n 
B 2 396 HIS 396 396 396 HIS HIS B . n 
B 2 397 TRP 397 397 397 TRP TRP B . n 
B 2 398 TYR 398 398 398 TYR TYR B . n 
B 2 399 THR 399 399 399 THR THR B . n 
B 2 400 GLY 400 400 400 GLY GLY B . n 
B 2 401 GLU 401 401 401 GLU GLU B . n 
B 2 402 GLY 402 402 402 GLY GLY B . n 
B 2 403 MET 403 403 403 MET MET B . n 
B 2 404 ASP 404 404 404 ASP ASP B . n 
B 2 405 GLU 405 405 405 GLU GLU B . n 
B 2 406 MET 406 406 406 MET MET B . n 
B 2 407 GLU 407 407 407 GLU GLU B . n 
B 2 408 PHE 408 408 408 PHE PHE B . n 
B 2 409 THR 409 409 409 THR THR B . n 
B 2 410 GLU 410 410 410 GLU GLU B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 GLU 412 412 412 GLU GLU B . n 
B 2 413 SER 413 413 413 SER SER B . n 
B 2 414 ASN 414 414 414 ASN ASN B . n 
B 2 415 MET 415 415 415 MET MET B . n 
B 2 416 ASN 416 416 416 ASN ASN B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 LEU 418 418 418 LEU LEU B . n 
B 2 419 VAL 419 419 419 VAL VAL B . n 
B 2 420 SER 420 420 420 SER SER B . n 
B 2 421 GLU 421 421 421 GLU GLU B . n 
B 2 422 TYR 422 422 422 TYR TYR B . n 
B 2 423 GLN 423 423 423 GLN GLN B . n 
B 2 424 GLN 424 424 424 GLN GLN B . n 
B 2 425 TYR 425 425 425 TYR TYR B . n 
B 2 426 GLN 426 426 426 GLN GLN B . n 
B 2 427 ASP 427 427 427 ASP ASP B . n 
B 2 428 ALA 428 428 428 ALA ALA B . n 
B 2 429 THR 429 429 ?   ?   ?   B . n 
B 2 430 ALA 430 430 ?   ?   ?   B . n 
B 2 431 ASP 431 431 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   ARG 2   2   2   ARG ARG C . n 
C 1 3   GLU 3   3   3   GLU GLU C . n 
C 1 4   CYS 4   4   4   CYS CYS C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   SER 6   6   6   SER SER C . n 
C 1 7   ILE 7   7   7   ILE ILE C . n 
C 1 8   HIS 8   8   8   HIS HIS C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  GLN 11  11  11  GLN GLN C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  GLY 13  13  13  GLY GLY C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  ILE 16  16  16  ILE ILE C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  ASN 18  18  18  ASN ASN C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  CYS 20  20  20  CYS CYS C . n 
C 1 21  TRP 21  21  21  TRP TRP C . n 
C 1 22  GLU 22  22  22  GLU GLU C . n 
C 1 23  LEU 23  23  23  LEU LEU C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  CYS 25  25  25  CYS CYS C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  HIS 28  28  28  HIS HIS C . n 
C 1 29  GLY 29  29  29  GLY GLY C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  PRO 32  32  32  PRO PRO C . n 
C 1 33  ASP 33  33  33  ASP ASP C . n 
C 1 34  GLY 34  34  34  GLY GLY C . n 
C 1 35  GLN 35  35  35  GLN GLN C . n 
C 1 36  MET 36  36  36  MET MET C . n 
C 1 37  PRO 37  37  37  PRO PRO C . n 
C 1 38  SER 38  38  38  SER SER C . n 
C 1 39  ASP 39  39  39  ASP ASP C . n 
C 1 40  LYS 40  40  40  LYS LYS C . n 
C 1 41  THR 41  41  41  THR THR C . n 
C 1 42  ILE 42  42  42  ILE ILE C . n 
C 1 43  GLY 43  43  43  GLY GLY C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  ASP 46  46  46  ASP ASP C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  PHE 49  49  49  PHE PHE C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  THR 51  51  51  THR THR C . n 
C 1 52  PHE 52  52  52  PHE PHE C . n 
C 1 53  PHE 53  53  53  PHE PHE C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  GLU 55  55  55  GLU GLU C . n 
C 1 56  THR 56  56  56  THR THR C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  ALA 58  58  58  ALA ALA C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  HIS 61  61  61  HIS HIS C . n 
C 1 62  VAL 62  62  62  VAL VAL C . n 
C 1 63  PRO 63  63  63  PRO PRO C . n 
C 1 64  ARG 64  64  64  ARG ARG C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  PHE 67  67  67  PHE PHE C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  GLU 71  71  71  GLU GLU C . n 
C 1 72  PRO 72  72  72  PRO PRO C . n 
C 1 73  THR 73  73  73  THR THR C . n 
C 1 74  VAL 74  74  74  VAL VAL C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  THR 80  80  80  THR THR C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  THR 82  82  82  THR THR C . n 
C 1 83  TYR 83  83  83  TYR TYR C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  GLN 85  85  85  GLN GLN C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  PHE 87  87  87  PHE PHE C . n 
C 1 88  HIS 88  88  88  HIS HIS C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  GLU 90  90  90  GLU GLU C . n 
C 1 91  GLN 91  91  91  GLN GLN C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  ILE 93  93  93  ILE ILE C . n 
C 1 94  THR 94  94  94  THR THR C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  LYS 96  96  96  LYS LYS C . n 
C 1 97  GLU 97  97  97  GLU GLU C . n 
C 1 98  ASP 98  98  98  ASP ASP C . n 
C 1 99  ALA 99  99  99  ALA ALA C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 ASN 101 101 101 ASN ASN C . n 
C 1 102 ASN 102 102 102 ASN ASN C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 ALA 104 104 104 ALA ALA C . n 
C 1 105 ARG 105 105 105 ARG ARG C . n 
C 1 106 GLY 106 106 106 GLY GLY C . n 
C 1 107 HIS 107 107 107 HIS HIS C . n 
C 1 108 TYR 108 108 108 TYR TYR C . n 
C 1 109 THR 109 109 109 THR THR C . n 
C 1 110 ILE 110 110 110 ILE ILE C . n 
C 1 111 GLY 111 111 111 GLY GLY C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 ILE 114 114 114 ILE ILE C . n 
C 1 115 ILE 115 115 115 ILE ILE C . n 
C 1 116 ASP 116 116 116 ASP ASP C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 ASP 120 120 120 ASP ASP C . n 
C 1 121 ARG 121 121 121 ARG ARG C . n 
C 1 122 ILE 122 122 122 ILE ILE C . n 
C 1 123 ARG 123 123 123 ARG ARG C . n 
C 1 124 LYS 124 124 124 LYS LYS C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 ALA 126 126 126 ALA ALA C . n 
C 1 127 ASP 127 127 127 ASP ASP C . n 
C 1 128 GLN 128 128 128 GLN GLN C . n 
C 1 129 CYS 129 129 129 CYS CYS C . n 
C 1 130 THR 130 130 130 THR THR C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 LEU 132 132 132 LEU LEU C . n 
C 1 133 GLN 133 133 133 GLN GLN C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 PHE 135 135 135 PHE PHE C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 PHE 138 138 138 PHE PHE C . n 
C 1 139 HIS 139 139 139 HIS HIS C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 PHE 141 141 141 PHE PHE C . n 
C 1 142 GLY 142 142 142 GLY GLY C . n 
C 1 143 GLY 143 143 143 GLY GLY C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 THR 145 145 145 THR THR C . n 
C 1 146 GLY 146 146 146 GLY GLY C . n 
C 1 147 SER 147 147 147 SER SER C . n 
C 1 148 GLY 148 148 148 GLY GLY C . n 
C 1 149 PHE 149 149 149 PHE PHE C . n 
C 1 150 THR 150 150 150 THR THR C . n 
C 1 151 SER 151 151 151 SER SER C . n 
C 1 152 LEU 152 152 152 LEU LEU C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 MET 154 154 154 MET MET C . n 
C 1 155 GLU 155 155 155 GLU GLU C . n 
C 1 156 ARG 156 156 156 ARG ARG C . n 
C 1 157 LEU 157 157 157 LEU LEU C . n 
C 1 158 SER 158 158 158 SER SER C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 ASP 160 160 160 ASP ASP C . n 
C 1 161 TYR 161 161 161 TYR TYR C . n 
C 1 162 GLY 162 162 162 GLY GLY C . n 
C 1 163 LYS 163 163 163 LYS LYS C . n 
C 1 164 LYS 164 164 164 LYS LYS C . n 
C 1 165 SER 165 165 165 SER SER C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 LEU 167 167 167 LEU LEU C . n 
C 1 168 GLU 168 168 168 GLU GLU C . n 
C 1 169 PHE 169 169 169 PHE PHE C . n 
C 1 170 SER 170 170 170 SER SER C . n 
C 1 171 ILE 171 171 171 ILE ILE C . n 
C 1 172 TYR 172 172 172 TYR TYR C . n 
C 1 173 PRO 173 173 173 PRO PRO C . n 
C 1 174 ALA 174 174 174 ALA ALA C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLN 176 176 176 GLN GLN C . n 
C 1 177 VAL 177 177 177 VAL VAL C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 THR 179 179 179 THR THR C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 VAL 181 181 181 VAL VAL C . n 
C 1 182 VAL 182 182 182 VAL VAL C . n 
C 1 183 GLU 183 183 183 GLU GLU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 TYR 185 185 185 TYR TYR C . n 
C 1 186 ASN 186 186 186 ASN ASN C . n 
C 1 187 SER 187 187 187 SER SER C . n 
C 1 188 ILE 188 188 188 ILE ILE C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 THR 191 191 191 THR THR C . n 
C 1 192 HIS 192 192 192 HIS HIS C . n 
C 1 193 THR 193 193 193 THR THR C . n 
C 1 194 THR 194 194 194 THR THR C . n 
C 1 195 LEU 195 195 195 LEU LEU C . n 
C 1 196 GLU 196 196 196 GLU GLU C . n 
C 1 197 HIS 197 197 197 HIS HIS C . n 
C 1 198 SER 198 198 198 SER SER C . n 
C 1 199 ASP 199 199 199 ASP ASP C . n 
C 1 200 CYS 200 200 200 CYS CYS C . n 
C 1 201 ALA 201 201 201 ALA ALA C . n 
C 1 202 PHE 202 202 202 PHE PHE C . n 
C 1 203 MET 203 203 203 MET MET C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
C 1 205 ASP 205 205 205 ASP ASP C . n 
C 1 206 ASN 206 206 206 ASN ASN C . n 
C 1 207 GLU 207 207 207 GLU GLU C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 ILE 209 209 209 ILE ILE C . n 
C 1 210 TYR 210 210 210 TYR TYR C . n 
C 1 211 ASP 211 211 211 ASP ASP C . n 
C 1 212 ILE 212 212 212 ILE ILE C . n 
C 1 213 CYS 213 213 213 CYS CYS C . n 
C 1 214 ARG 214 214 214 ARG ARG C . n 
C 1 215 ARG 215 215 215 ARG ARG C . n 
C 1 216 ASN 216 216 216 ASN ASN C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 ASP 218 218 218 ASP ASP C . n 
C 1 219 ILE 219 219 219 ILE ILE C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 ARG 221 221 221 ARG ARG C . n 
C 1 222 PRO 222 222 222 PRO PRO C . n 
C 1 223 THR 223 223 223 THR THR C . n 
C 1 224 TYR 224 224 224 TYR TYR C . n 
C 1 225 THR 225 225 225 THR THR C . n 
C 1 226 ASN 226 226 226 ASN ASN C . n 
C 1 227 LEU 227 227 227 LEU LEU C . n 
C 1 228 ASN 228 228 228 ASN ASN C . n 
C 1 229 ARG 229 229 229 ARG ARG C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 SER 232 232 232 SER SER C . n 
C 1 233 GLN 233 233 233 GLN GLN C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 VAL 235 235 235 VAL VAL C . n 
C 1 236 SER 236 236 236 SER SER C . n 
C 1 237 SER 237 237 237 SER SER C . n 
C 1 238 ILE 238 238 238 ILE ILE C . n 
C 1 239 THR 239 239 239 THR THR C . n 
C 1 240 ALA 240 240 240 ALA ALA C . n 
C 1 241 SER 241 241 241 SER SER C . n 
C 1 242 LEU 242 242 242 LEU LEU C . n 
C 1 243 ARG 243 243 243 ARG ARG C . n 
C 1 244 PHE 244 244 244 PHE PHE C . n 
C 1 245 ASP 245 245 245 ASP ASP C . n 
C 1 246 GLY 246 246 246 GLY GLY C . n 
C 1 247 ALA 247 247 247 ALA ALA C . n 
C 1 248 LEU 248 248 248 LEU LEU C . n 
C 1 249 ASN 249 249 249 ASN ASN C . n 
C 1 250 VAL 250 250 250 VAL VAL C . n 
C 1 251 ASP 251 251 251 ASP ASP C . n 
C 1 252 LEU 252 252 252 LEU LEU C . n 
C 1 253 THR 253 253 253 THR THR C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 PHE 255 255 255 PHE PHE C . n 
C 1 256 GLN 256 256 256 GLN GLN C . n 
C 1 257 THR 257 257 257 THR THR C . n 
C 1 258 ASN 258 258 258 ASN ASN C . n 
C 1 259 LEU 259 259 259 LEU LEU C . n 
C 1 260 VAL 260 260 260 VAL VAL C . n 
C 1 261 PRO 261 261 261 PRO PRO C . n 
C 1 262 TYR 262 262 262 TYR TYR C . n 
C 1 263 PRO 263 263 263 PRO PRO C . n 
C 1 264 ARG 264 264 264 ARG ARG C . n 
C 1 265 ILE 265 265 265 ILE ILE C . n 
C 1 266 HIS 266 266 266 HIS HIS C . n 
C 1 267 PHE 267 267 267 PHE PHE C . n 
C 1 268 PRO 268 268 268 PRO PRO C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 ALA 270 270 270 ALA ALA C . n 
C 1 271 THR 271 271 271 THR THR C . n 
C 1 272 TYR 272 272 272 TYR TYR C . n 
C 1 273 ALA 273 273 273 ALA ALA C . n 
C 1 274 PRO 274 274 274 PRO PRO C . n 
C 1 275 VAL 275 275 275 VAL VAL C . n 
C 1 276 ILE 276 276 276 ILE ILE C . n 
C 1 277 SER 277 277 277 SER SER C . n 
C 1 278 ALA 278 278 278 ALA ALA C . n 
C 1 279 GLU 279 279 279 GLU GLU C . n 
C 1 280 LYS 280 280 280 LYS LYS C . n 
C 1 281 ALA 281 281 281 ALA ALA C . n 
C 1 282 TYR 282 282 282 TYR TYR C . n 
C 1 283 HIS 283 283 283 HIS HIS C . n 
C 1 284 GLU 284 284 284 GLU GLU C . n 
C 1 285 GLN 285 285 285 GLN GLN C . n 
C 1 286 LEU 286 286 286 LEU LEU C . n 
C 1 287 SER 287 287 287 SER SER C . n 
C 1 288 VAL 288 288 288 VAL VAL C . n 
C 1 289 ALA 289 289 289 ALA ALA C . n 
C 1 290 GLU 290 290 290 GLU GLU C . n 
C 1 291 ILE 291 291 291 ILE ILE C . n 
C 1 292 THR 292 292 292 THR THR C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 ALA 294 294 294 ALA ALA C . n 
C 1 295 CYS 295 295 295 CYS CYS C . n 
C 1 296 PHE 296 296 296 PHE PHE C . n 
C 1 297 GLU 297 297 297 GLU GLU C . n 
C 1 298 PRO 298 298 298 PRO PRO C . n 
C 1 299 ALA 299 299 299 ALA ALA C . n 
C 1 300 ASN 300 300 300 ASN ASN C . n 
C 1 301 GLN 301 301 301 GLN GLN C . n 
C 1 302 MET 302 302 302 MET MET C . n 
C 1 303 VAL 303 303 303 VAL VAL C . n 
C 1 304 LYS 304 304 304 LYS LYS C . n 
C 1 305 CYS 305 305 305 CYS CYS C . n 
C 1 306 ASP 306 306 306 ASP ASP C . n 
C 1 307 PRO 307 307 307 PRO PRO C . n 
C 1 308 ARG 308 308 308 ARG ARG C . n 
C 1 309 HIS 309 309 309 HIS HIS C . n 
C 1 310 GLY 310 310 310 GLY GLY C . n 
C 1 311 LYS 311 311 311 LYS LYS C . n 
C 1 312 TYR 312 312 312 TYR TYR C . n 
C 1 313 MET 313 313 313 MET MET C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 CYS 315 315 315 CYS CYS C . n 
C 1 316 CYS 316 316 316 CYS CYS C . n 
C 1 317 LEU 317 317 317 LEU LEU C . n 
C 1 318 LEU 318 318 318 LEU LEU C . n 
C 1 319 TYR 319 319 319 TYR TYR C . n 
C 1 320 ARG 320 320 320 ARG ARG C . n 
C 1 321 GLY 321 321 321 GLY GLY C . n 
C 1 322 ASP 322 322 322 ASP ASP C . n 
C 1 323 VAL 323 323 323 VAL VAL C . n 
C 1 324 VAL 324 324 324 VAL VAL C . n 
C 1 325 PRO 325 325 325 PRO PRO C . n 
C 1 326 LYS 326 326 326 LYS LYS C . n 
C 1 327 ASP 327 327 327 ASP ASP C . n 
C 1 328 VAL 328 328 328 VAL VAL C . n 
C 1 329 ASN 329 329 329 ASN ASN C . n 
C 1 330 ALA 330 330 330 ALA ALA C . n 
C 1 331 ALA 331 331 331 ALA ALA C . n 
C 1 332 ILE 332 332 332 ILE ILE C . n 
C 1 333 ALA 333 333 333 ALA ALA C . n 
C 1 334 THR 334 334 334 THR THR C . n 
C 1 335 ILE 335 335 335 ILE ILE C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 THR 337 337 337 THR THR C . n 
C 1 338 LYS 338 338 338 LYS LYS C . n 
C 1 339 ARG 339 339 339 ARG ARG C . n 
C 1 340 SER 340 340 340 SER SER C . n 
C 1 341 ILE 341 341 341 ILE ILE C . n 
C 1 342 GLN 342 342 342 GLN GLN C . n 
C 1 343 PHE 343 343 343 PHE PHE C . n 
C 1 344 VAL 344 344 344 VAL VAL C . n 
C 1 345 ASP 345 345 345 ASP ASP C . n 
C 1 346 TRP 346 346 346 TRP TRP C . n 
C 1 347 CYS 347 347 347 CYS CYS C . n 
C 1 348 PRO 348 348 348 PRO PRO C . n 
C 1 349 THR 349 349 349 THR THR C . n 
C 1 350 GLY 350 350 350 GLY GLY C . n 
C 1 351 PHE 351 351 351 PHE PHE C . n 
C 1 352 LYS 352 352 352 LYS LYS C . n 
C 1 353 VAL 353 353 353 VAL VAL C . n 
C 1 354 GLY 354 354 354 GLY GLY C . n 
C 1 355 ILE 355 355 355 ILE ILE C . n 
C 1 356 ASN 356 356 356 ASN ASN C . n 
C 1 357 TYR 357 357 357 TYR TYR C . n 
C 1 358 GLN 358 358 358 GLN GLN C . n 
C 1 359 PRO 359 359 359 PRO PRO C . n 
C 1 360 PRO 360 360 360 PRO PRO C . n 
C 1 361 THR 361 361 361 THR THR C . n 
C 1 362 VAL 362 362 362 VAL VAL C . n 
C 1 363 VAL 363 363 363 VAL VAL C . n 
C 1 364 PRO 364 364 364 PRO PRO C . n 
C 1 365 GLY 365 365 365 GLY GLY C . n 
C 1 366 GLY 366 366 366 GLY GLY C . n 
C 1 367 ASP 367 367 367 ASP ASP C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 ALA 369 369 369 ALA ALA C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 VAL 371 371 371 VAL VAL C . n 
C 1 372 GLN 372 372 372 GLN GLN C . n 
C 1 373 ARG 373 373 373 ARG ARG C . n 
C 1 374 ALA 374 374 374 ALA ALA C . n 
C 1 375 VAL 375 375 375 VAL VAL C . n 
C 1 376 CYS 376 376 376 CYS CYS C . n 
C 1 377 MET 377 377 377 MET MET C . n 
C 1 378 LEU 378 378 378 LEU LEU C . n 
C 1 379 SER 379 379 379 SER SER C . n 
C 1 380 ASN 380 380 380 ASN ASN C . n 
C 1 381 THR 381 381 381 THR THR C . n 
C 1 382 THR 382 382 382 THR THR C . n 
C 1 383 ALA 383 383 383 ALA ALA C . n 
C 1 384 ILE 384 384 384 ILE ILE C . n 
C 1 385 ALA 385 385 385 ALA ALA C . n 
C 1 386 GLU 386 386 386 GLU GLU C . n 
C 1 387 ALA 387 387 387 ALA ALA C . n 
C 1 388 TRP 388 388 388 TRP TRP C . n 
C 1 389 ALA 389 389 389 ALA ALA C . n 
C 1 390 ARG 390 390 390 ARG ARG C . n 
C 1 391 LEU 391 391 391 LEU LEU C . n 
C 1 392 ASP 392 392 392 ASP ASP C . n 
C 1 393 HIS 393 393 393 HIS HIS C . n 
C 1 394 LYS 394 394 394 LYS LYS C . n 
C 1 395 PHE 395 395 395 PHE PHE C . n 
C 1 396 ASP 396 396 396 ASP ASP C . n 
C 1 397 LEU 397 397 397 LEU LEU C . n 
C 1 398 MET 398 398 398 MET MET C . n 
C 1 399 TYR 399 399 399 TYR TYR C . n 
C 1 400 ALA 400 400 400 ALA ALA C . n 
C 1 401 LYS 401 401 401 LYS LYS C . n 
C 1 402 ARG 402 402 402 ARG ARG C . n 
C 1 403 ALA 403 403 403 ALA ALA C . n 
C 1 404 PHE 404 404 404 PHE PHE C . n 
C 1 405 VAL 405 405 405 VAL VAL C . n 
C 1 406 HIS 406 406 406 HIS HIS C . n 
C 1 407 TRP 407 407 407 TRP TRP C . n 
C 1 408 TYR 408 408 408 TYR TYR C . n 
C 1 409 VAL 409 409 409 VAL VAL C . n 
C 1 410 GLY 410 410 410 GLY GLY C . n 
C 1 411 GLU 411 411 411 GLU GLU C . n 
C 1 412 GLY 412 412 412 GLY GLY C . n 
C 1 413 MET 413 413 413 MET MET C . n 
C 1 414 GLU 414 414 414 GLU GLU C . n 
C 1 415 GLU 415 415 415 GLU GLU C . n 
C 1 416 GLY 416 416 416 GLY GLY C . n 
C 1 417 GLU 417 417 417 GLU GLU C . n 
C 1 418 PHE 418 418 418 PHE PHE C . n 
C 1 419 SER 419 419 419 SER SER C . n 
C 1 420 GLU 420 420 420 GLU GLU C . n 
C 1 421 ALA 421 421 421 ALA ALA C . n 
C 1 422 ARG 422 422 422 ARG ARG C . n 
C 1 423 GLU 423 423 423 GLU GLU C . n 
C 1 424 ASP 424 424 424 ASP ASP C . n 
C 1 425 MET 425 425 425 MET MET C . n 
C 1 426 ALA 426 426 426 ALA ALA C . n 
C 1 427 ALA 427 427 427 ALA ALA C . n 
C 1 428 LEU 428 428 428 LEU LEU C . n 
C 1 429 GLU 429 429 429 GLU GLU C . n 
C 1 430 LYS 430 430 430 LYS LYS C . n 
C 1 431 ASP 431 431 431 ASP ASP C . n 
C 1 432 TYR 432 432 432 TYR TYR C . n 
C 1 433 GLU 433 433 433 GLU GLU C . n 
C 1 434 GLU 434 434 434 GLU GLU C . n 
C 1 435 VAL 435 435 435 VAL VAL C . n 
C 1 436 GLY 436 436 436 GLY GLY C . n 
C 1 437 VAL 437 437 437 VAL VAL C . n 
C 1 438 ASP 438 438 438 ASP ASP C . n 
C 1 439 SER 439 439 439 SER SER C . n 
C 1 440 VAL 440 440 440 VAL VAL C . n 
D 2 1   MET 1   1   1   MET MET D . n 
D 2 2   ARG 2   2   2   ARG ARG D . n 
D 2 3   GLU 3   3   3   GLU GLU D . n 
D 2 4   ILE 4   4   4   ILE ILE D . n 
D 2 5   VAL 5   5   5   VAL VAL D . n 
D 2 6   HIS 6   6   6   HIS HIS D . n 
D 2 7   ILE 7   7   7   ILE ILE D . n 
D 2 8   GLN 8   8   8   GLN GLN D . n 
D 2 9   ALA 9   9   9   ALA ALA D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  GLN 11  11  11  GLN GLN D . n 
D 2 12  CYS 12  12  12  CYS CYS D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  ASN 14  14  14  ASN ASN D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  ILE 16  16  16  ILE ILE D . n 
D 2 17  GLY 17  17  17  GLY GLY D . n 
D 2 18  ALA 18  18  18  ALA ALA D . n 
D 2 19  LYS 19  19  19  LYS LYS D . n 
D 2 20  PHE 20  20  20  PHE PHE D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  GLU 22  22  22  GLU GLU D . n 
D 2 23  VAL 23  23  23  VAL VAL D . n 
D 2 24  ILE 24  24  24  ILE ILE D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  ASP 26  26  26  ASP ASP D . n 
D 2 27  GLU 27  27  27  GLU GLU D . n 
D 2 28  HIS 28  28  28  HIS HIS D . n 
D 2 29  GLY 29  29  29  GLY GLY D . n 
D 2 30  ILE 30  30  30  ILE ILE D . n 
D 2 31  ASP 31  31  31  ASP ASP D . n 
D 2 32  PRO 32  32  32  PRO PRO D . n 
D 2 33  THR 33  33  33  THR THR D . n 
D 2 34  GLY 34  34  34  GLY GLY D . n 
D 2 35  SER 35  35  35  SER SER D . n 
D 2 36  TYR 36  36  36  TYR TYR D . n 
D 2 37  HIS 37  37  37  HIS HIS D . n 
D 2 38  GLY 38  38  38  GLY GLY D . n 
D 2 39  ASP 39  39  39  ASP ASP D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  ASP 41  41  41  ASP ASP D . n 
D 2 42  LEU 42  42  42  LEU LEU D . n 
D 2 43  GLN 43  43  43  GLN GLN D . n 
D 2 44  LEU 44  44  44  LEU LEU D . n 
D 2 45  GLU 45  45  45  GLU GLU D . n 
D 2 46  ARG 46  46  46  ARG ARG D . n 
D 2 47  ILE 47  47  47  ILE ILE D . n 
D 2 48  ASN 48  48  48  ASN ASN D . n 
D 2 49  VAL 49  49  49  VAL VAL D . n 
D 2 50  TYR 50  50  50  TYR TYR D . n 
D 2 51  TYR 51  51  51  TYR TYR D . n 
D 2 52  ASN 52  52  52  ASN ASN D . n 
D 2 53  GLU 53  53  53  GLU GLU D . n 
D 2 54  ALA 54  54  54  ALA ALA D . n 
D 2 55  THR 55  55  55  THR THR D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  ASN 57  57  57  ASN ASN D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  TYR 59  59  59  TYR TYR D . n 
D 2 60  VAL 60  60  60  VAL VAL D . n 
D 2 61  PRO 61  61  61  PRO PRO D . n 
D 2 62  ARG 62  62  62  ARG ARG D . n 
D 2 63  ALA 63  63  63  ALA ALA D . n 
D 2 64  ILE 64  64  64  ILE ILE D . n 
D 2 65  LEU 65  65  65  LEU LEU D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  ASP 67  67  67  ASP ASP D . n 
D 2 68  LEU 68  68  68  LEU LEU D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PRO 70  70  70  PRO PRO D . n 
D 2 71  GLY 71  71  71  GLY GLY D . n 
D 2 72  THR 72  72  72  THR THR D . n 
D 2 73  MET 73  73  73  MET MET D . n 
D 2 74  ASP 74  74  74  ASP ASP D . n 
D 2 75  SER 75  75  75  SER SER D . n 
D 2 76  VAL 76  76  76  VAL VAL D . n 
D 2 77  ARG 77  77  77  ARG ARG D . n 
D 2 78  SER 78  78  78  SER SER D . n 
D 2 79  GLY 79  79  79  GLY GLY D . n 
D 2 80  PRO 80  80  80  PRO PRO D . n 
D 2 81  PHE 81  81  81  PHE PHE D . n 
D 2 82  GLY 82  82  82  GLY GLY D . n 
D 2 83  GLN 83  83  83  GLN GLN D . n 
D 2 84  ILE 84  84  84  ILE ILE D . n 
D 2 85  PHE 85  85  85  PHE PHE D . n 
D 2 86  ARG 86  86  86  ARG ARG D . n 
D 2 87  PRO 87  87  87  PRO PRO D . n 
D 2 88  ASP 88  88  88  ASP ASP D . n 
D 2 89  ASN 89  89  89  ASN ASN D . n 
D 2 90  PHE 90  90  90  PHE PHE D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  PHE 92  92  92  PHE PHE D . n 
D 2 93  GLY 93  93  93  GLY GLY D . n 
D 2 94  GLN 94  94  94  GLN GLN D . n 
D 2 95  SER 95  95  95  SER SER D . n 
D 2 96  GLY 96  96  96  GLY GLY D . n 
D 2 97  ALA 97  97  97  ALA ALA D . n 
D 2 98  GLY 98  98  98  GLY GLY D . n 
D 2 99  ASN 99  99  99  ASN ASN D . n 
D 2 100 ASN 100 100 100 ASN ASN D . n 
D 2 101 TRP 101 101 101 TRP TRP D . n 
D 2 102 ALA 102 102 102 ALA ALA D . n 
D 2 103 LYS 103 103 103 LYS LYS D . n 
D 2 104 GLY 104 104 104 GLY GLY D . n 
D 2 105 HIS 105 105 105 HIS HIS D . n 
D 2 106 TYR 106 106 106 TYR TYR D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 GLU 108 108 108 GLU GLU D . n 
D 2 109 GLY 109 109 109 GLY GLY D . n 
D 2 110 ALA 110 110 110 ALA ALA D . n 
D 2 111 GLU 111 111 111 GLU GLU D . n 
D 2 112 LEU 112 112 112 LEU LEU D . n 
D 2 113 VAL 113 113 113 VAL VAL D . n 
D 2 114 ASP 114 114 114 ASP ASP D . n 
D 2 115 SER 115 115 115 SER SER D . n 
D 2 116 VAL 116 116 116 VAL VAL D . n 
D 2 117 LEU 117 117 117 LEU LEU D . n 
D 2 118 ASP 118 118 118 ASP ASP D . n 
D 2 119 VAL 119 119 119 VAL VAL D . n 
D 2 120 VAL 120 120 120 VAL VAL D . n 
D 2 121 ARG 121 121 121 ARG ARG D . n 
D 2 122 LYS 122 122 122 LYS LYS D . n 
D 2 123 GLU 123 123 123 GLU GLU D . n 
D 2 124 SER 124 124 124 SER SER D . n 
D 2 125 GLU 125 125 125 GLU GLU D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 CYS 127 127 127 CYS CYS D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 CYS 129 129 129 CYS CYS D . n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 GLN 131 131 131 GLN GLN D . n 
D 2 132 GLY 132 132 132 GLY GLY D . n 
D 2 133 PHE 133 133 133 PHE PHE D . n 
D 2 134 GLN 134 134 134 GLN GLN D . n 
D 2 135 LEU 135 135 135 LEU LEU D . n 
D 2 136 THR 136 136 136 THR THR D . n 
D 2 137 HIS 137 137 137 HIS HIS D . n 
D 2 138 SER 138 138 138 SER SER D . n 
D 2 139 LEU 139 139 139 LEU LEU D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 GLY 141 141 141 GLY GLY D . n 
D 2 142 GLY 142 142 142 GLY GLY D . n 
D 2 143 THR 143 143 143 THR THR D . n 
D 2 144 GLY 144 144 144 GLY GLY D . n 
D 2 145 SER 145 145 145 SER SER D . n 
D 2 146 GLY 146 146 146 GLY GLY D . n 
D 2 147 MET 147 147 147 MET MET D . n 
D 2 148 GLY 148 148 148 GLY GLY D . n 
D 2 149 THR 149 149 149 THR THR D . n 
D 2 150 LEU 150 150 150 LEU LEU D . n 
D 2 151 LEU 151 151 151 LEU LEU D . n 
D 2 152 ILE 152 152 152 ILE ILE D . n 
D 2 153 SER 153 153 153 SER SER D . n 
D 2 154 LYS 154 154 154 LYS LYS D . n 
D 2 155 ILE 155 155 155 ILE ILE D . n 
D 2 156 ARG 156 156 156 ARG ARG D . n 
D 2 157 GLU 157 157 157 GLU GLU D . n 
D 2 158 GLU 158 158 158 GLU GLU D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 ASP 161 161 161 ASP ASP D . n 
D 2 162 ARG 162 162 162 ARG ARG D . n 
D 2 163 ILE 163 163 163 ILE ILE D . n 
D 2 164 MET 164 164 164 MET MET D . n 
D 2 165 ASN 165 165 165 ASN ASN D . n 
D 2 166 THR 166 166 166 THR THR D . n 
D 2 167 PHE 167 167 167 PHE PHE D . n 
D 2 168 SER 168 168 168 SER SER D . n 
D 2 169 VAL 169 169 169 VAL VAL D . n 
D 2 170 MET 170 170 170 MET MET D . n 
D 2 171 PRO 171 171 171 PRO PRO D . n 
D 2 172 SER 172 172 172 SER SER D . n 
D 2 173 PRO 173 173 173 PRO PRO D . n 
D 2 174 LYS 174 174 174 LYS LYS D . n 
D 2 175 VAL 175 175 175 VAL VAL D . n 
D 2 176 SER 176 176 176 SER SER D . n 
D 2 177 ASP 177 177 177 ASP ASP D . n 
D 2 178 THR 178 178 178 THR THR D . n 
D 2 179 VAL 179 179 179 VAL VAL D . n 
D 2 180 VAL 180 180 180 VAL VAL D . n 
D 2 181 GLU 181 181 181 GLU GLU D . n 
D 2 182 PRO 182 182 182 PRO PRO D . n 
D 2 183 TYR 183 183 183 TYR TYR D . n 
D 2 184 ASN 184 184 184 ASN ASN D . n 
D 2 185 ALA 185 185 185 ALA ALA D . n 
D 2 186 THR 186 186 186 THR THR D . n 
D 2 187 LEU 187 187 187 LEU LEU D . n 
D 2 188 SER 188 188 188 SER SER D . n 
D 2 189 VAL 189 189 189 VAL VAL D . n 
D 2 190 HIS 190 190 190 HIS HIS D . n 
D 2 191 GLN 191 191 191 GLN GLN D . n 
D 2 192 LEU 192 192 192 LEU LEU D . n 
D 2 193 VAL 193 193 193 VAL VAL D . n 
D 2 194 GLU 194 194 194 GLU GLU D . n 
D 2 195 ASN 195 195 195 ASN ASN D . n 
D 2 196 THR 196 196 196 THR THR D . n 
D 2 197 ASP 197 197 197 ASP ASP D . n 
D 2 198 GLU 198 198 198 GLU GLU D . n 
D 2 199 THR 199 199 199 THR THR D . n 
D 2 200 TYR 200 200 200 TYR TYR D . n 
D 2 201 CYS 201 201 201 CYS CYS D . n 
D 2 202 ILE 202 202 202 ILE ILE D . n 
D 2 203 ASP 203 203 203 ASP ASP D . n 
D 2 204 ASN 204 204 204 ASN ASN D . n 
D 2 205 GLU 205 205 205 GLU GLU D . n 
D 2 206 ALA 206 206 206 ALA ALA D . n 
D 2 207 LEU 207 207 207 LEU LEU D . n 
D 2 208 TYR 208 208 208 TYR TYR D . n 
D 2 209 ASP 209 209 209 ASP ASP D . n 
D 2 210 ILE 210 210 210 ILE ILE D . n 
D 2 211 CYS 211 211 211 CYS CYS D . n 
D 2 212 PHE 212 212 212 PHE PHE D . n 
D 2 213 ARG 213 213 213 ARG ARG D . n 
D 2 214 THR 214 214 214 THR THR D . n 
D 2 215 LEU 215 215 215 LEU LEU D . n 
D 2 216 LYS 216 216 216 LYS LYS D . n 
D 2 217 LEU 217 217 217 LEU LEU D . n 
D 2 218 THR 218 218 218 THR THR D . n 
D 2 219 THR 219 219 219 THR THR D . n 
D 2 220 PRO 220 220 220 PRO PRO D . n 
D 2 221 THR 221 221 221 THR THR D . n 
D 2 222 TYR 222 222 222 TYR TYR D . n 
D 2 223 GLY 223 223 223 GLY GLY D . n 
D 2 224 ASP 224 224 224 ASP ASP D . n 
D 2 225 LEU 225 225 225 LEU LEU D . n 
D 2 226 ASN 226 226 226 ASN ASN D . n 
D 2 227 HIS 227 227 227 HIS HIS D . n 
D 2 228 LEU 228 228 228 LEU LEU D . n 
D 2 229 VAL 229 229 229 VAL VAL D . n 
D 2 230 SER 230 230 230 SER SER D . n 
D 2 231 ALA 231 231 231 ALA ALA D . n 
D 2 232 THR 232 232 232 THR THR D . n 
D 2 233 MET 233 233 233 MET MET D . n 
D 2 234 SER 234 234 234 SER SER D . n 
D 2 235 GLY 235 235 235 GLY GLY D . n 
D 2 236 VAL 236 236 236 VAL VAL D . n 
D 2 237 THR 237 237 237 THR THR D . n 
D 2 238 THR 238 238 238 THR THR D . n 
D 2 239 CYS 239 239 239 CYS CYS D . n 
D 2 240 LEU 240 240 240 LEU LEU D . n 
D 2 241 ARG 241 241 241 ARG ARG D . n 
D 2 242 PHE 242 242 242 PHE PHE D . n 
D 2 243 PRO 243 243 243 PRO PRO D . n 
D 2 244 GLY 244 244 244 GLY GLY D . n 
D 2 245 GLN 245 245 245 GLN GLN D . n 
D 2 246 LEU 246 246 246 LEU LEU D . n 
D 2 247 ASN 247 247 247 ASN ASN D . n 
D 2 248 ALA 248 248 248 ALA ALA D . n 
D 2 249 ASP 249 249 249 ASP ASP D . n 
D 2 250 LEU 250 250 250 LEU LEU D . n 
D 2 251 ARG 251 251 251 ARG ARG D . n 
D 2 252 LYS 252 252 252 LYS LYS D . n 
D 2 253 LEU 253 253 253 LEU LEU D . n 
D 2 254 ALA 254 254 254 ALA ALA D . n 
D 2 255 VAL 255 255 255 VAL VAL D . n 
D 2 256 ASN 256 256 256 ASN ASN D . n 
D 2 257 MET 257 257 257 MET MET D . n 
D 2 258 VAL 258 258 258 VAL VAL D . n 
D 2 259 PRO 259 259 259 PRO PRO D . n 
D 2 260 PHE 260 260 260 PHE PHE D . n 
D 2 261 PRO 261 261 261 PRO PRO D . n 
D 2 262 ARG 262 262 262 ARG ARG D . n 
D 2 263 LEU 263 263 263 LEU LEU D . n 
D 2 264 HIS 264 264 264 HIS HIS D . n 
D 2 265 PHE 265 265 265 PHE PHE D . n 
D 2 266 PHE 266 266 266 PHE PHE D . n 
D 2 267 MET 267 267 267 MET MET D . n 
D 2 268 PRO 268 268 268 PRO PRO D . n 
D 2 269 GLY 269 269 269 GLY GLY D . n 
D 2 270 PHE 270 270 270 PHE PHE D . n 
D 2 271 ALA 271 271 271 ALA ALA D . n 
D 2 272 PRO 272 272 272 PRO PRO D . n 
D 2 273 LEU 273 273 273 LEU LEU D . n 
D 2 274 THR 274 274 ?   ?   ?   D . n 
D 2 275 SER 275 275 ?   ?   ?   D . n 
D 2 276 ARG 276 276 ?   ?   ?   D . n 
D 2 277 GLY 277 277 ?   ?   ?   D . n 
D 2 278 SER 278 278 ?   ?   ?   D . n 
D 2 279 GLN 279 279 ?   ?   ?   D . n 
D 2 280 GLN 280 280 ?   ?   ?   D . n 
D 2 281 TYR 281 281 ?   ?   ?   D . n 
D 2 282 ARG 282 282 ?   ?   ?   D . n 
D 2 283 ALA 283 283 ?   ?   ?   D . n 
D 2 284 LEU 284 284 284 LEU LEU D . n 
D 2 285 THR 285 285 285 THR THR D . n 
D 2 286 VAL 286 286 286 VAL VAL D . n 
D 2 287 PRO 287 287 287 PRO PRO D . n 
D 2 288 GLU 288 288 288 GLU GLU D . n 
D 2 289 LEU 289 289 289 LEU LEU D . n 
D 2 290 THR 290 290 290 THR THR D . n 
D 2 291 GLN 291 291 291 GLN GLN D . n 
D 2 292 GLN 292 292 292 GLN GLN D . n 
D 2 293 MET 293 293 293 MET MET D . n 
D 2 294 PHE 294 294 294 PHE PHE D . n 
D 2 295 ASP 295 295 295 ASP ASP D . n 
D 2 296 SER 296 296 296 SER SER D . n 
D 2 297 LYS 297 297 297 LYS LYS D . n 
D 2 298 ASN 298 298 298 ASN ASN D . n 
D 2 299 MET 299 299 299 MET MET D . n 
D 2 300 MET 300 300 300 MET MET D . n 
D 2 301 ALA 301 301 301 ALA ALA D . n 
D 2 302 ALA 302 302 302 ALA ALA D . n 
D 2 303 CYS 303 303 303 CYS CYS D . n 
D 2 304 ASP 304 304 304 ASP ASP D . n 
D 2 305 PRO 305 305 305 PRO PRO D . n 
D 2 306 ARG 306 306 306 ARG ARG D . n 
D 2 307 HIS 307 307 307 HIS HIS D . n 
D 2 308 GLY 308 308 308 GLY GLY D . n 
D 2 309 ARG 309 309 309 ARG ARG D . n 
D 2 310 TYR 310 310 310 TYR TYR D . n 
D 2 311 LEU 311 311 311 LEU LEU D . n 
D 2 312 THR 312 312 312 THR THR D . n 
D 2 313 VAL 313 313 313 VAL VAL D . n 
D 2 314 ALA 314 314 314 ALA ALA D . n 
D 2 315 ALA 315 315 315 ALA ALA D . n 
D 2 316 ILE 316 316 316 ILE ILE D . n 
D 2 317 PHE 317 317 317 PHE PHE D . n 
D 2 318 ARG 318 318 318 ARG ARG D . n 
D 2 319 GLY 319 319 319 GLY GLY D . n 
D 2 320 ARG 320 320 320 ARG ARG D . n 
D 2 321 MET 321 321 321 MET MET D . n 
D 2 322 SER 322 322 322 SER SER D . n 
D 2 323 MET 323 323 323 MET MET D . n 
D 2 324 LYS 324 324 324 LYS LYS D . n 
D 2 325 GLU 325 325 325 GLU GLU D . n 
D 2 326 VAL 326 326 326 VAL VAL D . n 
D 2 327 ASP 327 327 327 ASP ASP D . n 
D 2 328 GLU 328 328 328 GLU GLU D . n 
D 2 329 GLN 329 329 329 GLN GLN D . n 
D 2 330 MET 330 330 330 MET MET D . n 
D 2 331 LEU 331 331 331 LEU LEU D . n 
D 2 332 ASN 332 332 332 ASN ASN D . n 
D 2 333 VAL 333 333 333 VAL VAL D . n 
D 2 334 GLN 334 334 334 GLN GLN D . n 
D 2 335 ASN 335 335 335 ASN ASN D . n 
D 2 336 LYS 336 336 336 LYS LYS D . n 
D 2 337 ASN 337 337 337 ASN ASN D . n 
D 2 338 SER 338 338 338 SER SER D . n 
D 2 339 SER 339 339 339 SER SER D . n 
D 2 340 TYR 340 340 340 TYR TYR D . n 
D 2 341 PHE 341 341 341 PHE PHE D . n 
D 2 342 VAL 342 342 342 VAL VAL D . n 
D 2 343 GLU 343 343 343 GLU GLU D . n 
D 2 344 TRP 344 344 344 TRP TRP D . n 
D 2 345 ILE 345 345 345 ILE ILE D . n 
D 2 346 PRO 346 346 346 PRO PRO D . n 
D 2 347 ASN 347 347 347 ASN ASN D . n 
D 2 348 ASN 348 348 348 ASN ASN D . n 
D 2 349 VAL 349 349 349 VAL VAL D . n 
D 2 350 LYS 350 350 350 LYS LYS D . n 
D 2 351 THR 351 351 351 THR THR D . n 
D 2 352 ALA 352 352 352 ALA ALA D . n 
D 2 353 VAL 353 353 353 VAL VAL D . n 
D 2 354 CYS 354 354 354 CYS CYS D . n 
D 2 355 ASP 355 355 355 ASP ASP D . n 
D 2 356 ILE 356 356 356 ILE ILE D . n 
D 2 357 PRO 357 357 357 PRO PRO D . n 
D 2 358 PRO 358 358 358 PRO PRO D . n 
D 2 359 ARG 359 359 359 ARG ARG D . n 
D 2 360 GLY 360 360 360 GLY GLY D . n 
D 2 361 LEU 361 361 361 LEU LEU D . n 
D 2 362 LYS 362 362 362 LYS LYS D . n 
D 2 363 MET 363 363 363 MET MET D . n 
D 2 364 SER 364 364 364 SER SER D . n 
D 2 365 ALA 365 365 365 ALA ALA D . n 
D 2 366 THR 366 366 366 THR THR D . n 
D 2 367 PHE 367 367 367 PHE PHE D . n 
D 2 368 ILE 368 368 368 ILE ILE D . n 
D 2 369 GLY 369 369 369 GLY GLY D . n 
D 2 370 ASN 370 370 370 ASN ASN D . n 
D 2 371 SER 371 371 371 SER SER D . n 
D 2 372 THR 372 372 372 THR THR D . n 
D 2 373 ALA 373 373 373 ALA ALA D . n 
D 2 374 ILE 374 374 374 ILE ILE D . n 
D 2 375 GLN 375 375 375 GLN GLN D . n 
D 2 376 GLU 376 376 376 GLU GLU D . n 
D 2 377 LEU 377 377 377 LEU LEU D . n 
D 2 378 PHE 378 378 378 PHE PHE D . n 
D 2 379 LYS 379 379 379 LYS LYS D . n 
D 2 380 ARG 380 380 380 ARG ARG D . n 
D 2 381 ILE 381 381 381 ILE ILE D . n 
D 2 382 SER 382 382 382 SER SER D . n 
D 2 383 GLU 383 383 383 GLU GLU D . n 
D 2 384 GLN 384 384 384 GLN GLN D . n 
D 2 385 PHE 385 385 385 PHE PHE D . n 
D 2 386 THR 386 386 386 THR THR D . n 
D 2 387 ALA 387 387 387 ALA ALA D . n 
D 2 388 MET 388 388 388 MET MET D . n 
D 2 389 PHE 389 389 389 PHE PHE D . n 
D 2 390 ARG 390 390 390 ARG ARG D . n 
D 2 391 ARG 391 391 391 ARG ARG D . n 
D 2 392 LYS 392 392 392 LYS LYS D . n 
D 2 393 ALA 393 393 393 ALA ALA D . n 
D 2 394 PHE 394 394 394 PHE PHE D . n 
D 2 395 LEU 395 395 395 LEU LEU D . n 
D 2 396 HIS 396 396 396 HIS HIS D . n 
D 2 397 TRP 397 397 397 TRP TRP D . n 
D 2 398 TYR 398 398 398 TYR TYR D . n 
D 2 399 THR 399 399 399 THR THR D . n 
D 2 400 GLY 400 400 400 GLY GLY D . n 
D 2 401 GLU 401 401 401 GLU GLU D . n 
D 2 402 GLY 402 402 402 GLY GLY D . n 
D 2 403 MET 403 403 403 MET MET D . n 
D 2 404 ASP 404 404 404 ASP ASP D . n 
D 2 405 GLU 405 405 405 GLU GLU D . n 
D 2 406 MET 406 406 406 MET MET D . n 
D 2 407 GLU 407 407 407 GLU GLU D . n 
D 2 408 PHE 408 408 408 PHE PHE D . n 
D 2 409 THR 409 409 409 THR THR D . n 
D 2 410 GLU 410 410 410 GLU GLU D . n 
D 2 411 ALA 411 411 411 ALA ALA D . n 
D 2 412 GLU 412 412 412 GLU GLU D . n 
D 2 413 SER 413 413 413 SER SER D . n 
D 2 414 ASN 414 414 414 ASN ASN D . n 
D 2 415 MET 415 415 415 MET MET D . n 
D 2 416 ASN 416 416 416 ASN ASN D . n 
D 2 417 ASP 417 417 417 ASP ASP D . n 
D 2 418 LEU 418 418 418 LEU LEU D . n 
D 2 419 VAL 419 419 419 VAL VAL D . n 
D 2 420 SER 420 420 420 SER SER D . n 
D 2 421 GLU 421 421 421 GLU GLU D . n 
D 2 422 TYR 422 422 422 TYR TYR D . n 
D 2 423 GLN 423 423 423 GLN GLN D . n 
D 2 424 GLN 424 424 424 GLN GLN D . n 
D 2 425 TYR 425 425 425 TYR TYR D . n 
D 2 426 GLN 426 426 426 GLN GLN D . n 
D 2 427 ASP 427 427 427 ASP ASP D . n 
D 2 428 ALA 428 428 428 ALA ALA D . n 
D 2 429 THR 429 429 429 THR THR D . n 
D 2 430 ALA 430 430 430 ALA ALA D . n 
D 2 431 ASP 431 431 431 ASP ASP D . n 
E 3 1   MET 1   3   ?   ?   ?   E . n 
E 3 2   ALA 2   4   ?   ?   ?   E . n 
E 3 3   ASP 3   5   ?   ?   ?   E . n 
E 3 4   MET 4   6   6   MET MET E . n 
E 3 5   GLU 5   7   7   GLU GLU E . n 
E 3 6   VAL 6   8   8   VAL VAL E . n 
E 3 7   ILE 7   9   9   ILE ILE E . n 
E 3 8   GLU 8   10  10  GLU GLU E . n 
E 3 9   LEU 9   11  11  LEU LEU E . n 
E 3 10  ASN 10  12  12  ASN ASN E . n 
E 3 11  LYS 11  13  13  LYS LYS E . n 
E 3 12  CYS 12  14  14  CYS CYS E . n 
E 3 13  THR 13  15  15  THR THR E . n 
E 3 14  SER 14  16  16  SER SER E . n 
E 3 15  GLY 15  17  17  GLY GLY E . n 
E 3 16  GLN 16  18  18  GLN GLN E . n 
E 3 17  SER 17  19  19  SER SER E . n 
E 3 18  PHE 18  20  20  PHE PHE E . n 
E 3 19  GLU 19  21  21  GLU GLU E . n 
E 3 20  VAL 20  22  22  VAL VAL E . n 
E 3 21  ILE 21  23  23  ILE ILE E . n 
E 3 22  LEU 22  24  24  LEU LEU E . n 
E 3 23  LYS 23  25  25  LYS LYS E . n 
E 3 24  PRO 24  26  26  PRO PRO E . n 
E 3 25  PRO 25  27  27  PRO PRO E . n 
E 3 26  SER 26  28  28  SER SER E . n 
E 3 27  PHE 27  29  ?   ?   ?   E . n 
E 3 28  ASP 28  30  ?   ?   ?   E . n 
E 3 29  GLY 29  31  ?   ?   ?   E . n 
E 3 30  VAL 30  32  ?   ?   ?   E . n 
E 3 31  PRO 31  33  ?   ?   ?   E . n 
E 3 32  GLU 32  34  ?   ?   ?   E . n 
E 3 33  PHE 33  35  ?   ?   ?   E . n 
E 3 34  ASN 34  36  ?   ?   ?   E . n 
E 3 35  ALA 35  37  ?   ?   ?   E . n 
E 3 36  SER 36  38  ?   ?   ?   E . n 
E 3 37  LEU 37  39  ?   ?   ?   E . n 
E 3 38  PRO 38  40  ?   ?   ?   E . n 
E 3 39  ARG 39  41  ?   ?   ?   E . n 
E 3 40  ARG 40  42  ?   ?   ?   E . n 
E 3 41  ARG 41  43  ?   ?   ?   E . n 
E 3 42  ASP 42  44  44  ASP ASP E . n 
E 3 43  PRO 43  45  45  PRO PRO E . n 
E 3 44  SER 44  46  46  SER SER E . n 
E 3 45  LEU 45  47  47  LEU LEU E . n 
E 3 46  GLU 46  48  48  GLU GLU E . n 
E 3 47  GLU 47  49  49  GLU GLU E . n 
E 3 48  ILE 48  50  50  ILE ILE E . n 
E 3 49  GLN 49  51  51  GLN GLN E . n 
E 3 50  LYS 50  52  52  LYS LYS E . n 
E 3 51  LYS 51  53  53  LYS LYS E . n 
E 3 52  LEU 52  54  54  LEU LEU E . n 
E 3 53  GLU 53  55  55  GLU GLU E . n 
E 3 54  ALA 54  56  56  ALA ALA E . n 
E 3 55  ALA 55  57  57  ALA ALA E . n 
E 3 56  GLU 56  58  58  GLU GLU E . n 
E 3 57  GLU 57  59  59  GLU GLU E . n 
E 3 58  ARG 58  60  60  ARG ARG E . n 
E 3 59  ARG 59  61  61  ARG ARG E . n 
E 3 60  LYS 60  62  62  LYS LYS E . n 
E 3 61  TYR 61  63  63  TYR TYR E . n 
E 3 62  GLN 62  64  64  GLN GLN E . n 
E 3 63  GLU 63  65  65  GLU GLU E . n 
E 3 64  ALA 64  66  66  ALA ALA E . n 
E 3 65  GLU 65  67  67  GLU GLU E . n 
E 3 66  LEU 66  68  68  LEU LEU E . n 
E 3 67  LEU 67  69  69  LEU LEU E . n 
E 3 68  LYS 68  70  70  LYS LYS E . n 
E 3 69  HIS 69  71  71  HIS HIS E . n 
E 3 70  LEU 70  72  72  LEU LEU E . n 
E 3 71  ALA 71  73  73  ALA ALA E . n 
E 3 72  GLU 72  74  74  GLU GLU E . n 
E 3 73  LYS 73  75  75  LYS LYS E . n 
E 3 74  ARG 74  76  76  ARG ARG E . n 
E 3 75  GLU 75  77  77  GLU GLU E . n 
E 3 76  HIS 76  78  78  HIS HIS E . n 
E 3 77  GLU 77  79  79  GLU GLU E . n 
E 3 78  ARG 78  80  80  ARG ARG E . n 
E 3 79  GLU 79  81  81  GLU GLU E . n 
E 3 80  VAL 80  82  82  VAL VAL E . n 
E 3 81  ILE 81  83  83  ILE ILE E . n 
E 3 82  GLN 82  84  84  GLN GLN E . n 
E 3 83  LYS 83  85  85  LYS LYS E . n 
E 3 84  ALA 84  86  86  ALA ALA E . n 
E 3 85  ILE 85  87  87  ILE ILE E . n 
E 3 86  GLU 86  88  88  GLU GLU E . n 
E 3 87  GLU 87  89  89  GLU GLU E . n 
E 3 88  ASN 88  90  90  ASN ASN E . n 
E 3 89  ASN 89  91  91  ASN ASN E . n 
E 3 90  ASN 90  92  92  ASN ASN E . n 
E 3 91  PHE 91  93  93  PHE PHE E . n 
E 3 92  ILE 92  94  94  ILE ILE E . n 
E 3 93  LYS 93  95  95  LYS LYS E . n 
E 3 94  MET 94  96  96  MET MET E . n 
E 3 95  ALA 95  97  97  ALA ALA E . n 
E 3 96  LYS 96  98  98  LYS LYS E . n 
E 3 97  GLU 97  99  99  GLU GLU E . n 
E 3 98  LYS 98  100 100 LYS LYS E . n 
E 3 99  LEU 99  101 101 LEU LEU E . n 
E 3 100 ALA 100 102 102 ALA ALA E . n 
E 3 101 GLN 101 103 103 GLN GLN E . n 
E 3 102 LYS 102 104 104 LYS LYS E . n 
E 3 103 MET 103 105 105 MET MET E . n 
E 3 104 GLU 104 106 106 GLU GLU E . n 
E 3 105 SER 105 107 107 SER SER E . n 
E 3 106 ASN 106 108 108 ASN ASN E . n 
E 3 107 LYS 107 109 109 LYS LYS E . n 
E 3 108 GLU 108 110 110 GLU GLU E . n 
E 3 109 ASN 109 111 111 ASN ASN E . n 
E 3 110 ARG 110 112 112 ARG ARG E . n 
E 3 111 GLU 111 113 113 GLU GLU E . n 
E 3 112 ALA 112 114 114 ALA ALA E . n 
E 3 113 HIS 113 115 115 HIS HIS E . n 
E 3 114 LEU 114 116 116 LEU LEU E . n 
E 3 115 ALA 115 117 117 ALA ALA E . n 
E 3 116 ALA 116 118 118 ALA ALA E . n 
E 3 117 MET 117 119 119 MET MET E . n 
E 3 118 LEU 118 120 120 LEU LEU E . n 
E 3 119 GLU 119 121 121 GLU GLU E . n 
E 3 120 ARG 120 122 122 ARG ARG E . n 
E 3 121 LEU 121 123 123 LEU LEU E . n 
E 3 122 GLN 122 124 124 GLN GLN E . n 
E 3 123 GLU 123 125 125 GLU GLU E . n 
E 3 124 LYS 124 126 126 LYS LYS E . n 
E 3 125 ASP 125 127 127 ASP ASP E . n 
E 3 126 LYS 126 128 128 LYS LYS E . n 
E 3 127 HIS 127 129 129 HIS HIS E . n 
E 3 128 ALA 128 130 130 ALA ALA E . n 
E 3 129 GLU 129 131 131 GLU GLU E . n 
E 3 130 GLU 130 132 132 GLU GLU E . n 
E 3 131 VAL 131 133 133 VAL VAL E . n 
E 3 132 ARG 132 134 134 ARG ARG E . n 
E 3 133 LYS 133 135 135 LYS LYS E . n 
E 3 134 ASN 134 136 136 ASN ASN E . n 
E 3 135 LYS 135 137 137 LYS LYS E . n 
E 3 136 GLU 136 138 138 GLU GLU E . n 
E 3 137 LEU 137 139 139 LEU LEU E . n 
E 3 138 LYS 138 140 140 LYS LYS E . n 
E 3 139 GLU 139 141 141 GLU GLU E . n 
E 3 140 GLU 140 142 ?   ?   ?   E . n 
E 3 141 ALA 141 143 ?   ?   ?   E . n 
E 3 142 SER 142 144 ?   ?   ?   E . n 
E 3 143 ARG 143 145 ?   ?   ?   E . n 
F 4 1   MET 1   1   1   MET MET F . n 
F 4 2   TYR 2   2   2   TYR TYR F . n 
F 4 3   THR 3   3   3   THR THR F . n 
F 4 4   PHE 4   4   4   PHE PHE F . n 
F 4 5   VAL 5   5   5   VAL VAL F . n 
F 4 6   VAL 6   6   6   VAL VAL F . n 
F 4 7   ARG 7   7   7   ARG ARG F . n 
F 4 8   ASP 8   8   8   ASP ASP F . n 
F 4 9   GLU 9   9   9   GLU GLU F . n 
F 4 10  ASN 10  10  10  ASN ASN F . n 
F 4 11  SER 11  11  11  SER SER F . n 
F 4 12  SER 12  12  12  SER SER F . n 
F 4 13  VAL 13  13  13  VAL VAL F . n 
F 4 14  TYR 14  14  14  TYR TYR F . n 
F 4 15  ALA 15  15  15  ALA ALA F . n 
F 4 16  GLU 16  16  16  GLU GLU F . n 
F 4 17  VAL 17  17  17  VAL VAL F . n 
F 4 18  SER 18  18  18  SER SER F . n 
F 4 19  ARG 19  19  19  ARG ARG F . n 
F 4 20  LEU 20  20  20  LEU LEU F . n 
F 4 21  LEU 21  21  21  LEU LEU F . n 
F 4 22  LEU 22  22  22  LEU LEU F . n 
F 4 23  ALA 23  23  23  ALA ALA F . n 
F 4 24  THR 24  24  24  THR THR F . n 
F 4 25  GLY 25  25  25  GLY GLY F . n 
F 4 26  GLN 26  26  26  GLN GLN F . n 
F 4 27  TRP 27  27  27  TRP TRP F . n 
F 4 28  LYS 28  28  28  LYS LYS F . n 
F 4 29  ARG 29  29  29  ARG ARG F . n 
F 4 30  LEU 30  30  30  LEU LEU F . n 
F 4 31  ARG 31  31  31  ARG ARG F . n 
F 4 32  LYS 32  32  32  LYS LYS F . n 
F 4 33  ASP 33  33  33  ASP ASP F . n 
F 4 34  ASN 34  34  34  ASN ASN F . n 
F 4 35  PRO 35  35  35  PRO PRO F . n 
F 4 36  ARG 36  36  36  ARG ARG F . n 
F 4 37  PHE 37  37  37  PHE PHE F . n 
F 4 38  ASN 38  38  38  ASN ASN F . n 
F 4 39  LEU 39  39  39  LEU LEU F . n 
F 4 40  MET 40  40  40  MET MET F . n 
F 4 41  LEU 41  41  41  LEU LEU F . n 
F 4 42  GLY 42  42  42  GLY GLY F . n 
F 4 43  GLU 43  43  43  GLU GLU F . n 
F 4 44  ARG 44  44  44  ARG ARG F . n 
F 4 45  ASN 45  45  45  ASN ASN F . n 
F 4 46  ARG 46  46  46  ARG ARG F . n 
F 4 47  LEU 47  47  47  LEU LEU F . n 
F 4 48  PRO 48  48  48  PRO PRO F . n 
F 4 49  PHE 49  49  49  PHE PHE F . n 
F 4 50  GLY 50  50  50  GLY GLY F . n 
F 4 51  ARG 51  51  51  ARG ARG F . n 
F 4 52  LEU 52  52  52  LEU LEU F . n 
F 4 53  GLY 53  53  53  GLY GLY F . n 
F 4 54  HIS 54  54  54  HIS HIS F . n 
F 4 55  GLU 55  55  55  GLU GLU F . n 
F 4 56  PRO 56  56  56  PRO PRO F . n 
F 4 57  GLY 57  57  57  GLY GLY F . n 
F 4 58  LEU 58  58  58  LEU LEU F . n 
F 4 59  VAL 59  59  59  VAL VAL F . n 
F 4 60  GLN 60  60  60  GLN GLN F . n 
F 4 61  LEU 61  61  61  LEU LEU F . n 
F 4 62  VAL 62  62  62  VAL VAL F . n 
F 4 63  ASN 63  63  63  ASN ASN F . n 
F 4 64  TYR 64  64  64  TYR TYR F . n 
F 4 65  TYR 65  65  65  TYR TYR F . n 
F 4 66  ARG 66  66  66  ARG ARG F . n 
F 4 67  GLY 67  67  67  GLY GLY F . n 
F 4 68  ALA 68  68  68  ALA ALA F . n 
F 4 69  ASP 69  69  69  ASP ASP F . n 
F 4 70  LYS 70  70  70  LYS LYS F . n 
F 4 71  LEU 71  71  71  LEU LEU F . n 
F 4 72  CYS 72  72  72  CYS CYS F . n 
F 4 73  ARG 73  73  73  ARG ARG F . n 
F 4 74  LYS 74  74  74  LYS LYS F . n 
F 4 75  ALA 75  75  75  ALA ALA F . n 
F 4 76  SER 76  76  76  SER SER F . n 
F 4 77  LEU 77  77  77  LEU LEU F . n 
F 4 78  VAL 78  78  78  VAL VAL F . n 
F 4 79  LYS 79  79  79  LYS LYS F . n 
F 4 80  LEU 80  80  80  LEU LEU F . n 
F 4 81  ILE 81  81  81  ILE ILE F . n 
F 4 82  LYS 82  82  82  LYS LYS F . n 
F 4 83  THR 83  83  83  THR THR F . n 
F 4 84  SER 84  84  84  SER SER F . n 
F 4 85  PRO 85  85  85  PRO PRO F . n 
F 4 86  GLU 86  86  86  GLU GLU F . n 
F 4 87  LEU 87  87  87  LEU LEU F . n 
F 4 88  SER 88  88  88  SER SER F . n 
F 4 89  GLU 89  89  89  GLU GLU F . n 
F 4 90  SER 90  90  90  SER SER F . n 
F 4 91  CYS 91  91  91  CYS CYS F . n 
F 4 92  THR 92  92  92  THR THR F . n 
F 4 93  TRP 93  93  93  TRP TRP F . n 
F 4 94  PHE 94  94  94  PHE PHE F . n 
F 4 95  PRO 95  95  95  PRO PRO F . n 
F 4 96  GLU 96  96  96  GLU GLU F . n 
F 4 97  SER 97  97  97  SER SER F . n 
F 4 98  TYR 98  98  98  TYR TYR F . n 
F 4 99  VAL 99  99  99  VAL VAL F . n 
F 4 100 ILE 100 100 100 ILE ILE F . n 
F 4 101 TYR 101 101 101 TYR TYR F . n 
F 4 102 PRO 102 102 102 PRO PRO F . n 
F 4 103 THR 103 103 103 THR THR F . n 
F 4 104 ASN 104 104 ?   ?   ?   F . n 
F 4 105 LEU 105 105 ?   ?   ?   F . n 
F 4 106 LYS 106 106 ?   ?   ?   F . n 
F 4 107 THR 107 107 ?   ?   ?   F . n 
F 4 108 PRO 108 108 ?   ?   ?   F . n 
F 4 109 VAL 109 109 ?   ?   ?   F . n 
F 4 110 ALA 110 110 ?   ?   ?   F . n 
F 4 111 PRO 111 111 ?   ?   ?   F . n 
F 4 112 ALA 112 112 ?   ?   ?   F . n 
F 4 113 GLN 113 113 ?   ?   ?   F . n 
F 4 114 ASN 114 114 ?   ?   ?   F . n 
F 4 115 GLY 115 115 ?   ?   ?   F . n 
F 4 116 ILE 116 116 ?   ?   ?   F . n 
F 4 117 ARG 117 117 ?   ?   ?   F . n 
F 4 118 HIS 118 118 ?   ?   ?   F . n 
F 4 119 LEU 119 119 ?   ?   ?   F . n 
F 4 120 ILE 120 120 ?   ?   ?   F . n 
F 4 121 ASN 121 121 ?   ?   ?   F . n 
F 4 122 ASN 122 122 ?   ?   ?   F . n 
F 4 123 THR 123 123 ?   ?   ?   F . n 
F 4 124 ARG 124 124 ?   ?   ?   F . n 
F 4 125 THR 125 125 ?   ?   ?   F . n 
F 4 126 ASP 126 126 ?   ?   ?   F . n 
F 4 127 GLU 127 127 ?   ?   ?   F . n 
F 4 128 ARG 128 128 128 ARG ARG F . n 
F 4 129 GLU 129 129 129 GLU GLU F . n 
F 4 130 VAL 130 130 130 VAL VAL F . n 
F 4 131 PHE 131 131 131 PHE PHE F . n 
F 4 132 LEU 132 132 132 LEU LEU F . n 
F 4 133 ALA 133 133 133 ALA ALA F . n 
F 4 134 ALA 134 134 134 ALA ALA F . n 
F 4 135 TYR 135 135 135 TYR TYR F . n 
F 4 136 ASN 136 136 136 ASN ASN F . n 
F 4 137 ARG 137 137 137 ARG ARG F . n 
F 4 138 ARG 138 138 138 ARG ARG F . n 
F 4 139 ARG 139 139 139 ARG ARG F . n 
F 4 140 GLU 140 140 140 GLU GLU F . n 
F 4 141 GLY 141 141 141 GLY GLY F . n 
F 4 142 ARG 142 142 142 ARG ARG F . n 
F 4 143 GLU 143 143 143 GLU GLU F . n 
F 4 144 GLY 144 144 144 GLY GLY F . n 
F 4 145 ASN 145 145 145 ASN ASN F . n 
F 4 146 VAL 146 146 146 VAL VAL F . n 
F 4 147 TRP 147 147 147 TRP TRP F . n 
F 4 148 ILE 148 148 148 ILE ILE F . n 
F 4 149 ALA 149 149 149 ALA ALA F . n 
F 4 150 LYS 150 150 ?   ?   ?   F . n 
F 4 151 SER 151 151 ?   ?   ?   F . n 
F 4 152 SER 152 152 ?   ?   ?   F . n 
F 4 153 ALA 153 153 ?   ?   ?   F . n 
F 4 154 GLY 154 154 ?   ?   ?   F . n 
F 4 155 ALA 155 155 ?   ?   ?   F . n 
F 4 156 LYS 156 156 ?   ?   ?   F . n 
F 4 157 GLY 157 157 ?   ?   ?   F . n 
F 4 158 GLU 158 158 ?   ?   ?   F . n 
F 4 159 GLY 159 159 ?   ?   ?   F . n 
F 4 160 ILE 160 160 ?   ?   ?   F . n 
F 4 161 LEU 161 161 161 LEU LEU F . n 
F 4 162 ILE 162 162 162 ILE ILE F . n 
F 4 163 SER 163 163 163 SER SER F . n 
F 4 164 SER 164 164 164 SER SER F . n 
F 4 165 GLU 165 165 165 GLU GLU F . n 
F 4 166 ALA 166 166 166 ALA ALA F . n 
F 4 167 SER 167 167 167 SER SER F . n 
F 4 168 GLU 168 168 168 GLU GLU F . n 
F 4 169 LEU 169 169 169 LEU LEU F . n 
F 4 170 LEU 170 170 170 LEU LEU F . n 
F 4 171 ASP 171 171 171 ASP ASP F . n 
F 4 172 PHE 172 172 172 PHE PHE F . n 
F 4 173 ILE 173 173 173 ILE ILE F . n 
F 4 174 ASP 174 174 174 ASP ASP F . n 
F 4 175 GLU 175 175 175 GLU GLU F . n 
F 4 176 GLN 176 176 176 GLN GLN F . n 
F 4 177 GLY 177 177 177 GLY GLY F . n 
F 4 178 GLN 178 178 178 GLN GLN F . n 
F 4 179 VAL 179 179 179 VAL VAL F . n 
F 4 180 HIS 180 180 180 HIS HIS F . n 
F 4 181 VAL 181 181 181 VAL VAL F . n 
F 4 182 ILE 182 182 182 ILE ILE F . n 
F 4 183 GLN 183 183 183 GLN GLN F . n 
F 4 184 LYS 184 184 184 LYS LYS F . n 
F 4 185 TYR 185 185 185 TYR TYR F . n 
F 4 186 LEU 186 186 186 LEU LEU F . n 
F 4 187 GLU 187 187 187 GLU GLU F . n 
F 4 188 LYS 188 188 188 LYS LYS F . n 
F 4 189 PRO 189 189 189 PRO PRO F . n 
F 4 190 LEU 190 190 190 LEU LEU F . n 
F 4 191 LEU 191 191 191 LEU LEU F . n 
F 4 192 LEU 192 192 192 LEU LEU F . n 
F 4 193 GLU 193 193 193 GLU GLU F . n 
F 4 194 PRO 194 194 194 PRO PRO F . n 
F 4 195 GLY 195 195 195 GLY GLY F . n 
F 4 196 HIS 196 196 196 HIS HIS F . n 
F 4 197 ARG 197 197 197 ARG ARG F . n 
F 4 198 LYS 198 198 198 LYS LYS F . n 
F 4 199 PHE 199 199 199 PHE PHE F . n 
F 4 200 ASP 200 200 200 ASP ASP F . n 
F 4 201 ILE 201 201 201 ILE ILE F . n 
F 4 202 ARG 202 202 202 ARG ARG F . n 
F 4 203 SER 203 203 203 SER SER F . n 
F 4 204 TRP 204 204 204 TRP TRP F . n 
F 4 205 VAL 205 205 205 VAL VAL F . n 
F 4 206 LEU 206 206 206 LEU LEU F . n 
F 4 207 VAL 207 207 207 VAL VAL F . n 
F 4 208 ASP 208 208 208 ASP ASP F . n 
F 4 209 HIS 209 209 209 HIS HIS F . n 
F 4 210 LEU 210 210 210 LEU LEU F . n 
F 4 211 TYR 211 211 211 TYR TYR F . n 
F 4 212 ASN 212 212 212 ASN ASN F . n 
F 4 213 ILE 213 213 213 ILE ILE F . n 
F 4 214 TYR 214 214 214 TYR TYR F . n 
F 4 215 LEU 215 215 215 LEU LEU F . n 
F 4 216 TYR 216 216 216 TYR TYR F . n 
F 4 217 ARG 217 217 217 ARG ARG F . n 
F 4 218 GLU 218 218 218 GLU GLU F . n 
F 4 219 GLY 219 219 219 GLY GLY F . n 
F 4 220 VAL 220 220 220 VAL VAL F . n 
F 4 221 LEU 221 221 221 LEU LEU F . n 
F 4 222 ARG 222 222 222 ARG ARG F . n 
F 4 223 THR 223 223 223 THR THR F . n 
F 4 224 SER 224 224 224 SER SER F . n 
F 4 225 SER 225 225 225 SER SER F . n 
F 4 226 GLU 226 226 226 GLU GLU F . n 
F 4 227 PRO 227 227 227 PRO PRO F . n 
F 4 228 TYR 228 228 228 TYR TYR F . n 
F 4 229 ASN 229 229 229 ASN ASN F . n 
F 4 230 SER 230 230 230 SER SER F . n 
F 4 231 ALA 231 231 231 ALA ALA F . n 
F 4 232 ASN 232 232 232 ASN ASN F . n 
F 4 233 PHE 233 233 233 PHE PHE F . n 
F 4 234 GLN 234 234 234 GLN GLN F . n 
F 4 235 ASP 235 235 235 ASP ASP F . n 
F 4 236 LYS 236 236 236 LYS LYS F . n 
F 4 237 THR 237 237 237 THR THR F . n 
F 4 238 CYS 238 238 238 CYS CYS F . n 
F 4 239 HIS 239 239 239 HIS HIS F . n 
F 4 240 LEU 240 240 240 LEU LEU F . n 
F 4 241 THR 241 241 241 THR THR F . n 
F 4 242 ASN 242 242 242 ASN ASN F . n 
F 4 243 HIS 243 243 243 HIS HIS F . n 
F 4 244 CYS 244 244 244 CYS CYS F . n 
F 4 245 ILE 245 245 245 ILE ILE F . n 
F 4 246 GLN 246 246 246 GLN GLN F . n 
F 4 247 LYS 247 247 247 LYS LYS F . n 
F 4 248 GLU 248 248 ?   ?   ?   F . n 
F 4 249 TYR 249 249 ?   ?   ?   F . n 
F 4 250 SER 250 250 ?   ?   ?   F . n 
F 4 251 LYS 251 251 ?   ?   ?   F . n 
F 4 252 ASN 252 252 252 ASN ASN F . n 
F 4 253 TYR 253 253 253 TYR TYR F . n 
F 4 254 GLY 254 254 254 GLY GLY F . n 
F 4 255 ARG 255 255 255 ARG ARG F . n 
F 4 256 TYR 256 256 256 TYR TYR F . n 
F 4 257 GLU 257 257 257 GLU GLU F . n 
F 4 258 GLU 258 258 258 GLU GLU F . n 
F 4 259 GLY 259 259 259 GLY GLY F . n 
F 4 260 ASN 260 260 260 ASN ASN F . n 
F 4 261 GLU 261 261 261 GLU GLU F . n 
F 4 262 MET 262 262 262 MET MET F . n 
F 4 263 PHE 263 263 263 PHE PHE F . n 
F 4 264 PHE 264 264 264 PHE PHE F . n 
F 4 265 GLU 265 265 265 GLU GLU F . n 
F 4 266 GLU 266 266 266 GLU GLU F . n 
F 4 267 PHE 267 267 267 PHE PHE F . n 
F 4 268 ASN 268 268 268 ASN ASN F . n 
F 4 269 GLN 269 269 269 GLN GLN F . n 
F 4 270 TYR 270 270 270 TYR TYR F . n 
F 4 271 LEU 271 271 271 LEU LEU F . n 
F 4 272 MET 272 272 272 MET MET F . n 
F 4 273 ASP 273 273 273 ASP ASP F . n 
F 4 274 ALA 274 274 274 ALA ALA F . n 
F 4 275 LEU 275 275 275 LEU LEU F . n 
F 4 276 ASN 276 276 276 ASN ASN F . n 
F 4 277 THR 277 277 277 THR THR F . n 
F 4 278 THR 278 278 278 THR THR F . n 
F 4 279 LEU 279 279 279 LEU LEU F . n 
F 4 280 GLU 280 280 280 GLU GLU F . n 
F 4 281 ASN 281 281 281 ASN ASN F . n 
F 4 282 SER 282 282 282 SER SER F . n 
F 4 283 ILE 283 283 283 ILE ILE F . n 
F 4 284 LEU 284 284 284 LEU LEU F . n 
F 4 285 LEU 285 285 285 LEU LEU F . n 
F 4 286 GLN 286 286 286 GLN GLN F . n 
F 4 287 ILE 287 287 287 ILE ILE F . n 
F 4 288 LYS 288 288 288 LYS LYS F . n 
F 4 289 HIS 289 289 289 HIS HIS F . n 
F 4 290 ILE 290 290 290 ILE ILE F . n 
F 4 291 ILE 291 291 291 ILE ILE F . n 
F 4 292 ARG 292 292 292 ARG ARG F . n 
F 4 293 SER 293 293 293 SER SER F . n 
F 4 294 CYS 294 294 294 CYS CYS F . n 
F 4 295 LEU 295 295 295 LEU LEU F . n 
F 4 296 MET 296 296 296 MET MET F . n 
F 4 297 CYS 297 297 297 CYS CYS F . n 
F 4 298 ILE 298 298 298 ILE ILE F . n 
F 4 299 GLU 299 299 299 GLU GLU F . n 
F 4 300 PRO 300 300 300 PRO PRO F . n 
F 4 301 ALA 301 301 301 ALA ALA F . n 
F 4 302 ILE 302 302 302 ILE ILE F . n 
F 4 303 SER 303 303 303 SER SER F . n 
F 4 304 THR 304 304 304 THR THR F . n 
F 4 305 LYS 305 305 305 LYS LYS F . n 
F 4 306 HIS 306 306 306 HIS HIS F . n 
F 4 307 LEU 307 307 307 LEU LEU F . n 
F 4 308 HIS 308 308 308 HIS HIS F . n 
F 4 309 TYR 309 309 309 TYR TYR F . n 
F 4 310 GLN 310 310 310 GLN GLN F . n 
F 4 311 SER 311 311 311 SER SER F . n 
F 4 312 PHE 312 312 312 PHE PHE F . n 
F 4 313 GLN 313 313 313 GLN GLN F . n 
F 4 314 LEU 314 314 314 LEU LEU F . n 
F 4 315 PHE 315 315 315 PHE PHE F . n 
F 4 316 GLY 316 316 316 GLY GLY F . n 
F 4 317 PHE 317 317 317 PHE PHE F . n 
F 4 318 ASP 318 318 318 ASP ASP F . n 
F 4 319 PHE 319 319 319 PHE PHE F . n 
F 4 320 MET 320 320 320 MET MET F . n 
F 4 321 VAL 321 321 321 VAL VAL F . n 
F 4 322 ASP 322 322 322 ASP ASP F . n 
F 4 323 GLU 323 323 323 GLU GLU F . n 
F 4 324 GLU 324 324 324 GLU GLU F . n 
F 4 325 LEU 325 325 325 LEU LEU F . n 
F 4 326 LYS 326 326 326 LYS LYS F . n 
F 4 327 VAL 327 327 327 VAL VAL F . n 
F 4 328 TRP 328 328 328 TRP TRP F . n 
F 4 329 LEU 329 329 329 LEU LEU F . n 
F 4 330 ILE 330 330 330 ILE ILE F . n 
F 4 331 GLU 331 331 331 GLU GLU F . n 
F 4 332 VAL 332 332 332 VAL VAL F . n 
F 4 333 ASN 333 333 333 ASN ASN F . n 
F 4 334 GLY 334 334 334 GLY GLY F . n 
F 4 335 ALA 335 335 335 ALA ALA F . n 
F 4 336 PRO 336 336 336 PRO PRO F . n 
F 4 337 ALA 337 337 337 ALA ALA F . n 
F 4 338 CYS 338 338 338 CYS CYS F . n 
F 4 339 ALA 339 339 339 ALA ALA F . n 
F 4 340 GLN 340 340 340 GLN GLN F . n 
F 4 341 LYS 341 341 341 LYS LYS F . n 
F 4 342 LEU 342 342 342 LEU LEU F . n 
F 4 343 TYR 343 343 343 TYR TYR F . n 
F 4 344 ALA 344 344 344 ALA ALA F . n 
F 4 345 GLU 345 345 345 GLU GLU F . n 
F 4 346 LEU 346 346 346 LEU LEU F . n 
F 4 347 CYS 347 347 347 CYS CYS F . n 
F 4 348 GLN 348 348 348 GLN GLN F . n 
F 4 349 GLY 349 349 349 GLY GLY F . n 
F 4 350 ILE 350 350 350 ILE ILE F . n 
F 4 351 VAL 351 351 351 VAL VAL F . n 
F 4 352 ASP 352 352 352 ASP ASP F . n 
F 4 353 VAL 353 353 353 VAL VAL F . n 
F 4 354 ALA 354 354 354 ALA ALA F . n 
F 4 355 ILE 355 355 355 ILE ILE F . n 
F 4 356 SER 356 356 356 SER SER F . n 
F 4 357 SER 357 357 357 SER SER F . n 
F 4 358 VAL 358 358 358 VAL VAL F . n 
F 4 359 PHE 359 359 359 PHE PHE F . n 
F 4 360 PRO 360 360 360 PRO PRO F . n 
F 4 361 LEU 361 361 361 LEU LEU F . n 
F 4 362 ALA 362 362 362 ALA ALA F . n 
F 4 363 ASP 363 363 ?   ?   ?   F . n 
F 4 364 THR 364 364 ?   ?   ?   F . n 
F 4 365 GLY 365 365 ?   ?   ?   F . n 
F 4 366 GLN 366 366 ?   ?   ?   F . n 
F 4 367 LYS 367 367 ?   ?   ?   F . n 
F 4 368 THR 368 368 ?   ?   ?   F . n 
F 4 369 SER 369 369 ?   ?   ?   F . n 
F 4 370 GLN 370 370 ?   ?   ?   F . n 
F 4 371 PRO 371 371 ?   ?   ?   F . n 
F 4 372 THR 372 372 372 THR THR F . n 
F 4 373 SER 373 373 373 SER SER F . n 
F 4 374 ILE 374 374 374 ILE ILE F . n 
F 4 375 PHE 375 375 375 PHE PHE F . n 
F 4 376 ILE 376 376 376 ILE ILE F . n 
F 4 377 LYS 377 377 377 LYS LYS F . n 
F 4 378 LEU 378 378 378 LEU LEU F . n 
F 4 379 HIS 379 379 379 HIS HIS F . n 
F 4 380 HIS 380 380 380 HIS HIS F . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D6L 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D6L 
_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  CA    1 502 502 CA    CA  A . 
I 7  MG    1 503 503 MG    MG  A . 
J 8  A1D6L 1 501 505 A1D6L LIG B . 
K 9  GDP   1 502 501 GDP   GDP B . 
L 10 MES   1 503 502 MES   MES B . 
M 10 MES   1 504 503 MES   MES B . 
N 7  MG    1 505 504 MG    MG  B . 
O 5  GTP   1 501 501 GTP   GTP C . 
P 6  CA    1 502 502 CA    CA  C . 
Q 7  MG    1 503 503 MG    MG  C . 
R 8  A1D6L 1 501 502 A1D6L LIG D . 
S 9  GDP   1 502 501 GDP   GDP D . 
T 11 ACP   1 401 401 ACP   ACP F . 
# 
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 LYS 163 ? CG  ? A LYS 163 CG  
2  1 Y 1 A LYS 163 ? CD  ? A LYS 163 CD  
3  1 Y 1 A LYS 163 ? CE  ? A LYS 163 CE  
4  1 Y 1 A LYS 163 ? NZ  ? A LYS 163 NZ  
5  1 Y 1 A TYR 262 ? CG  ? A TYR 262 CG  
6  1 Y 1 A TYR 262 ? CD1 ? A TYR 262 CD1 
7  1 Y 1 A TYR 262 ? CD2 ? A TYR 262 CD2 
8  1 Y 1 A TYR 262 ? CE1 ? A TYR 262 CE1 
9  1 Y 1 A TYR 262 ? CE2 ? A TYR 262 CE2 
10 1 Y 1 A TYR 262 ? CZ  ? A TYR 262 CZ  
11 1 Y 1 A TYR 262 ? OH  ? A TYR 262 OH  
12 1 Y 1 B LYS 122 ? CG  ? B LYS 122 CG  
13 1 Y 1 B LYS 122 ? CD  ? B LYS 122 CD  
14 1 Y 1 B LYS 122 ? CE  ? B LYS 122 CE  
15 1 Y 1 B LYS 122 ? NZ  ? B LYS 122 NZ  
16 1 Y 1 B ARG 282 ? CG  ? B ARG 282 CG  
17 1 Y 1 B ARG 282 ? CD  ? B ARG 282 CD  
18 1 Y 1 B ARG 282 ? NE  ? B ARG 282 NE  
19 1 Y 1 B ARG 282 ? CZ  ? B ARG 282 CZ  
20 1 Y 1 B ARG 282 ? NH1 ? B ARG 282 NH1 
21 1 Y 1 B ARG 282 ? NH2 ? B ARG 282 NH2 
22 1 Y 1 C LYS 280 ? CG  ? C LYS 280 CG  
23 1 Y 1 C LYS 280 ? CD  ? C LYS 280 CD  
24 1 Y 1 C LYS 280 ? CE  ? C LYS 280 CE  
25 1 Y 1 C LYS 280 ? NZ  ? C LYS 280 NZ  
26 1 Y 1 D ARG 359 ? CG  ? D ARG 359 CG  
27 1 Y 1 D ARG 359 ? CD  ? D ARG 359 CD  
28 1 Y 1 D ARG 359 ? NE  ? D ARG 359 NE  
29 1 Y 1 D ARG 359 ? CZ  ? D ARG 359 CZ  
30 1 Y 1 D ARG 359 ? NH1 ? D ARG 359 NH1 
31 1 Y 1 D ARG 359 ? NH2 ? D ARG 359 NH2 
32 1 Y 1 D ASP 431 ? CG  ? D ASP 431 CG  
33 1 Y 1 D ASP 431 ? OD1 ? D ASP 431 OD1 
34 1 Y 1 D ASP 431 ? OD2 ? D ASP 431 OD2 
35 1 Y 1 F LEU 169 ? CG  ? F LEU 169 CG  
36 1 Y 1 F LEU 169 ? CD1 ? F LEU 169 CD1 
37 1 Y 1 F LEU 169 ? CD2 ? F LEU 169 CD2 
38 1 Y 1 F LYS 184 ? CG  ? F LYS 184 CG  
39 1 Y 1 F LYS 184 ? CD  ? F LYS 184 CD  
40 1 Y 1 F LYS 184 ? CE  ? F LYS 184 CE  
41 1 Y 1 F LYS 184 ? NZ  ? F LYS 184 NZ  
42 1 Y 1 F LYS 236 ? CG  ? F LYS 236 CG  
43 1 Y 1 F LYS 236 ? CD  ? F LYS 236 CD  
44 1 Y 1 F LYS 236 ? CE  ? F LYS 236 CE  
45 1 Y 1 F LYS 236 ? NZ  ? F LYS 236 NZ  
46 1 Y 1 F LEU 240 ? CG  ? F LEU 240 CG  
47 1 Y 1 F LEU 240 ? CD1 ? F LEU 240 CD1 
48 1 Y 1 F LEU 240 ? CD2 ? F LEU 240 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  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                     8YEU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.949 
_cell.length_a_esd                 ? 
_cell.length_b                     156.625 
_cell.length_b_esd                 ? 
_cell.length_c                     181.639 
_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                         8YEU 
_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                   8YEU 
_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             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.01 
_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 4000, 5% Glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2' 
_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         2023-07-19 
_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   0.97853 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YEU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.05 
_reflns.d_resolution_low                               118.62 
_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                                     57813 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_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                                   0.978 
_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                                    3.05 
_reflns_shell.d_res_low                                     3.21 
_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                             8290 
_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                                  0.792 
_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                                 8YEU 
_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                            3.05 
_refine.ls_d_res_low                             62.76 
_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                     57712 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 3.46 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2122 
_refine.ls_R_factor_R_free                       0.2678 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2102 
_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                 27.13 
_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        17202 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         228 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               17430 
_refine_hist.d_res_high                       3.05 
_refine_hist.d_res_low                        62.76 
# 
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' ? 13.346 ? 2444 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 2626 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 3127 ? 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' 3.05 3.13 . . 140 3928 100.00 . . . . 0.2574 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 3.13 3.21 . . 141 3890 100.00 . . . . 0.2521 . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 3.21 3.30 . . 141 3957 100.00 . . . . 0.2578 . . . . . . . . . . . 0.3169 
'X-RAY DIFFRACTION' 3.30 3.41 . . 142 3944 100.00 . . . . 0.2673 . . . . . . . . . . . 0.3844 
'X-RAY DIFFRACTION' 3.41 3.53 . . 141 3935 100.00 . . . . 0.2438 . . . . . . . . . . . 0.3556 
'X-RAY DIFFRACTION' 3.53 3.67 . . 142 3928 100.00 . . . . 0.2274 . . . . . . . . . . . 0.2745 
'X-RAY DIFFRACTION' 3.67 3.84 . . 142 3974 100.00 . . . . 0.2132 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 3.84 4.04 . . 142 3957 100.00 . . . . 0.2083 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 4.04 4.30 . . 142 3960 100.00 . . . . 0.2065 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 4.30 4.63 . . 143 3979 100.00 . . . . 0.1662 . . . . . . . . . . . 0.2099 
'X-RAY DIFFRACTION' 4.63 5.10 . . 143 3997 100.00 . . . . 0.1692 . . . . . . . . . . . 0.2236 
'X-RAY DIFFRACTION' 5.10 5.83 . . 144 4027 100.00 . . . . 0.2032 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 5.83 7.34 . . 145 4040 100.00 . . . . 0.2243 . . . . . . . . . . . 0.2603 
# 
_struct.entry_id                     8YEU 
_struct.title                        'Tubulin-RB3_SLD-TTL in complex with compound 2NH2' 
_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        8YEU 
_struct_keywords.text            'Inhibitor, complex, tubulin, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1  ? 
B N N 2  ? 
C N N 1  ? 
D N N 2  ? 
E N N 3  ? 
F N N 4  ? 
G N N 5  ? 
H N N 6  ? 
I N N 7  ? 
J N N 8  ? 
K N N 9  ? 
L N N 10 ? 
M N N 10 ? 
N N N 7  ? 
O N N 5  ? 
P N N 6  ? 
Q N N 7  ? 
R N N 8  ? 
S N N 9  ? 
T N N 11 ? 
# 
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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
1  
2 UNP A0A8D0VN39_PIG   A0A8D0VN39 ? 2 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
1  
3 UNP STMN4_RAT        P63043     ? 3 
;DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ
KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
49 
4 UNP A0A8C9FGJ1_PAVCR A0A8C9FGJ1 ? 4 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKL
;
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 8YEU A 1 ? 440 ? Q2XVP4     1  ? 440 ? 1 440 
2 2 8YEU B 1 ? 431 ? A0A8D0VN39 1  ? 431 ? 1 431 
3 1 8YEU C 1 ? 440 ? Q2XVP4     1  ? 440 ? 1 440 
4 2 8YEU D 1 ? 431 ? A0A8D0VN39 1  ? 431 ? 1 431 
5 3 8YEU E 3 ? 143 ? P63043     49 ? 189 ? 5 145 
6 4 8YEU F 1 ? 378 ? A0A8C9FGJ1 1  ? 378 ? 1 378 
# 
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 
5 8YEU MET E 1   ? UNP P63043     ? ? 'initiating methionine' 3   1 
5 8YEU ALA E 2   ? UNP P63043     ? ? 'expression tag'        4   2 
6 8YEU HIS F 379 ? UNP A0A8C9FGJ1 ? ? 'expression tag'        379 3 
6 8YEU HIS F 380 ? UNP A0A8C9FGJ1 ? ? 'expression tag'        380 4 
# 
_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,R,S,T 
# 
_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 SER A 48  ? THR A 51  ? SER A 48  THR A 51  5 ? 4  
HELX_P HELX_P3   AA3 GLU A 71  ? ARG A 79  ? GLU A 71  ARG A 79  1 ? 9  
HELX_P HELX_P4   AA4 TYR A 83  ? PHE A 87  ? TYR A 83  PHE A 87  5 ? 5  
HELX_P HELX_P5   AA5 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P6   AA6 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P7   AA7 ILE A 110 ? GLU A 113 ? ILE A 110 GLU A 113 5 ? 4  
HELX_P HELX_P8   AA8 ILE A 114 ? ASP A 127 ? ILE A 114 ASP A 127 1 ? 14 
HELX_P HELX_P9   AA9 GLY A 143 ? TYR A 161 ? GLY A 143 TYR A 161 1 ? 19 
HELX_P HELX_P10  AB1 VAL A 182 ? LEU A 195 ? VAL A 182 LEU A 195 1 ? 14 
HELX_P HELX_P11  AB2 GLU A 196 ? SER A 198 ? GLU A 196 SER A 198 5 ? 3  
HELX_P HELX_P12  AB3 ASN A 206 ? ASN A 216 ? ASN A 206 ASN A 216 1 ? 11 
HELX_P HELX_P13  AB4 THR A 223 ? PHE A 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P14  AB5 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P15  AB6 SER A 287 ? CYS A 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P16  AB7 PHE A 296 ? GLN A 301 ? PHE A 296 GLN A 301 5 ? 6  
HELX_P HELX_P17  AB8 ASP A 306 ? GLY A 310 ? ASP A 306 GLY A 310 5 ? 5  
HELX_P HELX_P18  AB9 VAL A 324 ? ARG A 339 ? VAL A 324 ARG A 339 1 ? 16 
HELX_P HELX_P19  AC1 ILE A 384 ? LYS A 401 ? ILE A 384 LYS A 401 1 ? 18 
HELX_P HELX_P20  AC2 PHE A 404 ? GLY A 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P21  AC3 GLU A 414 ? GLY A 436 ? GLU A 414 GLY A 436 1 ? 23 
HELX_P HELX_P22  AC4 GLY B 10  ? HIS B 28  ? GLY B 10  HIS B 28  1 ? 19 
HELX_P HELX_P23  AC5 ASP B 41  ? ARG B 46  ? ASP B 41  ARG B 46  1 ? 6  
HELX_P HELX_P24  AC6 ILE B 47  ? VAL B 49  ? ILE B 47  VAL B 49  5 ? 3  
HELX_P HELX_P25  AC7 PRO B 70  ? GLY B 79  ? PRO B 70  GLY B 79  1 ? 10 
HELX_P HELX_P26  AC8 PHE B 81  ? PHE B 85  ? PHE B 81  PHE B 85  5 ? 5  
HELX_P HELX_P27  AC9 ARG B 86  ? ASP B 88  ? ARG B 86  ASP B 88  5 ? 3  
HELX_P HELX_P28  AD1 ASN B 100 ? TYR B 106 ? ASN B 100 TYR B 106 1 ? 7  
HELX_P HELX_P29  AD2 THR B 107 ? CYS B 127 ? THR B 107 CYS B 127 1 ? 21 
HELX_P HELX_P30  AD3 GLY B 142 ? TYR B 159 ? GLY B 142 TYR B 159 1 ? 18 
HELX_P HELX_P31  AD4 SER B 172 ? SER B 176 ? SER B 172 SER B 176 5 ? 5  
HELX_P HELX_P32  AD5 VAL B 180 ? THR B 196 ? VAL B 180 THR B 196 1 ? 17 
HELX_P HELX_P33  AD6 ASN B 204 ? ARG B 213 ? ASN B 204 ARG B 213 1 ? 10 
HELX_P HELX_P34  AD7 THR B 221 ? PHE B 242 ? THR B 221 PHE B 242 1 ? 22 
HELX_P HELX_P35  AD8 ASP B 249 ? VAL B 258 ? ASP B 249 VAL B 258 1 ? 10 
HELX_P HELX_P36  AD9 THR B 285 ? PHE B 294 ? THR B 285 PHE B 294 1 ? 10 
HELX_P HELX_P37  AE1 ASP B 295 ? MET B 299 ? ASP B 295 MET B 299 5 ? 5  
HELX_P HELX_P38  AE2 ASP B 304 ? GLY B 308 ? ASP B 304 GLY B 308 5 ? 5  
HELX_P HELX_P39  AE3 SER B 322 ? ASN B 337 ? SER B 322 ASN B 337 1 ? 16 
HELX_P HELX_P40  AE4 SER B 338 ? PHE B 341 ? SER B 338 PHE B 341 5 ? 4  
HELX_P HELX_P41  AE5 ILE B 374 ? ARG B 390 ? ILE B 374 ARG B 390 1 ? 17 
HELX_P HELX_P42  AE6 LEU B 395 ? GLY B 400 ? LEU B 395 GLY B 400 1 ? 6  
HELX_P HELX_P43  AE7 ASP B 404 ? TYR B 425 ? ASP B 404 TYR B 425 1 ? 22 
HELX_P HELX_P44  AE8 GLY C 10  ? GLY C 29  ? GLY C 10  GLY C 29  1 ? 20 
HELX_P HELX_P45  AE9 ASP C 47  ? THR C 51  ? ASP C 47  THR C 51  5 ? 5  
HELX_P HELX_P46  AF1 GLU C 71  ? GLY C 81  ? GLU C 71  GLY C 81  1 ? 11 
HELX_P HELX_P47  AF2 TYR C 83  ? PHE C 87  ? TYR C 83  PHE C 87  5 ? 5  
HELX_P HELX_P48  AF3 HIS C 88  ? GLU C 90  ? HIS C 88  GLU C 90  5 ? 3  
HELX_P HELX_P49  AF4 ASN C 102 ? TYR C 108 ? ASN C 102 TYR C 108 1 ? 7  
HELX_P HELX_P50  AF5 ILE C 110 ? GLU C 113 ? ILE C 110 GLU C 113 5 ? 4  
HELX_P HELX_P51  AF6 ILE C 114 ? GLN C 128 ? ILE C 114 GLN C 128 1 ? 15 
HELX_P HELX_P52  AF7 GLY C 143 ? GLY C 162 ? GLY C 143 GLY C 162 1 ? 20 
HELX_P HELX_P53  AF8 VAL C 182 ? LEU C 195 ? VAL C 182 LEU C 195 1 ? 14 
HELX_P HELX_P54  AF9 GLU C 196 ? SER C 198 ? GLU C 196 SER C 198 5 ? 3  
HELX_P HELX_P55  AG1 ASN C 206 ? LEU C 217 ? ASN C 206 LEU C 217 1 ? 12 
HELX_P HELX_P56  AG2 THR C 223 ? PHE C 244 ? THR C 223 PHE C 244 1 ? 22 
HELX_P HELX_P57  AG3 ASP C 251 ? VAL C 260 ? ASP C 251 VAL C 260 1 ? 10 
HELX_P HELX_P58  AG4 SER C 277 ? TYR C 282 ? SER C 277 TYR C 282 1 ? 6  
HELX_P HELX_P59  AG5 SER C 287 ? PHE C 296 ? SER C 287 PHE C 296 1 ? 10 
HELX_P HELX_P60  AG6 GLU C 297 ? GLN C 301 ? GLU C 297 GLN C 301 5 ? 5  
HELX_P HELX_P61  AG7 ASP C 306 ? GLY C 310 ? ASP C 306 GLY C 310 5 ? 5  
HELX_P HELX_P62  AG8 VAL C 324 ? ARG C 339 ? VAL C 324 ARG C 339 1 ? 16 
HELX_P HELX_P63  AG9 ILE C 384 ? LYS C 401 ? ILE C 384 LYS C 401 1 ? 18 
HELX_P HELX_P64  AH1 PHE C 404 ? GLY C 410 ? PHE C 404 GLY C 410 1 ? 7  
HELX_P HELX_P65  AH2 GLU C 414 ? VAL C 437 ? GLU C 414 VAL C 437 1 ? 24 
HELX_P HELX_P66  AH3 ALA D 9   ? GLY D 29  ? ALA D 9   GLY D 29  1 ? 21 
HELX_P HELX_P67  AH4 SER D 40  ? LEU D 44  ? SER D 40  LEU D 44  5 ? 5  
HELX_P HELX_P68  AH5 ARG D 46  ? VAL D 49  ? ARG D 46  VAL D 49  5 ? 4  
HELX_P HELX_P69  AH6 GLU D 69  ? GLY D 79  ? GLU D 69  GLY D 79  1 ? 11 
HELX_P HELX_P70  AH7 ARG D 86  ? ASP D 88  ? ARG D 86  ASP D 88  5 ? 3  
HELX_P HELX_P71  AH8 ASN D 100 ? TYR D 106 ? ASN D 100 TYR D 106 1 ? 7  
HELX_P HELX_P72  AH9 THR D 107 ? SER D 126 ? THR D 107 SER D 126 1 ? 20 
HELX_P HELX_P73  AI1 GLY D 142 ? TYR D 159 ? GLY D 142 TYR D 159 1 ? 18 
HELX_P HELX_P74  AI2 VAL D 180 ? THR D 196 ? VAL D 180 THR D 196 1 ? 17 
HELX_P HELX_P75  AI3 ASN D 204 ? THR D 214 ? ASN D 204 THR D 214 1 ? 11 
HELX_P HELX_P76  AI4 THR D 221 ? THR D 237 ? THR D 221 THR D 237 1 ? 17 
HELX_P HELX_P77  AI5 THR D 237 ? PHE D 242 ? THR D 237 PHE D 242 1 ? 6  
HELX_P HELX_P78  AI6 ASP D 249 ? VAL D 258 ? ASP D 249 VAL D 258 1 ? 10 
HELX_P HELX_P79  AI7 THR D 285 ? PHE D 294 ? THR D 285 PHE D 294 1 ? 10 
HELX_P HELX_P80  AI8 ASP D 295 ? MET D 299 ? ASP D 295 MET D 299 5 ? 5  
HELX_P HELX_P81  AI9 ASP D 304 ? GLY D 308 ? ASP D 304 GLY D 308 5 ? 5  
HELX_P HELX_P82  AJ1 SER D 322 ? ASN D 337 ? SER D 322 ASN D 337 1 ? 16 
HELX_P HELX_P83  AJ2 SER D 338 ? PHE D 341 ? SER D 338 PHE D 341 5 ? 4  
HELX_P HELX_P84  AJ3 ILE D 374 ? ARG D 390 ? ILE D 374 ARG D 390 1 ? 17 
HELX_P HELX_P85  AJ4 LEU D 395 ? GLY D 400 ? LEU D 395 GLY D 400 1 ? 6  
HELX_P HELX_P86  AJ5 ASP D 404 ? ALA D 428 ? ASP D 404 ALA D 428 1 ? 25 
HELX_P HELX_P87  AJ6 SER E 44  ? LEU E 137 ? SER E 46  LEU E 139 1 ? 94 
HELX_P HELX_P88  AJ7 SER F 11  ? ALA F 23  ? SER F 11  ALA F 23  1 ? 13 
HELX_P HELX_P89  AJ8 PRO F 48  ? LEU F 52  ? PRO F 48  LEU F 52  5 ? 5  
HELX_P HELX_P90  AJ9 ALA F 68  ? ARG F 73  ? ALA F 68  ARG F 73  1 ? 6  
HELX_P HELX_P91  AK1 ARG F 73  ? SER F 84  ? ARG F 73  SER F 84  1 ? 12 
HELX_P HELX_P92  AK2 VAL F 130 ? GLU F 140 ? VAL F 130 GLU F 140 1 ? 11 
HELX_P HELX_P93  AK3 GLU F 165 ? ASP F 174 ? GLU F 165 ASP F 174 1 ? 10 
HELX_P HELX_P94  AK4 GLU F 257 ? GLY F 259 ? GLU F 257 GLY F 259 5 ? 3  
HELX_P HELX_P95  AK5 PHE F 264 ? ASN F 276 ? PHE F 264 ASN F 276 1 ? 13 
HELX_P HELX_P96  AK6 THR F 278 ? ILE F 283 ? THR F 278 ILE F 283 1 ? 6  
HELX_P HELX_P97  AK7 ILE F 283 ? ILE F 298 ? ILE F 283 ILE F 298 1 ? 16 
HELX_P HELX_P98  AK8 ILE F 298 ? SER F 303 ? ILE F 298 SER F 303 1 ? 6  
HELX_P HELX_P99  AK9 ALA F 339 ? LYS F 341 ? ALA F 339 LYS F 341 5 ? 3  
HELX_P HELX_P100 AL1 LEU F 342 ? ILE F 355 ? LEU F 342 ILE F 355 1 ? 14 
# 
_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 H CA . CA ? ? A ASP 39  A CA 502 1_555 ? ? ? ? ? ? ? 3.039 ? ? 
metalc2  metalc ? ? A ASP 39  OD2 ? ? ? 1_555 H CA . CA ? ? A ASP 39  A CA 502 1_555 ? ? ? ? ? ? ? 3.081 ? ? 
metalc3  metalc ? ? A THR 41  O   ? ? ? 1_555 H CA . CA ? ? A THR 41  A CA 502 1_555 ? ? ? ? ? ? ? 2.919 ? ? 
metalc4  metalc ? ? A THR 41  OG1 ? ? ? 1_555 H CA . CA ? ? A THR 41  A CA 502 1_555 ? ? ? ? ? ? ? 3.057 ? ? 
metalc5  metalc ? ? A GLY 44  O   ? ? ? 1_555 H CA . CA ? ? A GLY 44  A CA 502 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc6  metalc ? ? A ASP 47  OD2 ? ? ? 1_555 H CA . CA ? ? A ASP 47  A CA 502 1_555 ? ? ? ? ? ? ? 2.994 ? ? 
metalc7  metalc ? ? A GLU 55  OE2 ? ? ? 1_555 H CA . CA ? ? A GLU 55  A CA 502 1_555 ? ? ? ? ? ? ? 2.560 ? ? 
metalc8  metalc ? ? A GLU 71  OE1 ? ? ? 1_555 I MG . MG ? ? A GLU 71  A MG 503 1_555 ? ? ? ? ? ? ? 2.644 ? ? 
metalc9  metalc ? ? G GTP .   O2G ? ? ? 1_555 I MG . MG ? ? A GTP 501 A MG 503 1_555 ? ? ? ? ? ? ? 2.750 ? ? 
metalc10 metalc ? ? G GTP .   O2B ? ? ? 1_555 I MG . MG ? ? A GTP 501 A MG 503 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc11 metalc ? ? B GLN 11  OE1 ? ? ? 1_555 N MG . MG ? ? B GLN 11  B MG 505 1_555 ? ? ? ? ? ? ? 1.759 ? ? 
metalc12 metalc ? ? B ASP 177 OD2 ? ? ? 1_555 N MG . MG ? ? B ASP 177 B MG 505 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc13 metalc ? ? K GDP .   O1A ? ? ? 1_555 N MG . MG ? ? B GDP 502 B MG 505 1_555 ? ? ? ? ? ? ? 2.622 ? ? 
metalc14 metalc ? ? C ASP 39  OD1 ? ? ? 1_555 P CA . CA ? ? C ASP 39  C CA 502 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc15 metalc ? ? C ASP 39  OD2 ? ? ? 1_555 P CA . CA ? ? C ASP 39  C CA 502 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc16 metalc ? ? C THR 41  O   ? ? ? 1_555 P CA . CA ? ? C THR 41  C CA 502 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc17 metalc ? ? C THR 41  OG1 ? ? ? 1_555 P CA . CA ? ? C THR 41  C CA 502 1_555 ? ? ? ? ? ? ? 1.860 ? ? 
metalc18 metalc ? ? C GLY 44  O   ? ? ? 1_555 P CA . CA ? ? C GLY 44  C CA 502 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc19 metalc ? ? C GLU 55  OE1 ? ? ? 1_555 P CA . CA ? ? C GLU 55  C CA 502 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc20 metalc ? ? C GLU 55  OE2 ? ? ? 1_555 P CA . CA ? ? C GLU 55  C CA 502 1_555 ? ? ? ? ? ? ? 1.909 ? ? 
metalc21 metalc ? ? O GTP .   O3G ? ? ? 1_555 Q MG . MG ? ? C GTP 501 C MG 503 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc22 metalc ? ? O GTP .   O2B ? ? ? 1_555 Q MG . MG ? ? C GTP 501 C MG 503 1_555 ? ? ? ? ? ? ? 2.615 ? ? 
# 
_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 ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 39  ? A ASP 39  ? 1_555 40.4  ? 
2  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A THR 41  ? A THR 41  ? 1_555 50.1  ? 
3  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A THR 41  ? A THR 41  ? 1_555 55.0  ? 
4  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 76.9  ? 
5  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 117.1 ? 
6  O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 84.9  ? 
7  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 105.6 ? 
8  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 88.8  ? 
9  O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 56.5  ? 
10 OG1 ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 108.3 ? 
11 OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 95.1  ? 
12 OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 103.9 ? 
13 O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 144.8 ? 
14 OG1 ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 81.5  ? 
15 O   ? A GLY 44  ? A GLY 44  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 158.6 ? 
16 OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 90.8  ? 
17 OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 50.7  ? 
18 O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 77.6  ? 
19 OG1 ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 162.4 ? 
20 O   ? A GLY 44  ? A GLY 44  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 62.6  ? 
21 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 112.5 ? 
22 OE1 ? A GLU 71  ? A GLU 71  ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2G ? G GTP .   ? A GTP 501 ? 1_555 107.1 ? 
23 OE1 ? A GLU 71  ? A GLU 71  ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2B ? G GTP .   ? A GTP 501 ? 1_555 161.7 ? 
24 O2G ? G GTP .   ? A GTP 501 ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2B ? G GTP .   ? A GTP 501 ? 1_555 62.7  ? 
25 OE1 ? B GLN 11  ? B GLN 11  ? 1_555 MG ? N MG . ? B MG 505 ? 1_555 OD2 ? B ASP 177 ? B ASP 177 ? 1_555 135.4 ? 
26 OE1 ? B GLN 11  ? B GLN 11  ? 1_555 MG ? N MG . ? B MG 505 ? 1_555 O1A ? K GDP .   ? B GDP 502 ? 1_555 64.5  ? 
27 OD2 ? B ASP 177 ? B ASP 177 ? 1_555 MG ? N MG . ? B MG 505 ? 1_555 O1A ? K GDP .   ? B GDP 502 ? 1_555 100.6 ? 
28 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 62.4  ? 
29 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C THR 41  ? C THR 41  ? 1_555 104.4 ? 
30 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C THR 41  ? C THR 41  ? 1_555 112.6 ? 
31 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 75.4  ? 
32 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 137.5 ? 
33 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 80.7  ? 
34 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 156.6 ? 
35 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 140.6 ? 
36 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 73.2  ? 
37 OG1 ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 81.3  ? 
38 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 125.7 ? 
39 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 71.8  ? 
40 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 67.4  ? 
41 OG1 ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 144.8 ? 
42 O   ? C GLY 44  ? C GLY 44  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 75.7  ? 
43 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 128.9 ? 
44 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 78.5  ? 
45 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 121.0 ? 
46 OG1 ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 130.6 ? 
47 O   ? C GLY 44  ? C GLY 44  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 66.8  ? 
48 OE1 ? C GLU 55  ? C GLU 55  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 62.0  ? 
49 O3G ? O GTP .   ? C GTP 501 ? 1_555 MG ? Q MG . ? C MG 503 ? 1_555 O2B ? O GTP .   ? C GTP 501 ? 1_555 70.5  ? 
# 
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 4.75  
2 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 3.53  
3 ALA 273 C . ? ALA 273 C PRO 274 C ? PRO 274 C 1 -0.23 
4 ALA 271 D . ? ALA 271 D PRO 272 D ? PRO 272 D 1 2.29  
5 GLU 193 F . ? GLU 193 F PRO 194 F ? PRO 194 F 1 7.69  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 6  ? 
AA4 ? 10 ? 
AA5 ? 2  ? 
AA6 ? 6  ? 
AA7 ? 2  ? 
AA8 ? 4  ? 
AA9 ? 10 ? 
AB1 ? 2  ? 
AB2 ? 5  ? 
AB3 ? 3  ? 
AB4 ? 5  ? 
AB5 ? 5  ? 
# 
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      
AA4 6 7  ? parallel      
AA4 7 8  ? anti-parallel 
AA4 8 9  ? anti-parallel 
AA4 9 10 ? parallel      
AA5 1 2  ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA6 5 6  ? parallel      
AA7 1 2  ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA8 2 3  ? anti-parallel 
AA8 3 4  ? parallel      
AA9 1 2  ? parallel      
AA9 2 3  ? parallel      
AA9 3 4  ? parallel      
AA9 4 5  ? parallel      
AA9 5 6  ? parallel      
AA9 6 7  ? parallel      
AA9 7 8  ? anti-parallel 
AA9 8 9  ? anti-parallel 
AA9 9 10 ? parallel      
AB1 1 2  ? anti-parallel 
AB2 1 2  ? parallel      
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB3 1 2  ? anti-parallel 
AB3 2 3  ? 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  ? anti-parallel 
AB5 2 3  ? anti-parallel 
AB5 3 4  ? anti-parallel 
AB5 4 5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LEU A 92  ? THR A 94  ? LEU A 92  THR A 94  
AA1 2  ALA A 65  ? ASP A 69  ? ALA A 65  ASP A 69  
AA1 3  CYS A 4   ? VAL A 9   ? CYS A 4   VAL A 9   
AA1 4  GLY A 134 ? SER A 140 ? GLY A 134 SER A 140 
AA1 5  SER A 165 ? TYR A 172 ? SER A 165 TYR A 172 
AA1 6  CYS A 200 ? ASP A 205 ? CYS A 200 ASP A 205 
AA2 1  PHE A 53  ? GLU A 55  ? PHE A 53  GLU A 55  
AA2 2  HIS A 61  ? PRO A 63  ? HIS A 61  PRO A 63  
AA3 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA3 2  ARG A 373 ? THR A 381 ? ARG A 373 THR A 381 
AA3 3  TYR A 312 ? GLY A 321 ? TYR A 312 GLY A 321 
AA3 4  GLY A 350 ? ASN A 356 ? GLY A 350 ASN A 356 
AA3 5  GLY E 15  ? ILE E 21  ? GLY E 17  ILE E 23  
AA3 6  GLU E 5   ? LYS E 11  ? GLU E 7   LYS E 13  
AA4 1  PHE B 90  ? PHE B 92  ? PHE B 90  PHE B 92  
AA4 2  ALA B 63  ? ASP B 67  ? ALA B 63  ASP B 67  
AA4 3  ILE B 4   ? ALA B 9   ? ILE B 4   ALA B 9   
AA4 4  GLY B 132 ? SER B 138 ? GLY B 132 SER B 138 
AA4 5  ILE B 163 ? MET B 170 ? ILE B 163 MET B 170 
AA4 6  GLU B 198 ? ASP B 203 ? GLU B 198 ASP B 203 
AA4 7  PHE B 265 ? ALA B 271 ? PHE B 265 ALA B 271 
AA4 8  MET B 363 ? SER B 371 ? MET B 363 SER B 371 
AA4 9  TYR B 310 ? GLY B 319 ? TYR B 310 GLY B 319 
AA4 10 VAL B 349 ? CYS B 354 ? VAL B 349 CYS B 354 
AA5 1  TYR B 51  ? ALA B 54  ? TYR B 51  ALA B 54  
AA5 2  LYS B 58  ? PRO B 61  ? LYS B 58  PRO B 61  
AA6 1  LEU C 92  ? THR C 94  ? LEU C 92  THR C 94  
AA6 2  ALA C 65  ? ASP C 69  ? ALA C 65  ASP C 69  
AA6 3  CYS C 4   ? VAL C 9   ? CYS C 4   VAL C 9   
AA6 4  GLY C 134 ? SER C 140 ? GLY C 134 SER C 140 
AA6 5  SER C 165 ? TYR C 172 ? SER C 165 TYR C 172 
AA6 6  CYS C 200 ? ASP C 205 ? CYS C 200 ASP C 205 
AA7 1  PHE C 53  ? GLU C 55  ? PHE C 53  GLU C 55  
AA7 2  HIS C 61  ? PRO C 63  ? HIS C 61  PRO C 63  
AA8 1  LEU C 269 ? ALA C 273 ? LEU C 269 ALA C 273 
AA8 2  ARG C 373 ? THR C 381 ? ARG C 373 THR C 381 
AA8 3  TYR C 312 ? GLY C 321 ? TYR C 312 GLY C 321 
AA8 4  LYS C 352 ? ASN C 356 ? LYS C 352 ASN C 356 
AA9 1  PHE D 90  ? PHE D 92  ? PHE D 90  PHE D 92  
AA9 2  ALA D 63  ? ASP D 67  ? ALA D 63  ASP D 67  
AA9 3  GLU D 3   ? GLN D 8   ? GLU D 3   GLN D 8   
AA9 4  LEU D 130 ? SER D 138 ? LEU D 130 SER D 138 
AA9 5  ILE D 163 ? MET D 170 ? ILE D 163 MET D 170 
AA9 6  GLU D 198 ? ASP D 203 ? GLU D 198 ASP D 203 
AA9 7  PHE D 265 ? ALA D 271 ? PHE D 265 ALA D 271 
AA9 8  MET D 363 ? SER D 371 ? MET D 363 SER D 371 
AA9 9  TYR D 310 ? GLY D 319 ? TYR D 310 GLY D 319 
AA9 10 VAL D 349 ? CYS D 354 ? VAL D 349 CYS D 354 
AB1 1  TYR D 51  ? ALA D 54  ? TYR D 51  ALA D 54  
AB1 2  LYS D 58  ? PRO D 61  ? LYS D 58  PRO D 61  
AB2 1  TRP F 27  ? ARG F 29  ? TRP F 27  ARG F 29  
AB2 2  TYR F 2   ? VAL F 6   ? TYR F 2   VAL F 6   
AB2 3  LEU F 39  ? LEU F 41  ? LEU F 39  LEU F 41  
AB2 4  LEU F 61  ? VAL F 62  ? LEU F 61  VAL F 62  
AB2 5  GLN F 310 ? SER F 311 ? GLN F 310 SER F 311 
AB3 1  SER F 97  ? ILE F 100 ? SER F 97  ILE F 100 
AB3 2  HIS F 180 ? LYS F 184 ? HIS F 180 LYS F 184 
AB3 3  TRP F 147 ? ILE F 148 ? TRP F 147 ILE F 148 
AB4 1  GLU F 261 ? PHE F 263 ? GLU F 261 PHE F 263 
AB4 2  VAL F 220 ? THR F 223 ? VAL F 220 THR F 223 
AB4 3  PHE F 199 ? VAL F 207 ? PHE F 199 VAL F 207 
AB4 4  GLN F 313 ? VAL F 321 ? GLN F 313 VAL F 321 
AB4 5  VAL F 327 ? ASN F 333 ? VAL F 327 ASN F 333 
AB5 1  GLU F 261 ? PHE F 263 ? GLU F 261 PHE F 263 
AB5 2  VAL F 220 ? THR F 223 ? VAL F 220 THR F 223 
AB5 3  PHE F 199 ? VAL F 207 ? PHE F 199 VAL F 207 
AB5 4  ILE F 213 ? TYR F 216 ? ILE F 213 TYR F 216 
AB5 5  PHE F 375 ? LYS F 377 ? PHE F 375 LYS F 377 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O ILE A 93  ? O ILE A 93  N PHE A 67  ? N PHE A 67  
AA1 2 3  O VAL A 68  ? O VAL A 68  N HIS A 8   ? N HIS A 8   
AA1 3 4  N VAL A 9   ? N VAL A 9   O PHE A 138 ? O PHE A 138 
AA1 4 5  N VAL A 137 ? N VAL A 137 O LEU A 167 ? O LEU A 167 
AA1 5 6  N GLU A 168 ? N GLU A 168 O PHE A 202 ? O PHE A 202 
AA2 1 2  N SER A 54  ? N SER A 54  O VAL A 62  ? O VAL A 62  
AA3 1 2  N LEU A 269 ? N LEU A 269 O SER A 379 ? O SER A 379 
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 E 18  ? O PHE E 20  
AA3 5 6  O SER E 17  ? O SER E 19  N ASN E 10  ? N ASN E 12  
AA4 1 2  O VAL B 91  ? O VAL B 91  N LEU B 65  ? N LEU B 65  
AA4 2 3  O ILE B 64  ? O ILE B 64  N HIS B 6   ? N HIS B 6   
AA4 3 4  N ILE B 7   ? N ILE B 7   O THR B 136 ? O THR B 136 
AA4 4 5  N PHE B 133 ? N PHE B 133 O ILE B 163 ? O ILE B 163 
AA4 5 6  N THR B 166 ? N THR B 166 O GLU B 198 ? O GLU B 198 
AA4 6 7  N CYS B 201 ? N CYS B 201 O PHE B 266 ? O PHE B 266 
AA4 7 8  N MET B 267 ? N MET B 267 O GLY B 369 ? O GLY B 369 
AA4 8 9  O SER B 364 ? O SER B 364 N ARG B 318 ? N ARG B 318 
AA4 9 10 N PHE B 317 ? N PHE B 317 O ALA B 352 ? O ALA B 352 
AA5 1 2  N ALA B 54  ? N ALA B 54  O LYS B 58  ? O LYS B 58  
AA6 1 2  O ILE C 93  ? O ILE C 93  N PHE C 67  ? N PHE C 67  
AA6 2 3  O VAL C 68  ? O VAL C 68  N HIS C 8   ? N HIS C 8   
AA6 3 4  N ILE C 7   ? N ILE C 7   O PHE C 138 ? O PHE C 138 
AA6 4 5  N VAL C 137 ? N VAL C 137 O LEU C 167 ? O LEU C 167 
AA6 5 6  N GLU C 168 ? N GLU C 168 O PHE C 202 ? O PHE C 202 
AA7 1 2  N SER C 54  ? N SER C 54  O VAL C 62  ? O VAL C 62  
AA8 1 2  N LEU C 269 ? N LEU C 269 O SER C 379 ? O SER C 379 
AA8 2 3  O ASN C 380 ? O ASN C 380 N MET C 313 ? N MET C 313 
AA8 3 4  N LEU C 317 ? N LEU C 317 O LYS C 352 ? O LYS C 352 
AA9 1 2  O VAL D 91  ? O VAL D 91  N LEU D 65  ? N LEU D 65  
AA9 2 3  O ILE D 64  ? O ILE D 64  N GLN D 8   ? N GLN D 8   
AA9 3 4  N GLU D 3   ? N GLU D 3   O GLN D 131 ? O GLN D 131 
AA9 4 5  N LEU D 135 ? N LEU D 135 O PHE D 167 ? O PHE D 167 
AA9 5 6  N SER D 168 ? N SER D 168 O ILE D 202 ? O ILE D 202 
AA9 6 7  N THR D 199 ? N THR D 199 O PHE D 266 ? O PHE D 266 
AA9 7 8  N GLY D 269 ? N GLY D 269 O PHE D 367 ? O PHE D 367 
AA9 8 9  O THR D 366 ? O THR D 366 N ILE D 316 ? N ILE D 316 
AA9 9 10 N PHE D 317 ? N PHE D 317 O ALA D 352 ? O ALA D 352 
AB1 1 2  N ASN D 52  ? N ASN D 52  O VAL D 60  ? O VAL D 60  
AB2 1 2  O LYS F 28  ? O LYS F 28  N TYR F 2   ? N TYR F 2   
AB2 2 3  N VAL F 5   ? N VAL F 5   O LEU F 39  ? O LEU F 39  
AB2 3 4  N MET F 40  ? N MET F 40  O LEU F 61  ? O LEU F 61  
AB2 4 5  N VAL F 62  ? N VAL F 62  O GLN F 310 ? O GLN F 310 
AB3 1 2  N ILE F 100 ? N ILE F 100 O HIS F 180 ? O HIS F 180 
AB3 2 3  O GLN F 183 ? O GLN F 183 N ILE F 148 ? N ILE F 148 
AB4 1 2  O MET F 262 ? O MET F 262 N LEU F 221 ? N LEU F 221 
AB4 2 3  O ARG F 222 ? O ARG F 222 N ASP F 200 ? N ASP F 200 
AB4 3 4  N ILE F 201 ? N ILE F 201 O PHE F 319 ? O PHE F 319 
AB4 4 5  N GLY F 316 ? N GLY F 316 O ASN F 333 ? O ASN F 333 
AB5 1 2  O MET F 262 ? O MET F 262 N LEU F 221 ? N LEU F 221 
AB5 2 3  O ARG F 222 ? O ARG F 222 N ASP F 200 ? N ASP F 200 
AB5 3 4  N LEU F 206 ? N LEU F 206 O TYR F 214 ? O TYR F 214 
AB5 4 5  N LEU F 215 ? N LEU F 215 O ILE F 376 ? O ILE F 376 
# 
_pdbx_entry_details.entry_id                   8YEU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 N   D GLN 11  ? ? O2B   D GDP 502 ? ? 1.30 
2  1 OD2 D ASP 67  ? ? OG1   D THR 72  ? ? 1.91 
3  1 OE2 D GLU 181 ? ? "O3'" D GDP 502 ? ? 1.97 
4  1 O   D TRP 21  ? ? OG    D SER 25  ? ? 1.97 
5  1 N   A HIS 88  ? ? OE1   A GLN 91  ? ? 2.00 
6  1 OE1 A GLU 90  ? ? NZ    A LYS 124 ? ? 2.04 
7  1 OH  F TYR 135 ? ? O     F SER 164 ? ? 2.04 
8  1 O   D GLY 140 ? ? ND2   D ASN 184 ? ? 2.06 
9  1 NH1 F ARG 138 ? ? O     F GLY 144 ? ? 2.09 
10 1 ND2 D ASN 100 ? ? O     D TRP 397 ? ? 2.15 
11 1 OE2 F GLU 226 ? ? ND2   F ASN 252 ? ? 2.18 
# 
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 THR A 41  ? ? -52.09  84.16   
2  1 PRO A 63  ? ? -35.16  131.42  
3  1 LEU A 70  ? ? -61.05  4.70    
4  1 ALA A 100 ? ? 38.22   54.22   
5  1 TYR A 108 ? ? -81.23  -96.23  
6  1 THR A 109 ? ? -29.85  -83.98  
7  1 TYR A 161 ? ? -159.45 34.45   
8  1 GLU A 196 ? ? -65.23  4.74    
9  1 ALA A 299 ? ? -49.51  -4.76   
10 1 HIS A 309 ? ? -101.34 66.97   
11 1 CYS A 315 ? ? -174.81 111.44  
12 1 ARG A 402 ? ? 48.33   27.22   
13 1 PHE A 404 ? ? 62.38   -6.79   
14 1 GLU A 415 ? ? -47.13  -12.65  
15 1 ASP B 39  ? ? -87.02  -81.20  
16 1 ASP B 88  ? ? -57.53  -9.17   
17 1 THR B 107 ? ? -115.56 -80.86  
18 1 THR B 143 ? ? -63.67  -80.17  
19 1 PHE B 212 ? ? -75.66  -71.09  
20 1 ARG B 213 ? ? -61.36  -73.37  
21 1 ASN B 247 ? ? 65.70   65.71   
22 1 ARG B 359 ? ? -37.59  111.75  
23 1 ASN B 370 ? ? -101.80 76.50   
24 1 PHE B 394 ? ? 49.29   8.08    
25 1 ASP C 47  ? ? -46.91  155.65  
26 1 ASP C 98  ? ? -77.00  -168.59 
27 1 TYR C 108 ? ? -104.22 -83.72  
28 1 THR C 109 ? ? -46.32  -70.42  
29 1 LYS C 164 ? ? -31.29  133.70  
30 1 ALA C 180 ? ? -171.16 128.13  
31 1 CYS C 200 ? ? -170.49 130.07  
32 1 ASP C 218 ? ? -21.34  94.21   
33 1 LEU C 248 ? ? -73.83  21.71   
34 1 HIS C 283 ? ? 69.89   -12.76  
35 1 ALA C 314 ? ? 164.96  147.26  
36 1 CYS C 315 ? ? -162.16 115.48  
37 1 PRO C 364 ? ? -36.96  132.68  
38 1 GLU D 45  ? ? -39.98  -38.55  
39 1 ASN D 57  ? ? 23.13   67.19   
40 1 PRO D 70  ? ? -57.99  -6.00   
41 1 PHE D 81  ? ? 74.73   -3.70   
42 1 GLN D 94  ? ? -148.22 -55.68  
43 1 THR D 107 ? ? -106.79 -89.98  
44 1 HIS D 137 ? ? -175.42 -167.53 
45 1 VAL D 175 ? ? -148.72 -26.79  
46 1 THR D 178 ? ? -59.51  103.47  
47 1 HIS D 190 ? ? -32.81  -30.59  
48 1 TYR D 222 ? ? -58.71  0.14    
49 1 PRO D 243 ? ? -62.20  -165.75 
50 1 MET D 300 ? ? -75.40  20.59   
51 1 ARG D 306 ? ? -69.27  7.25    
52 1 TYR D 398 ? ? -109.68 -60.28  
53 1 GLU E 10  ? ? 20.74   37.60   
54 1 LEU E 11  ? ? -60.72  99.60   
55 1 CYS E 14  ? ? -171.02 -172.94 
56 1 LYS E 25  ? ? 164.25  133.98  
57 1 PRO E 27  ? ? -57.52  -152.99 
58 1 LYS E 52  ? ? -54.77  -72.49  
59 1 ALA E 97  ? ? -52.85  -71.10  
60 1 LYS E 98  ? ? -37.94  -38.15  
61 1 GLN E 103 ? ? -57.60  -70.79  
62 1 SER E 107 ? ? -37.74  -36.84  
63 1 ALA F 23  ? ? -60.13  0.72    
64 1 LYS F 32  ? ? -13.84  -66.05  
65 1 ARG F 36  ? ? -96.90  57.80   
66 1 SER F 88  ? ? 67.37   149.69  
67 1 GLU F 129 ? ? -26.87  -75.83  
68 1 ARG F 142 ? ? 39.60   37.04   
69 1 HIS F 196 ? ? 45.37   74.94   
70 1 TYR F 253 ? ? -45.03  90.62   
71 1 ARG F 255 ? ? -56.63  -81.84  
72 1 THR F 277 ? ? -129.22 -168.89 
73 1 ILE F 283 ? ? -136.81 -44.10  
74 1 THR F 304 ? ? -97.79  42.33   
75 1 LEU F 361 ? ? -102.21 -137.54 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 LEU C 217 ? ? ASP C 218 ? ? -133.42 
2 1 SER F 311 ? ? PHE F 312 ? ? 148.11  
# 
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 ASP 438 ? A ASP 438 
2  1 Y 1 A SER 439 ? A SER 439 
3  1 Y 1 A VAL 440 ? A VAL 440 
4  1 Y 1 B MET 1   ? B MET 1   
5  1 Y 1 B THR 429 ? B THR 429 
6  1 Y 1 B ALA 430 ? B ALA 430 
7  1 Y 1 B ASP 431 ? B ASP 431 
8  1 Y 1 D THR 274 ? D THR 274 
9  1 Y 1 D SER 275 ? D SER 275 
10 1 Y 1 D ARG 276 ? D ARG 276 
11 1 Y 1 D GLY 277 ? D GLY 277 
12 1 Y 1 D SER 278 ? D SER 278 
13 1 Y 1 D GLN 279 ? D GLN 279 
14 1 Y 1 D GLN 280 ? D GLN 280 
15 1 Y 1 D TYR 281 ? D TYR 281 
16 1 Y 1 D ARG 282 ? D ARG 282 
17 1 Y 1 D ALA 283 ? D ALA 283 
18 1 Y 1 E MET 3   ? E MET 1   
19 1 Y 1 E ALA 4   ? E ALA 2   
20 1 Y 1 E ASP 5   ? E ASP 3   
21 1 Y 1 E PHE 29  ? E PHE 27  
22 1 Y 1 E ASP 30  ? E ASP 28  
23 1 Y 1 E GLY 31  ? E GLY 29  
24 1 Y 1 E VAL 32  ? E VAL 30  
25 1 Y 1 E PRO 33  ? E PRO 31  
26 1 Y 1 E GLU 34  ? E GLU 32  
27 1 Y 1 E PHE 35  ? E PHE 33  
28 1 Y 1 E ASN 36  ? E ASN 34  
29 1 Y 1 E ALA 37  ? E ALA 35  
30 1 Y 1 E SER 38  ? E SER 36  
31 1 Y 1 E LEU 39  ? E LEU 37  
32 1 Y 1 E PRO 40  ? E PRO 38  
33 1 Y 1 E ARG 41  ? E ARG 39  
34 1 Y 1 E ARG 42  ? E ARG 40  
35 1 Y 1 E ARG 43  ? E ARG 41  
36 1 Y 1 E GLU 142 ? E GLU 140 
37 1 Y 1 E ALA 143 ? E ALA 141 
38 1 Y 1 E SER 144 ? E SER 142 
39 1 Y 1 E ARG 145 ? E ARG 143 
40 1 Y 1 F ASN 104 ? F ASN 104 
41 1 Y 1 F LEU 105 ? F LEU 105 
42 1 Y 1 F LYS 106 ? F LYS 106 
43 1 Y 1 F THR 107 ? F THR 107 
44 1 Y 1 F PRO 108 ? F PRO 108 
45 1 Y 1 F VAL 109 ? F VAL 109 
46 1 Y 1 F ALA 110 ? F ALA 110 
47 1 Y 1 F PRO 111 ? F PRO 111 
48 1 Y 1 F ALA 112 ? F ALA 112 
49 1 Y 1 F GLN 113 ? F GLN 113 
50 1 Y 1 F ASN 114 ? F ASN 114 
51 1 Y 1 F GLY 115 ? F GLY 115 
52 1 Y 1 F ILE 116 ? F ILE 116 
53 1 Y 1 F ARG 117 ? F ARG 117 
54 1 Y 1 F HIS 118 ? F HIS 118 
55 1 Y 1 F LEU 119 ? F LEU 119 
56 1 Y 1 F ILE 120 ? F ILE 120 
57 1 Y 1 F ASN 121 ? F ASN 121 
58 1 Y 1 F ASN 122 ? F ASN 122 
59 1 Y 1 F THR 123 ? F THR 123 
60 1 Y 1 F ARG 124 ? F ARG 124 
61 1 Y 1 F THR 125 ? F THR 125 
62 1 Y 1 F ASP 126 ? F ASP 126 
63 1 Y 1 F GLU 127 ? F GLU 127 
64 1 Y 1 F LYS 150 ? F LYS 150 
65 1 Y 1 F SER 151 ? F SER 151 
66 1 Y 1 F SER 152 ? F SER 152 
67 1 Y 1 F ALA 153 ? F ALA 153 
68 1 Y 1 F GLY 154 ? F GLY 154 
69 1 Y 1 F ALA 155 ? F ALA 155 
70 1 Y 1 F LYS 156 ? F LYS 156 
71 1 Y 1 F GLY 157 ? F GLY 157 
72 1 Y 1 F GLU 158 ? F GLU 158 
73 1 Y 1 F GLY 159 ? F GLY 159 
74 1 Y 1 F ILE 160 ? F ILE 160 
75 1 Y 1 F GLU 248 ? F GLU 248 
76 1 Y 1 F TYR 249 ? F TYR 249 
77 1 Y 1 F SER 250 ? F SER 250 
78 1 Y 1 F LYS 251 ? F LYS 251 
79 1 Y 1 F ASP 363 ? F ASP 363 
80 1 Y 1 F THR 364 ? F THR 364 
81 1 Y 1 F GLY 365 ? F GLY 365 
82 1 Y 1 F GLN 366 ? F GLN 366 
83 1 Y 1 F LYS 367 ? F LYS 367 
84 1 Y 1 F THR 368 ? F THR 368 
85 1 Y 1 F SER 369 ? F SER 369 
86 1 Y 1 F GLN 370 ? F GLN 370 
87 1 Y 1 F PRO 371 ? F PRO 371 
88 1 N 0 A GTP 501 ? G GTP ?   
89 1 N 0 A CA  502 ? H CA  ?   
90 1 N 0 A MG  503 ? I MG  ?   
91 1 N 0 B GDP 502 ? K GDP ?   
92 1 N 0 B MES 503 ? L MES ?   
93 1 N 0 B MES 504 ? M MES ?   
94 1 N 0 B MG  505 ? N MG  ?   
95 1 N 0 C GTP 501 ? O GTP ?   
96 1 N 0 C CA  502 ? P CA  ?   
97 1 N 0 C MG  503 ? Q MG  ?   
98 1 N 0 D GDP 502 ? S GDP ?   
99 1 N 0 F ACP 401 ? T ACP ?   
# 
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 
A1D6L N12    N  N N 1   
A1D6L C13    C  Y N 2   
A1D6L C15    C  N N 3   
A1D6L C17    C  N N 4   
A1D6L C20    C  Y N 5   
A1D6L C21    C  Y N 6   
A1D6L C01    C  Y N 7   
A1D6L C02    C  Y N 8   
A1D6L C03    C  Y N 9   
A1D6L C04    C  Y N 10  
A1D6L C05    C  Y N 11  
A1D6L C06    C  Y N 12  
A1D6L C07    C  Y N 13  
A1D6L C09    C  Y N 14  
A1D6L C14    C  Y N 15  
A1D6L C16    C  N N 16  
A1D6L C18    C  Y N 17  
A1D6L C19    C  Y N 18  
A1D6L C23    C  N N 19  
A1D6L F24    F  N N 20  
A1D6L N08    N  Y N 21  
A1D6L N10    N  Y N 22  
A1D6L N11    N  N N 23  
A1D6L O22    O  N N 24  
A1D6L H151   H  N N 25  
A1D6L H152   H  N N 26  
A1D6L H172   H  N N 27  
A1D6L H171   H  N N 28  
A1D6L H201   H  N N 29  
A1D6L H211   H  N N 30  
A1D6L H021   H  N N 31  
A1D6L H031   H  N N 32  
A1D6L H061   H  N N 33  
A1D6L H161   H  N N 34  
A1D6L H162   H  N N 35  
A1D6L H181   H  N N 36  
A1D6L H231   H  N N 37  
A1D6L H232   H  N N 38  
A1D6L H233   H  N N 39  
A1D6L H112   H  N N 40  
A1D6L H111   H  N N 41  
ACP   PG     P  N N 42  
ACP   O1G    O  N N 43  
ACP   O2G    O  N N 44  
ACP   O3G    O  N N 45  
ACP   PB     P  N S 46  
ACP   O1B    O  N N 47  
ACP   O2B    O  N N 48  
ACP   C3B    C  N N 49  
ACP   PA     P  N R 50  
ACP   O1A    O  N N 51  
ACP   O2A    O  N N 52  
ACP   O3A    O  N N 53  
ACP   "O5'"  O  N N 54  
ACP   "C5'"  C  N N 55  
ACP   "C4'"  C  N R 56  
ACP   "O4'"  O  N N 57  
ACP   "C3'"  C  N S 58  
ACP   "O3'"  O  N N 59  
ACP   "C2'"  C  N R 60  
ACP   "O2'"  O  N N 61  
ACP   "C1'"  C  N R 62  
ACP   N9     N  Y N 63  
ACP   C8     C  Y N 64  
ACP   N7     N  Y N 65  
ACP   C5     C  Y N 66  
ACP   C6     C  Y N 67  
ACP   N6     N  N N 68  
ACP   N1     N  Y N 69  
ACP   C2     C  Y N 70  
ACP   N3     N  Y N 71  
ACP   C4     C  Y N 72  
ACP   HOG2   H  N N 73  
ACP   HOG3   H  N N 74  
ACP   HOB2   H  N N 75  
ACP   H3B1   H  N N 76  
ACP   H3B2   H  N N 77  
ACP   HOA2   H  N N 78  
ACP   "H5'1" H  N N 79  
ACP   "H5'2" H  N N 80  
ACP   "H4'"  H  N N 81  
ACP   "H3'"  H  N N 82  
ACP   "HO3'" H  N N 83  
ACP   "H2'"  H  N N 84  
ACP   "HO2'" H  N N 85  
ACP   "H1'"  H  N N 86  
ACP   H8     H  N N 87  
ACP   HN61   H  N N 88  
ACP   HN62   H  N N 89  
ACP   H2     H  N N 90  
ALA   N      N  N N 91  
ALA   CA     C  N S 92  
ALA   C      C  N N 93  
ALA   O      O  N N 94  
ALA   CB     C  N N 95  
ALA   OXT    O  N N 96  
ALA   H      H  N N 97  
ALA   H2     H  N N 98  
ALA   HA     H  N N 99  
ALA   HB1    H  N N 100 
ALA   HB2    H  N N 101 
ALA   HB3    H  N N 102 
ALA   HXT    H  N N 103 
ARG   N      N  N N 104 
ARG   CA     C  N S 105 
ARG   C      C  N N 106 
ARG   O      O  N N 107 
ARG   CB     C  N N 108 
ARG   CG     C  N N 109 
ARG   CD     C  N N 110 
ARG   NE     N  N N 111 
ARG   CZ     C  N N 112 
ARG   NH1    N  N N 113 
ARG   NH2    N  N N 114 
ARG   OXT    O  N N 115 
ARG   H      H  N N 116 
ARG   H2     H  N N 117 
ARG   HA     H  N N 118 
ARG   HB2    H  N N 119 
ARG   HB3    H  N N 120 
ARG   HG2    H  N N 121 
ARG   HG3    H  N N 122 
ARG   HD2    H  N N 123 
ARG   HD3    H  N N 124 
ARG   HE     H  N N 125 
ARG   HH11   H  N N 126 
ARG   HH12   H  N N 127 
ARG   HH21   H  N N 128 
ARG   HH22   H  N N 129 
ARG   HXT    H  N N 130 
ASN   N      N  N N 131 
ASN   CA     C  N S 132 
ASN   C      C  N N 133 
ASN   O      O  N N 134 
ASN   CB     C  N N 135 
ASN   CG     C  N N 136 
ASN   OD1    O  N N 137 
ASN   ND2    N  N N 138 
ASN   OXT    O  N N 139 
ASN   H      H  N N 140 
ASN   H2     H  N N 141 
ASN   HA     H  N N 142 
ASN   HB2    H  N N 143 
ASN   HB3    H  N N 144 
ASN   HD21   H  N N 145 
ASN   HD22   H  N N 146 
ASN   HXT    H  N N 147 
ASP   N      N  N N 148 
ASP   CA     C  N S 149 
ASP   C      C  N N 150 
ASP   O      O  N N 151 
ASP   CB     C  N N 152 
ASP   CG     C  N N 153 
ASP   OD1    O  N N 154 
ASP   OD2    O  N N 155 
ASP   OXT    O  N N 156 
ASP   H      H  N N 157 
ASP   H2     H  N N 158 
ASP   HA     H  N N 159 
ASP   HB2    H  N N 160 
ASP   HB3    H  N N 161 
ASP   HD2    H  N N 162 
ASP   HXT    H  N N 163 
CA    CA     CA N N 164 
CYS   N      N  N N 165 
CYS   CA     C  N R 166 
CYS   C      C  N N 167 
CYS   O      O  N N 168 
CYS   CB     C  N N 169 
CYS   SG     S  N N 170 
CYS   OXT    O  N N 171 
CYS   H      H  N N 172 
CYS   H2     H  N N 173 
CYS   HA     H  N N 174 
CYS   HB2    H  N N 175 
CYS   HB3    H  N N 176 
CYS   HG     H  N N 177 
CYS   HXT    H  N N 178 
GDP   PB     P  N N 179 
GDP   O1B    O  N N 180 
GDP   O2B    O  N N 181 
GDP   O3B    O  N N 182 
GDP   O3A    O  N N 183 
GDP   PA     P  N N 184 
GDP   O1A    O  N N 185 
GDP   O2A    O  N N 186 
GDP   "O5'"  O  N N 187 
GDP   "C5'"  C  N N 188 
GDP   "C4'"  C  N R 189 
GDP   "O4'"  O  N N 190 
GDP   "C3'"  C  N S 191 
GDP   "O3'"  O  N N 192 
GDP   "C2'"  C  N R 193 
GDP   "O2'"  O  N N 194 
GDP   "C1'"  C  N R 195 
GDP   N9     N  Y N 196 
GDP   C8     C  Y N 197 
GDP   N7     N  Y N 198 
GDP   C5     C  Y N 199 
GDP   C6     C  N N 200 
GDP   O6     O  N N 201 
GDP   N1     N  N N 202 
GDP   C2     C  N N 203 
GDP   N2     N  N N 204 
GDP   N3     N  N N 205 
GDP   C4     C  Y N 206 
GDP   HOB2   H  N N 207 
GDP   HOB3   H  N N 208 
GDP   HOA2   H  N N 209 
GDP   "H5'"  H  N N 210 
GDP   "H5''" H  N N 211 
GDP   "H4'"  H  N N 212 
GDP   "H3'"  H  N N 213 
GDP   "HO3'" H  N N 214 
GDP   "H2'"  H  N N 215 
GDP   "HO2'" H  N N 216 
GDP   "H1'"  H  N N 217 
GDP   H8     H  N N 218 
GDP   HN1    H  N N 219 
GDP   HN21   H  N N 220 
GDP   HN22   H  N N 221 
GLN   N      N  N N 222 
GLN   CA     C  N S 223 
GLN   C      C  N N 224 
GLN   O      O  N N 225 
GLN   CB     C  N N 226 
GLN   CG     C  N N 227 
GLN   CD     C  N N 228 
GLN   OE1    O  N N 229 
GLN   NE2    N  N N 230 
GLN   OXT    O  N N 231 
GLN   H      H  N N 232 
GLN   H2     H  N N 233 
GLN   HA     H  N N 234 
GLN   HB2    H  N N 235 
GLN   HB3    H  N N 236 
GLN   HG2    H  N N 237 
GLN   HG3    H  N N 238 
GLN   HE21   H  N N 239 
GLN   HE22   H  N N 240 
GLN   HXT    H  N N 241 
GLU   N      N  N N 242 
GLU   CA     C  N S 243 
GLU   C      C  N N 244 
GLU   O      O  N N 245 
GLU   CB     C  N N 246 
GLU   CG     C  N N 247 
GLU   CD     C  N N 248 
GLU   OE1    O  N N 249 
GLU   OE2    O  N N 250 
GLU   OXT    O  N N 251 
GLU   H      H  N N 252 
GLU   H2     H  N N 253 
GLU   HA     H  N N 254 
GLU   HB2    H  N N 255 
GLU   HB3    H  N N 256 
GLU   HG2    H  N N 257 
GLU   HG3    H  N N 258 
GLU   HE2    H  N N 259 
GLU   HXT    H  N N 260 
GLY   N      N  N N 261 
GLY   CA     C  N N 262 
GLY   C      C  N N 263 
GLY   O      O  N N 264 
GLY   OXT    O  N N 265 
GLY   H      H  N N 266 
GLY   H2     H  N N 267 
GLY   HA2    H  N N 268 
GLY   HA3    H  N N 269 
GLY   HXT    H  N N 270 
GTP   PG     P  N N 271 
GTP   O1G    O  N N 272 
GTP   O2G    O  N N 273 
GTP   O3G    O  N N 274 
GTP   O3B    O  N N 275 
GTP   PB     P  N N 276 
GTP   O1B    O  N N 277 
GTP   O2B    O  N N 278 
GTP   O3A    O  N N 279 
GTP   PA     P  N N 280 
GTP   O1A    O  N N 281 
GTP   O2A    O  N N 282 
GTP   "O5'"  O  N N 283 
GTP   "C5'"  C  N N 284 
GTP   "C4'"  C  N R 285 
GTP   "O4'"  O  N N 286 
GTP   "C3'"  C  N S 287 
GTP   "O3'"  O  N N 288 
GTP   "C2'"  C  N R 289 
GTP   "O2'"  O  N N 290 
GTP   "C1'"  C  N R 291 
GTP   N9     N  Y N 292 
GTP   C8     C  Y N 293 
GTP   N7     N  Y N 294 
GTP   C5     C  Y N 295 
GTP   C6     C  N N 296 
GTP   O6     O  N N 297 
GTP   N1     N  N N 298 
GTP   C2     C  N N 299 
GTP   N2     N  N N 300 
GTP   N3     N  N N 301 
GTP   C4     C  Y N 302 
GTP   HOG2   H  N N 303 
GTP   HOG3   H  N N 304 
GTP   HOB2   H  N N 305 
GTP   HOA2   H  N N 306 
GTP   "H5'"  H  N N 307 
GTP   "H5''" H  N N 308 
GTP   "H4'"  H  N N 309 
GTP   "H3'"  H  N N 310 
GTP   "HO3'" H  N N 311 
GTP   "H2'"  H  N N 312 
GTP   "HO2'" H  N N 313 
GTP   "H1'"  H  N N 314 
GTP   H8     H  N N 315 
GTP   HN1    H  N N 316 
GTP   HN21   H  N N 317 
GTP   HN22   H  N N 318 
HIS   N      N  N N 319 
HIS   CA     C  N S 320 
HIS   C      C  N N 321 
HIS   O      O  N N 322 
HIS   CB     C  N N 323 
HIS   CG     C  Y N 324 
HIS   ND1    N  Y N 325 
HIS   CD2    C  Y N 326 
HIS   CE1    C  Y N 327 
HIS   NE2    N  Y N 328 
HIS   OXT    O  N N 329 
HIS   H      H  N N 330 
HIS   H2     H  N N 331 
HIS   HA     H  N N 332 
HIS   HB2    H  N N 333 
HIS   HB3    H  N N 334 
HIS   HD1    H  N N 335 
HIS   HD2    H  N N 336 
HIS   HE1    H  N N 337 
HIS   HE2    H  N N 338 
HIS   HXT    H  N N 339 
ILE   N      N  N N 340 
ILE   CA     C  N S 341 
ILE   C      C  N N 342 
ILE   O      O  N N 343 
ILE   CB     C  N S 344 
ILE   CG1    C  N N 345 
ILE   CG2    C  N N 346 
ILE   CD1    C  N N 347 
ILE   OXT    O  N N 348 
ILE   H      H  N N 349 
ILE   H2     H  N N 350 
ILE   HA     H  N N 351 
ILE   HB     H  N N 352 
ILE   HG12   H  N N 353 
ILE   HG13   H  N N 354 
ILE   HG21   H  N N 355 
ILE   HG22   H  N N 356 
ILE   HG23   H  N N 357 
ILE   HD11   H  N N 358 
ILE   HD12   H  N N 359 
ILE   HD13   H  N N 360 
ILE   HXT    H  N N 361 
LEU   N      N  N N 362 
LEU   CA     C  N S 363 
LEU   C      C  N N 364 
LEU   O      O  N N 365 
LEU   CB     C  N N 366 
LEU   CG     C  N N 367 
LEU   CD1    C  N N 368 
LEU   CD2    C  N N 369 
LEU   OXT    O  N N 370 
LEU   H      H  N N 371 
LEU   H2     H  N N 372 
LEU   HA     H  N N 373 
LEU   HB2    H  N N 374 
LEU   HB3    H  N N 375 
LEU   HG     H  N N 376 
LEU   HD11   H  N N 377 
LEU   HD12   H  N N 378 
LEU   HD13   H  N N 379 
LEU   HD21   H  N N 380 
LEU   HD22   H  N N 381 
LEU   HD23   H  N N 382 
LEU   HXT    H  N N 383 
LYS   N      N  N N 384 
LYS   CA     C  N S 385 
LYS   C      C  N N 386 
LYS   O      O  N N 387 
LYS   CB     C  N N 388 
LYS   CG     C  N N 389 
LYS   CD     C  N N 390 
LYS   CE     C  N N 391 
LYS   NZ     N  N N 392 
LYS   OXT    O  N N 393 
LYS   H      H  N N 394 
LYS   H2     H  N N 395 
LYS   HA     H  N N 396 
LYS   HB2    H  N N 397 
LYS   HB3    H  N N 398 
LYS   HG2    H  N N 399 
LYS   HG3    H  N N 400 
LYS   HD2    H  N N 401 
LYS   HD3    H  N N 402 
LYS   HE2    H  N N 403 
LYS   HE3    H  N N 404 
LYS   HZ1    H  N N 405 
LYS   HZ2    H  N N 406 
LYS   HZ3    H  N N 407 
LYS   HXT    H  N N 408 
MES   O1     O  N N 409 
MES   C2     C  N N 410 
MES   C3     C  N N 411 
MES   N4     N  N N 412 
MES   C5     C  N N 413 
MES   C6     C  N N 414 
MES   C7     C  N N 415 
MES   C8     C  N N 416 
MES   S      S  N N 417 
MES   O1S    O  N N 418 
MES   O2S    O  N N 419 
MES   O3S    O  N N 420 
MES   H21    H  N N 421 
MES   H22    H  N N 422 
MES   H31    H  N N 423 
MES   H32    H  N N 424 
MES   HN4    H  N N 425 
MES   H51    H  N N 426 
MES   H52    H  N N 427 
MES   H61    H  N N 428 
MES   H62    H  N N 429 
MES   H71    H  N N 430 
MES   H72    H  N N 431 
MES   H81    H  N N 432 
MES   H82    H  N N 433 
MET   N      N  N N 434 
MET   CA     C  N S 435 
MET   C      C  N N 436 
MET   O      O  N N 437 
MET   CB     C  N N 438 
MET   CG     C  N N 439 
MET   SD     S  N N 440 
MET   CE     C  N N 441 
MET   OXT    O  N N 442 
MET   H      H  N N 443 
MET   H2     H  N N 444 
MET   HA     H  N N 445 
MET   HB2    H  N N 446 
MET   HB3    H  N N 447 
MET   HG2    H  N N 448 
MET   HG3    H  N N 449 
MET   HE1    H  N N 450 
MET   HE2    H  N N 451 
MET   HE3    H  N N 452 
MET   HXT    H  N N 453 
MG    MG     MG N N 454 
PHE   N      N  N N 455 
PHE   CA     C  N S 456 
PHE   C      C  N N 457 
PHE   O      O  N N 458 
PHE   CB     C  N N 459 
PHE   CG     C  Y N 460 
PHE   CD1    C  Y N 461 
PHE   CD2    C  Y N 462 
PHE   CE1    C  Y N 463 
PHE   CE2    C  Y N 464 
PHE   CZ     C  Y N 465 
PHE   OXT    O  N N 466 
PHE   H      H  N N 467 
PHE   H2     H  N N 468 
PHE   HA     H  N N 469 
PHE   HB2    H  N N 470 
PHE   HB3    H  N N 471 
PHE   HD1    H  N N 472 
PHE   HD2    H  N N 473 
PHE   HE1    H  N N 474 
PHE   HE2    H  N N 475 
PHE   HZ     H  N N 476 
PHE   HXT    H  N N 477 
PRO   N      N  N N 478 
PRO   CA     C  N S 479 
PRO   C      C  N N 480 
PRO   O      O  N N 481 
PRO   CB     C  N N 482 
PRO   CG     C  N N 483 
PRO   CD     C  N N 484 
PRO   OXT    O  N N 485 
PRO   H      H  N N 486 
PRO   HA     H  N N 487 
PRO   HB2    H  N N 488 
PRO   HB3    H  N N 489 
PRO   HG2    H  N N 490 
PRO   HG3    H  N N 491 
PRO   HD2    H  N N 492 
PRO   HD3    H  N N 493 
PRO   HXT    H  N N 494 
SER   N      N  N N 495 
SER   CA     C  N S 496 
SER   C      C  N N 497 
SER   O      O  N N 498 
SER   CB     C  N N 499 
SER   OG     O  N N 500 
SER   OXT    O  N N 501 
SER   H      H  N N 502 
SER   H2     H  N N 503 
SER   HA     H  N N 504 
SER   HB2    H  N N 505 
SER   HB3    H  N N 506 
SER   HG     H  N N 507 
SER   HXT    H  N N 508 
THR   N      N  N N 509 
THR   CA     C  N S 510 
THR   C      C  N N 511 
THR   O      O  N N 512 
THR   CB     C  N R 513 
THR   OG1    O  N N 514 
THR   CG2    C  N N 515 
THR   OXT    O  N N 516 
THR   H      H  N N 517 
THR   H2     H  N N 518 
THR   HA     H  N N 519 
THR   HB     H  N N 520 
THR   HG1    H  N N 521 
THR   HG21   H  N N 522 
THR   HG22   H  N N 523 
THR   HG23   H  N N 524 
THR   HXT    H  N N 525 
TRP   N      N  N N 526 
TRP   CA     C  N S 527 
TRP   C      C  N N 528 
TRP   O      O  N N 529 
TRP   CB     C  N N 530 
TRP   CG     C  Y N 531 
TRP   CD1    C  Y N 532 
TRP   CD2    C  Y N 533 
TRP   NE1    N  Y N 534 
TRP   CE2    C  Y N 535 
TRP   CE3    C  Y N 536 
TRP   CZ2    C  Y N 537 
TRP   CZ3    C  Y N 538 
TRP   CH2    C  Y N 539 
TRP   OXT    O  N N 540 
TRP   H      H  N N 541 
TRP   H2     H  N N 542 
TRP   HA     H  N N 543 
TRP   HB2    H  N N 544 
TRP   HB3    H  N N 545 
TRP   HD1    H  N N 546 
TRP   HE1    H  N N 547 
TRP   HE3    H  N N 548 
TRP   HZ2    H  N N 549 
TRP   HZ3    H  N N 550 
TRP   HH2    H  N N 551 
TRP   HXT    H  N N 552 
TYR   N      N  N N 553 
TYR   CA     C  N S 554 
TYR   C      C  N N 555 
TYR   O      O  N N 556 
TYR   CB     C  N N 557 
TYR   CG     C  Y N 558 
TYR   CD1    C  Y N 559 
TYR   CD2    C  Y N 560 
TYR   CE1    C  Y N 561 
TYR   CE2    C  Y N 562 
TYR   CZ     C  Y N 563 
TYR   OH     O  N N 564 
TYR   OXT    O  N N 565 
TYR   H      H  N N 566 
TYR   H2     H  N N 567 
TYR   HA     H  N N 568 
TYR   HB2    H  N N 569 
TYR   HB3    H  N N 570 
TYR   HD1    H  N N 571 
TYR   HD2    H  N N 572 
TYR   HE1    H  N N 573 
TYR   HE2    H  N N 574 
TYR   HH     H  N N 575 
TYR   HXT    H  N N 576 
VAL   N      N  N N 577 
VAL   CA     C  N S 578 
VAL   C      C  N N 579 
VAL   O      O  N N 580 
VAL   CB     C  N N 581 
VAL   CG1    C  N N 582 
VAL   CG2    C  N N 583 
VAL   OXT    O  N N 584 
VAL   H      H  N N 585 
VAL   H2     H  N N 586 
VAL   HA     H  N N 587 
VAL   HB     H  N N 588 
VAL   HG11   H  N N 589 
VAL   HG12   H  N N 590 
VAL   HG13   H  N N 591 
VAL   HG21   H  N N 592 
VAL   HG22   H  N N 593 
VAL   HG23   H  N N 594 
VAL   HXT    H  N N 595 
# 
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 
A1D6L N11   C09    sing N N 1   
A1D6L C09   N10    doub Y N 2   
A1D6L C09   N08    sing Y N 3   
A1D6L N10   C04    sing Y N 4   
A1D6L N08   C07    doub Y N 5   
A1D6L C04   C03    doub Y N 6   
A1D6L C04   C05    sing Y N 7   
A1D6L C03   C02    sing Y N 8   
A1D6L C07   C05    sing Y N 9   
A1D6L C07   N12    sing N N 10  
A1D6L C05   C06    doub Y N 11  
A1D6L C02   C01    doub Y N 12  
A1D6L C17   N12    sing N N 13  
A1D6L C17   C16    sing N N 14  
A1D6L N12   C13    sing N N 15  
A1D6L C06   C01    sing Y N 16  
A1D6L C01   F24    sing N N 17  
A1D6L C21   C13    doub Y N 18  
A1D6L C21   C20    sing Y N 19  
A1D6L C13   C14    sing Y N 20  
A1D6L C16   C15    sing N N 21  
A1D6L C20   C19    doub Y N 22  
A1D6L C14   C15    sing N N 23  
A1D6L C14   C18    doub Y N 24  
A1D6L C19   C18    sing Y N 25  
A1D6L C19   O22    sing N N 26  
A1D6L C23   O22    sing N N 27  
A1D6L C15   H151   sing N N 28  
A1D6L C15   H152   sing N N 29  
A1D6L C17   H172   sing N N 30  
A1D6L C17   H171   sing N N 31  
A1D6L C20   H201   sing N N 32  
A1D6L C21   H211   sing N N 33  
A1D6L C02   H021   sing N N 34  
A1D6L C03   H031   sing N N 35  
A1D6L C06   H061   sing N N 36  
A1D6L C16   H161   sing N N 37  
A1D6L C16   H162   sing N N 38  
A1D6L C18   H181   sing N N 39  
A1D6L C23   H231   sing N N 40  
A1D6L C23   H232   sing N N 41  
A1D6L C23   H233   sing N N 42  
A1D6L N11   H112   sing N N 43  
A1D6L N11   H111   sing N N 44  
ACP   PG    O1G    doub N N 45  
ACP   PG    O2G    sing N N 46  
ACP   PG    O3G    sing N N 47  
ACP   PG    C3B    sing N N 48  
ACP   O2G   HOG2   sing N N 49  
ACP   O3G   HOG3   sing N N 50  
ACP   PB    O1B    doub N N 51  
ACP   PB    O2B    sing N N 52  
ACP   PB    C3B    sing N N 53  
ACP   PB    O3A    sing N N 54  
ACP   O2B   HOB2   sing N N 55  
ACP   C3B   H3B1   sing N N 56  
ACP   C3B   H3B2   sing N N 57  
ACP   PA    O1A    doub N N 58  
ACP   PA    O2A    sing N N 59  
ACP   PA    O3A    sing N N 60  
ACP   PA    "O5'"  sing N N 61  
ACP   O2A   HOA2   sing N N 62  
ACP   "O5'" "C5'"  sing N N 63  
ACP   "C5'" "C4'"  sing N N 64  
ACP   "C5'" "H5'1" sing N N 65  
ACP   "C5'" "H5'2" sing N N 66  
ACP   "C4'" "O4'"  sing N N 67  
ACP   "C4'" "C3'"  sing N N 68  
ACP   "C4'" "H4'"  sing N N 69  
ACP   "O4'" "C1'"  sing N N 70  
ACP   "C3'" "O3'"  sing N N 71  
ACP   "C3'" "C2'"  sing N N 72  
ACP   "C3'" "H3'"  sing N N 73  
ACP   "O3'" "HO3'" sing N N 74  
ACP   "C2'" "O2'"  sing N N 75  
ACP   "C2'" "C1'"  sing N N 76  
ACP   "C2'" "H2'"  sing N N 77  
ACP   "O2'" "HO2'" sing N N 78  
ACP   "C1'" N9     sing N N 79  
ACP   "C1'" "H1'"  sing N N 80  
ACP   N9    C8     sing Y N 81  
ACP   N9    C4     sing Y N 82  
ACP   C8    N7     doub Y N 83  
ACP   C8    H8     sing N N 84  
ACP   N7    C5     sing Y N 85  
ACP   C5    C6     sing Y N 86  
ACP   C5    C4     doub Y N 87  
ACP   C6    N6     sing N N 88  
ACP   C6    N1     doub Y N 89  
ACP   N6    HN61   sing N N 90  
ACP   N6    HN62   sing N N 91  
ACP   N1    C2     sing Y N 92  
ACP   C2    N3     doub Y N 93  
ACP   C2    H2     sing N N 94  
ACP   N3    C4     sing Y N 95  
ALA   N     CA     sing N N 96  
ALA   N     H      sing N N 97  
ALA   N     H2     sing N N 98  
ALA   CA    C      sing N N 99  
ALA   CA    CB     sing N N 100 
ALA   CA    HA     sing N N 101 
ALA   C     O      doub N N 102 
ALA   C     OXT    sing N N 103 
ALA   CB    HB1    sing N N 104 
ALA   CB    HB2    sing N N 105 
ALA   CB    HB3    sing N N 106 
ALA   OXT   HXT    sing N N 107 
ARG   N     CA     sing N N 108 
ARG   N     H      sing N N 109 
ARG   N     H2     sing N N 110 
ARG   CA    C      sing N N 111 
ARG   CA    CB     sing N N 112 
ARG   CA    HA     sing N N 113 
ARG   C     O      doub N N 114 
ARG   C     OXT    sing N N 115 
ARG   CB    CG     sing N N 116 
ARG   CB    HB2    sing N N 117 
ARG   CB    HB3    sing N N 118 
ARG   CG    CD     sing N N 119 
ARG   CG    HG2    sing N N 120 
ARG   CG    HG3    sing N N 121 
ARG   CD    NE     sing N N 122 
ARG   CD    HD2    sing N N 123 
ARG   CD    HD3    sing N N 124 
ARG   NE    CZ     sing N N 125 
ARG   NE    HE     sing N N 126 
ARG   CZ    NH1    sing N N 127 
ARG   CZ    NH2    doub N N 128 
ARG   NH1   HH11   sing N N 129 
ARG   NH1   HH12   sing N N 130 
ARG   NH2   HH21   sing N N 131 
ARG   NH2   HH22   sing N N 132 
ARG   OXT   HXT    sing N N 133 
ASN   N     CA     sing N N 134 
ASN   N     H      sing N N 135 
ASN   N     H2     sing N N 136 
ASN   CA    C      sing N N 137 
ASN   CA    CB     sing N N 138 
ASN   CA    HA     sing N N 139 
ASN   C     O      doub N N 140 
ASN   C     OXT    sing N N 141 
ASN   CB    CG     sing N N 142 
ASN   CB    HB2    sing N N 143 
ASN   CB    HB3    sing N N 144 
ASN   CG    OD1    doub N N 145 
ASN   CG    ND2    sing N N 146 
ASN   ND2   HD21   sing N N 147 
ASN   ND2   HD22   sing N N 148 
ASN   OXT   HXT    sing N N 149 
ASP   N     CA     sing N N 150 
ASP   N     H      sing N N 151 
ASP   N     H2     sing N N 152 
ASP   CA    C      sing N N 153 
ASP   CA    CB     sing N N 154 
ASP   CA    HA     sing N N 155 
ASP   C     O      doub N N 156 
ASP   C     OXT    sing N N 157 
ASP   CB    CG     sing N N 158 
ASP   CB    HB2    sing N N 159 
ASP   CB    HB3    sing N N 160 
ASP   CG    OD1    doub N N 161 
ASP   CG    OD2    sing N N 162 
ASP   OD2   HD2    sing N N 163 
ASP   OXT   HXT    sing N N 164 
CYS   N     CA     sing N N 165 
CYS   N     H      sing N N 166 
CYS   N     H2     sing N N 167 
CYS   CA    C      sing N N 168 
CYS   CA    CB     sing N N 169 
CYS   CA    HA     sing N N 170 
CYS   C     O      doub N N 171 
CYS   C     OXT    sing N N 172 
CYS   CB    SG     sing N N 173 
CYS   CB    HB2    sing N N 174 
CYS   CB    HB3    sing N N 175 
CYS   SG    HG     sing N N 176 
CYS   OXT   HXT    sing N N 177 
GDP   PB    O1B    doub N N 178 
GDP   PB    O2B    sing N N 179 
GDP   PB    O3B    sing N N 180 
GDP   PB    O3A    sing N N 181 
GDP   O2B   HOB2   sing N N 182 
GDP   O3B   HOB3   sing N N 183 
GDP   O3A   PA     sing N N 184 
GDP   PA    O1A    doub N N 185 
GDP   PA    O2A    sing N N 186 
GDP   PA    "O5'"  sing N N 187 
GDP   O2A   HOA2   sing N N 188 
GDP   "O5'" "C5'"  sing N N 189 
GDP   "C5'" "C4'"  sing N N 190 
GDP   "C5'" "H5'"  sing N N 191 
GDP   "C5'" "H5''" sing N N 192 
GDP   "C4'" "O4'"  sing N N 193 
GDP   "C4'" "C3'"  sing N N 194 
GDP   "C4'" "H4'"  sing N N 195 
GDP   "O4'" "C1'"  sing N N 196 
GDP   "C3'" "O3'"  sing N N 197 
GDP   "C3'" "C2'"  sing N N 198 
GDP   "C3'" "H3'"  sing N N 199 
GDP   "O3'" "HO3'" sing N N 200 
GDP   "C2'" "O2'"  sing N N 201 
GDP   "C2'" "C1'"  sing N N 202 
GDP   "C2'" "H2'"  sing N N 203 
GDP   "O2'" "HO2'" sing N N 204 
GDP   "C1'" N9     sing N N 205 
GDP   "C1'" "H1'"  sing N N 206 
GDP   N9    C8     sing Y N 207 
GDP   N9    C4     sing Y N 208 
GDP   C8    N7     doub Y N 209 
GDP   C8    H8     sing N N 210 
GDP   N7    C5     sing Y N 211 
GDP   C5    C6     sing N N 212 
GDP   C5    C4     doub Y N 213 
GDP   C6    O6     doub N N 214 
GDP   C6    N1     sing N N 215 
GDP   N1    C2     sing N N 216 
GDP   N1    HN1    sing N N 217 
GDP   C2    N2     sing N N 218 
GDP   C2    N3     doub N N 219 
GDP   N2    HN21   sing N N 220 
GDP   N2    HN22   sing N N 221 
GDP   N3    C4     sing N N 222 
GLN   N     CA     sing N N 223 
GLN   N     H      sing N N 224 
GLN   N     H2     sing N N 225 
GLN   CA    C      sing N N 226 
GLN   CA    CB     sing N N 227 
GLN   CA    HA     sing N N 228 
GLN   C     O      doub N N 229 
GLN   C     OXT    sing N N 230 
GLN   CB    CG     sing N N 231 
GLN   CB    HB2    sing N N 232 
GLN   CB    HB3    sing N N 233 
GLN   CG    CD     sing N N 234 
GLN   CG    HG2    sing N N 235 
GLN   CG    HG3    sing N N 236 
GLN   CD    OE1    doub N N 237 
GLN   CD    NE2    sing N N 238 
GLN   NE2   HE21   sing N N 239 
GLN   NE2   HE22   sing N N 240 
GLN   OXT   HXT    sing N N 241 
GLU   N     CA     sing N N 242 
GLU   N     H      sing N N 243 
GLU   N     H2     sing N N 244 
GLU   CA    C      sing N N 245 
GLU   CA    CB     sing N N 246 
GLU   CA    HA     sing N N 247 
GLU   C     O      doub N N 248 
GLU   C     OXT    sing N N 249 
GLU   CB    CG     sing N N 250 
GLU   CB    HB2    sing N N 251 
GLU   CB    HB3    sing N N 252 
GLU   CG    CD     sing N N 253 
GLU   CG    HG2    sing N N 254 
GLU   CG    HG3    sing N N 255 
GLU   CD    OE1    doub N N 256 
GLU   CD    OE2    sing N N 257 
GLU   OE2   HE2    sing N N 258 
GLU   OXT   HXT    sing N N 259 
GLY   N     CA     sing N N 260 
GLY   N     H      sing N N 261 
GLY   N     H2     sing N N 262 
GLY   CA    C      sing N N 263 
GLY   CA    HA2    sing N N 264 
GLY   CA    HA3    sing N N 265 
GLY   C     O      doub N N 266 
GLY   C     OXT    sing N N 267 
GLY   OXT   HXT    sing N N 268 
GTP   PG    O1G    doub N N 269 
GTP   PG    O2G    sing N N 270 
GTP   PG    O3G    sing N N 271 
GTP   PG    O3B    sing N N 272 
GTP   O2G   HOG2   sing N N 273 
GTP   O3G   HOG3   sing N N 274 
GTP   O3B   PB     sing N N 275 
GTP   PB    O1B    doub N N 276 
GTP   PB    O2B    sing N N 277 
GTP   PB    O3A    sing N N 278 
GTP   O2B   HOB2   sing N N 279 
GTP   O3A   PA     sing N N 280 
GTP   PA    O1A    doub N N 281 
GTP   PA    O2A    sing N N 282 
GTP   PA    "O5'"  sing N N 283 
GTP   O2A   HOA2   sing N N 284 
GTP   "O5'" "C5'"  sing N N 285 
GTP   "C5'" "C4'"  sing N N 286 
GTP   "C5'" "H5'"  sing N N 287 
GTP   "C5'" "H5''" sing N N 288 
GTP   "C4'" "O4'"  sing N N 289 
GTP   "C4'" "C3'"  sing N N 290 
GTP   "C4'" "H4'"  sing N N 291 
GTP   "O4'" "C1'"  sing N N 292 
GTP   "C3'" "O3'"  sing N N 293 
GTP   "C3'" "C2'"  sing N N 294 
GTP   "C3'" "H3'"  sing N N 295 
GTP   "O3'" "HO3'" sing N N 296 
GTP   "C2'" "O2'"  sing N N 297 
GTP   "C2'" "C1'"  sing N N 298 
GTP   "C2'" "H2'"  sing N N 299 
GTP   "O2'" "HO2'" sing N N 300 
GTP   "C1'" N9     sing N N 301 
GTP   "C1'" "H1'"  sing N N 302 
GTP   N9    C8     sing Y N 303 
GTP   N9    C4     sing Y N 304 
GTP   C8    N7     doub Y N 305 
GTP   C8    H8     sing N N 306 
GTP   N7    C5     sing Y N 307 
GTP   C5    C6     sing N N 308 
GTP   C5    C4     doub Y N 309 
GTP   C6    O6     doub N N 310 
GTP   C6    N1     sing N N 311 
GTP   N1    C2     sing N N 312 
GTP   N1    HN1    sing N N 313 
GTP   C2    N2     sing N N 314 
GTP   C2    N3     doub N N 315 
GTP   N2    HN21   sing N N 316 
GTP   N2    HN22   sing N N 317 
GTP   N3    C4     sing N N 318 
HIS   N     CA     sing N N 319 
HIS   N     H      sing N N 320 
HIS   N     H2     sing N N 321 
HIS   CA    C      sing N N 322 
HIS   CA    CB     sing N N 323 
HIS   CA    HA     sing N N 324 
HIS   C     O      doub N N 325 
HIS   C     OXT    sing N N 326 
HIS   CB    CG     sing N N 327 
HIS   CB    HB2    sing N N 328 
HIS   CB    HB3    sing N N 329 
HIS   CG    ND1    sing Y N 330 
HIS   CG    CD2    doub Y N 331 
HIS   ND1   CE1    doub Y N 332 
HIS   ND1   HD1    sing N N 333 
HIS   CD2   NE2    sing Y N 334 
HIS   CD2   HD2    sing N N 335 
HIS   CE1   NE2    sing Y N 336 
HIS   CE1   HE1    sing N N 337 
HIS   NE2   HE2    sing N N 338 
HIS   OXT   HXT    sing N N 339 
ILE   N     CA     sing N N 340 
ILE   N     H      sing N N 341 
ILE   N     H2     sing N N 342 
ILE   CA    C      sing N N 343 
ILE   CA    CB     sing N N 344 
ILE   CA    HA     sing N N 345 
ILE   C     O      doub N N 346 
ILE   C     OXT    sing N N 347 
ILE   CB    CG1    sing N N 348 
ILE   CB    CG2    sing N N 349 
ILE   CB    HB     sing N N 350 
ILE   CG1   CD1    sing N N 351 
ILE   CG1   HG12   sing N N 352 
ILE   CG1   HG13   sing N N 353 
ILE   CG2   HG21   sing N N 354 
ILE   CG2   HG22   sing N N 355 
ILE   CG2   HG23   sing N N 356 
ILE   CD1   HD11   sing N N 357 
ILE   CD1   HD12   sing N N 358 
ILE   CD1   HD13   sing N N 359 
ILE   OXT   HXT    sing N N 360 
LEU   N     CA     sing N N 361 
LEU   N     H      sing N N 362 
LEU   N     H2     sing N N 363 
LEU   CA    C      sing N N 364 
LEU   CA    CB     sing N N 365 
LEU   CA    HA     sing N N 366 
LEU   C     O      doub N N 367 
LEU   C     OXT    sing N N 368 
LEU   CB    CG     sing N N 369 
LEU   CB    HB2    sing N N 370 
LEU   CB    HB3    sing N N 371 
LEU   CG    CD1    sing N N 372 
LEU   CG    CD2    sing N N 373 
LEU   CG    HG     sing N N 374 
LEU   CD1   HD11   sing N N 375 
LEU   CD1   HD12   sing N N 376 
LEU   CD1   HD13   sing N N 377 
LEU   CD2   HD21   sing N N 378 
LEU   CD2   HD22   sing N N 379 
LEU   CD2   HD23   sing N N 380 
LEU   OXT   HXT    sing N N 381 
LYS   N     CA     sing N N 382 
LYS   N     H      sing N N 383 
LYS   N     H2     sing N N 384 
LYS   CA    C      sing N N 385 
LYS   CA    CB     sing N N 386 
LYS   CA    HA     sing N N 387 
LYS   C     O      doub N N 388 
LYS   C     OXT    sing N N 389 
LYS   CB    CG     sing N N 390 
LYS   CB    HB2    sing N N 391 
LYS   CB    HB3    sing N N 392 
LYS   CG    CD     sing N N 393 
LYS   CG    HG2    sing N N 394 
LYS   CG    HG3    sing N N 395 
LYS   CD    CE     sing N N 396 
LYS   CD    HD2    sing N N 397 
LYS   CD    HD3    sing N N 398 
LYS   CE    NZ     sing N N 399 
LYS   CE    HE2    sing N N 400 
LYS   CE    HE3    sing N N 401 
LYS   NZ    HZ1    sing N N 402 
LYS   NZ    HZ2    sing N N 403 
LYS   NZ    HZ3    sing N N 404 
LYS   OXT   HXT    sing N N 405 
MES   O1    C2     sing N N 406 
MES   O1    C6     sing N N 407 
MES   C2    C3     sing N N 408 
MES   C2    H21    sing N N 409 
MES   C2    H22    sing N N 410 
MES   C3    N4     sing N N 411 
MES   C3    H31    sing N N 412 
MES   C3    H32    sing N N 413 
MES   N4    C5     sing N N 414 
MES   N4    C7     sing N N 415 
MES   N4    HN4    sing N N 416 
MES   C5    C6     sing N N 417 
MES   C5    H51    sing N N 418 
MES   C5    H52    sing N N 419 
MES   C6    H61    sing N N 420 
MES   C6    H62    sing N N 421 
MES   C7    C8     sing N N 422 
MES   C7    H71    sing N N 423 
MES   C7    H72    sing N N 424 
MES   C8    S      sing N N 425 
MES   C8    H81    sing N N 426 
MES   C8    H82    sing N N 427 
MES   S     O1S    doub N N 428 
MES   S     O2S    doub N N 429 
MES   S     O3S    sing N N 430 
MET   N     CA     sing N N 431 
MET   N     H      sing N N 432 
MET   N     H2     sing N N 433 
MET   CA    C      sing N N 434 
MET   CA    CB     sing N N 435 
MET   CA    HA     sing N N 436 
MET   C     O      doub N N 437 
MET   C     OXT    sing N N 438 
MET   CB    CG     sing N N 439 
MET   CB    HB2    sing N N 440 
MET   CB    HB3    sing N N 441 
MET   CG    SD     sing N N 442 
MET   CG    HG2    sing N N 443 
MET   CG    HG3    sing N N 444 
MET   SD    CE     sing N N 445 
MET   CE    HE1    sing N N 446 
MET   CE    HE2    sing N N 447 
MET   CE    HE3    sing N N 448 
MET   OXT   HXT    sing N N 449 
PHE   N     CA     sing N N 450 
PHE   N     H      sing N N 451 
PHE   N     H2     sing N N 452 
PHE   CA    C      sing N N 453 
PHE   CA    CB     sing N N 454 
PHE   CA    HA     sing N N 455 
PHE   C     O      doub N N 456 
PHE   C     OXT    sing N N 457 
PHE   CB    CG     sing N N 458 
PHE   CB    HB2    sing N N 459 
PHE   CB    HB3    sing N N 460 
PHE   CG    CD1    doub Y N 461 
PHE   CG    CD2    sing Y N 462 
PHE   CD1   CE1    sing Y N 463 
PHE   CD1   HD1    sing N N 464 
PHE   CD2   CE2    doub Y N 465 
PHE   CD2   HD2    sing N N 466 
PHE   CE1   CZ     doub Y N 467 
PHE   CE1   HE1    sing N N 468 
PHE   CE2   CZ     sing Y N 469 
PHE   CE2   HE2    sing N N 470 
PHE   CZ    HZ     sing N N 471 
PHE   OXT   HXT    sing N N 472 
PRO   N     CA     sing N N 473 
PRO   N     CD     sing N N 474 
PRO   N     H      sing N N 475 
PRO   CA    C      sing N N 476 
PRO   CA    CB     sing N N 477 
PRO   CA    HA     sing N N 478 
PRO   C     O      doub N N 479 
PRO   C     OXT    sing N N 480 
PRO   CB    CG     sing N N 481 
PRO   CB    HB2    sing N N 482 
PRO   CB    HB3    sing N N 483 
PRO   CG    CD     sing N N 484 
PRO   CG    HG2    sing N N 485 
PRO   CG    HG3    sing N N 486 
PRO   CD    HD2    sing N N 487 
PRO   CD    HD3    sing N N 488 
PRO   OXT   HXT    sing N N 489 
SER   N     CA     sing N N 490 
SER   N     H      sing N N 491 
SER   N     H2     sing N N 492 
SER   CA    C      sing N N 493 
SER   CA    CB     sing N N 494 
SER   CA    HA     sing N N 495 
SER   C     O      doub N N 496 
SER   C     OXT    sing N N 497 
SER   CB    OG     sing N N 498 
SER   CB    HB2    sing N N 499 
SER   CB    HB3    sing N N 500 
SER   OG    HG     sing N N 501 
SER   OXT   HXT    sing N N 502 
THR   N     CA     sing N N 503 
THR   N     H      sing N N 504 
THR   N     H2     sing N N 505 
THR   CA    C      sing N N 506 
THR   CA    CB     sing N N 507 
THR   CA    HA     sing N N 508 
THR   C     O      doub N N 509 
THR   C     OXT    sing N N 510 
THR   CB    OG1    sing N N 511 
THR   CB    CG2    sing N N 512 
THR   CB    HB     sing N N 513 
THR   OG1   HG1    sing N N 514 
THR   CG2   HG21   sing N N 515 
THR   CG2   HG22   sing N N 516 
THR   CG2   HG23   sing N N 517 
THR   OXT   HXT    sing N N 518 
TRP   N     CA     sing N N 519 
TRP   N     H      sing N N 520 
TRP   N     H2     sing N N 521 
TRP   CA    C      sing N N 522 
TRP   CA    CB     sing N N 523 
TRP   CA    HA     sing N N 524 
TRP   C     O      doub N N 525 
TRP   C     OXT    sing N N 526 
TRP   CB    CG     sing N N 527 
TRP   CB    HB2    sing N N 528 
TRP   CB    HB3    sing N N 529 
TRP   CG    CD1    doub Y N 530 
TRP   CG    CD2    sing Y N 531 
TRP   CD1   NE1    sing Y N 532 
TRP   CD1   HD1    sing N N 533 
TRP   CD2   CE2    doub Y N 534 
TRP   CD2   CE3    sing Y N 535 
TRP   NE1   CE2    sing Y N 536 
TRP   NE1   HE1    sing N N 537 
TRP   CE2   CZ2    sing Y N 538 
TRP   CE3   CZ3    doub Y N 539 
TRP   CE3   HE3    sing N N 540 
TRP   CZ2   CH2    doub Y N 541 
TRP   CZ2   HZ2    sing N N 542 
TRP   CZ3   CH2    sing Y N 543 
TRP   CZ3   HZ3    sing N N 544 
TRP   CH2   HH2    sing N N 545 
TRP   OXT   HXT    sing N N 546 
TYR   N     CA     sing N N 547 
TYR   N     H      sing N N 548 
TYR   N     H2     sing N N 549 
TYR   CA    C      sing N N 550 
TYR   CA    CB     sing N N 551 
TYR   CA    HA     sing N N 552 
TYR   C     O      doub N N 553 
TYR   C     OXT    sing N N 554 
TYR   CB    CG     sing N N 555 
TYR   CB    HB2    sing N N 556 
TYR   CB    HB3    sing N N 557 
TYR   CG    CD1    doub Y N 558 
TYR   CG    CD2    sing Y N 559 
TYR   CD1   CE1    sing Y N 560 
TYR   CD1   HD1    sing N N 561 
TYR   CD2   CE2    doub Y N 562 
TYR   CD2   HD2    sing N N 563 
TYR   CE1   CZ     doub Y N 564 
TYR   CE1   HE1    sing N N 565 
TYR   CE2   CZ     sing Y N 566 
TYR   CE2   HE2    sing N N 567 
TYR   CZ    OH     sing N N 568 
TYR   OH    HH     sing N N 569 
TYR   OXT   HXT    sing N N 570 
VAL   N     CA     sing N N 571 
VAL   N     H      sing N N 572 
VAL   N     H2     sing N N 573 
VAL   CA    C      sing N N 574 
VAL   CA    CB     sing N N 575 
VAL   CA    HA     sing N N 576 
VAL   C     O      doub N N 577 
VAL   C     OXT    sing N N 578 
VAL   CB    CG1    sing N N 579 
VAL   CB    CG2    sing N N 580 
VAL   CB    HB     sing N N 581 
VAL   CG1   HG11   sing N N 582 
VAL   CG1   HG12   sing N N 583 
VAL   CG1   HG13   sing N N 584 
VAL   CG2   HG21   sing N N 585 
VAL   CG2   HG22   sing N N 586 
VAL   CG2   HG23   sing N N 587 
VAL   OXT   HXT    sing N N 588 
# 
_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   6D88 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YEU 
_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]   0.009528 
_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]   0.006385 
_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]   0.005505 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
F  
H  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N      . MET   A 1  1   ? -39.870 -102.193 65.878  1.00 78.82  ? 1   MET   A N      1 
ATOM   2     C  CA     . MET   A 1  1   ? -38.853 -101.237 65.430  1.00 76.74  ? 1   MET   A CA     1 
ATOM   3     C  C      . MET   A 1  1   ? -39.416 -99.974  64.730  1.00 75.37  ? 1   MET   A C      1 
ATOM   4     O  O      . MET   A 1  1   ? -40.427 -100.041 64.001  1.00 72.69  ? 1   MET   A O      1 
ATOM   5     C  CB     . MET   A 1  1   ? -37.838 -101.977 64.539  1.00 74.52  ? 1   MET   A CB     1 
ATOM   6     C  CG     . MET   A 1  1   ? -36.748 -101.099 63.938  1.00 72.00  ? 1   MET   A CG     1 
ATOM   7     S  SD     . MET   A 1  1   ? -37.247 -100.185 62.454  1.00 69.80  ? 1   MET   A SD     1 
ATOM   8     C  CE     . MET   A 1  1   ? -37.547 -101.513 61.288  1.00 62.17  ? 1   MET   A CE     1 
ATOM   9     N  N      . ARG   A 1  2   ? -38.750 -98.835  64.978  1.00 69.43  ? 2   ARG   A N      1 
ATOM   10    C  CA     . ARG   A 1  2   ? -39.109 -97.524  64.438  1.00 69.79  ? 2   ARG   A CA     1 
ATOM   11    C  C      . ARG   A 1  2   ? -38.054 -97.014  63.445  1.00 69.76  ? 2   ARG   A C      1 
ATOM   12    O  O      . ARG   A 1  2   ? -36.845 -97.070  63.712  1.00 61.23  ? 2   ARG   A O      1 
ATOM   13    C  CB     . ARG   A 1  2   ? -39.292 -96.502  65.567  1.00 62.40  ? 2   ARG   A CB     1 
ATOM   14    C  CG     . ARG   A 1  2   ? -40.107 -96.970  66.752  1.00 66.36  ? 2   ARG   A CG     1 
ATOM   15    C  CD     . ARG   A 1  2   ? -40.784 -95.783  67.475  1.00 77.15  ? 2   ARG   A CD     1 
ATOM   16    N  NE     . ARG   A 1  2   ? -41.851 -95.165  66.682  1.00 80.92  ? 2   ARG   A NE     1 
ATOM   17    C  CZ     . ARG   A 1  2   ? -42.330 -93.940  66.875  1.00 74.67  ? 2   ARG   A CZ     1 
ATOM   18    N  NH1    . ARG   A 1  2   ? -41.879 -93.165  67.852  1.00 64.30  ? 2   ARG   A NH1    1 
ATOM   19    N  NH2    . ARG   A 1  2   ? -43.295 -93.487  66.077  1.00 69.92  ? 2   ARG   A NH2    1 
ATOM   20    N  N      . GLU   A 1  3   ? -38.523 -96.491  62.304  1.00 71.11  ? 3   GLU   A N      1 
ATOM   21    C  CA     . GLU   A 1  3   ? -37.671 -96.089  61.191  1.00 65.41  ? 3   GLU   A CA     1 
ATOM   22    C  C      . GLU   A 1  3   ? -37.343 -94.596  61.232  1.00 65.89  ? 3   GLU   A C      1 
ATOM   23    O  O      . GLU   A 1  3   ? -38.048 -93.785  61.849  1.00 60.54  ? 3   GLU   A O      1 
ATOM   24    C  CB     . GLU   A 1  3   ? -38.318 -96.436  59.842  1.00 62.71  ? 3   GLU   A CB     1 
ATOM   25    C  CG     . GLU   A 1  3   ? -38.539 -97.920  59.593  1.00 61.82  ? 3   GLU   A CG     1 
ATOM   26    C  CD     . GLU   A 1  3   ? -39.931 -98.407  60.014  1.00 68.08  ? 3   GLU   A CD     1 
ATOM   27    O  OE1    . GLU   A 1  3   ? -40.609 -97.718  60.819  1.00 65.40  ? 3   GLU   A OE1    1 
ATOM   28    O  OE2    . GLU   A 1  3   ? -40.328 -99.506  59.565  1.00 61.94  ? 3   GLU   A OE2    1 
ATOM   29    N  N      . CYS   A 1  4   ? -36.244 -94.252  60.545  1.00 65.18  ? 4   CYS   A N      1 
ATOM   30    C  CA     . CYS   A 1  4   ? -35.715 -92.893  60.445  1.00 63.81  ? 4   CYS   A CA     1 
ATOM   31    C  C      . CYS   A 1  4   ? -35.402 -92.538  58.998  1.00 61.28  ? 4   CYS   A C      1 
ATOM   32    O  O      . CYS   A 1  4   ? -34.653 -93.257  58.320  1.00 57.38  ? 4   CYS   A O      1 
ATOM   33    C  CB     . CYS   A 1  4   ? -34.442 -92.725  61.285  1.00 66.48  ? 4   CYS   A CB     1 
ATOM   34    S  SG     . CYS   A 1  4   ? -34.695 -92.658  63.045  1.00 62.10  ? 4   CYS   A SG     1 
ATOM   35    N  N      . ILE   A 1  5   ? -35.926 -91.398  58.545  1.00 58.93  ? 5   ILE   A N      1 
ATOM   36    C  CA     . ILE   A 1  5   ? -35.770 -90.962  57.158  1.00 57.56  ? 5   ILE   A CA     1 
ATOM   37    C  C      . ILE   A 1  5   ? -34.766 -89.815  57.117  1.00 55.71  ? 5   ILE   A C      1 
ATOM   38    O  O      . ILE   A 1  5   ? -34.934 -88.796  57.811  1.00 48.81  ? 5   ILE   A O      1 
ATOM   39    C  CB     . ILE   A 1  5   ? -37.116 -90.551  56.551  1.00 55.51  ? 5   ILE   A CB     1 
ATOM   40    C  CG1    . ILE   A 1  5   ? -38.040 -91.758  56.499  1.00 56.40  ? 5   ILE   A CG1    1 
ATOM   41    C  CG2    . ILE   A 1  5   ? -36.918 -90.076  55.169  1.00 51.90  ? 5   ILE   A CG2    1 
ATOM   42    C  CD1    . ILE   A 1  5   ? -39.468 -91.372  56.343  1.00 62.09  ? 5   ILE   A CD1    1 
ATOM   43    N  N      . SER   A 1  6   ? -33.717 -89.993  56.311  1.00 51.39  ? 6   SER   A N      1 
ATOM   44    C  CA     . SER   A 1  6   ? -32.667 -88.997  56.142  1.00 53.63  ? 6   SER   A CA     1 
ATOM   45    C  C      . SER   A 1  6   ? -32.937 -88.154  54.888  1.00 54.61  ? 6   SER   A C      1 
ATOM   46    O  O      . SER   A 1  6   ? -33.291 -88.691  53.829  1.00 52.32  ? 6   SER   A O      1 
ATOM   47    C  CB     . SER   A 1  6   ? -31.305 -89.682  56.051  1.00 52.02  ? 6   SER   A CB     1 
ATOM   48    O  OG     . SER   A 1  6   ? -30.969 -90.317  57.263  1.00 45.98  ? 6   SER   A OG     1 
ATOM   49    N  N      . ILE   A 1  7   ? -32.762 -86.837  55.018  1.00 50.37  ? 7   ILE   A N      1 
ATOM   50    C  CA     . ILE   A 1  7   ? -33.099 -85.852  53.991  1.00 49.30  ? 7   ILE   A CA     1 
ATOM   51    C  C      . ILE   A 1  7   ? -31.859 -84.974  53.788  1.00 47.16  ? 7   ILE   A C      1 
ATOM   52    O  O      . ILE   A 1  7   ? -31.557 -84.104  54.608  1.00 44.36  ? 7   ILE   A O      1 
ATOM   53    C  CB     . ILE   A 1  7   ? -34.315 -85.007  54.396  1.00 52.34  ? 7   ILE   A CB     1 
ATOM   54    C  CG1    . ILE   A 1  7   ? -35.505 -85.888  54.804  1.00 49.01  ? 7   ILE   A CG1    1 
ATOM   55    C  CG2    . ILE   A 1  7   ? -34.680 -84.014  53.303  1.00 44.92  ? 7   ILE   A CG2    1 
ATOM   56    C  CD1    . ILE   A 1  7   ? -36.728 -85.085  55.281  1.00 46.47  ? 7   ILE   A CD1    1 
ATOM   57    N  N      . HIS   A 1  8   ? -31.136 -85.199  52.721  1.00 41.01  ? 8   HIS   A N      1 
ATOM   58    C  CA     . HIS   A 1  8   ? -29.919 -84.455  52.457  1.00 45.52  ? 8   HIS   A CA     1 
ATOM   59    C  C      . HIS   A 1  8   ? -30.231 -83.350  51.443  1.00 49.68  ? 8   HIS   A C      1 
ATOM   60    O  O      . HIS   A 1  8   ? -30.695 -83.644  50.341  1.00 50.16  ? 8   HIS   A O      1 
ATOM   61    C  CB     . HIS   A 1  8   ? -28.864 -85.413  51.926  1.00 48.54  ? 8   HIS   A CB     1 
ATOM   62    C  CG     . HIS   A 1  8   ? -28.774 -86.687  52.705  1.00 51.43  ? 8   HIS   A CG     1 
ATOM   63    N  ND1    . HIS   A 1  8   ? -27.949 -86.846  53.798  1.00 56.40  ? 8   HIS   A ND1    1 
ATOM   64    C  CD2    . HIS   A 1  8   ? -29.442 -87.855  52.566  1.00 51.92  ? 8   HIS   A CD2    1 
ATOM   65    C  CE1    . HIS   A 1  8   ? -28.097 -88.064  54.285  1.00 50.95  ? 8   HIS   A CE1    1 
ATOM   66    N  NE2    . HIS   A 1  8   ? -28.998 -88.694  53.556  1.00 52.50  ? 8   HIS   A NE2    1 
ATOM   67    N  N      . VAL   A 1  9   ? -29.982 -82.085  51.806  1.00 43.62  ? 9   VAL   A N      1 
ATOM   68    C  CA     . VAL   A 1  9   ? -30.404 -80.954  50.988  1.00 41.71  ? 9   VAL   A CA     1 
ATOM   69    C  C      . VAL   A 1  9   ? -29.212 -80.111  50.570  1.00 49.55  ? 9   VAL   A C      1 
ATOM   70    O  O      . VAL   A 1  9   ? -28.273 -79.877  51.336  1.00 53.76  ? 9   VAL   A O      1 
ATOM   71    C  CB     . VAL   A 1  9   ? -31.430 -80.068  51.707  1.00 44.77  ? 9   VAL   A CB     1 
ATOM   72    C  CG1    . VAL   A 1  9   ? -31.839 -78.952  50.794  1.00 46.66  ? 9   VAL   A CG1    1 
ATOM   73    C  CG2    . VAL   A 1  9   ? -32.622 -80.877  52.057  1.00 44.48  ? 9   VAL   A CG2    1 
ATOM   74    N  N      . GLY   A 1  10  ? -29.278 -79.614  49.354  1.00 48.57  ? 10  GLY   A N      1 
ATOM   75    C  CA     . GLY   A 1  10  ? -28.174 -78.841  48.849  1.00 46.72  ? 10  GLY   A CA     1 
ATOM   76    C  C      . GLY   A 1  10  ? -26.989 -79.718  48.496  1.00 45.30  ? 10  GLY   A C      1 
ATOM   77    O  O      . GLY   A 1  10  ? -27.039 -80.939  48.519  1.00 46.05  ? 10  GLY   A O      1 
ATOM   78    N  N      . GLN   A 1  11  ? -25.903 -79.043  48.138  1.00 47.83  ? 11  GLN   A N      1 
ATOM   79    C  CA     . GLN   A 1  11  ? -24.638 -79.733  47.943  1.00 43.52  ? 11  GLN   A CA     1 
ATOM   80    C  C      . GLN   A 1  11  ? -24.058 -80.211  49.269  1.00 46.08  ? 11  GLN   A C      1 
ATOM   81    O  O      . GLN   A 1  11  ? -23.749 -81.397  49.432  1.00 45.03  ? 11  GLN   A O      1 
ATOM   82    C  CB     . GLN   A 1  11  ? -23.663 -78.814  47.225  1.00 43.06  ? 11  GLN   A CB     1 
ATOM   83    C  CG     . GLN   A 1  11  ? -22.296 -79.388  47.060  1.00 45.44  ? 11  GLN   A CG     1 
ATOM   84    C  CD     . GLN   A 1  11  ? -21.349 -78.425  46.377  1.00 43.81  ? 11  GLN   A CD     1 
ATOM   85    O  OE1    . GLN   A 1  11  ? -21.596 -77.994  45.256  1.00 45.24  ? 11  GLN   A OE1    1 
ATOM   86    N  NE2    . GLN   A 1  11  ? -20.276 -78.065  47.058  1.00 40.22  ? 11  GLN   A NE2    1 
ATOM   87    N  N      . ALA   A 1  12  ? -23.905 -79.308  50.231  1.00 43.22  ? 12  ALA   A N      1 
ATOM   88    C  CA     . ALA   A 1  12  ? -23.328 -79.705  51.507  1.00 41.44  ? 12  ALA   A CA     1 
ATOM   89    C  C      . ALA   A 1  12  ? -24.095 -80.870  52.119  1.00 44.49  ? 12  ALA   A C      1 
ATOM   90    O  O      . ALA   A 1  12  ? -23.501 -81.842  52.603  1.00 44.79  ? 12  ALA   A O      1 
ATOM   91    C  CB     . ALA   A 1  12  ? -23.307 -78.518  52.468  1.00 41.46  ? 12  ALA   A CB     1 
ATOM   92    N  N      . GLY   A 1  13  ? -25.422 -80.784  52.128  1.00 48.19  ? 13  GLY   A N      1 
ATOM   93    C  CA     . GLY   A 1  13  ? -26.203 -81.892  52.650  1.00 46.66  ? 13  GLY   A CA     1 
ATOM   94    C  C      . GLY   A 1  13  ? -25.956 -83.176  51.887  1.00 46.02  ? 13  GLY   A C      1 
ATOM   95    O  O      . GLY   A 1  13  ? -25.698 -84.221  52.487  1.00 47.46  ? 13  GLY   A O      1 
ATOM   96    N  N      . VAL   A 1  14  ? -25.985 -83.100  50.549  1.00 46.28  ? 14  VAL   A N      1 
ATOM   97    C  CA     . VAL   A 1  14  ? -25.896 -84.283  49.692  1.00 43.73  ? 14  VAL   A CA     1 
ATOM   98    C  C      . VAL   A 1  14  ? -24.519 -84.930  49.804  1.00 45.15  ? 14  VAL   A C      1 
ATOM   99    O  O      . VAL   A 1  14  ? -24.395 -86.153  49.907  1.00 46.31  ? 14  VAL   A O      1 
ATOM   100   C  CB     . VAL   A 1  14  ? -26.216 -83.902  48.231  1.00 40.27  ? 14  VAL   A CB     1 
ATOM   101   C  CG1    . VAL   A 1  14  ? -25.817 -85.007  47.296  1.00 44.16  ? 14  VAL   A CG1    1 
ATOM   102   C  CG2    . VAL   A 1  14  ? -27.684 -83.587  48.055  1.00 41.83  ? 14  VAL   A CG2    1 
ATOM   103   N  N      . GLN   A 1  15  ? -23.460 -84.122  49.773  1.00 48.13  ? 15  GLN   A N      1 
ATOM   104   C  CA     . GLN   A 1  15  ? -22.114 -84.671  49.858  1.00 46.34  ? 15  GLN   A CA     1 
ATOM   105   C  C      . GLN   A 1  15  ? -21.819 -85.210  51.249  1.00 47.70  ? 15  GLN   A C      1 
ATOM   106   O  O      . GLN   A 1  15  ? -21.161 -86.248  51.384  1.00 52.87  ? 15  GLN   A O      1 
ATOM   107   C  CB     . GLN   A 1  15  ? -21.093 -83.611  49.464  1.00 50.09  ? 15  GLN   A CB     1 
ATOM   108   C  CG     . GLN   A 1  15  ? -21.004 -83.435  47.970  1.00 54.31  ? 15  GLN   A CG     1 
ATOM   109   C  CD     . GLN   A 1  15  ? -20.134 -82.285  47.529  1.00 51.73  ? 15  GLN   A CD     1 
ATOM   110   O  OE1    . GLN   A 1  15  ? -19.524 -81.576  48.342  1.00 54.27  ? 15  GLN   A OE1    1 
ATOM   111   N  NE2    . GLN   A 1  15  ? -20.062 -82.099  46.222  1.00 55.56  ? 15  GLN   A NE2    1 
ATOM   112   N  N      . ILE   A 1  16  ? -22.282 -84.523  52.296  1.00 43.46  ? 16  ILE   A N      1 
ATOM   113   C  CA     . ILE   A 1  16  ? -22.133 -85.080  53.637  1.00 44.74  ? 16  ILE   A CA     1 
ATOM   114   C  C      . ILE   A 1  16  ? -22.911 -86.385  53.750  1.00 44.58  ? 16  ILE   A C      1 
ATOM   115   O  O      . ILE   A 1  16  ? -22.445 -87.341  54.378  1.00 41.94  ? 16  ILE   A O      1 
ATOM   116   C  CB     . ILE   A 1  16  ? -22.548 -84.048  54.704  1.00 43.63  ? 16  ILE   A CB     1 
ATOM   117   C  CG1    . ILE   A 1  16  ? -21.484 -82.942  54.802  1.00 41.98  ? 16  ILE   A CG1    1 
ATOM   118   C  CG2    . ILE   A 1  16  ? -22.788 -84.720  56.051  1.00 35.04  ? 16  ILE   A CG2    1 
ATOM   119   C  CD1    . ILE   A 1  16  ? -21.830 -81.791  55.733  1.00 35.29  ? 16  ILE   A CD1    1 
ATOM   120   N  N      . GLY   A 1  17  ? -24.083 -86.461  53.095  1.00 44.82  ? 17  GLY   A N      1 
ATOM   121   C  CA     . GLY   A 1  17  ? -24.872 -87.688  53.103  1.00 40.64  ? 17  GLY   A CA     1 
ATOM   122   C  C      . GLY   A 1  17  ? -24.145 -88.864  52.477  1.00 45.97  ? 17  GLY   A C      1 
ATOM   123   O  O      . GLY   A 1  17  ? -24.142 -89.970  53.024  1.00 45.55  ? 17  GLY   A O      1 
ATOM   124   N  N      . ASN   A 1  18  ? -23.530 -88.643  51.316  1.00 46.40  ? 18  ASN   A N      1 
ATOM   125   C  CA     . ASN   A 1  18  ? -22.647 -89.642  50.725  1.00 48.79  ? 18  ASN   A CA     1 
ATOM   126   C  C      . ASN   A 1  18  ? -21.628 -90.136  51.736  1.00 49.04  ? 18  ASN   A C      1 
ATOM   127   O  O      . ASN   A 1  18  ? -21.435 -91.342  51.916  1.00 47.59  ? 18  ASN   A O      1 
ATOM   128   C  CB     . ASN   A 1  18  ? -21.903 -89.033  49.545  1.00 51.64  ? 18  ASN   A CB     1 
ATOM   129   C  CG     . ASN   A 1  18  ? -22.730 -88.996  48.309  1.00 61.59  ? 18  ASN   A CG     1 
ATOM   130   O  OD1    . ASN   A 1  18  ? -23.436 -88.018  48.085  1.00 65.05  ? 18  ASN   A OD1    1 
ATOM   131   N  ND2    . ASN   A 1  18  ? -22.690 -90.065  47.508  1.00 62.98  ? 18  ASN   A ND2    1 
ATOM   132   N  N      . ALA   A 1  19  ? -20.925 -89.203  52.374  1.00 44.67  ? 19  ALA   A N      1 
ATOM   133   C  CA     . ALA   A 1  19  ? -19.918 -89.598  53.349  1.00 54.32  ? 19  ALA   A CA     1 
ATOM   134   C  C      . ALA   A 1  19  ? -20.514 -90.514  54.414  1.00 52.85  ? 19  ALA   A C      1 
ATOM   135   O  O      . ALA   A 1  19  ? -19.907 -91.527  54.781  1.00 53.93  ? 19  ALA   A O      1 
ATOM   136   C  CB     . ALA   A 1  19  ? -19.285 -88.357  53.982  1.00 51.24  ? 19  ALA   A CB     1 
ATOM   137   N  N      . CYS   A 1  20  ? -21.715 -90.188  54.898  1.00 47.07  ? 20  CYS   A N      1 
ATOM   138   C  CA     . CYS   A 1  20  ? -22.326 -90.965  55.967  1.00 44.56  ? 20  CYS   A CA     1 
ATOM   139   C  C      . CYS   A 1  20  ? -22.755 -92.335  55.478  1.00 48.16  ? 20  CYS   A C      1 
ATOM   140   O  O      . CYS   A 1  20  ? -22.298 -93.359  55.995  1.00 49.69  ? 20  CYS   A O      1 
ATOM   141   C  CB     . CYS   A 1  20  ? -23.511 -90.215  56.537  1.00 40.33  ? 20  CYS   A CB     1 
ATOM   142   S  SG     . CYS   A 1  20  ? -22.960 -88.800  57.398  1.00 42.47  ? 20  CYS   A SG     1 
ATOM   143   N  N      . TRP   A 1  21  ? -23.643 -92.374  54.487  1.00 46.20  ? 21  TRP   A N      1 
ATOM   144   C  CA     . TRP   A 1  21  ? -24.173 -93.651  54.033  1.00 43.88  ? 21  TRP   A CA     1 
ATOM   145   C  C      . TRP   A 1  21  ? -23.056 -94.599  53.641  1.00 41.71  ? 21  TRP   A C      1 
ATOM   146   O  O      . TRP   A 1  21  ? -23.097 -95.787  53.971  1.00 43.52  ? 21  TRP   A O      1 
ATOM   147   C  CB     . TRP   A 1  21  ? -25.143 -93.414  52.886  1.00 42.09  ? 21  TRP   A CB     1 
ATOM   148   C  CG     . TRP   A 1  21  ? -26.367 -92.851  53.442  1.00 48.12  ? 21  TRP   A CG     1 
ATOM   149   C  CD1    . TRP   A 1  21  ? -26.741 -91.554  53.405  1.00 43.59  ? 21  TRP   A CD1    1 
ATOM   150   C  CD2    . TRP   A 1  21  ? -27.381 -93.550  54.185  1.00 49.71  ? 21  TRP   A CD2    1 
ATOM   151   N  NE1    . TRP   A 1  21  ? -27.926 -91.393  54.061  1.00 48.67  ? 21  TRP   A NE1    1 
ATOM   152   C  CE2    . TRP   A 1  21  ? -28.347 -92.603  54.548  1.00 46.85  ? 21  TRP   A CE2    1 
ATOM   153   C  CE3    . TRP   A 1  21  ? -27.571 -94.886  54.557  1.00 48.29  ? 21  TRP   A CE3    1 
ATOM   154   C  CZ2    . TRP   A 1  21  ? -29.487 -92.937  55.283  1.00 44.19  ? 21  TRP   A CZ2    1 
ATOM   155   C  CZ3    . TRP   A 1  21  ? -28.703 -95.218  55.275  1.00 51.66  ? 21  TRP   A CZ3    1 
ATOM   156   C  CH2    . TRP   A 1  21  ? -29.649 -94.245  55.629  1.00 52.11  ? 21  TRP   A CH2    1 
ATOM   157   N  N      . GLU   A 1  22  ? -22.033 -94.093  52.962  1.00 43.14  ? 22  GLU   A N      1 
ATOM   158   C  CA     . GLU   A 1  22  ? -20.883 -94.937  52.695  1.00 49.33  ? 22  GLU   A CA     1 
ATOM   159   C  C      . GLU   A 1  22  ? -20.362 -95.533  53.989  1.00 55.53  ? 22  GLU   A C      1 
ATOM   160   O  O      . GLU   A 1  22  ? -20.075 -96.733  54.059  1.00 56.01  ? 22  GLU   A O      1 
ATOM   161   C  CB     . GLU   A 1  22  ? -19.762 -94.151  52.050  1.00 51.31  ? 22  GLU   A CB     1 
ATOM   162   C  CG     . GLU   A 1  22  ? -18.466 -94.920  52.151  1.00 55.95  ? 22  GLU   A CG     1 
ATOM   163   C  CD     . GLU   A 1  22  ? -17.272 -94.166  51.594  1.00 69.28  ? 22  GLU   A CD     1 
ATOM   164   O  OE1    . GLU   A 1  22  ? -17.145 -92.939  51.875  1.00 66.89  ? 22  GLU   A OE1    1 
ATOM   165   O  OE2    . GLU   A 1  22  ? -16.485 -94.800  50.843  1.00 63.83  ? 22  GLU   A OE2    1 
ATOM   166   N  N      . LEU   A 1  23  ? -20.234 -94.695  55.032  1.00 51.93  ? 23  LEU   A N      1 
ATOM   167   C  CA     . LEU   A 1  23  ? -19.725 -95.146  56.328  1.00 51.32  ? 23  LEU   A CA     1 
ATOM   168   C  C      . LEU   A 1  23  ? -20.673 -96.133  56.991  1.00 52.82  ? 23  LEU   A C      1 
ATOM   169   O  O      . LEU   A 1  23  ? -20.252 -97.217  57.408  1.00 53.55  ? 23  LEU   A O      1 
ATOM   170   C  CB     . LEU   A 1  23  ? -19.486 -93.953  57.246  1.00 53.03  ? 23  LEU   A CB     1 
ATOM   171   C  CG     . LEU   A 1  23  ? -18.911 -94.283  58.623  1.00 53.28  ? 23  LEU   A CG     1 
ATOM   172   C  CD1    . LEU   A 1  23  ? -17.570 -94.955  58.477  1.00 52.16  ? 23  LEU   A CD1    1 
ATOM   173   C  CD2    . LEU   A 1  23  ? -18.752 -92.998  59.401  1.00 52.38  ? 23  LEU   A CD2    1 
ATOM   174   N  N      . TYR   A 1  24  ? -21.954 -95.769  57.111  1.00 48.56  ? 24  TYR   A N      1 
ATOM   175   C  CA     . TYR   A 1  24  ? -22.958 -96.727  57.554  1.00 48.65  ? 24  TYR   A CA     1 
ATOM   176   C  C      . TYR   A 1  24  ? -22.763 -98.094  56.893  1.00 54.08  ? 24  TYR   A C      1 
ATOM   177   O  O      . TYR   A 1  24  ? -22.745 -99.125  57.569  1.00 52.79  ? 24  TYR   A O      1 
ATOM   178   C  CB     . TYR   A 1  24  ? -24.359 -96.212  57.256  1.00 46.30  ? 24  TYR   A CB     1 
ATOM   179   C  CG     . TYR   A 1  24  ? -24.722 -94.921  57.945  1.00 48.54  ? 24  TYR   A CG     1 
ATOM   180   C  CD1    . TYR   A 1  24  ? -23.951 -94.405  58.969  1.00 48.02  ? 24  TYR   A CD1    1 
ATOM   181   C  CD2    . TYR   A 1  24  ? -25.903 -94.257  57.613  1.00 50.78  ? 24  TYR   A CD2    1 
ATOM   182   C  CE1    . TYR   A 1  24  ? -24.324 -93.208  59.613  1.00 49.52  ? 24  TYR   A CE1    1 
ATOM   183   C  CE2    . TYR   A 1  24  ? -26.282 -93.087  58.244  1.00 51.81  ? 24  TYR   A CE2    1 
ATOM   184   C  CZ     . TYR   A 1  24  ? -25.493 -92.567  59.239  1.00 49.38  ? 24  TYR   A CZ     1 
ATOM   185   O  OH     . TYR   A 1  24  ? -25.885 -91.404  59.835  1.00 45.34  ? 24  TYR   A OH     1 
ATOM   186   N  N      . CYS   A 1  25  ? -22.603 -98.126  55.567  1.00 54.89  ? 25  CYS   A N      1 
ATOM   187   C  CA     . CYS   A 1  25  ? -22.498 -99.409  54.874  1.00 51.74  ? 25  CYS   A CA     1 
ATOM   188   C  C      . CYS   A 1  25  ? -21.314 -100.225 55.363  1.00 52.47  ? 25  CYS   A C      1 
ATOM   189   O  O      . CYS   A 1  25  ? -21.440 -101.431 55.595  1.00 56.21  ? 25  CYS   A O      1 
ATOM   190   C  CB     . CYS   A 1  25  ? -22.408 -99.196  53.372  1.00 50.09  ? 25  CYS   A CB     1 
ATOM   191   S  SG     . CYS   A 1  25  ? -23.972 -98.717  52.712  1.00 55.57  ? 25  CYS   A SG     1 
ATOM   192   N  N      . LEU   A 1  26  ? -20.148 -99.602  55.498  1.00 51.72  ? 26  LEU   A N      1 
ATOM   193   C  CA     . LEU   A 1  26  ? -19.011 -100.321 56.059  1.00 52.45  ? 26  LEU   A CA     1 
ATOM   194   C  C      . LEU   A 1  26  ? -19.329 -100.798 57.471  1.00 54.34  ? 26  LEU   A C      1 
ATOM   195   O  O      . LEU   A 1  26  ? -19.132 -101.970 57.807  1.00 57.12  ? 26  LEU   A O      1 
ATOM   196   C  CB     . LEU   A 1  26  ? -17.779 -99.423  56.056  1.00 48.76  ? 26  LEU   A CB     1 
ATOM   197   C  CG     . LEU   A 1  26  ? -17.262 -99.024  54.676  1.00 44.10  ? 26  LEU   A CG     1 
ATOM   198   C  CD1    . LEU   A 1  26  ? -16.142 -97.990  54.780  1.00 53.96  ? 26  LEU   A CD1    1 
ATOM   199   C  CD2    . LEU   A 1  26  ? -16.800 -100.222 53.944  1.00 44.41  ? 26  LEU   A CD2    1 
ATOM   200   N  N      . GLU   A 1  27  ? -19.861 -99.904  58.303  1.00 50.51  ? 27  GLU   A N      1 
ATOM   201   C  CA     . GLU   A 1  27  ? -20.167 -100.261 59.682  1.00 54.15  ? 27  GLU   A CA     1 
ATOM   202   C  C      . GLU   A 1  27  ? -21.157 -101.424 59.759  1.00 58.11  ? 27  GLU   A C      1 
ATOM   203   O  O      . GLU   A 1  27  ? -20.951 -102.369 60.529  1.00 67.71  ? 27  GLU   A O      1 
ATOM   204   C  CB     . GLU   A 1  27  ? -20.687 -99.031  60.429  1.00 49.28  ? 27  GLU   A CB     1 
ATOM   205   C  CG     . GLU   A 1  27  ? -19.620 -97.975  60.640  1.00 51.22  ? 27  GLU   A CG     1 
ATOM   206   C  CD     . GLU   A 1  27  ? -20.101 -96.807  61.464  1.00 51.26  ? 27  GLU   A CD     1 
ATOM   207   O  OE1    . GLU   A 1  27  ? -21.272 -96.855  61.887  1.00 51.85  ? 27  GLU   A OE1    1 
ATOM   208   O  OE2    . GLU   A 1  27  ? -19.311 -95.854  61.691  1.00 52.37  ? 27  GLU   A OE2    1 
ATOM   209   N  N      . HIS   A 1  28  ? -22.223 -101.383 58.969  1.00 53.01  ? 28  HIS   A N      1 
ATOM   210   C  CA     . HIS   A 1  28  ? -23.228 -102.436 58.960  1.00 55.25  ? 28  HIS   A CA     1 
ATOM   211   C  C      . HIS   A 1  28  ? -22.880 -103.607 58.040  1.00 56.70  ? 28  HIS   A C      1 
ATOM   212   O  O      . HIS   A 1  28  ? -23.634 -104.581 58.004  1.00 61.03  ? 28  HIS   A O      1 
ATOM   213   C  CB     . HIS   A 1  28  ? -24.578 -101.857 58.541  1.00 59.87  ? 28  HIS   A CB     1 
ATOM   214   C  CG     . HIS   A 1  28  ? -25.145 -100.872 59.513  1.00 59.24  ? 28  HIS   A CG     1 
ATOM   215   N  ND1    . HIS   A 1  28  ? -25.686 -101.245 60.722  1.00 59.31  ? 28  HIS   A ND1    1 
ATOM   216   C  CD2    . HIS   A 1  28  ? -25.263 -99.524  59.446  1.00 58.79  ? 28  HIS   A CD2    1 
ATOM   217   C  CE1    . HIS   A 1  28  ? -26.116 -100.169 61.358  1.00 59.01  ? 28  HIS   A CE1    1 
ATOM   218   N  NE2    . HIS   A 1  28  ? -25.865 -99.111  60.608  1.00 58.11  ? 28  HIS   A NE2    1 
ATOM   219   N  N      . GLY   A 1  29  ? -21.776 -103.542 57.295  1.00 56.59  ? 29  GLY   A N      1 
ATOM   220   C  CA     . GLY   A 1  29  ? -21.401 -104.622 56.401  1.00 54.27  ? 29  GLY   A CA     1 
ATOM   221   C  C      . GLY   A 1  29  ? -22.291 -104.795 55.193  1.00 60.77  ? 29  GLY   A C      1 
ATOM   222   O  O      . GLY   A 1  29  ? -22.363 -105.893 54.640  1.00 66.97  ? 29  GLY   A O      1 
ATOM   223   N  N      . ILE   A 1  30  ? -22.989 -103.747 54.786  1.00 62.55  ? 30  ILE   A N      1 
ATOM   224   C  CA     . ILE   A 1  30  ? -23.719 -103.721 53.525  1.00 60.63  ? 30  ILE   A CA     1 
ATOM   225   C  C      . ILE   A 1  30  ? -22.739 -103.420 52.406  1.00 62.05  ? 30  ILE   A C      1 
ATOM   226   O  O      . ILE   A 1  30  ? -21.834 -102.597 52.568  1.00 64.52  ? 30  ILE   A O      1 
ATOM   227   C  CB     . ILE   A 1  30  ? -24.817 -102.652 53.585  1.00 59.74  ? 30  ILE   A CB     1 
ATOM   228   C  CG1    . ILE   A 1  30  ? -25.704 -102.876 54.807  1.00 56.18  ? 30  ILE   A CG1    1 
ATOM   229   C  CG2    . ILE   A 1  30  ? -25.589 -102.593 52.279  1.00 62.64  ? 30  ILE   A CG2    1 
ATOM   230   C  CD1    . ILE   A 1  30  ? -26.825 -101.885 54.892  1.00 59.88  ? 30  ILE   A CD1    1 
ATOM   231   N  N      . GLN   A 1  31  ? -22.905 -104.072 51.261  1.00 71.59  ? 31  GLN   A N      1 
ATOM   232   C  CA     . GLN   A 1  31  ? -21.983 -103.703 50.190  1.00 72.59  ? 31  GLN   A CA     1 
ATOM   233   C  C      . GLN   A 1  31  ? -22.656 -102.773 49.186  1.00 69.31  ? 31  GLN   A C      1 
ATOM   234   O  O      . GLN   A 1  31  ? -23.885 -102.636 49.173  1.00 72.59  ? 31  GLN   A O      1 
ATOM   235   C  CB     . GLN   A 1  31  ? -21.454 -104.953 49.491  1.00 74.20  ? 31  GLN   A CB     1 
ATOM   236   C  CG     . GLN   A 1  31  ? -22.447 -106.096 49.491  1.00 76.61  ? 31  GLN   A CG     1 
ATOM   237   C  CD     . GLN   A 1  31  ? -21.797 -107.450 49.310  1.00 82.96  ? 31  GLN   A CD     1 
ATOM   238   O  OE1    . GLN   A 1  31  ? -20.633 -107.657 49.686  1.00 76.59  ? 31  GLN   A OE1    1 
ATOM   239   N  NE2    . GLN   A 1  31  ? -22.554 -108.391 48.726  1.00 80.63  ? 31  GLN   A NE2    1 
ATOM   240   N  N      . PRO   A 1  32  ? -21.866 -102.115 48.331  1.00 68.70  ? 32  PRO   A N      1 
ATOM   241   C  CA     . PRO   A 1  32  ? -22.415 -101.048 47.470  1.00 66.93  ? 32  PRO   A CA     1 
ATOM   242   C  C      . PRO   A 1  32  ? -23.607 -101.448 46.607  1.00 73.19  ? 32  PRO   A C      1 
ATOM   243   O  O      . PRO   A 1  32  ? -24.333 -100.558 46.143  1.00 71.19  ? 32  PRO   A O      1 
ATOM   244   C  CB     . PRO   A 1  32  ? -21.214 -100.665 46.601  1.00 60.24  ? 32  PRO   A CB     1 
ATOM   245   C  CG     . PRO   A 1  32  ? -20.052 -101.016 47.413  1.00 61.15  ? 32  PRO   A CG     1 
ATOM   246   C  CD     . PRO   A 1  32  ? -20.416 -102.266 48.147  1.00 68.64  ? 32  PRO   A CD     1 
ATOM   247   N  N      . ASP   A 1  33  ? -23.817 -102.737 46.343  1.00 76.18  ? 33  ASP   A N      1 
ATOM   248   C  CA     . ASP   A 1  33  ? -25.006 -103.183 45.625  1.00 70.40  ? 33  ASP   A CA     1 
ATOM   249   C  C      . ASP   A 1  33  ? -26.200 -103.398 46.545  1.00 72.72  ? 33  ASP   A C      1 
ATOM   250   O  O      . ASP   A 1  33  ? -27.241 -103.881 46.087  1.00 73.80  ? 33  ASP   A O      1 
ATOM   251   C  CB     . ASP   A 1  33  ? -24.707 -104.476 44.870  1.00 71.07  ? 33  ASP   A CB     1 
ATOM   252   C  CG     . ASP   A 1  33  ? -24.319 -105.607 45.789  1.00 76.29  ? 33  ASP   A CG     1 
ATOM   253   O  OD1    . ASP   A 1  33  ? -24.099 -105.347 46.986  1.00 81.61  ? 33  ASP   A OD1    1 
ATOM   254   O  OD2    . ASP   A 1  33  ? -24.202 -106.754 45.315  1.00 83.34  ? 33  ASP   A OD2    1 
ATOM   255   N  N      . GLY   A 1  34  ? -26.071 -103.071 47.827  1.00 72.52  ? 34  GLY   A N      1 
ATOM   256   C  CA     . GLY   A 1  34  ? -27.171 -103.181 48.756  1.00 71.78  ? 34  GLY   A CA     1 
ATOM   257   C  C      . GLY   A 1  34  ? -27.403 -104.556 49.337  1.00 72.70  ? 34  GLY   A C      1 
ATOM   258   O  O      . GLY   A 1  34  ? -28.431 -104.757 50.000  1.00 71.46  ? 34  GLY   A O      1 
ATOM   259   N  N      . GLN   A 1  35  ? -26.495 -105.511 49.101  1.00 72.14  ? 35  GLN   A N      1 
ATOM   260   C  CA     . GLN   A 1  35  ? -26.582 -106.839 49.699  1.00 73.68  ? 35  GLN   A CA     1 
ATOM   261   C  C      . GLN   A 1  35  ? -25.829 -106.875 51.013  1.00 72.10  ? 35  GLN   A C      1 
ATOM   262   O  O      . GLN   A 1  35  ? -24.726 -106.336 51.120  1.00 69.29  ? 35  GLN   A O      1 
ATOM   263   C  CB     . GLN   A 1  35  ? -26.031 -107.921 48.767  1.00 68.70  ? 35  GLN   A CB     1 
ATOM   264   C  CG     . GLN   A 1  35  ? -26.869 -108.113 47.543  1.00 68.99  ? 35  GLN   A CG     1 
ATOM   265   C  CD     . GLN   A 1  35  ? -28.077 -108.970 47.855  1.00 72.08  ? 35  GLN   A CD     1 
ATOM   266   O  OE1    . GLN   A 1  35  ? -29.218 -108.550 47.674  1.00 71.86  ? 35  GLN   A OE1    1 
ATOM   267   N  NE2    . GLN   A 1  35  ? -27.833 -110.166 48.366  1.00 78.88  ? 35  GLN   A NE2    1 
ATOM   268   N  N      . MET   A 1  36  ? -26.427 -107.528 52.008  1.00 71.87  ? 36  MET   A N      1 
ATOM   269   C  CA     . MET   A 1  36  ? -25.867 -107.586 53.355  1.00 71.44  ? 36  MET   A CA     1 
ATOM   270   C  C      . MET   A 1  36  ? -25.767 -109.027 53.827  1.00 70.62  ? 36  MET   A C      1 
ATOM   271   O  O      . MET   A 1  36  ? -26.609 -109.483 54.613  1.00 71.25  ? 36  MET   A O      1 
ATOM   272   C  CB     . MET   A 1  36  ? -26.707 -106.772 54.330  1.00 64.71  ? 36  MET   A CB     1 
ATOM   273   C  CG     . MET   A 1  36  ? -26.086 -106.664 55.681  1.00 63.82  ? 36  MET   A CG     1 
ATOM   274   S  SD     . MET   A 1  36  ? -27.233 -105.756 56.698  1.00 60.85  ? 36  MET   A SD     1 
ATOM   275   C  CE     . MET   A 1  36  ? -26.287 -105.629 58.201  1.00 68.16  ? 36  MET   A CE     1 
ATOM   276   N  N      . PRO   A 1  37  ? -24.709 -109.757 53.410  1.00 64.18  ? 37  PRO   A N      1 
ATOM   277   C  CA     . PRO   A 1  37  ? -24.578 -111.174 53.784  1.00 64.18  ? 37  PRO   A CA     1 
ATOM   278   C  C      . PRO   A 1  37  ? -25.118 -111.515 55.164  1.00 72.34  ? 37  PRO   A C      1 
ATOM   279   O  O      . PRO   A 1  37  ? -25.989 -112.382 55.292  1.00 71.46  ? 37  PRO   A O      1 
ATOM   280   C  CB     . PRO   A 1  37  ? -23.066 -111.413 53.710  1.00 61.25  ? 37  PRO   A CB     1 
ATOM   281   C  CG     . PRO   A 1  37  ? -22.580 -110.420 52.737  1.00 62.14  ? 37  PRO   A CG     1 
ATOM   282   C  CD     . PRO   A 1  37  ? -23.446 -109.210 52.889  1.00 67.55  ? 37  PRO   A CD     1 
ATOM   283   N  N      . SER   A 1  38  ? -24.635 -110.826 56.201  1.00 74.60  ? 38  SER   A N      1 
ATOM   284   C  CA     . SER   A 1  38  ? -25.014 -111.188 57.564  1.00 69.18  ? 38  SER   A CA     1 
ATOM   285   C  C      . SER   A 1  38  ? -26.519 -111.073 57.817  1.00 72.98  ? 38  SER   A C      1 
ATOM   286   O  O      . SER   A 1  38  ? -27.024 -111.713 58.747  1.00 74.64  ? 38  SER   A O      1 
ATOM   287   C  CB     . SER   A 1  38  ? -24.258 -110.330 58.576  1.00 67.87  ? 38  SER   A CB     1 
ATOM   288   O  OG     . SER   A 1  38  ? -24.105 -109.011 58.090  1.00 77.23  ? 38  SER   A OG     1 
ATOM   289   N  N      . ASP   A 1  39  ? -27.267 -110.266 57.044  1.00 70.10  ? 39  ASP   A N      1 
ATOM   290   C  CA     . ASP   A 1  39  ? -28.713 -110.260 57.277  1.00 68.30  ? 39  ASP   A CA     1 
ATOM   291   C  C      . ASP   A 1  39  ? -29.253 -111.598 56.828  1.00 72.42  ? 39  ASP   A C      1 
ATOM   292   O  O      . ASP   A 1  39  ? -29.199 -111.923 55.639  1.00 77.96  ? 39  ASP   A O      1 
ATOM   293   C  CB     . ASP   A 1  39  ? -29.463 -109.136 56.568  1.00 61.25  ? 39  ASP   A CB     1 
ATOM   294   C  CG     . ASP   A 1  39  ? -30.967 -109.111 56.941  1.00 64.01  ? 39  ASP   A CG     1 
ATOM   295   O  OD1    . ASP   A 1  39  ? -31.478 -110.039 57.572  1.00 65.48  ? 39  ASP   A OD1    1 
ATOM   296   O  OD2    . ASP   A 1  39  ? -31.663 -108.146 56.644  1.00 70.45  ? 39  ASP   A OD2    1 
ATOM   297   N  N      . LYS   A 1  40  ? -29.737 -112.387 57.779  1.00 66.17  ? 40  LYS   A N      1 
ATOM   298   C  CA     . LYS   A 1  40  ? -30.483 -113.565 57.393  1.00 64.21  ? 40  LYS   A CA     1 
ATOM   299   C  C      . LYS   A 1  40  ? -31.951 -113.217 57.180  1.00 66.14  ? 40  LYS   A C      1 
ATOM   300   O  O      . LYS   A 1  40  ? -32.546 -113.628 56.178  1.00 71.65  ? 40  LYS   A O      1 
ATOM   301   C  CB     . LYS   A 1  40  ? -30.312 -114.642 58.450  1.00 65.95  ? 40  LYS   A CB     1 
ATOM   302   C  CG     . LYS   A 1  40  ? -28.863 -114.864 58.839  1.00 59.59  ? 40  LYS   A CG     1 
ATOM   303   C  CD     . LYS   A 1  40  ? -27.980 -115.309 57.692  1.00 57.15  ? 40  LYS   A CD     1 
ATOM   304   C  CE     . LYS   A 1  40  ? -26.540 -115.216 58.153  1.00 65.45  ? 40  LYS   A CE     1 
ATOM   305   N  NZ     . LYS   A 1  40  ? -25.549 -115.697 57.179  1.00 69.95  ? 40  LYS   A NZ     1 
ATOM   306   N  N      . THR   A 1  41  ? -32.533 -112.415 58.075  1.00 68.70  ? 41  THR   A N      1 
ATOM   307   C  CA     . THR   A 1  41  ? -33.876 -111.879 57.869  1.00 76.41  ? 41  THR   A CA     1 
ATOM   308   C  C      . THR   A 1  41  ? -33.920 -111.219 56.494  1.00 76.88  ? 41  THR   A C      1 
ATOM   309   O  O      . THR   A 1  41  ? -33.715 -109.998 56.404  1.00 73.71  ? 41  THR   A O      1 
ATOM   310   C  CB     . THR   A 1  41  ? -34.252 -110.817 58.918  1.00 83.05  ? 41  THR   A CB     1 
ATOM   311   O  OG1    . THR   A 1  41  ? -33.889 -111.237 60.238  1.00 78.43  ? 41  THR   A OG1    1 
ATOM   312   C  CG2    . THR   A 1  41  ? -35.760 -110.600 58.906  1.00 86.40  ? 41  THR   A CG2    1 
ATOM   313   N  N      . ILE   A 1  42  ? -34.160 -112.013 55.423  1.00 71.53  ? 42  ILE   A N      1 
ATOM   314   C  CA     . ILE   A 1  42  ? -34.169 -111.493 54.057  1.00 69.37  ? 42  ILE   A CA     1 
ATOM   315   C  C      . ILE   A 1  42  ? -35.487 -110.804 53.756  1.00 72.28  ? 42  ILE   A C      1 
ATOM   316   O  O      . ILE   A 1  42  ? -36.557 -111.279 54.148  1.00 75.93  ? 42  ILE   A O      1 
ATOM   317   C  CB     . ILE   A 1  42  ? -33.928 -112.602 53.028  1.00 60.96  ? 42  ILE   A CB     1 
ATOM   318   C  CG1    . ILE   A 1  42  ? -32.620 -113.326 53.287  1.00 60.33  ? 42  ILE   A CG1    1 
ATOM   319   C  CG2    . ILE   A 1  42  ? -33.936 -111.994 51.661  1.00 66.46  ? 42  ILE   A CG2    1 
ATOM   320   C  CD1    . ILE   A 1  42  ? -32.255 -114.293 52.197  1.00 46.38  ? 42  ILE   A CD1    1 
ATOM   321   N  N      . GLY   A 1  43  ? -35.419 -109.707 53.012  1.00 69.70  ? 43  GLY   A N      1 
ATOM   322   C  CA     . GLY   A 1  43  ? -36.625 -108.994 52.658  1.00 72.17  ? 43  GLY   A CA     1 
ATOM   323   C  C      . GLY   A 1  43  ? -37.339 -108.390 53.852  1.00 73.82  ? 43  GLY   A C      1 
ATOM   324   O  O      . GLY   A 1  43  ? -38.451 -107.869 53.700  1.00 69.02  ? 43  GLY   A O      1 
ATOM   325   N  N      . GLY   A 1  44  ? -36.725 -108.458 55.033  1.00 75.42  ? 44  GLY   A N      1 
ATOM   326   C  CA     . GLY   A 1  44  ? -37.286 -107.781 56.187  1.00 77.56  ? 44  GLY   A CA     1 
ATOM   327   C  C      . GLY   A 1  44  ? -36.464 -107.956 57.445  1.00 70.51  ? 44  GLY   A C      1 
ATOM   328   O  O      . GLY   A 1  44  ? -35.300 -108.364 57.425  1.00 67.99  ? 44  GLY   A O      1 
ATOM   329   N  N      . GLY   A 1  45  ? -37.119 -107.633 58.550  1.00 72.10  ? 45  GLY   A N      1 
ATOM   330   C  CA     . GLY   A 1  45  ? -36.533 -107.675 59.877  1.00 82.57  ? 45  GLY   A CA     1 
ATOM   331   C  C      . GLY   A 1  45  ? -36.881 -106.419 60.657  1.00 84.24  ? 45  GLY   A C      1 
ATOM   332   O  O      . GLY   A 1  45  ? -36.913 -105.321 60.080  1.00 81.37  ? 45  GLY   A O      1 
ATOM   333   N  N      . ASP   A 1  46  ? -37.175 -106.547 61.952  1.00 81.17  ? 46  ASP   A N      1 
ATOM   334   C  CA     . ASP   A 1  46  ? -37.249 -105.368 62.816  1.00 82.13  ? 46  ASP   A CA     1 
ATOM   335   C  C      . ASP   A 1  46  ? -35.975 -105.232 63.648  1.00 79.55  ? 46  ASP   A C      1 
ATOM   336   O  O      . ASP   A 1  46  ? -36.012 -104.811 64.808  1.00 80.40  ? 46  ASP   A O      1 
ATOM   337   C  CB     . ASP   A 1  46  ? -38.511 -105.376 63.692  1.00 86.95  ? 46  ASP   A CB     1 
ATOM   338   C  CG     . ASP   A 1  46  ? -38.545 -106.525 64.685  1.00 98.02  ? 46  ASP   A CG     1 
ATOM   339   O  OD1    . ASP   A 1  46  ? -37.810 -107.518 64.468  1.00 98.64  ? 46  ASP   A OD1    1 
ATOM   340   O  OD2    . ASP   A 1  46  ? -39.325 -106.439 65.669  1.00 92.93  ? 46  ASP   A OD2    1 
ATOM   341   N  N      . ASP   A 1  47  ? -34.835 -105.580 63.034  1.00 76.68  ? 47  ASP   A N      1 
ATOM   342   C  CA     . ASP   A 1  47  ? -33.492 -105.289 63.529  1.00 72.84  ? 47  ASP   A CA     1 
ATOM   343   C  C      . ASP   A 1  47  ? -33.269 -103.785 63.684  1.00 70.48  ? 47  ASP   A C      1 
ATOM   344   O  O      . ASP   A 1  47  ? -34.044 -102.954 63.200  1.00 71.32  ? 47  ASP   A O      1 
ATOM   345   C  CB     . ASP   A 1  47  ? -32.439 -105.837 62.572  1.00 68.71  ? 47  ASP   A CB     1 
ATOM   346   C  CG     . ASP   A 1  47  ? -32.467 -107.326 62.484  1.00 72.05  ? 47  ASP   A CG     1 
ATOM   347   O  OD1    . ASP   A 1  47  ? -32.822 -107.955 63.499  1.00 70.34  ? 47  ASP   A OD1    1 
ATOM   348   O  OD2    . ASP   A 1  47  ? -32.184 -107.863 61.391  1.00 76.49  ? 47  ASP   A OD2    1 
ATOM   349   N  N      . SER   A 1  48  ? -32.158 -103.434 64.341  1.00 68.01  ? 48  SER   A N      1 
ATOM   350   C  CA     . SER   A 1  48  ? -31.906 -102.022 64.604  1.00 67.50  ? 48  SER   A CA     1 
ATOM   351   C  C      . SER   A 1  48  ? -31.234 -101.323 63.424  1.00 62.29  ? 48  SER   A C      1 
ATOM   352   O  O      . SER   A 1  48  ? -31.411 -100.109 63.264  1.00 60.84  ? 48  SER   A O      1 
ATOM   353   C  CB     . SER   A 1  48  ? -31.105 -101.838 65.907  1.00 57.95  ? 48  SER   A CB     1 
ATOM   354   O  OG     . SER   A 1  48  ? -30.010 -102.728 65.997  1.00 67.42  ? 48  SER   A OG     1 
ATOM   355   N  N      . PHE   A 1  49  ? -30.514 -102.036 62.556  1.00 57.83  ? 49  PHE   A N      1 
ATOM   356   C  CA     . PHE   A 1  49  ? -30.124 -101.336 61.338  1.00 58.61  ? 49  PHE   A CA     1 
ATOM   357   C  C      . PHE   A 1  49  ? -31.318 -101.106 60.424  1.00 61.82  ? 49  PHE   A C      1 
ATOM   358   O  O      . PHE   A 1  49  ? -31.273 -100.211 59.569  1.00 56.38  ? 49  PHE   A O      1 
ATOM   359   C  CB     . PHE   A 1  49  ? -28.989 -102.060 60.597  1.00 58.55  ? 49  PHE   A CB     1 
ATOM   360   C  CG     . PHE   A 1  49  ? -29.369 -103.378 60.007  1.00 62.67  ? 49  PHE   A CG     1 
ATOM   361   C  CD1    . PHE   A 1  49  ? -29.426 -104.512 60.801  1.00 66.92  ? 49  PHE   A CD1    1 
ATOM   362   C  CD2    . PHE   A 1  49  ? -29.624 -103.499 58.655  1.00 65.96  ? 49  PHE   A CD2    1 
ATOM   363   C  CE1    . PHE   A 1  49  ? -29.758 -105.734 60.265  1.00 65.35  ? 49  PHE   A CE1    1 
ATOM   364   C  CE2    . PHE   A 1  49  ? -29.969 -104.720 58.108  1.00 67.91  ? 49  PHE   A CE2    1 
ATOM   365   C  CZ     . PHE   A 1  49  ? -30.035 -105.838 58.915  1.00 71.03  ? 49  PHE   A CZ     1 
ATOM   366   N  N      . ASN   A 1  50  ? -32.411 -101.841 60.623  1.00 64.67  ? 50  ASN   A N      1 
ATOM   367   C  CA     . ASN   A 1  50  ? -33.567 -101.569 59.786  1.00 64.88  ? 50  ASN   A CA     1 
ATOM   368   C  C      . ASN   A 1  50  ? -34.170 -100.210 60.064  1.00 59.82  ? 50  ASN   A C      1 
ATOM   369   O  O      . ASN   A 1  50  ? -35.087 -99.800  59.350  1.00 59.89  ? 50  ASN   A O      1 
ATOM   370   C  CB     . ASN   A 1  50  ? -34.605 -102.670 59.950  1.00 61.88  ? 50  ASN   A CB     1 
ATOM   371   C  CG     . ASN   A 1  50  ? -34.183 -103.932 59.237  1.00 72.68  ? 50  ASN   A CG     1 
ATOM   372   O  OD1    . ASN   A 1  50  ? -34.220 -105.024 59.804  1.00 77.78  ? 50  ASN   A OD1    1 
ATOM   373   N  ND2    . ASN   A 1  50  ? -33.660 -103.771 58.019  1.00 66.62  ? 50  ASN   A ND2    1 
ATOM   374   N  N      . THR   A 1  51  ? -33.661 -99.494  61.068  1.00 58.48  ? 51  THR   A N      1 
ATOM   375   C  CA     . THR   A 1  51  ? -34.030 -98.095  61.253  1.00 63.66  ? 51  THR   A CA     1 
ATOM   376   C  C      . THR   A 1  51  ? -33.570 -97.232  60.083  1.00 63.94  ? 51  THR   A C      1 
ATOM   377   O  O      . THR   A 1  51  ? -34.200 -96.213  59.770  1.00 63.18  ? 51  THR   A O      1 
ATOM   378   C  CB     . THR   A 1  51  ? -33.445 -97.566  62.568  1.00 61.39  ? 51  THR   A CB     1 
ATOM   379   O  OG1    . THR   A 1  51  ? -33.978 -98.295  63.680  1.00 57.50  ? 51  THR   A OG1    1 
ATOM   380   C  CG2    . THR   A 1  51  ? -33.739 -96.081  62.726  1.00 66.82  ? 51  THR   A CG2    1 
ATOM   381   N  N      . PHE   A 1  52  ? -32.479 -97.615  59.433  1.00 58.62  ? 52  PHE   A N      1 
ATOM   382   C  CA     . PHE   A 1  52  ? -31.893 -96.807  58.385  1.00 58.39  ? 52  PHE   A CA     1 
ATOM   383   C  C      . PHE   A 1  52  ? -31.950 -97.480  57.029  1.00 58.39  ? 52  PHE   A C      1 
ATOM   384   O  O      . PHE   A 1  52  ? -31.819 -96.800  56.006  1.00 55.11  ? 52  PHE   A O      1 
ATOM   385   C  CB     . PHE   A 1  52  ? -30.445 -96.459  58.750  1.00 55.73  ? 52  PHE   A CB     1 
ATOM   386   C  CG     . PHE   A 1  52  ? -30.334 -95.286  59.674  1.00 51.29  ? 52  PHE   A CG     1 
ATOM   387   C  CD1    . PHE   A 1  52  ? -31.101 -95.226  60.832  1.00 57.70  ? 52  PHE   A CD1    1 
ATOM   388   C  CD2    . PHE   A 1  52  ? -29.433 -94.267  59.417  1.00 48.99  ? 52  PHE   A CD2    1 
ATOM   389   C  CE1    . PHE   A 1  52  ? -30.995 -94.139  61.707  1.00 61.45  ? 52  PHE   A CE1    1 
ATOM   390   C  CE2    . PHE   A 1  52  ? -29.310 -93.192  60.286  1.00 53.96  ? 52  PHE   A CE2    1 
ATOM   391   C  CZ     . PHE   A 1  52  ? -30.090 -93.123  61.437  1.00 53.33  ? 52  PHE   A CZ     1 
ATOM   392   N  N      . PHE   A 1  53  ? -32.183 -98.774  56.994  1.00 58.69  ? 53  PHE   A N      1 
ATOM   393   C  CA     . PHE   A 1  53  ? -32.366 -99.498  55.759  1.00 56.59  ? 53  PHE   A CA     1 
ATOM   394   C  C      . PHE   A 1  53  ? -33.732 -100.156 55.784  1.00 60.59  ? 53  PHE   A C      1 
ATOM   395   O  O      . PHE   A 1  53  ? -34.268 -100.473 56.848  1.00 60.66  ? 53  PHE   A O      1 
ATOM   396   C  CB     . PHE   A 1  53  ? -31.256 -100.515 55.610  1.00 53.94  ? 53  PHE   A CB     1 
ATOM   397   C  CG     . PHE   A 1  53  ? -29.927 -99.885  55.541  1.00 52.35  ? 53  PHE   A CG     1 
ATOM   398   C  CD1    . PHE   A 1  53  ? -29.248 -99.583  56.693  1.00 55.88  ? 53  PHE   A CD1    1 
ATOM   399   C  CD2    . PHE   A 1  53  ? -29.363 -99.553  54.335  1.00 59.15  ? 53  PHE   A CD2    1 
ATOM   400   C  CE1    . PHE   A 1  53  ? -28.011 -98.971  56.649  1.00 57.93  ? 53  PHE   A CE1    1 
ATOM   401   C  CE2    . PHE   A 1  53  ? -28.126 -98.944  54.275  1.00 59.67  ? 53  PHE   A CE2    1 
ATOM   402   C  CZ     . PHE   A 1  53  ? -27.447 -98.655  55.437  1.00 61.43  ? 53  PHE   A CZ     1 
ATOM   403   N  N      . SER   A 1  54  ? -34.321 -100.294 54.607  1.00 68.43  ? 54  SER   A N      1 
ATOM   404   C  CA     . SER   A 1  54  ? -35.352 -101.287 54.361  1.00 65.77  ? 54  SER   A CA     1 
ATOM   405   C  C      . SER   A 1  54  ? -34.744 -102.369 53.479  1.00 64.22  ? 54  SER   A C      1 
ATOM   406   O  O      . SER   A 1  54  ? -33.688 -102.181 52.858  1.00 57.57  ? 54  SER   A O      1 
ATOM   407   C  CB     . SER   A 1  54  ? -36.601 -100.672 53.714  1.00 61.74  ? 54  SER   A CB     1 
ATOM   408   O  OG     . SER   A 1  54  ? -36.284 -100.072 52.472  1.00 68.45  ? 54  SER   A OG     1 
ATOM   409   N  N      . GLU   A 1  55  ? -35.387 -103.529 53.478  1.00 65.12  ? 55  GLU   A N      1 
ATOM   410   C  CA     . GLU   A 1  55  ? -34.871 -104.675 52.753  1.00 71.21  ? 55  GLU   A CA     1 
ATOM   411   C  C      . GLU   A 1  55  ? -35.831 -105.012 51.617  1.00 73.37  ? 55  GLU   A C      1 
ATOM   412   O  O      . GLU   A 1  55  ? -37.039 -104.761 51.702  1.00 75.69  ? 55  GLU   A O      1 
ATOM   413   C  CB     . GLU   A 1  55  ? -34.662 -105.873 53.697  1.00 72.09  ? 55  GLU   A CB     1 
ATOM   414   C  CG     . GLU   A 1  55  ? -33.982 -105.526 55.047  1.00 70.89  ? 55  GLU   A CG     1 
ATOM   415   C  CD     . GLU   A 1  55  ? -33.722 -106.751 55.907  1.00 75.69  ? 55  GLU   A CD     1 
ATOM   416   O  OE1    . GLU   A 1  55  ? -33.686 -107.854 55.335  1.00 78.17  ? 55  GLU   A OE1    1 
ATOM   417   O  OE2    . GLU   A 1  55  ? -33.546 -106.640 57.145  1.00 77.58  ? 55  GLU   A OE2    1 
ATOM   418   N  N      . THR   A 1  56  ? -35.286 -105.539 50.530  1.00 68.70  ? 56  THR   A N      1 
ATOM   419   C  CA     . THR   A 1  56  ? -36.082 -105.815 49.350  1.00 73.26  ? 56  THR   A CA     1 
ATOM   420   C  C      . THR   A 1  56  ? -36.247 -107.314 49.171  1.00 75.66  ? 56  THR   A C      1 
ATOM   421   O  O      . THR   A 1  56  ? -35.346 -108.092 49.490  1.00 72.67  ? 56  THR   A O      1 
ATOM   422   C  CB     . THR   A 1  56  ? -35.434 -105.236 48.106  1.00 73.23  ? 56  THR   A CB     1 
ATOM   423   O  OG1    . THR   A 1  56  ? -34.217 -105.942 47.842  1.00 72.49  ? 56  THR   A OG1    1 
ATOM   424   C  CG2    . THR   A 1  56  ? -35.115 -103.788 48.334  1.00 69.03  ? 56  THR   A CG2    1 
ATOM   425   N  N      . GLY   A 1  57  ? -37.402 -107.706 48.630  1.00 77.17  ? 57  GLY   A N      1 
ATOM   426   C  CA     . GLY   A 1  57  ? -37.678 -109.102 48.364  1.00 73.34  ? 57  GLY   A CA     1 
ATOM   427   C  C      . GLY   A 1  57  ? -36.443 -109.830 47.876  1.00 75.57  ? 57  GLY   A C      1 
ATOM   428   O  O      . GLY   A 1  57  ? -36.219 -110.997 48.208  1.00 75.62  ? 57  GLY   A O      1 
ATOM   429   N  N      . ALA   A 1  58  ? -35.619 -109.138 47.092  1.00 76.50  ? 58  ALA   A N      1 
ATOM   430   C  CA     . ALA   A 1  58  ? -34.373 -109.692 46.589  1.00 71.33  ? 58  ALA   A CA     1 
ATOM   431   C  C      . ALA   A 1  58  ? -33.208 -109.434 47.525  1.00 76.66  ? 58  ALA   A C      1 
ATOM   432   O  O      . ALA   A 1  58  ? -32.049 -109.600 47.125  1.00 75.54  ? 58  ALA   A O      1 
ATOM   433   C  CB     . ALA   A 1  58  ? -34.069 -109.133 45.200  1.00 74.51  ? 58  ALA   A CB     1 
ATOM   434   N  N      . GLY   A 1  59  ? -33.486 -109.007 48.753  1.00 74.60  ? 59  GLY   A N      1 
ATOM   435   C  CA     . GLY   A 1  59  ? -32.461 -108.947 49.772  1.00 75.47  ? 59  GLY   A CA     1 
ATOM   436   C  C      . GLY   A 1  59  ? -31.562 -107.736 49.734  1.00 75.23  ? 59  GLY   A C      1 
ATOM   437   O  O      . GLY   A 1  59  ? -30.508 -107.743 50.386  1.00 74.04  ? 59  GLY   A O      1 
ATOM   438   N  N      . LYS   A 1  60  ? -31.932 -106.700 48.993  1.00 78.25  ? 60  LYS   A N      1 
ATOM   439   C  CA     . LYS   A 1  60  ? -31.161 -105.469 49.016  1.00 72.67  ? 60  LYS   A CA     1 
ATOM   440   C  C      . LYS   A 1  60  ? -31.528 -104.643 50.236  1.00 67.03  ? 60  LYS   A C      1 
ATOM   441   O  O      . LYS   A 1  60  ? -32.668 -104.675 50.715  1.00 64.47  ? 60  LYS   A O      1 
ATOM   442   C  CB     . LYS   A 1  60  ? -31.374 -104.656 47.736  1.00 69.04  ? 60  LYS   A CB     1 
ATOM   443   C  CG     . LYS   A 1  60  ? -30.918 -103.220 47.916  1.00 74.61  ? 60  LYS   A CG     1 
ATOM   444   C  CD     . LYS   A 1  60  ? -31.273 -102.283 46.777  1.00 66.40  ? 60  LYS   A CD     1 
ATOM   445   C  CE     . LYS   A 1  60  ? -30.394 -102.541 45.581  1.00 60.60  ? 60  LYS   A CE     1 
ATOM   446   N  NZ     . LYS   A 1  60  ? -30.624 -101.489 44.585  1.00 64.38  ? 60  LYS   A NZ     1 
ATOM   447   N  N      . HIS   A 1  61  ? -30.538 -103.923 50.755  1.00 65.44  ? 61  HIS   A N      1 
ATOM   448   C  CA     . HIS   A 1  61  ? -30.743 -103.031 51.887  1.00 67.54  ? 61  HIS   A CA     1 
ATOM   449   C  C      . HIS   A 1  61  ? -30.595 -101.604 51.382  1.00 65.35  ? 61  HIS   A C      1 
ATOM   450   O  O      . HIS   A 1  61  ? -29.530 -101.226 50.881  1.00 67.54  ? 61  HIS   A O      1 
ATOM   451   C  CB     . HIS   A 1  61  ? -29.749 -103.317 53.013  1.00 65.33  ? 61  HIS   A CB     1 
ATOM   452   C  CG     . HIS   A 1  61  ? -29.839 -104.709 53.548  1.00 68.62  ? 61  HIS   A CG     1 
ATOM   453   N  ND1    . HIS   A 1  61  ? -29.534 -105.819 52.789  1.00 73.14  ? 61  HIS   A ND1    1 
ATOM   454   C  CD2    . HIS   A 1  61  ? -30.325 -105.180 54.721  1.00 70.36  ? 61  HIS   A CD2    1 
ATOM   455   C  CE1    . HIS   A 1  61  ? -29.753 -106.910 53.500  1.00 74.53  ? 61  HIS   A CE1    1 
ATOM   456   N  NE2    . HIS   A 1  61  ? -30.240 -106.550 54.674  1.00 73.95  ? 61  HIS   A NE2    1 
ATOM   457   N  N      . VAL   A 1  62  ? -31.656 -100.820 51.511  1.00 58.50  ? 62  VAL   A N      1 
ATOM   458   C  CA     . VAL   A 1  62  ? -31.805 -99.575  50.771  1.00 62.03  ? 62  VAL   A CA     1 
ATOM   459   C  C      . VAL   A 1  62  ? -31.954 -98.421  51.752  1.00 61.11  ? 62  VAL   A C      1 
ATOM   460   O  O      . VAL   A 1  62  ? -32.961 -98.342  52.463  1.00 61.08  ? 62  VAL   A O      1 
ATOM   461   C  CB     . VAL   A 1  62  ? -33.006 -99.618  49.810  1.00 62.97  ? 62  VAL   A CB     1 
ATOM   462   C  CG1    . VAL   A 1  62  ? -33.003 -98.401  48.883  1.00 61.79  ? 62  VAL   A CG1    1 
ATOM   463   C  CG2    . VAL   A 1  62  ? -32.972 -100.883 48.991  1.00 63.98  ? 62  VAL   A CG2    1 
ATOM   464   N  N      . PRO   A 1  63  ? -31.015 -97.482  51.785  1.00 58.39  ? 63  PRO   A N      1 
ATOM   465   C  CA     . PRO   A 1  63  ? -31.178 -96.279  52.613  1.00 56.57  ? 63  PRO   A CA     1 
ATOM   466   C  C      . PRO   A 1  63  ? -32.601 -95.755  52.717  1.00 57.35  ? 63  PRO   A C      1 
ATOM   467   O  O      . PRO   A 1  63  ? -33.279 -95.634  51.701  1.00 57.73  ? 63  PRO   A O      1 
ATOM   468   C  CB     . PRO   A 1  63  ? -30.274 -95.264  51.906  1.00 54.83  ? 63  PRO   A CB     1 
ATOM   469   C  CG     . PRO   A 1  63  ? -29.199 -96.117  51.261  1.00 57.56  ? 63  PRO   A CG     1 
ATOM   470   C  CD     . PRO   A 1  63  ? -29.858 -97.393  50.873  1.00 59.93  ? 63  PRO   A CD     1 
ATOM   471   N  N      . ARG   A 1  64  ? -33.077 -95.467  53.933  1.00 60.05  ? 64  ARG   A N      1 
ATOM   472   C  CA     . ARG   A 1  64  ? -34.286 -94.667  54.095  1.00 56.34  ? 64  ARG   A CA     1 
ATOM   473   C  C      . ARG   A 1  64  ? -33.892 -93.213  53.908  1.00 57.93  ? 64  ARG   A C      1 
ATOM   474   O  O      . ARG   A 1  64  ? -34.173 -92.354  54.758  1.00 57.97  ? 64  ARG   A O      1 
ATOM   475   C  CB     . ARG   A 1  64  ? -34.950 -94.897  55.455  1.00 61.12  ? 64  ARG   A CB     1 
ATOM   476   C  CG     . ARG   A 1  64  ? -35.346 -96.352  55.706  1.00 61.25  ? 64  ARG   A CG     1 
ATOM   477   C  CD     . ARG   A 1  64  ? -36.062 -96.549  57.045  1.00 62.64  ? 64  ARG   A CD     1 
ATOM   478   N  NE     . ARG   A 1  64  ? -36.160 -97.975  57.288  1.00 58.43  ? 64  ARG   A NE     1 
ATOM   479   C  CZ     . ARG   A 1  64  ? -37.132 -98.735  56.819  1.00 58.39  ? 64  ARG   A CZ     1 
ATOM   480   N  NH1    . ARG   A 1  64  ? -38.176 -98.216  56.196  1.00 62.09  ? 64  ARG   A NH1    1 
ATOM   481   N  NH2    . ARG   A 1  64  ? -37.035 -100.051 56.942  1.00 64.37  ? 64  ARG   A NH2    1 
ATOM   482   N  N      . ALA   A 1  65  ? -33.239 -92.948  52.782  1.00 52.73  ? 65  ALA   A N      1 
ATOM   483   C  CA     . ALA   A 1  65  ? -32.717 -91.643  52.445  1.00 54.99  ? 65  ALA   A CA     1 
ATOM   484   C  C      . ALA   A 1  65  ? -33.442 -91.079  51.234  1.00 60.68  ? 65  ALA   A C      1 
ATOM   485   O  O      . ALA   A 1  65  ? -33.932 -91.824  50.372  1.00 55.96  ? 65  ALA   A O      1 
ATOM   486   C  CB     . ALA   A 1  65  ? -31.221 -91.722  52.142  1.00 56.30  ? 65  ALA   A CB     1 
ATOM   487   N  N      . VAL   A 1  66  ? -33.511 -89.749  51.197  1.00 57.91  ? 66  VAL   A N      1 
ATOM   488   C  CA     . VAL   A 1  66  ? -33.820 -88.981  50.000  1.00 53.35  ? 66  VAL   A CA     1 
ATOM   489   C  C      . VAL   A 1  66  ? -32.834 -87.828  49.919  1.00 51.91  ? 66  VAL   A C      1 
ATOM   490   O  O      . VAL   A 1  66  ? -32.517 -87.196  50.931  1.00 54.52  ? 66  VAL   A O      1 
ATOM   491   C  CB     . VAL   A 1  66  ? -35.261 -88.440  50.000  1.00 50.25  ? 66  VAL   A CB     1 
ATOM   492   C  CG1    . VAL   A 1  66  ? -35.399 -87.333  50.993  1.00 47.42  ? 66  VAL   A CG1    1 
ATOM   493   C  CG2    . VAL   A 1  66  ? -35.590 -87.913  48.639  1.00 57.72  ? 66  VAL   A CG2    1 
ATOM   494   N  N      . PHE   A 1  67  ? -32.359 -87.550  48.714  1.00 53.07  ? 67  PHE   A N      1 
ATOM   495   C  CA     . PHE   A 1  67  ? -31.439 -86.455  48.440  1.00 47.22  ? 67  PHE   A CA     1 
ATOM   496   C  C      . PHE   A 1  67  ? -32.179 -85.478  47.536  1.00 47.57  ? 67  PHE   A C      1 
ATOM   497   O  O      . PHE   A 1  67  ? -32.791 -85.889  46.557  1.00 53.98  ? 67  PHE   A O      1 
ATOM   498   C  CB     . PHE   A 1  67  ? -30.185 -86.975  47.745  1.00 45.79  ? 67  PHE   A CB     1 
ATOM   499   C  CG     . PHE   A 1  67  ? -29.325 -87.856  48.595  1.00 49.58  ? 67  PHE   A CG     1 
ATOM   500   C  CD1    . PHE   A 1  67  ? -29.847 -88.990  49.178  1.00 58.97  ? 67  PHE   A CD1    1 
ATOM   501   C  CD2    . PHE   A 1  67  ? -27.976 -87.634  48.701  1.00 53.28  ? 67  PHE   A CD2    1 
ATOM   502   C  CE1    . PHE   A 1  67  ? -29.063 -89.825  49.935  1.00 54.49  ? 67  PHE   A CE1    1 
ATOM   503   C  CE2    . PHE   A 1  67  ? -27.183 -88.479  49.445  1.00 51.01  ? 67  PHE   A CE2    1 
ATOM   504   C  CZ     . PHE   A 1  67  ? -27.732 -89.572  50.056  1.00 52.97  ? 67  PHE   A CZ     1 
ATOM   505   N  N      . VAL   A 1  68  ? -32.167 -84.204  47.875  1.00 43.48  ? 68  VAL   A N      1 
ATOM   506   C  CA     . VAL   A 1  68  ? -32.846 -83.182  47.102  1.00 41.44  ? 68  VAL   A CA     1 
ATOM   507   C  C      . VAL   A 1  68  ? -31.828 -82.090  46.819  1.00 51.92  ? 68  VAL   A C      1 
ATOM   508   O  O      . VAL   A 1  68  ? -31.207 -81.565  47.749  1.00 57.23  ? 68  VAL   A O      1 
ATOM   509   C  CB     . VAL   A 1  68  ? -34.052 -82.610  47.860  1.00 43.09  ? 68  VAL   A CB     1 
ATOM   510   C  CG1    . VAL   A 1  68  ? -33.613 -82.129  49.191  1.00 51.75  ? 68  VAL   A CG1    1 
ATOM   511   C  CG2    . VAL   A 1  68  ? -34.620 -81.423  47.146  1.00 51.81  ? 68  VAL   A CG2    1 
ATOM   512   N  N      . ASP   A 1  69  ? -31.635 -81.754  45.551  1.00 52.66  ? 69  ASP   A N      1 
ATOM   513   C  CA     . ASP   A 1  69  ? -30.822 -80.589  45.233  1.00 50.66  ? 69  ASP   A CA     1 
ATOM   514   C  C      . ASP   A 1  69  ? -31.466 -79.849  44.078  1.00 53.12  ? 69  ASP   A C      1 
ATOM   515   O  O      . ASP   A 1  69  ? -31.800 -80.460  43.055  1.00 55.25  ? 69  ASP   A O      1 
ATOM   516   C  CB     . ASP   A 1  69  ? -29.382 -80.954  44.855  1.00 49.32  ? 69  ASP   A CB     1 
ATOM   517   C  CG     . ASP   A 1  69  ? -28.469 -79.735  44.845  1.00 57.10  ? 69  ASP   A CG     1 
ATOM   518   O  OD1    . ASP   A 1  69  ? -28.982 -78.646  45.227  1.00 51.62  ? 69  ASP   A OD1    1 
ATOM   519   O  OD2    . ASP   A 1  69  ? -27.278 -79.851  44.428  1.00 60.16  ? 69  ASP   A OD2    1 
ATOM   520   N  N      . LEU   A 1  70  ? -31.591 -78.532  44.226  1.00 48.50  ? 70  LEU   A N      1 
ATOM   521   C  CA     . LEU   A 1  70  ? -32.108 -77.680  43.162  1.00 47.14  ? 70  LEU   A CA     1 
ATOM   522   C  C      . LEU   A 1  70  ? -31.257 -77.715  41.892  1.00 49.21  ? 70  LEU   A C      1 
ATOM   523   O  O      . LEU   A 1  70  ? -31.541 -76.968  40.955  1.00 55.55  ? 70  LEU   A O      1 
ATOM   524   C  CB     . LEU   A 1  70  ? -32.208 -76.238  43.655  1.00 42.89  ? 70  LEU   A CB     1 
ATOM   525   C  CG     . LEU   A 1  70  ? -33.238 -76.193  44.769  1.00 36.13  ? 70  LEU   A CG     1 
ATOM   526   C  CD1    . LEU   A 1  70  ? -33.660 -74.782  45.166  1.00 33.60  ? 70  LEU   A CD1    1 
ATOM   527   C  CD2    . LEU   A 1  70  ? -34.403 -77.058  44.355  1.00 43.87  ? 70  LEU   A CD2    1 
ATOM   528   N  N      . GLU   A 1  71  ? -30.219 -78.558  41.833  1.00 44.75  ? 71  GLU   A N      1 
ATOM   529   C  CA     . GLU   A 1  71  ? -29.263 -78.512  40.740  1.00 48.34  ? 71  GLU   A CA     1 
ATOM   530   C  C      . GLU   A 1  71  ? -28.653 -79.883  40.498  1.00 56.67  ? 71  GLU   A C      1 
ATOM   531   O  O      . GLU   A 1  71  ? -28.211 -80.540  41.456  1.00 58.04  ? 71  GLU   A O      1 
ATOM   532   C  CB     . GLU   A 1  71  ? -28.140 -77.520  41.024  1.00 48.77  ? 71  GLU   A CB     1 
ATOM   533   C  CG     . GLU   A 1  71  ? -26.867 -77.885  40.314  1.00 51.30  ? 71  GLU   A CG     1 
ATOM   534   C  CD     . GLU   A 1  71  ? -25.654 -77.418  41.075  1.00 62.89  ? 71  GLU   A CD     1 
ATOM   535   O  OE1    . GLU   A 1  71  ? -25.810 -76.681  42.090  1.00 68.11  ? 71  GLU   A OE1    1 
ATOM   536   O  OE2    . GLU   A 1  71  ? -24.540 -77.824  40.669  1.00 64.93  ? 71  GLU   A OE2    1 
ATOM   537   N  N      . PRO   A 1  72  ? -28.572 -80.317  39.237  1.00 52.55  ? 72  PRO   A N      1 
ATOM   538   C  CA     . PRO   A 1  72  ? -28.283 -81.723  38.947  1.00 48.60  ? 72  PRO   A CA     1 
ATOM   539   C  C      . PRO   A 1  72  ? -26.861 -82.163  39.168  1.00 56.85  ? 72  PRO   A C      1 
ATOM   540   O  O      . PRO   A 1  72  ? -26.605 -83.372  39.105  1.00 58.83  ? 72  PRO   A O      1 
ATOM   541   C  CB     . PRO   A 1  72  ? -28.641 -81.833  37.470  1.00 49.37  ? 72  PRO   A CB     1 
ATOM   542   C  CG     . PRO   A 1  72  ? -28.312 -80.512  36.943  1.00 51.62  ? 72  PRO   A CG     1 
ATOM   543   C  CD     . PRO   A 1  72  ? -28.708 -79.531  38.005  1.00 50.63  ? 72  PRO   A CD     1 
ATOM   544   N  N      . THR   A 1  73  ? -25.926 -81.253  39.400  1.00 58.19  ? 73  THR   A N      1 
ATOM   545   C  CA     . THR   A 1  73  ? -24.524 -81.648  39.352  1.00 58.58  ? 73  THR   A CA     1 
ATOM   546   C  C      . THR   A 1  73  ? -24.193 -82.667  40.438  1.00 60.78  ? 73  THR   A C      1 
ATOM   547   O  O      . THR   A 1  73  ? -23.621 -83.728  40.158  1.00 61.09  ? 73  THR   A O      1 
ATOM   548   C  CB     . THR   A 1  73  ? -23.647 -80.420  39.512  1.00 58.32  ? 73  THR   A CB     1 
ATOM   549   O  OG1    . THR   A 1  73  ? -24.214 -79.374  38.737  1.00 63.19  ? 73  THR   A OG1    1 
ATOM   550   C  CG2    . THR   A 1  73  ? -22.260 -80.709  39.004  1.00 62.39  ? 73  THR   A CG2    1 
ATOM   551   N  N      . VAL   A 1  74  ? -24.534 -82.354  41.693  1.00 59.01  ? 74  VAL   A N      1 
ATOM   552   C  CA     . VAL   A 1  74  ? -23.992 -83.114  42.809  1.00 52.06  ? 74  VAL   A CA     1 
ATOM   553   C  C      . VAL   A 1  74  ? -24.702 -84.451  42.920  1.00 54.87  ? 74  VAL   A C      1 
ATOM   554   O  O      . VAL   A 1  74  ? -24.069 -85.503  43.047  1.00 51.43  ? 74  VAL   A O      1 
ATOM   555   C  CB     . VAL   A 1  74  ? -24.089 -82.305  44.114  1.00 54.37  ? 74  VAL   A CB     1 
ATOM   556   C  CG1    . VAL   A 1  74  ? -23.302 -82.996  45.204  1.00 51.84  ? 74  VAL   A CG1    1 
ATOM   557   C  CG2    . VAL   A 1  74  ? -23.565 -80.893  43.921  1.00 48.85  ? 74  VAL   A CG2    1 
ATOM   558   N  N      . ILE   A 1  75  ? -26.032 -84.437  42.846  1.00 54.99  ? 75  ILE   A N      1 
ATOM   559   C  CA     . ILE   A 1  75  ? -26.751 -85.694  42.959  1.00 52.18  ? 75  ILE   A CA     1 
ATOM   560   C  C      . ILE   A 1  75  ? -26.471 -86.599  41.764  1.00 52.33  ? 75  ILE   A C      1 
ATOM   561   O  O      . ILE   A 1  75  ? -26.729 -87.806  41.831  1.00 57.86  ? 75  ILE   A O      1 
ATOM   562   C  CB     . ILE   A 1  75  ? -28.250 -85.400  43.169  1.00 50.74  ? 75  ILE   A CB     1 
ATOM   563   C  CG1    . ILE   A 1  75  ? -28.475 -84.958  44.612  1.00 45.78  ? 75  ILE   A CG1    1 
ATOM   564   C  CG2    . ILE   A 1  75  ? -29.093 -86.635  42.915  1.00 50.31  ? 75  ILE   A CG2    1 
ATOM   565   C  CD1    . ILE   A 1  75  ? -29.834 -84.406  44.885  1.00 45.69  ? 75  ILE   A CD1    1 
ATOM   566   N  N      . ASP   A 1  76  ? -25.920 -86.057  40.676  1.00 53.71  ? 76  ASP   A N      1 
ATOM   567   C  CA     . ASP   A 1  76  ? -25.529 -86.889  39.542  1.00 54.79  ? 76  ASP   A CA     1 
ATOM   568   C  C      . ASP   A 1  76  ? -24.334 -87.761  39.883  1.00 62.94  ? 76  ASP   A C      1 
ATOM   569   O  O      . ASP   A 1  76  ? -24.252 -88.912  39.436  1.00 67.03  ? 76  ASP   A O      1 
ATOM   570   C  CB     . ASP   A 1  76  ? -25.212 -86.022  38.326  1.00 57.69  ? 76  ASP   A CB     1 
ATOM   571   C  CG     . ASP   A 1  76  ? -26.434 -85.751  37.470  1.00 62.19  ? 76  ASP   A CG     1 
ATOM   572   O  OD1    . ASP   A 1  76  ? -27.417 -86.516  37.588  1.00 67.21  ? 76  ASP   A OD1    1 
ATOM   573   O  OD2    . ASP   A 1  76  ? -26.418 -84.770  36.695  1.00 54.61  ? 76  ASP   A OD2    1 
ATOM   574   N  N      . GLU   A 1  77  ? -23.396 -87.241  40.675  1.00 64.95  ? 77  GLU   A N      1 
ATOM   575   C  CA     . GLU   A 1  77  ? -22.311 -88.101  41.133  1.00 65.58  ? 77  GLU   A CA     1 
ATOM   576   C  C      . GLU   A 1  77  ? -22.811 -89.163  42.096  1.00 62.88  ? 77  GLU   A C      1 
ATOM   577   O  O      . GLU   A 1  77  ? -22.295 -90.286  42.089  1.00 70.44  ? 77  GLU   A O      1 
ATOM   578   C  CB     . GLU   A 1  77  ? -21.204 -87.264  41.750  1.00 66.50  ? 77  GLU   A CB     1 
ATOM   579   C  CG     . GLU   A 1  77  ? -20.643 -86.306  40.727  1.00 71.61  ? 77  GLU   A CG     1 
ATOM   580   C  CD     . GLU   A 1  77  ? -19.256 -85.837  41.059  1.00 81.64  ? 77  GLU   A CD     1 
ATOM   581   O  OE1    . GLU   A 1  77  ? -19.118 -84.872  41.849  1.00 73.66  ? 77  GLU   A OE1    1 
ATOM   582   O  OE2    . GLU   A 1  77  ? -18.303 -86.451  40.520  1.00 98.41  ? 77  GLU   A OE2    1 
ATOM   583   N  N      . VAL   A 1  78  ? -23.826 -88.848  42.907  1.00 59.24  ? 78  VAL   A N      1 
ATOM   584   C  CA     . VAL   A 1  78  ? -24.566 -89.915  43.572  1.00 59.55  ? 78  VAL   A CA     1 
ATOM   585   C  C      . VAL   A 1  78  ? -25.119 -90.886  42.535  1.00 64.79  ? 78  VAL   A C      1 
ATOM   586   O  O      . VAL   A 1  78  ? -24.868 -92.094  42.609  1.00 74.34  ? 78  VAL   A O      1 
ATOM   587   C  CB     . VAL   A 1  78  ? -25.672 -89.348  44.481  1.00 61.88  ? 78  VAL   A CB     1 
ATOM   588   C  CG1    . VAL   A 1  78  ? -26.399 -90.481  45.209  1.00 64.14  ? 78  VAL   A CG1    1 
ATOM   589   C  CG2    . VAL   A 1  78  ? -25.083 -88.408  45.514  1.00 54.88  ? 78  VAL   A CG2    1 
ATOM   590   N  N      . ARG   A 1  79  ? -25.838 -90.375  41.524  1.00 58.12  ? 79  ARG   A N      1 
ATOM   591   C  CA     . ARG   A 1  79  ? -26.412 -91.252  40.501  1.00 59.22  ? 79  ARG   A CA     1 
ATOM   592   C  C      . ARG   A 1  79  ? -25.389 -92.110  39.766  1.00 62.55  ? 79  ARG   A C      1 
ATOM   593   O  O      . ARG   A 1  79  ? -25.786 -93.008  39.015  1.00 65.72  ? 79  ARG   A O      1 
ATOM   594   C  CB     . ARG   A 1  79  ? -27.179 -90.439  39.476  1.00 53.21  ? 79  ARG   A CB     1 
ATOM   595   C  CG     . ARG   A 1  79  ? -28.468 -89.932  39.971  1.00 52.16  ? 79  ARG   A CG     1 
ATOM   596   C  CD     . ARG   A 1  79  ? -28.964 -88.854  39.069  1.00 53.31  ? 79  ARG   A CD     1 
ATOM   597   N  NE     . ARG   A 1  79  ? -30.270 -88.397  39.515  1.00 56.33  ? 79  ARG   A NE     1 
ATOM   598   C  CZ     . ARG   A 1  79  ? -30.660 -87.132  39.519  1.00 54.65  ? 79  ARG   A CZ     1 
ATOM   599   N  NH1    . ARG   A 1  79  ? -29.841 -86.153  39.170  1.00 56.17  ? 79  ARG   A NH1    1 
ATOM   600   N  NH2    . ARG   A 1  79  ? -31.905 -86.841  39.880  1.00 52.53  ? 79  ARG   A NH2    1 
ATOM   601   N  N      . THR   A 1  80  ? -24.100 -91.861  39.939  1.00 60.01  ? 80  THR   A N      1 
ATOM   602   C  CA     . THR   A 1  80  ? -23.105 -92.584  39.165  1.00 61.42  ? 80  THR   A CA     1 
ATOM   603   C  C      . THR   A 1  80  ? -21.931 -93.052  40.010  1.00 67.84  ? 80  THR   A C      1 
ATOM   604   O  O      . THR   A 1  80  ? -20.939 -93.531  39.447  1.00 73.67  ? 80  THR   A O      1 
ATOM   605   C  CB     . THR   A 1  80  ? -22.611 -91.701  38.020  1.00 68.68  ? 80  THR   A CB     1 
ATOM   606   O  OG1    . THR   A 1  80  ? -21.928 -90.555  38.555  1.00 69.15  ? 80  THR   A OG1    1 
ATOM   607   C  CG2    . THR   A 1  80  ? -23.785 -91.249  37.142  1.00 64.26  ? 80  THR   A CG2    1 
ATOM   608   N  N      . GLY   A 1  81  ? -22.011 -92.933  41.337  1.00 66.92  ? 81  GLY   A N      1 
ATOM   609   C  CA     . GLY   A 1  81  ? -20.922 -93.331  42.201  1.00 66.79  ? 81  GLY   A CA     1 
ATOM   610   C  C      . GLY   A 1  81  ? -20.996 -94.784  42.627  1.00 65.43  ? 81  GLY   A C      1 
ATOM   611   O  O      . GLY   A 1  81  ? -21.985 -95.481  42.402  1.00 64.74  ? 81  GLY   A O      1 
ATOM   612   N  N      . THR   A 1  82  ? -19.917 -95.226  43.274  1.00 58.18  ? 82  THR   A N      1 
ATOM   613   C  CA     . THR   A 1  82  ? -19.773 -96.622  43.666  1.00 69.46  ? 82  THR   A CA     1 
ATOM   614   C  C      . THR   A 1  82  ? -21.050 -97.145  44.331  1.00 69.71  ? 82  THR   A C      1 
ATOM   615   O  O      . THR   A 1  82  ? -21.367 -98.341  44.245  1.00 63.03  ? 82  THR   A O      1 
ATOM   616   C  CB     . THR   A 1  82  ? -18.567 -96.781  44.592  1.00 63.23  ? 82  THR   A CB     1 
ATOM   617   O  OG1    . THR   A 1  82  ? -18.929 -96.367  45.908  1.00 78.81  ? 82  THR   A OG1    1 
ATOM   618   C  CG2    . THR   A 1  82  ? -17.449 -95.880  44.143  1.00 51.28  ? 82  THR   A CG2    1 
ATOM   619   N  N      . TYR   A 1  83  ? -21.802 -96.247  44.974  1.00 63.48  ? 83  TYR   A N      1 
ATOM   620   C  CA     . TYR   A 1  83  ? -23.032 -96.606  45.663  1.00 64.31  ? 83  TYR   A CA     1 
ATOM   621   C  C      . TYR   A 1  83  ? -24.268 -96.235  44.868  1.00 63.67  ? 83  TYR   A C      1 
ATOM   622   O  O      . TYR   A 1  83  ? -25.335 -96.003  45.444  1.00 63.19  ? 83  TYR   A O      1 
ATOM   623   C  CB     . TYR   A 1  83  ? -23.056 -95.968  47.049  1.00 63.70  ? 83  TYR   A CB     1 
ATOM   624   C  CG     . TYR   A 1  83  ? -22.035 -96.580  47.960  1.00 60.97  ? 83  TYR   A CG     1 
ATOM   625   C  CD1    . TYR   A 1  83  ? -22.335 -97.697  48.729  1.00 64.97  ? 83  TYR   A CD1    1 
ATOM   626   C  CD2    . TYR   A 1  83  ? -20.750 -96.092  47.984  1.00 58.77  ? 83  TYR   A CD2    1 
ATOM   627   C  CE1    . TYR   A 1  83  ? -21.373 -98.270  49.549  1.00 69.96  ? 83  TYR   A CE1    1 
ATOM   628   C  CE2    . TYR   A 1  83  ? -19.783 -96.646  48.782  1.00 63.01  ? 83  TYR   A CE2    1 
ATOM   629   C  CZ     . TYR   A 1  83  ? -20.079 -97.732  49.571  1.00 72.00  ? 83  TYR   A CZ     1 
ATOM   630   O  OH     . TYR   A 1  83  ? -19.061 -98.261  50.371  1.00 66.72  ? 83  TYR   A OH     1 
ATOM   631   N  N      . ARG   A 1  84  ? -24.151 -96.195  43.546  1.00 63.45  ? 84  ARG   A N      1 
ATOM   632   C  CA     . ARG   A 1  84  ? -25.344 -96.029  42.725  1.00 70.79  ? 84  ARG   A CA     1 
ATOM   633   C  C      . ARG   A 1  84  ? -26.393 -97.088  43.057  1.00 72.11  ? 84  ARG   A C      1 
ATOM   634   O  O      . ARG   A 1  84  ? -27.519 -96.758  43.444  1.00 74.92  ? 84  ARG   A O      1 
ATOM   635   C  CB     . ARG   A 1  84  ? -24.975 -96.040  41.238  1.00 65.37  ? 84  ARG   A CB     1 
ATOM   636   C  CG     . ARG   A 1  84  ? -24.138 -97.213  40.818  1.00 74.38  ? 84  ARG   A CG     1 
ATOM   637   C  CD     . ARG   A 1  84  ? -23.691 -97.109  39.380  1.00 77.69  ? 84  ARG   A CD     1 
ATOM   638   N  NE     . ARG   A 1  84  ? -23.126 -98.381  38.951  1.00 92.67  ? 84  ARG   A NE     1 
ATOM   639   C  CZ     . ARG   A 1  84  ? -23.845 -99.383  38.464  1.00 105.52 ? 84  ARG   A CZ     1 
ATOM   640   N  NH1    . ARG   A 1  84  ? -25.161 -99.292  38.341  1.00 105.66 ? 84  ARG   A NH1    1 
ATOM   641   N  NH2    . ARG   A 1  84  ? -23.231 -100.508 38.100  1.00 102.37 ? 84  ARG   A NH2    1 
ATOM   642   N  N      . GLN   A 1  85  ? -26.036 -98.366  42.959  1.00 65.65  ? 85  GLN   A N      1 
ATOM   643   C  CA     . GLN   A 1  85  ? -27.036 -99.416  43.099  1.00 65.66  ? 85  GLN   A CA     1 
ATOM   644   C  C      . GLN   A 1  85  ? -27.741 -99.308  44.444  1.00 72.68  ? 85  GLN   A C      1 
ATOM   645   O  O      . GLN   A 1  85  ? -28.818 -99.882  44.652  1.00 76.72  ? 85  GLN   A O      1 
ATOM   646   C  CB     . GLN   A 1  85  ? -26.394 -100.791 42.939  1.00 79.17  ? 85  GLN   A CB     1 
ATOM   647   C  CG     . GLN   A 1  85  ? -25.593 -100.954 41.658  1.00 87.13  ? 85  GLN   A CG     1 
ATOM   648   C  CD     . GLN   A 1  85  ? -25.574 -102.387 41.181  1.00 94.87  ? 85  GLN   A CD     1 
ATOM   649   O  OE1    . GLN   A 1  85  ? -26.569 -103.102 41.315  1.00 97.30  ? 85  GLN   A OE1    1 
ATOM   650   N  NE2    . GLN   A 1  85  ? -24.445 -102.820 40.625  1.00 100.03 ? 85  GLN   A NE2    1 
ATOM   651   N  N      . LEU   A 1  86  ? -27.138 -98.550  45.355  1.00 68.60  ? 86  LEU   A N      1 
ATOM   652   C  CA     . LEU   A 1  86  ? -27.695 -98.405  46.691  1.00 67.20  ? 86  LEU   A CA     1 
ATOM   653   C  C      . LEU   A 1  86  ? -29.113 -97.837  46.655  1.00 65.18  ? 86  LEU   A C      1 
ATOM   654   O  O      . LEU   A 1  86  ? -30.041 -98.424  47.227  1.00 67.29  ? 86  LEU   A O      1 
ATOM   655   C  CB     . LEU   A 1  86  ? -26.768 -97.522  47.517  1.00 70.25  ? 86  LEU   A CB     1 
ATOM   656   C  CG     . LEU   A 1  86  ? -26.761 -97.881  48.989  1.00 71.89  ? 86  LEU   A CG     1 
ATOM   657   C  CD1    . LEU   A 1  86  ? -26.237 -99.311  49.141  1.00 68.98  ? 86  LEU   A CD1    1 
ATOM   658   C  CD2    . LEU   A 1  86  ? -25.897 -96.873  49.721  1.00 63.54  ? 86  LEU   A CD2    1 
ATOM   659   N  N      . PHE   A 1  87  ? -29.303 -96.707  45.974  1.00 66.41  ? 87  PHE   A N      1 
ATOM   660   C  CA     . PHE   A 1  87  ? -30.502 -95.882  46.086  1.00 66.85  ? 87  PHE   A CA     1 
ATOM   661   C  C      . PHE   A 1  87  ? -31.544 -96.143  45.000  1.00 68.10  ? 87  PHE   A C      1 
ATOM   662   O  O      . PHE   A 1  87  ? -31.226 -96.519  43.870  1.00 67.67  ? 87  PHE   A O      1 
ATOM   663   C  CB     . PHE   A 1  87  ? -30.103 -94.410  46.039  1.00 63.78  ? 87  PHE   A CB     1 
ATOM   664   C  CG     . PHE   A 1  87  ? -29.076 -94.026  47.062  1.00 65.00  ? 87  PHE   A CG     1 
ATOM   665   C  CD1    . PHE   A 1  87  ? -29.460 -93.687  48.348  1.00 64.07  ? 87  PHE   A CD1    1 
ATOM   666   C  CD2    . PHE   A 1  87  ? -27.728 -94.053  46.762  1.00 62.67  ? 87  PHE   A CD2    1 
ATOM   667   C  CE1    . PHE   A 1  87  ? -28.520 -93.331  49.297  1.00 61.10  ? 87  PHE   A CE1    1 
ATOM   668   C  CE2    . PHE   A 1  87  ? -26.786 -93.707  47.716  1.00 60.02  ? 87  PHE   A CE2    1 
ATOM   669   C  CZ     . PHE   A 1  87  ? -27.181 -93.348  48.980  1.00 56.95  ? 87  PHE   A CZ     1 
ATOM   670   N  N      . HIS   A 1  88  ? -32.798 -95.908  45.348  1.00 69.93  ? 88  HIS   A N      1 
ATOM   671   C  CA     . HIS   A 1  88  ? -33.825 -95.925  44.321  1.00 70.81  ? 88  HIS   A CA     1 
ATOM   672   C  C      . HIS   A 1  88  ? -33.837 -94.590  43.595  1.00 75.71  ? 88  HIS   A C      1 
ATOM   673   O  O      . HIS   A 1  88  ? -33.973 -93.539  44.236  1.00 73.99  ? 88  HIS   A O      1 
ATOM   674   C  CB     . HIS   A 1  88  ? -35.223 -96.201  44.883  1.00 76.10  ? 88  HIS   A CB     1 
ATOM   675   C  CG     . HIS   A 1  88  ? -36.266 -96.335  43.810  1.00 84.87  ? 88  HIS   A CG     1 
ATOM   676   N  ND1    . HIS   A 1  88  ? -36.404 -97.475  43.043  1.00 91.11  ? 88  HIS   A ND1    1 
ATOM   677   C  CD2    . HIS   A 1  88  ? -37.175 -95.452  43.331  1.00 84.04  ? 88  HIS   A CD2    1 
ATOM   678   C  CE1    . HIS   A 1  88  ? -37.370 -97.298  42.159  1.00 84.98  ? 88  HIS   A CE1    1 
ATOM   679   N  NE2    . HIS   A 1  88  ? -37.854 -96.078  42.313  1.00 87.26  ? 88  HIS   A NE2    1 
ATOM   680   N  N      . PRO   A 1  89  ? -33.698 -94.591  42.287  1.00 75.07  ? 89  PRO   A N      1 
ATOM   681   C  CA     . PRO   A 1  89  ? -33.812 -93.343  41.530  1.00 71.47  ? 89  PRO   A CA     1 
ATOM   682   C  C      . PRO   A 1  89  ? -34.824 -92.348  42.079  1.00 66.45  ? 89  PRO   A C      1 
ATOM   683   O  O      . PRO   A 1  89  ? -34.475 -91.171  42.166  1.00 67.25  ? 89  PRO   A O      1 
ATOM   684   C  CB     . PRO   A 1  89  ? -34.174 -93.838  40.131  1.00 72.99  ? 89  PRO   A CB     1 
ATOM   685   C  CG     . PRO   A 1  89  ? -33.433 -95.146  40.051  1.00 74.90  ? 89  PRO   A CG     1 
ATOM   686   C  CD     . PRO   A 1  89  ? -33.465 -95.754  41.418  1.00 72.42  ? 89  PRO   A CD     1 
ATOM   687   N  N      . GLU   A 1  90  ? -36.036 -92.753  42.475  1.00 67.18  ? 90  GLU   A N      1 
ATOM   688   C  CA     . GLU   A 1  90  ? -36.971 -91.752  42.992  1.00 69.32  ? 90  GLU   A CA     1 
ATOM   689   C  C      . GLU   A 1  90  ? -36.421 -91.023  44.205  1.00 70.40  ? 90  GLU   A C      1 
ATOM   690   O  O      . GLU   A 1  90  ? -36.937 -89.958  44.564  1.00 72.24  ? 90  GLU   A O      1 
ATOM   691   C  CB     . GLU   A 1  90  ? -38.319 -92.354  43.389  1.00 75.60  ? 90  GLU   A CB     1 
ATOM   692   C  CG     . GLU   A 1  90  ? -39.058 -93.176  42.350  1.00 88.36  ? 90  GLU   A CG     1 
ATOM   693   C  CD     . GLU   A 1  90  ? -40.477 -93.506  42.805  1.00 97.47  ? 90  GLU   A CD     1 
ATOM   694   O  OE1    . GLU   A 1  90  ? -40.635 -93.963  43.962  1.00 94.58  ? 90  GLU   A OE1    1 
ATOM   695   O  OE2    . GLU   A 1  90  ? -41.428 -93.290  42.012  1.00 98.57  ? 90  GLU   A OE2    1 
ATOM   696   N  N      . GLN   A 1  91  ? -35.395 -91.579  44.846  1.00 66.52  ? 91  GLN   A N      1 
ATOM   697   C  CA     . GLN   A 1  91  ? -34.843 -91.019  46.070  1.00 65.15  ? 91  GLN   A CA     1 
ATOM   698   C  C      . GLN   A 1  91  ? -33.981 -89.792  45.822  1.00 64.25  ? 91  GLN   A C      1 
ATOM   699   O  O      . GLN   A 1  91  ? -33.755 -89.008  46.752  1.00 56.38  ? 91  GLN   A O      1 
ATOM   700   C  CB     . GLN   A 1  91  ? -33.954 -92.044  46.758  1.00 74.10  ? 91  GLN   A CB     1 
ATOM   701   C  CG     . GLN   A 1  91  ? -34.640 -93.202  47.448  1.00 73.33  ? 91  GLN   A CG     1 
ATOM   702   C  CD     . GLN   A 1  91  ? -33.608 -94.219  47.901  1.00 70.83  ? 91  GLN   A CD     1 
ATOM   703   O  OE1    . GLN   A 1  91  ? -33.181 -95.078  47.131  1.00 67.85  ? 91  GLN   A OE1    1 
ATOM   704   N  NE2    . GLN   A 1  91  ? -33.184 -94.106  49.162  1.00 70.05  ? 91  GLN   A NE2    1 
ATOM   705   N  N      . LEU   A 1  92  ? -33.439 -89.667  44.610  1.00 65.80  ? 92  LEU   A N      1 
ATOM   706   C  CA     . LEU   A 1  92  ? -32.507 -88.617  44.216  1.00 51.75  ? 92  LEU   A CA     1 
ATOM   707   C  C      . LEU   A 1  92  ? -33.270 -87.634  43.336  1.00 57.29  ? 92  LEU   A C      1 
ATOM   708   O  O      . LEU   A 1  92  ? -33.425 -87.856  42.136  1.00 68.45  ? 92  LEU   A O      1 
ATOM   709   C  CB     . LEU   A 1  92  ? -31.311 -89.231  43.493  1.00 51.03  ? 92  LEU   A CB     1 
ATOM   710   C  CG     . LEU   A 1  92  ? -30.803 -90.534  44.131  1.00 54.51  ? 92  LEU   A CG     1 
ATOM   711   C  CD1    . LEU   A 1  92  ? -29.650 -91.118  43.391  1.00 46.51  ? 92  LEU   A CD1    1 
ATOM   712   C  CD2    . LEU   A 1  92  ? -30.364 -90.285  45.570  1.00 62.24  ? 92  LEU   A CD2    1 
ATOM   713   N  N      . ILE   A 1  93  ? -33.759 -86.552  43.943  1.00 56.63  ? 93  ILE   A N      1 
ATOM   714   C  CA     . ILE   A 1  93  ? -34.500 -85.473  43.286  1.00 52.99  ? 93  ILE   A CA     1 
ATOM   715   C  C      . ILE   A 1  93  ? -33.538 -84.369  42.866  1.00 55.59  ? 93  ILE   A C      1 
ATOM   716   O  O      . ILE   A 1  93  ? -32.606 -84.033  43.599  1.00 58.15  ? 93  ILE   A O      1 
ATOM   717   C  CB     . ILE   A 1  93  ? -35.589 -84.920  44.232  1.00 50.75  ? 93  ILE   A CB     1 
ATOM   718   C  CG1    . ILE   A 1  93  ? -36.424 -86.046  44.826  1.00 55.00  ? 93  ILE   A CG1    1 
ATOM   719   C  CG2    . ILE   A 1  93  ? -36.433 -83.853  43.583  1.00 46.89  ? 93  ILE   A CG2    1 
ATOM   720   C  CD1    . ILE   A 1  93  ? -37.517 -85.531  45.715  1.00 58.86  ? 93  ILE   A CD1    1 
ATOM   721   N  N      . THR   A 1  94  ? -33.784 -83.774  41.696  1.00 61.96  ? 94  THR   A N      1 
ATOM   722   C  CA     . THR   A 1  94  ? -32.888 -82.788  41.103  1.00 49.01  ? 94  THR   A CA     1 
ATOM   723   C  C      . THR   A 1  94  ? -33.659 -81.687  40.398  1.00 53.52  ? 94  THR   A C      1 
ATOM   724   O  O      . THR   A 1  94  ? -34.566 -81.953  39.604  1.00 56.49  ? 94  THR   A O      1 
ATOM   725   C  CB     . THR   A 1  94  ? -31.944 -83.439  40.094  1.00 51.68  ? 94  THR   A CB     1 
ATOM   726   O  OG1    . THR   A 1  94  ? -31.456 -84.670  40.623  1.00 57.42  ? 94  THR   A OG1    1 
ATOM   727   C  CG2    . THR   A 1  94  ? -30.807 -82.558  39.852  1.00 57.02  ? 94  THR   A CG2    1 
ATOM   728   N  N      . GLY   A 1  95  ? -33.264 -80.456  40.659  1.00 54.31  ? 95  GLY   A N      1 
ATOM   729   C  CA     . GLY   A 1  95  ? -33.724 -79.336  39.872  1.00 51.76  ? 95  GLY   A CA     1 
ATOM   730   C  C      . GLY   A 1  95  ? -32.942 -79.233  38.579  1.00 53.30  ? 95  GLY   A C      1 
ATOM   731   O  O      . GLY   A 1  95  ? -32.301 -80.183  38.119  1.00 49.42  ? 95  GLY   A O      1 
ATOM   732   N  N      . LYS   A 1  96  ? -33.015 -78.048  37.979  1.00 61.48  ? 96  LYS   A N      1 
ATOM   733   C  CA     . LYS   A 1  96  ? -32.178 -77.657  36.849  1.00 64.39  ? 96  LYS   A CA     1 
ATOM   734   C  C      . LYS   A 1  96  ? -31.351 -76.413  37.109  1.00 61.60  ? 96  LYS   A C      1 
ATOM   735   O  O      . LYS   A 1  96  ? -30.203 -76.351  36.669  1.00 64.98  ? 96  LYS   A O      1 
ATOM   736   C  CB     . LYS   A 1  96  ? -33.032 -77.419  35.594  1.00 69.06  ? 96  LYS   A CB     1 
ATOM   737   C  CG     . LYS   A 1  96  ? -32.414 -77.997  34.325  1.00 82.78  ? 96  LYS   A CG     1 
ATOM   738   C  CD     . LYS   A 1  96  ? -33.261 -77.679  33.075  1.00 89.55  ? 96  LYS   A CD     1 
ATOM   739   C  CE     . LYS   A 1  96  ? -33.106 -78.748  31.970  1.00 87.70  ? 96  LYS   A CE     1 
ATOM   740   N  NZ     . LYS   A 1  96  ? -33.457 -80.165  32.324  1.00 92.91  ? 96  LYS   A NZ     1 
ATOM   741   N  N      . GLU   A 1  97  ? -31.915 -75.420  37.794  1.00 54.93  ? 97  GLU   A N      1 
ATOM   742   C  CA     . GLU   A 1  97  ? -31.287 -74.129  38.044  1.00 55.14  ? 97  GLU   A CA     1 
ATOM   743   C  C      . GLU   A 1  97  ? -31.124 -73.991  39.549  1.00 58.20  ? 97  GLU   A C      1 
ATOM   744   O  O      . GLU   A 1  97  ? -32.122 -74.098  40.276  1.00 65.99  ? 97  GLU   A O      1 
ATOM   745   C  CB     . GLU   A 1  97  ? -32.193 -73.002  37.538  1.00 51.82  ? 97  GLU   A CB     1 
ATOM   746   C  CG     . GLU   A 1  97  ? -31.529 -71.733  37.144  1.00 53.70  ? 97  GLU   A CG     1 
ATOM   747   C  CD     . GLU   A 1  97  ? -32.524 -70.741  36.587  1.00 64.17  ? 97  GLU   A CD     1 
ATOM   748   O  OE1    . GLU   A 1  97  ? -33.742 -70.937  36.813  1.00 64.19  ? 97  GLU   A OE1    1 
ATOM   749   O  OE2    . GLU   A 1  97  ? -32.099 -69.787  35.898  1.00 68.48  ? 97  GLU   A OE2    1 
ATOM   750   N  N      . ASP   A 1  98  ? -29.905 -73.740  40.039  1.00 46.23  ? 98  ASP   A N      1 
ATOM   751   C  CA     . ASP   A 1  98  ? -29.745 -73.704  41.493  1.00 43.36  ? 98  ASP   A CA     1 
ATOM   752   C  C      . ASP   A 1  98  ? -30.283 -72.378  42.056  1.00 40.04  ? 98  ASP   A C      1 
ATOM   753   O  O      . ASP   A 1  98  ? -30.845 -71.550  41.338  1.00 46.81  ? 98  ASP   A O      1 
ATOM   754   C  CB     . ASP   A 1  98  ? -28.296 -73.973  41.892  1.00 45.70  ? 98  ASP   A CB     1 
ATOM   755   C  CG     . ASP   A 1  98  ? -27.378 -72.814  41.637  1.00 47.67  ? 98  ASP   A CG     1 
ATOM   756   O  OD1    . ASP   A 1  98  ? -27.739 -71.659  42.005  1.00 39.44  ? 98  ASP   A OD1    1 
ATOM   757   O  OD2    . ASP   A 1  98  ? -26.272 -73.072  41.111  1.00 55.07  ? 98  ASP   A OD2    1 
ATOM   758   N  N      . ALA   A 1  99  ? -30.147 -72.163  43.362  1.00 36.94  ? 99  ALA   A N      1 
ATOM   759   C  CA     . ALA   A 1  99  ? -30.709 -70.987  44.017  1.00 38.72  ? 99  ALA   A CA     1 
ATOM   760   C  C      . ALA   A 1  99  ? -29.696 -69.853  44.180  1.00 43.65  ? 99  ALA   A C      1 
ATOM   761   O  O      . ALA   A 1  99  ? -29.897 -68.980  45.039  1.00 42.03  ? 99  ALA   A O      1 
ATOM   762   C  CB     . ALA   A 1  99  ? -31.294 -71.345  45.383  1.00 32.70  ? 99  ALA   A CB     1 
ATOM   763   N  N      . ALA   A 1  100 ? -28.610 -69.866  43.400  1.00 34.15  ? 100 ALA   A N      1 
ATOM   764   C  CA     . ALA   A 1  100 ? -27.618 -68.787  43.373  1.00 40.05  ? 100 ALA   A CA     1 
ATOM   765   C  C      . ALA   A 1  100 ? -27.335 -68.179  44.754  1.00 40.67  ? 100 ALA   A C      1 
ATOM   766   O  O      . ALA   A 1  100 ? -27.409 -66.964  44.960  1.00 40.36  ? 100 ALA   A O      1 
ATOM   767   C  CB     . ALA   A 1  100 ? -28.050 -67.702  42.397  1.00 40.07  ? 100 ALA   A CB     1 
ATOM   768   N  N      . ASN   A 1  101 ? -26.979 -69.040  45.705  1.00 38.15  ? 101 ASN   A N      1 
ATOM   769   C  CA     . ASN   A 1  101 ? -26.565 -68.616  47.037  1.00 39.64  ? 101 ASN   A CA     1 
ATOM   770   C  C      . ASN   A 1  101 ? -27.604 -67.710  47.691  1.00 39.23  ? 101 ASN   A C      1 
ATOM   771   O  O      . ASN   A 1  101 ? -27.292 -66.918  48.583  1.00 35.08  ? 101 ASN   A O      1 
ATOM   772   C  CB     . ASN   A 1  101 ? -25.217 -67.892  47.007  1.00 38.85  ? 101 ASN   A CB     1 
ATOM   773   C  CG     . ASN   A 1  101 ? -24.133 -68.692  46.326  1.00 46.22  ? 101 ASN   A CG     1 
ATOM   774   O  OD1    . ASN   A 1  101 ? -23.340 -68.145  45.571  1.00 48.67  ? 101 ASN   A OD1    1 
ATOM   775   N  ND2    . ASN   A 1  101 ? -24.165 -70.007  46.499  1.00 51.86  ? 101 ASN   A ND2    1 
ATOM   776   N  N      . ASN   A 1  102 ? -28.855 -67.815  47.269  1.00 42.10  ? 102 ASN   A N      1 
ATOM   777   C  CA     . ASN   A 1  102 ? -29.870 -66.817  47.589  1.00 43.40  ? 102 ASN   A CA     1 
ATOM   778   C  C      . ASN   A 1  102 ? -30.962 -67.504  48.396  1.00 44.66  ? 102 ASN   A C      1 
ATOM   779   O  O      . ASN   A 1  102 ? -31.722 -68.308  47.841  1.00 47.42  ? 102 ASN   A O      1 
ATOM   780   C  CB     . ASN   A 1  102 ? -30.438 -66.226  46.301  1.00 44.12  ? 102 ASN   A CB     1 
ATOM   781   C  CG     . ASN   A 1  102 ? -31.271 -64.990  46.537  1.00 45.71  ? 102 ASN   A CG     1 
ATOM   782   O  OD1    . ASN   A 1  102 ? -31.703 -64.718  47.649  1.00 48.44  ? 102 ASN   A OD1    1 
ATOM   783   N  ND2    . ASN   A 1  102 ? -31.525 -64.249  45.480  1.00 47.97  ? 102 ASN   A ND2    1 
ATOM   784   N  N      . TYR   A 1  103 ? -31.056 -67.193  49.697  1.00 43.72  ? 103 TYR   A N      1 
ATOM   785   C  CA     . TYR   A 1  103 ? -32.083 -67.835  50.529  1.00 45.79  ? 103 TYR   A CA     1 
ATOM   786   C  C      . TYR   A 1  103 ? -33.487 -67.648  49.961  1.00 48.29  ? 103 TYR   A C      1 
ATOM   787   O  O      . TYR   A 1  103 ? -34.276 -68.597  49.918  1.00 47.63  ? 103 TYR   A O      1 
ATOM   788   C  CB     . TYR   A 1  103 ? -32.027 -67.330  51.978  1.00 46.07  ? 103 TYR   A CB     1 
ATOM   789   C  CG     . TYR   A 1  103 ? -33.264 -67.719  52.797  1.00 53.44  ? 103 TYR   A CG     1 
ATOM   790   C  CD1    . TYR   A 1  103 ? -33.380 -68.962  53.423  1.00 52.60  ? 103 TYR   A CD1    1 
ATOM   791   C  CD2    . TYR   A 1  103 ? -34.284 -66.813  53.001  1.00 54.77  ? 103 TYR   A CD2    1 
ATOM   792   C  CE1    . TYR   A 1  103 ? -34.524 -69.305  54.165  1.00 51.00  ? 103 TYR   A CE1    1 
ATOM   793   C  CE2    . TYR   A 1  103 ? -35.414 -67.145  53.749  1.00 57.76  ? 103 TYR   A CE2    1 
ATOM   794   C  CZ     . TYR   A 1  103 ? -35.536 -68.380  54.328  1.00 52.08  ? 103 TYR   A CZ     1 
ATOM   795   O  OH     . TYR   A 1  103 ? -36.682 -68.652  55.055  1.00 49.39  ? 103 TYR   A OH     1 
ATOM   796   N  N      . ALA   A 1  104 ? -33.819 -66.422  49.535  1.00 55.31  ? 104 ALA   A N      1 
ATOM   797   C  CA     . ALA   A 1  104 ? -35.145 -66.123  48.996  1.00 47.93  ? 104 ALA   A CA     1 
ATOM   798   C  C      . ALA   A 1  104 ? -35.409 -66.877  47.693  1.00 41.59  ? 104 ALA   A C      1 
ATOM   799   O  O      . ALA   A 1  104 ? -36.525 -67.343  47.455  1.00 45.73  ? 104 ALA   A O      1 
ATOM   800   C  CB     . ALA   A 1  104 ? -35.301 -64.608  48.807  1.00 41.82  ? 104 ALA   A CB     1 
ATOM   801   N  N      . ARG   A 1  105 ? -34.401 -67.026  46.843  1.00 45.95  ? 105 ARG   A N      1 
ATOM   802   C  CA     . ARG   A 1  105 ? -34.606 -67.785  45.616  1.00 42.88  ? 105 ARG   A CA     1 
ATOM   803   C  C      . ARG   A 1  105 ? -34.943 -69.231  45.905  1.00 43.30  ? 105 ARG   A C      1 
ATOM   804   O  O      . ARG   A 1  105 ? -35.690 -69.848  45.142  1.00 46.49  ? 105 ARG   A O      1 
ATOM   805   C  CB     . ARG   A 1  105 ? -33.365 -67.708  44.730  1.00 45.36  ? 105 ARG   A CB     1 
ATOM   806   C  CG     . ARG   A 1  105 ? -33.488 -68.393  43.377  1.00 45.04  ? 105 ARG   A CG     1 
ATOM   807   C  CD     . ARG   A 1  105 ? -32.247 -68.100  42.557  1.00 44.98  ? 105 ARG   A CD     1 
ATOM   808   N  NE     . ARG   A 1  105 ? -32.360 -68.401  41.134  1.00 47.77  ? 105 ARG   A NE     1 
ATOM   809   C  CZ     . ARG   A 1  105 ? -32.813 -67.553  40.218  1.00 51.12  ? 105 ARG   A CZ     1 
ATOM   810   N  NH1    . ARG   A 1  105 ? -33.337 -66.380  40.559  1.00 42.82  ? 105 ARG   A NH1    1 
ATOM   811   N  NH2    . ARG   A 1  105 ? -32.708 -67.876  38.928  1.00 50.00  ? 105 ARG   A NH2    1 
ATOM   812   N  N      . GLY   A 1  106 ? -34.411 -69.790  46.994  1.00 44.81  ? 106 GLY   A N      1 
ATOM   813   C  CA     . GLY   A 1  106 ? -34.534 -71.221  47.236  1.00 46.15  ? 106 GLY   A CA     1 
ATOM   814   C  C      . GLY   A 1  106 ? -35.811 -71.595  47.957  1.00 46.02  ? 106 GLY   A C      1 
ATOM   815   O  O      . GLY   A 1  106 ? -36.418 -72.644  47.718  1.00 47.39  ? 106 GLY   A O      1 
ATOM   816   N  N      . HIS   A 1  107 ? -36.210 -70.701  48.857  1.00 43.53  ? 107 HIS   A N      1 
ATOM   817   C  CA     . HIS   A 1  107 ? -37.421 -70.838  49.650  1.00 43.40  ? 107 HIS   A CA     1 
ATOM   818   C  C      . HIS   A 1  107 ? -38.655 -70.514  48.827  1.00 51.02  ? 107 HIS   A C      1 
ATOM   819   O  O      . HIS   A 1  107 ? -39.550 -71.355  48.654  1.00 49.06  ? 107 HIS   A O      1 
ATOM   820   C  CB     . HIS   A 1  107 ? -37.331 -69.906  50.859  1.00 46.64  ? 107 HIS   A CB     1 
ATOM   821   C  CG     . HIS   A 1  107 ? -38.449 -70.074  51.839  1.00 55.64  ? 107 HIS   A CG     1 
ATOM   822   N  ND1    . HIS   A 1  107 ? -38.279 -70.679  53.067  1.00 58.30  ? 107 HIS   A ND1    1 
ATOM   823   C  CD2    . HIS   A 1  107 ? -39.750 -69.710  51.775  1.00 51.36  ? 107 HIS   A CD2    1 
ATOM   824   C  CE1    . HIS   A 1  107 ? -39.429 -70.686  53.713  1.00 56.08  ? 107 HIS   A CE1    1 
ATOM   825   N  NE2    . HIS   A 1  107 ? -40.336 -70.098  52.955  1.00 55.99  ? 107 HIS   A NE2    1 
ATOM   826   N  N      . TYR   A 1  108 ? -38.707 -69.282  48.315  1.00 53.24  ? 108 TYR   A N      1 
ATOM   827   C  CA     . TYR   A 1  108 ? -39.815 -68.778  47.522  1.00 46.80  ? 108 TYR   A CA     1 
ATOM   828   C  C      . TYR   A 1  108 ? -39.709 -69.235  46.078  1.00 46.79  ? 108 TYR   A C      1 
ATOM   829   O  O      . TYR   A 1  108 ? -40.106 -70.351  45.731  1.00 51.68  ? 108 TYR   A O      1 
ATOM   830   C  CB     . TYR   A 1  108 ? -39.824 -67.272  47.615  1.00 35.09  ? 108 TYR   A CB     1 
ATOM   831   C  CG     . TYR   A 1  108 ? -40.019 -66.806  49.020  1.00 41.01  ? 108 TYR   A CG     1 
ATOM   832   C  CD1    . TYR   A 1  108 ? -41.278 -66.700  49.576  1.00 44.01  ? 108 TYR   A CD1    1 
ATOM   833   C  CD2    . TYR   A 1  108 ? -38.938 -66.496  49.804  1.00 44.92  ? 108 TYR   A CD2    1 
ATOM   834   C  CE1    . TYR   A 1  108 ? -41.436 -66.261  50.877  1.00 41.73  ? 108 TYR   A CE1    1 
ATOM   835   C  CE2    . TYR   A 1  108 ? -39.084 -66.063  51.097  1.00 44.03  ? 108 TYR   A CE2    1 
ATOM   836   C  CZ     . TYR   A 1  108 ? -40.327 -65.948  51.634  1.00 40.67  ? 108 TYR   A CZ     1 
ATOM   837   O  OH     . TYR   A 1  108 ? -40.424 -65.523  52.934  1.00 38.73  ? 108 TYR   A OH     1 
ATOM   838   N  N      . THR   A 1  109 ? -39.151 -68.378  45.240  1.00 48.37  ? 109 THR   A N      1 
ATOM   839   C  CA     . THR   A 1  109 ? -39.065 -68.579  43.797  1.00 49.69  ? 109 THR   A CA     1 
ATOM   840   C  C      . THR   A 1  109 ? -38.986 -70.041  43.376  1.00 50.92  ? 109 THR   A C      1 
ATOM   841   O  O      . THR   A 1  109 ? -40.010 -70.638  43.025  1.00 51.73  ? 109 THR   A O      1 
ATOM   842   C  CB     . THR   A 1  109 ? -37.851 -67.842  43.268  1.00 45.68  ? 109 THR   A CB     1 
ATOM   843   O  OG1    . THR   A 1  109 ? -38.037 -66.441  43.473  1.00 40.71  ? 109 THR   A OG1    1 
ATOM   844   C  CG2    . THR   A 1  109 ? -37.679 -68.148  41.817  1.00 48.28  ? 109 THR   A CG2    1 
ATOM   845   N  N      . ILE   A 1  110 ? -37.771 -70.607  43.395  1.00 51.92  ? 110 ILE   A N      1 
ATOM   846   C  CA     . ILE   A 1  110 ? -37.553 -72.000  43.014  1.00 50.41  ? 110 ILE   A CA     1 
ATOM   847   C  C      . ILE   A 1  110 ? -38.125 -72.979  44.030  1.00 52.79  ? 110 ILE   A C      1 
ATOM   848   O  O      . ILE   A 1  110 ? -38.523 -74.089  43.660  1.00 52.98  ? 110 ILE   A O      1 
ATOM   849   C  CB     . ILE   A 1  110 ? -36.058 -72.280  42.789  1.00 47.05  ? 110 ILE   A CB     1 
ATOM   850   C  CG1    . ILE   A 1  110 ? -35.509 -71.403  41.667  1.00 53.30  ? 110 ILE   A CG1    1 
ATOM   851   C  CG2    . ILE   A 1  110 ? -35.822 -73.765  42.533  1.00 45.69  ? 110 ILE   A CG2    1 
ATOM   852   C  CD1    . ILE   A 1  110 ? -34.017 -71.628  41.418  1.00 55.12  ? 110 ILE   A CD1    1 
ATOM   853   N  N      . GLY   A 1  111 ? -38.139 -72.623  45.314  1.00 53.01  ? 111 GLY   A N      1 
ATOM   854   C  CA     . GLY   A 1  111 ? -38.643 -73.519  46.332  1.00 46.32  ? 111 GLY   A CA     1 
ATOM   855   C  C      . GLY   A 1  111 ? -40.017 -74.037  45.986  1.00 49.72  ? 111 GLY   A C      1 
ATOM   856   O  O      . GLY   A 1  111 ? -40.205 -75.240  45.795  1.00 50.28  ? 111 GLY   A O      1 
ATOM   857   N  N      . LYS   A 1  112 ? -40.970 -73.115  45.849  1.00 51.82  ? 112 LYS   A N      1 
ATOM   858   C  CA     . LYS   A 1  112 ? -42.375 -73.450  45.642  1.00 50.92  ? 112 LYS   A CA     1 
ATOM   859   C  C      . LYS   A 1  112 ? -42.575 -74.403  44.469  1.00 54.03  ? 112 LYS   A C      1 
ATOM   860   O  O      . LYS   A 1  112 ? -43.555 -75.151  44.441  1.00 53.74  ? 112 LYS   A O      1 
ATOM   861   C  CB     . LYS   A 1  112 ? -43.133 -72.148  45.438  1.00 50.20  ? 112 LYS   A CB     1 
ATOM   862   C  CG     . LYS   A 1  112 ? -44.635 -72.196  45.324  1.00 68.57  ? 112 LYS   A CG     1 
ATOM   863   C  CD     . LYS   A 1  112 ? -45.143 -71.177  44.304  1.00 77.49  ? 112 LYS   A CD     1 
ATOM   864   C  CE     . LYS   A 1  112 ? -46.616 -70.837  44.531  1.00 84.53  ? 112 LYS   A CE     1 
ATOM   865   N  NZ     . LYS   A 1  112 ? -46.689 -69.956  45.765  1.00 80.21  ? 112 LYS   A NZ     1 
ATOM   866   N  N      . GLU   A 1  113 ? -41.635 -74.448  43.538  1.00 54.24  ? 113 GLU   A N      1 
ATOM   867   C  CA     . GLU   A 1  113 ? -41.786 -75.282  42.362  1.00 47.18  ? 113 GLU   A CA     1 
ATOM   868   C  C      . GLU   A 1  113 ? -41.446 -76.737  42.623  1.00 46.52  ? 113 GLU   A C      1 
ATOM   869   O  O      . GLU   A 1  113 ? -41.646 -77.566  41.736  1.00 52.31  ? 113 GLU   A O      1 
ATOM   870   C  CB     . GLU   A 1  113 ? -40.889 -74.764  41.225  1.00 59.35  ? 113 GLU   A CB     1 
ATOM   871   C  CG     . GLU   A 1  113 ? -41.104 -73.291  40.832  1.00 64.98  ? 113 GLU   A CG     1 
ATOM   872   C  CD     . GLU   A 1  113 ? -42.384 -73.040  40.028  1.00 83.45  ? 113 GLU   A CD     1 
ATOM   873   O  OE1    . GLU   A 1  113 ? -42.617 -73.736  38.999  1.00 89.64  ? 113 GLU   A OE1    1 
ATOM   874   O  OE2    . GLU   A 1  113 ? -43.161 -72.140  40.447  1.00 80.18  ? 113 GLU   A OE2    1 
ATOM   875   N  N      . ILE   A 1  114 ? -40.905 -77.088  43.782  1.00 51.52  ? 114 ILE   A N      1 
ATOM   876   C  CA     . ILE   A 1  114 ? -40.462 -78.472  43.939  1.00 56.88  ? 114 ILE   A CA     1 
ATOM   877   C  C      . ILE   A 1  114 ? -40.877 -79.022  45.299  1.00 53.29  ? 114 ILE   A C      1 
ATOM   878   O  O      . ILE   A 1  114 ? -40.810 -80.236  45.533  1.00 54.32  ? 114 ILE   A O      1 
ATOM   879   C  CB     . ILE   A 1  114 ? -38.940 -78.600  43.718  1.00 47.82  ? 114 ILE   A CB     1 
ATOM   880   C  CG1    . ILE   A 1  114 ? -38.552 -80.049  43.438  1.00 36.56  ? 114 ILE   A CG1    1 
ATOM   881   C  CG2    . ILE   A 1  114 ? -38.167 -78.061  44.899  1.00 48.51  ? 114 ILE   A CG2    1 
ATOM   882   C  CD1    . ILE   A 1  114 ? -37.221 -80.159  42.760  1.00 40.11  ? 114 ILE   A CD1    1 
ATOM   883   N  N      . ILE   A 1  115 ? -41.345 -78.143  46.189  1.00 50.67  ? 115 ILE   A N      1 
ATOM   884   C  CA     . ILE   A 1  115 ? -41.721 -78.577  47.534  1.00 55.04  ? 115 ILE   A CA     1 
ATOM   885   C  C      . ILE   A 1  115 ? -42.732 -79.714  47.448  1.00 54.04  ? 115 ILE   A C      1 
ATOM   886   O  O      . ILE   A 1  115 ? -42.570 -80.761  48.080  1.00 53.16  ? 115 ILE   A O      1 
ATOM   887   C  CB     . ILE   A 1  115 ? -42.256 -77.386  48.356  1.00 56.17  ? 115 ILE   A CB     1 
ATOM   888   C  CG1    . ILE   A 1  115 ? -42.629 -77.821  49.775  1.00 52.69  ? 115 ILE   A CG1    1 
ATOM   889   C  CG2    . ILE   A 1  115 ? -43.420 -76.722  47.654  1.00 53.71  ? 115 ILE   A CG2    1 
ATOM   890   C  CD1    . ILE   A 1  115 ? -41.440 -78.111  50.627  1.00 46.72  ? 115 ILE   A CD1    1 
ATOM   891   N  N      . ASP   A 1  116 ? -43.758 -79.553  46.609  1.00 60.84  ? 116 ASP   A N      1 
ATOM   892   C  CA     . ASP   A 1  116 ? -44.734 -80.629  46.437  1.00 59.70  ? 116 ASP   A CA     1 
ATOM   893   C  C      . ASP   A 1  116 ? -44.078 -81.890  45.886  1.00 52.70  ? 116 ASP   A C      1 
ATOM   894   O  O      . ASP   A 1  116 ? -44.366 -82.997  46.340  1.00 59.54  ? 116 ASP   A O      1 
ATOM   895   C  CB     . ASP   A 1  116 ? -45.889 -80.174  45.543  1.00 51.94  ? 116 ASP   A CB     1 
ATOM   896   C  CG     . ASP   A 1  116 ? -46.806 -79.175  46.253  1.00 73.12  ? 116 ASP   A CG     1 
ATOM   897   O  OD1    . ASP   A 1  116 ? -46.873 -79.203  47.510  1.00 69.25  ? 116 ASP   A OD1    1 
ATOM   898   O  OD2    . ASP   A 1  116 ? -47.498 -78.394  45.558  1.00 83.53  ? 116 ASP   A OD2    1 
ATOM   899   N  N      . LEU   A 1  117 ? -43.176 -81.754  44.930  1.00 49.18  ? 117 LEU   A N      1 
ATOM   900   C  CA     . LEU   A 1  117 ? -42.592 -82.957  44.360  1.00 50.05  ? 117 LEU   A CA     1 
ATOM   901   C  C      . LEU   A 1  117 ? -41.775 -83.707  45.399  1.00 56.74  ? 117 LEU   A C      1 
ATOM   902   O  O      . LEU   A 1  117 ? -41.811 -84.944  45.459  1.00 55.20  ? 117 LEU   A O      1 
ATOM   903   C  CB     . LEU   A 1  117 ? -41.730 -82.604  43.159  1.00 49.46  ? 117 LEU   A CB     1 
ATOM   904   C  CG     . LEU   A 1  117 ? -40.798 -83.749  42.821  1.00 48.35  ? 117 LEU   A CG     1 
ATOM   905   C  CD1    . LEU   A 1  117 ? -41.616 -84.956  42.478  1.00 50.82  ? 117 LEU   A CD1    1 
ATOM   906   C  CD2    . LEU   A 1  117 ? -39.972 -83.357  41.656  1.00 47.98  ? 117 LEU   A CD2    1 
ATOM   907   N  N      . VAL   A 1  118 ? -41.037 -82.971  46.231  1.00 60.57  ? 118 VAL   A N      1 
ATOM   908   C  CA     . VAL   A 1  118 ? -40.201 -83.608  47.246  1.00 58.87  ? 118 VAL   A CA     1 
ATOM   909   C  C      . VAL   A 1  118 ? -41.067 -84.317  48.270  1.00 57.18  ? 118 VAL   A C      1 
ATOM   910   O  O      . VAL   A 1  118 ? -40.847 -85.493  48.578  1.00 60.36  ? 118 VAL   A O      1 
ATOM   911   C  CB     . VAL   A 1  118 ? -39.271 -82.575  47.906  1.00 55.47  ? 118 VAL   A CB     1 
ATOM   912   C  CG1    . VAL   A 1  118 ? -38.656 -83.146  49.171  1.00 52.61  ? 118 VAL   A CG1    1 
ATOM   913   C  CG2    . VAL   A 1  118 ? -38.190 -82.137  46.915  1.00 50.00  ? 118 VAL   A CG2    1 
ATOM   914   N  N      . LEU   A 1  119 ? -42.089 -83.621  48.783  1.00 57.84  ? 119 LEU   A N      1 
ATOM   915   C  CA     . LEU   A 1  119 ? -42.930 -84.173  49.839  1.00 59.38  ? 119 LEU   A CA     1 
ATOM   916   C  C      . LEU   A 1  119 ? -43.672 -85.432  49.385  1.00 61.72  ? 119 LEU   A C      1 
ATOM   917   O  O      . LEU   A 1  119 ? -44.030 -86.259  50.231  1.00 66.21  ? 119 LEU   A O      1 
ATOM   918   C  CB     . LEU   A 1  119 ? -43.931 -83.125  50.340  1.00 45.75  ? 119 LEU   A CB     1 
ATOM   919   C  CG     . LEU   A 1  119 ? -43.450 -81.919  51.162  1.00 50.24  ? 119 LEU   A CG     1 
ATOM   920   C  CD1    . LEU   A 1  119 ? -44.550 -80.894  51.178  1.00 59.85  ? 119 LEU   A CD1    1 
ATOM   921   C  CD2    . LEU   A 1  119 ? -43.007 -82.189  52.588  1.00 52.00  ? 119 LEU   A CD2    1 
ATOM   922   N  N      . ASP   A 1  120 ? -43.916 -85.615  48.084  1.00 54.07  ? 120 ASP   A N      1 
ATOM   923   C  CA     . ASP   A 1  120 ? -44.434 -86.920  47.686  1.00 62.82  ? 120 ASP   A CA     1 
ATOM   924   C  C      . ASP   A 1  120 ? -43.356 -87.991  47.729  1.00 64.01  ? 120 ASP   A C      1 
ATOM   925   O  O      . ASP   A 1  120 ? -43.622 -89.111  48.167  1.00 68.58  ? 120 ASP   A O      1 
ATOM   926   C  CB     . ASP   A 1  120 ? -45.087 -86.904  46.289  1.00 68.17  ? 120 ASP   A CB     1 
ATOM   927   C  CG     . ASP   A 1  120 ? -46.504 -86.322  46.291  1.00 78.86  ? 120 ASP   A CG     1 
ATOM   928   O  OD1    . ASP   A 1  120 ? -47.141 -86.273  47.372  1.00 85.68  ? 120 ASP   A OD1    1 
ATOM   929   O  OD2    . ASP   A 1  120 ? -47.008 -85.973  45.193  1.00 86.08  ? 120 ASP   A OD2    1 
ATOM   930   N  N      . ARG   A 1  121 ? -42.143 -87.700  47.270  1.00 64.21  ? 121 ARG   A N      1 
ATOM   931   C  CA     . ARG   A 1  121 ? -41.120 -88.734  47.380  1.00 66.87  ? 121 ARG   A CA     1 
ATOM   932   C  C      . ARG   A 1  121 ? -40.815 -89.041  48.841  1.00 65.07  ? 121 ARG   A C      1 
ATOM   933   O  O      . ARG   A 1  121 ? -40.461 -90.175  49.186  1.00 59.07  ? 121 ARG   A O      1 
ATOM   934   C  CB     . ARG   A 1  121 ? -39.859 -88.325  46.619  1.00 62.27  ? 121 ARG   A CB     1 
ATOM   935   C  CG     . ARG   A 1  121 ? -40.139 -88.024  45.180  1.00 63.09  ? 121 ARG   A CG     1 
ATOM   936   C  CD     . ARG   A 1  121 ? -39.906 -89.267  44.363  1.00 70.14  ? 121 ARG   A CD     1 
ATOM   937   N  NE     . ARG   A 1  121 ? -40.598 -89.222  43.081  1.00 76.47  ? 121 ARG   A NE     1 
ATOM   938   C  CZ     . ARG   A 1  121 ? -40.026 -88.911  41.926  1.00 82.02  ? 121 ARG   A CZ     1 
ATOM   939   N  NH1    . ARG   A 1  121 ? -38.734 -88.636  41.846  1.00 78.16  ? 121 ARG   A NH1    1 
ATOM   940   N  NH2    . ARG   A 1  121 ? -40.764 -88.913  40.817  1.00 91.31  ? 121 ARG   A NH2    1 
ATOM   941   N  N      . ILE   A 1  122 ? -40.962 -88.049  49.712  1.00 62.09  ? 122 ILE   A N      1 
ATOM   942   C  CA     . ILE   A 1  122 ? -40.798 -88.295  51.136  1.00 62.97  ? 122 ILE   A CA     1 
ATOM   943   C  C      . ILE   A 1  122 ? -41.954 -89.143  51.670  1.00 70.09  ? 122 ILE   A C      1 
ATOM   944   O  O      . ILE   A 1  122 ? -41.733 -90.132  52.378  1.00 74.16  ? 122 ILE   A O      1 
ATOM   945   C  CB     . ILE   A 1  122 ? -40.653 -86.960  51.883  1.00 58.10  ? 122 ILE   A CB     1 
ATOM   946   C  CG1    . ILE   A 1  122 ? -39.316 -86.331  51.539  1.00 49.12  ? 122 ILE   A CG1    1 
ATOM   947   C  CG2    . ILE   A 1  122 ? -40.803 -87.154  53.387  1.00 60.71  ? 122 ILE   A CG2    1 
ATOM   948   C  CD1    . ILE   A 1  122 ? -39.077 -85.050  52.263  1.00 51.82  ? 122 ILE   A CD1    1 
ATOM   949   N  N      . ARG   A 1  123 ? -43.204 -88.787  51.332  1.00 70.36  ? 123 ARG   A N      1 
ATOM   950   C  CA     . ARG   A 1  123 ? -44.329 -89.644  51.707  1.00 66.00  ? 123 ARG   A CA     1 
ATOM   951   C  C      . ARG   A 1  123 ? -44.197 -91.053  51.143  1.00 64.70  ? 123 ARG   A C      1 
ATOM   952   O  O      . ARG   A 1  123 ? -44.822 -91.977  51.666  1.00 68.95  ? 123 ARG   A O      1 
ATOM   953   C  CB     . ARG   A 1  123 ? -45.655 -89.049  51.241  1.00 64.01  ? 123 ARG   A CB     1 
ATOM   954   C  CG     . ARG   A 1  123 ? -46.880 -89.840  51.686  1.00 59.23  ? 123 ARG   A CG     1 
ATOM   955   C  CD     . ARG   A 1  123 ? -47.175 -89.567  53.152  1.00 64.59  ? 123 ARG   A CD     1 
ATOM   956   N  NE     . ARG   A 1  123 ? -47.751 -88.238  53.335  1.00 64.90  ? 123 ARG   A NE     1 
ATOM   957   C  CZ     . ARG   A 1  123 ? -47.967 -87.660  54.513  1.00 71.19  ? 123 ARG   A CZ     1 
ATOM   958   N  NH1    . ARG   A 1  123 ? -47.661 -88.267  55.650  1.00 66.08  ? 123 ARG   A NH1    1 
ATOM   959   N  NH2    . ARG   A 1  123 ? -48.477 -86.427  54.550  1.00 72.02  ? 123 ARG   A NH2    1 
ATOM   960   N  N      . LYS   A 1  124 ? -43.402 -91.249  50.092  1.00 64.58  ? 124 LYS   A N      1 
ATOM   961   C  CA     . LYS   A 1  124 ? -43.258 -92.594  49.543  1.00 69.29  ? 124 LYS   A CA     1 
ATOM   962   C  C      . LYS   A 1  124 ? -42.453 -93.503  50.460  1.00 72.65  ? 124 LYS   A C      1 
ATOM   963   O  O      . LYS   A 1  124 ? -42.696 -94.715  50.487  1.00 73.72  ? 124 LYS   A O      1 
ATOM   964   C  CB     . LYS   A 1  124 ? -42.604 -92.557  48.162  1.00 72.49  ? 124 LYS   A CB     1 
ATOM   965   C  CG     . LYS   A 1  124 ? -43.534 -92.316  46.984  1.00 79.40  ? 124 LYS   A CG     1 
ATOM   966   C  CD     . LYS   A 1  124 ? -42.923 -93.008  45.775  1.00 89.17  ? 124 LYS   A CD     1 
ATOM   967   C  CE     . LYS   A 1  124 ? -42.514 -94.424  46.176  1.00 94.05  ? 124 LYS   A CE     1 
ATOM   968   N  NZ     . LYS   A 1  124 ? -41.828 -95.168  45.098  1.00 99.86  ? 124 LYS   A NZ     1 
ATOM   969   N  N      . LEU   A 1  125 ? -41.465 -92.953  51.176  1.00 70.23  ? 125 LEU   A N      1 
ATOM   970   C  CA     . LEU   A 1  125 ? -40.731 -93.741  52.158  1.00 67.41  ? 125 LEU   A CA     1 
ATOM   971   C  C      . LEU   A 1  125 ? -41.442 -93.777  53.505  1.00 69.83  ? 125 LEU   A C      1 
ATOM   972   O  O      . LEU   A 1  125 ? -41.367 -94.794  54.209  1.00 75.91  ? 125 LEU   A O      1 
ATOM   973   C  CB     . LEU   A 1  125 ? -39.297 -93.223  52.320  1.00 56.16  ? 125 LEU   A CB     1 
ATOM   974   C  CG     . LEU   A 1  125 ? -38.345 -93.454  51.135  1.00 51.36  ? 125 LEU   A CG     1 
ATOM   975   C  CD1    . LEU   A 1  125 ? -36.917 -93.172  51.517  1.00 50.63  ? 125 LEU   A CD1    1 
ATOM   976   C  CD2    . LEU   A 1  125 ? -38.462 -94.849  50.529  1.00 60.60  ? 125 LEU   A CD2    1 
ATOM   977   N  N      . ALA   A 1  126 ? -42.160 -92.709  53.865  1.00 63.20  ? 126 ALA   A N      1 
ATOM   978   C  CA     . ALA   A 1  126 ? -42.990 -92.742  55.063  1.00 68.37  ? 126 ALA   A CA     1 
ATOM   979   C  C      . ALA   A 1  126 ? -44.010 -93.876  55.018  1.00 74.38  ? 126 ALA   A C      1 
ATOM   980   O  O      . ALA   A 1  126 ? -44.426 -94.372  56.076  1.00 76.00  ? 126 ALA   A O      1 
ATOM   981   C  CB     . ALA   A 1  126 ? -43.689 -91.393  55.249  1.00 64.18  ? 126 ALA   A CB     1 
ATOM   982   N  N      . ASP   A 1  127 ? -44.413 -94.303  53.819  1.00 77.21  ? 127 ASP   A N      1 
ATOM   983   C  CA     . ASP   A 1  127 ? -45.412 -95.353  53.648  1.00 76.72  ? 127 ASP   A CA     1 
ATOM   984   C  C      . ASP   A 1  127 ? -44.808 -96.744  53.662  1.00 72.57  ? 127 ASP   A C      1 
ATOM   985   O  O      . ASP   A 1  127 ? -45.533 -97.722  53.475  1.00 75.48  ? 127 ASP   A O      1 
ATOM   986   C  CB     . ASP   A 1  127 ? -46.187 -95.154  52.346  1.00 70.08  ? 127 ASP   A CB     1 
ATOM   987   C  CG     . ASP   A 1  127 ? -47.206 -94.042  52.451  1.00 70.90  ? 127 ASP   A CG     1 
ATOM   988   O  OD1    . ASP   A 1  127 ? -47.372 -93.474  53.566  1.00 58.53  ? 127 ASP   A OD1    1 
ATOM   989   O  OD2    . ASP   A 1  127 ? -47.862 -93.770  51.422  1.00 70.79  ? 127 ASP   A OD2    1 
ATOM   990   N  N      . GLN   A 1  128 ? -43.498 -96.849  53.844  1.00 63.65  ? 128 GLN   A N      1 
ATOM   991   C  CA     . GLN   A 1  128 ? -42.856 -98.111  54.151  1.00 70.07  ? 128 GLN   A CA     1 
ATOM   992   C  C      . GLN   A 1  128 ? -42.442 -98.190  55.612  1.00 70.06  ? 128 GLN   A C      1 
ATOM   993   O  O      . GLN   A 1  128 ? -41.601 -99.016  55.980  1.00 62.10  ? 128 GLN   A O      1 
ATOM   994   C  CB     . GLN   A 1  128 ? -41.645 -98.296  53.262  1.00 75.08  ? 128 GLN   A CB     1 
ATOM   995   C  CG     . GLN   A 1  128 ? -41.953 -98.501  51.824  1.00 77.91  ? 128 GLN   A CG     1 
ATOM   996   C  CD     . GLN   A 1  128 ? -40.686 -98.829  51.089  1.00 91.75  ? 128 GLN   A CD     1 
ATOM   997   O  OE1    . GLN   A 1  128 ? -40.282 -99.992  51.036  1.00 102.81 ? 128 GLN   A OE1    1 
ATOM   998   N  NE2    . GLN   A 1  128 ? -40.009 -97.797  50.562  1.00 79.71  ? 128 GLN   A NE2    1 
ATOM   999   N  N      . CYS   A 1  129 ? -42.994 -97.328  56.447  1.00 66.31  ? 129 CYS   A N      1 
ATOM   1000  C  CA     . CYS   A 1  129 ? -42.570 -97.217  57.828  1.00 67.93  ? 129 CYS   A CA     1 
ATOM   1001  C  C      . CYS   A 1  129 ? -43.707 -97.644  58.733  1.00 75.53  ? 129 CYS   A C      1 
ATOM   1002  O  O      . CYS   A 1  129 ? -44.744 -96.971  58.797  1.00 76.00  ? 129 CYS   A O      1 
ATOM   1003  C  CB     . CYS   A 1  129 ? -42.103 -95.797  58.161  1.00 69.72  ? 129 CYS   A CB     1 
ATOM   1004  S  SG     . CYS   A 1  129 ? -40.571 -95.354  57.334  1.00 64.15  ? 129 CYS   A SG     1 
ATOM   1005  N  N      . THR   A 1  130 ? -43.487 -98.762  59.427  1.00 74.25  ? 130 THR   A N      1 
ATOM   1006  C  CA     . THR   A 1  130 ? -44.424 -99.259  60.424  1.00 69.67  ? 130 THR   A CA     1 
ATOM   1007  C  C      . THR   A 1  130 ? -44.615 -98.269  61.570  1.00 70.90  ? 130 THR   A C      1 
ATOM   1008  O  O      . THR   A 1  130 ? -45.739 -98.075  62.052  1.00 73.05  ? 130 THR   A O      1 
ATOM   1009  C  CB     . THR   A 1  130 ? -43.914 -100.596 60.929  1.00 70.00  ? 130 THR   A CB     1 
ATOM   1010  O  OG1    . THR   A 1  130 ? -42.708 -100.376 61.682  1.00 73.45  ? 130 THR   A OG1    1 
ATOM   1011  C  CG2    . THR   A 1  130 ? -43.613 -101.502 59.730  1.00 55.37  ? 130 THR   A CG2    1 
ATOM   1012  N  N      . GLY   A 1  131 ? -43.539 -97.630  62.020  1.00 71.76  ? 131 GLY   A N      1 
ATOM   1013  C  CA     . GLY   A 1  131 ? -43.642 -96.674  63.109  1.00 73.19  ? 131 GLY   A CA     1 
ATOM   1014  C  C      . GLY   A 1  131 ? -42.637 -95.546  62.993  1.00 73.72  ? 131 GLY   A C      1 
ATOM   1015  O  O      . GLY   A 1  131 ? -41.662 -95.501  63.745  1.00 73.62  ? 131 GLY   A O      1 
ATOM   1016  N  N      . LEU   A 1  132 ? -42.890 -94.618  62.068  1.00 71.13  ? 132 LEU   A N      1 
ATOM   1017  C  CA     . LEU   A 1  132 ? -41.934 -93.577  61.722  1.00 63.11  ? 132 LEU   A CA     1 
ATOM   1018  C  C      . LEU   A 1  132 ? -41.571 -92.719  62.928  1.00 64.08  ? 132 LEU   A C      1 
ATOM   1019  O  O      . LEU   A 1  132 ? -42.441 -92.164  63.607  1.00 63.18  ? 132 LEU   A O      1 
ATOM   1020  C  CB     . LEU   A 1  132 ? -42.514 -92.667  60.651  1.00 71.69  ? 132 LEU   A CB     1 
ATOM   1021  C  CG     . LEU   A 1  132 ? -41.623 -91.453  60.387  1.00 69.26  ? 132 LEU   A CG     1 
ATOM   1022  C  CD1    . LEU   A 1  132 ? -40.447 -91.901  59.474  1.00 62.30  ? 132 LEU   A CD1    1 
ATOM   1023  C  CD2    . LEU   A 1  132 ? -42.371 -90.201  59.905  1.00 60.16  ? 132 LEU   A CD2    1 
ATOM   1024  N  N      . GLN   A 1  133 ? -40.267 -92.545  63.130  1.00 63.00  ? 133 GLN   A N      1 
ATOM   1025  C  CA     . GLN   A 1  133 ? -39.734 -91.785  64.248  1.00 59.95  ? 133 GLN   A CA     1 
ATOM   1026  C  C      . GLN   A 1  133 ? -39.673 -90.300  63.948  1.00 60.78  ? 133 GLN   A C      1 
ATOM   1027  O  O      . GLN   A 1  133 ? -40.113 -89.470  64.753  1.00 55.27  ? 133 GLN   A O      1 
ATOM   1028  C  CB     . GLN   A 1  133 ? -38.331 -92.277  64.544  1.00 64.23  ? 133 GLN   A CB     1 
ATOM   1029  C  CG     . GLN   A 1  133 ? -38.240 -93.396  65.503  1.00 63.33  ? 133 GLN   A CG     1 
ATOM   1030  C  CD     . GLN   A 1  133 ? -36.839 -93.530  65.970  1.00 58.81  ? 133 GLN   A CD     1 
ATOM   1031  O  OE1    . GLN   A 1  133 ? -36.314 -92.631  66.614  1.00 59.00  ? 133 GLN   A OE1    1 
ATOM   1032  N  NE2    . GLN   A 1  133 ? -36.183 -94.615  65.573  1.00 55.73  ? 133 GLN   A NE2    1 
ATOM   1033  N  N      . GLY   A 1  134 ? -39.080 -89.956  62.813  1.00 61.89  ? 134 GLY   A N      1 
ATOM   1034  C  CA     . GLY   A 1  134 ? -38.815 -88.574  62.475  1.00 56.56  ? 134 GLY   A CA     1 
ATOM   1035  C  C      . GLY   A 1  134 ? -37.785 -88.511  61.367  1.00 53.87  ? 134 GLY   A C      1 
ATOM   1036  O  O      . GLY   A 1  134 ? -37.507 -89.515  60.701  1.00 53.70  ? 134 GLY   A O      1 
ATOM   1037  N  N      . PHE   A 1  135 ? -37.212 -87.315  61.205  1.00 51.65  ? 135 PHE   A N      1 
ATOM   1038  C  CA     . PHE   A 1  135 ? -36.289 -87.046  60.108  1.00 50.86  ? 135 PHE   A CA     1 
ATOM   1039  C  C      . PHE   A 1  135 ? -34.951 -86.522  60.606  1.00 49.74  ? 135 PHE   A C      1 
ATOM   1040  O  O      . PHE   A 1  135 ? -34.879 -85.791  61.599  1.00 46.42  ? 135 PHE   A O      1 
ATOM   1041  C  CB     . PHE   A 1  135 ? -36.887 -86.049  59.120  1.00 48.94  ? 135 PHE   A CB     1 
ATOM   1042  C  CG     . PHE   A 1  135 ? -38.255 -86.424  58.648  1.00 50.42  ? 135 PHE   A CG     1 
ATOM   1043  C  CD1    . PHE   A 1  135 ? -39.374 -86.031  59.354  1.00 43.18  ? 135 PHE   A CD1    1 
ATOM   1044  C  CD2    . PHE   A 1  135 ? -38.421 -87.180  57.492  1.00 51.81  ? 135 PHE   A CD2    1 
ATOM   1045  C  CE1    . PHE   A 1  135 ? -40.627 -86.392  58.918  1.00 46.83  ? 135 PHE   A CE1    1 
ATOM   1046  C  CE2    . PHE   A 1  135 ? -39.678 -87.546  57.059  1.00 45.55  ? 135 PHE   A CE2    1 
ATOM   1047  C  CZ     . PHE   A 1  135 ? -40.778 -87.147  57.766  1.00 46.07  ? 135 PHE   A CZ     1 
ATOM   1048  N  N      . LEU   A 1  136 ? -33.895 -86.937  59.903  1.00 52.93  ? 136 LEU   A N      1 
ATOM   1049  C  CA     . LEU   A 1  136 ? -32.543 -86.395  60.032  1.00 51.91  ? 136 LEU   A CA     1 
ATOM   1050  C  C      . LEU   A 1  136 ? -32.295 -85.542  58.793  1.00 51.94  ? 136 LEU   A C      1 
ATOM   1051  O  O      . LEU   A 1  136 ? -32.178 -86.076  57.685  1.00 53.02  ? 136 LEU   A O      1 
ATOM   1052  C  CB     . LEU   A 1  136 ? -31.516 -87.521  60.145  1.00 51.98  ? 136 LEU   A CB     1 
ATOM   1053  C  CG     . LEU   A 1  136 ? -31.668 -88.510  61.305  1.00 45.23  ? 136 LEU   A CG     1 
ATOM   1054  C  CD1    . LEU   A 1  136 ? -30.503 -89.435  61.330  1.00 42.99  ? 136 LEU   A CD1    1 
ATOM   1055  C  CD2    . LEU   A 1  136 ? -31.690 -87.726  62.576  1.00 48.42  ? 136 LEU   A CD2    1 
ATOM   1056  N  N      . VAL   A 1  137 ? -32.248 -84.227  58.968  1.00 45.48  ? 137 VAL   A N      1 
ATOM   1057  C  CA     . VAL   A 1  137 ? -32.199 -83.288  57.853  1.00 45.54  ? 137 VAL   A CA     1 
ATOM   1058  C  C      . VAL   A 1  137 ? -30.799 -82.694  57.787  1.00 41.43  ? 137 VAL   A C      1 
ATOM   1059  O  O      . VAL   A 1  137 ? -30.400 -81.962  58.696  1.00 46.26  ? 137 VAL   A O      1 
ATOM   1060  C  CB     . VAL   A 1  137 ? -33.260 -82.188  58.003  1.00 51.08  ? 137 VAL   A CB     1 
ATOM   1061  C  CG1    . VAL   A 1  137 ? -33.329 -81.342  56.749  1.00 49.08  ? 137 VAL   A CG1    1 
ATOM   1062  C  CG2    . VAL   A 1  137 ? -34.621 -82.789  58.308  1.00 48.09  ? 137 VAL   A CG2    1 
ATOM   1063  N  N      . PHE   A 1  138 ? -30.071 -82.976  56.704  1.00 42.27  ? 138 PHE   A N      1 
ATOM   1064  C  CA     . PHE   A 1  138 ? -28.682 -82.550  56.513  1.00 43.21  ? 138 PHE   A CA     1 
ATOM   1065  C  C      . PHE   A 1  138 ? -28.624 -81.392  55.522  1.00 44.07  ? 138 PHE   A C      1 
ATOM   1066  O  O      . PHE   A 1  138 ? -29.099 -81.524  54.395  1.00 49.62  ? 138 PHE   A O      1 
ATOM   1067  C  CB     . PHE   A 1  138 ? -27.835 -83.700  55.959  1.00 42.39  ? 138 PHE   A CB     1 
ATOM   1068  C  CG     . PHE   A 1  138 ? -27.774 -84.883  56.864  1.00 49.81  ? 138 PHE   A CG     1 
ATOM   1069  C  CD1    . PHE   A 1  138 ? -28.843 -85.752  56.959  1.00 52.72  ? 138 PHE   A CD1    1 
ATOM   1070  C  CD2    . PHE   A 1  138 ? -26.681 -85.093  57.683  1.00 52.31  ? 138 PHE   A CD2    1 
ATOM   1071  C  CE1    . PHE   A 1  138 ? -28.797 -86.839  57.825  1.00 55.76  ? 138 PHE   A CE1    1 
ATOM   1072  C  CE2    . PHE   A 1  138 ? -26.637 -86.172  58.551  1.00 49.37  ? 138 PHE   A CE2    1 
ATOM   1073  C  CZ     . PHE   A 1  138 ? -27.692 -87.038  58.627  1.00 49.48  ? 138 PHE   A CZ     1 
ATOM   1074  N  N      . HIS   A 1  139 ? -28.006 -80.283  55.902  1.00 40.85  ? 139 HIS   A N      1 
ATOM   1075  C  CA     . HIS   A 1  139 ? -27.954 -79.135  54.994  1.00 38.74  ? 139 HIS   A CA     1 
ATOM   1076  C  C      . HIS   A 1  139 ? -26.903 -78.146  55.480  1.00 38.99  ? 139 HIS   A C      1 
ATOM   1077  O  O      . HIS   A 1  139 ? -26.264 -78.343  56.516  1.00 43.10  ? 139 HIS   A O      1 
ATOM   1078  C  CB     . HIS   A 1  139 ? -29.318 -78.467  54.919  1.00 44.88  ? 139 HIS   A CB     1 
ATOM   1079  C  CG     . HIS   A 1  139 ? -29.739 -77.828  56.208  1.00 41.88  ? 139 HIS   A CG     1 
ATOM   1080  N  ND1    . HIS   A 1  139 ? -29.533 -76.492  56.479  1.00 45.38  ? 139 HIS   A ND1    1 
ATOM   1081  C  CD2    . HIS   A 1  139 ? -30.315 -78.350  57.313  1.00 37.24  ? 139 HIS   A CD2    1 
ATOM   1082  C  CE1    . HIS   A 1  139 ? -29.983 -76.213  57.688  1.00 42.53  ? 139 HIS   A CE1    1 
ATOM   1083  N  NE2    . HIS   A 1  139 ? -30.457 -77.325  58.216  1.00 42.77  ? 139 HIS   A NE2    1 
ATOM   1084  N  N      . SER   A 1  140 ? -26.759 -77.047  54.753  1.00 40.24  ? 140 SER   A N      1 
ATOM   1085  C  CA     . SER   A 1  140 ? -25.806 -76.003  55.112  1.00 37.69  ? 140 SER   A CA     1 
ATOM   1086  C  C      . SER   A 1  140 ? -26.544 -74.704  55.401  1.00 39.69  ? 140 SER   A C      1 
ATOM   1087  O  O      . SER   A 1  140 ? -27.595 -74.441  54.817  1.00 42.42  ? 140 SER   A O      1 
ATOM   1088  C  CB     . SER   A 1  140 ? -24.788 -75.785  53.991  1.00 37.61  ? 140 SER   A CB     1 
ATOM   1089  O  OG     . SER   A 1  140 ? -25.404 -75.214  52.863  1.00 33.95  ? 140 SER   A OG     1 
ATOM   1090  N  N      . PHE   A 1  141 ? -25.999 -73.883  56.308  1.00 35.78  ? 141 PHE   A N      1 
ATOM   1091  C  CA     . PHE   A 1  141 ? -26.638 -72.594  56.578  1.00 41.82  ? 141 PHE   A CA     1 
ATOM   1092  C  C      . PHE   A 1  141 ? -26.431 -71.591  55.435  1.00 45.14  ? 141 PHE   A C      1 
ATOM   1093  O  O      . PHE   A 1  141 ? -27.017 -70.502  55.470  1.00 39.83  ? 141 PHE   A O      1 
ATOM   1094  C  CB     . PHE   A 1  141 ? -26.080 -71.926  57.850  1.00 43.64  ? 141 PHE   A CB     1 
ATOM   1095  C  CG     . PHE   A 1  141 ? -26.555 -72.523  59.144  1.00 42.23  ? 141 PHE   A CG     1 
ATOM   1096  C  CD1    . PHE   A 1  141 ? -27.501 -73.517  59.164  1.00 42.83  ? 141 PHE   A CD1    1 
ATOM   1097  C  CD2    . PHE   A 1  141 ? -26.059 -72.052  60.355  1.00 41.83  ? 141 PHE   A CD2    1 
ATOM   1098  C  CE1    . PHE   A 1  141 ? -27.916 -74.056  60.372  1.00 44.19  ? 141 PHE   A CE1    1 
ATOM   1099  C  CE2    . PHE   A 1  141 ? -26.474 -72.584  61.553  1.00 37.26  ? 141 PHE   A CE2    1 
ATOM   1100  C  CZ     . PHE   A 1  141 ? -27.405 -73.580  61.559  1.00 41.65  ? 141 PHE   A CZ     1 
ATOM   1101  N  N      . GLY   A 1  142 ? -25.592 -71.917  54.447  1.00 42.12  ? 142 GLY   A N      1 
ATOM   1102  C  CA     . GLY   A 1  142 ? -25.069 -70.921  53.539  1.00 37.81  ? 142 GLY   A CA     1 
ATOM   1103  C  C      . GLY   A 1  142 ? -25.521 -71.060  52.109  1.00 40.62  ? 142 GLY   A C      1 
ATOM   1104  O  O      . GLY   A 1  142 ? -25.767 -70.055  51.444  1.00 44.46  ? 142 GLY   A O      1 
ATOM   1105  N  N      . GLY   A 1  143 ? -25.604 -72.281  51.601  1.00 40.41  ? 143 GLY   A N      1 
ATOM   1106  C  CA     . GLY   A 1  143 ? -26.170 -72.455  50.281  1.00 42.15  ? 143 GLY   A CA     1 
ATOM   1107  C  C      . GLY   A 1  143 ? -27.527 -71.793  50.247  1.00 41.88  ? 143 GLY   A C      1 
ATOM   1108  O  O      . GLY   A 1  143 ? -28.165 -71.668  51.294  1.00 44.10  ? 143 GLY   A O      1 
ATOM   1109  N  N      . GLY   A 1  144 ? -27.967 -71.321  49.077  1.00 45.97  ? 144 GLY   A N      1 
ATOM   1110  C  CA     . GLY   A 1  144 ? -29.333 -70.831  48.968  1.00 40.40  ? 144 GLY   A CA     1 
ATOM   1111  C  C      . GLY   A 1  144 ? -30.353 -71.956  49.056  1.00 44.14  ? 144 GLY   A C      1 
ATOM   1112  O  O      . GLY   A 1  144 ? -31.373 -71.827  49.740  1.00 44.59  ? 144 GLY   A O      1 
ATOM   1113  N  N      . THR   A 1  145 ? -30.100 -73.066  48.344  1.00 45.16  ? 145 THR   A N      1 
ATOM   1114  C  CA     . THR   A 1  145 ? -30.831 -74.312  48.565  1.00 37.15  ? 145 THR   A CA     1 
ATOM   1115  C  C      . THR   A 1  145 ? -30.629 -74.825  49.975  1.00 43.62  ? 145 THR   A C      1 
ATOM   1116  O  O      . THR   A 1  145 ? -31.593 -75.076  50.703  1.00 45.87  ? 145 THR   A O      1 
ATOM   1117  C  CB     . THR   A 1  145 ? -30.380 -75.363  47.566  1.00 38.80  ? 145 THR   A CB     1 
ATOM   1118  O  OG1    . THR   A 1  145 ? -30.465 -74.816  46.245  1.00 50.12  ? 145 THR   A OG1    1 
ATOM   1119  C  CG2    . THR   A 1  145 ? -31.190 -76.616  47.668  1.00 38.43  ? 145 THR   A CG2    1 
ATOM   1120  N  N      . GLY   A 1  146 ? -29.383 -75.008  50.372  1.00 43.55  ? 146 GLY   A N      1 
ATOM   1121  C  CA     . GLY   A 1  146 ? -29.118 -75.300  51.757  1.00 43.94  ? 146 GLY   A CA     1 
ATOM   1122  C  C      . GLY   A 1  146 ? -30.002 -74.550  52.731  1.00 40.72  ? 146 GLY   A C      1 
ATOM   1123  O  O      . GLY   A 1  146 ? -30.679 -75.166  53.559  1.00 45.33  ? 146 GLY   A O      1 
ATOM   1124  N  N      . SER   A 1  147 ? -30.009 -73.228  52.664  1.00 36.97  ? 147 SER   A N      1 
ATOM   1125  C  CA     . SER   A 1  147 ? -30.678 -72.484  53.725  1.00 41.02  ? 147 SER   A CA     1 
ATOM   1126  C  C      . SER   A 1  147 ? -32.156 -72.281  53.465  1.00 46.14  ? 147 SER   A C      1 
ATOM   1127  O  O      . SER   A 1  147 ? -32.968 -72.474  54.377  1.00 46.45  ? 147 SER   A O      1 
ATOM   1128  C  CB     . SER   A 1  147 ? -29.998 -71.132  53.945  1.00 39.94  ? 147 SER   A CB     1 
ATOM   1129  O  OG     . SER   A 1  147 ? -30.032 -70.335  52.790  1.00 42.12  ? 147 SER   A OG     1 
ATOM   1130  N  N      . GLY   A 1  148 ? -32.513 -71.919  52.225  1.00 51.95  ? 148 GLY   A N      1 
ATOM   1131  C  CA     . GLY   A 1  148 ? -33.867 -71.574  51.837  1.00 45.69  ? 148 GLY   A CA     1 
ATOM   1132  C  C      . GLY   A 1  148 ? -34.810 -72.726  51.561  1.00 45.48  ? 148 GLY   A C      1 
ATOM   1133  O  O      . GLY   A 1  148 ? -35.975 -72.645  51.943  1.00 45.22  ? 148 GLY   A O      1 
ATOM   1134  N  N      . PHE   A 1  149 ? -34.366 -73.793  50.896  1.00 41.57  ? 149 PHE   A N      1 
ATOM   1135  C  CA     . PHE   A 1  149 ? -35.302 -74.889  50.685  1.00 42.44  ? 149 PHE   A CA     1 
ATOM   1136  C  C      . PHE   A 1  149 ? -35.493 -75.744  51.934  1.00 52.29  ? 149 PHE   A C      1 
ATOM   1137  O  O      . PHE   A 1  149 ? -36.560 -76.351  52.118  1.00 50.53  ? 149 PHE   A O      1 
ATOM   1138  C  CB     . PHE   A 1  149 ? -34.874 -75.731  49.512  1.00 40.00  ? 149 PHE   A CB     1 
ATOM   1139  C  CG     . PHE   A 1  149 ? -35.812 -76.831  49.247  1.00 50.03  ? 149 PHE   A CG     1 
ATOM   1140  C  CD1    . PHE   A 1  149 ? -37.095 -76.553  48.812  1.00 52.65  ? 149 PHE   A CD1    1 
ATOM   1141  C  CD2    . PHE   A 1  149 ? -35.407 -78.145  49.353  1.00 52.84  ? 149 PHE   A CD2    1 
ATOM   1142  C  CE1    . PHE   A 1  149 ? -37.987 -77.561  48.574  1.00 51.57  ? 149 PHE   A CE1    1 
ATOM   1143  C  CE2    . PHE   A 1  149 ? -36.281 -79.168  49.089  1.00 58.98  ? 149 PHE   A CE2    1 
ATOM   1144  C  CZ     . PHE   A 1  149 ? -37.578 -78.873  48.696  1.00 62.92  ? 149 PHE   A CZ     1 
ATOM   1145  N  N      . THR   A 1  150 ? -34.488 -75.793  52.803  1.00 49.30  ? 150 THR   A N      1 
ATOM   1146  C  CA     . THR   A 1  150 ? -34.640 -76.475  54.077  1.00 48.15  ? 150 THR   A CA     1 
ATOM   1147  C  C      . THR   A 1  150 ? -35.721 -75.839  54.941  1.00 50.73  ? 150 THR   A C      1 
ATOM   1148  O  O      . THR   A 1  150 ? -36.522 -76.555  55.552  1.00 57.45  ? 150 THR   A O      1 
ATOM   1149  C  CB     . THR   A 1  150 ? -33.293 -76.501  54.795  1.00 47.03  ? 150 THR   A CB     1 
ATOM   1150  O  OG1    . THR   A 1  150 ? -32.339 -77.148  53.937  1.00 44.49  ? 150 THR   A OG1    1 
ATOM   1151  C  CG2    . THR   A 1  150 ? -33.393 -77.209  56.146  1.00 42.50  ? 150 THR   A CG2    1 
ATOM   1152  N  N      . SER   A 1  151 ? -35.765 -74.509  55.039  1.00 41.44  ? 151 SER   A N      1 
ATOM   1153  C  CA     . SER   A 1  151 ? -36.803 -73.967  55.906  1.00 44.82  ? 151 SER   A CA     1 
ATOM   1154  C  C      . SER   A 1  151 ? -38.193 -74.235  55.333  1.00 53.46  ? 151 SER   A C      1 
ATOM   1155  O  O      . SER   A 1  151 ? -39.112 -74.559  56.092  1.00 55.21  ? 151 SER   A O      1 
ATOM   1156  C  CB     . SER   A 1  151 ? -36.605 -72.474  56.174  1.00 47.65  ? 151 SER   A CB     1 
ATOM   1157  O  OG     . SER   A 1  151 ? -36.682 -71.696  54.997  1.00 49.87  ? 151 SER   A OG     1 
ATOM   1158  N  N      . LEU   A 1  152 ? -38.377 -74.125  54.011  1.00 53.28  ? 152 LEU   A N      1 
ATOM   1159  C  CA     . LEU   A 1  152 ? -39.668 -74.487  53.430  1.00 52.37  ? 152 LEU   A CA     1 
ATOM   1160  C  C      . LEU   A 1  152 ? -40.008 -75.938  53.729  1.00 50.63  ? 152 LEU   A C      1 
ATOM   1161  O  O      . LEU   A 1  152 ? -41.073 -76.229  54.281  1.00 55.10  ? 152 LEU   A O      1 
ATOM   1162  C  CB     . LEU   A 1  152 ? -39.701 -74.229  51.921  1.00 53.21  ? 152 LEU   A CB     1 
ATOM   1163  C  CG     . LEU   A 1  152 ? -41.072 -74.587  51.295  1.00 54.52  ? 152 LEU   A CG     1 
ATOM   1164  C  CD1    . LEU   A 1  152 ? -42.255 -73.880  51.979  1.00 53.93  ? 152 LEU   A CD1    1 
ATOM   1165  C  CD2    . LEU   A 1  152 ? -41.097 -74.402  49.774  1.00 50.40  ? 152 LEU   A CD2    1 
ATOM   1166  N  N      . LEU   A 1  153 ? -39.111 -76.860  53.379  1.00 46.30  ? 153 LEU   A N      1 
ATOM   1167  C  CA     . LEU   A 1  153 ? -39.331 -78.273  53.677  1.00 46.29  ? 153 LEU   A CA     1 
ATOM   1168  C  C      . LEU   A 1  153 ? -39.566 -78.535  55.165  1.00 50.45  ? 153 LEU   A C      1 
ATOM   1169  O  O      . LEU   A 1  153 ? -40.474 -79.293  55.520  1.00 50.62  ? 153 LEU   A O      1 
ATOM   1170  C  CB     . LEU   A 1  153 ? -38.156 -79.094  53.170  1.00 45.51  ? 153 LEU   A CB     1 
ATOM   1171  C  CG     . LEU   A 1  153 ? -38.351 -80.535  53.557  1.00 41.33  ? 153 LEU   A CG     1 
ATOM   1172  C  CD1    . LEU   A 1  153 ? -39.563 -81.038  52.881  1.00 46.85  ? 153 LEU   A CD1    1 
ATOM   1173  C  CD2    . LEU   A 1  153 ? -37.158 -81.287  53.067  1.00 44.63  ? 153 LEU   A CD2    1 
ATOM   1174  N  N      . MET   A 1  154 ? -38.747 -77.947  56.048  1.00 49.04  ? 154 MET   A N      1 
ATOM   1175  C  CA     . MET   A 1  154 ? -38.985 -78.071  57.481  1.00 47.71  ? 154 MET   A CA     1 
ATOM   1176  C  C      . MET   A 1  154 ? -40.402 -77.655  57.875  1.00 53.21  ? 154 MET   A C      1 
ATOM   1177  O  O      . MET   A 1  154 ? -41.081 -78.376  58.609  1.00 57.21  ? 154 MET   A O      1 
ATOM   1178  C  CB     . MET   A 1  154 ? -37.945 -77.271  58.277  1.00 48.16  ? 154 MET   A CB     1 
ATOM   1179  C  CG     . MET   A 1  154 ? -36.558 -77.902  58.425  1.00 52.46  ? 154 MET   A CG     1 
ATOM   1180  S  SD     . MET   A 1  154 ? -36.502 -79.531  59.264  1.00 53.93  ? 154 MET   A SD     1 
ATOM   1181  C  CE     . MET   A 1  154 ? -35.902 -79.037  60.880  1.00 46.83  ? 154 MET   A CE     1 
ATOM   1182  N  N      . GLU   A 1  155 ? -40.867 -76.490  57.427  1.00 56.75  ? 155 GLU   A N      1 
ATOM   1183  C  CA     . GLU   A 1  155 ? -42.215 -76.065  57.809  1.00 57.92  ? 155 GLU   A CA     1 
ATOM   1184  C  C      . GLU   A 1  155 ? -43.258 -77.096  57.394  1.00 57.63  ? 155 GLU   A C      1 
ATOM   1185  O  O      . GLU   A 1  155 ? -44.176 -77.413  58.160  1.00 61.28  ? 155 GLU   A O      1 
ATOM   1186  C  CB     . GLU   A 1  155 ? -42.578 -74.708  57.194  1.00 60.27  ? 155 GLU   A CB     1 
ATOM   1187  C  CG     . GLU   A 1  155 ? -41.805 -73.492  57.677  1.00 59.94  ? 155 GLU   A CG     1 
ATOM   1188  C  CD     . GLU   A 1  155 ? -42.481 -72.213  57.220  1.00 61.07  ? 155 GLU   A CD     1 
ATOM   1189  O  OE1    . GLU   A 1  155 ? -42.708 -72.095  55.991  1.00 65.13  ? 155 GLU   A OE1    1 
ATOM   1190  O  OE2    . GLU   A 1  155 ? -42.801 -71.352  58.088  1.00 57.91  ? 155 GLU   A OE2    1 
ATOM   1191  N  N      . ARG   A 1  156 ? -43.162 -77.600  56.161  1.00 50.22  ? 156 ARG   A N      1 
ATOM   1192  C  CA     . ARG   A 1  156 ? -44.143 -78.570  55.695  1.00 53.76  ? 156 ARG   A CA     1 
ATOM   1193  C  C      . ARG   A 1  156 ? -44.109 -79.823  56.559  1.00 60.01  ? 156 ARG   A C      1 
ATOM   1194  O  O      . ARG   A 1  156 ? -45.139 -80.251  57.090  1.00 63.19  ? 156 ARG   A O      1 
ATOM   1195  C  CB     . ARG   A 1  156 ? -43.904 -78.890  54.217  1.00 56.99  ? 156 ARG   A CB     1 
ATOM   1196  C  CG     . ARG   A 1  156 ? -44.371 -77.758  53.319  1.00 61.39  ? 156 ARG   A CG     1 
ATOM   1197  C  CD     . ARG   A 1  156 ? -45.894 -77.613  53.268  1.00 66.83  ? 156 ARG   A CD     1 
ATOM   1198  N  NE     . ARG   A 1  156 ? -46.478 -78.566  52.333  1.00 62.75  ? 156 ARG   A NE     1 
ATOM   1199  C  CZ     . ARG   A 1  156 ? -46.598 -78.316  51.036  1.00 71.15  ? 156 ARG   A CZ     1 
ATOM   1200  N  NH1    . ARG   A 1  156 ? -46.314 -77.121  50.535  1.00 69.39  ? 156 ARG   A NH1    1 
ATOM   1201  N  NH2    . ARG   A 1  156 ? -46.978 -79.293  50.218  1.00 72.17  ? 156 ARG   A NH2    1 
ATOM   1202  N  N      . LEU   A 1  157 ? -42.926 -80.417  56.731  1.00 60.86  ? 157 LEU   A N      1 
ATOM   1203  C  CA     . LEU   A 1  157 ? -42.816 -81.597  57.587  1.00 57.12  ? 157 LEU   A CA     1 
ATOM   1204  C  C      . LEU   A 1  157 ? -43.559 -81.381  58.910  1.00 52.28  ? 157 LEU   A C      1 
ATOM   1205  O  O      . LEU   A 1  157 ? -44.354 -82.224  59.326  1.00 52.67  ? 157 LEU   A O      1 
ATOM   1206  C  CB     . LEU   A 1  157 ? -41.334 -81.935  57.796  1.00 49.82  ? 157 LEU   A CB     1 
ATOM   1207  C  CG     . LEU   A 1  157 ? -40.614 -82.437  56.535  1.00 44.00  ? 157 LEU   A CG     1 
ATOM   1208  C  CD1    . LEU   A 1  157 ? -39.237 -82.949  56.832  1.00 40.86  ? 157 LEU   A CD1    1 
ATOM   1209  C  CD2    . LEU   A 1  157 ? -41.412 -83.500  55.820  1.00 49.14  ? 157 LEU   A CD2    1 
ATOM   1210  N  N      . SER   A 1  158 ? -43.370 -80.226  59.549  1.00 47.72  ? 158 SER   A N      1 
ATOM   1211  C  CA     . SER   A 1  158 ? -44.116 -79.927  60.760  1.00 47.20  ? 158 SER   A CA     1 
ATOM   1212  C  C      . SER   A 1  158 ? -45.617 -79.957  60.533  1.00 53.59  ? 158 SER   A C      1 
ATOM   1213  O  O      . SER   A 1  158 ? -46.384 -79.945  61.498  1.00 62.51  ? 158 SER   A O      1 
ATOM   1214  C  CB     . SER   A 1  158 ? -43.718 -78.560  61.307  1.00 52.61  ? 158 SER   A CB     1 
ATOM   1215  O  OG     . SER   A 1  158 ? -42.450 -78.612  61.924  1.00 60.51  ? 158 SER   A OG     1 
ATOM   1216  N  N      . VAL   A 1  159 ? -46.060 -79.975  59.287  1.00 56.10  ? 159 VAL   A N      1 
ATOM   1217  C  CA     . VAL   A 1  159 ? -47.480 -80.011  58.963  1.00 56.94  ? 159 VAL   A CA     1 
ATOM   1218  C  C      . VAL   A 1  159 ? -47.926 -81.416  58.604  1.00 53.96  ? 159 VAL   A C      1 
ATOM   1219  O  O      . VAL   A 1  159 ? -48.901 -81.921  59.155  1.00 66.18  ? 159 VAL   A O      1 
ATOM   1220  C  CB     . VAL   A 1  159 ? -47.800 -78.995  57.839  1.00 55.74  ? 159 VAL   A CB     1 
ATOM   1221  C  CG1    . VAL   A 1  159 ? -49.111 -79.299  57.217  1.00 59.40  ? 159 VAL   A CG1    1 
ATOM   1222  C  CG2    . VAL   A 1  159 ? -47.855 -77.586  58.409  1.00 51.05  ? 159 VAL   A CG2    1 
ATOM   1223  N  N      . ASP   A 1  160 ? -47.207 -82.087  57.715  1.00 49.37  ? 160 ASP   A N      1 
ATOM   1224  C  CA     . ASP   A 1  160 ? -47.611 -83.415  57.276  1.00 53.63  ? 160 ASP   A CA     1 
ATOM   1225  C  C      . ASP   A 1  160 ? -47.138 -84.532  58.206  1.00 60.89  ? 160 ASP   A C      1 
ATOM   1226  O  O      . ASP   A 1  160 ? -47.289 -85.710  57.850  1.00 59.14  ? 160 ASP   A O      1 
ATOM   1227  C  CB     . ASP   A 1  160 ? -47.086 -83.698  55.869  1.00 56.97  ? 160 ASP   A CB     1 
ATOM   1228  C  CG     . ASP   A 1  160 ? -47.570 -82.697  54.873  1.00 64.59  ? 160 ASP   A CG     1 
ATOM   1229  O  OD1    . ASP   A 1  160 ? -48.379 -81.830  55.276  1.00 65.63  ? 160 ASP   A OD1    1 
ATOM   1230  O  OD2    . ASP   A 1  160 ? -47.198 -82.820  53.686  1.00 63.46  ? 160 ASP   A OD2    1 
ATOM   1231  N  N      . TYR   A 1  161 ? -46.548 -84.189  59.366  1.00 61.33  ? 161 TYR   A N      1 
ATOM   1232  C  CA     . TYR   A 1  161 ? -45.981 -85.148  60.319  1.00 52.86  ? 161 TYR   A CA     1 
ATOM   1233  C  C      . TYR   A 1  161 ? -45.856 -84.530  61.702  1.00 51.70  ? 161 TYR   A C      1 
ATOM   1234  O  O      . TYR   A 1  161 ? -44.908 -84.835  62.421  1.00 58.03  ? 161 TYR   A O      1 
ATOM   1235  C  CB     . TYR   A 1  161 ? -44.591 -85.636  59.892  1.00 46.19  ? 161 TYR   A CB     1 
ATOM   1236  C  CG     . TYR   A 1  161 ? -44.526 -86.291  58.540  1.00 51.19  ? 161 TYR   A CG     1 
ATOM   1237  C  CD1    . TYR   A 1  161 ? -44.439 -85.540  57.385  1.00 54.36  ? 161 TYR   A CD1    1 
ATOM   1238  C  CD2    . TYR   A 1  161 ? -44.558 -87.659  58.413  1.00 55.49  ? 161 TYR   A CD2    1 
ATOM   1239  C  CE1    . TYR   A 1  161 ? -44.398 -86.139  56.156  1.00 52.00  ? 161 TYR   A CE1    1 
ATOM   1240  C  CE2    . TYR   A 1  161 ? -44.516 -88.255  57.180  1.00 48.69  ? 161 TYR   A CE2    1 
ATOM   1241  C  CZ     . TYR   A 1  161 ? -44.436 -87.492  56.066  1.00 50.06  ? 161 TYR   A CZ     1 
ATOM   1242  O  OH     . TYR   A 1  161 ? -44.371 -88.105  54.842  1.00 65.41  ? 161 TYR   A OH     1 
ATOM   1243  N  N      . GLY   A 1  162 ? -46.775 -83.665  62.089  1.00 47.93  ? 162 GLY   A N      1 
ATOM   1244  C  CA     . GLY   A 1  162 ? -46.659 -82.990  63.370  1.00 53.22  ? 162 GLY   A CA     1 
ATOM   1245  C  C      . GLY   A 1  162 ? -46.216 -83.835  64.551  1.00 57.37  ? 162 GLY   A C      1 
ATOM   1246  O  O      . GLY   A 1  162 ? -45.725 -83.293  65.547  1.00 61.67  ? 162 GLY   A O      1 
ATOM   1247  N  N      . LYS   A 1  163 ? -46.368 -85.161  64.457  1.00 62.40  ? 163 LYS   A N      1 
ATOM   1248  C  CA     . LYS   A 1  163 ? -46.098 -86.069  65.571  1.00 65.76  ? 163 LYS   A CA     1 
ATOM   1249  C  C      . LYS   A 1  163 ? -44.680 -86.650  65.568  1.00 66.73  ? 163 LYS   A C      1 
ATOM   1250  O  O      . LYS   A 1  163 ? -44.282 -87.295  66.552  1.00 66.47  ? 163 LYS   A O      1 
ATOM   1251  C  CB     . LYS   A 1  163 ? -47.130 -87.209  65.581  1.00 55.47  ? 163 LYS   A CB     1 
ATOM   1252  N  N      . LYS   A 1  164 ? -43.901 -86.421  64.516  1.00 61.01  ? 164 LYS   A N      1 
ATOM   1253  C  CA     . LYS   A 1  164 ? -42.578 -87.013  64.400  1.00 58.01  ? 164 LYS   A CA     1 
ATOM   1254  C  C      . LYS   A 1  164 ? -41.498 -85.995  64.741  1.00 57.58  ? 164 LYS   A C      1 
ATOM   1255  O  O      . LYS   A 1  164 ? -41.741 -84.788  64.809  1.00 57.80  ? 164 LYS   A O      1 
ATOM   1256  C  CB     . LYS   A 1  164 ? -42.368 -87.592  62.996  1.00 54.25  ? 164 LYS   A CB     1 
ATOM   1257  C  CG     . LYS   A 1  164 ? -43.676 -87.975  62.333  1.00 60.02  ? 164 LYS   A CG     1 
ATOM   1258  C  CD     . LYS   A 1  164 ? -44.442 -89.027  63.147  1.00 62.91  ? 164 LYS   A CD     1 
ATOM   1259  C  CE     . LYS   A 1  164 ? -45.903 -89.147  62.671  1.00 70.17  ? 164 LYS   A CE     1 
ATOM   1260  N  NZ     . LYS   A 1  164 ? -46.752 -87.886  62.879  1.00 60.65  ? 164 LYS   A NZ     1 
ATOM   1261  N  N      . SER   A 1  165 ? -40.300 -86.512  64.994  1.00 55.01  ? 165 SER   A N      1 
ATOM   1262  C  CA     . SER   A 1  165 ? -39.180 -85.687  65.408  1.00 57.29  ? 165 SER   A CA     1 
ATOM   1263  C  C      . SER   A 1  165 ? -38.371 -85.242  64.198  1.00 59.97  ? 165 SER   A C      1 
ATOM   1264  O  O      . SER   A 1  165 ? -38.191 -85.999  63.229  1.00 55.50  ? 165 SER   A O      1 
ATOM   1265  C  CB     . SER   A 1  165 ? -38.276 -86.446  66.376  1.00 57.98  ? 165 SER   A CB     1 
ATOM   1266  O  OG     . SER   A 1  165 ? -38.717 -86.261  67.698  1.00 56.82  ? 165 SER   A OG     1 
ATOM   1267  N  N      . LYS   A 1  166 ? -37.880 -84.006  64.262  1.00 55.81  ? 166 LYS   A N      1 
ATOM   1268  C  CA     . LYS   A 1  166 ? -37.008 -83.451  63.233  1.00 57.83  ? 166 LYS   A CA     1 
ATOM   1269  C  C      . LYS   A 1  166 ? -35.661 -83.092  63.857  1.00 50.86  ? 166 LYS   A C      1 
ATOM   1270  O  O      . LYS   A 1  166 ? -35.590 -82.259  64.768  1.00 49.75  ? 166 LYS   A O      1 
ATOM   1271  C  CB     . LYS   A 1  166 ? -37.674 -82.243  62.554  1.00 57.10  ? 166 LYS   A CB     1 
ATOM   1272  C  CG     . LYS   A 1  166 ? -39.026 -82.562  61.890  1.00 53.99  ? 166 LYS   A CG     1 
ATOM   1273  C  CD     . LYS   A 1  166 ? -39.651 -81.334  61.249  1.00 47.47  ? 166 LYS   A CD     1 
ATOM   1274  C  CE     . LYS   A 1  166 ? -41.045 -81.239  61.783  1.00 55.03  ? 166 LYS   A CE     1 
ATOM   1275  N  NZ     . LYS   A 1  166 ? -40.992 -81.188  63.296  1.00 60.77  ? 166 LYS   A NZ     1 
ATOM   1276  N  N      . LEU   A 1  167 ? -34.606 -83.737  63.377  1.00 44.97  ? 167 LEU   A N      1 
ATOM   1277  C  CA     . LEU   A 1  167 ? -33.244 -83.457  63.790  1.00 46.57  ? 167 LEU   A CA     1 
ATOM   1278  C  C      . LEU   A 1  167 ? -32.444 -82.849  62.632  1.00 52.81  ? 167 LEU   A C      1 
ATOM   1279  O  O      . LEU   A 1  167 ? -32.657 -83.182  61.458  1.00 51.64  ? 167 LEU   A O      1 
ATOM   1280  C  CB     . LEU   A 1  167 ? -32.575 -84.744  64.273  1.00 45.88  ? 167 LEU   A CB     1 
ATOM   1281  C  CG     . LEU   A 1  167 ? -32.721 -85.107  65.745  1.00 52.06  ? 167 LEU   A CG     1 
ATOM   1282  C  CD1    . LEU   A 1  167 ? -34.171 -85.394  66.096  1.00 54.55  ? 167 LEU   A CD1    1 
ATOM   1283  C  CD2    . LEU   A 1  167 ? -31.864 -86.303  66.025  1.00 49.38  ? 167 LEU   A CD2    1 
ATOM   1284  N  N      . GLU   A 1  168 ? -31.493 -81.968  62.965  1.00 49.56  ? 168 GLU   A N      1 
ATOM   1285  C  CA     . GLU   A 1  168 ? -30.691 -81.267  61.968  1.00 48.53  ? 168 GLU   A CA     1 
ATOM   1286  C  C      . GLU   A 1  168 ? -29.198 -81.480  62.154  1.00 47.06  ? 168 GLU   A C      1 
ATOM   1287  O  O      . GLU   A 1  168 ? -28.666 -81.337  63.259  1.00 44.76  ? 168 GLU   A O      1 
ATOM   1288  C  CB     . GLU   A 1  168 ? -30.903 -79.790  62.041  1.00 49.21  ? 168 GLU   A CB     1 
ATOM   1289  C  CG     . GLU   A 1  168 ? -32.050 -79.247  61.300  1.00 48.70  ? 168 GLU   A CG     1 
ATOM   1290  C  CD     . GLU   A 1  168 ? -32.050 -77.761  61.450  1.00 47.99  ? 168 GLU   A CD     1 
ATOM   1291  O  OE1    . GLU   A 1  168 ? -32.200 -77.290  62.596  1.00 53.05  ? 168 GLU   A OE1    1 
ATOM   1292  O  OE2    . GLU   A 1  168 ? -31.861 -77.055  60.454  1.00 44.10  ? 168 GLU   A OE2    1 
ATOM   1293  N  N      . PHE   A 1  169 ? -28.518 -81.725  61.047  1.00 44.76  ? 169 PHE   A N      1 
ATOM   1294  C  CA     . PHE   A 1  169 ? -27.065 -81.633  60.961  1.00 41.78  ? 169 PHE   A CA     1 
ATOM   1295  C  C      . PHE   A 1  169 ? -26.771 -80.481  60.000  1.00 42.62  ? 169 PHE   A C      1 
ATOM   1296  O  O      . PHE   A 1  169 ? -26.882 -80.649  58.782  1.00 39.41  ? 169 PHE   A O      1 
ATOM   1297  C  CB     . PHE   A 1  169 ? -26.474 -82.945  60.474  1.00 43.54  ? 169 PHE   A CB     1 
ATOM   1298  C  CG     . PHE   A 1  169 ? -26.623 -84.063  61.458  1.00 50.87  ? 169 PHE   A CG     1 
ATOM   1299  C  CD1    . PHE   A 1  169 ? -25.800 -84.147  62.569  1.00 44.55  ? 169 PHE   A CD1    1 
ATOM   1300  C  CD2    . PHE   A 1  169 ? -27.617 -85.022  61.285  1.00 49.36  ? 169 PHE   A CD2    1 
ATOM   1301  C  CE1    . PHE   A 1  169 ? -25.961 -85.161  63.478  1.00 44.91  ? 169 PHE   A CE1    1 
ATOM   1302  C  CE2    . PHE   A 1  169 ? -27.771 -86.048  62.189  1.00 47.34  ? 169 PHE   A CE2    1 
ATOM   1303  C  CZ     . PHE   A 1  169 ? -26.944 -86.120  63.286  1.00 43.77  ? 169 PHE   A CZ     1 
ATOM   1304  N  N      . SER   A 1  170 ? -26.417 -79.314  60.543  1.00 40.39  ? 170 SER   A N      1 
ATOM   1305  C  CA     . SER   A 1  170 ? -26.257 -78.080  59.777  1.00 37.70  ? 170 SER   A CA     1 
ATOM   1306  C  C      . SER   A 1  170 ? -24.793 -77.679  59.684  1.00 32.92  ? 170 SER   A C      1 
ATOM   1307  O  O      . SER   A 1  170 ? -24.115 -77.615  60.705  1.00 36.14  ? 170 SER   A O      1 
ATOM   1308  C  CB     . SER   A 1  170 ? -27.013 -76.933  60.439  1.00 37.92  ? 170 SER   A CB     1 
ATOM   1309  O  OG     . SER   A 1  170 ? -28.306 -77.310  60.851  1.00 44.38  ? 170 SER   A OG     1 
ATOM   1310  N  N      . ILE   A 1  171 ? -24.325 -77.318  58.491  1.00 34.62  ? 171 ILE   A N      1 
ATOM   1311  C  CA     . ILE   A 1  171 ? -22.957 -76.815  58.333  1.00 36.58  ? 171 ILE   A CA     1 
ATOM   1312  C  C      . ILE   A 1  171 ? -22.940 -75.300  58.527  1.00 35.86  ? 171 ILE   A C      1 
ATOM   1313  O  O      . ILE   A 1  171 ? -23.546 -74.558  57.748  1.00 45.61  ? 171 ILE   A O      1 
ATOM   1314  C  CB     . ILE   A 1  171 ? -22.369 -77.170  56.964  1.00 30.95  ? 171 ILE   A CB     1 
ATOM   1315  C  CG1    . ILE   A 1  171 ? -22.391 -78.682  56.724  1.00 32.18  ? 171 ILE   A CG1    1 
ATOM   1316  C  CG2    . ILE   A 1  171 ? -20.956 -76.648  56.927  1.00 30.24  ? 171 ILE   A CG2    1 
ATOM   1317  C  CD1    . ILE   A 1  171 ? -21.935 -79.536  57.880  1.00 30.46  ? 171 ILE   A CD1    1 
ATOM   1318  N  N      . TYR   A 1  172 ? -22.244 -74.850  59.492  1.00 32.48  ? 172 TYR   A N      1 
ATOM   1319  C  CA     . TYR   A 1  172 ? -22.122 -73.425  59.779  1.00 33.51  ? 172 TYR   A CA     1 
ATOM   1320  C  C      . TYR   A 1  172 ? -20.971 -72.812  58.970  1.00 36.53  ? 172 TYR   A C      1 
ATOM   1321  O  O      . TYR   A 1  172 ? -19.948 -73.468  58.735  1.00 34.85  ? 172 TYR   A O      1 
ATOM   1322  C  CB     . TYR   A 1  172 ? -21.909 -73.226  61.274  1.00 33.06  ? 172 TYR   A CB     1 
ATOM   1323  C  CG     . TYR   A 1  172 ? -21.624 -71.838  61.802  1.00 31.67  ? 172 TYR   A CG     1 
ATOM   1324  C  CD1    . TYR   A 1  172 ? -20.353 -71.290  61.684  1.00 31.19  ? 172 TYR   A CD1    1 
ATOM   1325  C  CD2    . TYR   A 1  172 ? -22.575 -71.135  62.550  1.00 28.84  ? 172 TYR   A CD2    1 
ATOM   1326  C  CE1    . TYR   A 1  172 ? -20.046 -70.056  62.228  1.00 34.40  ? 172 TYR   A CE1    1 
ATOM   1327  C  CE2    . TYR   A 1  172 ? -22.272 -69.887  63.119  1.00 29.08  ? 172 TYR   A CE2    1 
ATOM   1328  C  CZ     . TYR   A 1  172 ? -20.998 -69.352  62.945  1.00 33.42  ? 172 TYR   A CZ     1 
ATOM   1329  O  OH     . TYR   A 1  172 ? -20.643 -68.120  63.467  1.00 32.23  ? 172 TYR   A OH     1 
ATOM   1330  N  N      . PRO   A 1  173 ? -21.133 -71.544  58.511  1.00 35.31  ? 173 PRO   A N      1 
ATOM   1331  C  CA     . PRO   A 1  173 ? -20.311 -71.025  57.411  1.00 30.66  ? 173 PRO   A CA     1 
ATOM   1332  C  C      . PRO   A 1  173 ? -18.924 -70.550  57.799  1.00 33.57  ? 173 PRO   A C      1 
ATOM   1333  O  O      . PRO   A 1  173 ? -18.748 -69.714  58.690  1.00 37.07  ? 173 PRO   A O      1 
ATOM   1334  C  CB     . PRO   A 1  173 ? -21.140 -69.848  56.910  1.00 30.09  ? 173 PRO   A CB     1 
ATOM   1335  C  CG     . PRO   A 1  173 ? -21.753 -69.346  58.139  1.00 34.31  ? 173 PRO   A CG     1 
ATOM   1336  C  CD     . PRO   A 1  173 ? -22.124 -70.545  58.949  1.00 36.49  ? 173 PRO   A CD     1 
ATOM   1337  N  N      . ALA   A 1  174 ? -17.923 -71.050  57.095  1.00 37.68  ? 174 ALA   A N      1 
ATOM   1338  C  CA     . ALA   A 1  174 ? -16.570 -70.684  57.385  1.00 40.21  ? 174 ALA   A CA     1 
ATOM   1339  C  C      . ALA   A 1  174 ? -15.946 -70.088  56.142  1.00 42.11  ? 174 ALA   A C      1 
ATOM   1340  O  O      . ALA   A 1  174 ? -16.017 -70.698  55.067  1.00 42.31  ? 174 ALA   A O      1 
ATOM   1341  C  CB     . ALA   A 1  174 ? -15.743 -71.897  57.853  1.00 41.34  ? 174 ALA   A CB     1 
ATOM   1342  N  N      . PRO   A 1  175 ? -15.345 -68.906  56.251  1.00 44.90  ? 175 PRO   A N      1 
ATOM   1343  C  CA     . PRO   A 1  175 ? -14.747 -68.261  55.074  1.00 43.29  ? 175 PRO   A CA     1 
ATOM   1344  C  C      . PRO   A 1  175 ? -13.616 -69.023  54.409  1.00 44.60  ? 175 PRO   A C      1 
ATOM   1345  O  O      . PRO   A 1  175 ? -13.473 -68.859  53.197  1.00 51.11  ? 175 PRO   A O      1 
ATOM   1346  C  CB     . PRO   A 1  175 ? -14.281 -66.907  55.623  1.00 40.96  ? 175 PRO   A CB     1 
ATOM   1347  C  CG     . PRO   A 1  175 ? -15.276 -66.641  56.730  1.00 39.47  ? 175 PRO   A CG     1 
ATOM   1348  C  CD     . PRO   A 1  175 ? -15.510 -67.969  57.375  1.00 42.84  ? 175 PRO   A CD     1 
ATOM   1349  N  N      . GLN   A 1  176 ? -12.798 -69.833  55.101  1.00 46.96  ? 176 GLN   A N      1 
ATOM   1350  C  CA     . GLN   A 1  176 ? -11.784 -70.575  54.340  1.00 45.36  ? 176 GLN   A CA     1 
ATOM   1351  C  C      . GLN   A 1  176 ? -12.428 -71.416  53.260  1.00 51.93  ? 176 GLN   A C      1 
ATOM   1352  O  O      . GLN   A 1  176 ? -11.982 -71.404  52.110  1.00 56.74  ? 176 GLN   A O      1 
ATOM   1353  C  CB     . GLN   A 1  176 ? -10.896 -71.471  55.210  1.00 43.47  ? 176 GLN   A CB     1 
ATOM   1354  C  CG     . GLN   A 1  176 ? -9.892  -70.754  56.078  1.00 48.92  ? 176 GLN   A CG     1 
ATOM   1355  C  CD     . GLN   A 1  176 ? -10.474 -70.340  57.406  1.00 70.04  ? 176 GLN   A CD     1 
ATOM   1356  O  OE1    . GLN   A 1  176 ? -11.707 -70.129  57.550  1.00 66.58  ? 176 GLN   A OE1    1 
ATOM   1357  N  NE2    . GLN   A 1  176 ? -9.600  -70.246  58.409  1.00 73.76  ? 176 GLN   A NE2    1 
ATOM   1358  N  N      . VAL   A 1  177 ? -13.501 -72.127  53.595  1.00 51.20  ? 177 VAL   A N      1 
ATOM   1359  C  CA     . VAL   A 1  177 ? -14.106 -73.039  52.653  1.00 47.46  ? 177 VAL   A CA     1 
ATOM   1360  C  C      . VAL   A 1  177 ? -15.284 -72.418  51.905  1.00 51.94  ? 177 VAL   A C      1 
ATOM   1361  O  O      . VAL   A 1  177 ? -15.821 -73.058  50.984  1.00 61.73  ? 177 VAL   A O      1 
ATOM   1362  C  CB     . VAL   A 1  177 ? -14.500 -74.324  53.402  1.00 46.88  ? 177 VAL   A CB     1 
ATOM   1363  C  CG1    . VAL   A 1  177 ? -13.252 -75.031  53.874  1.00 37.43  ? 177 VAL   A CG1    1 
ATOM   1364  C  CG2    . VAL   A 1  177 ? -15.313 -73.960  54.605  1.00 52.57  ? 177 VAL   A CG2    1 
ATOM   1365  N  N      . SER   A 1  178 ? -15.659 -71.167  52.215  1.00 51.99  ? 178 SER   A N      1 
ATOM   1366  C  CA     . SER   A 1  178 ? -16.982 -70.660  51.831  1.00 58.14  ? 178 SER   A CA     1 
ATOM   1367  C  C      . SER   A 1  178 ? -17.048 -70.353  50.360  1.00 54.80  ? 178 SER   A C      1 
ATOM   1368  O  O      . SER   A 1  178 ? -16.090 -69.869  49.764  1.00 62.19  ? 178 SER   A O      1 
ATOM   1369  C  CB     . SER   A 1  178 ? -17.367 -69.369  52.545  1.00 58.57  ? 178 SER   A CB     1 
ATOM   1370  O  OG     . SER   A 1  178 ? -16.647 -68.287  51.986  1.00 66.53  ? 178 SER   A OG     1 
ATOM   1371  N  N      . THR   A 1  179 ? -18.231 -70.549  49.803  1.00 62.81  ? 179 THR   A N      1 
ATOM   1372  C  CA     . THR   A 1  179 ? -18.468 -70.295  48.390  1.00 80.51  ? 179 THR   A CA     1 
ATOM   1373  C  C      . THR   A 1  179 ? -19.076 -68.914  48.135  1.00 77.65  ? 179 THR   A C      1 
ATOM   1374  O  O      . THR   A 1  179 ? -19.383 -68.602  46.974  1.00 73.49  ? 179 THR   A O      1 
ATOM   1375  C  CB     . THR   A 1  179 ? -19.384 -71.393  47.793  1.00 69.89  ? 179 THR   A CB     1 
ATOM   1376  O  OG1    . THR   A 1  179 ? -20.675 -71.350  48.417  1.00 63.47  ? 179 THR   A OG1    1 
ATOM   1377  C  CG2    . THR   A 1  179 ? -18.784 -72.796  48.012  1.00 60.32  ? 179 THR   A CG2    1 
ATOM   1378  N  N      . ALA   A 1  180 ? -19.261 -68.081  49.172  1.00 58.13  ? 180 ALA   A N      1 
ATOM   1379  C  CA     . ALA   A 1  180 ? -20.177 -66.963  49.008  1.00 48.38  ? 180 ALA   A CA     1 
ATOM   1380  C  C      . ALA   A 1  180 ? -19.989 -65.946  50.107  1.00 54.21  ? 180 ALA   A C      1 
ATOM   1381  O  O      . ALA   A 1  180 ? -19.503 -66.253  51.198  1.00 63.20  ? 180 ALA   A O      1 
ATOM   1382  C  CB     . ALA   A 1  180 ? -21.634 -67.425  49.006  1.00 49.65  ? 180 ALA   A CB     1 
ATOM   1383  N  N      . VAL   A 1  181 ? -20.458 -64.737  49.810  1.00 46.77  ? 181 VAL   A N      1 
ATOM   1384  C  CA     . VAL   A 1  181 ? -20.315 -63.573  50.677  1.00 42.94  ? 181 VAL   A CA     1 
ATOM   1385  C  C      . VAL   A 1  181 ? -21.607 -63.269  51.431  1.00 40.56  ? 181 VAL   A C      1 
ATOM   1386  O  O      . VAL   A 1  181 ? -21.576 -62.562  52.457  1.00 34.79  ? 181 VAL   A O      1 
ATOM   1387  C  CB     . VAL   A 1  181 ? -19.853 -62.366  49.824  1.00 42.22  ? 181 VAL   A CB     1 
ATOM   1388  C  CG1    . VAL   A 1  181 ? -20.943 -61.995  48.823  1.00 43.69  ? 181 VAL   A CG1    1 
ATOM   1389  C  CG2    . VAL   A 1  181 ? -19.487 -61.165  50.683  1.00 37.45  ? 181 VAL   A CG2    1 
ATOM   1390  N  N      . VAL   A 1  182 ? -22.733 -63.795  50.965  1.00 42.66  ? 182 VAL   A N      1 
ATOM   1391  C  CA     . VAL   A 1  182 ? -24.024 -63.537  51.562  1.00 40.50  ? 182 VAL   A CA     1 
ATOM   1392  C  C      . VAL   A 1  182 ? -24.432 -64.662  52.507  1.00 42.02  ? 182 VAL   A C      1 
ATOM   1393  O  O      . VAL   A 1  182 ? -25.598 -64.758  52.877  1.00 43.15  ? 182 VAL   A O      1 
ATOM   1394  C  CB     . VAL   A 1  182 ? -25.104 -63.283  50.493  1.00 35.71  ? 182 VAL   A CB     1 
ATOM   1395  C  CG1    . VAL   A 1  182 ? -24.840 -61.971  49.820  1.00 36.41  ? 182 VAL   A CG1    1 
ATOM   1396  C  CG2    . VAL   A 1  182 ? -25.054 -64.343  49.431  1.00 30.44  ? 182 VAL   A CG2    1 
ATOM   1397  N  N      . GLU   A 1  183 ? -23.490 -65.509  52.918  1.00 43.81  ? 183 GLU   A N      1 
ATOM   1398  C  CA     . GLU   A 1  183 ? -23.880 -66.671  53.714  1.00 44.10  ? 183 GLU   A CA     1 
ATOM   1399  C  C      . GLU   A 1  183 ? -24.404 -66.257  55.085  1.00 41.34  ? 183 GLU   A C      1 
ATOM   1400  O  O      . GLU   A 1  183 ? -25.245 -66.970  55.642  1.00 40.60  ? 183 GLU   A O      1 
ATOM   1401  C  CB     . GLU   A 1  183 ? -22.714 -67.652  53.827  1.00 40.14  ? 183 GLU   A CB     1 
ATOM   1402  C  CG     . GLU   A 1  183 ? -22.465 -68.365  52.514  1.00 43.40  ? 183 GLU   A CG     1 
ATOM   1403  C  CD     . GLU   A 1  183 ? -21.428 -69.473  52.605  1.00 59.96  ? 183 GLU   A CD     1 
ATOM   1404  O  OE1    . GLU   A 1  183 ? -21.575 -70.408  53.431  1.00 49.84  ? 183 GLU   A OE1    1 
ATOM   1405  O  OE2    . GLU   A 1  183 ? -20.420 -69.374  51.855  1.00 70.67  ? 183 GLU   A OE2    1 
ATOM   1406  N  N      . PRO   A 1  184 ? -23.968 -65.119  55.650  1.00 38.52  ? 184 PRO   A N      1 
ATOM   1407  C  CA     . PRO   A 1  184 ? -24.544 -64.684  56.936  1.00 40.13  ? 184 PRO   A CA     1 
ATOM   1408  C  C      . PRO   A 1  184 ? -26.008 -64.311  56.813  1.00 44.16  ? 184 PRO   A C      1 
ATOM   1409  O  O      . PRO   A 1  184 ? -26.770 -64.423  57.785  1.00 46.15  ? 184 PRO   A O      1 
ATOM   1410  C  CB     . PRO   A 1  184 ? -23.700 -63.456  57.315  1.00 31.77  ? 184 PRO   A CB     1 
ATOM   1411  C  CG     . PRO   A 1  184 ? -22.461 -63.634  56.601  1.00 36.18  ? 184 PRO   A CG     1 
ATOM   1412  C  CD     . PRO   A 1  184 ? -22.817 -64.285  55.285  1.00 32.69  ? 184 PRO   A CD     1 
ATOM   1413  N  N      . TYR   A 1  185 ? -26.428 -63.832  55.643  1.00 42.27  ? 185 TYR   A N      1 
ATOM   1414  C  CA     . TYR   A 1  185 ? -27.841 -63.543  55.474  1.00 44.28  ? 185 TYR   A CA     1 
ATOM   1415  C  C      . TYR   A 1  185 ? -28.647 -64.836  55.476  1.00 43.91  ? 185 TYR   A C      1 
ATOM   1416  O  O      . TYR   A 1  185 ? -29.709 -64.913  56.101  1.00 40.94  ? 185 TYR   A O      1 
ATOM   1417  C  CB     . TYR   A 1  185 ? -28.075 -62.764  54.181  1.00 39.95  ? 185 TYR   A CB     1 
ATOM   1418  C  CG     . TYR   A 1  185 ? -27.759 -61.284  54.227  1.00 39.40  ? 185 TYR   A CG     1 
ATOM   1419  C  CD1    . TYR   A 1  185 ? -27.420 -60.659  55.408  1.00 39.78  ? 185 TYR   A CD1    1 
ATOM   1420  C  CD2    . TYR   A 1  185 ? -27.869 -60.497  53.077  1.00 41.51  ? 185 TYR   A CD2    1 
ATOM   1421  C  CE1    . TYR   A 1  185 ? -27.150 -59.285  55.435  1.00 46.63  ? 185 TYR   A CE1    1 
ATOM   1422  C  CE2    . TYR   A 1  185 ? -27.611 -59.136  53.093  1.00 34.85  ? 185 TYR   A CE2    1 
ATOM   1423  C  CZ     . TYR   A 1  185 ? -27.251 -58.529  54.270  1.00 41.54  ? 185 TYR   A CZ     1 
ATOM   1424  O  OH     . TYR   A 1  185 ? -26.988 -57.173  54.282  1.00 38.31  ? 185 TYR   A OH     1 
ATOM   1425  N  N      . ASN   A 1  186 ? -28.144 -65.872  54.803  1.00 42.74  ? 186 ASN   A N      1 
ATOM   1426  C  CA     . ASN   A 1  186 ? -28.920 -67.094  54.669  1.00 40.56  ? 186 ASN   A CA     1 
ATOM   1427  C  C      . ASN   A 1  186 ? -29.005 -67.822  55.990  1.00 40.46  ? 186 ASN   A C      1 
ATOM   1428  O  O      . ASN   A 1  186 ? -30.036 -68.419  56.307  1.00 41.23  ? 186 ASN   A O      1 
ATOM   1429  C  CB     . ASN   A 1  186 ? -28.302 -68.015  53.625  1.00 41.51  ? 186 ASN   A CB     1 
ATOM   1430  C  CG     . ASN   A 1  186 ? -28.175 -67.368  52.274  1.00 43.85  ? 186 ASN   A CG     1 
ATOM   1431  O  OD1    . ASN   A 1  186 ? -28.858 -66.388  51.961  1.00 42.45  ? 186 ASN   A OD1    1 
ATOM   1432  N  ND2    . ASN   A 1  186 ? -27.320 -67.944  51.437  1.00 42.86  ? 186 ASN   A ND2    1 
ATOM   1433  N  N      . SER   A 1  187 ? -27.909 -67.816  56.750  1.00 44.03  ? 187 SER   A N      1 
ATOM   1434  C  CA     . SER   A 1  187 ? -27.890 -68.447  58.068  1.00 45.07  ? 187 SER   A CA     1 
ATOM   1435  C  C      . SER   A 1  187 ? -28.982 -67.878  58.970  1.00 44.46  ? 187 SER   A C      1 
ATOM   1436  O  O      . SER   A 1  187 ? -29.818 -68.623  59.497  1.00 45.66  ? 187 SER   A O      1 
ATOM   1437  C  CB     . SER   A 1  187 ? -26.511 -68.272  58.709  1.00 44.74  ? 187 SER   A CB     1 
ATOM   1438  O  OG     . SER   A 1  187 ? -25.472 -68.700  57.843  1.00 44.37  ? 187 SER   A OG     1 
ATOM   1439  N  N      . ILE   A 1  188 ? -29.003 -66.555  59.152  1.00 42.28  ? 188 ILE   A N      1 
ATOM   1440  C  CA     . ILE   A 1  188 ? -30.019 -65.955  60.009  1.00 41.65  ? 188 ILE   A CA     1 
ATOM   1441  C  C      . ILE   A 1  188 ? -31.414 -66.192  59.443  1.00 41.00  ? 188 ILE   A C      1 
ATOM   1442  O  O      . ILE   A 1  188 ? -32.340 -66.540  60.175  1.00 44.35  ? 188 ILE   A O      1 
ATOM   1443  C  CB     . ILE   A 1  188 ? -29.743 -64.459  60.204  1.00 42.79  ? 188 ILE   A CB     1 
ATOM   1444  C  CG1    . ILE   A 1  188 ? -28.846 -64.249  61.417  1.00 43.00  ? 188 ILE   A CG1    1 
ATOM   1445  C  CG2    . ILE   A 1  188 ? -31.052 -63.728  60.390  1.00 42.69  ? 188 ILE   A CG2    1 
ATOM   1446  C  CD1    . ILE   A 1  188 ? -27.502 -64.917  61.283  1.00 42.19  ? 188 ILE   A CD1    1 
ATOM   1447  N  N      . LEU   A 1  189 ? -31.595 -66.012  58.139  1.00 42.68  ? 189 LEU   A N      1 
ATOM   1448  C  CA     . LEU   A 1  189 ? -32.926 -66.203  57.576  1.00 49.11  ? 189 LEU   A CA     1 
ATOM   1449  C  C      . LEU   A 1  189 ? -33.433 -67.613  57.840  1.00 46.88  ? 189 LEU   A C      1 
ATOM   1450  O  O      . LEU   A 1  189 ? -34.589 -67.798  58.236  1.00 50.21  ? 189 LEU   A O      1 
ATOM   1451  C  CB     . LEU   A 1  189 ? -32.946 -65.906  56.066  1.00 50.45  ? 189 LEU   A CB     1 
ATOM   1452  C  CG     . LEU   A 1  189 ? -32.795 -64.446  55.604  1.00 44.30  ? 189 LEU   A CG     1 
ATOM   1453  C  CD1    . LEU   A 1  189 ? -32.895 -64.334  54.084  1.00 43.67  ? 189 LEU   A CD1    1 
ATOM   1454  C  CD2    . LEU   A 1  189 ? -33.727 -63.475  56.332  1.00 45.88  ? 189 LEU   A CD2    1 
ATOM   1455  N  N      . THR   A 1  190 ? -32.581 -68.619  57.631  1.00 45.21  ? 190 THR   A N      1 
ATOM   1456  C  CA     . THR   A 1  190 ? -32.999 -70.011  57.743  1.00 43.97  ? 190 THR   A CA     1 
ATOM   1457  C  C      . THR   A 1  190 ? -33.156 -70.465  59.186  1.00 46.53  ? 190 THR   A C      1 
ATOM   1458  O  O      . THR   A 1  190 ? -34.010 -71.317  59.478  1.00 47.87  ? 190 THR   A O      1 
ATOM   1459  C  CB     . THR   A 1  190 ? -32.005 -70.910  57.022  1.00 41.94  ? 190 THR   A CB     1 
ATOM   1460  O  OG1    . THR   A 1  190 ? -32.592 -72.198  56.825  1.00 44.63  ? 190 THR   A OG1    1 
ATOM   1461  C  CG2    . THR   A 1  190 ? -30.736 -71.033  57.821  1.00 40.54  ? 190 THR   A CG2    1 
ATOM   1462  N  N      . THR   A 1  191 ? -32.369 -69.919  60.105  1.00 41.80  ? 191 THR   A N      1 
ATOM   1463  C  CA     . THR   A 1  191 ? -32.546 -70.340  61.487  1.00 48.39  ? 191 THR   A CA     1 
ATOM   1464  C  C      . THR   A 1  191 ? -33.868 -69.834  62.047  1.00 51.38  ? 191 THR   A C      1 
ATOM   1465  O  O      . THR   A 1  191 ? -34.621 -70.602  62.663  1.00 50.66  ? 191 THR   A O      1 
ATOM   1466  C  CB     . THR   A 1  191 ? -31.347 -69.903  62.332  1.00 44.44  ? 191 THR   A CB     1 
ATOM   1467  O  OG1    . THR   A 1  191 ? -30.209 -70.703  61.971  1.00 40.09  ? 191 THR   A OG1    1 
ATOM   1468  C  CG2    . THR   A 1  191 ? -31.631 -70.021  63.820  1.00 42.90  ? 191 THR   A CG2    1 
ATOM   1469  N  N      . HIS   A 1  192 ? -34.179 -68.556  61.818  1.00 50.70  ? 192 HIS   A N      1 
ATOM   1470  C  CA     . HIS   A 1  192 ? -35.430 -67.986  62.311  1.00 48.04  ? 192 HIS   A CA     1 
ATOM   1471  C  C      . HIS   A 1  192 ? -36.650 -68.737  61.790  1.00 47.33  ? 192 HIS   A C      1 
ATOM   1472  O  O      . HIS   A 1  192 ? -37.611 -68.980  62.527  1.00 53.51  ? 192 HIS   A O      1 
ATOM   1473  C  CB     . HIS   A 1  192 ? -35.502 -66.523  61.917  1.00 47.79  ? 192 HIS   A CB     1 
ATOM   1474  C  CG     . HIS   A 1  192 ? -36.894 -66.001  61.860  1.00 54.18  ? 192 HIS   A CG     1 
ATOM   1475  N  ND1    . HIS   A 1  192 ? -37.732 -66.005  62.953  1.00 54.14  ? 192 HIS   A ND1    1 
ATOM   1476  C  CD2    . HIS   A 1  192 ? -37.602 -65.468  60.837  1.00 57.79  ? 192 HIS   A CD2    1 
ATOM   1477  C  CE1    . HIS   A 1  192 ? -38.893 -65.480  62.609  1.00 60.00  ? 192 HIS   A CE1    1 
ATOM   1478  N  NE2    . HIS   A 1  192 ? -38.842 -65.148  61.330  1.00 61.76  ? 192 HIS   A NE2    1 
ATOM   1479  N  N      . THR   A 1  193 ? -36.638 -69.100  60.529  1.00 46.92  ? 193 THR   A N      1 
ATOM   1480  C  CA     . THR   A 1  193 ? -37.762 -69.807  59.951  1.00 46.88  ? 193 THR   A CA     1 
ATOM   1481  C  C      . THR   A 1  193 ? -37.776 -71.280  60.299  1.00 46.84  ? 193 THR   A C      1 
ATOM   1482  O  O      . THR   A 1  193 ? -38.847 -71.885  60.266  1.00 52.64  ? 193 THR   A O      1 
ATOM   1483  C  CB     . THR   A 1  193 ? -37.751 -69.623  58.425  1.00 50.68  ? 193 THR   A CB     1 
ATOM   1484  O  OG1    . THR   A 1  193 ? -37.780 -68.218  58.104  1.00 51.23  ? 193 THR   A OG1    1 
ATOM   1485  C  CG2    . THR   A 1  193 ? -38.879 -70.394  57.740  1.00 48.61  ? 193 THR   A CG2    1 
ATOM   1486  N  N      . THR   A 1  194 ? -36.627 -71.876  60.627  1.00 46.73  ? 194 THR   A N      1 
ATOM   1487  C  CA     . THR   A 1  194 ? -36.567 -73.314  60.881  1.00 48.18  ? 194 THR   A CA     1 
ATOM   1488  C  C      . THR   A 1  194 ? -36.649 -73.678  62.368  1.00 48.67  ? 194 THR   A C      1 
ATOM   1489  O  O      . THR   A 1  194 ? -36.857 -74.857  62.684  1.00 49.79  ? 194 THR   A O      1 
ATOM   1490  C  CB     . THR   A 1  194 ? -35.277 -73.922  60.291  1.00 46.57  ? 194 THR   A CB     1 
ATOM   1491  O  OG1    . THR   A 1  194 ? -35.206 -73.651  58.885  1.00 50.30  ? 194 THR   A OG1    1 
ATOM   1492  C  CG2    . THR   A 1  194 ? -35.272 -75.448  60.476  1.00 43.65  ? 194 THR   A CG2    1 
ATOM   1493  N  N      . LEU   A 1  195 ? -36.534 -72.698  63.277  1.00 46.74  ? 195 LEU   A N      1 
ATOM   1494  C  CA     . LEU   A 1  195 ? -36.210 -72.968  64.680  1.00 42.02  ? 195 LEU   A CA     1 
ATOM   1495  C  C      . LEU   A 1  195 ? -37.286 -73.810  65.367  1.00 46.30  ? 195 LEU   A C      1 
ATOM   1496  O  O      . LEU   A 1  195 ? -37.023 -74.907  65.868  1.00 48.64  ? 195 LEU   A O      1 
ATOM   1497  C  CB     . LEU   A 1  195 ? -35.994 -71.637  65.388  1.00 38.52  ? 195 LEU   A CB     1 
ATOM   1498  C  CG     . LEU   A 1  195 ? -35.340 -71.595  66.767  1.00 44.10  ? 195 LEU   A CG     1 
ATOM   1499  C  CD1    . LEU   A 1  195 ? -34.037 -72.383  66.869  1.00 46.27  ? 195 LEU   A CD1    1 
ATOM   1500  C  CD2    . LEU   A 1  195 ? -35.100 -70.141  67.185  1.00 45.11  ? 195 LEU   A CD2    1 
ATOM   1501  N  N      . GLU   A 1  196 ? -38.515 -73.335  65.360  1.00 51.96  ? 196 GLU   A N      1 
ATOM   1502  C  CA     . GLU   A 1  196 ? -39.627 -74.080  65.928  1.00 51.80  ? 196 GLU   A CA     1 
ATOM   1503  C  C      . GLU   A 1  196 ? -39.944 -75.386  65.189  1.00 46.50  ? 196 GLU   A C      1 
ATOM   1504  O  O      . GLU   A 1  196 ? -40.909 -76.080  65.521  1.00 60.26  ? 196 GLU   A O      1 
ATOM   1505  C  CB     . GLU   A 1  196 ? -40.845 -73.160  65.974  1.00 52.90  ? 196 GLU   A CB     1 
ATOM   1506  C  CG     . GLU   A 1  196 ? -40.888 -72.312  67.230  1.00 65.69  ? 196 GLU   A CG     1 
ATOM   1507  C  CD     . GLU   A 1  196 ? -42.033 -71.319  67.226  1.00 96.22  ? 196 GLU   A CD     1 
ATOM   1508  O  OE1    . GLU   A 1  196 ? -42.809 -71.305  66.233  1.00 90.37  ? 196 GLU   A OE1    1 
ATOM   1509  O  OE2    . GLU   A 1  196 ? -42.153 -70.563  68.223  1.00 103.13 ? 196 GLU   A OE2    1 
ATOM   1510  N  N      . HIS   A 1  197 ? -39.149 -75.750  64.205  1.00 43.09  ? 197 HIS   A N      1 
ATOM   1511  C  CA     . HIS   A 1  197 ? -39.404 -76.950  63.434  1.00 49.20  ? 197 HIS   A CA     1 
ATOM   1512  C  C      . HIS   A 1  197 ? -38.339 -78.007  63.621  1.00 53.11  ? 197 HIS   A C      1 
ATOM   1513  O  O      . HIS   A 1  197 ? -38.550 -79.153  63.202  1.00 54.70  ? 197 HIS   A O      1 
ATOM   1514  C  CB     . HIS   A 1  197 ? -39.513 -76.612  61.940  1.00 56.48  ? 197 HIS   A CB     1 
ATOM   1515  C  CG     . HIS   A 1  197 ? -40.616 -75.655  61.604  1.00 58.62  ? 197 HIS   A CG     1 
ATOM   1516  N  ND1    . HIS   A 1  197 ? -41.882 -76.073  61.261  1.00 56.64  ? 197 HIS   A ND1    1 
ATOM   1517  C  CD2    . HIS   A 1  197 ? -40.657 -74.301  61.614  1.00 58.40  ? 197 HIS   A CD2    1 
ATOM   1518  C  CE1    . HIS   A 1  197 ? -42.640 -75.016  61.031  1.00 63.68  ? 197 HIS   A CE1    1 
ATOM   1519  N  NE2    . HIS   A 1  197 ? -41.923 -73.929  61.246  1.00 58.21  ? 197 HIS   A NE2    1 
ATOM   1520  N  N      . SER   A 1  198 ? -37.205 -77.646  64.214  1.00 47.45  ? 198 SER   A N      1 
ATOM   1521  C  CA     . SER   A 1  198 ? -36.157 -78.582  64.587  1.00 47.85  ? 198 SER   A CA     1 
ATOM   1522  C  C      . SER   A 1  198 ? -36.187 -78.850  66.080  1.00 50.78  ? 198 SER   A C      1 
ATOM   1523  O  O      . SER   A 1  198 ? -36.262 -77.915  66.892  1.00 48.52  ? 198 SER   A O      1 
ATOM   1524  C  CB     . SER   A 1  198 ? -34.778 -78.052  64.218  1.00 56.01  ? 198 SER   A CB     1 
ATOM   1525  O  OG     . SER   A 1  198 ? -33.862 -79.128  64.104  1.00 61.50  ? 198 SER   A OG     1 
ATOM   1526  N  N      . ASP   A 1  199 ? -36.092 -80.128  66.429  1.00 52.49  ? 199 ASP   A N      1 
ATOM   1527  C  CA     . ASP   A 1  199 ? -36.102 -80.551  67.824  1.00 54.83  ? 199 ASP   A CA     1 
ATOM   1528  C  C      . ASP   A 1  199 ? -34.717 -80.539  68.448  1.00 50.02  ? 199 ASP   A C      1 
ATOM   1529  O  O      . ASP   A 1  199 ? -34.588 -80.372  69.661  1.00 43.45  ? 199 ASP   A O      1 
ATOM   1530  C  CB     . ASP   A 1  199 ? -36.708 -81.944  67.919  1.00 46.86  ? 199 ASP   A CB     1 
ATOM   1531  C  CG     . ASP   A 1  199 ? -38.147 -81.935  67.544  1.00 53.57  ? 199 ASP   A CG     1 
ATOM   1532  O  OD1    . ASP   A 1  199 ? -38.872 -81.147  68.205  1.00 50.48  ? 199 ASP   A OD1    1 
ATOM   1533  O  OD2    . ASP   A 1  199 ? -38.533 -82.661  66.581  1.00 53.81  ? 199 ASP   A OD2    1 
ATOM   1534  N  N      . CYS   A 1  200 ? -33.683 -80.672  67.626  1.00 51.49  ? 200 CYS   A N      1 
ATOM   1535  C  CA     . CYS   A 1  200 ? -32.308 -80.757  68.079  1.00 44.26  ? 200 CYS   A CA     1 
ATOM   1536  C  C      . CYS   A 1  200 ? -31.442 -80.604  66.841  1.00 48.97  ? 200 CYS   A C      1 
ATOM   1537  O  O      . CYS   A 1  200 ? -31.642 -81.324  65.853  1.00 49.78  ? 200 CYS   A O      1 
ATOM   1538  C  CB     . CYS   A 1  200 ? -32.078 -82.090  68.782  1.00 39.06  ? 200 CYS   A CB     1 
ATOM   1539  S  SG     . CYS   A 1  200 ? -30.404 -82.450  69.250  1.00 49.65  ? 200 CYS   A SG     1 
ATOM   1540  N  N      . ALA   A 1  201 ? -30.523 -79.640  66.863  1.00 43.29  ? 201 ALA   A N      1 
ATOM   1541  C  CA     . ALA   A 1  201 ? -29.651 -79.412  65.718  1.00 40.50  ? 201 ALA   A CA     1 
ATOM   1542  C  C      . ALA   A 1  201 ? -28.195 -79.457  66.145  1.00 38.01  ? 201 ALA   A C      1 
ATOM   1543  O  O      . ALA   A 1  201 ? -27.771 -78.720  67.040  1.00 43.12  ? 201 ALA   A O      1 
ATOM   1544  C  CB     . ALA   A 1  201 ? -29.953 -78.070  65.047  1.00 43.69  ? 201 ALA   A CB     1 
ATOM   1545  N  N      . PHE   A 1  202 ? -27.423 -80.283  65.479  1.00 36.64  ? 202 PHE   A N      1 
ATOM   1546  C  CA     . PHE   A 1  202 ? -25.987 -80.300  65.677  1.00 39.47  ? 202 PHE   A CA     1 
ATOM   1547  C  C      . PHE   A 1  202 ? -25.335 -79.417  64.610  1.00 40.02  ? 202 PHE   A C      1 
ATOM   1548  O  O      . PHE   A 1  202 ? -25.493 -79.665  63.413  1.00 40.89  ? 202 PHE   A O      1 
ATOM   1549  C  CB     . PHE   A 1  202 ? -25.489 -81.739  65.623  1.00 37.95  ? 202 PHE   A CB     1 
ATOM   1550  C  CG     . PHE   A 1  202 ? -26.180 -82.612  66.597  1.00 41.89  ? 202 PHE   A CG     1 
ATOM   1551  C  CD1    . PHE   A 1  202 ? -25.922 -82.493  67.944  1.00 42.02  ? 202 PHE   A CD1    1 
ATOM   1552  C  CD2    . PHE   A 1  202 ? -27.127 -83.532  66.174  1.00 42.31  ? 202 PHE   A CD2    1 
ATOM   1553  C  CE1    . PHE   A 1  202 ? -26.595 -83.291  68.854  1.00 45.45  ? 202 PHE   A CE1    1 
ATOM   1554  C  CE2    . PHE   A 1  202 ? -27.796 -84.331  67.088  1.00 38.20  ? 202 PHE   A CE2    1 
ATOM   1555  C  CZ     . PHE   A 1  202 ? -27.531 -84.212  68.420  1.00 35.84  ? 202 PHE   A CZ     1 
ATOM   1556  N  N      . MET   A 1  203 ? -24.667 -78.352  65.045  1.00 39.04  ? 203 MET   A N      1 
ATOM   1557  C  CA     . MET   A 1  203 ? -23.958 -77.448  64.154  1.00 33.54  ? 203 MET   A CA     1 
ATOM   1558  C  C      . MET   A 1  203 ? -22.525 -77.912  63.992  1.00 35.14  ? 203 MET   A C      1 
ATOM   1559  O  O      . MET   A 1  203 ? -21.862 -78.265  64.964  1.00 44.15  ? 203 MET   A O      1 
ATOM   1560  C  CB     . MET   A 1  203 ? -23.924 -76.048  64.732  1.00 34.00  ? 203 MET   A CB     1 
ATOM   1561  C  CG     . MET   A 1  203 ? -25.227 -75.357  64.709  1.00 37.94  ? 203 MET   A CG     1 
ATOM   1562  S  SD     . MET   A 1  203 ? -24.940 -73.598  64.865  1.00 64.52  ? 203 MET   A SD     1 
ATOM   1563  C  CE     . MET   A 1  203 ? -24.477 -73.365  66.569  1.00 38.82  ? 203 MET   A CE     1 
ATOM   1564  N  N      . VAL   A 1  204 ? -22.036 -77.879  62.766  1.00 37.90  ? 204 VAL   A N      1 
ATOM   1565  C  CA     . VAL   A 1  204 ? -20.644 -78.173  62.461  1.00 35.31  ? 204 VAL   A CA     1 
ATOM   1566  C  C      . VAL   A 1  204 ? -20.083 -76.948  61.764  1.00 36.91  ? 204 VAL   A C      1 
ATOM   1567  O  O      . VAL   A 1  204 ? -20.481 -76.634  60.638  1.00 42.80  ? 204 VAL   A O      1 
ATOM   1568  C  CB     . VAL   A 1  204 ? -20.503 -79.425  61.601  1.00 35.08  ? 204 VAL   A CB     1 
ATOM   1569  C  CG1    . VAL   A 1  204 ? -19.063 -79.763  61.399  1.00 41.05  ? 204 VAL   A CG1    1 
ATOM   1570  C  CG2    . VAL   A 1  204 ? -21.142 -80.536  62.320  1.00 40.42  ? 204 VAL   A CG2    1 
ATOM   1571  N  N      . ASP   A 1  205 ? -19.191 -76.234  62.439  1.00 35.47  ? 205 ASP   A N      1 
ATOM   1572  C  CA     . ASP   A 1  205 ? -18.596 -75.034  61.878  1.00 34.73  ? 205 ASP   A CA     1 
ATOM   1573  C  C      . ASP   A 1  205 ? -17.395 -75.445  61.033  1.00 36.17  ? 205 ASP   A C      1 
ATOM   1574  O  O      . ASP   A 1  205 ? -16.407 -75.961  61.558  1.00 32.84  ? 205 ASP   A O      1 
ATOM   1575  C  CB     . ASP   A 1  205 ? -18.216 -74.079  63.003  1.00 34.66  ? 205 ASP   A CB     1 
ATOM   1576  C  CG     . ASP   A 1  205 ? -17.403 -72.868  62.537  1.00 42.07  ? 205 ASP   A CG     1 
ATOM   1577  O  OD1    . ASP   A 1  205 ? -17.090 -72.729  61.316  1.00 39.02  ? 205 ASP   A OD1    1 
ATOM   1578  O  OD2    . ASP   A 1  205 ? -17.071 -72.044  63.438  1.00 44.39  ? 205 ASP   A OD2    1 
ATOM   1579  N  N      . ASN   A 1  206 ? -17.497 -75.234  59.717  1.00 35.87  ? 206 ASN   A N      1 
ATOM   1580  C  CA     . ASN   A 1  206 ? -16.457 -75.687  58.809  1.00 34.20  ? 206 ASN   A CA     1 
ATOM   1581  C  C      . ASN   A 1  206 ? -15.074 -75.225  59.259  1.00 36.03  ? 206 ASN   A C      1 
ATOM   1582  O  O      . ASN   A 1  206 ? -14.085 -75.950  59.081  1.00 32.48  ? 206 ASN   A O      1 
ATOM   1583  C  CB     . ASN   A 1  206 ? -16.769 -75.205  57.395  1.00 30.62  ? 206 ASN   A CB     1 
ATOM   1584  C  CG     . ASN   A 1  206 ? -17.361 -76.297  56.547  1.00 38.38  ? 206 ASN   A CG     1 
ATOM   1585  O  OD1    . ASN   A 1  206 ? -17.344 -77.453  56.942  1.00 48.56  ? 206 ASN   A OD1    1 
ATOM   1586  N  ND2    . ASN   A 1  206 ? -17.881 -75.952  55.380  1.00 36.59  ? 206 ASN   A ND2    1 
ATOM   1587  N  N      . GLU   A 1  207 ? -14.978 -74.022  59.833  1.00 34.02  ? 207 GLU   A N      1 
ATOM   1588  C  CA     . GLU   A 1  207 ? -13.717 -73.566  60.401  1.00 32.05  ? 207 GLU   A CA     1 
ATOM   1589  C  C      . GLU   A 1  207 ? -13.101 -74.657  61.278  1.00 41.24  ? 207 GLU   A C      1 
ATOM   1590  O  O      . GLU   A 1  207 ? -11.992 -75.140  61.012  1.00 46.81  ? 207 GLU   A O      1 
ATOM   1591  C  CB     . GLU   A 1  207 ? -13.968 -72.294  61.198  1.00 32.85  ? 207 GLU   A CB     1 
ATOM   1592  C  CG     . GLU   A 1  207 ? -12.761 -71.528  61.639  1.00 34.40  ? 207 GLU   A CG     1 
ATOM   1593  C  CD     . GLU   A 1  207 ? -13.059 -70.608  62.807  1.00 43.31  ? 207 GLU   A CD     1 
ATOM   1594  O  OE1    . GLU   A 1  207 ? -13.690 -71.065  63.794  1.00 44.77  ? 207 GLU   A OE1    1 
ATOM   1595  O  OE2    . GLU   A 1  207 ? -12.710 -69.408  62.706  1.00 45.40  ? 207 GLU   A OE2    1 
ATOM   1596  N  N      . ALA   A 1  208 ? -13.840 -75.081  62.314  1.00 39.63  ? 208 ALA   A N      1 
ATOM   1597  C  CA     . ALA   A 1  208 ? -13.414 -76.155  63.209  1.00 35.99  ? 208 ALA   A CA     1 
ATOM   1598  C  C      . ALA   A 1  208 ? -12.949 -77.391  62.443  1.00 36.33  ? 208 ALA   A C      1 
ATOM   1599  O  O      . ALA   A 1  208 ? -11.831 -77.869  62.639  1.00 39.90  ? 208 ALA   A O      1 
ATOM   1600  C  CB     . ALA   A 1  208 ? -14.560 -76.512  64.155  1.00 34.19  ? 208 ALA   A CB     1 
ATOM   1601  N  N      . ILE   A 1  209 ? -13.807 -77.939  61.581  1.00 32.49  ? 209 ILE   A N      1 
ATOM   1602  C  CA     . ILE   A 1  209 ? -13.494 -79.198  60.917  1.00 32.02  ? 209 ILE   A CA     1 
ATOM   1603  C  C      . ILE   A 1  209 ? -12.223 -79.051  60.094  1.00 40.56  ? 209 ILE   A C      1 
ATOM   1604  O  O      . ILE   A 1  209 ? -11.423 -79.988  59.963  1.00 43.74  ? 209 ILE   A O      1 
ATOM   1605  C  CB     . ILE   A 1  209 ? -14.677 -79.635  60.039  1.00 36.29  ? 209 ILE   A CB     1 
ATOM   1606  C  CG1    . ILE   A 1  209 ? -15.951 -79.669  60.840  1.00 37.51  ? 209 ILE   A CG1    1 
ATOM   1607  C  CG2    . ILE   A 1  209 ? -14.473 -81.049  59.583  1.00 45.33  ? 209 ILE   A CG2    1 
ATOM   1608  C  CD1    . ILE   A 1  209 ? -15.858 -80.597  62.008  1.00 41.15  ? 209 ILE   A CD1    1 
ATOM   1609  N  N      . TYR   A 1  210 ? -12.029 -77.867  59.521  1.00 41.70  ? 210 TYR   A N      1 
ATOM   1610  C  CA     . TYR   A 1  210 ? -10.864 -77.569  58.698  1.00 42.73  ? 210 TYR   A CA     1 
ATOM   1611  C  C      . TYR   A 1  210 ? -9.572  -77.566  59.505  1.00 44.35  ? 210 TYR   A C      1 
ATOM   1612  O  O      . TYR   A 1  210 ? -8.600  -78.207  59.107  1.00 47.12  ? 210 TYR   A O      1 
ATOM   1613  C  CB     . TYR   A 1  210 ? -11.089 -76.226  58.031  1.00 44.15  ? 210 TYR   A CB     1 
ATOM   1614  C  CG     . TYR   A 1  210 ? -10.138 -75.816  56.950  1.00 43.67  ? 210 TYR   A CG     1 
ATOM   1615  C  CD1    . TYR   A 1  210 ? -9.022  -75.060  57.264  1.00 53.50  ? 210 TYR   A CD1    1 
ATOM   1616  C  CD2    . TYR   A 1  210 ? -10.410 -76.063  55.622  1.00 42.50  ? 210 TYR   A CD2    1 
ATOM   1617  C  CE1    . TYR   A 1  210 ? -8.166  -74.616  56.297  1.00 56.06  ? 210 TYR   A CE1    1 
ATOM   1618  C  CE2    . TYR   A 1  210 ? -9.553  -75.633  54.638  1.00 48.53  ? 210 TYR   A CE2    1 
ATOM   1619  C  CZ     . TYR   A 1  210 ? -8.428  -74.902  54.983  1.00 54.26  ? 210 TYR   A CZ     1 
ATOM   1620  O  OH     . TYR   A 1  210 ? -7.545  -74.455  54.023  1.00 62.66  ? 210 TYR   A OH     1 
ATOM   1621  N  N      . ASP   A 1  211 ? -9.520  -76.836  60.632  1.00 45.79  ? 211 ASP   A N      1 
ATOM   1622  C  CA     . ASP   A 1  211 ? -8.290  -76.846  61.436  1.00 49.13  ? 211 ASP   A CA     1 
ATOM   1623  C  C      . ASP   A 1  211 ? -7.992  -78.208  62.010  1.00 45.97  ? 211 ASP   A C      1 
ATOM   1624  O  O      . ASP   A 1  211 ? -6.826  -78.592  62.114  1.00 50.31  ? 211 ASP   A O      1 
ATOM   1625  C  CB     . ASP   A 1  211 ? -8.327  -75.844  62.580  1.00 55.57  ? 211 ASP   A CB     1 
ATOM   1626  C  CG     . ASP   A 1  211 ? -8.041  -74.447  62.124  1.00 70.12  ? 211 ASP   A CG     1 
ATOM   1627  O  OD1    . ASP   A 1  211 ? -7.574  -74.317  60.969  1.00 70.34  ? 211 ASP   A OD1    1 
ATOM   1628  O  OD2    . ASP   A 1  211 ? -8.258  -73.496  62.912  1.00 74.71  ? 211 ASP   A OD2    1 
ATOM   1629  N  N      . ILE   A 1  212 ? -9.019  -78.942  62.428  1.00 45.28  ? 212 ILE   A N      1 
ATOM   1630  C  CA     . ILE   A 1  212 ? -8.783  -80.315  62.865  1.00 43.61  ? 212 ILE   A CA     1 
ATOM   1631  C  C      . ILE   A 1  212 ? -8.084  -81.103  61.763  1.00 48.53  ? 212 ILE   A C      1 
ATOM   1632  O  O      . ILE   A 1  212 ? -7.092  -81.798  62.014  1.00 49.71  ? 212 ILE   A O      1 
ATOM   1633  C  CB     . ILE   A 1  212 ? -10.098 -80.980  63.305  1.00 37.18  ? 212 ILE   A CB     1 
ATOM   1634  C  CG1    . ILE   A 1  212 ? -10.609 -80.323  64.600  1.00 37.82  ? 212 ILE   A CG1    1 
ATOM   1635  C  CG2    . ILE   A 1  212 ? -9.908  -82.467  63.445  1.00 33.06  ? 212 ILE   A CG2    1 
ATOM   1636  C  CD1    . ILE   A 1  212 ? -11.994 -80.704  64.971  1.00 35.72  ? 212 ILE   A CD1    1 
ATOM   1637  N  N      . CYS   A 1  213 ? -8.550  -80.966  60.516  1.00 46.74  ? 213 CYS   A N      1 
ATOM   1638  C  CA     . CYS   A 1  213 ? -7.943  -81.722  59.425  1.00 44.68  ? 213 CYS   A CA     1 
ATOM   1639  C  C      . CYS   A 1  213 ? -6.490  -81.315  59.193  1.00 48.68  ? 213 CYS   A C      1 
ATOM   1640  O  O      . CYS   A 1  213 ? -5.685  -82.132  58.733  1.00 54.52  ? 213 CYS   A O      1 
ATOM   1641  C  CB     . CYS   A 1  213 ? -8.753  -81.529  58.155  1.00 41.79  ? 213 CYS   A CB     1 
ATOM   1642  S  SG     . CYS   A 1  213 ? -10.218 -82.554  58.054  1.00 45.75  ? 213 CYS   A SG     1 
ATOM   1643  N  N      . ARG   A 1  214 ? -6.135  -80.066  59.501  1.00 46.28  ? 214 ARG   A N      1 
ATOM   1644  C  CA     . ARG   A 1  214 ? -4.772  -79.571  59.308  1.00 50.53  ? 214 ARG   A CA     1 
ATOM   1645  C  C      . ARG   A 1  214 ? -3.854  -79.949  60.464  1.00 50.69  ? 214 ARG   A C      1 
ATOM   1646  O  O      . ARG   A 1  214 ? -2.747  -80.446  60.240  1.00 52.99  ? 214 ARG   A O      1 
ATOM   1647  C  CB     . ARG   A 1  214 ? -4.795  -78.049  59.122  1.00 52.04  ? 214 ARG   A CB     1 
ATOM   1648  C  CG     . ARG   A 1  214 ? -5.172  -77.586  57.732  1.00 51.74  ? 214 ARG   A CG     1 
ATOM   1649  C  CD     . ARG   A 1  214 ? -4.561  -76.231  57.447  1.00 54.62  ? 214 ARG   A CD     1 
ATOM   1650  N  NE     . ARG   A 1  214 ? -5.079  -75.239  58.385  1.00 70.65  ? 214 ARG   A NE     1 
ATOM   1651  C  CZ     . ARG   A 1  214 ? -4.892  -73.925  58.295  1.00 76.40  ? 214 ARG   A CZ     1 
ATOM   1652  N  NH1    . ARG   A 1  214 ? -4.090  -73.396  57.385  1.00 78.66  ? 214 ARG   A NH1    1 
ATOM   1653  N  NH2    . ARG   A 1  214 ? -5.531  -73.119  59.138  1.00 70.56  ? 214 ARG   A NH2    1 
ATOM   1654  N  N      . ARG   A 1  215 ? -4.297  -79.694  61.698  1.00 47.74  ? 215 ARG   A N      1 
ATOM   1655  C  CA     . ARG   A 1  215 ? -3.525  -80.040  62.886  1.00 41.93  ? 215 ARG   A CA     1 
ATOM   1656  C  C      . ARG   A 1  215 ? -3.337  -81.547  63.003  1.00 50.05  ? 215 ARG   A C      1 
ATOM   1657  O  O      . ARG   A 1  215 ? -2.210  -82.045  63.081  1.00 56.51  ? 215 ARG   A O      1 
ATOM   1658  C  CB     . ARG   A 1  215 ? -4.225  -79.516  64.144  1.00 46.26  ? 215 ARG   A CB     1 
ATOM   1659  C  CG     . ARG   A 1  215 ? -3.916  -78.096  64.519  1.00 54.61  ? 215 ARG   A CG     1 
ATOM   1660  C  CD     . ARG   A 1  215 ? -4.426  -77.735  65.935  1.00 60.79  ? 215 ARG   A CD     1 
ATOM   1661  N  NE     . ARG   A 1  215 ? -5.841  -77.391  66.011  1.00 62.56  ? 215 ARG   A NE     1 
ATOM   1662  C  CZ     . ARG   A 1  215 ? -6.777  -78.149  66.571  1.00 60.61  ? 215 ARG   A CZ     1 
ATOM   1663  N  NH1    . ARG   A 1  215 ? -6.494  -79.346  67.082  1.00 60.30  ? 215 ARG   A NH1    1 
ATOM   1664  N  NH2    . ARG   A 1  215 ? -8.021  -77.682  66.649  1.00 52.84  ? 215 ARG   A NH2    1 
ATOM   1665  N  N      . ASN   A 1  216 ? -4.441  -82.291  63.036  1.00 48.03  ? 216 ASN   A N      1 
ATOM   1666  C  CA     . ASN   A 1  216 ? -4.446  -83.689  63.434  1.00 43.67  ? 216 ASN   A CA     1 
ATOM   1667  C  C      . ASN   A 1  216 ? -4.413  -84.652  62.256  1.00 51.18  ? 216 ASN   A C      1 
ATOM   1668  O  O      . ASN   A 1  216 ? -4.238  -85.857  62.464  1.00 57.87  ? 216 ASN   A O      1 
ATOM   1669  C  CB     . ASN   A 1  216 ? -5.673  -83.957  64.295  1.00 35.59  ? 216 ASN   A CB     1 
ATOM   1670  C  CG     . ASN   A 1  216 ? -5.651  -83.162  65.568  1.00 42.40  ? 216 ASN   A CG     1 
ATOM   1671  O  OD1    . ASN   A 1  216 ? -4.777  -82.325  65.754  1.00 47.34  ? 216 ASN   A OD1    1 
ATOM   1672  N  ND2    . ASN   A 1  216 ? -6.666  -83.342  66.417  1.00 48.31  ? 216 ASN   A ND2    1 
ATOM   1673  N  N      . LEU   A 1  217 ? -4.572  -84.174  61.032  1.00 46.05  ? 217 LEU   A N      1 
ATOM   1674  C  CA     . LEU   A 1  217 ? -4.427  -85.045  59.881  1.00 49.43  ? 217 LEU   A CA     1 
ATOM   1675  C  C      . LEU   A 1  217 ? -3.276  -84.616  58.998  1.00 56.51  ? 217 LEU   A C      1 
ATOM   1676  O  O      . LEU   A 1  217 ? -3.094  -85.192  57.914  1.00 55.63  ? 217 LEU   A O      1 
ATOM   1677  C  CB     . LEU   A 1  217 ? -5.707  -85.106  59.047  1.00 48.14  ? 217 LEU   A CB     1 
ATOM   1678  C  CG     . LEU   A 1  217 ? -6.939  -85.754  59.653  1.00 48.76  ? 217 LEU   A CG     1 
ATOM   1679  C  CD1    . LEU   A 1  217 ? -8.038  -85.833  58.595  1.00 48.36  ? 217 LEU   A CD1    1 
ATOM   1680  C  CD2    . LEU   A 1  217 ? -6.583  -87.110  60.202  1.00 43.99  ? 217 LEU   A CD2    1 
ATOM   1681  N  N      . ASP   A 1  218 ? -2.515  -83.606  59.413  1.00 57.25  ? 218 ASP   A N      1 
ATOM   1682  C  CA     . ASP   A 1  218 ? -1.404  -83.109  58.604  1.00 61.36  ? 218 ASP   A CA     1 
ATOM   1683  C  C      . ASP   A 1  218 ? -1.836  -82.938  57.150  1.00 54.65  ? 218 ASP   A C      1 
ATOM   1684  O  O      . ASP   A 1  218 ? -1.134  -83.338  56.225  1.00 48.48  ? 218 ASP   A O      1 
ATOM   1685  C  CB     . ASP   A 1  218 ? -0.206  -84.057  58.679  1.00 65.21  ? 218 ASP   A CB     1 
ATOM   1686  C  CG     . ASP   A 1  218 ? 0.308   -84.244  60.085  1.00 70.77  ? 218 ASP   A CG     1 
ATOM   1687  O  OD1    . ASP   A 1  218 ? 0.503   -83.218  60.781  1.00 74.40  ? 218 ASP   A OD1    1 
ATOM   1688  O  OD2    . ASP   A 1  218 ? 0.509   -85.425  60.476  1.00 71.51  ? 218 ASP   A OD2    1 
ATOM   1689  N  N      . ILE   A 1  219 ? -3.030  -82.397  56.950  1.00 49.71  ? 219 ILE   A N      1 
ATOM   1690  C  CA     . ILE   A 1  219 ? -3.543  -82.106  55.622  1.00 48.14  ? 219 ILE   A CA     1 
ATOM   1691  C  C      . ILE   A 1  219 ? -3.386  -80.608  55.387  1.00 56.54  ? 219 ILE   A C      1 
ATOM   1692  O  O      . ILE   A 1  219 ? -3.968  -79.798  56.117  1.00 54.34  ? 219 ILE   A O      1 
ATOM   1693  C  CB     . ILE   A 1  219 ? -5.008  -82.535  55.477  1.00 48.69  ? 219 ILE   A CB     1 
ATOM   1694  C  CG1    . ILE   A 1  219 ? -5.141  -84.047  55.483  1.00 55.58  ? 219 ILE   A CG1    1 
ATOM   1695  C  CG2    . ILE   A 1  219 ? -5.590  -82.002  54.202  1.00 50.47  ? 219 ILE   A CG2    1 
ATOM   1696  C  CD1    . ILE   A 1  219 ? -6.411  -84.519  56.135  1.00 56.08  ? 219 ILE   A CD1    1 
ATOM   1697  N  N      . GLU   A 1  220 ? -2.611  -80.242  54.356  1.00 61.44  ? 220 GLU   A N      1 
ATOM   1698  C  CA     . GLU   A 1  220 ? -2.221  -78.850  54.143  1.00 57.31  ? 220 GLU   A CA     1 
ATOM   1699  C  C      . GLU   A 1  220 ? -3.422  -77.948  53.893  1.00 60.75  ? 220 GLU   A C      1 
ATOM   1700  O  O      . GLU   A 1  220 ? -3.615  -76.940  54.586  1.00 64.42  ? 220 GLU   A O      1 
ATOM   1701  C  CB     . GLU   A 1  220 ? -1.258  -78.759  52.973  1.00 62.95  ? 220 GLU   A CB     1 
ATOM   1702  C  CG     . GLU   A 1  220 ? 0.095   -79.310  53.255  1.00 74.69  ? 220 GLU   A CG     1 
ATOM   1703  C  CD     . GLU   A 1  220 ? 1.148   -78.519  52.518  1.00 88.64  ? 220 GLU   A CD     1 
ATOM   1704  O  OE1    . GLU   A 1  220 ? 0.915   -78.215  51.326  1.00 82.83  ? 220 GLU   A OE1    1 
ATOM   1705  O  OE2    . GLU   A 1  220 ? 2.185   -78.172  53.133  1.00 104.55 ? 220 GLU   A OE2    1 
ATOM   1706  N  N      . ARG   A 1  221 ? -4.191  -78.247  52.850  1.00 58.62  ? 221 ARG   A N      1 
ATOM   1707  C  CA     . ARG   A 1  221 ? -5.438  -77.548  52.548  1.00 54.46  ? 221 ARG   A CA     1 
ATOM   1708  C  C      . ARG   A 1  221 ? -6.506  -78.612  52.376  1.00 56.15  ? 221 ARG   A C      1 
ATOM   1709  O  O      . ARG   A 1  221 ? -6.612  -79.203  51.287  1.00 53.84  ? 221 ARG   A O      1 
ATOM   1710  C  CB     . ARG   A 1  221 ? -5.355  -76.706  51.286  1.00 57.53  ? 221 ARG   A CB     1 
ATOM   1711  C  CG     . ARG   A 1  221 ? -6.620  -75.921  51.096  1.00 68.36  ? 221 ARG   A CG     1 
ATOM   1712  C  CD     . ARG   A 1  221 ? -6.645  -75.060  49.867  1.00 78.39  ? 221 ARG   A CD     1 
ATOM   1713  N  NE     . ARG   A 1  221 ? -7.911  -74.337  49.811  1.00 85.49  ? 221 ARG   A NE     1 
ATOM   1714  C  CZ     . ARG   A 1  221 ? -8.337  -73.662  48.753  1.00 99.10  ? 221 ARG   A CZ     1 
ATOM   1715  N  NH1    . ARG   A 1  221 ? -7.668  -73.680  47.610  1.00 103.57 ? 221 ARG   A NH1    1 
ATOM   1716  N  NH2    . ARG   A 1  221 ? -9.495  -73.005  48.821  1.00 92.35  ? 221 ARG   A NH2    1 
ATOM   1717  N  N      . PRO   A 1  222 ? -7.319  -78.871  53.402  1.00 55.67  ? 222 PRO   A N      1 
ATOM   1718  C  CA     . PRO   A 1  222 ? -8.334  -79.933  53.305  1.00 52.19  ? 222 PRO   A CA     1 
ATOM   1719  C  C      . PRO   A 1  222 ? -9.324  -79.678  52.182  1.00 50.05  ? 222 PRO   A C      1 
ATOM   1720  O  O      . PRO   A 1  222 ? -9.731  -78.539  51.942  1.00 48.13  ? 222 PRO   A O      1 
ATOM   1721  C  CB     . PRO   A 1  222 ? -9.022  -79.888  54.677  1.00 45.43  ? 222 PRO   A CB     1 
ATOM   1722  C  CG     . PRO   A 1  222 ? -8.035  -79.214  55.581  1.00 47.36  ? 222 PRO   A CG     1 
ATOM   1723  C  CD     . PRO   A 1  222 ? -7.318  -78.223  54.720  1.00 53.15  ? 222 PRO   A CD     1 
ATOM   1724  N  N      . THR   A 1  223 ? -9.711  -80.758  51.501  1.00 45.68  ? 223 THR   A N      1 
ATOM   1725  C  CA     . THR   A 1  223 ? -10.814 -80.712  50.553  1.00 48.96  ? 223 THR   A CA     1 
ATOM   1726  C  C      . THR   A 1  223 ? -12.132 -81.029  51.252  1.00 48.37  ? 223 THR   A C      1 
ATOM   1727  O  O      . THR   A 1  223 ? -12.170 -81.403  52.426  1.00 46.63  ? 223 THR   A O      1 
ATOM   1728  C  CB     . THR   A 1  223 ? -10.603 -81.690  49.392  1.00 53.56  ? 223 THR   A CB     1 
ATOM   1729  O  OG1    . THR   A 1  223 ? -10.460 -83.036  49.882  1.00 52.47  ? 223 THR   A OG1    1 
ATOM   1730  C  CG2    . THR   A 1  223 ? -9.381  -81.295  48.584  1.00 51.05  ? 223 THR   A CG2    1 
ATOM   1731  N  N      . TYR   A 1  224 ? -13.235 -80.868  50.519  1.00 48.46  ? 224 TYR   A N      1 
ATOM   1732  C  CA     . TYR   A 1  224 ? -14.506 -81.288  51.089  1.00 46.31  ? 224 TYR   A CA     1 
ATOM   1733  C  C      . TYR   A 1  224 ? -14.480 -82.777  51.411  1.00 52.31  ? 224 TYR   A C      1 
ATOM   1734  O  O      . TYR   A 1  224 ? -15.134 -83.215  52.376  1.00 52.36  ? 224 TYR   A O      1 
ATOM   1735  C  CB     . TYR   A 1  224 ? -15.664 -80.973  50.146  1.00 40.17  ? 224 TYR   A CB     1 
ATOM   1736  C  CG     . TYR   A 1  224 ? -16.030 -79.521  50.059  1.00 39.30  ? 224 TYR   A CG     1 
ATOM   1737  C  CD1    . TYR   A 1  224 ? -15.946 -78.687  51.147  1.00 36.96  ? 224 TYR   A CD1    1 
ATOM   1738  C  CD2    . TYR   A 1  224 ? -16.431 -78.977  48.852  1.00 47.92  ? 224 TYR   A CD2    1 
ATOM   1739  C  CE1    . TYR   A 1  224 ? -16.270 -77.324  51.037  1.00 45.00  ? 224 TYR   A CE1    1 
ATOM   1740  C  CE2    . TYR   A 1  224 ? -16.756 -77.630  48.726  1.00 49.72  ? 224 TYR   A CE2    1 
ATOM   1741  C  CZ     . TYR   A 1  224 ? -16.677 -76.803  49.817  1.00 50.21  ? 224 TYR   A CZ     1 
ATOM   1742  O  OH     . TYR   A 1  224 ? -17.004 -75.464  49.666  1.00 52.30  ? 224 TYR   A OH     1 
ATOM   1743  N  N      . THR   A 1  225 ? -13.721 -83.570  50.633  1.00 43.60  ? 225 THR   A N      1 
ATOM   1744  C  CA     . THR   A 1  225 ? -13.645 -84.996  50.935  1.00 41.64  ? 225 THR   A CA     1 
ATOM   1745  C  C      . THR   A 1  225 ? -12.981 -85.236  52.271  1.00 48.92  ? 225 THR   A C      1 
ATOM   1746  O  O      . THR   A 1  225 ? -13.450 -86.068  53.063  1.00 52.40  ? 225 THR   A O      1 
ATOM   1747  C  CB     . THR   A 1  225 ? -12.911 -85.760  49.844  1.00 43.32  ? 225 THR   A CB     1 
ATOM   1748  O  OG1    . THR   A 1  225 ? -13.449 -85.414  48.562  1.00 51.93  ? 225 THR   A OG1    1 
ATOM   1749  C  CG2    . THR   A 1  225 ? -13.025 -87.249  50.080  1.00 40.19  ? 225 THR   A CG2    1 
ATOM   1750  N  N      . ASN   A 1  226 ? -11.883 -84.522  52.533  1.00 49.00  ? 226 ASN   A N      1 
ATOM   1751  C  CA     . ASN   A 1  226 ? -11.258 -84.559  53.849  1.00 47.96  ? 226 ASN   A CA     1 
ATOM   1752  C  C      . ASN   A 1  226 ? -12.285 -84.229  54.922  1.00 46.96  ? 226 ASN   A C      1 
ATOM   1753  O  O      . ASN   A 1  226 ? -12.466 -84.984  55.877  1.00 48.94  ? 226 ASN   A O      1 
ATOM   1754  C  CB     . ASN   A 1  226 ? -10.097 -83.564  53.896  1.00 51.11  ? 226 ASN   A CB     1 
ATOM   1755  C  CG     . ASN   A 1  226 ? -8.974  -83.934  52.956  1.00 52.27  ? 226 ASN   A CG     1 
ATOM   1756  O  OD1    . ASN   A 1  226 ? -8.455  -83.080  52.227  1.00 51.55  ? 226 ASN   A OD1    1 
ATOM   1757  N  ND2    . ASN   A 1  226 ? -8.587  -85.207  52.964  1.00 54.82  ? 226 ASN   A ND2    1 
ATOM   1758  N  N      . LEU   A 1  227 ? -12.994 -83.110  54.752  1.00 46.48  ? 227 LEU   A N      1 
ATOM   1759  C  CA     . LEU   A 1  227 ? -13.917 -82.647  55.776  1.00 43.64  ? 227 LEU   A CA     1 
ATOM   1760  C  C      . LEU   A 1  227 ? -15.095 -83.580  55.906  1.00 45.69  ? 227 LEU   A C      1 
ATOM   1761  O  O      . LEU   A 1  227 ? -15.593 -83.822  57.011  1.00 45.43  ? 227 LEU   A O      1 
ATOM   1762  C  CB     . LEU   A 1  227 ? -14.427 -81.248  55.449  1.00 47.36  ? 227 LEU   A CB     1 
ATOM   1763  C  CG     . LEU   A 1  227 ? -13.476 -80.132  55.064  1.00 43.61  ? 227 LEU   A CG     1 
ATOM   1764  C  CD1    . LEU   A 1  227 ? -14.282 -78.979  54.528  1.00 34.56  ? 227 LEU   A CD1    1 
ATOM   1765  C  CD2    . LEU   A 1  227 ? -12.675 -79.726  56.295  1.00 42.74  ? 227 LEU   A CD2    1 
ATOM   1766  N  N      . ASN   A 1  228 ? -15.597 -84.068  54.792  1.00 46.15  ? 228 ASN   A N      1 
ATOM   1767  C  CA     . ASN   A 1  228 ? -16.837 -84.804  54.914  1.00 49.73  ? 228 ASN   A CA     1 
ATOM   1768  C  C      . ASN   A 1  228 ? -16.619 -86.154  55.572  1.00 50.61  ? 228 ASN   A C      1 
ATOM   1769  O  O      . ASN   A 1  228 ? -17.466 -86.602  56.352  1.00 49.06  ? 228 ASN   A O      1 
ATOM   1770  C  CB     . ASN   A 1  228 ? -17.490 -84.931  53.552  1.00 48.27  ? 228 ASN   A CB     1 
ATOM   1771  C  CG     . ASN   A 1  228 ? -18.027 -83.636  53.095  1.00 46.41  ? 228 ASN   A CG     1 
ATOM   1772  O  OD1    . ASN   A 1  228 ? -18.051 -82.687  53.859  1.00 46.46  ? 228 ASN   A OD1    1 
ATOM   1773  N  ND2    . ASN   A 1  228 ? -18.505 -83.580  51.861  1.00 57.37  ? 228 ASN   A ND2    1 
ATOM   1774  N  N      . ARG   A 1  229 ? -15.485 -86.810  55.292  1.00 51.37  ? 229 ARG   A N      1 
ATOM   1775  C  CA     . ARG   A 1  229 ? -15.236 -88.110  55.912  1.00 47.09  ? 229 ARG   A CA     1 
ATOM   1776  C  C      . ARG   A 1  229 ? -15.070 -87.971  57.426  1.00 49.06  ? 229 ARG   A C      1 
ATOM   1777  O  O      . ARG   A 1  229 ? -15.548 -88.816  58.193  1.00 49.21  ? 229 ARG   A O      1 
ATOM   1778  C  CB     . ARG   A 1  229 ? -14.045 -88.786  55.239  1.00 42.63  ? 229 ARG   A CB     1 
ATOM   1779  C  CG     . ARG   A 1  229 ? -14.432 -89.412  53.881  1.00 48.90  ? 229 ARG   A CG     1 
ATOM   1780  C  CD     . ARG   A 1  229 ? -13.570 -90.626  53.512  1.00 56.09  ? 229 ARG   A CD     1 
ATOM   1781  N  NE     . ARG   A 1  229 ? -12.437 -90.372  52.631  1.00 63.17  ? 229 ARG   A NE     1 
ATOM   1782  C  CZ     . ARG   A 1  229 ? -12.367 -90.826  51.385  1.00 67.32  ? 229 ARG   A CZ     1 
ATOM   1783  N  NH1    . ARG   A 1  229 ? -13.313 -91.613  50.884  1.00 64.32  ? 229 ARG   A NH1    1 
ATOM   1784  N  NH2    . ARG   A 1  229 ? -11.296 -90.537  50.643  1.00 63.48  ? 229 ARG   A NH2    1 
ATOM   1785  N  N      . LEU   A 1  230 ? -14.455 -86.877  57.872  1.00 43.19  ? 230 LEU   A N      1 
ATOM   1786  C  CA     . LEU   A 1  230 ? -14.413 -86.558  59.288  1.00 37.20  ? 230 LEU   A CA     1 
ATOM   1787  C  C      . LEU   A 1  230 ? -15.798 -86.228  59.839  1.00 46.86  ? 230 LEU   A C      1 
ATOM   1788  O  O      . LEU   A 1  230 ? -16.137 -86.646  60.952  1.00 50.48  ? 230 LEU   A O      1 
ATOM   1789  C  CB     . LEU   A 1  230 ? -13.456 -85.399  59.505  1.00 37.87  ? 230 LEU   A CB     1 
ATOM   1790  C  CG     . LEU   A 1  230 ? -13.257 -84.767  60.879  1.00 42.40  ? 230 LEU   A CG     1 
ATOM   1791  C  CD1    . LEU   A 1  230 ? -13.015 -85.783  61.971  1.00 29.67  ? 230 LEU   A CD1    1 
ATOM   1792  C  CD2    . LEU   A 1  230 ? -12.123 -83.763  60.783  1.00 36.93  ? 230 LEU   A CD2    1 
ATOM   1793  N  N      . ILE   A 1  231 ? -16.617 -85.470  59.096  1.00 49.63  ? 231 ILE   A N      1 
ATOM   1794  C  CA     . ILE   A 1  231 ? -17.946 -85.118  59.623  1.00 46.89  ? 231 ILE   A CA     1 
ATOM   1795  C  C      . ILE   A 1  231 ? -18.863 -86.327  59.704  1.00 47.19  ? 231 ILE   A C      1 
ATOM   1796  O  O      . ILE   A 1  231 ? -19.838 -86.319  60.459  1.00 46.93  ? 231 ILE   A O      1 
ATOM   1797  C  CB     . ILE   A 1  231 ? -18.630 -84.009  58.804  1.00 44.42  ? 231 ILE   A CB     1 
ATOM   1798  C  CG1    . ILE   A 1  231 ? -17.859 -82.703  58.906  1.00 50.79  ? 231 ILE   A CG1    1 
ATOM   1799  C  CG2    . ILE   A 1  231 ? -20.042 -83.797  59.295  1.00 31.99  ? 231 ILE   A CG2    1 
ATOM   1800  C  CD1    . ILE   A 1  231 ? -18.370 -81.652  57.984  1.00 47.77  ? 231 ILE   A CD1    1 
ATOM   1801  N  N      . SER   A 1  232 ? -18.612 -87.364  58.909  1.00 49.20  ? 232 SER   A N      1 
ATOM   1802  C  CA     . SER   A 1  232 ? -19.468 -88.541  58.986  1.00 50.89  ? 232 SER   A CA     1 
ATOM   1803  C  C      . SER   A 1  232 ? -19.198 -89.310  60.271  1.00 46.27  ? 232 SER   A C      1 
ATOM   1804  O  O      . SER   A 1  232 ? -20.126 -89.599  61.040  1.00 44.18  ? 232 SER   A O      1 
ATOM   1805  C  CB     . SER   A 1  232 ? -19.252 -89.406  57.754  1.00 56.00  ? 232 SER   A CB     1 
ATOM   1806  O  OG     . SER   A 1  232 ? -17.878 -89.733  57.655  1.00 66.78  ? 232 SER   A OG     1 
ATOM   1807  N  N      . GLN   A 1  233 ? -17.922 -89.615  60.525  1.00 43.03  ? 233 GLN   A N      1 
ATOM   1808  C  CA     . GLN   A 1  233 ? -17.422 -90.085  61.812  1.00 45.98  ? 233 GLN   A CA     1 
ATOM   1809  C  C      . GLN   A 1  233 ? -18.220 -89.490  62.971  1.00 49.44  ? 233 GLN   A C      1 
ATOM   1810  O  O      . GLN   A 1  233 ? -18.747 -90.236  63.803  1.00 48.44  ? 233 GLN   A O      1 
ATOM   1811  C  CB     . GLN   A 1  233 ? -15.954 -89.700  61.962  1.00 43.73  ? 233 GLN   A CB     1 
ATOM   1812  C  CG     . GLN   A 1  233 ? -15.048 -90.481  61.078  1.00 44.79  ? 233 GLN   A CG     1 
ATOM   1813  C  CD     . GLN   A 1  233 ? -15.001 -91.916  61.436  1.00 51.37  ? 233 GLN   A CD     1 
ATOM   1814  O  OE1    . GLN   A 1  233 ? -14.948 -92.260  62.621  1.00 67.19  ? 233 GLN   A OE1    1 
ATOM   1815  N  NE2    . GLN   A 1  233 ? -15.044 -92.782  60.433  1.00 46.00  ? 233 GLN   A NE2    1 
ATOM   1816  N  N      . ILE   A 1  234 ? -18.321 -88.153  63.044  1.00 44.21  ? 234 ILE   A N      1 
ATOM   1817  C  CA     . ILE   A 1  234 ? -19.099 -87.556  64.129  1.00 43.22  ? 234 ILE   A CA     1 
ATOM   1818  C  C      . ILE   A 1  234 ? -20.585 -87.853  63.932  1.00 41.88  ? 234 ILE   A C      1 
ATOM   1819  O  O      . ILE   A 1  234 ? -21.309 -88.113  64.897  1.00 40.50  ? 234 ILE   A O      1 
ATOM   1820  C  CB     . ILE   A 1  234 ? -18.844 -86.036  64.260  1.00 39.80  ? 234 ILE   A CB     1 
ATOM   1821  C  CG1    . ILE   A 1  234 ? -17.471 -85.715  64.826  1.00 39.23  ? 234 ILE   A CG1    1 
ATOM   1822  C  CG2    . ILE   A 1  234 ? -19.793 -85.431  65.254  1.00 34.58  ? 234 ILE   A CG2    1 
ATOM   1823  C  CD1    . ILE   A 1  234 ? -16.336 -86.105  63.913  1.00 46.97  ? 234 ILE   A CD1    1 
ATOM   1824  N  N      . VAL   A 1  235 ? -21.068 -87.827  62.685  1.00 41.16  ? 235 VAL   A N      1 
ATOM   1825  C  CA     . VAL   A 1  235 ? -22.484 -88.116  62.466  1.00 45.37  ? 235 VAL   A CA     1 
ATOM   1826  C  C      . VAL   A 1  235 ? -22.778 -89.546  62.872  1.00 47.56  ? 235 VAL   A C      1 
ATOM   1827  O  O      . VAL   A 1  235 ? -23.812 -89.844  63.490  1.00 44.74  ? 235 VAL   A O      1 
ATOM   1828  C  CB     . VAL   A 1  235 ? -22.893 -87.870  61.002  1.00 43.44  ? 235 VAL   A CB     1 
ATOM   1829  C  CG1    . VAL   A 1  235 ? -24.334 -88.340  60.770  1.00 39.44  ? 235 VAL   A CG1    1 
ATOM   1830  C  CG2    . VAL   A 1  235 ? -22.769 -86.429  60.666  1.00 44.30  ? 235 VAL   A CG2    1 
ATOM   1831  N  N      . SER   A 1  236 ? -21.866 -90.453  62.541  1.00 43.27  ? 236 SER   A N      1 
ATOM   1832  C  CA     . SER   A 1  236 ? -22.100 -91.848  62.846  1.00 45.06  ? 236 SER   A CA     1 
ATOM   1833  C  C      . SER   A 1  236 ? -22.143 -92.046  64.364  1.00 51.46  ? 236 SER   A C      1 
ATOM   1834  O  O      . SER   A 1  236 ? -23.104 -92.612  64.899  1.00 54.90  ? 236 SER   A O      1 
ATOM   1835  C  CB     . SER   A 1  236 ? -21.024 -92.685  62.157  1.00 43.80  ? 236 SER   A CB     1 
ATOM   1836  O  OG     . SER   A 1  236 ? -21.281 -94.062  62.274  1.00 46.25  ? 236 SER   A OG     1 
ATOM   1837  N  N      . SER   A 1  237 ? -21.144 -91.528  65.091  1.00 47.99  ? 237 SER   A N      1 
ATOM   1838  C  CA     . SER   A 1  237 ? -21.186 -91.517  66.558  1.00 47.70  ? 237 SER   A CA     1 
ATOM   1839  C  C      . SER   A 1  237 ? -22.535 -91.074  67.096  1.00 50.14  ? 237 SER   A C      1 
ATOM   1840  O  O      . SER   A 1  237 ? -23.042 -91.647  68.068  1.00 52.38  ? 237 SER   A O      1 
ATOM   1841  C  CB     . SER   A 1  237 ? -20.139 -90.575  67.137  1.00 45.17  ? 237 SER   A CB     1 
ATOM   1842  O  OG     . SER   A 1  237 ? -18.858 -90.888  66.667  1.00 51.90  ? 237 SER   A OG     1 
ATOM   1843  N  N      . ILE   A 1  238 ? -23.102 -90.031  66.478  1.00 47.81  ? 238 ILE   A N      1 
ATOM   1844  C  CA     . ILE   A 1  238 ? -24.332 -89.428  66.980  1.00 45.77  ? 238 ILE   A CA     1 
ATOM   1845  C  C      . ILE   A 1  238 ? -25.541 -90.255  66.596  1.00 49.88  ? 238 ILE   A C      1 
ATOM   1846  O  O      . ILE   A 1  238 ? -26.569 -90.215  67.292  1.00 49.03  ? 238 ILE   A O      1 
ATOM   1847  C  CB     . ILE   A 1  238 ? -24.498 -87.996  66.465  1.00 39.98  ? 238 ILE   A CB     1 
ATOM   1848  C  CG1    . ILE   A 1  238 ? -23.279 -87.163  66.839  1.00 43.99  ? 238 ILE   A CG1    1 
ATOM   1849  C  CG2    . ILE   A 1  238 ? -25.752 -87.383  67.051  1.00 38.07  ? 238 ILE   A CG2    1 
ATOM   1850  C  CD1    . ILE   A 1  238 ? -23.387 -85.724  66.412  1.00 41.30  ? 238 ILE   A CD1    1 
ATOM   1851  N  N      . THR   A 1  239 ? -25.463 -90.995  65.487  1.00 46.94  ? 239 THR   A N      1 
ATOM   1852  C  CA     . THR   A 1  239 ? -26.608 -91.780  65.062  1.00 43.10  ? 239 THR   A CA     1 
ATOM   1853  C  C      . THR   A 1  239 ? -26.463 -93.242  65.406  1.00 46.20  ? 239 THR   A C      1 
ATOM   1854  O  O      . THR   A 1  239 ? -27.398 -93.993  65.152  1.00 57.65  ? 239 THR   A O      1 
ATOM   1855  C  CB     . THR   A 1  239 ? -26.843 -91.660  63.552  1.00 44.65  ? 239 THR   A CB     1 
ATOM   1856  O  OG1    . THR   A 1  239 ? -25.708 -92.180  62.850  1.00 47.91  ? 239 THR   A OG1    1 
ATOM   1857  C  CG2    . THR   A 1  239 ? -27.015 -90.205  63.158  1.00 40.47  ? 239 THR   A CG2    1 
ATOM   1858  N  N      . ALA   A 1  240 ? -25.334 -93.662  65.990  1.00 46.47  ? 240 ALA   A N      1 
ATOM   1859  C  CA     . ALA   A 1  240 ? -25.062 -95.091  66.155  1.00 46.87  ? 240 ALA   A CA     1 
ATOM   1860  C  C      . ALA   A 1  240 ? -26.092 -95.771  67.053  1.00 50.33  ? 240 ALA   A C      1 
ATOM   1861  O  O      . ALA   A 1  240 ? -26.458 -96.928  66.816  1.00 49.63  ? 240 ALA   A O      1 
ATOM   1862  C  CB     . ALA   A 1  240 ? -23.653 -95.292  66.704  1.00 45.43  ? 240 ALA   A CB     1 
ATOM   1863  N  N      . SER   A 1  241 ? -26.581 -95.070  68.083  1.00 46.99  ? 241 SER   A N      1 
ATOM   1864  C  CA     . SER   A 1  241 ? -27.531 -95.688  69.005  1.00 48.93  ? 241 SER   A CA     1 
ATOM   1865  C  C      . SER   A 1  241 ? -28.821 -96.070  68.310  1.00 50.48  ? 241 SER   A C      1 
ATOM   1866  O  O      . SER   A 1  241 ? -29.499 -97.010  68.735  1.00 58.33  ? 241 SER   A O      1 
ATOM   1867  C  CB     . SER   A 1  241 ? -27.870 -94.747  70.146  1.00 51.26  ? 241 SER   A CB     1 
ATOM   1868  O  OG     . SER   A 1  241 ? -28.141 -93.461  69.641  1.00 58.82  ? 241 SER   A OG     1 
ATOM   1869  N  N      . LEU   A 1  242 ? -29.208 -95.318  67.286  1.00 50.00  ? 242 LEU   A N      1 
ATOM   1870  C  CA     . LEU   A 1  242 ? -30.402 -95.617  66.501  1.00 48.97  ? 242 LEU   A CA     1 
ATOM   1871  C  C      . LEU   A 1  242 ? -30.218 -96.838  65.610  1.00 47.41  ? 242 LEU   A C      1 
ATOM   1872  O  O      . LEU   A 1  242 ? -31.202 -97.478  65.238  1.00 54.77  ? 242 LEU   A O      1 
ATOM   1873  C  CB     . LEU   A 1  242 ? -30.759 -94.395  65.657  1.00 41.30  ? 242 LEU   A CB     1 
ATOM   1874  C  CG     . LEU   A 1  242 ? -31.080 -93.133  66.440  1.00 44.63  ? 242 LEU   A CG     1 
ATOM   1875  C  CD1    . LEU   A 1  242 ? -31.209 -91.939  65.542  1.00 49.79  ? 242 LEU   A CD1    1 
ATOM   1876  C  CD2    . LEU   A 1  242 ? -32.393 -93.358  67.097  1.00 49.82  ? 242 LEU   A CD2    1 
ATOM   1877  N  N      . ARG   A 1  243 ? -28.986 -97.177  65.267  1.00 42.82  ? 243 ARG   A N      1 
ATOM   1878  C  CA     . ARG   A 1  243 ? -28.725 -98.262  64.343  1.00 49.34  ? 243 ARG   A CA     1 
ATOM   1879  C  C      . ARG   A 1  243 ? -28.112 -99.468  65.027  1.00 55.75  ? 243 ARG   A C      1 
ATOM   1880  O  O      . ARG   A 1  243 ? -27.779 -100.451 64.349  1.00 55.47  ? 243 ARG   A O      1 
ATOM   1881  C  CB     . ARG   A 1  243 ? -27.789 -97.811  63.223  1.00 50.34  ? 243 ARG   A CB     1 
ATOM   1882  C  CG     . ARG   A 1  243 ? -27.920 -96.358  62.782  1.00 50.48  ? 243 ARG   A CG     1 
ATOM   1883  C  CD     . ARG   A 1  243 ? -27.074 -96.132  61.507  1.00 56.10  ? 243 ARG   A CD     1 
ATOM   1884  N  NE     . ARG   A 1  243 ? -25.655 -96.420  61.697  1.00 52.72  ? 243 ARG   A NE     1 
ATOM   1885  C  CZ     . ARG   A 1  243 ? -24.766 -95.570  62.188  1.00 51.18  ? 243 ARG   A CZ     1 
ATOM   1886  N  NH1    . ARG   A 1  243 ? -25.077 -94.307  62.427  1.00 53.04  ? 243 ARG   A NH1    1 
ATOM   1887  N  NH2    . ARG   A 1  243 ? -23.524 -95.988  62.404  1.00 49.98  ? 243 ARG   A NH2    1 
ATOM   1888  N  N      . PHE   A 1  244 ? -27.921 -99.412  66.345  1.00 58.97  ? 244 PHE   A N      1 
ATOM   1889  C  CA     . PHE   A 1  244 ? -27.290 -100.503 67.071  1.00 55.11  ? 244 PHE   A CA     1 
ATOM   1890  C  C      . PHE   A 1  244 ? -28.060 -100.812 68.354  1.00 54.38  ? 244 PHE   A C      1 
ATOM   1891  O  O      . PHE   A 1  244 ? -28.743 -99.958  68.928  1.00 51.07  ? 244 PHE   A O      1 
ATOM   1892  C  CB     . PHE   A 1  244 ? -25.815 -100.190 67.380  1.00 53.89  ? 244 PHE   A CB     1 
ATOM   1893  C  CG     . PHE   A 1  244 ? -24.912 -100.226 66.170  1.00 52.86  ? 244 PHE   A CG     1 
ATOM   1894  C  CD1    . PHE   A 1  244 ? -24.699 -101.417 65.488  1.00 57.17  ? 244 PHE   A CD1    1 
ATOM   1895  C  CD2    . PHE   A 1  244 ? -24.224 -99.100  65.761  1.00 54.52  ? 244 PHE   A CD2    1 
ATOM   1896  C  CE1    . PHE   A 1  244 ? -23.862 -101.476 64.387  1.00 57.97  ? 244 PHE   A CE1    1 
ATOM   1897  C  CE2    . PHE   A 1  244 ? -23.372 -99.153  64.659  1.00 56.84  ? 244 PHE   A CE2    1 
ATOM   1898  C  CZ     . PHE   A 1  244 ? -23.193 -100.345 63.971  1.00 56.97  ? 244 PHE   A CZ     1 
ATOM   1899  N  N      . ASP   A 1  245 ? -27.966 -102.066 68.775  1.00 61.60  ? 245 ASP   A N      1 
ATOM   1900  C  CA     . ASP   A 1  245 ? -28.534 -102.470 70.048  1.00 59.33  ? 245 ASP   A CA     1 
ATOM   1901  C  C      . ASP   A 1  245 ? -27.941 -101.571 71.130  1.00 56.88  ? 245 ASP   A C      1 
ATOM   1902  O  O      . ASP   A 1  245 ? -26.740 -101.284 71.126  1.00 55.95  ? 245 ASP   A O      1 
ATOM   1903  C  CB     . ASP   A 1  245 ? -28.224 -103.962 70.270  1.00 62.18  ? 245 ASP   A CB     1 
ATOM   1904  C  CG     . ASP   A 1  245 ? -28.852 -104.543 71.530  1.00 67.47  ? 245 ASP   A CG     1 
ATOM   1905  O  OD1    . ASP   A 1  245 ? -30.047 -104.260 71.756  1.00 68.10  ? 245 ASP   A OD1    1 
ATOM   1906  O  OD2    . ASP   A 1  245 ? -28.188 -105.350 72.237  1.00 69.25  ? 245 ASP   A OD2    1 
ATOM   1907  N  N      . GLY   A 1  246 ? -28.792 -101.052 72.002  1.00 56.18  ? 246 GLY   A N      1 
ATOM   1908  C  CA     . GLY   A 1  246 ? -28.323 -100.127 73.020  1.00 49.66  ? 246 GLY   A CA     1 
ATOM   1909  C  C      . GLY   A 1  246 ? -29.474 -99.704  73.904  1.00 57.69  ? 246 GLY   A C      1 
ATOM   1910  O  O      . GLY   A 1  246 ? -30.644 -99.998  73.629  1.00 55.66  ? 246 GLY   A O      1 
ATOM   1911  N  N      . ALA   A 1  247 ? -29.119 -99.005  74.986  1.00 59.36  ? 247 ALA   A N      1 
ATOM   1912  C  CA     . ALA   A 1  247 ? -30.092 -98.502  75.950  1.00 56.81  ? 247 ALA   A CA     1 
ATOM   1913  C  C      . ALA   A 1  247 ? -30.161 -96.983  76.004  1.00 63.94  ? 247 ALA   A C      1 
ATOM   1914  O  O      . ALA   A 1  247 ? -31.077 -96.443  76.641  1.00 68.64  ? 247 ALA   A O      1 
ATOM   1915  C  CB     . ALA   A 1  247 ? -29.774 -99.035  77.353  1.00 61.18  ? 247 ALA   A CB     1 
ATOM   1916  N  N      . LEU   A 1  248 ? -29.227 -96.293  75.346  1.00 59.89  ? 248 LEU   A N      1 
ATOM   1917  C  CA     . LEU   A 1  248 ? -29.102 -94.842  75.364  1.00 59.87  ? 248 LEU   A CA     1 
ATOM   1918  C  C      . LEU   A 1  248 ? -29.317 -94.276  73.968  1.00 59.50  ? 248 LEU   A C      1 
ATOM   1919  O  O      . LEU   A 1  248 ? -28.652 -94.714  73.017  1.00 52.75  ? 248 LEU   A O      1 
ATOM   1920  C  CB     . LEU   A 1  248 ? -27.715 -94.422  75.849  1.00 61.70  ? 248 LEU   A CB     1 
ATOM   1921  C  CG     . LEU   A 1  248 ? -27.546 -92.905  75.936  1.00 58.56  ? 248 LEU   A CG     1 
ATOM   1922  C  CD1    . LEU   A 1  248 ? -28.520 -92.277  76.961  1.00 55.26  ? 248 LEU   A CD1    1 
ATOM   1923  C  CD2    . LEU   A 1  248 ? -26.094 -92.520  76.164  1.00 55.05  ? 248 LEU   A CD2    1 
ATOM   1924  N  N      . ASN   A 1  249 ? -30.194 -93.267  73.868  1.00 56.94  ? 249 ASN   A N      1 
ATOM   1925  C  CA     . ASN   A 1  249 ? -30.549 -92.597  72.611  1.00 52.32  ? 249 ASN   A CA     1 
ATOM   1926  C  C      . ASN   A 1  249 ? -31.029 -93.613  71.573  1.00 58.31  ? 249 ASN   A C      1 
ATOM   1927  O  O      . ASN   A 1  249 ? -30.405 -93.857  70.536  1.00 57.22  ? 249 ASN   A O      1 
ATOM   1928  C  CB     . ASN   A 1  249 ? -29.377 -91.773  72.065  1.00 52.12  ? 249 ASN   A CB     1 
ATOM   1929  C  CG     . ASN   A 1  249 ? -29.058 -90.556  72.917  1.00 52.45  ? 249 ASN   A CG     1 
ATOM   1930  O  OD1    . ASN   A 1  249 ? -29.910 -90.033  73.631  1.00 55.63  ? 249 ASN   A OD1    1 
ATOM   1931  N  ND2    . ASN   A 1  249 ? -27.813 -90.112  72.856  1.00 50.67  ? 249 ASN   A ND2    1 
ATOM   1932  N  N      . VAL   A 1  250 ? -32.174 -94.212  71.889  1.00 56.84  ? 250 VAL   A N      1 
ATOM   1933  C  CA     . VAL   A 1  250 ? -32.737 -95.253  71.039  1.00 54.83  ? 250 VAL   A CA     1 
ATOM   1934  C  C      . VAL   A 1  250 ? -33.814 -94.724  70.094  1.00 54.44  ? 250 VAL   A C      1 
ATOM   1935  O  O      . VAL   A 1  250 ? -34.152 -95.413  69.122  1.00 52.77  ? 250 VAL   A O      1 
ATOM   1936  C  CB     . VAL   A 1  250 ? -33.263 -96.419  71.908  1.00 60.44  ? 250 VAL   A CB     1 
ATOM   1937  C  CG1    . VAL   A 1  250 ? -32.103 -97.178  72.496  1.00 54.76  ? 250 VAL   A CG1    1 
ATOM   1938  C  CG2    . VAL   A 1  250 ? -34.100 -95.881  73.076  1.00 63.86  ? 250 VAL   A CG2    1 
ATOM   1939  N  N      . ASP   A 1  251 ? -34.347 -93.520  70.333  1.00 52.50  ? 251 ASP   A N      1 
ATOM   1940  C  CA     . ASP   A 1  251 ? -35.248 -92.857  69.397  1.00 54.44  ? 251 ASP   A CA     1 
ATOM   1941  C  C      . ASP   A 1  251 ? -34.935 -91.364  69.367  1.00 55.69  ? 251 ASP   A C      1 
ATOM   1942  O  O      . ASP   A 1  251 ? -34.351 -90.821  70.302  1.00 63.13  ? 251 ASP   A O      1 
ATOM   1943  C  CB     . ASP   A 1  251 ? -36.735 -93.087  69.742  1.00 58.03  ? 251 ASP   A CB     1 
ATOM   1944  C  CG     . ASP   A 1  251 ? -37.134 -92.533  71.126  1.00 68.37  ? 251 ASP   A CG     1 
ATOM   1945  O  OD1    . ASP   A 1  251 ? -36.883 -91.331  71.408  1.00 65.99  ? 251 ASP   A OD1    1 
ATOM   1946  O  OD2    . ASP   A 1  251 ? -37.752 -93.294  71.919  1.00 68.55  ? 251 ASP   A OD2    1 
ATOM   1947  N  N      . LEU   A 1  252 ? -35.347 -90.696  68.283  1.00 53.11  ? 252 LEU   A N      1 
ATOM   1948  C  CA     . LEU   A 1  252 ? -35.113 -89.260  68.120  1.00 53.61  ? 252 LEU   A CA     1 
ATOM   1949  C  C      . LEU   A 1  252 ? -35.723 -88.448  69.253  1.00 56.14  ? 252 LEU   A C      1 
ATOM   1950  O  O      . LEU   A 1  252 ? -35.365 -87.283  69.448  1.00 58.63  ? 252 LEU   A O      1 
ATOM   1951  C  CB     . LEU   A 1  252 ? -35.708 -88.778  66.795  1.00 54.16  ? 252 LEU   A CB     1 
ATOM   1952  C  CG     . LEU   A 1  252 ? -35.259 -89.534  65.553  1.00 53.39  ? 252 LEU   A CG     1 
ATOM   1953  C  CD1    . LEU   A 1  252 ? -36.008 -89.006  64.365  1.00 52.74  ? 252 LEU   A CD1    1 
ATOM   1954  C  CD2    . LEU   A 1  252 ? -33.771 -89.353  65.377  1.00 49.80  ? 252 LEU   A CD2    1 
ATOM   1955  N  N      . THR   A 1  253 ? -36.672 -89.018  69.979  1.00 57.51  ? 253 THR   A N      1 
ATOM   1956  C  CA     . THR   A 1  253 ? -37.231 -88.283  71.097  1.00 55.93  ? 253 THR   A CA     1 
ATOM   1957  C  C      . THR   A 1  253 ? -36.190 -88.176  72.189  1.00 58.98  ? 253 THR   A C      1 
ATOM   1958  O  O      . THR   A 1  253 ? -36.056 -87.134  72.844  1.00 59.32  ? 253 THR   A O      1 
ATOM   1959  C  CB     . THR   A 1  253 ? -38.490 -88.983  71.612  1.00 55.53  ? 253 THR   A CB     1 
ATOM   1960  O  OG1    . THR   A 1  253 ? -39.226 -89.518  70.504  1.00 52.04  ? 253 THR   A OG1    1 
ATOM   1961  C  CG2    . THR   A 1  253 ? -39.388 -87.974  72.309  1.00 50.76  ? 253 THR   A CG2    1 
ATOM   1962  N  N      . GLU   A 1  254 ? -35.408 -89.238  72.361  1.00 58.95  ? 254 GLU   A N      1 
ATOM   1963  C  CA     . GLU   A 1  254 ? -34.452 -89.264  73.451  1.00 58.90  ? 254 GLU   A CA     1 
ATOM   1964  C  C      . GLU   A 1  254 ? -33.441 -88.130  73.340  1.00 62.08  ? 254 GLU   A C      1 
ATOM   1965  O  O      . GLU   A 1  254 ? -32.942 -87.652  74.372  1.00 60.02  ? 254 GLU   A O      1 
ATOM   1966  C  CB     . GLU   A 1  254 ? -33.738 -90.605  73.487  1.00 58.40  ? 254 GLU   A CB     1 
ATOM   1967  C  CG     . GLU   A 1  254 ? -33.281 -90.961  74.884  1.00 63.58  ? 254 GLU   A CG     1 
ATOM   1968  C  CD     . GLU   A 1  254 ? -32.995 -92.442  75.052  1.00 71.03  ? 254 GLU   A CD     1 
ATOM   1969  O  OE1    . GLU   A 1  254 ? -33.821 -93.280  74.587  1.00 69.97  ? 254 GLU   A OE1    1 
ATOM   1970  O  OE2    . GLU   A 1  254 ? -31.951 -92.751  75.687  1.00 65.53  ? 254 GLU   A OE2    1 
ATOM   1971  N  N      . PHE   A 1  255 ? -33.124 -87.683  72.105  1.00 56.53  ? 255 PHE   A N      1 
ATOM   1972  C  CA     . PHE   A 1  255 ? -32.162 -86.588  71.948  1.00 53.09  ? 255 PHE   A CA     1 
ATOM   1973  C  C      . PHE   A 1  255 ? -32.712 -85.285  72.522  1.00 54.72  ? 255 PHE   A C      1 
ATOM   1974  O  O      . PHE   A 1  255 ? -31.981 -84.545  73.194  1.00 52.91  ? 255 PHE   A O      1 
ATOM   1975  C  CB     . PHE   A 1  255 ? -31.763 -86.388  70.486  1.00 45.53  ? 255 PHE   A CB     1 
ATOM   1976  C  CG     . PHE   A 1  255 ? -30.854 -87.479  69.905  1.00 51.71  ? 255 PHE   A CG     1 
ATOM   1977  C  CD1    . PHE   A 1  255 ? -31.372 -88.687  69.442  1.00 53.88  ? 255 PHE   A CD1    1 
ATOM   1978  C  CD2    . PHE   A 1  255 ? -29.489 -87.287  69.798  1.00 44.19  ? 255 PHE   A CD2    1 
ATOM   1979  C  CE1    . PHE   A 1  255 ? -30.545 -89.677  68.882  1.00 43.89  ? 255 PHE   A CE1    1 
ATOM   1980  C  CE2    . PHE   A 1  255 ? -28.670 -88.274  69.242  1.00 44.45  ? 255 PHE   A CE2    1 
ATOM   1981  C  CZ     . PHE   A 1  255 ? -29.203 -89.471  68.797  1.00 41.62  ? 255 PHE   A CZ     1 
ATOM   1982  N  N      . GLN   A 1  256 ? -33.991 -84.981  72.271  1.00 54.51  ? 256 GLN   A N      1 
ATOM   1983  C  CA     . GLN   A 1  256 ? -34.633 -83.871  72.968  1.00 52.90  ? 256 GLN   A CA     1 
ATOM   1984  C  C      . GLN   A 1  256 ? -34.523 -84.062  74.474  1.00 56.35  ? 256 GLN   A C      1 
ATOM   1985  O  O      . GLN   A 1  256 ? -33.909 -83.246  75.171  1.00 52.74  ? 256 GLN   A O      1 
ATOM   1986  C  CB     . GLN   A 1  256 ? -36.100 -83.752  72.555  1.00 54.91  ? 256 GLN   A CB     1 
ATOM   1987  C  CG     . GLN   A 1  256 ? -36.339 -83.991  71.051  1.00 61.79  ? 256 GLN   A CG     1 
ATOM   1988  C  CD     . GLN   A 1  256 ? -37.810 -84.340  70.675  1.00 68.32  ? 256 GLN   A CD     1 
ATOM   1989  O  OE1    . GLN   A 1  256 ? -38.048 -85.046  69.681  1.00 66.35  ? 256 GLN   A OE1    1 
ATOM   1990  N  NE2    . GLN   A 1  256 ? -38.784 -83.841  71.458  1.00 54.89  ? 256 GLN   A NE2    1 
ATOM   1991  N  N      . THR   A 1  257 ? -35.103 -85.161  74.985  1.00 56.35  ? 257 THR   A N      1 
ATOM   1992  C  CA     . THR   A 1  257 ? -35.097 -85.439  76.422  1.00 55.45  ? 257 THR   A CA     1 
ATOM   1993  C  C      . THR   A 1  257 ? -33.724 -85.256  77.028  1.00 54.80  ? 257 THR   A C      1 
ATOM   1994  O  O      . THR   A 1  257 ? -33.573 -84.609  78.065  1.00 59.62  ? 257 THR   A O      1 
ATOM   1995  C  CB     . THR   A 1  257 ? -35.549 -86.863  76.717  1.00 52.93  ? 257 THR   A CB     1 
ATOM   1996  O  OG1    . THR   A 1  257 ? -36.916 -87.034  76.360  1.00 51.24  ? 257 THR   A OG1    1 
ATOM   1997  C  CG2    . THR   A 1  257 ? -35.361 -87.144  78.182  1.00 54.51  ? 257 THR   A CG2    1 
ATOM   1998  N  N      . ASN   A 1  258 ? -32.716 -85.855  76.411  1.00 54.63  ? 258 ASN   A N      1 
ATOM   1999  C  CA     . ASN   A 1  258 ? -31.399 -85.928  77.024  1.00 55.83  ? 258 ASN   A CA     1 
ATOM   2000  C  C      . ASN   A 1  258 ? -30.618 -84.637  76.891  1.00 49.70  ? 258 ASN   A C      1 
ATOM   2001  O  O      . ASN   A 1  258 ? -29.909 -84.253  77.823  1.00 52.41  ? 258 ASN   A O      1 
ATOM   2002  C  CB     . ASN   A 1  258 ? -30.624 -87.071  76.395  1.00 54.81  ? 258 ASN   A CB     1 
ATOM   2003  C  CG     . ASN   A 1  258 ? -31.124 -88.380  76.859  1.00 55.68  ? 258 ASN   A CG     1 
ATOM   2004  O  OD1    . ASN   A 1  258 ? -31.971 -88.427  77.745  1.00 58.04  ? 258 ASN   A OD1    1 
ATOM   2005  N  ND2    . ASN   A 1  258 ? -30.695 -89.450  76.217  1.00 57.84  ? 258 ASN   A ND2    1 
ATOM   2006  N  N      . LEU   A 1  259 ? -30.745 -83.957  75.761  1.00 53.39  ? 259 LEU   A N      1 
ATOM   2007  C  CA     . LEU   A 1  259 ? -29.902 -82.824  75.428  1.00 51.79  ? 259 LEU   A CA     1 
ATOM   2008  C  C      . LEU   A 1  259 ? -30.633 -81.489  75.371  1.00 51.78  ? 259 LEU   A C      1 
ATOM   2009  O  O      . LEU   A 1  259 ? -29.970 -80.448  75.369  1.00 49.64  ? 259 LEU   A O      1 
ATOM   2010  C  CB     . LEU   A 1  259 ? -29.216 -83.089  74.083  1.00 48.78  ? 259 LEU   A CB     1 
ATOM   2011  C  CG     . LEU   A 1  259 ? -28.265 -84.262  74.238  1.00 43.67  ? 259 LEU   A CG     1 
ATOM   2012  C  CD1    . LEU   A 1  259 ? -27.853 -84.829  72.913  1.00 42.72  ? 259 LEU   A CD1    1 
ATOM   2013  C  CD2    . LEU   A 1  259 ? -27.067 -83.730  74.954  1.00 47.04  ? 259 LEU   A CD2    1 
ATOM   2014  N  N      . VAL   A 1  260 ? -31.960 -81.473  75.346  1.00 52.45  ? 260 VAL   A N      1 
ATOM   2015  C  CA     . VAL   A 1  260 ? -32.653 -80.206  75.145  1.00 54.33  ? 260 VAL   A CA     1 
ATOM   2016  C  C      . VAL   A 1  260 ? -33.719 -79.997  76.216  1.00 54.60  ? 260 VAL   A C      1 
ATOM   2017  O  O      . VAL   A 1  260 ? -34.876 -80.404  76.036  1.00 50.23  ? 260 VAL   A O      1 
ATOM   2018  C  CB     . VAL   A 1  260 ? -33.255 -80.143  73.736  1.00 50.65  ? 260 VAL   A CB     1 
ATOM   2019  C  CG1    . VAL   A 1  260 ? -33.948 -78.821  73.526  1.00 51.60  ? 260 VAL   A CG1    1 
ATOM   2020  C  CG2    . VAL   A 1  260 ? -32.174 -80.364  72.708  1.00 50.07  ? 260 VAL   A CG2    1 
ATOM   2021  N  N      . PRO   A 1  261 ? -33.382 -79.362  77.336  1.00 55.36  ? 261 PRO   A N      1 
ATOM   2022  C  CA     . PRO   A 1  261 ? -34.411 -79.054  78.336  1.00 57.23  ? 261 PRO   A CA     1 
ATOM   2023  C  C      . PRO   A 1  261 ? -35.273 -77.883  77.887  1.00 58.19  ? 261 PRO   A C      1 
ATOM   2024  O  O      . PRO   A 1  261 ? -36.495 -78.008  77.779  1.00 49.79  ? 261 PRO   A O      1 
ATOM   2025  C  CB     . PRO   A 1  261 ? -33.595 -78.718  79.595  1.00 53.16  ? 261 PRO   A CB     1 
ATOM   2026  C  CG     . PRO   A 1  261 ? -32.311 -78.212  79.084  1.00 59.33  ? 261 PRO   A CG     1 
ATOM   2027  C  CD     . PRO   A 1  261 ? -32.043 -78.927  77.770  1.00 59.30  ? 261 PRO   A CD     1 
ATOM   2028  N  N      . TYR   A 1  262 ? -34.647 -76.726  77.657  1.00 63.20  ? 262 TYR   A N      1 
ATOM   2029  C  CA     . TYR   A 1  262 ? -35.462 -75.686  77.052  1.00 55.18  ? 262 TYR   A CA     1 
ATOM   2030  C  C      . TYR   A 1  262 ? -35.437 -75.855  75.532  1.00 54.77  ? 262 TYR   A C      1 
ATOM   2031  O  O      . TYR   A 1  262 ? -34.405 -76.234  74.973  1.00 54.68  ? 262 TYR   A O      1 
ATOM   2032  C  CB     . TYR   A 1  262 ? -34.959 -74.298  77.458  1.00 42.39  ? 262 TYR   A CB     1 
ATOM   2033  N  N      . PRO   A 1  263 ? -36.581 -75.622  74.845  1.00 56.98  ? 263 PRO   A N      1 
ATOM   2034  C  CA     . PRO   A 1  263 ? -36.714 -76.005  73.428  1.00 52.48  ? 263 PRO   A CA     1 
ATOM   2035  C  C      . PRO   A 1  263 ? -35.949 -75.163  72.418  1.00 52.05  ? 263 PRO   A C      1 
ATOM   2036  O  O      . PRO   A 1  263 ? -35.313 -75.739  71.536  1.00 50.03  ? 263 PRO   A O      1 
ATOM   2037  C  CB     . PRO   A 1  263 ? -38.221 -75.873  73.175  1.00 52.33  ? 263 PRO   A CB     1 
ATOM   2038  C  CG     . PRO   A 1  263 ? -38.836 -76.035  74.469  1.00 56.42  ? 263 PRO   A CG     1 
ATOM   2039  C  CD     . PRO   A 1  263 ? -37.894 -75.384  75.456  1.00 58.52  ? 263 PRO   A CD     1 
ATOM   2040  N  N      . ARG   A 1  264 ? -36.042 -73.829  72.465  1.00 58.08  ? 264 ARG   A N      1 
ATOM   2041  C  CA     . ARG   A 1  264 ? -35.236 -73.019  71.550  1.00 52.67  ? 264 ARG   A CA     1 
ATOM   2042  C  C      . ARG   A 1  264 ? -33.781 -73.415  71.655  1.00 53.85  ? 264 ARG   A C      1 
ATOM   2043  O  O      . ARG   A 1  264 ? -33.127 -73.727  70.656  1.00 55.10  ? 264 ARG   A O      1 
ATOM   2044  C  CB     . ARG   A 1  264 ? -35.352 -71.526  71.866  1.00 48.17  ? 264 ARG   A CB     1 
ATOM   2045  C  CG     . ARG   A 1  264 ? -36.642 -70.919  71.468  1.00 49.91  ? 264 ARG   A CG     1 
ATOM   2046  C  CD     . ARG   A 1  264 ? -36.827 -69.532  72.037  1.00 51.27  ? 264 ARG   A CD     1 
ATOM   2047  N  NE     . ARG   A 1  264 ? -35.920 -68.568  71.435  1.00 57.39  ? 264 ARG   A NE     1 
ATOM   2048  C  CZ     . ARG   A 1  264 ? -36.148 -67.979  70.266  1.00 56.58  ? 264 ARG   A CZ     1 
ATOM   2049  N  NH1    . ARG   A 1  264 ? -37.188 -68.319  69.515  1.00 46.21  ? 264 ARG   A NH1    1 
ATOM   2050  N  NH2    . ARG   A 1  264 ? -35.297 -67.049  69.828  1.00 52.94  ? 264 ARG   A NH2    1 
ATOM   2051  N  N      . ILE   A 1  265 ? -33.262 -73.404  72.874  1.00 47.85  ? 265 ILE   A N      1 
ATOM   2052  C  CA     . ILE   A 1  265 ? -31.848 -73.593  73.085  1.00 45.74  ? 265 ILE   A CA     1 
ATOM   2053  C  C      . ILE   A 1  265 ? -31.523 -75.044  72.790  1.00 49.28  ? 265 ILE   A C      1 
ATOM   2054  O  O      . ILE   A 1  265 ? -31.239 -75.815  73.714  1.00 52.09  ? 265 ILE   A O      1 
ATOM   2055  C  CB     . ILE   A 1  265 ? -31.482 -73.216  74.515  1.00 47.53  ? 265 ILE   A CB     1 
ATOM   2056  C  CG1    . ILE   A 1  265 ? -31.810 -71.751  74.710  1.00 49.77  ? 265 ILE   A CG1    1 
ATOM   2057  C  CG2    . ILE   A 1  265 ? -30.005 -73.415  74.715  1.00 46.59  ? 265 ILE   A CG2    1 
ATOM   2058  C  CD1    . ILE   A 1  265 ? -31.415 -71.209  76.038  1.00 50.69  ? 265 ILE   A CD1    1 
ATOM   2059  N  N      . HIS   A 1  266 ? -31.572 -75.432  71.508  1.00 46.91  ? 266 HIS   A N      1 
ATOM   2060  C  CA     . HIS   A 1  266 ? -31.458 -76.842  71.143  1.00 45.13  ? 266 HIS   A CA     1 
ATOM   2061  C  C      . HIS   A 1  266 ? -30.292 -77.124  70.204  1.00 47.57  ? 266 HIS   A C      1 
ATOM   2062  O  O      . HIS   A 1  266 ? -30.429 -77.899  69.248  1.00 45.28  ? 266 HIS   A O      1 
ATOM   2063  C  CB     . HIS   A 1  266 ? -32.789 -77.345  70.561  1.00 40.96  ? 266 HIS   A CB     1 
ATOM   2064  C  CG     . HIS   A 1  266 ? -33.230 -76.663  69.298  1.00 51.25  ? 266 HIS   A CG     1 
ATOM   2065  N  ND1    . HIS   A 1  266 ? -34.304 -75.795  69.261  1.00 54.94  ? 266 HIS   A ND1    1 
ATOM   2066  C  CD2    . HIS   A 1  266 ? -32.823 -76.803  68.013  1.00 54.40  ? 266 HIS   A CD2    1 
ATOM   2067  C  CE1    . HIS   A 1  266 ? -34.491 -75.376  68.023  1.00 48.99  ? 266 HIS   A CE1    1 
ATOM   2068  N  NE2    . HIS   A 1  266 ? -33.610 -75.977  67.244  1.00 50.63  ? 266 HIS   A NE2    1 
ATOM   2069  N  N      . PHE   A 1  267 ? -29.119 -76.552  70.513  1.00 50.53  ? 267 PHE   A N      1 
ATOM   2070  C  CA     . PHE   A 1  267 ? -27.922 -76.690  69.682  1.00 45.70  ? 267 PHE   A CA     1 
ATOM   2071  C  C      . PHE   A 1  267 ? -26.820 -77.254  70.557  1.00 40.49  ? 267 PHE   A C      1 
ATOM   2072  O  O      . PHE   A 1  267 ? -26.051 -76.503  71.174  1.00 42.84  ? 267 PHE   A O      1 
ATOM   2073  C  CB     . PHE   A 1  267 ? -27.528 -75.356  69.052  1.00 49.63  ? 267 PHE   A CB     1 
ATOM   2074  C  CG     . PHE   A 1  267 ? -28.622 -74.760  68.203  1.00 47.67  ? 267 PHE   A CG     1 
ATOM   2075  C  CD1    . PHE   A 1  267 ? -29.601 -73.959  68.780  1.00 47.32  ? 267 PHE   A CD1    1 
ATOM   2076  C  CD2    . PHE   A 1  267 ? -28.720 -75.063  66.858  1.00 43.84  ? 267 PHE   A CD2    1 
ATOM   2077  C  CE1    . PHE   A 1  267 ? -30.627 -73.444  68.024  1.00 49.44  ? 267 PHE   A CE1    1 
ATOM   2078  C  CE2    . PHE   A 1  267 ? -29.744 -74.547  66.094  1.00 45.79  ? 267 PHE   A CE2    1 
ATOM   2079  C  CZ     . PHE   A 1  267 ? -30.702 -73.740  66.672  1.00 46.87  ? 267 PHE   A CZ     1 
ATOM   2080  N  N      . PRO   A 1  268 ? -26.736 -78.579  70.666  1.00 37.73  ? 268 PRO   A N      1 
ATOM   2081  C  CA     . PRO   A 1  268 ? -25.724 -79.207  71.512  1.00 37.05  ? 268 PRO   A CA     1 
ATOM   2082  C  C      . PRO   A 1  268 ? -24.371 -79.151  70.829  1.00 36.97  ? 268 PRO   A C      1 
ATOM   2083  O  O      . PRO   A 1  268 ? -24.212 -79.659  69.719  1.00 43.66  ? 268 PRO   A O      1 
ATOM   2084  C  CB     . PRO   A 1  268 ? -26.224 -80.652  71.642  1.00 39.11  ? 268 PRO   A CB     1 
ATOM   2085  C  CG     . PRO   A 1  268 ? -27.642 -80.629  71.208  1.00 39.00  ? 268 PRO   A CG     1 
ATOM   2086  C  CD     . PRO   A 1  268 ? -27.701 -79.566  70.171  1.00 40.56  ? 268 PRO   A CD     1 
ATOM   2087  N  N      . LEU   A 1  269 ? -23.396 -78.537  71.494  1.00 36.48  ? 269 LEU   A N      1 
ATOM   2088  C  CA     . LEU   A 1  269 ? -22.011 -78.606  71.042  1.00 35.00  ? 269 LEU   A CA     1 
ATOM   2089  C  C      . LEU   A 1  269 ? -21.523 -80.058  70.998  1.00 36.72  ? 269 LEU   A C      1 
ATOM   2090  O  O      . LEU   A 1  269 ? -21.752 -80.832  71.926  1.00 40.53  ? 269 LEU   A O      1 
ATOM   2091  C  CB     . LEU   A 1  269 ? -21.122 -77.778  71.978  1.00 33.07  ? 269 LEU   A CB     1 
ATOM   2092  C  CG     . LEU   A 1  269 ? -19.619 -77.836  71.698  1.00 36.46  ? 269 LEU   A CG     1 
ATOM   2093  C  CD1    . LEU   A 1  269 ? -19.301 -77.389  70.267  1.00 38.35  ? 269 LEU   A CD1    1 
ATOM   2094  C  CD2    . LEU   A 1  269 ? -18.796 -77.082  72.741  1.00 31.68  ? 269 LEU   A CD2    1 
ATOM   2095  N  N      . ALA   A 1  270 ? -20.841 -80.439  69.920  1.00 35.92  ? 270 ALA   A N      1 
ATOM   2096  C  CA     . ALA   A 1  270 ? -20.204 -81.744  69.839  1.00 31.85  ? 270 ALA   A CA     1 
ATOM   2097  C  C      . ALA   A 1  270 ? -18.687 -81.593  69.834  1.00 41.09  ? 270 ALA   A C      1 
ATOM   2098  O  O      . ALA   A 1  270 ? -18.137 -80.817  69.051  1.00 39.40  ? 270 ALA   A O      1 
ATOM   2099  C  CB     . ALA   A 1  270 ? -20.646 -82.498  68.595  1.00 26.44  ? 270 ALA   A CB     1 
ATOM   2100  N  N      . THR   A 1  271 ? -18.019 -82.337  70.715  1.00 46.69  ? 271 THR   A N      1 
ATOM   2101  C  CA     . THR   A 1  271 ? -16.578 -82.543  70.687  1.00 39.88  ? 271 THR   A CA     1 
ATOM   2102  C  C      . THR   A 1  271 ? -16.307 -84.015  70.413  1.00 39.89  ? 271 THR   A C      1 
ATOM   2103  O  O      . THR   A 1  271 ? -17.066 -84.881  70.865  1.00 42.11  ? 271 THR   A O      1 
ATOM   2104  C  CB     . THR   A 1  271 ? -15.935 -82.138  72.008  1.00 40.22  ? 271 THR   A CB     1 
ATOM   2105  O  OG1    . THR   A 1  271 ? -16.535 -80.923  72.470  1.00 47.13  ? 271 THR   A OG1    1 
ATOM   2106  C  CG2    . THR   A 1  271 ? -14.458 -81.908  71.811  1.00 40.53  ? 271 THR   A CG2    1 
ATOM   2107  N  N      . TYR   A 1  272 ? -15.234 -84.295  69.666  1.00 39.27  ? 272 TYR   A N      1 
ATOM   2108  C  CA     . TYR   A 1  272 ? -14.892 -85.644  69.201  1.00 39.95  ? 272 TYR   A CA     1 
ATOM   2109  C  C      . TYR   A 1  272 ? -13.380 -85.842  69.209  1.00 42.68  ? 272 TYR   A C      1 
ATOM   2110  O  O      . TYR   A 1  272 ? -12.647 -85.013  68.654  1.00 49.60  ? 272 TYR   A O      1 
ATOM   2111  C  CB     . TYR   A 1  272 ? -15.411 -85.901  67.778  1.00 36.96  ? 272 TYR   A CB     1 
ATOM   2112  C  CG     . TYR   A 1  272 ? -15.147 -87.302  67.260  1.00 39.72  ? 272 TYR   A CG     1 
ATOM   2113  C  CD1    . TYR   A 1  272 ? -16.040 -88.329  67.478  1.00 37.69  ? 272 TYR   A CD1    1 
ATOM   2114  C  CD2    . TYR   A 1  272 ? -13.962 -87.608  66.610  1.00 37.70  ? 272 TYR   A CD2    1 
ATOM   2115  C  CE1    . TYR   A 1  272 ? -15.778 -89.607  67.018  1.00 37.92  ? 272 TYR   A CE1    1 
ATOM   2116  C  CE2    . TYR   A 1  272 ? -13.696 -88.887  66.161  1.00 35.96  ? 272 TYR   A CE2    1 
ATOM   2117  C  CZ     . TYR   A 1  272 ? -14.601 -89.886  66.359  1.00 35.00  ? 272 TYR   A CZ     1 
ATOM   2118  O  OH     . TYR   A 1  272 ? -14.331 -91.166  65.884  1.00 35.68  ? 272 TYR   A OH     1 
ATOM   2119  N  N      . ALA   A 1  273 ? -12.927 -86.957  69.789  1.00 35.78  ? 273 ALA   A N      1 
ATOM   2120  C  CA     . ALA   A 1  273 ? -11.524 -87.358  69.827  1.00 39.90  ? 273 ALA   A CA     1 
ATOM   2121  C  C      . ALA   A 1  273 ? -11.446 -88.876  69.902  1.00 43.98  ? 273 ALA   A C      1 
ATOM   2122  O  O      . ALA   A 1  273 ? -12.351 -89.519  70.456  1.00 42.46  ? 273 ALA   A O      1 
ATOM   2123  C  CB     . ALA   A 1  273 ? -10.771 -86.745  71.019  1.00 35.77  ? 273 ALA   A CB     1 
ATOM   2124  N  N      . PRO   A 1  274 ? -10.360 -89.475  69.411  1.00 39.49  ? 274 PRO   A N      1 
ATOM   2125  C  CA     . PRO   A 1  274 ? -9.152  -88.841  68.875  1.00 45.18  ? 274 PRO   A CA     1 
ATOM   2126  C  C      . PRO   A 1  274 ? -9.084  -88.831  67.349  1.00 45.25  ? 274 PRO   A C      1 
ATOM   2127  O  O      . PRO   A 1  274 ? -9.376  -89.837  66.710  1.00 45.92  ? 274 PRO   A O      1 
ATOM   2128  C  CB     . PRO   A 1  274 ? -8.042  -89.726  69.450  1.00 41.48  ? 274 PRO   A CB     1 
ATOM   2129  C  CG     . PRO   A 1  274 ? -8.663  -91.091  69.374  1.00 47.29  ? 274 PRO   A CG     1 
ATOM   2130  C  CD     . PRO   A 1  274 ? -10.117 -90.893  69.720  1.00 39.95  ? 274 PRO   A CD     1 
ATOM   2131  N  N      . VAL   A 1  275 ? -8.659  -87.734  66.730  1.00 44.04  ? 275 VAL   A N      1 
ATOM   2132  C  CA     . VAL   A 1  275 ? -8.482  -87.675  65.282  1.00 45.06  ? 275 VAL   A CA     1 
ATOM   2133  C  C      . VAL   A 1  275 ? -7.007  -87.875  64.978  1.00 44.38  ? 275 VAL   A C      1 
ATOM   2134  O  O      . VAL   A 1  275 ? -6.196  -86.966  65.172  1.00 43.92  ? 275 VAL   A O      1 
ATOM   2135  C  CB     . VAL   A 1  275 ? -9.033  -86.366  64.702  1.00 38.22  ? 275 VAL   A CB     1 
ATOM   2136  C  CG1    . VAL   A 1  275 ? -8.709  -86.242  63.235  1.00 37.27  ? 275 VAL   A CG1    1 
ATOM   2137  C  CG2    . VAL   A 1  275 ? -10.527 -86.376  64.863  1.00 33.58  ? 275 VAL   A CG2    1 
ATOM   2138  N  N      . ILE   A 1  276 ? -6.667  -89.067  64.488  1.00 46.25  ? 276 ILE   A N      1 
ATOM   2139  C  CA     . ILE   A 1  276 ? -5.285  -89.494  64.280  1.00 50.94  ? 276 ILE   A CA     1 
ATOM   2140  C  C      . ILE   A 1  276 ? -5.058  -89.709  62.792  1.00 49.48  ? 276 ILE   A C      1 
ATOM   2141  O  O      . ILE   A 1  276 ? -5.884  -90.335  62.122  1.00 48.63  ? 276 ILE   A O      1 
ATOM   2142  C  CB     . ILE   A 1  276 ? -4.955  -90.802  65.035  1.00 52.87  ? 276 ILE   A CB     1 
ATOM   2143  C  CG1    . ILE   A 1  276 ? -5.211  -90.674  66.546  1.00 48.19  ? 276 ILE   A CG1    1 
ATOM   2144  C  CG2    . ILE   A 1  276 ? -3.547  -91.201  64.739  1.00 53.91  ? 276 ILE   A CG2    1 
ATOM   2145  C  CD1    . ILE   A 1  276 ? -4.558  -89.515  67.169  1.00 46.42  ? 276 ILE   A CD1    1 
ATOM   2146  N  N      . SER   A 1  277 ? -3.910  -89.246  62.295  1.00 52.21  ? 277 SER   A N      1 
ATOM   2147  C  CA     . SER   A 1  277 ? -3.565  -89.355  60.878  1.00 54.51  ? 277 SER   A CA     1 
ATOM   2148  C  C      . SER   A 1  277 ? -3.196  -90.782  60.475  1.00 53.37  ? 277 SER   A C      1 
ATOM   2149  O  O      . SER   A 1  277 ? -2.422  -91.457  61.153  1.00 58.79  ? 277 SER   A O      1 
ATOM   2150  C  CB     . SER   A 1  277 ? -2.395  -88.428  60.556  1.00 59.28  ? 277 SER   A CB     1 
ATOM   2151  O  OG     . SER   A 1  277 ? -1.813  -88.777  59.316  1.00 64.65  ? 277 SER   A OG     1 
ATOM   2152  N  N      . ALA   A 1  278 ? -3.727  -91.237  59.342  1.00 57.14  ? 278 ALA   A N      1 
ATOM   2153  C  CA     . ALA   A 1  278 ? -3.339  -92.560  58.861  1.00 60.55  ? 278 ALA   A CA     1 
ATOM   2154  C  C      . ALA   A 1  278 ? -1.912  -92.598  58.322  1.00 64.10  ? 278 ALA   A C      1 
ATOM   2155  O  O      . ALA   A 1  278 ? -1.397  -93.693  58.088  1.00 59.87  ? 278 ALA   A O      1 
ATOM   2156  C  CB     . ALA   A 1  278 ? -4.318  -93.049  57.791  1.00 51.54  ? 278 ALA   A CB     1 
ATOM   2157  N  N      . GLU   A 1  279 ? -1.268  -91.434  58.133  1.00 70.64  ? 279 GLU   A N      1 
ATOM   2158  C  CA     . GLU   A 1  279 ? 0.134   -91.370  57.712  1.00 69.12  ? 279 GLU   A CA     1 
ATOM   2159  C  C      . GLU   A 1  279 ? 1.108   -91.665  58.846  1.00 70.35  ? 279 GLU   A C      1 
ATOM   2160  O  O      . GLU   A 1  279 ? 2.214   -92.145  58.579  1.00 80.63  ? 279 GLU   A O      1 
ATOM   2161  C  CB     . GLU   A 1  279 ? 0.453   -89.994  57.101  1.00 74.34  ? 279 GLU   A CB     1 
ATOM   2162  C  CG     . GLU   A 1  279 ? -0.258  -89.696  55.789  1.00 74.34  ? 279 GLU   A CG     1 
ATOM   2163  C  CD     . GLU   A 1  279 ? -0.361  -90.939  54.932  1.00 76.50  ? 279 GLU   A CD     1 
ATOM   2164  O  OE1    . GLU   A 1  279 ? 0.663   -91.640  54.801  1.00 72.42  ? 279 GLU   A OE1    1 
ATOM   2165  O  OE2    . GLU   A 1  279 ? -1.455  -91.236  54.410  1.00 81.99  ? 279 GLU   A OE2    1 
ATOM   2166  N  N      . LYS   A 1  280 ? 0.747   -91.365  60.096  1.00 69.72  ? 280 LYS   A N      1 
ATOM   2167  C  CA     . LYS   A 1  280 ? 1.617   -91.695  61.225  1.00 75.14  ? 280 LYS   A CA     1 
ATOM   2168  C  C      . LYS   A 1  280 ? 1.827   -93.199  61.317  1.00 88.99  ? 280 LYS   A C      1 
ATOM   2169  O  O      . LYS   A 1  280 ? 0.860   -93.952  61.476  1.00 94.25  ? 280 LYS   A O      1 
ATOM   2170  C  CB     . LYS   A 1  280 ? 1.023   -91.154  62.526  1.00 68.36  ? 280 LYS   A CB     1 
ATOM   2171  C  CG     . LYS   A 1  280 ? 1.381   -89.711  62.834  1.00 66.64  ? 280 LYS   A CG     1 
ATOM   2172  C  CD     . LYS   A 1  280 ? 0.775   -89.340  64.156  1.00 70.17  ? 280 LYS   A CD     1 
ATOM   2173  C  CE     . LYS   A 1  280 ? 1.240   -90.259  65.264  1.00 71.50  ? 280 LYS   A CE     1 
ATOM   2174  N  NZ     . LYS   A 1  280 ? 0.620   -89.910  66.573  1.00 65.11  ? 280 LYS   A NZ     1 
ATOM   2175  N  N      . ALA   A 1  281 ? 3.091   -93.638  61.214  1.00 93.48  ? 281 ALA   A N      1 
ATOM   2176  C  CA     . ALA   A 1  281 ? 3.386   -95.070  61.220  1.00 101.56 ? 281 ALA   A CA     1 
ATOM   2177  C  C      . ALA   A 1  281 ? 3.430   -95.636  62.637  1.00 111.74 ? 281 ALA   A C      1 
ATOM   2178  O  O      . ALA   A 1  281 ? 3.012   -96.778  62.867  1.00 112.50 ? 281 ALA   A O      1 
ATOM   2179  C  CB     . ALA   A 1  281 ? 4.708   -95.337  60.497  1.00 104.38 ? 281 ALA   A CB     1 
ATOM   2180  N  N      . TYR   A 1  282 ? 3.945   -94.858  63.586  1.00 112.70 ? 282 TYR   A N      1 
ATOM   2181  C  CA     . TYR   A 1  282 ? 3.994   -95.226  64.996  1.00 111.81 ? 282 TYR   A CA     1 
ATOM   2182  C  C      . TYR   A 1  282 ? 3.034   -94.333  65.768  1.00 108.01 ? 282 TYR   A C      1 
ATOM   2183  O  O      . TYR   A 1  282 ? 3.180   -93.103  65.759  1.00 105.29 ? 282 TYR   A O      1 
ATOM   2184  C  CB     . TYR   A 1  282 ? 5.411   -95.094  65.559  1.00 116.46 ? 282 TYR   A CB     1 
ATOM   2185  C  CG     . TYR   A 1  282 ? 5.485   -95.349  67.047  1.00 118.19 ? 282 TYR   A CG     1 
ATOM   2186  C  CD1    . TYR   A 1  282 ? 5.418   -96.631  67.562  1.00 119.14 ? 282 TYR   A CD1    1 
ATOM   2187  C  CD2    . TYR   A 1  282 ? 5.590   -94.292  67.941  1.00 119.26 ? 282 TYR   A CD2    1 
ATOM   2188  C  CE1    . TYR   A 1  282 ? 5.474   -96.850  68.922  1.00 119.53 ? 282 TYR   A CE1    1 
ATOM   2189  C  CE2    . TYR   A 1  282 ? 5.644   -94.505  69.303  1.00 119.85 ? 282 TYR   A CE2    1 
ATOM   2190  C  CZ     . TYR   A 1  282 ? 5.586   -95.789  69.791  1.00 119.87 ? 282 TYR   A CZ     1 
ATOM   2191  O  OH     . TYR   A 1  282 ? 5.643   -96.007  71.151  1.00 119.00 ? 282 TYR   A OH     1 
ATOM   2192  N  N      . HIS   A 1  283 ? 2.066   -94.950  66.442  1.00 104.62 ? 283 HIS   A N      1 
ATOM   2193  C  CA     . HIS   A 1  283 ? 1.094   -94.193  67.203  1.00 89.67  ? 283 HIS   A CA     1 
ATOM   2194  C  C      . HIS   A 1  283 ? 0.829   -94.885  68.528  1.00 85.95  ? 283 HIS   A C      1 
ATOM   2195  O  O      . HIS   A 1  283 ? 0.773   -96.113  68.605  1.00 94.85  ? 283 HIS   A O      1 
ATOM   2196  C  CB     . HIS   A 1  283 ? -0.219  -94.025  66.440  1.00 90.57  ? 283 HIS   A CB     1 
ATOM   2197  C  CG     . HIS   A 1  283 ? -1.271  -93.342  67.242  1.00 84.46  ? 283 HIS   A CG     1 
ATOM   2198  N  ND1    . HIS   A 1  283 ? -1.106  -92.066  67.735  1.00 86.16  ? 283 HIS   A ND1    1 
ATOM   2199  C  CD2    . HIS   A 1  283 ? -2.490  -93.759  67.658  1.00 86.01  ? 283 HIS   A CD2    1 
ATOM   2200  C  CE1    . HIS   A 1  283 ? -2.182  -91.723  68.420  1.00 81.62  ? 283 HIS   A CE1    1 
ATOM   2201  N  NE2    . HIS   A 1  283 ? -3.037  -92.732  68.390  1.00 85.61  ? 283 HIS   A NE2    1 
ATOM   2202  N  N      . GLU   A 1  284 ? 0.650   -94.078  69.565  1.00 77.80  ? 284 GLU   A N      1 
ATOM   2203  C  CA     . GLU   A 1  284 ? 0.411   -94.556  70.922  1.00 74.95  ? 284 GLU   A CA     1 
ATOM   2204  C  C      . GLU   A 1  284 ? -1.086  -94.450  71.204  1.00 70.79  ? 284 GLU   A C      1 
ATOM   2205  O  O      . GLU   A 1  284 ? -1.646  -93.351  71.210  1.00 72.04  ? 284 GLU   A O      1 
ATOM   2206  C  CB     . GLU   A 1  284 ? 1.255   -93.740  71.905  1.00 77.62  ? 284 GLU   A CB     1 
ATOM   2207  C  CG     . GLU   A 1  284 ? 2.758   -93.786  71.574  1.00 79.63  ? 284 GLU   A CG     1 
ATOM   2208  C  CD     . GLU   A 1  284 ? 3.667   -93.115  72.617  1.00 76.72  ? 284 GLU   A CD     1 
ATOM   2209  O  OE1    . GLU   A 1  284 ? 3.296   -92.028  73.119  1.00 81.35  ? 284 GLU   A OE1    1 
ATOM   2210  O  OE2    . GLU   A 1  284 ? 4.765   -93.655  72.913  1.00 70.90  ? 284 GLU   A OE2    1 
ATOM   2211  N  N      . GLN   A 1  285 ? -1.740  -95.588  71.418  1.00 70.36  ? 285 GLN   A N      1 
ATOM   2212  C  CA     . GLN   A 1  285 ? -3.195  -95.593  71.524  1.00 65.19  ? 285 GLN   A CA     1 
ATOM   2213  C  C      . GLN   A 1  285 ? -3.657  -94.878  72.789  1.00 60.00  ? 285 GLN   A C      1 
ATOM   2214  O  O      . GLN   A 1  285 ? -3.275  -95.243  73.905  1.00 65.49  ? 285 GLN   A O      1 
ATOM   2215  C  CB     . GLN   A 1  285 ? -3.739  -97.021  71.460  1.00 69.40  ? 285 GLN   A CB     1 
ATOM   2216  C  CG     . GLN   A 1  285 ? -3.539  -97.661  70.067  1.00 81.14  ? 285 GLN   A CG     1 
ATOM   2217  C  CD     . GLN   A 1  285 ? -4.514  -97.139  68.990  1.00 74.84  ? 285 GLN   A CD     1 
ATOM   2218  O  OE1    . GLN   A 1  285 ? -5.493  -96.452  69.283  1.00 71.87  ? 285 GLN   A OE1    1 
ATOM   2219  N  NE2    . GLN   A 1  285 ? -4.208  -97.436  67.736  1.00 74.63  ? 285 GLN   A NE2    1 
ATOM   2220  N  N      . LEU   A 1  286 ? -4.497  -93.866  72.599  1.00 55.79  ? 286 LEU   A N      1 
ATOM   2221  C  CA     . LEU   A 1  286 ? -4.964  -93.028  73.695  1.00 53.86  ? 286 LEU   A CA     1 
ATOM   2222  C  C      . LEU   A 1  286 ? -5.943  -93.745  74.622  1.00 50.24  ? 286 LEU   A C      1 
ATOM   2223  O  O      . LEU   A 1  286 ? -6.764  -94.558  74.193  1.00 50.28  ? 286 LEU   A O      1 
ATOM   2224  C  CB     . LEU   A 1  286 ? -5.604  -91.777  73.104  1.00 51.17  ? 286 LEU   A CB     1 
ATOM   2225  C  CG     . LEU   A 1  286 ? -4.487  -90.938  72.526  1.00 45.81  ? 286 LEU   A CG     1 
ATOM   2226  C  CD1    . LEU   A 1  286 ? -4.497  -90.983  71.049  1.00 56.69  ? 286 LEU   A CD1    1 
ATOM   2227  C  CD2    . LEU   A 1  286 ? -4.826  -89.585  72.985  1.00 43.85  ? 286 LEU   A CD2    1 
ATOM   2228  N  N      . SER   A 1  287 ? -5.870  -93.409  75.902  1.00 50.86  ? 287 SER   A N      1 
ATOM   2229  C  CA     . SER   A 1  287 ? -6.616  -94.083  76.949  1.00 49.91  ? 287 SER   A CA     1 
ATOM   2230  C  C      . SER   A 1  287 ? -7.990  -93.473  77.104  1.00 46.82  ? 287 SER   A C      1 
ATOM   2231  O  O      . SER   A 1  287 ? -8.242  -92.345  76.698  1.00 47.47  ? 287 SER   A O      1 
ATOM   2232  C  CB     . SER   A 1  287 ? -5.899  -93.954  78.281  1.00 50.81  ? 287 SER   A CB     1 
ATOM   2233  O  OG     . SER   A 1  287 ? -5.841  -92.588  78.643  1.00 51.20  ? 287 SER   A OG     1 
ATOM   2234  N  N      . VAL   A 1  288 ? -8.869  -94.209  77.774  1.00 49.73  ? 288 VAL   A N      1 
ATOM   2235  C  CA     . VAL   A 1  288 ? -10.192 -93.660  78.036  1.00 43.98  ? 288 VAL   A CA     1 
ATOM   2236  C  C      . VAL   A 1  288 ? -10.072 -92.278  78.662  1.00 45.84  ? 288 VAL   A C      1 
ATOM   2237  O  O      . VAL   A 1  288 ? -10.822 -91.362  78.318  1.00 48.95  ? 288 VAL   A O      1 
ATOM   2238  C  CB     . VAL   A 1  288 ? -11.006 -94.621  78.915  1.00 38.01  ? 288 VAL   A CB     1 
ATOM   2239  C  CG1    . VAL   A 1  288 ? -12.245 -93.929  79.493  1.00 31.96  ? 288 VAL   A CG1    1 
ATOM   2240  C  CG2    . VAL   A 1  288 ? -11.365 -95.829  78.100  1.00 41.96  ? 288 VAL   A CG2    1 
ATOM   2241  N  N      . ALA   A 1  289 ? -9.106  -92.081  79.560  1.00 50.63  ? 289 ALA   A N      1 
ATOM   2242  C  CA     . ALA   A 1  289 ? -9.016  -90.749  80.151  1.00 53.16  ? 289 ALA   A CA     1 
ATOM   2243  C  C      . ALA   A 1  289 ? -8.406  -89.749  79.172  1.00 50.78  ? 289 ALA   A C      1 
ATOM   2244  O  O      . ALA   A 1  289 ? -8.911  -88.626  79.045  1.00 57.28  ? 289 ALA   A O      1 
ATOM   2245  C  CB     . ALA   A 1  289 ? -8.241  -90.774  81.467  1.00 48.14  ? 289 ALA   A CB     1 
ATOM   2246  N  N      . GLU   A 1  290 ? -7.353  -90.122  78.445  1.00 41.79  ? 290 GLU   A N      1 
ATOM   2247  C  CA     . GLU   A 1  290 ? -6.803  -89.187  77.458  1.00 50.24  ? 290 GLU   A CA     1 
ATOM   2248  C  C      . GLU   A 1  290 ? -7.874  -88.733  76.451  1.00 51.73  ? 290 GLU   A C      1 
ATOM   2249  O  O      . GLU   A 1  290 ? -8.038  -87.528  76.205  1.00 49.48  ? 290 GLU   A O      1 
ATOM   2250  C  CB     . GLU   A 1  290 ? -5.573  -89.788  76.750  1.00 46.99  ? 290 GLU   A CB     1 
ATOM   2251  C  CG     . GLU   A 1  290 ? -4.364  -90.093  77.665  1.00 45.34  ? 290 GLU   A CG     1 
ATOM   2252  C  CD     . GLU   A 1  290 ? -3.166  -90.668  76.916  1.00 57.69  ? 290 GLU   A CD     1 
ATOM   2253  O  OE1    . GLU   A 1  290 ? -3.234  -91.839  76.480  1.00 57.47  ? 290 GLU   A OE1    1 
ATOM   2254  O  OE2    . GLU   A 1  290 ? -2.143  -89.960  76.775  1.00 67.73  ? 290 GLU   A OE2    1 
ATOM   2255  N  N      . ILE   A 1  291 ? -8.638  -89.675  75.879  1.00 49.46  ? 291 ILE   A N      1 
ATOM   2256  C  CA     . ILE   A 1  291 ? -9.686  -89.270  74.948  1.00 43.15  ? 291 ILE   A CA     1 
ATOM   2257  C  C      . ILE   A 1  291 ? -10.781 -88.496  75.678  1.00 44.69  ? 291 ILE   A C      1 
ATOM   2258  O  O      . ILE   A 1  291 ? -11.220 -87.444  75.208  1.00 47.02  ? 291 ILE   A O      1 
ATOM   2259  C  CB     . ILE   A 1  291 ? -10.249 -90.473  74.151  1.00 40.74  ? 291 ILE   A CB     1 
ATOM   2260  C  CG1    . ILE   A 1  291 ? -11.078 -91.424  74.994  1.00 42.93  ? 291 ILE   A CG1    1 
ATOM   2261  C  CG2    . ILE   A 1  291 ? -9.164  -91.248  73.433  1.00 41.46  ? 291 ILE   A CG2    1 
ATOM   2262  C  CD1    . ILE   A 1  291 ? -11.624 -92.550  74.144  1.00 44.22  ? 291 ILE   A CD1    1 
ATOM   2263  N  N      . THR   A 1  292 ? -11.225 -88.969  76.843  1.00 44.46  ? 292 THR   A N      1 
ATOM   2264  C  CA     . THR   A 1  292 ? -12.281 -88.231  77.536  1.00 43.32  ? 292 THR   A CA     1 
ATOM   2265  C  C      . THR   A 1  292 ? -11.802 -86.862  78.008  1.00 48.63  ? 292 THR   A C      1 
ATOM   2266  O  O      . THR   A 1  292 ? -12.605 -85.929  78.132  1.00 47.52  ? 292 THR   A O      1 
ATOM   2267  C  CB     . THR   A 1  292 ? -12.818 -89.014  78.727  1.00 40.08  ? 292 THR   A CB     1 
ATOM   2268  O  OG1    . THR   A 1  292 ? -13.125 -90.341  78.317  1.00 48.99  ? 292 THR   A OG1    1 
ATOM   2269  C  CG2    . THR   A 1  292 ? -14.105 -88.412  79.175  1.00 35.32  ? 292 THR   A CG2    1 
ATOM   2270  N  N      . ASN   A 1  293 ? -10.511 -86.708  78.296  1.00 52.39  ? 293 ASN   A N      1 
ATOM   2271  C  CA     . ASN   A 1  293 ? -10.055 -85.370  78.644  1.00 53.63  ? 293 ASN   A CA     1 
ATOM   2272  C  C      . ASN   A 1  293 ? -10.154 -84.442  77.444  1.00 48.38  ? 293 ASN   A C      1 
ATOM   2273  O  O      . ASN   A 1  293 ? -10.472 -83.256  77.611  1.00 49.22  ? 293 ASN   A O      1 
ATOM   2274  C  CB     . ASN   A 1  293 ? -8.624  -85.382  79.199  1.00 51.85  ? 293 ASN   A CB     1 
ATOM   2275  C  CG     . ASN   A 1  293 ? -8.279  -84.084  79.916  1.00 54.11  ? 293 ASN   A CG     1 
ATOM   2276  O  OD1    . ASN   A 1  293 ? -9.121  -83.521  80.619  1.00 59.41  ? 293 ASN   A OD1    1 
ATOM   2277  N  ND2    . ASN   A 1  293 ? -7.063  -83.570  79.698  1.00 48.75  ? 293 ASN   A ND2    1 
ATOM   2278  N  N      . ALA   A 1  294 ? -9.912  -84.974  76.232  1.00 50.95  ? 294 ALA   A N      1 
ATOM   2279  C  CA     . ALA   A 1  294 ? -9.936  -84.196  74.990  1.00 45.70  ? 294 ALA   A CA     1 
ATOM   2280  C  C      . ALA   A 1  294 ? -11.316 -83.670  74.636  1.00 40.69  ? 294 ALA   A C      1 
ATOM   2281  O  O      . ALA   A 1  294 ? -11.419 -82.825  73.753  1.00 43.25  ? 294 ALA   A O      1 
ATOM   2282  C  CB     . ALA   A 1  294 ? -9.413  -85.023  73.821  1.00 36.40  ? 294 ALA   A CB     1 
ATOM   2283  N  N      . CYS   A 1  295 ? -12.366 -84.140  75.294  1.00 39.55  ? 295 CYS   A N      1 
ATOM   2284  C  CA     . CYS   A 1  295 ? -13.685 -83.594  75.075  1.00 38.55  ? 295 CYS   A CA     1 
ATOM   2285  C  C      . CYS   A 1  295 ? -13.851 -82.215  75.692  1.00 43.12  ? 295 CYS   A C      1 
ATOM   2286  O  O      . CYS   A 1  295 ? -14.854 -81.547  75.414  1.00 46.64  ? 295 CYS   A O      1 
ATOM   2287  C  CB     . CYS   A 1  295 ? -14.735 -84.565  75.618  1.00 42.72  ? 295 CYS   A CB     1 
ATOM   2288  S  SG     . CYS   A 1  295 ? -14.720 -86.166  74.738  1.00 50.54  ? 295 CYS   A SG     1 
ATOM   2289  N  N      . PHE   A 1  296 ? -12.897 -81.760  76.499  1.00 41.94  ? 296 PHE   A N      1 
ATOM   2290  C  CA     . PHE   A 1  296 ? -12.974 -80.439  77.107  1.00 41.21  ? 296 PHE   A CA     1 
ATOM   2291  C  C      . PHE   A 1  296 ? -11.870 -79.523  76.630  1.00 48.51  ? 296 PHE   A C      1 
ATOM   2292  O  O      . PHE   A 1  296 ? -11.691 -78.443  77.190  1.00 58.28  ? 296 PHE   A O      1 
ATOM   2293  C  CB     . PHE   A 1  296 ? -12.970 -80.543  78.627  1.00 44.64  ? 296 PHE   A CB     1 
ATOM   2294  C  CG     . PHE   A 1  296 ? -14.106 -81.347  79.152  1.00 45.92  ? 296 PHE   A CG     1 
ATOM   2295  C  CD1    . PHE   A 1  296 ? -14.020 -82.722  79.244  1.00 42.13  ? 296 PHE   A CD1    1 
ATOM   2296  C  CD2    . PHE   A 1  296 ? -15.291 -80.716  79.525  1.00 42.46  ? 296 PHE   A CD2    1 
ATOM   2297  C  CE1    . PHE   A 1  296 ? -15.090 -83.452  79.708  1.00 43.16  ? 296 PHE   A CE1    1 
ATOM   2298  C  CE2    . PHE   A 1  296 ? -16.362 -81.436  79.987  1.00 39.94  ? 296 PHE   A CE2    1 
ATOM   2299  C  CZ     . PHE   A 1  296 ? -16.267 -82.807  80.085  1.00 44.13  ? 296 PHE   A CZ     1 
ATOM   2300  N  N      . GLU   A 1  297 ? -11.132 -79.927  75.615  1.00 46.80  ? 297 GLU   A N      1 
ATOM   2301  C  CA     . GLU   A 1  297 ? -10.252 -79.033  74.904  1.00 47.10  ? 297 GLU   A CA     1 
ATOM   2302  C  C      . GLU   A 1  297 ? -11.023 -78.430  73.727  1.00 53.89  ? 297 GLU   A C      1 
ATOM   2303  O  O      . GLU   A 1  297 ? -11.542 -79.190  72.892  1.00 52.90  ? 297 GLU   A O      1 
ATOM   2304  C  CB     . GLU   A 1  297 ? -9.057  -79.810  74.399  1.00 50.97  ? 297 GLU   A CB     1 
ATOM   2305  C  CG     . GLU   A 1  297 ? -7.768  -79.060  74.373  1.00 67.32  ? 297 GLU   A CG     1 
ATOM   2306  C  CD     . GLU   A 1  297 ? -7.226  -78.938  75.770  1.00 79.34  ? 297 GLU   A CD     1 
ATOM   2307  O  OE1    . GLU   A 1  297 ? -7.087  -79.990  76.429  1.00 79.70  ? 297 GLU   A OE1    1 
ATOM   2308  O  OE2    . GLU   A 1  297 ? -6.905  -77.807  76.197  1.00 87.80  ? 297 GLU   A OE2    1 
ATOM   2309  N  N      . PRO   A 1  298 ? -11.151 -77.097  73.616  1.00 53.44  ? 298 PRO   A N      1 
ATOM   2310  C  CA     . PRO   A 1  298 ? -11.880 -76.528  72.467  1.00 43.22  ? 298 PRO   A CA     1 
ATOM   2311  C  C      . PRO   A 1  298 ? -11.387 -77.047  71.137  1.00 42.28  ? 298 PRO   A C      1 
ATOM   2312  O  O      . PRO   A 1  298 ? -12.185 -77.361  70.254  1.00 40.37  ? 298 PRO   A O      1 
ATOM   2313  C  CB     . PRO   A 1  298 ? -11.604 -75.033  72.601  1.00 46.09  ? 298 PRO   A CB     1 
ATOM   2314  C  CG     . PRO   A 1  298 ? -11.370 -74.837  74.062  1.00 53.33  ? 298 PRO   A CG     1 
ATOM   2315  C  CD     . PRO   A 1  298 ? -10.589 -76.044  74.474  1.00 59.86  ? 298 PRO   A CD     1 
ATOM   2316  N  N      . ALA   A 1  299 ? -10.074 -77.166  70.982  1.00 43.75  ? 299 ALA   A N      1 
ATOM   2317  C  CA     . ALA   A 1  299 ? -9.470  -77.587  69.728  1.00 42.37  ? 299 ALA   A CA     1 
ATOM   2318  C  C      . ALA   A 1  299 ? -10.091 -78.843  69.143  1.00 38.67  ? 299 ALA   A C      1 
ATOM   2319  O  O      . ALA   A 1  299 ? -9.722  -79.249  68.042  1.00 44.10  ? 299 ALA   A O      1 
ATOM   2320  C  CB     . ALA   A 1  299 ? -7.973  -77.813  69.920  1.00 46.44  ? 299 ALA   A CB     1 
ATOM   2321  N  N      . ASN   A 1  300 ? -11.018 -79.467  69.850  1.00 36.97  ? 300 ASN   A N      1 
ATOM   2322  C  CA     . ASN   A 1  300 ? -11.659 -80.684  69.375  1.00 41.46  ? 300 ASN   A CA     1 
ATOM   2323  C  C      . ASN   A 1  300 ? -13.130 -80.507  69.060  1.00 44.15  ? 300 ASN   A C      1 
ATOM   2324  O  O      . ASN   A 1  300 ? -13.790 -81.473  68.661  1.00 45.36  ? 300 ASN   A O      1 
ATOM   2325  C  CB     . ASN   A 1  300 ? -11.502 -81.799  70.404  1.00 36.41  ? 300 ASN   A CB     1 
ATOM   2326  C  CG     . ASN   A 1  300 ? -10.086 -82.024  70.752  1.00 35.10  ? 300 ASN   A CG     1 
ATOM   2327  O  OD1    . ASN   A 1  300 ? -9.212  -81.926  69.898  1.00 35.45  ? 300 ASN   A OD1    1 
ATOM   2328  N  ND2    . ASN   A 1  300 ? -9.826  -82.294  72.016  1.00 43.94  ? 300 ASN   A ND2    1 
ATOM   2329  N  N      . GLN   A 1  301 ? -13.662 -79.313  69.233  1.00 43.30  ? 301 GLN   A N      1 
ATOM   2330  C  CA     . GLN   A 1  301 ? -15.091 -79.143  69.133  1.00 42.00  ? 301 GLN   A CA     1 
ATOM   2331  C  C      . GLN   A 1  301 ? -15.490 -78.980  67.671  1.00 41.15  ? 301 GLN   A C      1 
ATOM   2332  O  O      . GLN   A 1  301 ? -14.665 -78.690  66.805  1.00 39.96  ? 301 GLN   A O      1 
ATOM   2333  C  CB     . GLN   A 1  301 ? -15.492 -77.969  70.014  1.00 37.34  ? 301 GLN   A CB     1 
ATOM   2334  C  CG     . GLN   A 1  301 ? -14.760 -78.118  71.314  1.00 40.13  ? 301 GLN   A CG     1 
ATOM   2335  C  CD     . GLN   A 1  301 ? -15.221 -77.202  72.403  1.00 48.26  ? 301 GLN   A CD     1 
ATOM   2336  O  OE1    . GLN   A 1  301 ? -15.709 -76.109  72.154  1.00 46.15  ? 301 GLN   A OE1    1 
ATOM   2337  N  NE2    . GLN   A 1  301 ? -15.106 -77.668  73.638  1.00 50.81  ? 301 GLN   A NE2    1 
ATOM   2338  N  N      . MET   A 1  302 ? -16.765 -79.247  67.392  1.00 42.19  ? 302 MET   A N      1 
ATOM   2339  C  CA     . MET   A 1  302 ? -17.302 -78.923  66.085  1.00 37.60  ? 302 MET   A CA     1 
ATOM   2340  C  C      . MET   A 1  302 ? -17.526 -77.436  65.936  1.00 37.61  ? 302 MET   A C      1 
ATOM   2341  O  O      . MET   A 1  302 ? -17.731 -76.957  64.825  1.00 38.12  ? 302 MET   A O      1 
ATOM   2342  C  CB     . MET   A 1  302 ? -18.611 -79.664  65.846  1.00 40.46  ? 302 MET   A CB     1 
ATOM   2343  C  CG     . MET   A 1  302 ? -18.481 -81.167  65.906  1.00 46.45  ? 302 MET   A CG     1 
ATOM   2344  S  SD     . MET   A 1  302 ? -17.140 -81.793  64.876  1.00 54.84  ? 302 MET   A SD     1 
ATOM   2345  C  CE     . MET   A 1  302 ? -15.881 -82.118  66.102  1.00 46.43  ? 302 MET   A CE     1 
ATOM   2346  N  N      . VAL   A 1  303 ? -17.496 -76.689  67.021  1.00 40.41  ? 303 VAL   A N      1 
ATOM   2347  C  CA     . VAL   A 1  303 ? -17.600 -75.244  66.943  1.00 41.75  ? 303 VAL   A CA     1 
ATOM   2348  C  C      . VAL   A 1  303 ? -16.582 -74.713  67.932  1.00 43.51  ? 303 VAL   A C      1 
ATOM   2349  O  O      . VAL   A 1  303 ? -16.560 -75.161  69.082  1.00 40.57  ? 303 VAL   A O      1 
ATOM   2350  C  CB     . VAL   A 1  303 ? -19.022 -74.757  67.284  1.00 39.01  ? 303 VAL   A CB     1 
ATOM   2351  C  CG1    . VAL   A 1  303 ? -19.085 -73.248  67.277  1.00 40.89  ? 303 VAL   A CG1    1 
ATOM   2352  C  CG2    . VAL   A 1  303 ? -20.064 -75.399  66.371  1.00 38.12  ? 303 VAL   A CG2    1 
ATOM   2353  N  N      . LYS   A 1  304 ? -15.706 -73.810  67.488  1.00 42.28  ? 304 LYS   A N      1 
ATOM   2354  C  CA     . LYS   A 1  304 ? -14.765 -73.217  68.433  1.00 45.22  ? 304 LYS   A CA     1 
ATOM   2355  C  C      . LYS   A 1  304 ? -15.484 -72.250  69.372  1.00 43.32  ? 304 LYS   A C      1 
ATOM   2356  O  O      . LYS   A 1  304 ? -16.180 -71.331  68.926  1.00 47.22  ? 304 LYS   A O      1 
ATOM   2357  C  CB     . LYS   A 1  304 ? -13.639 -72.507  67.706  1.00 41.18  ? 304 LYS   A CB     1 
ATOM   2358  C  CG     . LYS   A 1  304 ? -12.840 -73.391  66.851  1.00 40.68  ? 304 LYS   A CG     1 
ATOM   2359  C  CD     . LYS   A 1  304 ? -11.497 -72.759  66.598  1.00 47.25  ? 304 LYS   A CD     1 
ATOM   2360  C  CE     . LYS   A 1  304 ? -11.196 -72.716  65.134  1.00 51.39  ? 304 LYS   A CE     1 
ATOM   2361  N  NZ     . LYS   A 1  304 ? -9.768  -73.013  64.890  1.00 61.49  ? 304 LYS   A NZ     1 
ATOM   2362  N  N      . CYS   A 1  305 ? -15.306 -72.454  70.667  1.00 38.20  ? 305 CYS   A N      1 
ATOM   2363  C  CA     . CYS   A 1  305 ? -15.969 -71.667  71.698  1.00 43.54  ? 305 CYS   A CA     1 
ATOM   2364  C  C      . CYS   A 1  305 ? -15.419 -72.154  73.020  1.00 46.50  ? 305 CYS   A C      1 
ATOM   2365  O  O      . CYS   A 1  305 ? -14.733 -73.176  73.088  1.00 48.98  ? 305 CYS   A O      1 
ATOM   2366  C  CB     . CYS   A 1  305 ? -17.488 -71.793  71.672  1.00 41.49  ? 305 CYS   A CB     1 
ATOM   2367  S  SG     . CYS   A 1  305 ? -18.115 -73.479  71.633  1.00 42.78  ? 305 CYS   A SG     1 
ATOM   2368  N  N      . ASP   A 1  306 ? -15.723 -71.415  74.074  1.00 41.67  ? 306 ASP   A N      1 
ATOM   2369  C  CA     . ASP   A 1  306 ? -15.043 -71.619  75.345  1.00 43.51  ? 306 ASP   A CA     1 
ATOM   2370  C  C      . ASP   A 1  306 ? -16.094 -72.061  76.353  1.00 50.46  ? 306 ASP   A C      1 
ATOM   2371  O  O      . ASP   A 1  306 ? -16.774 -71.217  76.964  1.00 51.92  ? 306 ASP   A O      1 
ATOM   2372  C  CB     . ASP   A 1  306 ? -14.346 -70.346  75.786  1.00 47.30  ? 306 ASP   A CB     1 
ATOM   2373  C  CG     . ASP   A 1  306 ? -13.171 -70.617  76.662  1.00 49.66  ? 306 ASP   A CG     1 
ATOM   2374  O  OD1    . ASP   A 1  306 ? -13.179 -71.621  77.401  1.00 52.75  ? 306 ASP   A OD1    1 
ATOM   2375  O  OD2    . ASP   A 1  306 ? -12.230 -69.813  76.606  1.00 52.23  ? 306 ASP   A OD2    1 
ATOM   2376  N  N      . PRO   A 1  307 ? -16.289 -73.371  76.541  1.00 45.18  ? 307 PRO   A N      1 
ATOM   2377  C  CA     . PRO   A 1  307 ? -17.338 -73.821  77.454  1.00 47.86  ? 307 PRO   A CA     1 
ATOM   2378  C  C      . PRO   A 1  307 ? -17.055 -73.469  78.899  1.00 54.49  ? 307 PRO   A C      1 
ATOM   2379  O  O      . PRO   A 1  307 ? -17.975 -73.543  79.722  1.00 60.63  ? 307 PRO   A O      1 
ATOM   2380  C  CB     . PRO   A 1  307 ? -17.354 -75.332  77.233  1.00 46.37  ? 307 PRO   A CB     1 
ATOM   2381  C  CG     . PRO   A 1  307 ? -16.770 -75.513  75.919  1.00 41.13  ? 307 PRO   A CG     1 
ATOM   2382  C  CD     . PRO   A 1  307 ? -15.705 -74.505  75.821  1.00 42.91  ? 307 PRO   A CD     1 
ATOM   2383  N  N      . ARG   A 1  308 ? -15.811 -73.110  79.243  1.00 46.57  ? 308 ARG   A N      1 
ATOM   2384  C  CA     . ARG   A 1  308 ? -15.549 -72.603  80.583  1.00 46.03  ? 308 ARG   A CA     1 
ATOM   2385  C  C      . ARG   A 1  308 ? -16.426 -71.404  80.875  1.00 50.61  ? 308 ARG   A C      1 
ATOM   2386  O  O      . ARG   A 1  308 ? -16.938 -71.250  81.990  1.00 61.31  ? 308 ARG   A O      1 
ATOM   2387  C  CB     . ARG   A 1  308 ? -14.080 -72.231  80.741  1.00 45.08  ? 308 ARG   A CB     1 
ATOM   2388  C  CG     . ARG   A 1  308 ? -13.127 -73.336  80.453  1.00 46.85  ? 308 ARG   A CG     1 
ATOM   2389  C  CD     . ARG   A 1  308 ? -11.701 -72.859  80.549  1.00 48.36  ? 308 ARG   A CD     1 
ATOM   2390  N  NE     . ARG   A 1  308 ? -11.332 -71.947  79.479  1.00 49.40  ? 308 ARG   A NE     1 
ATOM   2391  C  CZ     . ARG   A 1  308 ? -10.097 -71.522  79.258  1.00 45.53  ? 308 ARG   A CZ     1 
ATOM   2392  N  NH1    . ARG   A 1  308 ? -9.119  -71.764  80.108  1.00 40.40  ? 308 ARG   A NH1    1 
ATOM   2393  N  NH2    . ARG   A 1  308 ? -9.841  -70.831  78.158  1.00 45.11  ? 308 ARG   A NH2    1 
ATOM   2394  N  N      . HIS   A 1  309 ? -16.626 -70.559  79.881  1.00 50.26  ? 309 HIS   A N      1 
ATOM   2395  C  CA     . HIS   A 1  309 ? -17.361 -69.314  80.057  1.00 52.18  ? 309 HIS   A CA     1 
ATOM   2396  C  C      . HIS   A 1  309 ? -18.778 -69.468  79.528  1.00 52.20  ? 309 HIS   A C      1 
ATOM   2397  O  O      . HIS   A 1  309 ? -19.200 -68.855  78.547  1.00 60.89  ? 309 HIS   A O      1 
ATOM   2398  C  CB     . HIS   A 1  309 ? -16.604 -68.172  79.402  1.00 45.68  ? 309 HIS   A CB     1 
ATOM   2399  C  CG     . HIS   A 1  309 ? -15.237 -68.007  79.976  1.00 50.08  ? 309 HIS   A CG     1 
ATOM   2400  N  ND1    . HIS   A 1  309 ? -14.115 -68.546  79.386  1.00 51.74  ? 309 HIS   A ND1    1 
ATOM   2401  C  CD2    . HIS   A 1  309 ? -14.821 -67.448  81.139  1.00 52.47  ? 309 HIS   A CD2    1 
ATOM   2402  C  CE1    . HIS   A 1  309 ? -13.055 -68.279  80.131  1.00 53.03  ? 309 HIS   A CE1    1 
ATOM   2403  N  NE2    . HIS   A 1  309 ? -13.457 -67.612  81.201  1.00 56.38  ? 309 HIS   A NE2    1 
ATOM   2404  N  N      . GLY   A 1  310 ? -19.490 -70.320  80.252  1.00 47.85  ? 310 GLY   A N      1 
ATOM   2405  C  CA     . GLY   A 1  310 ? -20.843 -70.729  79.937  1.00 57.76  ? 310 GLY   A CA     1 
ATOM   2406  C  C      . GLY   A 1  310 ? -21.227 -71.830  80.899  1.00 60.52  ? 310 GLY   A C      1 
ATOM   2407  O  O      . GLY   A 1  310 ? -20.445 -72.223  81.771  1.00 65.07  ? 310 GLY   A O      1 
ATOM   2408  N  N      . LYS   A 1  311 ? -22.443 -72.330  80.741  1.00 53.81  ? 311 LYS   A N      1 
ATOM   2409  C  CA     . LYS   A 1  311 ? -22.963 -73.307  81.679  1.00 52.16  ? 311 LYS   A CA     1 
ATOM   2410  C  C      . LYS   A 1  311 ? -23.563 -74.473  80.920  1.00 50.68  ? 311 LYS   A C      1 
ATOM   2411  O  O      . LYS   A 1  311 ? -24.025 -74.319  79.790  1.00 52.75  ? 311 LYS   A O      1 
ATOM   2412  C  CB     . LYS   A 1  311 ? -23.987 -72.676  82.594  1.00 57.54  ? 311 LYS   A CB     1 
ATOM   2413  C  CG     . LYS   A 1  311 ? -23.346 -71.739  83.601  1.00 66.20  ? 311 LYS   A CG     1 
ATOM   2414  C  CD     . LYS   A 1  311 ? -24.354 -71.189  84.595  1.00 70.02  ? 311 LYS   A CD     1 
ATOM   2415  C  CE     . LYS   A 1  311 ? -23.636 -70.436  85.688  1.00 69.31  ? 311 LYS   A CE     1 
ATOM   2416  N  NZ     . LYS   A 1  311 ? -24.570 -69.605  86.481  1.00 80.79  ? 311 LYS   A NZ     1 
ATOM   2417  N  N      . TYR   A 1  312 ? -23.525 -75.645  81.535  1.00 47.10  ? 312 TYR   A N      1 
ATOM   2418  C  CA     . TYR   A 1  312 ? -24.058 -76.817  80.874  1.00 44.91  ? 312 TYR   A CA     1 
ATOM   2419  C  C      . TYR   A 1  312 ? -25.498 -77.046  81.287  1.00 48.17  ? 312 TYR   A C      1 
ATOM   2420  O  O      . TYR   A 1  312 ? -25.968 -76.559  82.315  1.00 50.37  ? 312 TYR   A O      1 
ATOM   2421  C  CB     . TYR   A 1  312 ? -23.240 -78.060  81.185  1.00 43.32  ? 312 TYR   A CB     1 
ATOM   2422  C  CG     . TYR   A 1  312 ? -21.848 -78.100  80.600  1.00 45.43  ? 312 TYR   A CG     1 
ATOM   2423  C  CD1    . TYR   A 1  312 ? -20.783 -77.525  81.259  1.00 47.72  ? 312 TYR   A CD1    1 
ATOM   2424  C  CD2    . TYR   A 1  312 ? -21.587 -78.777  79.414  1.00 48.38  ? 312 TYR   A CD2    1 
ATOM   2425  C  CE1    . TYR   A 1  312 ? -19.512 -77.576  80.736  1.00 46.72  ? 312 TYR   A CE1    1 
ATOM   2426  C  CE2    . TYR   A 1  312 ? -20.304 -78.835  78.888  1.00 43.18  ? 312 TYR   A CE2    1 
ATOM   2427  C  CZ     . TYR   A 1  312 ? -19.280 -78.232  79.561  1.00 42.91  ? 312 TYR   A CZ     1 
ATOM   2428  O  OH     . TYR   A 1  312 ? -18.008 -78.279  79.056  1.00 53.76  ? 312 TYR   A OH     1 
ATOM   2429  N  N      . MET   A 1  313 ? -26.202 -77.786  80.440  1.00 45.37  ? 313 MET   A N      1 
ATOM   2430  C  CA     . MET   A 1  313 ? -27.542 -78.268  80.721  1.00 47.22  ? 313 MET   A CA     1 
ATOM   2431  C  C      . MET   A 1  313 ? -27.666 -79.752  80.534  1.00 47.03  ? 313 MET   A C      1 
ATOM   2432  O  O      . MET   A 1  313 ? -28.601 -80.350  81.070  1.00 57.11  ? 313 MET   A O      1 
ATOM   2433  C  CB     . MET   A 1  313 ? -28.572 -77.578  79.819  1.00 47.68  ? 313 MET   A CB     1 
ATOM   2434  C  CG     . MET   A 1  313 ? -28.483 -76.083  79.877  1.00 51.96  ? 313 MET   A CG     1 
ATOM   2435  S  SD     . MET   A 1  313 ? -29.392 -75.332  78.542  1.00 54.99  ? 313 MET   A SD     1 
ATOM   2436  C  CE     . MET   A 1  313 ? -27.981 -74.866  77.534  1.00 50.35  ? 313 MET   A CE     1 
ATOM   2437  N  N      . ALA   A 1  314 ? -26.756 -80.371  79.813  1.00 43.19  ? 314 ALA   A N      1 
ATOM   2438  C  CA     . ALA   A 1  314 ? -26.851 -81.796  79.572  1.00 49.63  ? 314 ALA   A CA     1 
ATOM   2439  C  C      . ALA   A 1  314 ? -25.499 -82.255  79.058  1.00 56.80  ? 314 ALA   A C      1 
ATOM   2440  O  O      . ALA   A 1  314 ? -24.624 -81.447  78.735  1.00 58.34  ? 314 ALA   A O      1 
ATOM   2441  C  CB     . ALA   A 1  314 ? -27.982 -82.119  78.592  1.00 44.72  ? 314 ALA   A CB     1 
ATOM   2442  N  N      . CYS   A 1  315 ? -25.333 -83.561  78.974  1.00 50.43  ? 315 CYS   A N      1 
ATOM   2443  C  CA     . CYS   A 1  315 ? -24.031 -84.005  78.547  1.00 41.34  ? 315 CYS   A CA     1 
ATOM   2444  C  C      . CYS   A 1  315 ? -24.015 -85.506  78.372  1.00 49.40  ? 315 CYS   A C      1 
ATOM   2445  O  O      . CYS   A 1  315 ? -24.172 -86.237  79.350  1.00 58.82  ? 315 CYS   A O      1 
ATOM   2446  C  CB     . CYS   A 1  315 ? -23.019 -83.534  79.567  1.00 45.39  ? 315 CYS   A CB     1 
ATOM   2447  S  SG     . CYS   A 1  315 ? -21.402 -83.459  78.936  1.00 64.73  ? 315 CYS   A SG     1 
ATOM   2448  N  N      . CYS   A 1  316 ? -23.897 -85.972  77.131  1.00 45.31  ? 316 CYS   A N      1 
ATOM   2449  C  CA     . CYS   A 1  316 ? -23.708 -87.383  76.831  1.00 43.44  ? 316 CYS   A CA     1 
ATOM   2450  C  C      . CYS   A 1  316 ? -22.251 -87.642  76.510  1.00 46.14  ? 316 CYS   A C      1 
ATOM   2451  O  O      . CYS   A 1  316 ? -21.528 -86.751  76.062  1.00 50.04  ? 316 CYS   A O      1 
ATOM   2452  C  CB     . CYS   A 1  316 ? -24.546 -87.861  75.640  1.00 45.16  ? 316 CYS   A CB     1 
ATOM   2453  S  SG     . CYS   A 1  316 ? -26.334 -87.849  75.847  1.00 66.40  ? 316 CYS   A SG     1 
ATOM   2454  N  N      . LEU   A 1  317 ? -21.821 -88.875  76.744  1.00 47.16  ? 317 LEU   A N      1 
ATOM   2455  C  CA     . LEU   A 1  317 ? -20.538 -89.357  76.246  1.00 44.17  ? 317 LEU   A CA     1 
ATOM   2456  C  C      . LEU   A 1  317 ? -20.801 -90.610  75.432  1.00 40.73  ? 317 LEU   A C      1 
ATOM   2457  O  O      . LEU   A 1  317 ? -21.378 -91.582  75.928  1.00 42.56  ? 317 LEU   A O      1 
ATOM   2458  C  CB     . LEU   A 1  317 ? -19.542 -89.640  77.377  1.00 47.32  ? 317 LEU   A CB     1 
ATOM   2459  C  CG     . LEU   A 1  317 ? -19.094 -88.430  78.188  1.00 47.52  ? 317 LEU   A CG     1 
ATOM   2460  C  CD1    . LEU   A 1  317 ? -18.506 -88.887  79.511  1.00 49.48  ? 317 LEU   A CD1    1 
ATOM   2461  C  CD2    . LEU   A 1  317 ? -18.072 -87.655  77.390  1.00 41.86  ? 317 LEU   A CD2    1 
ATOM   2462  N  N      . LEU   A 1  318 ? -20.416 -90.574  74.194  1.00 37.09  ? 318 LEU   A N      1 
ATOM   2463  C  CA     . LEU   A 1  318 ? -20.702 -91.659  73.291  1.00 37.21  ? 318 LEU   A CA     1 
ATOM   2464  C  C      . LEU   A 1  318 ? -19.354 -92.284  72.991  1.00 39.54  ? 318 LEU   A C      1 
ATOM   2465  O  O      . LEU   A 1  318 ? -18.529 -91.679  72.298  1.00 41.57  ? 318 LEU   A O      1 
ATOM   2466  C  CB     . LEU   A 1  318 ? -21.415 -91.137  72.050  1.00 36.59  ? 318 LEU   A CB     1 
ATOM   2467  C  CG     . LEU   A 1  318 ? -22.692 -90.394  72.475  1.00 37.09  ? 318 LEU   A CG     1 
ATOM   2468  C  CD1    . LEU   A 1  318 ? -23.489 -89.851  71.292  1.00 41.28  ? 318 LEU   A CD1    1 
ATOM   2469  C  CD2    . LEU   A 1  318 ? -23.564 -91.180  73.445  1.00 37.19  ? 318 LEU   A CD2    1 
ATOM   2470  N  N      . TYR   A 1  319 ? -19.110 -93.461  73.565  1.00 39.56  ? 319 TYR   A N      1 
ATOM   2471  C  CA     . TYR   A 1  319 ? -17.876 -94.201  73.341  1.00 42.08  ? 319 TYR   A CA     1 
ATOM   2472  C  C      . TYR   A 1  319 ? -18.093 -95.307  72.317  1.00 46.72  ? 319 TYR   A C      1 
ATOM   2473  O  O      . TYR   A 1  319 ? -19.167 -95.918  72.262  1.00 46.80  ? 319 TYR   A O      1 
ATOM   2474  C  CB     . TYR   A 1  319 ? -17.377 -94.812  74.638  1.00 42.06  ? 319 TYR   A CB     1 
ATOM   2475  C  CG     . TYR   A 1  319 ? -16.912 -93.811  75.625  1.00 39.76  ? 319 TYR   A CG     1 
ATOM   2476  C  CD1    . TYR   A 1  319 ? -15.585 -93.362  75.627  1.00 38.85  ? 319 TYR   A CD1    1 
ATOM   2477  C  CD2    . TYR   A 1  319 ? -17.796 -93.281  76.542  1.00 36.99  ? 319 TYR   A CD2    1 
ATOM   2478  C  CE1    . TYR   A 1  319 ? -15.148 -92.437  76.564  1.00 32.66  ? 319 TYR   A CE1    1 
ATOM   2479  C  CE2    . TYR   A 1  319 ? -17.380 -92.348  77.464  1.00 39.37  ? 319 TYR   A CE2    1 
ATOM   2480  C  CZ     . TYR   A 1  319 ? -16.064 -91.935  77.473  1.00 36.32  ? 319 TYR   A CZ     1 
ATOM   2481  O  OH     . TYR   A 1  319 ? -15.688 -91.005  78.404  1.00 40.39  ? 319 TYR   A OH     1 
ATOM   2482  N  N      . ARG   A 1  320 ? -17.069 -95.536  71.498  1.00 41.79  ? 320 ARG   A N      1 
ATOM   2483  C  CA     . ARG   A 1  320 ? -17.049 -96.612  70.517  1.00 45.35  ? 320 ARG   A CA     1 
ATOM   2484  C  C      . ARG   A 1  320 ? -15.674 -97.237  70.554  1.00 52.14  ? 320 ARG   A C      1 
ATOM   2485  O  O      . ARG   A 1  320 ? -14.693 -96.613  70.132  1.00 50.24  ? 320 ARG   A O      1 
ATOM   2486  C  CB     . ARG   A 1  320 ? -17.356 -96.143  69.096  1.00 51.84  ? 320 ARG   A CB     1 
ATOM   2487  C  CG     . ARG   A 1  320 ? -18.721 -95.587  68.900  1.00 47.55  ? 320 ARG   A CG     1 
ATOM   2488  C  CD     . ARG   A 1  320 ? -18.837 -95.101  67.509  1.00 48.30  ? 320 ARG   A CD     1 
ATOM   2489  N  NE     . ARG   A 1  320 ? -19.358 -96.135  66.628  1.00 48.71  ? 320 ARG   A NE     1 
ATOM   2490  C  CZ     . ARG   A 1  320 ? -19.838 -95.894  65.416  1.00 51.76  ? 320 ARG   A CZ     1 
ATOM   2491  N  NH1    . ARG   A 1  320 ? -19.893 -94.668  64.929  1.00 49.18  ? 320 ARG   A NH1    1 
ATOM   2492  N  NH2    . ARG   A 1  320 ? -20.277 -96.908  64.676  1.00 53.74  ? 320 ARG   A NH2    1 
ATOM   2493  N  N      . GLY   A 1  321 ? -15.625 -98.471  71.027  1.00 56.66  ? 321 GLY   A N      1 
ATOM   2494  C  CA     . GLY   A 1  321 ? -14.437 -99.281  71.086  1.00 55.00  ? 321 GLY   A CA     1 
ATOM   2495  C  C      . GLY   A 1  321 ? -14.228 -99.821  72.479  1.00 52.43  ? 321 GLY   A C      1 
ATOM   2496  O  O      . GLY   A 1  321 ? -15.176 -100.021 73.254  1.00 48.47  ? 321 GLY   A O      1 
ATOM   2497  N  N      . ASP   A 1  322 ? -12.960 -100.057 72.772  1.00 48.30  ? 322 ASP   A N      1 
ATOM   2498  C  CA     . ASP   A 1  322 ? -12.558 -100.741 73.984  1.00 46.21  ? 322 ASP   A CA     1 
ATOM   2499  C  C      . ASP   A 1  322 ? -12.704 -99.775  75.154  1.00 39.86  ? 322 ASP   A C      1 
ATOM   2500  O  O      . ASP   A 1  322 ? -11.753 -99.154  75.626  1.00 50.07  ? 322 ASP   A O      1 
ATOM   2501  C  CB     . ASP   A 1  322 ? -11.142 -101.259 73.807  1.00 48.46  ? 322 ASP   A CB     1 
ATOM   2502  C  CG     . ASP   A 1  322 ? -10.682 -102.054 74.965  1.00 58.09  ? 322 ASP   A CG     1 
ATOM   2503  O  OD1    . ASP   A 1  322 ? -11.446 -102.945 75.404  1.00 59.95  ? 322 ASP   A OD1    1 
ATOM   2504  O  OD2    . ASP   A 1  322 ? -9.569  -101.766 75.449  1.00 64.85  ? 322 ASP   A OD2    1 
ATOM   2505  N  N      . VAL   A 1  323 ? -13.925 -99.640  75.634  1.00 33.89  ? 323 VAL   A N      1 
ATOM   2506  C  CA     . VAL   A 1  323 ? -14.187 -98.879  76.845  1.00 42.33  ? 323 VAL   A CA     1 
ATOM   2507  C  C      . VAL   A 1  323 ? -15.063 -99.714  77.767  1.00 48.81  ? 323 VAL   A C      1 
ATOM   2508  O  O      . VAL   A 1  323 ? -15.935 -100.458 77.300  1.00 51.29  ? 323 VAL   A O      1 
ATOM   2509  C  CB     . VAL   A 1  323 ? -14.851 -97.518  76.527  1.00 47.12  ? 323 VAL   A CB     1 
ATOM   2510  C  CG1    . VAL   A 1  323 ? -15.316 -96.796  77.810  1.00 39.37  ? 323 VAL   A CG1    1 
ATOM   2511  C  CG2    . VAL   A 1  323 ? -13.891 -96.631  75.719  1.00 44.38  ? 323 VAL   A CG2    1 
ATOM   2512  N  N      . VAL   A 1  324 ? -14.811 -99.607  79.076  1.00 54.64  ? 324 VAL   A N      1 
ATOM   2513  C  CA     . VAL   A 1  324 ? -15.660 -100.183 80.128  1.00 51.92  ? 324 VAL   A CA     1 
ATOM   2514  C  C      . VAL   A 1  324 ? -16.037 -99.087  81.108  1.00 46.77  ? 324 VAL   A C      1 
ATOM   2515  O  O      . VAL   A 1  324 ? -15.182 -98.260  81.460  1.00 48.04  ? 324 VAL   A O      1 
ATOM   2516  C  CB     . VAL   A 1  324 ? -14.967 -101.317 80.897  1.00 45.68  ? 324 VAL   A CB     1 
ATOM   2517  C  CG1    . VAL   A 1  324 ? -14.772 -102.528 80.008  1.00 38.15  ? 324 VAL   A CG1    1 
ATOM   2518  C  CG2    . VAL   A 1  324 ? -13.650 -100.789 81.470  1.00 45.96  ? 324 VAL   A CG2    1 
ATOM   2519  N  N      . PRO   A 1  325 ? -17.268 -99.100  81.623  1.00 47.74  ? 325 PRO   A N      1 
ATOM   2520  C  CA     . PRO   A 1  325 ? -17.731 -98.047  82.545  1.00 48.51  ? 325 PRO   A CA     1 
ATOM   2521  C  C      . PRO   A 1  325 ? -16.727 -97.590  83.593  1.00 47.99  ? 325 PRO   A C      1 
ATOM   2522  O  O      . PRO   A 1  325 ? -16.686 -96.402  83.916  1.00 51.50  ? 325 PRO   A O      1 
ATOM   2523  C  CB     . PRO   A 1  325 ? -18.952 -98.695  83.216  1.00 44.64  ? 325 PRO   A CB     1 
ATOM   2524  C  CG     . PRO   A 1  325 ? -19.485 -99.629  82.183  1.00 50.19  ? 325 PRO   A CG     1 
ATOM   2525  C  CD     . PRO   A 1  325 ? -18.244 -100.196 81.501  1.00 49.37  ? 325 PRO   A CD     1 
ATOM   2526  N  N      . LYS   A 1  326 ? -15.913 -98.496  84.135  1.00 54.82  ? 326 LYS   A N      1 
ATOM   2527  C  CA     . LYS   A 1  326 ? -15.072 -98.126  85.271  1.00 54.03  ? 326 LYS   A CA     1 
ATOM   2528  C  C      . LYS   A 1  326 ? -14.013 -97.106  84.867  1.00 52.71  ? 326 LYS   A C      1 
ATOM   2529  O  O      . LYS   A 1  326 ? -13.859 -96.066  85.520  1.00 45.89  ? 326 LYS   A O      1 
ATOM   2530  C  CB     . LYS   A 1  326 ? -14.424 -99.368  85.878  1.00 51.55  ? 326 LYS   A CB     1 
ATOM   2531  C  CG     . LYS   A 1  326 ? -13.571 -99.051  87.075  1.00 62.23  ? 326 LYS   A CG     1 
ATOM   2532  C  CD     . LYS   A 1  326 ? -13.126 -100.294 87.805  1.00 68.12  ? 326 LYS   A CD     1 
ATOM   2533  C  CE     . LYS   A 1  326 ? -12.116 -101.076 86.985  1.00 75.64  ? 326 LYS   A CE     1 
ATOM   2534  N  NZ     . LYS   A 1  326 ? -11.794 -102.383 87.633  1.00 97.82  ? 326 LYS   A NZ     1 
ATOM   2535  N  N      . ASP   A 1  327 ? -13.265 -97.392  83.793  1.00 54.03  ? 327 ASP   A N      1 
ATOM   2536  C  CA     . ASP   A 1  327 ? -12.317 -96.422  83.251  1.00 51.14  ? 327 ASP   A CA     1 
ATOM   2537  C  C      . ASP   A 1  327 ? -12.969 -95.099  82.899  1.00 47.77  ? 327 ASP   A C      1 
ATOM   2538  O  O      . ASP   A 1  327 ? -12.283 -94.071  82.869  1.00 48.96  ? 327 ASP   A O      1 
ATOM   2539  C  CB     . ASP   A 1  327 ? -11.654 -96.963  81.998  1.00 53.45  ? 327 ASP   A CB     1 
ATOM   2540  C  CG     . ASP   A 1  327 ? -10.888 -98.209  82.256  1.00 56.99  ? 327 ASP   A CG     1 
ATOM   2541  O  OD1    . ASP   A 1  327 ? -10.437 -98.344  83.399  1.00 67.07  ? 327 ASP   A OD1    1 
ATOM   2542  O  OD2    . ASP   A 1  327 ? -10.727 -99.036  81.334  1.00 60.93  ? 327 ASP   A OD2    1 
ATOM   2543  N  N      . VAL   A 1  328 ? -14.264 -95.103  82.605  1.00 48.09  ? 328 VAL   A N      1 
ATOM   2544  C  CA     . VAL   A 1  328 ? -14.960 -93.863  82.277  1.00 49.86  ? 328 VAL   A CA     1 
ATOM   2545  C  C      . VAL   A 1  328 ? -15.149 -93.019  83.531  1.00 46.90  ? 328 VAL   A C      1 
ATOM   2546  O  O      . VAL   A 1  328 ? -14.677 -91.878  83.611  1.00 49.83  ? 328 VAL   A O      1 
ATOM   2547  C  CB     . VAL   A 1  328 ? -16.303 -94.164  81.578  1.00 46.24  ? 328 VAL   A CB     1 
ATOM   2548  C  CG1    . VAL   A 1  328 ? -17.096 -92.890  81.380  1.00 42.36  ? 328 VAL   A CG1    1 
ATOM   2549  C  CG2    . VAL   A 1  328 ? -16.077 -94.896  80.238  1.00 38.29  ? 328 VAL   A CG2    1 
ATOM   2550  N  N      . ASN   A 1  329 ? -15.792 -93.598  84.550  1.00 45.65  ? 329 ASN   A N      1 
ATOM   2551  C  CA     . ASN   A 1  329 ? -16.010 -92.900  85.817  1.00 52.94  ? 329 ASN   A CA     1 
ATOM   2552  C  C      . ASN   A 1  329 ? -14.706 -92.439  86.458  1.00 53.25  ? 329 ASN   A C      1 
ATOM   2553  O  O      . ASN   A 1  329 ? -14.673 -91.400  87.129  1.00 50.10  ? 329 ASN   A O      1 
ATOM   2554  C  CB     . ASN   A 1  329 ? -16.779 -93.818  86.750  1.00 49.07  ? 329 ASN   A CB     1 
ATOM   2555  C  CG     . ASN   A 1  329 ? -18.132 -94.193  86.178  1.00 61.05  ? 329 ASN   A CG     1 
ATOM   2556  O  OD1    . ASN   A 1  329 ? -18.737 -93.417  85.418  1.00 66.42  ? 329 ASN   A OD1    1 
ATOM   2557  N  ND2    . ASN   A 1  329 ? -18.590 -95.413  86.480  1.00 63.35  ? 329 ASN   A ND2    1 
ATOM   2558  N  N      . ALA   A 1  330 ? -13.630 -93.203  86.274  1.00 52.32  ? 330 ALA   A N      1 
ATOM   2559  C  CA     . ALA   A 1  330 ? -12.317 -92.756  86.711  1.00 49.41  ? 330 ALA   A CA     1 
ATOM   2560  C  C      . ALA   A 1  330 ? -11.898 -91.479  85.988  1.00 56.13  ? 330 ALA   A C      1 
ATOM   2561  O  O      . ALA   A 1  330 ? -11.544 -90.479  86.624  1.00 56.96  ? 330 ALA   A O      1 
ATOM   2562  C  CB     . ALA   A 1  330 ? -11.299 -93.866  86.481  1.00 41.34  ? 330 ALA   A CB     1 
ATOM   2563  N  N      . ALA   A 1  331 ? -11.914 -91.502  84.651  1.00 51.64  ? 331 ALA   A N      1 
ATOM   2564  C  CA     . ALA   A 1  331 ? -11.536 -90.316  83.896  1.00 53.20  ? 331 ALA   A CA     1 
ATOM   2565  C  C      . ALA   A 1  331 ? -12.449 -89.145  84.224  1.00 57.79  ? 331 ALA   A C      1 
ATOM   2566  O  O      . ALA   A 1  331 ? -11.986 -87.998  84.287  1.00 56.66  ? 331 ALA   A O      1 
ATOM   2567  C  CB     . ALA   A 1  331 ? -11.550 -90.621  82.395  1.00 46.61  ? 331 ALA   A CB     1 
ATOM   2568  N  N      . ILE   A 1  332 ? -13.742 -89.419  84.449  1.00 57.66  ? 332 ILE   A N      1 
ATOM   2569  C  CA     . ILE   A 1  332 ? -14.703 -88.381  84.837  1.00 53.75  ? 332 ILE   A CA     1 
ATOM   2570  C  C      . ILE   A 1  332 ? -14.325 -87.766  86.178  1.00 57.34  ? 332 ILE   A C      1 
ATOM   2571  O  O      . ILE   A 1  332 ? -14.334 -86.543  86.345  1.00 60.49  ? 332 ILE   A O      1 
ATOM   2572  C  CB     . ILE   A 1  332 ? -16.121 -88.966  84.903  1.00 50.09  ? 332 ILE   A CB     1 
ATOM   2573  C  CG1    . ILE   A 1  332 ? -16.598 -89.404  83.524  1.00 49.98  ? 332 ILE   A CG1    1 
ATOM   2574  C  CG2    . ILE   A 1  332 ? -17.071 -87.964  85.555  1.00 54.91  ? 332 ILE   A CG2    1 
ATOM   2575  C  CD1    . ILE   A 1  332 ? -18.036 -89.881  83.527  1.00 53.34  ? 332 ILE   A CD1    1 
ATOM   2576  N  N      . ALA   A 1  333 ? -14.047 -88.617  87.168  1.00 60.30  ? 333 ALA   A N      1 
ATOM   2577  C  CA     . ALA   A 1  333 ? -13.663 -88.154  88.498  1.00 61.20  ? 333 ALA   A CA     1 
ATOM   2578  C  C      . ALA   A 1  333 ? -12.487 -87.194  88.430  1.00 62.86  ? 333 ALA   A C      1 
ATOM   2579  O  O      . ALA   A 1  333 ? -12.579 -86.044  88.872  1.00 69.59  ? 333 ALA   A O      1 
ATOM   2580  C  CB     . ALA   A 1  333 ? -13.313 -89.352  89.377  1.00 59.18  ? 333 ALA   A CB     1 
ATOM   2581  N  N      . THR   A 1  334 ? -11.359 -87.668  87.897  1.00 64.04  ? 334 THR   A N      1 
ATOM   2582  C  CA     . THR   A 1  334 ? -10.180 -86.820  87.755  1.00 64.89  ? 334 THR   A CA     1 
ATOM   2583  C  C      . THR   A 1  334 ? -10.491 -85.550  86.976  1.00 65.69  ? 334 THR   A C      1 
ATOM   2584  O  O      . THR   A 1  334 ? -10.040 -84.462  87.347  1.00 71.53  ? 334 THR   A O      1 
ATOM   2585  C  CB     . THR   A 1  334 ? -9.037  -87.601  87.092  1.00 62.80  ? 334 THR   A CB     1 
ATOM   2586  O  OG1    . THR   A 1  334 ? -9.485  -88.212  85.873  1.00 63.22  ? 334 THR   A OG1    1 
ATOM   2587  C  CG2    . THR   A 1  334 ? -8.509  -88.683  88.036  1.00 67.55  ? 334 THR   A CG2    1 
ATOM   2588  N  N      . ILE   A 1  335 ? -11.276 -85.654  85.908  1.00 64.60  ? 335 ILE   A N      1 
ATOM   2589  C  CA     . ILE   A 1  335 ? -11.541 -84.460  85.115  1.00 68.52  ? 335 ILE   A CA     1 
ATOM   2590  C  C      . ILE   A 1  335 ? -12.444 -83.486  85.879  1.00 75.46  ? 335 ILE   A C      1 
ATOM   2591  O  O      . ILE   A 1  335 ? -12.253 -82.266  85.803  1.00 78.37  ? 335 ILE   A O      1 
ATOM   2592  C  CB     . ILE   A 1  335 ? -12.122 -84.845  83.745  1.00 62.31  ? 335 ILE   A CB     1 
ATOM   2593  C  CG1    . ILE   A 1  335 ? -11.036 -85.511  82.890  1.00 65.35  ? 335 ILE   A CG1    1 
ATOM   2594  C  CG2    . ILE   A 1  335 ? -12.637 -83.608  83.046  1.00 64.75  ? 335 ILE   A CG2    1 
ATOM   2595  C  CD1    . ILE   A 1  335 ? -11.514 -86.054  81.537  1.00 53.16  ? 335 ILE   A CD1    1 
ATOM   2596  N  N      . LYS   A 1  336 ? -13.425 -83.994  86.640  1.00 68.20  ? 336 LYS   A N      1 
ATOM   2597  C  CA     . LYS   A 1  336 ? -14.293 -83.088  87.391  1.00 70.05  ? 336 LYS   A CA     1 
ATOM   2598  C  C      . LYS   A 1  336 ? -13.472 -82.094  88.192  1.00 75.61  ? 336 LYS   A C      1 
ATOM   2599  O  O      . LYS   A 1  336 ? -13.797 -80.901  88.250  1.00 79.19  ? 336 LYS   A O      1 
ATOM   2600  C  CB     . LYS   A 1  336 ? -15.233 -83.857  88.324  1.00 67.74  ? 336 LYS   A CB     1 
ATOM   2601  C  CG     . LYS   A 1  336 ? -16.301 -82.942  88.922  1.00 67.57  ? 336 LYS   A CG     1 
ATOM   2602  C  CD     . LYS   A 1  336 ? -16.885 -82.038  87.834  1.00 67.76  ? 336 LYS   A CD     1 
ATOM   2603  C  CE     . LYS   A 1  336 ? -18.012 -81.159  88.337  1.00 69.31  ? 336 LYS   A CE     1 
ATOM   2604  N  NZ     . LYS   A 1  336 ? -17.541 -80.214  89.382  1.00 68.71  ? 336 LYS   A NZ     1 
ATOM   2605  N  N      . THR   A 1  337 ? -12.393 -82.569  88.804  1.00 72.26  ? 337 THR   A N      1 
ATOM   2606  C  CA     . THR   A 1  337 ? -11.526 -81.687  89.566  1.00 75.88  ? 337 THR   A CA     1 
ATOM   2607  C  C      . THR   A 1  337 ? -10.936 -80.599  88.673  1.00 81.27  ? 337 THR   A C      1 
ATOM   2608  O  O      . THR   A 1  337 ? -11.222 -79.408  88.853  1.00 85.81  ? 337 THR   A O      1 
ATOM   2609  C  CB     . THR   A 1  337 ? -10.420 -82.509  90.218  1.00 78.78  ? 337 THR   A CB     1 
ATOM   2610  O  OG1    . THR   A 1  337 ? -9.528  -82.978  89.198  1.00 72.43  ? 337 THR   A OG1    1 
ATOM   2611  C  CG2    . THR   A 1  337 ? -11.028 -83.716  90.952  1.00 70.52  ? 337 THR   A CG2    1 
ATOM   2612  N  N      . LYS   A 1  338 ? -10.139 -81.005  87.670  1.00 81.67  ? 338 LYS   A N      1 
ATOM   2613  C  CA     . LYS   A 1  338 ? -9.249  -80.110  86.924  1.00 79.04  ? 338 LYS   A CA     1 
ATOM   2614  C  C      . LYS   A 1  338 ? -9.957  -79.196  85.920  1.00 80.69  ? 338 LYS   A C      1 
ATOM   2615  O  O      . LYS   A 1  338 ? -9.307  -78.296  85.375  1.00 77.33  ? 338 LYS   A O      1 
ATOM   2616  C  CB     . LYS   A 1  338 ? -8.195  -80.917  86.160  1.00 74.25  ? 338 LYS   A CB     1 
ATOM   2617  C  CG     . LYS   A 1  338 ? -7.173  -81.658  87.014  1.00 78.01  ? 338 LYS   A CG     1 
ATOM   2618  C  CD     . LYS   A 1  338 ? -6.292  -82.530  86.112  1.00 82.79  ? 338 LYS   A CD     1 
ATOM   2619  C  CE     . LYS   A 1  338 ? -5.152  -83.206  86.871  1.00 74.35  ? 338 LYS   A CE     1 
ATOM   2620  N  NZ     . LYS   A 1  338 ? -3.941  -82.366  87.058  1.00 62.46  ? 338 LYS   A NZ     1 
ATOM   2621  N  N      . ARG   A 1  339 ? -11.239 -79.393  85.633  1.00 81.51  ? 339 ARG   A N      1 
ATOM   2622  C  CA     . ARG   A 1  339 ? -11.888 -78.586  84.613  1.00 80.66  ? 339 ARG   A CA     1 
ATOM   2623  C  C      . ARG   A 1  339 ? -12.968 -77.713  85.239  1.00 79.96  ? 339 ARG   A C      1 
ATOM   2624  O  O      . ARG   A 1  339 ? -13.474 -77.987  86.335  1.00 74.48  ? 339 ARG   A O      1 
ATOM   2625  C  CB     . ARG   A 1  339 ? -12.500 -79.458  83.501  1.00 80.08  ? 339 ARG   A CB     1 
ATOM   2626  C  CG     . ARG   A 1  339 ? -11.514 -80.271  82.643  1.00 68.55  ? 339 ARG   A CG     1 
ATOM   2627  C  CD     . ARG   A 1  339 ? -10.737 -79.462  81.609  1.00 67.77  ? 339 ARG   A CD     1 
ATOM   2628  N  NE     . ARG   A 1  339 ? -10.048 -80.344  80.662  1.00 67.15  ? 339 ARG   A NE     1 
ATOM   2629  C  CZ     . ARG   A 1  339 ? -9.281  -79.943  79.649  1.00 65.79  ? 339 ARG   A CZ     1 
ATOM   2630  N  NH1    . ARG   A 1  339 ? -9.089  -78.657  79.385  1.00 64.89  ? 339 ARG   A NH1    1 
ATOM   2631  N  NH2    . ARG   A 1  339 ? -8.690  -80.855  78.879  1.00 58.89  ? 339 ARG   A NH2    1 
ATOM   2632  N  N      . SER   A 1  340 ? -13.307 -76.648  84.509  1.00 85.09  ? 340 SER   A N      1 
ATOM   2633  C  CA     . SER   A 1  340 ? -14.357 -75.700  84.885  1.00 80.14  ? 340 SER   A CA     1 
ATOM   2634  C  C      . SER   A 1  340 ? -15.648 -76.181  84.240  1.00 71.99  ? 340 SER   A C      1 
ATOM   2635  O  O      . SER   A 1  340 ? -15.979 -75.803  83.113  1.00 72.48  ? 340 SER   A O      1 
ATOM   2636  C  CB     . SER   A 1  340 ? -14.000 -74.295  84.414  1.00 69.49  ? 340 SER   A CB     1 
ATOM   2637  O  OG     . SER   A 1  340 ? -12.789 -73.862  85.001  1.00 67.92  ? 340 SER   A OG     1 
ATOM   2638  N  N      . ILE   A 1  341 ? -16.383 -77.036  84.946  1.00 64.08  ? 341 ILE   A N      1 
ATOM   2639  C  CA     . ILE   A 1  341 ? -17.618 -77.615  84.414  1.00 60.77  ? 341 ILE   A CA     1 
ATOM   2640  C  C      . ILE   A 1  341 ? -18.780 -77.177  85.297  1.00 63.72  ? 341 ILE   A C      1 
ATOM   2641  O  O      . ILE   A 1  341 ? -19.100 -77.824  86.299  1.00 69.32  ? 341 ILE   A O      1 
ATOM   2642  C  CB     . ILE   A 1  341 ? -17.551 -79.137  84.299  1.00 56.29  ? 341 ILE   A CB     1 
ATOM   2643  C  CG1    . ILE   A 1  341 ? -16.533 -79.527  83.237  1.00 59.49  ? 341 ILE   A CG1    1 
ATOM   2644  C  CG2    . ILE   A 1  341 ? -18.920 -79.702  83.994  1.00 54.96  ? 341 ILE   A CG2    1 
ATOM   2645  C  CD1    . ILE   A 1  341 ? -16.024 -80.960  83.363  1.00 62.82  ? 341 ILE   A CD1    1 
ATOM   2646  N  N      . GLN   A 1  342 ? -19.444 -76.102  84.903  1.00 62.14  ? 342 GLN   A N      1 
ATOM   2647  C  CA     . GLN   A 1  342 ? -20.507 -75.499  85.683  1.00 57.50  ? 342 GLN   A CA     1 
ATOM   2648  C  C      . GLN   A 1  342 ? -21.818 -75.806  84.981  1.00 56.93  ? 342 GLN   A C      1 
ATOM   2649  O  O      . GLN   A 1  342 ? -21.966 -75.503  83.796  1.00 57.99  ? 342 GLN   A O      1 
ATOM   2650  C  CB     . GLN   A 1  342 ? -20.290 -73.994  85.792  1.00 57.52  ? 342 GLN   A CB     1 
ATOM   2651  C  CG     . GLN   A 1  342 ? -19.776 -73.546  87.116  1.00 61.33  ? 342 GLN   A CG     1 
ATOM   2652  C  CD     . GLN   A 1  342 ? -20.843 -73.645  88.172  1.00 80.09  ? 342 GLN   A CD     1 
ATOM   2653  O  OE1    . GLN   A 1  342 ? -21.980 -73.220  87.961  1.00 76.82  ? 342 GLN   A OE1    1 
ATOM   2654  N  NE2    . GLN   A 1  342 ? -20.492 -74.220  89.319  1.00 86.10  ? 342 GLN   A NE2    1 
ATOM   2655  N  N      . PHE   A 1  343 ? -22.752 -76.424  85.694  1.00 58.05  ? 343 PHE   A N      1 
ATOM   2656  C  CA     . PHE   A 1  343 ? -24.095 -76.653  85.176  1.00 56.10  ? 343 PHE   A CA     1 
ATOM   2657  C  C      . PHE   A 1  343 ? -25.065 -75.594  85.669  1.00 57.68  ? 343 PHE   A C      1 
ATOM   2658  O  O      . PHE   A 1  343 ? -24.901 -75.003  86.734  1.00 60.14  ? 343 PHE   A O      1 
ATOM   2659  C  CB     . PHE   A 1  343 ? -24.634 -78.012  85.596  1.00 56.85  ? 343 PHE   A CB     1 
ATOM   2660  C  CG     . PHE   A 1  343 ? -24.253 -79.128  84.697  1.00 51.37  ? 343 PHE   A CG     1 
ATOM   2661  C  CD1    . PHE   A 1  343 ? -22.951 -79.595  84.662  1.00 52.68  ? 343 PHE   A CD1    1 
ATOM   2662  C  CD2    . PHE   A 1  343 ? -25.212 -79.766  83.948  1.00 50.69  ? 343 PHE   A CD2    1 
ATOM   2663  C  CE1    . PHE   A 1  343 ? -22.612 -80.648  83.858  1.00 51.10  ? 343 PHE   A CE1    1 
ATOM   2664  C  CE2    . PHE   A 1  343 ? -24.878 -80.818  83.140  1.00 52.62  ? 343 PHE   A CE2    1 
ATOM   2665  C  CZ     . PHE   A 1  343 ? -23.579 -81.262  83.093  1.00 53.96  ? 343 PHE   A CZ     1 
ATOM   2666  N  N      . VAL   A 1  344 ? -26.106 -75.382  84.874  1.00 60.84  ? 344 VAL   A N      1 
ATOM   2667  C  CA     . VAL   A 1  344 ? -27.213 -74.565  85.322  1.00 64.66  ? 344 VAL   A CA     1 
ATOM   2668  C  C      . VAL   A 1  344 ? -27.764 -75.169  86.596  1.00 72.03  ? 344 VAL   A C      1 
ATOM   2669  O  O      . VAL   A 1  344 ? -27.929 -76.390  86.707  1.00 73.91  ? 344 VAL   A O      1 
ATOM   2670  C  CB     . VAL   A 1  344 ? -28.286 -74.484  84.228  1.00 68.65  ? 344 VAL   A CB     1 
ATOM   2671  C  CG1    . VAL   A 1  344 ? -27.656 -74.059  82.911  1.00 63.10  ? 344 VAL   A CG1    1 
ATOM   2672  C  CG2    . VAL   A 1  344 ? -28.956 -75.832  84.078  1.00 67.14  ? 344 VAL   A CG2    1 
ATOM   2673  N  N      . ASP   A 1  345 ? -28.047 -74.303  87.571  1.00 77.49  ? 345 ASP   A N      1 
ATOM   2674  C  CA     . ASP   A 1  345 ? -28.427 -74.753  88.905  1.00 72.54  ? 345 ASP   A CA     1 
ATOM   2675  C  C      . ASP   A 1  345 ? -29.572 -75.756  88.871  1.00 78.11  ? 345 ASP   A C      1 
ATOM   2676  O  O      . ASP   A 1  345 ? -29.689 -76.593  89.770  1.00 79.12  ? 345 ASP   A O      1 
ATOM   2677  C  CB     . ASP   A 1  345 ? -28.810 -73.541  89.749  1.00 71.31  ? 345 ASP   A CB     1 
ATOM   2678  C  CG     . ASP   A 1  345 ? -27.609 -72.764  90.212  1.00 81.05  ? 345 ASP   A CG     1 
ATOM   2679  O  OD1    . ASP   A 1  345 ? -26.556 -73.396  90.451  1.00 85.15  ? 345 ASP   A OD1    1 
ATOM   2680  O  OD2    . ASP   A 1  345 ? -27.704 -71.522  90.309  1.00 88.98  ? 345 ASP   A OD2    1 
ATOM   2681  N  N      . TRP   A 1  346 ? -30.424 -75.697  87.854  1.00 76.62  ? 346 TRP   A N      1 
ATOM   2682  C  CA     . TRP   A 1  346 ? -31.632 -76.501  87.824  1.00 75.55  ? 346 TRP   A CA     1 
ATOM   2683  C  C      . TRP   A 1  346 ? -31.461 -77.775  87.016  1.00 77.74  ? 346 TRP   A C      1 
ATOM   2684  O  O      . TRP   A 1  346 ? -32.455 -78.357  86.567  1.00 76.20  ? 346 TRP   A O      1 
ATOM   2685  C  CB     . TRP   A 1  346 ? -32.773 -75.675  87.262  1.00 75.75  ? 346 TRP   A CB     1 
ATOM   2686  C  CG     . TRP   A 1  346 ? -32.444 -75.138  85.926  1.00 82.83  ? 346 TRP   A CG     1 
ATOM   2687  C  CD1    . TRP   A 1  346 ? -31.744 -73.991  85.637  1.00 81.42  ? 346 TRP   A CD1    1 
ATOM   2688  C  CD2    . TRP   A 1  346 ? -32.809 -75.714  84.667  1.00 86.62  ? 346 TRP   A CD2    1 
ATOM   2689  N  NE1    . TRP   A 1  346 ? -31.656 -73.820  84.268  1.00 76.89  ? 346 TRP   A NE1    1 
ATOM   2690  C  CE2    . TRP   A 1  346 ? -32.299 -74.864  83.652  1.00 82.42  ? 346 TRP   A CE2    1 
ATOM   2691  C  CE3    . TRP   A 1  346 ? -33.522 -76.865  84.297  1.00 82.43  ? 346 TRP   A CE3    1 
ATOM   2692  C  CZ2    . TRP   A 1  346 ? -32.476 -75.134  82.296  1.00 80.30  ? 346 TRP   A CZ2    1 
ATOM   2693  C  CZ3    . TRP   A 1  346 ? -33.700 -77.128  82.950  1.00 86.36  ? 346 TRP   A CZ3    1 
ATOM   2694  C  CH2    . TRP   A 1  346 ? -33.177 -76.265  81.962  1.00 84.11  ? 346 TRP   A CH2    1 
ATOM   2695  N  N      . CYS   A 1  347 ? -30.219 -78.191  86.787  1.00 76.36  ? 347 CYS   A N      1 
ATOM   2696  C  CA     . CYS   A 1  347 ? -29.893 -79.440  86.129  1.00 73.28  ? 347 CYS   A CA     1 
ATOM   2697  C  C      . CYS   A 1  347 ? -28.865 -80.174  86.968  1.00 75.13  ? 347 CYS   A C      1 
ATOM   2698  O  O      . CYS   A 1  347 ? -27.934 -79.555  87.510  1.00 73.12  ? 347 CYS   A O      1 
ATOM   2699  C  CB     . CYS   A 1  347 ? -29.315 -79.237  84.721  1.00 71.34  ? 347 CYS   A CB     1 
ATOM   2700  S  SG     . CYS   A 1  347 ? -30.484 -78.619  83.523  1.00 79.96  ? 347 CYS   A SG     1 
ATOM   2701  N  N      . PRO   A 1  348 ? -29.016 -81.483  87.106  1.00 72.40  ? 348 PRO   A N      1 
ATOM   2702  C  CA     . PRO   A 1  348 ? -27.955 -82.282  87.717  1.00 67.59  ? 348 PRO   A CA     1 
ATOM   2703  C  C      . PRO   A 1  348 ? -26.654 -82.171  86.949  1.00 59.72  ? 348 PRO   A C      1 
ATOM   2704  O  O      . PRO   A 1  348 ? -26.637 -81.986  85.736  1.00 58.20  ? 348 PRO   A O      1 
ATOM   2705  C  CB     . PRO   A 1  348 ? -28.516 -83.701  87.680  1.00 67.90  ? 348 PRO   A CB     1 
ATOM   2706  C  CG     . PRO   A 1  348 ? -29.572 -83.674  86.628  1.00 75.24  ? 348 PRO   A CG     1 
ATOM   2707  C  CD     . PRO   A 1  348 ? -30.143 -82.295  86.632  1.00 68.89  ? 348 PRO   A CD     1 
ATOM   2708  N  N      . THR   A 1  349 ? -25.557 -82.242  87.698  1.00 60.03  ? 349 THR   A N      1 
ATOM   2709  C  CA     . THR   A 1  349 ? -24.204 -82.216  87.158  1.00 53.34  ? 349 THR   A CA     1 
ATOM   2710  C  C      . THR   A 1  349 ? -23.797 -83.663  86.905  1.00 65.51  ? 349 THR   A C      1 
ATOM   2711  O  O      . THR   A 1  349 ? -22.982 -84.245  87.622  1.00 73.47  ? 349 THR   A O      1 
ATOM   2712  C  CB     . THR   A 1  349 ? -23.254 -81.534  88.138  1.00 61.77  ? 349 THR   A CB     1 
ATOM   2713  O  OG1    . THR   A 1  349 ? -23.678 -80.181  88.359  1.00 64.01  ? 349 THR   A OG1    1 
ATOM   2714  C  CG2    . THR   A 1  349 ? -21.806 -81.559  87.635  1.00 55.48  ? 349 THR   A CG2    1 
ATOM   2715  N  N      . GLY   A 1  350 ? -24.396 -84.268  85.867  1.00 71.68  ? 350 GLY   A N      1 
ATOM   2716  C  CA     . GLY   A 1  350 ? -24.115 -85.650  85.538  1.00 60.74  ? 350 GLY   A CA     1 
ATOM   2717  C  C      . GLY   A 1  350 ? -23.794 -85.820  84.067  1.00 57.66  ? 350 GLY   A C      1 
ATOM   2718  O  O      . GLY   A 1  350 ? -23.903 -84.888  83.273  1.00 57.10  ? 350 GLY   A O      1 
ATOM   2719  N  N      . PHE   A 1  351 ? -23.416 -87.052  83.721  1.00 55.40  ? 351 PHE   A N      1 
ATOM   2720  C  CA     . PHE   A 1  351 ? -23.090 -87.467  82.361  1.00 47.65  ? 351 PHE   A CA     1 
ATOM   2721  C  C      . PHE   A 1  351 ? -23.853 -88.737  82.000  1.00 55.47  ? 351 PHE   A C      1 
ATOM   2722  O  O      . PHE   A 1  351 ? -23.553 -89.809  82.532  1.00 56.37  ? 351 PHE   A O      1 
ATOM   2723  C  CB     . PHE   A 1  351 ? -21.605 -87.737  82.230  1.00 55.46  ? 351 PHE   A CB     1 
ATOM   2724  C  CG     . PHE   A 1  351 ? -20.747 -86.553  82.445  1.00 60.48  ? 351 PHE   A CG     1 
ATOM   2725  C  CD1    . PHE   A 1  351 ? -20.523 -86.071  83.719  1.00 64.03  ? 351 PHE   A CD1    1 
ATOM   2726  C  CD2    . PHE   A 1  351 ? -20.054 -85.998  81.388  1.00 53.37  ? 351 PHE   A CD2    1 
ATOM   2727  C  CE1    . PHE   A 1  351 ? -19.691 -84.998  83.917  1.00 61.15  ? 351 PHE   A CE1    1 
ATOM   2728  C  CE2    . PHE   A 1  351 ? -19.216 -84.939  81.589  1.00 47.44  ? 351 PHE   A CE2    1 
ATOM   2729  C  CZ     . PHE   A 1  351 ? -19.035 -84.438  82.852  1.00 49.75  ? 351 PHE   A CZ     1 
ATOM   2730  N  N      . LYS   A 1  352 ? -24.789 -88.649  81.057  1.00 51.07  ? 352 LYS   A N      1 
ATOM   2731  C  CA     . LYS   A 1  352 ? -25.336 -89.863  80.470  1.00 44.87  ? 352 LYS   A CA     1 
ATOM   2732  C  C      . LYS   A 1  352 ? -24.290 -90.448  79.532  1.00 49.89  ? 352 LYS   A C      1 
ATOM   2733  O  O      . LYS   A 1  352 ? -23.670 -89.720  78.752  1.00 49.92  ? 352 LYS   A O      1 
ATOM   2734  C  CB     . LYS   A 1  352 ? -26.625 -89.563  79.719  1.00 45.68  ? 352 LYS   A CB     1 
ATOM   2735  C  CG     . LYS   A 1  352 ? -27.703 -89.022  80.621  1.00 55.35  ? 352 LYS   A CG     1 
ATOM   2736  C  CD     . LYS   A 1  352 ? -29.086 -89.084  80.016  1.00 55.13  ? 352 LYS   A CD     1 
ATOM   2737  C  CE     . LYS   A 1  352 ? -30.050 -88.338  80.922  1.00 61.07  ? 352 LYS   A CE     1 
ATOM   2738  N  NZ     . LYS   A 1  352 ? -31.480 -88.525  80.567  1.00 74.00  ? 352 LYS   A NZ     1 
ATOM   2739  N  N      . VAL   A 1  353 ? -24.063 -91.754  79.610  1.00 49.65  ? 353 VAL   A N      1 
ATOM   2740  C  CA     . VAL   A 1  353 ? -22.931 -92.365  78.922  1.00 46.61  ? 353 VAL   A CA     1 
ATOM   2741  C  C      . VAL   A 1  353 ? -23.414 -93.542  78.089  1.00 43.83  ? 353 VAL   A C      1 
ATOM   2742  O  O      . VAL   A 1  353 ? -24.271 -94.315  78.525  1.00 48.69  ? 353 VAL   A O      1 
ATOM   2743  C  CB     . VAL   A 1  353 ? -21.850 -92.820  79.920  1.00 45.67  ? 353 VAL   A CB     1 
ATOM   2744  C  CG1    . VAL   A 1  353 ? -20.614 -93.373  79.190  1.00 37.61  ? 353 VAL   A CG1    1 
ATOM   2745  C  CG2    . VAL   A 1  353 ? -21.513 -91.677  80.873  1.00 45.44  ? 353 VAL   A CG2    1 
ATOM   2746  N  N      . GLY   A 1  354 ? -22.874 -93.671  76.894  1.00 37.86  ? 354 GLY   A N      1 
ATOM   2747  C  CA     . GLY   A 1  354 ? -23.110 -94.848  76.076  1.00 36.13  ? 354 GLY   A CA     1 
ATOM   2748  C  C      . GLY   A 1  354 ? -21.795 -95.397  75.579  1.00 41.50  ? 354 GLY   A C      1 
ATOM   2749  O  O      . GLY   A 1  354 ? -20.893 -94.638  75.218  1.00 44.04  ? 354 GLY   A O      1 
ATOM   2750  N  N      . ILE   A 1  355 ? -21.676 -96.728  75.606  1.00 38.32  ? 355 ILE   A N      1 
ATOM   2751  C  CA     . ILE   A 1  355 ? -20.528 -97.424  75.034  1.00 39.69  ? 355 ILE   A CA     1 
ATOM   2752  C  C      . ILE   A 1  355 ? -21.033 -98.427  74.020  1.00 43.75  ? 355 ILE   A C      1 
ATOM   2753  O  O      . ILE   A 1  355 ? -21.934 -99.213  74.319  1.00 49.88  ? 355 ILE   A O      1 
ATOM   2754  C  CB     . ILE   A 1  355 ? -19.665 -98.136  76.093  1.00 44.37  ? 355 ILE   A CB     1 
ATOM   2755  C  CG1    . ILE   A 1  355 ? -19.177 -97.158  77.160  1.00 47.09  ? 355 ILE   A CG1    1 
ATOM   2756  C  CG2    . ILE   A 1  355 ? -18.504 -98.889  75.443  1.00 45.34  ? 355 ILE   A CG2    1 
ATOM   2757  C  CD1    . ILE   A 1  355 ? -18.254 -97.798  78.147  1.00 47.86  ? 355 ILE   A CD1    1 
ATOM   2758  N  N      . ASN   A 1  356 ? -20.461 -98.382  72.822  1.00 44.70  ? 356 ASN   A N      1 
ATOM   2759  C  CA     . ASN   A 1  356 ? -20.605 -99.411  71.805  1.00 47.04  ? 356 ASN   A CA     1 
ATOM   2760  C  C      . ASN   A 1  356 ? -19.252 -100.071 71.611  1.00 50.21  ? 356 ASN   A C      1 
ATOM   2761  O  O      . ASN   A 1  356 ? -18.253 -99.388  71.370  1.00 49.51  ? 356 ASN   A O      1 
ATOM   2762  C  CB     . ASN   A 1  356 ? -21.117 -98.836  70.484  1.00 52.05  ? 356 ASN   A CB     1 
ATOM   2763  C  CG     . ASN   A 1  356 ? -21.925 -99.854  69.688  1.00 67.14  ? 356 ASN   A CG     1 
ATOM   2764  O  OD1    . ASN   A 1  356 ? -21.365 -100.777 69.071  1.00 66.43  ? 356 ASN   A OD1    1 
ATOM   2765  N  ND2    . ASN   A 1  356 ? -23.243 -99.724  69.738  1.00 66.36  ? 356 ASN   A ND2    1 
ATOM   2766  N  N      . TYR   A 1  357 ? -19.220 -101.393 71.725  1.00 54.13  ? 357 TYR   A N      1 
ATOM   2767  C  CA     . TYR   A 1  357 ? -17.941 -102.082 71.729  1.00 52.97  ? 357 TYR   A CA     1 
ATOM   2768  C  C      . TYR   A 1  357 ? -17.288 -102.133 70.354  1.00 52.85  ? 357 TYR   A C      1 
ATOM   2769  O  O      . TYR   A 1  357 ? -16.063 -102.302 70.290  1.00 48.76  ? 357 TYR   A O      1 
ATOM   2770  C  CB     . TYR   A 1  357 ? -18.101 -103.503 72.288  1.00 51.15  ? 357 TYR   A CB     1 
ATOM   2771  C  CG     . TYR   A 1  357 ? -18.461 -103.583 73.764  1.00 56.35  ? 357 TYR   A CG     1 
ATOM   2772  C  CD1    . TYR   A 1  357 ? -17.894 -102.718 74.702  1.00 59.48  ? 357 TYR   A CD1    1 
ATOM   2773  C  CD2    . TYR   A 1  357 ? -19.331 -104.556 74.225  1.00 59.37  ? 357 TYR   A CD2    1 
ATOM   2774  C  CE1    . TYR   A 1  357 ? -18.209 -102.821 76.051  1.00 55.54  ? 357 TYR   A CE1    1 
ATOM   2775  C  CE2    . TYR   A 1  357 ? -19.647 -104.667 75.563  1.00 55.84  ? 357 TYR   A CE2    1 
ATOM   2776  C  CZ     . TYR   A 1  357 ? -19.095 -103.803 76.467  1.00 57.79  ? 357 TYR   A CZ     1 
ATOM   2777  O  OH     . TYR   A 1  357 ? -19.447 -103.947 77.788  1.00 62.71  ? 357 TYR   A OH     1 
ATOM   2778  N  N      . GLN   A 1  358 ? -18.059 -101.989 69.257  1.00 54.92  ? 358 GLN   A N      1 
ATOM   2779  C  CA     . GLN   A 1  358 ? -17.454 -102.054 67.910  1.00 56.04  ? 358 GLN   A CA     1 
ATOM   2780  C  C      . GLN   A 1  358 ? -16.615 -100.798 67.696  1.00 55.65  ? 358 GLN   A C      1 
ATOM   2781  O  O      . GLN   A 1  358 ? -17.175 -99.687  67.658  1.00 52.21  ? 358 GLN   A O      1 
ATOM   2782  C  CB     . GLN   A 1  358 ? -18.509 -102.150 66.810  1.00 61.52  ? 358 GLN   A CB     1 
ATOM   2783  C  CG     . GLN   A 1  358 ? -17.970 -102.578 65.409  1.00 64.07  ? 358 GLN   A CG     1 
ATOM   2784  C  CD     . GLN   A 1  358 ? -18.913 -102.209 64.215  1.00 77.28  ? 358 GLN   A CD     1 
ATOM   2785  O  OE1    . GLN   A 1  358 ? -19.430 -101.087 64.119  1.00 71.28  ? 358 GLN   A OE1    1 
ATOM   2786  N  NE2    . GLN   A 1  358 ? -19.215 -103.199 63.379  1.00 74.10  ? 358 GLN   A NE2    1 
ATOM   2787  N  N      . PRO   A 1  359 ? -15.296 -100.908 67.556  1.00 58.80  ? 359 PRO   A N      1 
ATOM   2788  C  CA     . PRO   A 1  359 ? -14.446 -99.704  67.477  1.00 52.30  ? 359 PRO   A CA     1 
ATOM   2789  C  C      . PRO   A 1  359 ? -14.727 -98.905  66.218  1.00 53.79  ? 359 PRO   A C      1 
ATOM   2790  O  O      . PRO   A 1  359 ? -15.347 -99.409  65.268  1.00 54.87  ? 359 PRO   A O      1 
ATOM   2791  C  CB     . PRO   A 1  359 ? -13.020 -100.270 67.479  1.00 48.34  ? 359 PRO   A CB     1 
ATOM   2792  C  CG     . PRO   A 1  359 ? -13.152 -101.697 67.034  1.00 45.96  ? 359 PRO   A CG     1 
ATOM   2793  C  CD     . PRO   A 1  359 ? -14.519 -102.159 67.477  1.00 55.04  ? 359 PRO   A CD     1 
ATOM   2794  N  N      . PRO   A 1  360 ? -14.284 -97.653  66.171  1.00 51.59  ? 360 PRO   A N      1 
ATOM   2795  C  CA     . PRO   A 1  360 ? -14.639 -96.794  65.038  1.00 48.49  ? 360 PRO   A CA     1 
ATOM   2796  C  C      . PRO   A 1  360 ? -14.228 -97.415  63.723  1.00 52.00  ? 360 PRO   A C      1 
ATOM   2797  O  O      . PRO   A 1  360 ? -13.220 -98.122  63.626  1.00 55.64  ? 360 PRO   A O      1 
ATOM   2798  C  CB     . PRO   A 1  360 ? -13.875 -95.499  65.312  1.00 48.69  ? 360 PRO   A CB     1 
ATOM   2799  C  CG     . PRO   A 1  360 ? -13.653 -95.522  66.793  1.00 56.38  ? 360 PRO   A CG     1 
ATOM   2800  C  CD     . PRO   A 1  360 ? -13.464 -96.952  67.165  1.00 56.41  ? 360 PRO   A CD     1 
ATOM   2801  N  N      . THR   A 1  361 ? -15.045 -97.159  62.711  1.00 57.26  ? 361 THR   A N      1 
ATOM   2802  C  CA     . THR   A 1  361 ? -14.851 -97.691  61.371  1.00 53.73  ? 361 THR   A CA     1 
ATOM   2803  C  C      . THR   A 1  361 ? -14.258 -96.593  60.507  1.00 52.52  ? 361 THR   A C      1 
ATOM   2804  O  O      . THR   A 1  361 ? -14.759 -95.465  60.502  1.00 56.19  ? 361 THR   A O      1 
ATOM   2805  C  CB     . THR   A 1  361 ? -16.178 -98.188  60.789  1.00 49.17  ? 361 THR   A CB     1 
ATOM   2806  O  OG1    . THR   A 1  361 ? -16.909 -98.914  61.795  1.00 55.94  ? 361 THR   A OG1    1 
ATOM   2807  C  CG2    . THR   A 1  361 ? -15.937 -99.089  59.617  1.00 51.38  ? 361 THR   A CG2    1 
ATOM   2808  N  N      . VAL   A 1  362 ? -13.172 -96.904  59.817  1.00 53.75  ? 362 VAL   A N      1 
ATOM   2809  C  CA     . VAL   A 1  362 ? -12.492 -95.929  58.973  1.00 64.99  ? 362 VAL   A CA     1 
ATOM   2810  C  C      . VAL   A 1  362 ? -12.552 -96.417  57.535  1.00 64.22  ? 362 VAL   A C      1 
ATOM   2811  O  O      . VAL   A 1  362 ? -12.473 -97.623  57.275  1.00 65.61  ? 362 VAL   A O      1 
ATOM   2812  C  CB     . VAL   A 1  362 ? -11.028 -95.675  59.401  1.00 59.93  ? 362 VAL   A CB     1 
ATOM   2813  C  CG1    . VAL   A 1  362 ? -10.986 -94.736  60.597  1.00 50.06  ? 362 VAL   A CG1    1 
ATOM   2814  C  CG2    . VAL   A 1  362 ? -10.294 -96.997  59.662  1.00 49.15  ? 362 VAL   A CG2    1 
ATOM   2815  N  N      . VAL   A 1  363 ? -12.684 -95.477  56.606  1.00 55.04  ? 363 VAL   A N      1 
ATOM   2816  C  CA     . VAL   A 1  363 ? -12.848 -95.821  55.200  1.00 61.91  ? 363 VAL   A CA     1 
ATOM   2817  C  C      . VAL   A 1  363 ? -11.508 -96.269  54.643  1.00 61.58  ? 363 VAL   A C      1 
ATOM   2818  O  O      . VAL   A 1  363 ? -10.536 -95.512  54.708  1.00 59.86  ? 363 VAL   A O      1 
ATOM   2819  C  CB     . VAL   A 1  363 ? -13.444 -94.648  54.407  1.00 65.22  ? 363 VAL   A CB     1 
ATOM   2820  C  CG1    . VAL   A 1  363 ? -13.604 -95.012  52.968  1.00 69.66  ? 363 VAL   A CG1    1 
ATOM   2821  C  CG2    . VAL   A 1  363 ? -14.809 -94.325  54.959  1.00 66.54  ? 363 VAL   A CG2    1 
ATOM   2822  N  N      . PRO   A 1  364 ? -11.406 -97.488  54.104  1.00 64.98  ? 364 PRO   A N      1 
ATOM   2823  C  CA     . PRO   A 1  364 ? -10.141 -97.912  53.510  1.00 59.96  ? 364 PRO   A CA     1 
ATOM   2824  C  C      . PRO   A 1  364 ? -9.659  -96.866  52.533  1.00 65.71  ? 364 PRO   A C      1 
ATOM   2825  O  O      . PRO   A 1  364 ? -10.398 -96.484  51.616  1.00 60.68  ? 364 PRO   A O      1 
ATOM   2826  C  CB     . PRO   A 1  364 ? -10.500 -99.230  52.820  1.00 56.51  ? 364 PRO   A CB     1 
ATOM   2827  C  CG     . PRO   A 1  364 ? -11.669 -99.733  53.586  1.00 63.86  ? 364 PRO   A CG     1 
ATOM   2828  C  CD     . PRO   A 1  364 ? -12.452 -98.508  53.938  1.00 62.51  ? 364 PRO   A CD     1 
ATOM   2829  N  N      . GLY   A 1  365 ? -8.444  -96.367  52.755  1.00 67.42  ? 365 GLY   A N      1 
ATOM   2830  C  CA     . GLY   A 1  365 ? -7.876  -95.319  51.932  1.00 69.06  ? 365 GLY   A CA     1 
ATOM   2831  C  C      . GLY   A 1  365 ? -8.146  -93.915  52.418  1.00 69.49  ? 365 GLY   A C      1 
ATOM   2832  O  O      . GLY   A 1  365 ? -7.823  -92.956  51.710  1.00 75.13  ? 365 GLY   A O      1 
ATOM   2833  N  N      . GLY   A 1  366 ? -8.729  -93.761  53.599  1.00 70.84  ? 366 GLY   A N      1 
ATOM   2834  C  CA     . GLY   A 1  366 ? -9.059  -92.456  54.122  1.00 63.94  ? 366 GLY   A CA     1 
ATOM   2835  C  C      . GLY   A 1  366 ? -7.864  -91.789  54.768  1.00 58.42  ? 366 GLY   A C      1 
ATOM   2836  O  O      . GLY   A 1  366 ? -6.716  -92.209  54.632  1.00 57.97  ? 366 GLY   A O      1 
ATOM   2837  N  N      . ASP   A 1  367 ? -8.158  -90.709  55.474  1.00 60.65  ? 367 ASP   A N      1 
ATOM   2838  C  CA     . ASP   A 1  367 ? -7.159  -89.926  56.171  1.00 55.08  ? 367 ASP   A CA     1 
ATOM   2839  C  C      . ASP   A 1  367 ? -7.118  -90.228  57.658  1.00 52.28  ? 367 ASP   A C      1 
ATOM   2840  O  O      . ASP   A 1  367 ? -6.185  -89.796  58.333  1.00 55.93  ? 367 ASP   A O      1 
ATOM   2841  C  CB     . ASP   A 1  367 ? -7.434  -88.429  55.956  1.00 61.09  ? 367 ASP   A CB     1 
ATOM   2842  C  CG     . ASP   A 1  367 ? -7.588  -88.058  54.478  1.00 67.10  ? 367 ASP   A CG     1 
ATOM   2843  O  OD1    . ASP   A 1  367 ? -6.605  -88.240  53.719  1.00 62.38  ? 367 ASP   A OD1    1 
ATOM   2844  O  OD2    . ASP   A 1  367 ? -8.700  -87.627  54.074  1.00 62.77  ? 367 ASP   A OD2    1 
ATOM   2845  N  N      . LEU   A 1  368 ? -8.099  -90.953  58.177  1.00 51.92  ? 368 LEU   A N      1 
ATOM   2846  C  CA     . LEU   A 1  368 ? -8.199  -91.235  59.600  1.00 50.72  ? 368 LEU   A CA     1 
ATOM   2847  C  C      . LEU   A 1  368 ? -7.594  -92.603  59.861  1.00 55.67  ? 368 LEU   A C      1 
ATOM   2848  O  O      . LEU   A 1  368 ? -7.846  -93.554  59.115  1.00 58.74  ? 368 LEU   A O      1 
ATOM   2849  C  CB     . LEU   A 1  368 ? -9.653  -91.238  60.075  1.00 43.78  ? 368 LEU   A CB     1 
ATOM   2850  C  CG     . LEU   A 1  368 ? -10.373 -89.907  60.300  1.00 42.03  ? 368 LEU   A CG     1 
ATOM   2851  C  CD1    . LEU   A 1  368 ? -11.829 -90.141  60.688  1.00 41.03  ? 368 LEU   A CD1    1 
ATOM   2852  C  CD2    . LEU   A 1  368 ? -9.670  -88.951  61.240  1.00 50.08  ? 368 LEU   A CD2    1 
ATOM   2853  N  N      . ALA   A 1  369 ? -6.823  -92.704  60.935  1.00 53.27  ? 369 ALA   A N      1 
ATOM   2854  C  CA     . ALA   A 1  369 ? -6.308  -93.989  61.372  1.00 48.58  ? 369 ALA   A CA     1 
ATOM   2855  C  C      . ALA   A 1  369 ? -7.368  -94.744  62.169  1.00 49.10  ? 369 ALA   A C      1 
ATOM   2856  O  O      . ALA   A 1  369 ? -8.230  -94.140  62.813  1.00 51.07  ? 369 ALA   A O      1 
ATOM   2857  C  CB     . ALA   A 1  369 ? -5.055  -93.772  62.211  1.00 48.74  ? 369 ALA   A CB     1 
ATOM   2858  N  N      . LYS   A 1  370 ? -7.314  -96.076  62.105  1.00 49.81  ? 370 LYS   A N      1 
ATOM   2859  C  CA     . LYS   A 1  370 ? -8.130  -96.882  63.004  1.00 54.28  ? 370 LYS   A CA     1 
ATOM   2860  C  C      . LYS   A 1  370 ? -7.616  -96.753  64.433  1.00 56.26  ? 370 LYS   A C      1 
ATOM   2861  O  O      . LYS   A 1  370 ? -6.433  -96.517  64.676  1.00 55.41  ? 370 LYS   A O      1 
ATOM   2862  C  CB     . LYS   A 1  370 ? -8.138  -98.354  62.594  1.00 56.46  ? 370 LYS   A CB     1 
ATOM   2863  C  CG     . LYS   A 1  370 ? -9.286  -99.176  63.250  1.00 68.63  ? 370 LYS   A CG     1 
ATOM   2864  C  CD     . LYS   A 1  370 ? -8.887  -99.727  64.637  1.00 75.34  ? 370 LYS   A CD     1 
ATOM   2865  C  CE     . LYS   A 1  370 ? -9.985  -100.574 65.312  1.00 67.98  ? 370 LYS   A CE     1 
ATOM   2866  N  NZ     . LYS   A 1  370 ? -9.469  -101.286 66.540  1.00 64.45  ? 370 LYS   A NZ     1 
ATOM   2867  N  N      . VAL   A 1  371 ? -8.523  -96.906  65.390  1.00 55.52  ? 371 VAL   A N      1 
ATOM   2868  C  CA     . VAL   A 1  371 ? -8.185  -96.683  66.784  1.00 56.92  ? 371 VAL   A CA     1 
ATOM   2869  C  C      . VAL   A 1  371 ? -8.931  -97.686  67.651  1.00 63.99  ? 371 VAL   A C      1 
ATOM   2870  O  O      . VAL   A 1  371 ? -9.972  -98.232  67.266  1.00 59.44  ? 371 VAL   A O      1 
ATOM   2871  C  CB     . VAL   A 1  371 ? -8.516  -95.248  67.222  1.00 54.71  ? 371 VAL   A CB     1 
ATOM   2872  C  CG1    . VAL   A 1  371 ? -7.648  -94.258  66.468  1.00 46.68  ? 371 VAL   A CG1    1 
ATOM   2873  C  CG2    . VAL   A 1  371 ? -9.995  -94.967  67.026  1.00 54.76  ? 371 VAL   A CG2    1 
ATOM   2874  N  N      . GLN   A 1  372 ? -8.371  -97.915  68.846  1.00 59.72  ? 372 GLN   A N      1 
ATOM   2875  C  CA     . GLN   A 1  372 ? -8.913  -98.928  69.742  1.00 61.17  ? 372 GLN   A CA     1 
ATOM   2876  C  C      . GLN   A 1  372 ? -10.174 -98.425  70.415  1.00 60.84  ? 372 GLN   A C      1 
ATOM   2877  O  O      . GLN   A 1  372 ? -11.135 -99.181  70.607  1.00 60.56  ? 372 GLN   A O      1 
ATOM   2878  C  CB     . GLN   A 1  372 ? -7.864  -99.299  70.781  1.00 66.66  ? 372 GLN   A CB     1 
ATOM   2879  C  CG     . GLN   A 1  372 ? -6.731  -100.129 70.227  1.00 78.17  ? 372 GLN   A CG     1 
ATOM   2880  C  CD     . GLN   A 1  372 ? -5.556  -100.212 71.184  1.00 85.75  ? 372 GLN   A CD     1 
ATOM   2881  O  OE1    . GLN   A 1  372 ? -5.672  -99.858  72.364  1.00 83.82  ? 372 GLN   A OE1    1 
ATOM   2882  N  NE2    . GLN   A 1  372 ? -4.406  -100.667 70.677  1.00 87.13  ? 372 GLN   A NE2    1 
ATOM   2883  N  N      . ARG   A 1  373 ? -10.187 -97.149  70.775  1.00 58.31  ? 373 ARG   A N      1 
ATOM   2884  C  CA     . ARG   A 1  373 ? -11.330 -96.550  71.431  1.00 55.15  ? 373 ARG   A CA     1 
ATOM   2885  C  C      . ARG   A 1  373 ? -11.426 -95.119  70.931  1.00 51.27  ? 373 ARG   A C      1 
ATOM   2886  O  O      . ARG   A 1  373 ? -10.418 -94.526  70.536  1.00 48.95  ? 373 ARG   A O      1 
ATOM   2887  C  CB     . ARG   A 1  373 ? -11.192 -96.631  72.968  1.00 53.30  ? 373 ARG   A CB     1 
ATOM   2888  C  CG     . ARG   A 1  373 ? -10.004 -95.878  73.555  1.00 52.22  ? 373 ARG   A CG     1 
ATOM   2889  C  CD     . ARG   A 1  373 ? -9.590  -96.389  74.929  1.00 50.80  ? 373 ARG   A CD     1 
ATOM   2890  N  NE     . ARG   A 1  373 ? -9.192  -97.789  74.872  1.00 57.71  ? 373 ARG   A NE     1 
ATOM   2891  C  CZ     . ARG   A 1  373 ? -8.002  -98.213  74.461  1.00 63.99  ? 373 ARG   A CZ     1 
ATOM   2892  N  NH1    . ARG   A 1  373 ? -7.066  -97.366  74.083  1.00 63.25  ? 373 ARG   A NH1    1 
ATOM   2893  N  NH2    . ARG   A 1  373 ? -7.746  -99.521  74.429  1.00 62.22  ? 373 ARG   A NH2    1 
ATOM   2894  N  N      . ALA   A 1  374 ? -12.654 -94.594  70.906  1.00 48.39  ? 374 ALA   A N      1 
ATOM   2895  C  CA     . ALA   A 1  374 ? -12.913 -93.192  70.600  1.00 47.59  ? 374 ALA   A CA     1 
ATOM   2896  C  C      . ALA   A 1  374 ? -14.209 -92.766  71.281  1.00 47.37  ? 374 ALA   A C      1 
ATOM   2897  O  O      . ALA   A 1  374 ? -15.038 -93.602  71.659  1.00 48.85  ? 374 ALA   A O      1 
ATOM   2898  C  CB     . ALA   A 1  374 ? -12.979 -92.937  69.092  1.00 42.68  ? 374 ALA   A CB     1 
ATOM   2899  N  N      . VAL   A 1  375 ? -14.359 -91.449  71.462  1.00 40.78  ? 375 VAL   A N      1 
ATOM   2900  C  CA     . VAL   A 1  375 ? -15.510 -90.878  72.154  1.00 38.08  ? 375 VAL   A CA     1 
ATOM   2901  C  C      . VAL   A 1  375 ? -15.973 -89.658  71.379  1.00 38.53  ? 375 VAL   A C      1 
ATOM   2902  O  O      . VAL   A 1  375 ? -15.170 -88.964  70.749  1.00 40.69  ? 375 VAL   A O      1 
ATOM   2903  C  CB     . VAL   A 1  375 ? -15.204 -90.497  73.630  1.00 36.29  ? 375 VAL   A CB     1 
ATOM   2904  C  CG1    . VAL   A 1  375 ? -14.128 -89.446  73.694  1.00 37.32  ? 375 VAL   A CG1    1 
ATOM   2905  C  CG2    . VAL   A 1  375 ? -16.465 -89.970  74.340  1.00 31.32  ? 375 VAL   A CG2    1 
ATOM   2906  N  N      . CYS   A 1  376 ? -17.285 -89.404  71.434  1.00 35.51  ? 376 CYS   A N      1 
ATOM   2907  C  CA     . CYS   A 1  376 ? -17.916 -88.178  70.946  1.00 37.62  ? 376 CYS   A CA     1 
ATOM   2908  C  C      . CYS   A 1  376 ? -18.743 -87.570  72.068  1.00 40.79  ? 376 CYS   A C      1 
ATOM   2909  O  O      . CYS   A 1  376 ? -19.801 -88.106  72.415  1.00 42.48  ? 376 CYS   A O      1 
ATOM   2910  C  CB     . CYS   A 1  376 ? -18.809 -88.467  69.736  1.00 39.97  ? 376 CYS   A CB     1 
ATOM   2911  S  SG     . CYS   A 1  376 ? -19.795 -87.051  69.102  1.00 38.11  ? 376 CYS   A SG     1 
ATOM   2912  N  N      . MET   A 1  377 ? -18.297 -86.459  72.643  1.00 35.74  ? 377 MET   A N      1 
ATOM   2913  C  CA     . MET   A 1  377 ? -19.096 -85.861  73.700  1.00 41.60  ? 377 MET   A CA     1 
ATOM   2914  C  C      . MET   A 1  377 ? -20.136 -84.945  73.060  1.00 45.03  ? 377 MET   A C      1 
ATOM   2915  O  O      . MET   A 1  377 ? -19.832 -84.258  72.083  1.00 46.02  ? 377 MET   A O      1 
ATOM   2916  C  CB     . MET   A 1  377 ? -18.238 -85.104  74.716  1.00 38.82  ? 377 MET   A CB     1 
ATOM   2917  C  CG     . MET   A 1  377 ? -19.102 -84.487  75.793  1.00 42.35  ? 377 MET   A CG     1 
ATOM   2918  S  SD     . MET   A 1  377 ? -18.298 -83.853  77.266  1.00 53.07  ? 377 MET   A SD     1 
ATOM   2919  C  CE     . MET   A 1  377 ? -17.569 -82.339  76.699  1.00 45.51  ? 377 MET   A CE     1 
ATOM   2920  N  N      . LEU   A 1  378 ? -21.371 -84.974  73.582  1.00 41.94  ? 378 LEU   A N      1 
ATOM   2921  C  CA     . LEU   A 1  378 ? -22.444 -84.072  73.165  1.00 40.63  ? 378 LEU   A CA     1 
ATOM   2922  C  C      . LEU   A 1  378 ? -22.869 -83.266  74.371  1.00 38.73  ? 378 LEU   A C      1 
ATOM   2923  O  O      . LEU   A 1  378 ? -23.542 -83.793  75.257  1.00 46.79  ? 378 LEU   A O      1 
ATOM   2924  C  CB     . LEU   A 1  378 ? -23.670 -84.798  72.617  1.00 41.53  ? 378 LEU   A CB     1 
ATOM   2925  C  CG     . LEU   A 1  378 ? -23.561 -85.760  71.455  1.00 40.38  ? 378 LEU   A CG     1 
ATOM   2926  C  CD1    . LEU   A 1  378 ? -24.961 -86.291  71.051  1.00 38.18  ? 378 LEU   A CD1    1 
ATOM   2927  C  CD2    . LEU   A 1  378 ? -22.817 -85.094  70.333  1.00 39.22  ? 378 LEU   A CD2    1 
ATOM   2928  N  N      . SER   A 1  379 ? -22.541 -81.986  74.380  1.00 39.27  ? 379 SER   A N      1 
ATOM   2929  C  CA     . SER   A 1  379 ? -22.766 -81.150  75.548  1.00 43.48  ? 379 SER   A CA     1 
ATOM   2930  C  C      . SER   A 1  379 ? -23.510 -79.894  75.136  1.00 44.08  ? 379 SER   A C      1 
ATOM   2931  O  O      . SER   A 1  379 ? -22.999 -79.092  74.350  1.00 44.67  ? 379 SER   A O      1 
ATOM   2932  C  CB     . SER   A 1  379 ? -21.434 -80.802  76.230  1.00 45.56  ? 379 SER   A CB     1 
ATOM   2933  O  OG     . SER   A 1  379 ? -20.436 -80.410  75.296  1.00 46.03  ? 379 SER   A OG     1 
ATOM   2934  N  N      . ASN   A 1  380 ? -24.695 -79.702  75.690  1.00 43.37  ? 380 ASN   A N      1 
ATOM   2935  C  CA     . ASN   A 1  380 ? -25.460 -78.500  75.405  1.00 38.62  ? 380 ASN   A CA     1 
ATOM   2936  C  C      . ASN   A 1  380 ? -24.988 -77.377  76.318  1.00 40.59  ? 380 ASN   A C      1 
ATOM   2937  O  O      . ASN   A 1  380 ? -25.625 -77.038  77.310  1.00 40.79  ? 380 ASN   A O      1 
ATOM   2938  C  CB     . ASN   A 1  380 ? -26.931 -78.780  75.603  1.00 41.50  ? 380 ASN   A CB     1 
ATOM   2939  C  CG     . ASN   A 1  380 ? -27.768 -77.664  75.162  1.00 44.06  ? 380 ASN   A CG     1 
ATOM   2940  O  OD1    . ASN   A 1  380 ? -27.313 -76.526  75.140  1.00 51.11  ? 380 ASN   A OD1    1 
ATOM   2941  N  ND2    . ASN   A 1  380 ? -29.004 -77.957  74.783  1.00 47.04  ? 380 ASN   A ND2    1 
ATOM   2942  N  N      . THR   A 1  381 ? -23.844 -76.789  75.981  1.00 43.66  ? 381 THR   A N      1 
ATOM   2943  C  CA     . THR   A 1  381 ? -23.337 -75.649  76.736  1.00 43.98  ? 381 THR   A CA     1 
ATOM   2944  C  C      . THR   A 1  381 ? -23.833 -74.354  76.124  1.00 48.96  ? 381 THR   A C      1 
ATOM   2945  O  O      . THR   A 1  381 ? -24.065 -74.275  74.914  1.00 47.70  ? 381 THR   A O      1 
ATOM   2946  C  CB     . THR   A 1  381 ? -21.820 -75.597  76.752  1.00 45.06  ? 381 THR   A CB     1 
ATOM   2947  O  OG1    . THR   A 1  381 ? -21.408 -74.346  77.323  1.00 50.11  ? 381 THR   A OG1    1 
ATOM   2948  C  CG2    . THR   A 1  381 ? -21.290 -75.690  75.346  1.00 39.62  ? 381 THR   A CG2    1 
ATOM   2949  N  N      . THR   A 1  382 ? -23.983 -73.326  76.968  1.00 48.80  ? 382 THR   A N      1 
ATOM   2950  C  CA     . THR   A 1  382 ? -24.400 -72.030  76.441  1.00 48.23  ? 382 THR   A CA     1 
ATOM   2951  C  C      . THR   A 1  382 ? -23.298 -71.379  75.626  1.00 45.38  ? 382 THR   A C      1 
ATOM   2952  O  O      . THR   A 1  382 ? -23.587 -70.495  74.815  1.00 44.66  ? 382 THR   A O      1 
ATOM   2953  C  CB     . THR   A 1  382 ? -24.851 -71.077  77.558  1.00 44.79  ? 382 THR   A CB     1 
ATOM   2954  O  OG1    . THR   A 1  382 ? -23.740 -70.713  78.391  1.00 52.28  ? 382 THR   A OG1    1 
ATOM   2955  C  CG2    . THR   A 1  382 ? -25.946 -71.699  78.392  1.00 43.14  ? 382 THR   A CG2    1 
ATOM   2956  N  N      . ALA   A 1  383 ? -22.052 -71.819  75.800  1.00 44.28  ? 383 ALA   A N      1 
ATOM   2957  C  CA     . ALA   A 1  383 ? -20.921 -71.214  75.104  1.00 48.27  ? 383 ALA   A CA     1 
ATOM   2958  C  C      . ALA   A 1  383 ? -21.009 -71.340  73.583  1.00 43.83  ? 383 ALA   A C      1 
ATOM   2959  O  O      . ALA   A 1  383 ? -20.232 -70.691  72.881  1.00 44.62  ? 383 ALA   A O      1 
ATOM   2960  C  CB     . ALA   A 1  383 ? -19.608 -71.823  75.609  1.00 46.38  ? 383 ALA   A CB     1 
ATOM   2961  N  N      . ILE   A 1  384 ? -21.934 -72.142  73.054  1.00 45.20  ? 384 ILE   A N      1 
ATOM   2962  C  CA     . ILE   A 1  384 ? -22.148 -72.193  71.616  1.00 40.08  ? 384 ILE   A CA     1 
ATOM   2963  C  C      . ILE   A 1  384 ? -22.818 -70.935  71.110  1.00 40.89  ? 384 ILE   A C      1 
ATOM   2964  O  O      . ILE   A 1  384 ? -22.834 -70.688  69.906  1.00 42.86  ? 384 ILE   A O      1 
ATOM   2965  C  CB     . ILE   A 1  384 ? -23.018 -73.400  71.210  1.00 39.51  ? 384 ILE   A CB     1 
ATOM   2966  C  CG1    . ILE   A 1  384 ? -22.825 -73.748  69.739  1.00 33.22  ? 384 ILE   A CG1    1 
ATOM   2967  C  CG2    . ILE   A 1  384 ? -24.455 -73.121  71.488  1.00 35.32  ? 384 ILE   A CG2    1 
ATOM   2968  C  CD1    . ILE   A 1  384 ? -22.951 -75.201  69.492  1.00 36.57  ? 384 ILE   A CD1    1 
ATOM   2969  N  N      . ALA   A 1  385 ? -23.382 -70.122  71.990  1.00 43.35  ? 385 ALA   A N      1 
ATOM   2970  C  CA     . ALA   A 1  385 ? -23.976 -68.905  71.475  1.00 43.34  ? 385 ALA   A CA     1 
ATOM   2971  C  C      . ALA   A 1  385 ? -22.917 -67.988  70.915  1.00 38.33  ? 385 ALA   A C      1 
ATOM   2972  O  O      . ALA   A 1  385 ? -23.255 -67.102  70.134  1.00 46.21  ? 385 ALA   A O      1 
ATOM   2973  C  CB     . ALA   A 1  385 ? -24.800 -68.193  72.547  1.00 44.01  ? 385 ALA   A CB     1 
ATOM   2974  N  N      . GLU   A 1  386 ? -21.651 -68.187  71.274  1.00 33.40  ? 386 GLU   A N      1 
ATOM   2975  C  CA     . GLU   A 1  386 ? -20.586 -67.440  70.611  1.00 39.99  ? 386 GLU   A CA     1 
ATOM   2976  C  C      . GLU   A 1  386 ? -20.771 -67.477  69.101  1.00 42.20  ? 386 GLU   A C      1 
ATOM   2977  O  O      . GLU   A 1  386 ? -20.572 -66.468  68.407  1.00 39.08  ? 386 GLU   A O      1 
ATOM   2978  C  CB     . GLU   A 1  386 ? -19.211 -68.004  70.999  1.00 42.38  ? 386 GLU   A CB     1 
ATOM   2979  C  CG     . GLU   A 1  386 ? -18.612 -67.446  72.303  1.00 45.41  ? 386 GLU   A CG     1 
ATOM   2980  C  CD     . GLU   A 1  386 ? -17.444 -68.280  72.858  1.00 48.63  ? 386 GLU   A CD     1 
ATOM   2981  O  OE1    . GLU   A 1  386 ? -16.507 -68.590  72.073  1.00 49.34  ? 386 GLU   A OE1    1 
ATOM   2982  O  OE2    . GLU   A 1  386 ? -17.463 -68.585  74.087  1.00 45.26  ? 386 GLU   A OE2    1 
ATOM   2983  N  N      . ALA   A 1  387 ? -21.174 -68.638  68.579  1.00 42.08  ? 387 ALA   A N      1 
ATOM   2984  C  CA     . ALA   A 1  387 ? -21.366 -68.779  67.145  1.00 39.52  ? 387 ALA   A CA     1 
ATOM   2985  C  C      . ALA   A 1  387 ? -22.457 -67.847  66.674  1.00 39.97  ? 387 ALA   A C      1 
ATOM   2986  O  O      . ALA   A 1  387 ? -22.344 -67.241  65.605  1.00 41.45  ? 387 ALA   A O      1 
ATOM   2987  C  CB     . ALA   A 1  387 ? -21.689 -70.230  66.787  1.00 31.37  ? 387 ALA   A CB     1 
ATOM   2988  N  N      . TRP   A 1  388 ? -23.520 -67.706  67.470  1.00 43.42  ? 388 TRP   A N      1 
ATOM   2989  C  CA     . TRP   A 1  388 ? -24.599 -66.795  67.103  1.00 41.42  ? 388 TRP   A CA     1 
ATOM   2990  C  C      . TRP   A 1  388 ? -24.135 -65.343  67.142  1.00 46.15  ? 388 TRP   A C      1 
ATOM   2991  O  O      . TRP   A 1  388 ? -24.478 -64.550  66.263  1.00 45.83  ? 388 TRP   A O      1 
ATOM   2992  C  CB     . TRP   A 1  388 ? -25.786 -66.989  68.033  1.00 39.52  ? 388 TRP   A CB     1 
ATOM   2993  C  CG     . TRP   A 1  388 ? -26.392 -68.347  68.014  1.00 45.76  ? 388 TRP   A CG     1 
ATOM   2994  C  CD1    . TRP   A 1  388 ? -26.744 -69.114  69.103  1.00 48.68  ? 388 TRP   A CD1    1 
ATOM   2995  C  CD2    . TRP   A 1  388 ? -26.700 -69.136  66.857  1.00 39.94  ? 388 TRP   A CD2    1 
ATOM   2996  N  NE1    . TRP   A 1  388 ? -27.293 -70.309  68.679  1.00 47.04  ? 388 TRP   A NE1    1 
ATOM   2997  C  CE2    . TRP   A 1  388 ? -27.267 -70.346  67.309  1.00 41.39  ? 388 TRP   A CE2    1 
ATOM   2998  C  CE3    . TRP   A 1  388 ? -26.570 -68.929  65.489  1.00 39.36  ? 388 TRP   A CE3    1 
ATOM   2999  C  CZ2    . TRP   A 1  388 ? -27.694 -71.336  66.435  1.00 46.14  ? 388 TRP   A CZ2    1 
ATOM   3000  C  CZ3    . TRP   A 1  388 ? -26.998 -69.922  64.623  1.00 40.98  ? 388 TRP   A CZ3    1 
ATOM   3001  C  CH2    . TRP   A 1  388 ? -27.551 -71.101  65.095  1.00 42.45  ? 388 TRP   A CH2    1 
ATOM   3002  N  N      . ALA   A 1  389 ? -23.369 -64.968  68.161  1.00 42.32  ? 389 ALA   A N      1 
ATOM   3003  C  CA     . ALA   A 1  389 ? -22.775 -63.644  68.178  1.00 40.73  ? 389 ALA   A CA     1 
ATOM   3004  C  C      . ALA   A 1  389 ? -22.015 -63.373  66.887  1.00 44.24  ? 389 ALA   A C      1 
ATOM   3005  O  O      . ALA   A 1  389 ? -22.301 -62.410  66.175  1.00 46.63  ? 389 ALA   A O      1 
ATOM   3006  C  CB     . ALA   A 1  389 ? -21.851 -63.513  69.382  1.00 40.62  ? 389 ALA   A CB     1 
ATOM   3007  N  N      . ARG   A 1  390 ? -21.035 -64.216  66.570  1.00 43.41  ? 390 ARG   A N      1 
ATOM   3008  C  CA     . ARG   A 1  390 ? -20.211 -64.010  65.381  1.00 46.50  ? 390 ARG   A CA     1 
ATOM   3009  C  C      . ARG   A 1  390 ? -21.072 -63.817  64.132  1.00 43.78  ? 390 ARG   A C      1 
ATOM   3010  O  O      . ARG   A 1  390 ? -21.067 -62.760  63.499  1.00 44.28  ? 390 ARG   A O      1 
ATOM   3011  C  CB     . ARG   A 1  390 ? -19.278 -65.214  65.201  1.00 51.52  ? 390 ARG   A CB     1 
ATOM   3012  C  CG     . ARG   A 1  390 ? -18.275 -65.392  66.346  1.00 52.95  ? 390 ARG   A CG     1 
ATOM   3013  C  CD     . ARG   A 1  390 ? -17.344 -66.597  66.178  1.00 48.53  ? 390 ARG   A CD     1 
ATOM   3014  N  NE     . ARG   A 1  390 ? -17.325 -67.168  64.839  1.00 44.92  ? 390 ARG   A NE     1 
ATOM   3015  C  CZ     . ARG   A 1  390 ? -17.315 -68.474  64.617  1.00 50.74  ? 390 ARG   A CZ     1 
ATOM   3016  N  NH1    . ARG   A 1  390 ? -17.534 -69.338  65.598  1.00 55.71  ? 390 ARG   A NH1    1 
ATOM   3017  N  NH2    . ARG   A 1  390 ? -17.107 -68.928  63.383  1.00 42.56  ? 390 ARG   A NH2    1 
ATOM   3018  N  N      . LEU   A 1  391 ? -21.813 -64.848  63.760  1.00 43.98  ? 391 LEU   A N      1 
ATOM   3019  C  CA     . LEU   A 1  391 ? -22.692 -64.760  62.607  1.00 40.51  ? 391 LEU   A CA     1 
ATOM   3020  C  C      . LEU   A 1  391 ? -23.569 -63.513  62.678  1.00 41.40  ? 391 LEU   A C      1 
ATOM   3021  O  O      . LEU   A 1  391 ? -23.647 -62.738  61.723  1.00 40.37  ? 391 LEU   A O      1 
ATOM   3022  C  CB     . LEU   A 1  391 ? -23.536 -66.023  62.558  1.00 31.54  ? 391 LEU   A CB     1 
ATOM   3023  C  CG     . LEU   A 1  391 ? -24.112 -66.509  61.252  1.00 35.38  ? 391 LEU   A CG     1 
ATOM   3024  C  CD1    . LEU   A 1  391 ? -23.027 -67.045  60.320  1.00 28.83  ? 391 LEU   A CD1    1 
ATOM   3025  C  CD2    . LEU   A 1  391 ? -25.122 -67.576  61.614  1.00 36.42  ? 391 LEU   A CD2    1 
ATOM   3026  N  N      . ASP   A 1  392 ? -24.232 -63.294  63.816  1.00 44.85  ? 392 ASP   A N      1 
ATOM   3027  C  CA     . ASP   A 1  392 ? -25.147 -62.154  63.930  1.00 45.31  ? 392 ASP   A CA     1 
ATOM   3028  C  C      . ASP   A 1  392 ? -24.432 -60.840  63.668  1.00 39.99  ? 392 ASP   A C      1 
ATOM   3029  O  O      . ASP   A 1  392 ? -24.998 -59.932  63.064  1.00 40.69  ? 392 ASP   A O      1 
ATOM   3030  C  CB     . ASP   A 1  392 ? -25.816 -62.115  65.312  1.00 47.48  ? 392 ASP   A CB     1 
ATOM   3031  C  CG     . ASP   A 1  392 ? -26.932 -63.154  65.473  1.00 51.82  ? 392 ASP   A CG     1 
ATOM   3032  O  OD1    . ASP   A 1  392 ? -27.468 -63.655  64.455  1.00 48.83  ? 392 ASP   A OD1    1 
ATOM   3033  O  OD2    . ASP   A 1  392 ? -27.286 -63.454  66.636  1.00 53.72  ? 392 ASP   A OD2    1 
ATOM   3034  N  N      . HIS   A 1  393 ? -23.192 -60.714  64.122  1.00 43.64  ? 393 HIS   A N      1 
ATOM   3035  C  CA     . HIS   A 1  393 ? -22.439 -59.487  63.885  1.00 46.45  ? 393 HIS   A CA     1 
ATOM   3036  C  C      . HIS   A 1  393 ? -22.209 -59.268  62.398  1.00 47.84  ? 393 HIS   A C      1 
ATOM   3037  O  O      . HIS   A 1  393 ? -22.464 -58.176  61.872  1.00 49.99  ? 393 HIS   A O      1 
ATOM   3038  C  CB     . HIS   A 1  393 ? -21.093 -59.549  64.591  1.00 46.93  ? 393 HIS   A CB     1 
ATOM   3039  C  CG     . HIS   A 1  393 ? -20.318 -58.279  64.522  1.00 47.50  ? 393 HIS   A CG     1 
ATOM   3040  N  ND1    . HIS   A 1  393 ? -20.702 -57.143  65.202  1.00 54.14  ? 393 HIS   A ND1    1 
ATOM   3041  C  CD2    . HIS   A 1  393 ? -19.207 -57.948  63.823  1.00 48.21  ? 393 HIS   A CD2    1 
ATOM   3042  C  CE1    . HIS   A 1  393 ? -19.827 -56.181  64.969  1.00 55.68  ? 393 HIS   A CE1    1 
ATOM   3043  N  NE2    . HIS   A 1  393 ? -18.914 -56.643  64.131  1.00 54.91  ? 393 HIS   A NE2    1 
ATOM   3044  N  N      . LYS   A 1  394 ? -21.682 -60.283  61.704  1.00 40.76  ? 394 LYS   A N      1 
ATOM   3045  C  CA     . LYS   A 1  394 ? -21.504 -60.128  60.272  1.00 37.55  ? 394 LYS   A CA     1 
ATOM   3046  C  C      . LYS   A 1  394 ? -22.805 -59.668  59.654  1.00 39.39  ? 394 LYS   A C      1 
ATOM   3047  O  O      . LYS   A 1  394 ? -22.849 -58.650  58.957  1.00 43.83  ? 394 LYS   A O      1 
ATOM   3048  C  CB     . LYS   A 1  394 ? -21.001 -61.425  59.640  1.00 32.51  ? 394 LYS   A CB     1 
ATOM   3049  C  CG     . LYS   A 1  394 ? -19.720 -61.835  60.248  1.00 34.76  ? 394 LYS   A CG     1 
ATOM   3050  C  CD     . LYS   A 1  394 ? -19.165 -63.148  59.800  1.00 31.15  ? 394 LYS   A CD     1 
ATOM   3051  C  CE     . LYS   A 1  394 ? -17.640 -63.055  59.765  1.00 35.10  ? 394 LYS   A CE     1 
ATOM   3052  N  NZ     . LYS   A 1  394 ? -17.001 -64.396  59.651  1.00 53.93  ? 394 LYS   A NZ     1 
ATOM   3053  N  N      . PHE   A 1  395 ? -23.893 -60.361  59.977  1.00 37.16  ? 395 PHE   A N      1 
ATOM   3054  C  CA     . PHE   A 1  395 ? -25.191 -59.972  59.447  1.00 42.09  ? 395 PHE   A CA     1 
ATOM   3055  C  C      . PHE   A 1  395 ? -25.429 -58.487  59.666  1.00 43.01  ? 395 PHE   A C      1 
ATOM   3056  O  O      . PHE   A 1  395 ? -25.800 -57.754  58.738  1.00 44.23  ? 395 PHE   A O      1 
ATOM   3057  C  CB     . PHE   A 1  395 ? -26.274 -60.822  60.104  1.00 41.17  ? 395 PHE   A CB     1 
ATOM   3058  C  CG     . PHE   A 1  395 ? -27.666 -60.462  59.705  1.00 41.19  ? 395 PHE   A CG     1 
ATOM   3059  C  CD1    . PHE   A 1  395 ? -28.287 -59.320  60.219  1.00 40.34  ? 395 PHE   A CD1    1 
ATOM   3060  C  CD2    . PHE   A 1  395 ? -28.368 -61.277  58.828  1.00 41.16  ? 395 PHE   A CD2    1 
ATOM   3061  C  CE1    . PHE   A 1  395 ? -29.587 -58.992  59.858  1.00 38.07  ? 395 PHE   A CE1    1 
ATOM   3062  C  CE2    . PHE   A 1  395 ? -29.672 -60.958  58.464  1.00 40.70  ? 395 PHE   A CE2    1 
ATOM   3063  C  CZ     . PHE   A 1  395 ? -30.282 -59.810  58.979  1.00 38.12  ? 395 PHE   A CZ     1 
ATOM   3064  N  N      . ASP   A 1  396 ? -25.147 -58.016  60.871  1.00 39.50  ? 396 ASP   A N      1 
ATOM   3065  C  CA     . ASP   A 1  396 ? -25.385 -56.621  61.184  1.00 41.17  ? 396 ASP   A CA     1 
ATOM   3066  C  C      . ASP   A 1  396 ? -24.545 -55.720  60.289  1.00 44.67  ? 396 ASP   A C      1 
ATOM   3067  O  O      . ASP   A 1  396 ? -25.062 -54.755  59.708  1.00 45.29  ? 396 ASP   A O      1 
ATOM   3068  C  CB     . ASP   A 1  396 ? -25.082 -56.385  62.658  1.00 41.34  ? 396 ASP   A CB     1 
ATOM   3069  C  CG     . ASP   A 1  396 ? -26.135 -57.025  63.579  1.00 45.50  ? 396 ASP   A CG     1 
ATOM   3070  O  OD1    . ASP   A 1  396 ? -27.209 -57.456  63.078  1.00 45.35  ? 396 ASP   A OD1    1 
ATOM   3071  O  OD2    . ASP   A 1  396 ? -25.869 -57.123  64.800  1.00 41.30  ? 396 ASP   A OD2    1 
ATOM   3072  N  N      . LEU   A 1  397 ? -23.257 -56.037  60.129  1.00 41.41  ? 397 LEU   A N      1 
ATOM   3073  C  CA     . LEU   A 1  397 ? -22.402 -55.166  59.328  1.00 43.84  ? 397 LEU   A CA     1 
ATOM   3074  C  C      . LEU   A 1  397 ? -22.992 -54.941  57.944  1.00 46.74  ? 397 LEU   A C      1 
ATOM   3075  O  O      . LEU   A 1  397 ? -23.150 -53.794  57.510  1.00 49.95  ? 397 LEU   A O      1 
ATOM   3076  C  CB     . LEU   A 1  397 ? -20.974 -55.715  59.221  1.00 40.39  ? 397 LEU   A CB     1 
ATOM   3077  C  CG     . LEU   A 1  397 ? -20.080 -55.634  60.464  1.00 38.48  ? 397 LEU   A CG     1 
ATOM   3078  C  CD1    . LEU   A 1  397 ? -18.831 -56.439  60.307  1.00 44.66  ? 397 LEU   A CD1    1 
ATOM   3079  C  CD2    . LEU   A 1  397 ? -19.713 -54.214  60.789  1.00 33.51  ? 397 LEU   A CD2    1 
ATOM   3080  N  N      . MET   A 1  398 ? -23.332 -56.023  57.232  1.00 46.09  ? 398 MET   A N      1 
ATOM   3081  C  CA     . MET   A 1  398 ? -23.801 -55.868  55.858  1.00 41.20  ? 398 MET   A CA     1 
ATOM   3082  C  C      . MET   A 1  398 ? -25.160 -55.200  55.838  1.00 47.29  ? 398 MET   A C      1 
ATOM   3083  O  O      . MET   A 1  398 ? -25.400 -54.268  55.058  1.00 48.06  ? 398 MET   A O      1 
ATOM   3084  C  CB     . MET   A 1  398 ? -23.894 -57.214  55.157  1.00 38.12  ? 398 MET   A CB     1 
ATOM   3085  C  CG     . MET   A 1  398 ? -22.563 -57.844  54.893  1.00 45.83  ? 398 MET   A CG     1 
ATOM   3086  S  SD     . MET   A 1  398 ? -22.805 -59.456  54.147  1.00 52.06  ? 398 MET   A SD     1 
ATOM   3087  C  CE     . MET   A 1  398 ? -23.540 -58.927  52.617  1.00 37.55  ? 398 MET   A CE     1 
ATOM   3088  N  N      . TYR   A 1  399 ? -26.064 -55.670  56.703  1.00 45.25  ? 399 TYR   A N      1 
ATOM   3089  C  CA     . TYR   A 1  399 ? -27.435 -55.194  56.690  1.00 41.62  ? 399 TYR   A CA     1 
ATOM   3090  C  C      . TYR   A 1  399 ? -27.549 -53.718  57.008  1.00 42.76  ? 399 TYR   A C      1 
ATOM   3091  O  O      . TYR   A 1  399 ? -28.570 -53.113  56.667  1.00 41.74  ? 399 TYR   A O      1 
ATOM   3092  C  CB     . TYR   A 1  399 ? -28.276 -55.968  57.686  1.00 39.49  ? 399 TYR   A CB     1 
ATOM   3093  C  CG     . TYR   A 1  399 ? -29.733 -55.734  57.464  1.00 38.22  ? 399 TYR   A CG     1 
ATOM   3094  C  CD1    . TYR   A 1  399 ? -30.379 -56.313  56.398  1.00 49.01  ? 399 TYR   A CD1    1 
ATOM   3095  C  CD2    . TYR   A 1  399 ? -30.452 -54.883  58.273  1.00 35.20  ? 399 TYR   A CD2    1 
ATOM   3096  C  CE1    . TYR   A 1  399 ? -31.722 -56.093  56.166  1.00 50.74  ? 399 TYR   A CE1    1 
ATOM   3097  C  CE2    . TYR   A 1  399 ? -31.785 -54.659  58.057  1.00 39.54  ? 399 TYR   A CE2    1 
ATOM   3098  C  CZ     . TYR   A 1  399 ? -32.416 -55.263  56.994  1.00 47.24  ? 399 TYR   A CZ     1 
ATOM   3099  O  OH     . TYR   A 1  399 ? -33.746 -55.059  56.739  1.00 47.84  ? 399 TYR   A OH     1 
ATOM   3100  N  N      . ALA   A 1  400 ? -26.549 -53.125  57.677  1.00 45.01  ? 400 ALA   A N      1 
ATOM   3101  C  CA     . ALA   A 1  400 ? -26.658 -51.700  57.991  1.00 47.41  ? 400 ALA   A CA     1 
ATOM   3102  C  C      . ALA   A 1  400 ? -26.540 -50.848  56.744  1.00 43.94  ? 400 ALA   A C      1 
ATOM   3103  O  O      . ALA   A 1  400 ? -27.039 -49.725  56.723  1.00 48.96  ? 400 ALA   A O      1 
ATOM   3104  C  CB     . ALA   A 1  400 ? -25.615 -51.265  59.016  1.00 40.76  ? 400 ALA   A CB     1 
ATOM   3105  N  N      . LYS   A 1  401 ? -25.876 -51.352  55.718  1.00 42.15  ? 401 LYS   A N      1 
ATOM   3106  C  CA     . LYS   A 1  401 ? -25.871 -50.728  54.411  1.00 43.14  ? 401 LYS   A CA     1 
ATOM   3107  C  C      . LYS   A 1  401 ? -26.899 -51.336  53.482  1.00 38.17  ? 401 LYS   A C      1 
ATOM   3108  O  O      . LYS   A 1  401 ? -27.005 -50.919  52.336  1.00 40.75  ? 401 LYS   A O      1 
ATOM   3109  C  CB     . LYS   A 1  401 ? -24.471 -50.831  53.813  1.00 45.18  ? 401 LYS   A CB     1 
ATOM   3110  C  CG     . LYS   A 1  401 ? -23.409 -50.543  54.850  1.00 43.28  ? 401 LYS   A CG     1 
ATOM   3111  C  CD     . LYS   A 1  401 ? -23.370 -49.048  55.058  1.00 45.96  ? 401 LYS   A CD     1 
ATOM   3112  C  CE     . LYS   A 1  401 ? -22.307 -48.625  56.065  1.00 63.50  ? 401 LYS   A CE     1 
ATOM   3113  N  NZ     . LYS   A 1  401 ? -22.575 -49.146  57.440  1.00 66.24  ? 401 LYS   A NZ     1 
ATOM   3114  N  N      . ARG   A 1  402 ? -27.672 -52.293  53.966  1.00 42.82  ? 402 ARG   A N      1 
ATOM   3115  C  CA     . ARG   A 1  402 ? -28.544 -53.131  53.135  1.00 45.03  ? 402 ARG   A CA     1 
ATOM   3116  C  C      . ARG   A 1  402 ? -27.833 -53.706  51.914  1.00 36.28  ? 402 ARG   A C      1 
ATOM   3117  O  O      . ARG   A 1  402 ? -28.469 -54.042  50.919  1.00 34.56  ? 402 ARG   A O      1 
ATOM   3118  C  CB     . ARG   A 1  402 ? -29.823 -52.384  52.747  1.00 39.87  ? 402 ARG   A CB     1 
ATOM   3119  C  CG     . ARG   A 1  402 ? -30.825 -52.504  53.848  1.00 44.76  ? 402 ARG   A CG     1 
ATOM   3120  C  CD     . ARG   A 1  402 ? -31.843 -51.413  53.924  1.00 51.58  ? 402 ARG   A CD     1 
ATOM   3121  N  NE     . ARG   A 1  402 ? -32.626 -51.638  55.128  1.00 48.06  ? 402 ARG   A NE     1 
ATOM   3122  C  CZ     . ARG   A 1  402 ? -32.092 -51.705  56.337  1.00 45.80  ? 402 ARG   A CZ     1 
ATOM   3123  N  NH1    . ARG   A 1  402 ? -30.802 -51.492  56.537  1.00 47.68  ? 402 ARG   A NH1    1 
ATOM   3124  N  NH2    . ARG   A 1  402 ? -32.867 -51.998  57.373  1.00 51.64  ? 402 ARG   A NH2    1 
ATOM   3125  N  N      . ALA   A 1  403 ? -26.521 -53.884  52.009  1.00 34.82  ? 403 ALA   A N      1 
ATOM   3126  C  CA     . ALA   A 1  403 ? -25.797 -54.538  50.935  1.00 36.48  ? 403 ALA   A CA     1 
ATOM   3127  C  C      . ALA   A 1  403 ? -26.426 -55.891  50.619  1.00 34.39  ? 403 ALA   A C      1 
ATOM   3128  O  O      . ALA   A 1  403 ? -26.835 -56.626  51.511  1.00 38.73  ? 403 ALA   A O      1 
ATOM   3129  C  CB     . ALA   A 1  403 ? -24.318 -54.696  51.306  1.00 40.35  ? 403 ALA   A CB     1 
ATOM   3130  N  N      . PHE   A 1  404 ? -26.553 -56.187  49.330  1.00 36.86  ? 404 PHE   A N      1 
ATOM   3131  C  CA     . PHE   A 1  404 ? -27.171 -57.401  48.801  1.00 35.60  ? 404 PHE   A CA     1 
ATOM   3132  C  C      . PHE   A 1  404 ? -28.651 -57.615  49.120  1.00 34.29  ? 404 PHE   A C      1 
ATOM   3133  O  O      . PHE   A 1  404 ? -29.264 -58.537  48.567  1.00 33.87  ? 404 PHE   A O      1 
ATOM   3134  C  CB     . PHE   A 1  404 ? -26.391 -58.605  49.263  1.00 33.59  ? 404 PHE   A CB     1 
ATOM   3135  C  CG     . PHE   A 1  404 ? -24.964 -58.522  48.955  1.00 35.46  ? 404 PHE   A CG     1 
ATOM   3136  C  CD1    . PHE   A 1  404 ? -24.492 -58.952  47.723  1.00 33.09  ? 404 PHE   A CD1    1 
ATOM   3137  C  CD2    . PHE   A 1  404 ? -24.077 -58.040  49.900  1.00 34.90  ? 404 PHE   A CD2    1 
ATOM   3138  C  CE1    . PHE   A 1  404 ? -23.139 -58.895  47.429  1.00 34.93  ? 404 PHE   A CE1    1 
ATOM   3139  C  CE2    . PHE   A 1  404 ? -22.724 -57.989  49.631  1.00 40.06  ? 404 PHE   A CE2    1 
ATOM   3140  C  CZ     . PHE   A 1  404 ? -22.250 -58.413  48.380  1.00 39.19  ? 404 PHE   A CZ     1 
ATOM   3141  N  N      . VAL   A 1  405 ? -29.254 -56.773  49.963  1.00 32.08  ? 405 VAL   A N      1 
ATOM   3142  C  CA     . VAL   A 1  405 ? -30.678 -56.934  50.274  1.00 34.99  ? 405 VAL   A CA     1 
ATOM   3143  C  C      . VAL   A 1  405 ? -31.531 -57.079  49.007  1.00 40.85  ? 405 VAL   A C      1 
ATOM   3144  O  O      . VAL   A 1  405 ? -32.557 -57.775  49.002  1.00 38.93  ? 405 VAL   A O      1 
ATOM   3145  C  CB     . VAL   A 1  405 ? -31.166 -55.756  51.127  1.00 35.51  ? 405 VAL   A CB     1 
ATOM   3146  C  CG1    . VAL   A 1  405 ? -32.674 -55.749  51.124  1.00 41.65  ? 405 VAL   A CG1    1 
ATOM   3147  C  CG2    . VAL   A 1  405 ? -30.610 -55.845  52.530  1.00 43.14  ? 405 VAL   A CG2    1 
ATOM   3148  N  N      . HIS   A 1  406 ? -31.142 -56.402  47.921  1.00 41.43  ? 406 HIS   A N      1 
ATOM   3149  C  CA     . HIS   A 1  406 ? -32.017 -56.349  46.761  1.00 35.65  ? 406 HIS   A CA     1 
ATOM   3150  C  C      . HIS   A 1  406 ? -32.125 -57.697  46.069  1.00 38.20  ? 406 HIS   A C      1 
ATOM   3151  O  O      . HIS   A 1  406 ? -33.181 -58.034  45.529  1.00 39.70  ? 406 HIS   A O      1 
ATOM   3152  C  CB     . HIS   A 1  406 ? -31.542 -55.273  45.788  1.00 37.06  ? 406 HIS   A CB     1 
ATOM   3153  C  CG     . HIS   A 1  406 ? -30.293 -55.620  45.058  1.00 35.36  ? 406 HIS   A CG     1 
ATOM   3154  N  ND1    . HIS   A 1  406 ? -29.042 -55.330  45.555  1.00 40.35  ? 406 HIS   A ND1    1 
ATOM   3155  C  CD2    . HIS   A 1  406 ? -30.100 -56.261  43.881  1.00 37.18  ? 406 HIS   A CD2    1 
ATOM   3156  C  CE1    . HIS   A 1  406 ? -28.129 -55.767  44.703  1.00 40.43  ? 406 HIS   A CE1    1 
ATOM   3157  N  NE2    . HIS   A 1  406 ? -28.745 -56.345  43.685  1.00 38.13  ? 406 HIS   A NE2    1 
ATOM   3158  N  N      . TRP   A 1  407 ? -31.058 -58.481  46.062  1.00 39.99  ? 407 TRP   A N      1 
ATOM   3159  C  CA     . TRP   A 1  407 ? -31.154 -59.797  45.455  1.00 39.26  ? 407 TRP   A CA     1 
ATOM   3160  C  C      . TRP   A 1  407 ? -32.259 -60.622  46.091  1.00 41.48  ? 407 TRP   A C      1 
ATOM   3161  O  O      . TRP   A 1  407 ? -32.897 -61.431  45.412  1.00 44.88  ? 407 TRP   A O      1 
ATOM   3162  C  CB     . TRP   A 1  407 ? -29.809 -60.497  45.555  1.00 38.88  ? 407 TRP   A CB     1 
ATOM   3163  C  CG     . TRP   A 1  407 ? -28.773 -59.920  44.660  1.00 34.63  ? 407 TRP   A CG     1 
ATOM   3164  C  CD1    . TRP   A 1  407 ? -27.669 -59.230  45.033  1.00 36.18  ? 407 TRP   A CD1    1 
ATOM   3165  C  CD2    . TRP   A 1  407 ? -28.688 -60.089  43.235  1.00 36.29  ? 407 TRP   A CD2    1 
ATOM   3166  N  NE1    . TRP   A 1  407 ? -26.925 -58.905  43.919  1.00 42.49  ? 407 TRP   A NE1    1 
ATOM   3167  C  CE2    . TRP   A 1  407 ? -27.530 -59.429  42.805  1.00 40.72  ? 407 TRP   A CE2    1 
ATOM   3168  C  CE3    . TRP   A 1  407 ? -29.492 -60.722  42.277  1.00 34.05  ? 407 TRP   A CE3    1 
ATOM   3169  C  CZ2    . TRP   A 1  407 ? -27.155 -59.376  41.451  1.00 39.77  ? 407 TRP   A CZ2    1 
ATOM   3170  C  CZ3    . TRP   A 1  407 ? -29.124 -60.663  40.932  1.00 29.90  ? 407 TRP   A CZ3    1 
ATOM   3171  C  CH2    . TRP   A 1  407 ? -27.970 -59.998  40.535  1.00 35.58  ? 407 TRP   A CH2    1 
ATOM   3172  N  N      . TYR   A 1  408 ? -32.520 -60.409  47.378  1.00 44.25  ? 408 TYR   A N      1 
ATOM   3173  C  CA     . TYR   A 1  408 ? -33.541 -61.184  48.074  1.00 45.44  ? 408 TYR   A CA     1 
ATOM   3174  C  C      . TYR   A 1  408 ? -34.935 -60.644  47.776  1.00 44.94  ? 408 TYR   A C      1 
ATOM   3175  O  O      . TYR   A 1  408 ? -35.820 -61.388  47.318  1.00 42.99  ? 408 TYR   A O      1 
ATOM   3176  C  CB     . TYR   A 1  408 ? -33.258 -61.176  49.587  1.00 46.08  ? 408 TYR   A CB     1 
ATOM   3177  C  CG     . TYR   A 1  408 ? -31.952 -61.849  49.961  1.00 45.32  ? 408 TYR   A CG     1 
ATOM   3178  C  CD1    . TYR   A 1  408 ? -30.739 -61.176  49.842  1.00 40.16  ? 408 TYR   A CD1    1 
ATOM   3179  C  CD2    . TYR   A 1  408 ? -31.928 -63.166  50.373  1.00 43.25  ? 408 TYR   A CD2    1 
ATOM   3180  C  CE1    . TYR   A 1  408 ? -29.552 -61.781  50.159  1.00 34.39  ? 408 TYR   A CE1    1 
ATOM   3181  C  CE2    . TYR   A 1  408 ? -30.744 -63.783  50.680  1.00 45.08  ? 408 TYR   A CE2    1 
ATOM   3182  C  CZ     . TYR   A 1  408 ? -29.556 -63.082  50.574  1.00 42.41  ? 408 TYR   A CZ     1 
ATOM   3183  O  OH     . TYR   A 1  408 ? -28.362 -63.696  50.892  1.00 45.64  ? 408 TYR   A OH     1 
ATOM   3184  N  N      . VAL   A 1  409 ? -35.136 -59.346  48.033  1.00 41.48  ? 409 VAL   A N      1 
ATOM   3185  C  CA     . VAL   A 1  409 ? -36.401 -58.690  47.715  1.00 40.91  ? 409 VAL   A CA     1 
ATOM   3186  C  C      . VAL   A 1  409 ? -36.848 -59.038  46.304  1.00 47.10  ? 409 VAL   A C      1 
ATOM   3187  O  O      . VAL   A 1  409 ? -38.005 -59.408  46.062  1.00 47.08  ? 409 VAL   A O      1 
ATOM   3188  C  CB     . VAL   A 1  409 ? -36.261 -57.177  47.885  1.00 34.17  ? 409 VAL   A CB     1 
ATOM   3189  C  CG1    . VAL   A 1  409 ? -37.479 -56.551  47.387  1.00 38.92  ? 409 VAL   A CG1    1 
ATOM   3190  C  CG2    . VAL   A 1  409 ? -36.052 -56.840  49.347  1.00 39.66  ? 409 VAL   A CG2    1 
ATOM   3191  N  N      . GLY   A 1  410 ? -35.929 -58.921  45.350  1.00 43.01  ? 410 GLY   A N      1 
ATOM   3192  C  CA     . GLY   A 1  410 ? -36.209 -59.221  43.964  1.00 42.30  ? 410 GLY   A CA     1 
ATOM   3193  C  C      . GLY   A 1  410 ? -36.750 -60.604  43.717  1.00 46.57  ? 410 GLY   A C      1 
ATOM   3194  O  O      . GLY   A 1  410 ? -37.273 -60.856  42.626  1.00 55.55  ? 410 GLY   A O      1 
ATOM   3195  N  N      . GLU   A 1  411 ? -36.632 -61.509  44.679  1.00 48.55  ? 411 GLU   A N      1 
ATOM   3196  C  CA     . GLU   A 1  411 ? -37.210 -62.835  44.532  1.00 49.35  ? 411 GLU   A CA     1 
ATOM   3197  C  C      . GLU   A 1  411 ? -38.592 -62.940  45.154  1.00 50.41  ? 411 GLU   A C      1 
ATOM   3198  O  O      . GLU   A 1  411 ? -39.167 -64.027  45.149  1.00 50.82  ? 411 GLU   A O      1 
ATOM   3199  C  CB     . GLU   A 1  411 ? -36.292 -63.886  45.150  1.00 46.04  ? 411 GLU   A CB     1 
ATOM   3200  C  CG     . GLU   A 1  411 ? -34.948 -64.066  44.459  1.00 46.78  ? 411 GLU   A CG     1 
ATOM   3201  C  CD     . GLU   A 1  411 ? -35.079 -64.694  43.082  1.00 51.44  ? 411 GLU   A CD     1 
ATOM   3202  O  OE1    . GLU   A 1  411 ? -36.213 -65.070  42.724  1.00 50.23  ? 411 GLU   A OE1    1 
ATOM   3203  O  OE2    . GLU   A 1  411 ? -34.043 -64.883  42.390  1.00 53.37  ? 411 GLU   A OE2    1 
ATOM   3204  N  N      . GLY   A 1  412 ? -39.136 -61.848  45.690  1.00 46.48  ? 412 GLY   A N      1 
ATOM   3205  C  CA     . GLY   A 1  412 ? -40.424 -61.872  46.350  1.00 46.19  ? 412 GLY   A CA     1 
ATOM   3206  C  C      . GLY   A 1  412 ? -40.361 -61.683  47.848  1.00 55.33  ? 412 GLY   A C      1 
ATOM   3207  O  O      . GLY   A 1  412 ? -41.415 -61.645  48.496  1.00 58.70  ? 412 GLY   A O      1 
ATOM   3208  N  N      . MET   A 1  413 ? -39.166 -61.564  48.426  1.00 57.88  ? 413 MET   A N      1 
ATOM   3209  C  CA     . MET   A 1  413 ? -39.034 -61.413  49.863  1.00 49.94  ? 413 MET   A CA     1 
ATOM   3210  C  C      . MET   A 1  413 ? -39.310 -59.960  50.244  1.00 54.42  ? 413 MET   A C      1 
ATOM   3211  O  O      . MET   A 1  413 ? -39.553 -59.098  49.386  1.00 56.28  ? 413 MET   A O      1 
ATOM   3212  C  CB     . MET   A 1  413 ? -37.647 -61.854  50.315  1.00 48.49  ? 413 MET   A CB     1 
ATOM   3213  C  CG     . MET   A 1  413 ? -37.702 -62.889  51.436  1.00 59.68  ? 413 MET   A CG     1 
ATOM   3214  S  SD     . MET   A 1  413 ? -36.113 -63.357  52.142  1.00 54.12  ? 413 MET   A SD     1 
ATOM   3215  C  CE     . MET   A 1  413 ? -35.763 -61.865  53.042  1.00 40.52  ? 413 MET   A CE     1 
ATOM   3216  N  N      . GLU   A 1  414 ? -39.279 -59.673  51.544  1.00 48.09  ? 414 GLU   A N      1 
ATOM   3217  C  CA     . GLU   A 1  414 ? -39.611 -58.339  52.019  1.00 44.49  ? 414 GLU   A CA     1 
ATOM   3218  C  C      . GLU   A 1  414 ? -38.567 -57.902  53.019  1.00 42.43  ? 414 GLU   A C      1 
ATOM   3219  O  O      . GLU   A 1  414 ? -38.298 -58.622  53.979  1.00 44.93  ? 414 GLU   A O      1 
ATOM   3220  C  CB     . GLU   A 1  414 ? -40.995 -58.281  52.679  1.00 51.86  ? 414 GLU   A CB     1 
ATOM   3221  C  CG     . GLU   A 1  414 ? -42.148 -58.874  51.850  1.00 64.30  ? 414 GLU   A CG     1 
ATOM   3222  C  CD     . GLU   A 1  414 ? -43.507 -58.630  52.487  1.00 69.20  ? 414 GLU   A CD     1 
ATOM   3223  O  OE1    . GLU   A 1  414 ? -43.861 -57.444  52.652  1.00 75.92  ? 414 GLU   A OE1    1 
ATOM   3224  O  OE2    . GLU   A 1  414 ? -44.209 -59.604  52.842  1.00 70.08  ? 414 GLU   A OE2    1 
ATOM   3225  N  N      . GLU   A 1  415 ? -38.035 -56.698  52.840  1.00 43.76  ? 415 GLU   A N      1 
ATOM   3226  C  CA     . GLU   A 1  415 ? -36.946 -56.219  53.683  1.00 45.49  ? 415 GLU   A CA     1 
ATOM   3227  C  C      . GLU   A 1  415 ? -37.246 -56.468  55.162  1.00 46.19  ? 415 GLU   A C      1 
ATOM   3228  O  O      . GLU   A 1  415 ? -36.347 -56.384  56.000  1.00 54.53  ? 415 GLU   A O      1 
ATOM   3229  C  CB     . GLU   A 1  415 ? -36.669 -54.726  53.412  1.00 40.78  ? 415 GLU   A CB     1 
ATOM   3230  C  CG     . GLU   A 1  415 ? -35.282 -54.248  53.841  1.00 38.70  ? 415 GLU   A CG     1 
ATOM   3231  C  CD     . GLU   A 1  415 ? -34.973 -52.778  53.502  1.00 55.31  ? 415 GLU   A CD     1 
ATOM   3232  O  OE1    . GLU   A 1  415 ? -34.492 -52.497  52.363  1.00 57.18  ? 415 GLU   A OE1    1 
ATOM   3233  O  OE2    . GLU   A 1  415 ? -35.158 -51.903  54.391  1.00 56.92  ? 415 GLU   A OE2    1 
ATOM   3234  N  N      . GLY   A 1  416 ? -38.483 -56.814  55.499  1.00 45.29  ? 416 GLY   A N      1 
ATOM   3235  C  CA     . GLY   A 1  416 ? -38.869 -56.985  56.890  1.00 47.38  ? 416 GLY   A CA     1 
ATOM   3236  C  C      . GLY   A 1  416 ? -38.544 -58.343  57.468  1.00 47.53  ? 416 GLY   A C      1 
ATOM   3237  O  O      . GLY   A 1  416 ? -38.104 -58.442  58.619  1.00 48.81  ? 416 GLY   A O      1 
ATOM   3238  N  N      . GLU   A 1  417 ? -38.756 -59.404  56.683  1.00 43.30  ? 417 GLU   A N      1 
ATOM   3239  C  CA     . GLU   A 1  417 ? -38.240 -60.706  57.085  1.00 46.52  ? 417 GLU   A CA     1 
ATOM   3240  C  C      . GLU   A 1  417 ? -36.760 -60.636  57.462  1.00 50.77  ? 417 GLU   A C      1 
ATOM   3241  O  O      . GLU   A 1  417 ? -36.287 -61.470  58.236  1.00 56.04  ? 417 GLU   A O      1 
ATOM   3242  C  CB     . GLU   A 1  417 ? -38.447 -61.733  55.972  1.00 40.08  ? 417 GLU   A CB     1 
ATOM   3243  C  CG     . GLU   A 1  417 ? -38.014 -63.149  56.365  1.00 44.79  ? 417 GLU   A CG     1 
ATOM   3244  C  CD     . GLU   A 1  417 ? -38.455 -64.202  55.346  1.00 50.40  ? 417 GLU   A CD     1 
ATOM   3245  O  OE1    . GLU   A 1  417 ? -39.028 -63.804  54.288  1.00 41.41  ? 417 GLU   A OE1    1 
ATOM   3246  O  OE2    . GLU   A 1  417 ? -38.253 -65.420  55.626  1.00 44.09  ? 417 GLU   A OE2    1 
ATOM   3247  N  N      . PHE   A 1  418 ? -36.010 -59.668  56.934  1.00 48.53  ? 418 PHE   A N      1 
ATOM   3248  C  CA     . PHE   A 1  418 ? -34.635 -59.490  57.382  1.00 51.01  ? 418 PHE   A CA     1 
ATOM   3249  C  C      . PHE   A 1  418 ? -34.581 -59.093  58.856  1.00 54.20  ? 418 PHE   A C      1 
ATOM   3250  O  O      . PHE   A 1  418 ? -33.898 -59.743  59.659  1.00 52.33  ? 418 PHE   A O      1 
ATOM   3251  C  CB     . PHE   A 1  418 ? -33.913 -58.453  56.511  1.00 52.43  ? 418 PHE   A CB     1 
ATOM   3252  C  CG     . PHE   A 1  418 ? -33.268 -59.036  55.279  1.00 54.71  ? 418 PHE   A CG     1 
ATOM   3253  C  CD1    . PHE   A 1  418 ? -34.004 -59.251  54.111  1.00 53.77  ? 418 PHE   A CD1    1 
ATOM   3254  C  CD2    . PHE   A 1  418 ? -31.928 -59.408  55.299  1.00 45.76  ? 418 PHE   A CD2    1 
ATOM   3255  C  CE1    . PHE   A 1  418 ? -33.396 -59.805  52.960  1.00 48.93  ? 418 PHE   A CE1    1 
ATOM   3256  C  CE2    . PHE   A 1  418 ? -31.320 -59.964  54.163  1.00 46.89  ? 418 PHE   A CE2    1 
ATOM   3257  C  CZ     . PHE   A 1  418 ? -32.061 -60.167  52.990  1.00 45.83  ? 418 PHE   A CZ     1 
ATOM   3258  N  N      . SER   A 1  419 ? -35.283 -58.019  59.237  1.00 51.94  ? 419 SER   A N      1 
ATOM   3259  C  CA     . SER   A 1  419 ? -35.226 -57.581  60.629  1.00 52.73  ? 419 SER   A CA     1 
ATOM   3260  C  C      . SER   A 1  419 ? -36.030 -58.493  61.536  1.00 55.79  ? 419 SER   A C      1 
ATOM   3261  O  O      . SER   A 1  419 ? -35.851 -58.465  62.756  1.00 56.08  ? 419 SER   A O      1 
ATOM   3262  C  CB     . SER   A 1  419 ? -35.744 -56.159  60.757  1.00 49.51  ? 419 SER   A CB     1 
ATOM   3263  O  OG     . SER   A 1  419 ? -36.944 -56.053  60.029  1.00 61.11  ? 419 SER   A OG     1 
ATOM   3264  N  N      . GLU   A 1  420 ? -36.915 -59.297  60.965  1.00 52.74  ? 420 GLU   A N      1 
ATOM   3265  C  CA     . GLU   A 1  420 ? -37.709 -60.185  61.788  1.00 54.21  ? 420 GLU   A CA     1 
ATOM   3266  C  C      . GLU   A 1  420 ? -36.915 -61.431  62.151  1.00 57.91  ? 420 GLU   A C      1 
ATOM   3267  O  O      . GLU   A 1  420 ? -36.883 -61.829  63.326  1.00 61.38  ? 420 GLU   A O      1 
ATOM   3268  C  CB     . GLU   A 1  420 ? -39.005 -60.506  61.050  1.00 51.47  ? 420 GLU   A CB     1 
ATOM   3269  C  CG     . GLU   A 1  420 ? -39.828 -61.618  61.619  1.00 64.01  ? 420 GLU   A CG     1 
ATOM   3270  C  CD     . GLU   A 1  420 ? -40.938 -61.980  60.676  1.00 68.89  ? 420 GLU   A CD     1 
ATOM   3271  O  OE1    . GLU   A 1  420 ? -41.627 -61.025  60.237  1.00 65.86  ? 420 GLU   A OE1    1 
ATOM   3272  O  OE2    . GLU   A 1  420 ? -41.087 -63.189  60.351  1.00 66.57  ? 420 GLU   A OE2    1 
ATOM   3273  N  N      . ALA   A 1  421 ? -36.230 -62.031  61.169  1.00 51.75  ? 421 ALA   A N      1 
ATOM   3274  C  CA     . ALA   A 1  421 ? -35.368 -63.167  61.465  1.00 49.68  ? 421 ALA   A CA     1 
ATOM   3275  C  C      . ALA   A 1  421 ? -34.201 -62.764  62.362  1.00 51.64  ? 421 ALA   A C      1 
ATOM   3276  O  O      . ALA   A 1  421 ? -33.692 -63.594  63.124  1.00 49.17  ? 421 ALA   A O      1 
ATOM   3277  C  CB     . ALA   A 1  421 ? -34.859 -63.799  60.170  1.00 49.67  ? 421 ALA   A CB     1 
ATOM   3278  N  N      . ARG   A 1  422 ? -33.769 -61.501  62.304  1.00 49.76  ? 422 ARG   A N      1 
ATOM   3279  C  CA     . ARG   A 1  422 ? -32.669 -61.051  63.155  1.00 44.54  ? 422 ARG   A CA     1 
ATOM   3280  C  C      . ARG   A 1  422 ? -33.127 -60.700  64.572  1.00 50.65  ? 422 ARG   A C      1 
ATOM   3281  O  O      . ARG   A 1  422 ? -32.347 -60.841  65.525  1.00 52.20  ? 422 ARG   A O      1 
ATOM   3282  C  CB     . ARG   A 1  422 ? -31.971 -59.863  62.506  1.00 39.45  ? 422 ARG   A CB     1 
ATOM   3283  C  CG     . ARG   A 1  422 ? -30.969 -59.199  63.377  1.00 33.97  ? 422 ARG   A CG     1 
ATOM   3284  C  CD     . ARG   A 1  422 ? -29.683 -59.989  63.382  1.00 38.45  ? 422 ARG   A CD     1 
ATOM   3285  N  NE     . ARG   A 1  422 ? -28.643 -59.264  64.094  1.00 40.96  ? 422 ARG   A NE     1 
ATOM   3286  C  CZ     . ARG   A 1  422 ? -28.390 -59.399  65.392  1.00 44.53  ? 422 ARG   A CZ     1 
ATOM   3287  N  NH1    . ARG   A 1  422 ? -29.096 -60.217  66.164  1.00 43.27  ? 422 ARG   A NH1    1 
ATOM   3288  N  NH2    . ARG   A 1  422 ? -27.423 -58.672  65.939  1.00 43.22  ? 422 ARG   A NH2    1 
ATOM   3289  N  N      . GLU   A 1  423 ? -34.363 -60.229  64.745  1.00 53.21  ? 423 GLU   A N      1 
ATOM   3290  C  CA     . GLU   A 1  423 ? -34.885 -60.052  66.097  1.00 58.95  ? 423 GLU   A CA     1 
ATOM   3291  C  C      . GLU   A 1  423 ? -34.972 -61.388  66.816  1.00 54.87  ? 423 GLU   A C      1 
ATOM   3292  O  O      . GLU   A 1  423 ? -34.620 -61.498  68.001  1.00 49.31  ? 423 GLU   A O      1 
ATOM   3293  C  CB     . GLU   A 1  423 ? -36.258 -59.387  66.045  1.00 68.93  ? 423 GLU   A CB     1 
ATOM   3294  C  CG     . GLU   A 1  423 ? -36.292 -57.860  66.101  1.00 73.92  ? 423 GLU   A CG     1 
ATOM   3295  C  CD     . GLU   A 1  423 ? -37.656 -57.313  65.641  1.00 89.71  ? 423 GLU   A CD     1 
ATOM   3296  O  OE1    . GLU   A 1  423 ? -38.699 -57.875  66.048  1.00 92.35  ? 423 GLU   A OE1    1 
ATOM   3297  O  OE2    . GLU   A 1  423 ? -37.686 -56.314  64.886  1.00 91.38  ? 423 GLU   A OE2    1 
ATOM   3298  N  N      . ASP   A 1  424 ? -35.453 -62.409  66.112  1.00 49.81  ? 424 ASP   A N      1 
ATOM   3299  C  CA     . ASP   A 1  424 ? -35.496 -63.746  66.680  1.00 49.50  ? 424 ASP   A CA     1 
ATOM   3300  C  C      . ASP   A 1  424 ? -34.126 -64.121  67.231  1.00 52.75  ? 424 ASP   A C      1 
ATOM   3301  O  O      . ASP   A 1  424 ? -33.970 -64.414  68.423  1.00 55.20  ? 424 ASP   A O      1 
ATOM   3302  C  CB     . ASP   A 1  424 ? -35.961 -64.730  65.606  1.00 45.64  ? 424 ASP   A CB     1 
ATOM   3303  C  CG     . ASP   A 1  424 ? -36.539 -65.970  66.189  1.00 44.30  ? 424 ASP   A CG     1 
ATOM   3304  O  OD1    . ASP   A 1  424 ? -36.568 -66.008  67.431  1.00 52.59  ? 424 ASP   A OD1    1 
ATOM   3305  O  OD2    . ASP   A 1  424 ? -36.991 -66.874  65.436  1.00 46.10  ? 424 ASP   A OD2    1 
ATOM   3306  N  N      . MET   A 1  425 ? -33.111 -64.078  66.364  1.00 49.49  ? 425 MET   A N      1 
ATOM   3307  C  CA     . MET   A 1  425 ? -31.729 -64.246  66.787  1.00 47.29  ? 425 MET   A CA     1 
ATOM   3308  C  C      . MET   A 1  425 ? -31.447 -63.434  68.043  1.00 47.12  ? 425 MET   A C      1 
ATOM   3309  O  O      . MET   A 1  425 ? -30.944 -63.960  69.034  1.00 45.37  ? 425 MET   A O      1 
ATOM   3310  C  CB     . MET   A 1  425 ? -30.797 -63.817  65.651  1.00 44.99  ? 425 MET   A CB     1 
ATOM   3311  C  CG     . MET   A 1  425 ? -30.958 -64.669  64.414  1.00 44.95  ? 425 MET   A CG     1 
ATOM   3312  S  SD     . MET   A 1  425 ? -30.873 -66.437  64.719  1.00 47.00  ? 425 MET   A SD     1 
ATOM   3313  C  CE     . MET   A 1  425 ? -29.225 -66.513  65.405  1.00 47.43  ? 425 MET   A CE     1 
ATOM   3314  N  N      . ALA   A 1  426 ? -31.763 -62.136  68.015  1.00 50.94  ? 426 ALA   A N      1 
ATOM   3315  C  CA     . ALA   A 1  426 ? -31.488 -61.293  69.177  1.00 51.37  ? 426 ALA   A CA     1 
ATOM   3316  C  C      . ALA   A 1  426 ? -32.157 -61.832  70.434  1.00 52.98  ? 426 ALA   A C      1 
ATOM   3317  O  O      . ALA   A 1  426 ? -31.613 -61.691  71.537  1.00 52.57  ? 426 ALA   A O      1 
ATOM   3318  C  CB     . ALA   A 1  426 ? -31.941 -59.867  68.906  1.00 42.63  ? 426 ALA   A CB     1 
ATOM   3319  N  N      . ALA   A 1  427 ? -33.338 -62.436  70.292  1.00 50.37  ? 427 ALA   A N      1 
ATOM   3320  C  CA     . ALA   A 1  427 ? -33.919 -63.204  71.385  1.00 48.87  ? 427 ALA   A CA     1 
ATOM   3321  C  C      . ALA   A 1  427 ? -32.998 -64.334  71.784  1.00 52.78  ? 427 ALA   A C      1 
ATOM   3322  O  O      . ALA   A 1  427 ? -32.436 -64.345  72.883  1.00 53.04  ? 427 ALA   A O      1 
ATOM   3323  C  CB     . ALA   A 1  427 ? -35.268 -63.779  70.967  1.00 54.59  ? 427 ALA   A CB     1 
ATOM   3324  N  N      . LEU   A 1  428 ? -32.842 -65.302  70.880  1.00 51.60  ? 428 LEU   A N      1 
ATOM   3325  C  CA     . LEU   A 1  428 ? -31.998 -66.463  71.109  1.00 47.17  ? 428 LEU   A CA     1 
ATOM   3326  C  C      . LEU   A 1  428 ? -30.715 -66.106  71.858  1.00 48.73  ? 428 LEU   A C      1 
ATOM   3327  O  O      . LEU   A 1  428 ? -30.356 -66.775  72.827  1.00 55.85  ? 428 LEU   A O      1 
ATOM   3328  C  CB     . LEU   A 1  428 ? -31.688 -67.124  69.767  1.00 39.77  ? 428 LEU   A CB     1 
ATOM   3329  C  CG     . LEU   A 1  428 ? -31.119 -68.508  69.934  1.00 38.05  ? 428 LEU   A CG     1 
ATOM   3330  C  CD1    . LEU   A 1  428 ? -32.161 -69.251  70.711  1.00 49.83  ? 428 LEU   A CD1    1 
ATOM   3331  C  CD2    . LEU   A 1  428 ? -30.903 -69.167  68.608  1.00 39.72  ? 428 LEU   A CD2    1 
ATOM   3332  N  N      . GLU   A 1  429 ? -30.007 -65.048  71.441  1.00 47.36  ? 429 GLU   A N      1 
ATOM   3333  C  CA     . GLU   A 1  429 ? -28.780 -64.681  72.149  1.00 49.66  ? 429 GLU   A CA     1 
ATOM   3334  C  C      . GLU   A 1  429 ? -29.061 -64.242  73.575  1.00 55.42  ? 429 GLU   A C      1 
ATOM   3335  O  O      . GLU   A 1  429 ? -28.200 -64.393  74.448  1.00 61.56  ? 429 GLU   A O      1 
ATOM   3336  C  CB     . GLU   A 1  429 ? -28.008 -63.563  71.435  1.00 49.78  ? 429 GLU   A CB     1 
ATOM   3337  C  CG     . GLU   A 1  429 ? -27.150 -64.001  70.270  1.00 49.81  ? 429 GLU   A CG     1 
ATOM   3338  C  CD     . GLU   A 1  429 ? -26.108 -62.952  69.886  1.00 60.71  ? 429 GLU   A CD     1 
ATOM   3339  O  OE1    . GLU   A 1  429 ? -25.224 -62.640  70.733  1.00 50.67  ? 429 GLU   A OE1    1 
ATOM   3340  O  OE2    . GLU   A 1  429 ? -26.169 -62.451  68.732  1.00 60.69  ? 429 GLU   A OE2    1 
ATOM   3341  N  N      . LYS   A 1  430 ? -30.238 -63.680  73.825  1.00 56.56  ? 430 LYS   A N      1 
ATOM   3342  C  CA     . LYS   A 1  430 ? -30.607 -63.275  75.174  1.00 60.71  ? 430 LYS   A CA     1 
ATOM   3343  C  C      . LYS   A 1  430 ? -30.977 -64.487  76.022  1.00 56.84  ? 430 LYS   A C      1 
ATOM   3344  O  O      . LYS   A 1  430 ? -30.476 -64.643  77.139  1.00 59.33  ? 430 LYS   A O      1 
ATOM   3345  C  CB     . LYS   A 1  430 ? -31.748 -62.256  75.082  1.00 64.42  ? 430 LYS   A CB     1 
ATOM   3346  C  CG     . LYS   A 1  430 ? -32.248 -61.613  76.362  1.00 69.97  ? 430 LYS   A CG     1 
ATOM   3347  C  CD     . LYS   A 1  430 ? -32.873 -60.268  75.991  1.00 77.71  ? 430 LYS   A CD     1 
ATOM   3348  C  CE     . LYS   A 1  430 ? -33.334 -59.460  77.195  1.00 76.97  ? 430 LYS   A CE     1 
ATOM   3349  N  NZ     . LYS   A 1  430 ? -34.454 -60.186  77.849  1.00 72.59  ? 430 LYS   A NZ     1 
ATOM   3350  N  N      . ASP   A 1  431 ? -31.833 -65.366  75.493  1.00 51.49  ? 431 ASP   A N      1 
ATOM   3351  C  CA     . ASP   A 1  431 ? -32.116 -66.631  76.158  1.00 52.64  ? 431 ASP   A CA     1 
ATOM   3352  C  C      . ASP   A 1  431 ? -30.826 -67.283  76.623  1.00 56.51  ? 431 ASP   A C      1 
ATOM   3353  O  O      . ASP   A 1  431 ? -30.654 -67.586  77.809  1.00 59.26  ? 431 ASP   A O      1 
ATOM   3354  C  CB     . ASP   A 1  431 ? -32.859 -67.570  75.210  1.00 51.01  ? 431 ASP   A CB     1 
ATOM   3355  C  CG     . ASP   A 1  431 ? -34.168 -66.986  74.705  1.00 60.82  ? 431 ASP   A CG     1 
ATOM   3356  O  OD1    . ASP   A 1  431 ? -34.703 -66.062  75.347  1.00 67.67  ? 431 ASP   A OD1    1 
ATOM   3357  O  OD2    . ASP   A 1  431 ? -34.684 -67.476  73.673  1.00 58.24  ? 431 ASP   A OD2    1 
ATOM   3358  N  N      . TYR   A 1  432 ? -29.899 -67.504  75.690  1.00 54.28  ? 432 TYR   A N      1 
ATOM   3359  C  CA     . TYR   A 1  432 ? -28.625 -68.110  76.055  1.00 55.37  ? 432 TYR   A CA     1 
ATOM   3360  C  C      . TYR   A 1  432 ? -27.998 -67.388  77.241  1.00 56.18  ? 432 TYR   A C      1 
ATOM   3361  O  O      . TYR   A 1  432 ? -27.536 -68.023  78.190  1.00 62.42  ? 432 TYR   A O      1 
ATOM   3362  C  CB     . TYR   A 1  432 ? -27.660 -68.106  74.870  1.00 51.02  ? 432 TYR   A CB     1 
ATOM   3363  C  CG     . TYR   A 1  432 ? -27.749 -69.344  74.007  1.00 52.99  ? 432 TYR   A CG     1 
ATOM   3364  C  CD1    . TYR   A 1  432 ? -27.084 -70.510  74.359  1.00 44.72  ? 432 TYR   A CD1    1 
ATOM   3365  C  CD2    . TYR   A 1  432 ? -28.447 -69.320  72.791  1.00 52.88  ? 432 TYR   A CD2    1 
ATOM   3366  C  CE1    . TYR   A 1  432 ? -27.161 -71.636  73.558  1.00 47.98  ? 432 TYR   A CE1    1 
ATOM   3367  C  CE2    . TYR   A 1  432 ? -28.514 -70.429  71.967  1.00 44.87  ? 432 TYR   A CE2    1 
ATOM   3368  C  CZ     . TYR   A 1  432 ? -27.876 -71.596  72.349  1.00 51.70  ? 432 TYR   A CZ     1 
ATOM   3369  O  OH     . TYR   A 1  432 ? -27.942 -72.725  71.519  1.00 49.52  ? 432 TYR   A OH     1 
ATOM   3370  N  N      . GLU   A 1  433 ? -27.988 -66.059  77.222  1.00 58.92  ? 433 GLU   A N      1 
ATOM   3371  C  CA     . GLU   A 1  433 ? -27.238 -65.352  78.252  1.00 61.14  ? 433 GLU   A CA     1 
ATOM   3372  C  C      . GLU   A 1  433 ? -27.920 -65.429  79.604  1.00 66.81  ? 433 GLU   A C      1 
ATOM   3373  O  O      . GLU   A 1  433 ? -27.239 -65.432  80.643  1.00 72.20  ? 433 GLU   A O      1 
ATOM   3374  C  CB     . GLU   A 1  433 ? -27.015 -63.895  77.875  1.00 65.12  ? 433 GLU   A CB     1 
ATOM   3375  C  CG     . GLU   A 1  433 ? -25.807 -63.342  78.604  1.00 71.02  ? 433 GLU   A CG     1 
ATOM   3376  C  CD     . GLU   A 1  433 ? -25.345 -62.026  78.067  1.00 80.44  ? 433 GLU   A CD     1 
ATOM   3377  O  OE1    . GLU   A 1  433 ? -26.197 -61.268  77.550  1.00 86.08  ? 433 GLU   A OE1    1 
ATOM   3378  O  OE2    . GLU   A 1  433 ? -24.125 -61.763  78.154  1.00 82.34  ? 433 GLU   A OE2    1 
ATOM   3379  N  N      . GLU   A 1  434 ? -29.253 -65.468  79.618  1.00 66.95  ? 434 GLU   A N      1 
ATOM   3380  C  CA     . GLU   A 1  434 ? -29.950 -65.643  80.884  1.00 69.22  ? 434 GLU   A CA     1 
ATOM   3381  C  C      . GLU   A 1  434 ? -29.536 -66.962  81.510  1.00 66.17  ? 434 GLU   A C      1 
ATOM   3382  O  O      . GLU   A 1  434 ? -29.093 -67.006  82.664  1.00 73.90  ? 434 GLU   A O      1 
ATOM   3383  C  CB     . GLU   A 1  434 ? -31.462 -65.577  80.670  1.00 63.82  ? 434 GLU   A CB     1 
ATOM   3384  C  CG     . GLU   A 1  434 ? -31.977 -64.153  80.614  1.00 73.14  ? 434 GLU   A CG     1 
ATOM   3385  C  CD     . GLU   A 1  434 ? -33.407 -64.073  80.113  1.00 92.10  ? 434 GLU   A CD     1 
ATOM   3386  O  OE1    . GLU   A 1  434 ? -34.114 -65.106  80.167  1.00 97.06  ? 434 GLU   A OE1    1 
ATOM   3387  O  OE2    . GLU   A 1  434 ? -33.796 -63.001  79.583  1.00 86.15  ? 434 GLU   A OE2    1 
ATOM   3388  N  N      . VAL   A 1  435 ? -29.603 -68.042  80.725  1.00 57.13  ? 435 VAL   A N      1 
ATOM   3389  C  CA     . VAL   A 1  435 ? -29.286 -69.370  81.228  1.00 55.37  ? 435 VAL   A CA     1 
ATOM   3390  C  C      . VAL   A 1  435 ? -27.824 -69.484  81.653  1.00 62.32  ? 435 VAL   A C      1 
ATOM   3391  O  O      . VAL   A 1  435 ? -27.473 -70.384  82.424  1.00 69.71  ? 435 VAL   A O      1 
ATOM   3392  C  CB     . VAL   A 1  435 ? -29.652 -70.417  80.159  1.00 50.86  ? 435 VAL   A CB     1 
ATOM   3393  C  CG1    . VAL   A 1  435 ? -29.352 -71.816  80.648  1.00 50.07  ? 435 VAL   A CG1    1 
ATOM   3394  C  CG2    . VAL   A 1  435 ? -31.099 -70.283  79.778  1.00 48.46  ? 435 VAL   A CG2    1 
ATOM   3395  N  N      . GLY   A 1  436 ? -26.966 -68.567  81.210  1.00 60.90  ? 436 GLY   A N      1 
ATOM   3396  C  CA     . GLY   A 1  436 ? -25.540 -68.742  81.382  1.00 64.92  ? 436 GLY   A CA     1 
ATOM   3397  C  C      . GLY   A 1  436 ? -24.824 -67.750  82.274  1.00 78.85  ? 436 GLY   A C      1 
ATOM   3398  O  O      . GLY   A 1  436 ? -23.602 -67.594  82.146  1.00 82.40  ? 436 GLY   A O      1 
ATOM   3399  N  N      . VAL   A 1  437 ? -25.532 -67.088  83.189  1.00 84.35  ? 437 VAL   A N      1 
ATOM   3400  C  CA     . VAL   A 1  437 ? -24.846 -66.180  84.114  1.00 86.46  ? 437 VAL   A CA     1 
ATOM   3401  C  C      . VAL   A 1  437 ? -25.382 -66.267  85.547  1.00 83.31  ? 437 VAL   A C      1 
ATOM   3402  O  O      . VAL   A 1  437 ? -24.727 -65.818  86.495  1.00 78.82  ? 437 VAL   A O      1 
ATOM   3403  C  CB     . VAL   A 1  437 ? -24.942 -64.752  83.620  1.00 82.23  ? 437 VAL   A CB     1 
ATOM   3404  C  CG1    . VAL   A 1  437 ? -24.459 -63.788  84.714  1.00 83.11  ? 437 VAL   A CG1    1 
ATOM   3405  C  CG2    . VAL   A 1  437 ? -24.179 -64.614  82.312  1.00 71.24  ? 437 VAL   A CG2    1 
ATOM   3406  N  N      . ARG   B 2  2   ? -26.115 -75.230  31.242  1.00 50.05  ? 2   ARG   B N      1 
ATOM   3407  C  CA     . ARG   B 2  2   ? -26.172 -73.792  31.495  1.00 51.85  ? 2   ARG   B CA     1 
ATOM   3408  C  C      . ARG   B 2  2   ? -25.417 -73.055  30.389  1.00 61.88  ? 2   ARG   B C      1 
ATOM   3409  O  O      . ARG   B 2  2   ? -24.296 -72.559  30.584  1.00 59.76  ? 2   ARG   B O      1 
ATOM   3410  C  CB     . ARG   B 2  2   ? -25.597 -73.443  32.865  1.00 43.38  ? 2   ARG   B CB     1 
ATOM   3411  C  CG     . ARG   B 2  2   ? -26.328 -74.031  34.016  1.00 47.84  ? 2   ARG   B CG     1 
ATOM   3412  C  CD     . ARG   B 2  2   ? -27.608 -73.310  34.386  1.00 48.21  ? 2   ARG   B CD     1 
ATOM   3413  N  NE     . ARG   B 2  2   ? -27.303 -71.939  34.799  1.00 52.67  ? 2   ARG   B NE     1 
ATOM   3414  C  CZ     . ARG   B 2  2   ? -28.192 -70.992  35.095  1.00 51.21  ? 2   ARG   B CZ     1 
ATOM   3415  N  NH1    . ARG   B 2  2   ? -29.493 -71.236  35.106  1.00 51.42  ? 2   ARG   B NH1    1 
ATOM   3416  N  NH2    . ARG   B 2  2   ? -27.763 -69.770  35.405  1.00 51.79  ? 2   ARG   B NH2    1 
ATOM   3417  N  N      . GLU   B 2  3   ? -26.048 -72.976  29.221  1.00 61.68  ? 3   GLU   B N      1 
ATOM   3418  C  CA     . GLU   B 2  3   ? -25.428 -72.335  28.077  1.00 54.23  ? 3   GLU   B CA     1 
ATOM   3419  C  C      . GLU   B 2  3   ? -25.360 -70.823  28.272  1.00 56.09  ? 3   GLU   B C      1 
ATOM   3420  O  O      . GLU   B 2  3   ? -26.186 -70.213  28.965  1.00 50.88  ? 3   GLU   B O      1 
ATOM   3421  C  CB     . GLU   B 2  3   ? -26.201 -72.684  26.815  1.00 51.98  ? 3   GLU   B CB     1 
ATOM   3422  C  CG     . GLU   B 2  3   ? -26.210 -74.189  26.551  1.00 63.38  ? 3   GLU   B CG     1 
ATOM   3423  C  CD     . GLU   B 2  3   ? -27.334 -74.930  27.281  1.00 66.70  ? 3   GLU   B CD     1 
ATOM   3424  O  OE1    . GLU   B 2  3   ? -27.991 -74.329  28.162  1.00 63.36  ? 3   GLU   B OE1    1 
ATOM   3425  O  OE2    . GLU   B 2  3   ? -27.556 -76.120  26.968  1.00 63.77  ? 3   GLU   B OE2    1 
ATOM   3426  N  N      . ILE   B 2  4   ? -24.318 -70.232  27.696  1.00 53.92  ? 4   ILE   B N      1 
ATOM   3427  C  CA     . ILE   B 2  4   ? -24.161 -68.789  27.602  1.00 49.13  ? 4   ILE   B CA     1 
ATOM   3428  C  C      . ILE   B 2  4   ? -24.303 -68.434  26.141  1.00 47.14  ? 4   ILE   B C      1 
ATOM   3429  O  O      . ILE   B 2  4   ? -23.860 -69.201  25.282  1.00 51.01  ? 4   ILE   B O      1 
ATOM   3430  C  CB     . ILE   B 2  4   ? -22.804 -68.313  28.155  1.00 46.57  ? 4   ILE   B CB     1 
ATOM   3431  C  CG1    . ILE   B 2  4   ? -22.719 -68.587  29.654  1.00 44.94  ? 4   ILE   B CG1    1 
ATOM   3432  C  CG2    . ILE   B 2  4   ? -22.566 -66.855  27.816  1.00 48.62  ? 4   ILE   B CG2    1 
ATOM   3433  C  CD1    . ILE   B 2  4   ? -21.442 -68.153  30.292  1.00 39.41  ? 4   ILE   B CD1    1 
ATOM   3434  N  N      . VAL   B 2  5   ? -24.955 -67.307  25.851  1.00 48.73  ? 5   VAL   B N      1 
ATOM   3435  C  CA     . VAL   B 2  5   ? -25.119 -66.846  24.471  1.00 52.55  ? 5   VAL   B CA     1 
ATOM   3436  C  C      . VAL   B 2  5   ? -24.311 -65.565  24.285  1.00 51.68  ? 5   VAL   B C      1 
ATOM   3437  O  O      . VAL   B 2  5   ? -24.525 -64.556  24.979  1.00 46.11  ? 5   VAL   B O      1 
ATOM   3438  C  CB     . VAL   B 2  5   ? -26.591 -66.654  24.080  1.00 47.07  ? 5   VAL   B CB     1 
ATOM   3439  C  CG1    . VAL   B 2  5   ? -26.668 -66.139  22.675  1.00 38.26  ? 5   VAL   B CG1    1 
ATOM   3440  C  CG2    . VAL   B 2  5   ? -27.347 -67.975  24.189  1.00 48.05  ? 5   VAL   B CG2    1 
ATOM   3441  N  N      . HIS   B 2  6   ? -23.377 -65.628  23.342  1.00 47.49  ? 6   HIS   B N      1 
ATOM   3442  C  CA     . HIS   B 2  6   ? -22.400 -64.588  23.087  1.00 41.98  ? 6   HIS   B CA     1 
ATOM   3443  C  C      . HIS   B 2  6   ? -22.822 -63.738  21.898  1.00 46.99  ? 6   HIS   B C      1 
ATOM   3444  O  O      . HIS   B 2  6   ? -23.282 -64.254  20.870  1.00 46.08  ? 6   HIS   B O      1 
ATOM   3445  C  CB     . HIS   B 2  6   ? -21.038 -65.218  22.816  1.00 44.71  ? 6   HIS   B CB     1 
ATOM   3446  C  CG     . HIS   B 2  6   ? -20.002 -64.248  22.349  1.00 45.28  ? 6   HIS   B CG     1 
ATOM   3447  N  ND1    . HIS   B 2  6   ? -19.245 -63.485  23.215  1.00 42.70  ? 6   HIS   B ND1    1 
ATOM   3448  C  CD2    . HIS   B 2  6   ? -19.593 -63.928  21.096  1.00 39.77  ? 6   HIS   B CD2    1 
ATOM   3449  C  CE1    . HIS   B 2  6   ? -18.422 -62.730  22.508  1.00 48.01  ? 6   HIS   B CE1    1 
ATOM   3450  N  NE2    . HIS   B 2  6   ? -18.619 -62.975  21.221  1.00 41.96  ? 6   HIS   B NE2    1 
ATOM   3451  N  N      . ILE   B 2  7   ? -22.615 -62.436  22.032  1.00 41.45  ? 7   ILE   B N      1 
ATOM   3452  C  CA     . ILE   B 2  7   ? -23.053 -61.460  21.051  1.00 36.91  ? 7   ILE   B CA     1 
ATOM   3453  C  C      . ILE   B 2  7   ? -21.924 -60.457  20.905  1.00 39.94  ? 7   ILE   B C      1 
ATOM   3454  O  O      . ILE   B 2  7   ? -21.453 -59.909  21.906  1.00 43.92  ? 7   ILE   B O      1 
ATOM   3455  C  CB     . ILE   B 2  7   ? -24.346 -60.780  21.536  1.00 41.25  ? 7   ILE   B CB     1 
ATOM   3456  C  CG1    . ILE   B 2  7   ? -25.382 -61.839  21.907  1.00 38.61  ? 7   ILE   B CG1    1 
ATOM   3457  C  CG2    . ILE   B 2  7   ? -24.889 -59.809  20.524  1.00 36.50  ? 7   ILE   B CG2    1 
ATOM   3458  C  CD1    . ILE   B 2  7   ? -26.697 -61.261  22.269  1.00 36.18  ? 7   ILE   B CD1    1 
ATOM   3459  N  N      . GLN   B 2  8   ? -21.468 -60.229  19.681  1.00 37.65  ? 8   GLN   B N      1 
ATOM   3460  C  CA     . GLN   B 2  8   ? -20.427 -59.237  19.446  1.00 39.26  ? 8   GLN   B CA     1 
ATOM   3461  C  C      . GLN   B 2  8   ? -20.916 -58.278  18.370  1.00 39.36  ? 8   GLN   B C      1 
ATOM   3462  O  O      . GLN   B 2  8   ? -21.359 -58.717  17.308  1.00 38.91  ? 8   GLN   B O      1 
ATOM   3463  C  CB     . GLN   B 2  8   ? -19.122 -59.903  19.034  1.00 37.61  ? 8   GLN   B CB     1 
ATOM   3464  C  CG     . GLN   B 2  8   ? -19.240 -60.808  17.821  1.00 41.42  ? 8   GLN   B CG     1 
ATOM   3465  C  CD     . GLN   B 2  8   ? -18.015 -61.696  17.652  1.00 46.53  ? 8   GLN   B CD     1 
ATOM   3466  O  OE1    . GLN   B 2  8   ? -17.622 -62.424  18.577  1.00 46.09  ? 8   GLN   B OE1    1 
ATOM   3467  N  NE2    . GLN   B 2  8   ? -17.352 -61.573  16.508  1.00 45.84  ? 8   GLN   B NE2    1 
ATOM   3468  N  N      . ALA   B 2  9   ? -20.827 -56.975  18.641  1.00 36.62  ? 9   ALA   B N      1 
ATOM   3469  C  CA     . ALA   B 2  9   ? -21.535 -55.965  17.865  1.00 35.97  ? 9   ALA   B CA     1 
ATOM   3470  C  C      . ALA   B 2  9   ? -20.584 -54.842  17.484  1.00 38.65  ? 9   ALA   B C      1 
ATOM   3471  O  O      . ALA   B 2  9   ? -20.040 -54.163  18.365  1.00 43.26  ? 9   ALA   B O      1 
ATOM   3472  C  CB     . ALA   B 2  9   ? -22.719 -55.407  18.660  1.00 33.00  ? 9   ALA   B CB     1 
ATOM   3473  N  N      . GLY   B 2  10  ? -20.387 -54.643  16.182  1.00 31.14  ? 10  GLY   B N      1 
ATOM   3474  C  CA     . GLY   B 2  10  ? -19.579 -53.550  15.688  1.00 33.02  ? 10  GLY   B CA     1 
ATOM   3475  C  C      . GLY   B 2  10  ? -18.097 -53.873  15.555  1.00 35.51  ? 10  GLY   B C      1 
ATOM   3476  O  O      . GLY   B 2  10  ? -17.610 -54.930  15.954  1.00 36.91  ? 10  GLY   B O      1 
ATOM   3477  N  N      . GLN   B 2  11  ? -17.368 -52.913  14.963  1.00 41.37  ? 11  GLN   B N      1 
ATOM   3478  C  CA     . GLN   B 2  11  ? -15.928 -52.992  14.703  1.00 38.18  ? 11  GLN   B CA     1 
ATOM   3479  C  C      . GLN   B 2  11  ? -15.264 -53.559  15.948  1.00 41.18  ? 11  GLN   B C      1 
ATOM   3480  O  O      . GLN   B 2  11  ? -14.815 -54.717  15.950  1.00 40.01  ? 11  GLN   B O      1 
ATOM   3481  C  CB     . GLN   B 2  11  ? -15.360 -51.595  14.352  1.00 42.91  ? 11  GLN   B CB     1 
ATOM   3482  C  CG     . GLN   B 2  11  ? -13.891 -51.474  13.831  1.00 40.13  ? 11  GLN   B CG     1 
ATOM   3483  C  CD     . GLN   B 2  11  ? -13.440 -49.989  13.500  1.00 56.07  ? 11  GLN   B CD     1 
ATOM   3484  O  OE1    . GLN   B 2  11  ? -14.117 -48.961  13.804  1.00 46.08  ? 11  GLN   B OE1    1 
ATOM   3485  N  NE2    . GLN   B 2  11  ? -12.313 -49.903  12.800  1.00 67.47  ? 11  GLN   B NE2    1 
ATOM   3486  N  N      . CYS   B 2  12  ? -15.254 -52.754  17.026  1.00 37.60  ? 12  CYS   B N      1 
ATOM   3487  C  CA     . CYS   B 2  12  ? -14.603 -53.164  18.266  1.00 31.79  ? 12  CYS   B CA     1 
ATOM   3488  C  C      . CYS   B 2  12  ? -15.217 -54.439  18.811  1.00 41.46  ? 12  CYS   B C      1 
ATOM   3489  O  O      . CYS   B 2  12  ? -14.511 -55.415  19.105  1.00 39.73  ? 12  CYS   B O      1 
ATOM   3490  C  CB     . CYS   B 2  12  ? -14.689 -52.070  19.308  1.00 34.68  ? 12  CYS   B CB     1 
ATOM   3491  S  SG     . CYS   B 2  12  ? -13.980 -52.580  20.908  1.00 32.29  ? 12  CYS   B SG     1 
ATOM   3492  N  N      . GLY   B 2  13  ? -16.537 -54.449  18.963  1.00 42.58  ? 13  GLY   B N      1 
ATOM   3493  C  CA     . GLY   B 2  13  ? -17.196 -55.661  19.403  1.00 39.28  ? 13  GLY   B CA     1 
ATOM   3494  C  C      . GLY   B 2  13  ? -16.655 -56.919  18.754  1.00 35.81  ? 13  GLY   B C      1 
ATOM   3495  O  O      . GLY   B 2  13  ? -16.228 -57.825  19.459  1.00 37.47  ? 13  GLY   B O      1 
ATOM   3496  N  N      . ASN   B 2  14  ? -16.657 -56.981  17.419  1.00 38.19  ? 14  ASN   B N      1 
ATOM   3497  C  CA     . ASN   B 2  14  ? -16.364 -58.229  16.713  1.00 40.57  ? 14  ASN   B CA     1 
ATOM   3498  C  C      . ASN   B 2  14  ? -14.889 -58.565  16.742  1.00 44.08  ? 14  ASN   B C      1 
ATOM   3499  O  O      . ASN   B 2  14  ? -14.527 -59.745  16.719  1.00 38.06  ? 14  ASN   B O      1 
ATOM   3500  C  CB     . ASN   B 2  14  ? -16.848 -58.145  15.261  1.00 37.17  ? 14  ASN   B CB     1 
ATOM   3501  C  CG     . ASN   B 2  14  ? -18.318 -58.381  15.141  1.00 39.10  ? 14  ASN   B CG     1 
ATOM   3502  O  OD1    . ASN   B 2  14  ? -18.749 -59.513  15.040  1.00 43.46  ? 14  ASN   B OD1    1 
ATOM   3503  N  ND2    . ASN   B 2  14  ? -19.106 -57.324  15.202  1.00 41.51  ? 14  ASN   B ND2    1 
ATOM   3504  N  N      . GLN   B 2  15  ? -14.029 -57.547  16.797  1.00 46.63  ? 15  GLN   B N      1 
ATOM   3505  C  CA     . GLN   B 2  15  ? -12.599 -57.794  16.885  1.00 43.44  ? 15  GLN   B CA     1 
ATOM   3506  C  C      . GLN   B 2  15  ? -12.215 -58.393  18.238  1.00 38.63  ? 15  GLN   B C      1 
ATOM   3507  O  O      . GLN   B 2  15  ? -11.628 -59.481  18.295  1.00 39.23  ? 15  GLN   B O      1 
ATOM   3508  C  CB     . GLN   B 2  15  ? -11.838 -56.512  16.526  1.00 40.41  ? 15  GLN   B CB     1 
ATOM   3509  C  CG     . GLN   B 2  15  ? -11.363 -56.617  15.056  1.00 52.90  ? 15  GLN   B CG     1 
ATOM   3510  C  CD     . GLN   B 2  15  ? -11.244 -55.302  14.294  1.00 62.82  ? 15  GLN   B CD     1 
ATOM   3511  O  OE1    . GLN   B 2  15  ? -11.352 -54.210  14.859  1.00 58.92  ? 15  GLN   B OE1    1 
ATOM   3512  N  NE2    . GLN   B 2  15  ? -11.010 -55.414  12.981  1.00 62.04  ? 15  GLN   B NE2    1 
ATOM   3513  N  N      . ILE   B 2  16  ? -12.575 -57.756  19.351  1.00 34.94  ? 16  ILE   B N      1 
ATOM   3514  C  CA     . ILE   B 2  16  ? -12.263 -58.453  20.597  1.00 41.56  ? 16  ILE   B CA     1 
ATOM   3515  C  C      . ILE   B 2  16  ? -13.051 -59.751  20.662  1.00 37.20  ? 16  ILE   B C      1 
ATOM   3516  O  O      . ILE   B 2  16  ? -12.506 -60.814  20.973  1.00 40.36  ? 16  ILE   B O      1 
ATOM   3517  C  CB     . ILE   B 2  16  ? -12.474 -57.568  21.843  1.00 37.95  ? 16  ILE   B CB     1 
ATOM   3518  C  CG1    . ILE   B 2  16  ? -13.939 -57.521  22.253  1.00 41.54  ? 16  ILE   B CG1    1 
ATOM   3519  C  CG2    . ILE   B 2  16  ? -11.906 -56.175  21.621  1.00 33.07  ? 16  ILE   B CG2    1 
ATOM   3520  C  CD1    . ILE   B 2  16  ? -14.165 -56.650  23.467  1.00 43.14  ? 16  ILE   B CD1    1 
ATOM   3521  N  N      . GLY   B 2  17  ? -14.317 -59.704  20.310  1.00 39.94  ? 17  GLY   B N      1 
ATOM   3522  C  CA     . GLY   B 2  17  ? -15.083 -60.926  20.178  1.00 40.16  ? 17  GLY   B CA     1 
ATOM   3523  C  C      . GLY   B 2  17  ? -14.319 -62.023  19.473  1.00 41.19  ? 17  GLY   B C      1 
ATOM   3524  O  O      . GLY   B 2  17  ? -14.269 -63.153  19.953  1.00 43.52  ? 17  GLY   B O      1 
ATOM   3525  N  N      . ALA   B 2  18  ? -13.684 -61.706  18.345  1.00 47.69  ? 18  ALA   B N      1 
ATOM   3526  C  CA     . ALA   B 2  18  ? -13.077 -62.770  17.549  1.00 42.85  ? 18  ALA   B CA     1 
ATOM   3527  C  C      . ALA   B 2  18  ? -11.810 -63.311  18.199  1.00 42.38  ? 18  ALA   B C      1 
ATOM   3528  O  O      . ALA   B 2  18  ? -11.537 -64.509  18.108  1.00 46.65  ? 18  ALA   B O      1 
ATOM   3529  C  CB     . ALA   B 2  18  ? -12.801 -62.282  16.134  1.00 36.75  ? 18  ALA   B CB     1 
ATOM   3530  N  N      . LYS   B 2  19  ? -11.025 -62.461  18.866  1.00 41.58  ? 19  LYS   B N      1 
ATOM   3531  C  CA     . LYS   B 2  19  ? -9.856  -62.973  19.578  1.00 47.83  ? 19  LYS   B CA     1 
ATOM   3532  C  C      . LYS   B 2  19  ? -10.274 -63.942  20.683  1.00 51.21  ? 19  LYS   B C      1 
ATOM   3533  O  O      . LYS   B 2  19  ? -9.732  -65.049  20.809  1.00 47.61  ? 19  LYS   B O      1 
ATOM   3534  C  CB     . LYS   B 2  19  ? -9.046  -61.817  20.161  1.00 45.05  ? 19  LYS   B CB     1 
ATOM   3535  C  CG     . LYS   B 2  19  ? -8.480  -60.934  19.136  1.00 45.25  ? 19  LYS   B CG     1 
ATOM   3536  C  CD     . LYS   B 2  19  ? -7.444  -61.671  18.286  1.00 50.21  ? 19  LYS   B CD     1 
ATOM   3537  C  CE     . LYS   B 2  19  ? -7.002  -60.788  17.096  1.00 61.84  ? 19  LYS   B CE     1 
ATOM   3538  N  NZ     . LYS   B 2  19  ? -6.197  -61.475  16.040  1.00 67.91  ? 19  LYS   B NZ     1 
ATOM   3539  N  N      . PHE   B 2  20  ? -11.241 -63.527  21.501  1.00 49.90  ? 20  PHE   B N      1 
ATOM   3540  C  CA     . PHE   B 2  20  ? -11.720 -64.364  22.586  1.00 46.75  ? 20  PHE   B CA     1 
ATOM   3541  C  C      . PHE   B 2  20  ? -11.978 -65.788  22.103  1.00 48.38  ? 20  PHE   B C      1 
ATOM   3542  O  O      . PHE   B 2  20  ? -11.450 -66.751  22.665  1.00 46.92  ? 20  PHE   B O      1 
ATOM   3543  C  CB     . PHE   B 2  20  ? -12.981 -63.737  23.172  1.00 43.88  ? 20  PHE   B CB     1 
ATOM   3544  C  CG     . PHE   B 2  20  ? -13.683 -64.616  24.119  1.00 45.86  ? 20  PHE   B CG     1 
ATOM   3545  C  CD1    . PHE   B 2  20  ? -13.235 -64.725  25.431  1.00 43.97  ? 20  PHE   B CD1    1 
ATOM   3546  C  CD2    . PHE   B 2  20  ? -14.779 -65.357  23.712  1.00 49.10  ? 20  PHE   B CD2    1 
ATOM   3547  C  CE1    . PHE   B 2  20  ? -13.878 -65.550  26.327  1.00 45.45  ? 20  PHE   B CE1    1 
ATOM   3548  C  CE2    . PHE   B 2  20  ? -15.438 -66.198  24.614  1.00 50.18  ? 20  PHE   B CE2    1 
ATOM   3549  C  CZ     . PHE   B 2  20  ? -14.987 -66.293  25.919  1.00 45.98  ? 20  PHE   B CZ     1 
ATOM   3550  N  N      . TRP   B 2  21  ? -12.760 -65.939  21.029  1.00 48.58  ? 21  TRP   B N      1 
ATOM   3551  C  CA     . TRP   B 2  21  ? -13.045 -67.277  20.519  1.00 45.66  ? 21  TRP   B CA     1 
ATOM   3552  C  C      . TRP   B 2  21  ? -11.774 -68.005  20.086  1.00 51.94  ? 21  TRP   B C      1 
ATOM   3553  O  O      . TRP   B 2  21  ? -11.619 -69.199  20.364  1.00 56.77  ? 21  TRP   B O      1 
ATOM   3554  C  CB     . TRP   B 2  21  ? -14.057 -67.213  19.380  1.00 42.00  ? 21  TRP   B CB     1 
ATOM   3555  C  CG     . TRP   B 2  21  ? -15.432 -66.869  19.866  1.00 48.49  ? 21  TRP   B CG     1 
ATOM   3556  C  CD1    . TRP   B 2  21  ? -16.089 -65.680  19.715  1.00 50.20  ? 21  TRP   B CD1    1 
ATOM   3557  C  CD2    . TRP   B 2  21  ? -16.302 -67.706  20.643  1.00 49.34  ? 21  TRP   B CD2    1 
ATOM   3558  N  NE1    . TRP   B 2  21  ? -17.329 -65.737  20.325  1.00 44.99  ? 21  TRP   B NE1    1 
ATOM   3559  C  CE2    . TRP   B 2  21  ? -17.475 -66.968  20.907  1.00 47.10  ? 21  TRP   B CE2    1 
ATOM   3560  C  CE3    . TRP   B 2  21  ? -16.208 -69.008  21.130  1.00 48.87  ? 21  TRP   B CE3    1 
ATOM   3561  C  CZ2    . TRP   B 2  21  ? -18.535 -67.494  21.636  1.00 46.00  ? 21  TRP   B CZ2    1 
ATOM   3562  C  CZ3    . TRP   B 2  21  ? -17.261 -69.519  21.857  1.00 48.73  ? 21  TRP   B CZ3    1 
ATOM   3563  C  CH2    . TRP   B 2  21  ? -18.407 -68.768  22.102  1.00 46.66  ? 21  TRP   B CH2    1 
ATOM   3564  N  N      . GLU   B 2  22  ? -10.851 -67.323  19.405  1.00 48.81  ? 22  GLU   B N      1 
ATOM   3565  C  CA     . GLU   B 2  22  ? -9.553  -67.945  19.165  1.00 52.13  ? 22  GLU   B CA     1 
ATOM   3566  C  C      . GLU   B 2  22  ? -8.936  -68.448  20.465  1.00 55.23  ? 22  GLU   B C      1 
ATOM   3567  O  O      . GLU   B 2  22  ? -8.423  -69.573  20.537  1.00 56.18  ? 22  GLU   B O      1 
ATOM   3568  C  CB     . GLU   B 2  22  ? -8.579  -66.958  18.539  1.00 53.11  ? 22  GLU   B CB     1 
ATOM   3569  C  CG     . GLU   B 2  22  ? -8.633  -66.774  17.071  1.00 61.25  ? 22  GLU   B CG     1 
ATOM   3570  C  CD     . GLU   B 2  22  ? -7.749  -65.625  16.689  1.00 64.20  ? 22  GLU   B CD     1 
ATOM   3571  O  OE1    . GLU   B 2  22  ? -6.663  -65.529  17.330  1.00 59.78  ? 22  GLU   B OE1    1 
ATOM   3572  O  OE2    . GLU   B 2  22  ? -8.130  -64.838  15.787  1.00 62.43  ? 22  GLU   B OE2    1 
ATOM   3573  N  N      . VAL   B 2  23  ? -8.954  -67.593  21.494  1.00 46.36  ? 23  VAL   B N      1 
ATOM   3574  C  CA     . VAL   B 2  23  ? -8.161  -67.793  22.698  1.00 40.41  ? 23  VAL   B CA     1 
ATOM   3575  C  C      . VAL   B 2  23  ? -8.725  -68.941  23.514  1.00 49.24  ? 23  VAL   B C      1 
ATOM   3576  O  O      . VAL   B 2  23  ? -7.980  -69.756  24.070  1.00 54.93  ? 23  VAL   B O      1 
ATOM   3577  C  CB     . VAL   B 2  23  ? -8.118  -66.478  23.507  1.00 46.35  ? 23  VAL   B CB     1 
ATOM   3578  C  CG1    . VAL   B 2  23  ? -7.365  -66.626  24.828  1.00 39.39  ? 23  VAL   B CG1    1 
ATOM   3579  C  CG2    . VAL   B 2  23  ? -7.525  -65.332  22.668  1.00 45.89  ? 23  VAL   B CG2    1 
ATOM   3580  N  N      . ILE   B 2  24  ? -10.050 -69.032  23.598  1.00 50.72  ? 24  ILE   B N      1 
ATOM   3581  C  CA     . ILE   B 2  24  ? -10.654 -70.105  24.368  1.00 51.98  ? 24  ILE   B CA     1 
ATOM   3582  C  C      . ILE   B 2  24  ? -10.865 -71.349  23.520  1.00 49.76  ? 24  ILE   B C      1 
ATOM   3583  O  O      . ILE   B 2  24  ? -11.023 -72.440  24.075  1.00 57.86  ? 24  ILE   B O      1 
ATOM   3584  C  CB     . ILE   B 2  24  ? -11.996 -69.698  25.016  1.00 52.20  ? 24  ILE   B CB     1 
ATOM   3585  C  CG1    . ILE   B 2  24  ? -13.111 -69.653  23.975  1.00 53.99  ? 24  ILE   B CG1    1 
ATOM   3586  C  CG2    . ILE   B 2  24  ? -11.896 -68.369  25.738  1.00 42.00  ? 24  ILE   B CG2    1 
ATOM   3587  C  CD1    . ILE   B 2  24  ? -14.502 -69.554  24.575  1.00 53.02  ? 24  ILE   B CD1    1 
ATOM   3588  N  N      . SER   B 2  25  ? -10.883 -71.230  22.198  1.00 49.64  ? 25  SER   B N      1 
ATOM   3589  C  CA     . SER   B 2  25  ? -10.893 -72.459  21.417  1.00 59.12  ? 25  SER   B CA     1 
ATOM   3590  C  C      . SER   B 2  25  ? -9.566  -73.190  21.561  1.00 62.71  ? 25  SER   B C      1 
ATOM   3591  O  O      . SER   B 2  25  ? -9.527  -74.427  21.635  1.00 60.91  ? 25  SER   B O      1 
ATOM   3592  C  CB     . SER   B 2  25  ? -11.218 -72.170  19.951  1.00 56.20  ? 25  SER   B CB     1 
ATOM   3593  O  OG     . SER   B 2  25  ? -12.500 -71.588  19.812  1.00 48.13  ? 25  SER   B OG     1 
ATOM   3594  N  N      . ASP   B 2  26  ? -8.474  -72.429  21.640  1.00 62.37  ? 26  ASP   B N      1 
ATOM   3595  C  CA     . ASP   B 2  26  ? -7.163  -73.009  21.899  1.00 64.38  ? 26  ASP   B CA     1 
ATOM   3596  C  C      . ASP   B 2  26  ? -7.091  -73.665  23.281  1.00 62.58  ? 26  ASP   B C      1 
ATOM   3597  O  O      . ASP   B 2  26  ? -6.420  -74.684  23.451  1.00 66.25  ? 26  ASP   B O      1 
ATOM   3598  C  CB     . ASP   B 2  26  ? -6.107  -71.915  21.748  1.00 62.99  ? 26  ASP   B CB     1 
ATOM   3599  C  CG     . ASP   B 2  26  ? -4.732  -72.374  22.137  1.00 76.43  ? 26  ASP   B CG     1 
ATOM   3600  O  OD1    . ASP   B 2  26  ? -4.110  -73.133  21.351  1.00 81.07  ? 26  ASP   B OD1    1 
ATOM   3601  O  OD2    . ASP   B 2  26  ? -4.278  -71.972  23.235  1.00 76.20  ? 26  ASP   B OD2    1 
ATOM   3602  N  N      . GLU   B 2  27  ? -7.778  -73.111  24.277  1.00 57.74  ? 27  GLU   B N      1 
ATOM   3603  C  CA     . GLU   B 2  27  ? -7.755  -73.720  25.601  1.00 57.11  ? 27  GLU   B CA     1 
ATOM   3604  C  C      . GLU   B 2  27  ? -8.546  -75.017  25.621  1.00 60.09  ? 27  GLU   B C      1 
ATOM   3605  O  O      . GLU   B 2  27  ? -8.136  -76.002  26.248  1.00 63.90  ? 27  GLU   B O      1 
ATOM   3606  C  CB     . GLU   B 2  27  ? -8.320  -72.746  26.634  1.00 54.47  ? 27  GLU   B CB     1 
ATOM   3607  C  CG     . GLU   B 2  27  ? -7.635  -71.405  26.616  1.00 54.30  ? 27  GLU   B CG     1 
ATOM   3608  C  CD     . GLU   B 2  27  ? -7.894  -70.617  27.868  1.00 54.95  ? 27  GLU   B CD     1 
ATOM   3609  O  OE1    . GLU   B 2  27  ? -8.776  -71.037  28.647  1.00 56.10  ? 27  GLU   B OE1    1 
ATOM   3610  O  OE2    . GLU   B 2  27  ? -7.195  -69.600  28.087  1.00 49.83  ? 27  GLU   B OE2    1 
ATOM   3611  N  N      . HIS   B 2  28  ? -9.698  -75.029  24.975  1.00 61.84  ? 28  HIS   B N      1 
ATOM   3612  C  CA     . HIS   B 2  28  ? -10.518 -76.223  24.928  1.00 64.09  ? 28  HIS   B CA     1 
ATOM   3613  C  C      . HIS   B 2  28  ? -10.067 -77.148  23.823  1.00 66.12  ? 28  HIS   B C      1 
ATOM   3614  O  O      . HIS   B 2  28  ? -10.733 -78.151  23.551  1.00 67.83  ? 28  HIS   B O      1 
ATOM   3615  C  CB     . HIS   B 2  28  ? -11.991 -75.839  24.779  1.00 55.23  ? 28  HIS   B CB     1 
ATOM   3616  C  CG     . HIS   B 2  28  ? -12.524 -75.108  25.970  1.00 58.22  ? 28  HIS   B CG     1 
ATOM   3617  N  ND1    . HIS   B 2  28  ? -12.831 -75.739  27.157  1.00 65.39  ? 28  HIS   B ND1    1 
ATOM   3618  C  CD2    . HIS   B 2  28  ? -12.751 -73.790  26.179  1.00 54.02  ? 28  HIS   B CD2    1 
ATOM   3619  C  CE1    . HIS   B 2  28  ? -13.247 -74.846  28.038  1.00 59.39  ? 28  HIS   B CE1    1 
ATOM   3620  N  NE2    . HIS   B 2  28  ? -13.209 -73.655  27.469  1.00 56.86  ? 28  HIS   B NE2    1 
ATOM   3621  N  N      . GLY   B 2  29  ? -8.943  -76.830  23.191  1.00 63.56  ? 29  GLY   B N      1 
ATOM   3622  C  CA     . GLY   B 2  29  ? -8.370  -77.710  22.194  1.00 66.85  ? 29  GLY   B CA     1 
ATOM   3623  C  C      . GLY   B 2  29  ? -9.263  -77.953  21.000  1.00 69.37  ? 29  GLY   B C      1 
ATOM   3624  O  O      . GLY   B 2  29  ? -9.284  -79.071  20.470  1.00 71.89  ? 29  GLY   B O      1 
ATOM   3625  N  N      . ILE   B 2  30  ? -10.020 -76.936  20.571  1.00 63.32  ? 30  ILE   B N      1 
ATOM   3626  C  CA     . ILE   B 2  30  ? -10.781 -76.990  19.328  1.00 62.68  ? 30  ILE   B CA     1 
ATOM   3627  C  C      . ILE   B 2  30  ? -10.027 -76.191  18.275  1.00 66.21  ? 30  ILE   B C      1 
ATOM   3628  O  O      . ILE   B 2  30  ? -9.438  -75.145  18.577  1.00 67.85  ? 30  ILE   B O      1 
ATOM   3629  C  CB     . ILE   B 2  30  ? -12.213 -76.458  19.512  1.00 60.91  ? 30  ILE   B CB     1 
ATOM   3630  C  CG1    . ILE   B 2  30  ? -13.038 -77.420  20.347  1.00 63.61  ? 30  ILE   B CG1    1 
ATOM   3631  C  CG2    . ILE   B 2  30  ? -12.880 -76.291  18.181  1.00 65.08  ? 30  ILE   B CG2    1 
ATOM   3632  C  CD1    . ILE   B 2  30  ? -12.825 -77.277  21.809  1.00 71.19  ? 30  ILE   B CD1    1 
ATOM   3633  N  N      . ASP   B 2  31  ? -10.027 -76.687  17.040  1.00 68.16  ? 31  ASP   B N      1 
ATOM   3634  C  CA     . ASP   B 2  31  ? -9.303  -76.010  15.970  1.00 70.08  ? 31  ASP   B CA     1 
ATOM   3635  C  C      . ASP   B 2  31  ? -10.262 -75.251  15.066  1.00 69.47  ? 31  ASP   B C      1 
ATOM   3636  O  O      . ASP   B 2  31  ? -11.487 -75.340  15.230  1.00 67.56  ? 31  ASP   B O      1 
ATOM   3637  C  CB     . ASP   B 2  31  ? -8.509  -77.002  15.126  1.00 71.82  ? 31  ASP   B CB     1 
ATOM   3638  C  CG     . ASP   B 2  31  ? -9.347  -78.167  14.679  1.00 71.78  ? 31  ASP   B CG     1 
ATOM   3639  O  OD1    . ASP   B 2  31  ? -10.581 -78.026  14.685  1.00 72.28  ? 31  ASP   B OD1    1 
ATOM   3640  O  OD2    . ASP   B 2  31  ? -8.784  -79.219  14.323  1.00 75.45  ? 31  ASP   B OD2    1 
ATOM   3641  N  N      . PRO   B 2  32  ? -9.743  -74.508  14.091  1.00 66.53  ? 32  PRO   B N      1 
ATOM   3642  C  CA     . PRO   B 2  32  ? -10.636 -73.707  13.247  1.00 65.15  ? 32  PRO   B CA     1 
ATOM   3643  C  C      . PRO   B 2  32  ? -11.650 -74.539  12.492  1.00 73.72  ? 32  PRO   B C      1 
ATOM   3644  O  O      . PRO   B 2  32  ? -12.725 -74.026  12.167  1.00 75.73  ? 32  PRO   B O      1 
ATOM   3645  C  CB     . PRO   B 2  32  ? -9.666  -72.986  12.310  1.00 68.40  ? 32  PRO   B CB     1 
ATOM   3646  C  CG     . PRO   B 2  32  ? -8.406  -72.894  13.096  1.00 69.72  ? 32  PRO   B CG     1 
ATOM   3647  C  CD     . PRO   B 2  32  ? -8.327  -74.194  13.850  1.00 65.46  ? 32  PRO   B CD     1 
ATOM   3648  N  N      . THR   B 2  33  ? -11.351 -75.809  12.200  1.00 80.22  ? 33  THR   B N      1 
ATOM   3649  C  CA     . THR   B 2  33  ? -12.357 -76.685  11.603  1.00 76.23  ? 33  THR   B CA     1 
ATOM   3650  C  C      . THR   B 2  33  ? -13.482 -77.036  12.565  1.00 71.03  ? 33  THR   B C      1 
ATOM   3651  O  O      . THR   B 2  33  ? -14.532 -77.507  12.120  1.00 70.41  ? 33  THR   B O      1 
ATOM   3652  C  CB     . THR   B 2  33  ? -11.720 -77.975  11.087  1.00 81.06  ? 33  THR   B CB     1 
ATOM   3653  O  OG1    . THR   B 2  33  ? -12.752 -78.853  10.615  1.00 93.21  ? 33  THR   B OG1    1 
ATOM   3654  C  CG2    . THR   B 2  33  ? -10.929 -78.675  12.170  1.00 75.87  ? 33  THR   B CG2    1 
ATOM   3655  N  N      . GLY   B 2  34  ? -13.288 -76.827  13.863  1.00 71.21  ? 34  GLY   B N      1 
ATOM   3656  C  CA     . GLY   B 2  34  ? -14.273 -77.199  14.855  1.00 75.52  ? 34  GLY   B CA     1 
ATOM   3657  C  C      . GLY   B 2  34  ? -14.076 -78.555  15.509  1.00 74.35  ? 34  GLY   B C      1 
ATOM   3658  O  O      . GLY   B 2  34  ? -14.883 -78.921  16.374  1.00 72.02  ? 34  GLY   B O      1 
ATOM   3659  N  N      . SER   B 2  35  ? -13.028 -79.299  15.135  1.00 75.24  ? 35  SER   B N      1 
ATOM   3660  C  CA     . SER   B 2  35  ? -12.781 -80.648  15.642  1.00 76.14  ? 35  SER   B CA     1 
ATOM   3661  C  C      . SER   B 2  35  ? -11.872 -80.609  16.865  1.00 71.51  ? 35  SER   B C      1 
ATOM   3662  O  O      . SER   B 2  35  ? -10.791 -80.006  16.831  1.00 64.55  ? 35  SER   B O      1 
ATOM   3663  C  CB     . SER   B 2  35  ? -12.147 -81.544  14.570  1.00 75.41  ? 35  SER   B CB     1 
ATOM   3664  O  OG     . SER   B 2  35  ? -12.982 -81.712  13.440  1.00 76.74  ? 35  SER   B OG     1 
ATOM   3665  N  N      . TYR   B 2  36  ? -12.297 -81.293  17.928  1.00 73.48  ? 36  TYR   B N      1 
ATOM   3666  C  CA     . TYR   B 2  36  ? -11.541 -81.312  19.171  1.00 70.49  ? 36  TYR   B CA     1 
ATOM   3667  C  C      . TYR   B 2  36  ? -10.329 -82.220  19.031  1.00 68.91  ? 36  TYR   B C      1 
ATOM   3668  O  O      . TYR   B 2  36  ? -10.477 -83.410  18.749  1.00 71.14  ? 36  TYR   B O      1 
ATOM   3669  C  CB     . TYR   B 2  36  ? -12.425 -81.767  20.329  1.00 73.26  ? 36  TYR   B CB     1 
ATOM   3670  C  CG     . TYR   B 2  36  ? -11.627 -82.092  21.560  1.00 70.31  ? 36  TYR   B CG     1 
ATOM   3671  C  CD1    . TYR   B 2  36  ? -10.926 -81.110  22.217  1.00 73.02  ? 36  TYR   B CD1    1 
ATOM   3672  C  CD2    . TYR   B 2  36  ? -11.584 -83.373  22.067  1.00 69.01  ? 36  TYR   B CD2    1 
ATOM   3673  C  CE1    . TYR   B 2  36  ? -10.197 -81.400  23.332  1.00 77.64  ? 36  TYR   B CE1    1 
ATOM   3674  C  CE2    . TYR   B 2  36  ? -10.851 -83.672  23.186  1.00 68.66  ? 36  TYR   B CE2    1 
ATOM   3675  C  CZ     . TYR   B 2  36  ? -10.162 -82.683  23.811  1.00 73.29  ? 36  TYR   B CZ     1 
ATOM   3676  O  OH     . TYR   B 2  36  ? -9.415  -82.958  24.924  1.00 79.17  ? 36  TYR   B OH     1 
ATOM   3677  N  N      . HIS   B 2  37  ? -9.128  -81.653  19.218  1.00 72.30  ? 37  HIS   B N      1 
ATOM   3678  C  CA     . HIS   B 2  37  ? -7.872  -82.410  19.298  1.00 76.54  ? 37  HIS   B CA     1 
ATOM   3679  C  C      . HIS   B 2  37  ? -7.178  -82.051  20.620  1.00 77.36  ? 37  HIS   B C      1 
ATOM   3680  O  O      . HIS   B 2  37  ? -6.170  -81.337  20.625  1.00 76.96  ? 37  HIS   B O      1 
ATOM   3681  C  CB     . HIS   B 2  37  ? -6.956  -82.118  18.110  1.00 71.42  ? 37  HIS   B CB     1 
ATOM   3682  C  CG     . HIS   B 2  37  ? -7.388  -82.755  16.824  1.00 81.18  ? 37  HIS   B CG     1 
ATOM   3683  N  ND1    . HIS   B 2  37  ? -8.416  -82.255  16.052  1.00 83.75  ? 37  HIS   B ND1    1 
ATOM   3684  C  CD2    . HIS   B 2  37  ? -6.922  -83.845  16.166  1.00 92.85  ? 37  HIS   B CD2    1 
ATOM   3685  C  CE1    . HIS   B 2  37  ? -8.569  -83.013  14.978  1.00 88.15  ? 37  HIS   B CE1    1 
ATOM   3686  N  NE2    . HIS   B 2  37  ? -7.673  -83.983  15.022  1.00 95.44  ? 37  HIS   B NE2    1 
ATOM   3687  N  N      . GLY   B 2  38  ? -7.703  -82.568  21.737  1.00 73.02  ? 38  GLY   B N      1 
ATOM   3688  C  CA     . GLY   B 2  38  ? -7.319  -82.105  23.050  1.00 78.53  ? 38  GLY   B CA     1 
ATOM   3689  C  C      . GLY   B 2  38  ? -6.619  -83.131  23.929  1.00 82.96  ? 38  GLY   B C      1 
ATOM   3690  O  O      . GLY   B 2  38  ? -6.656  -84.342  23.698  1.00 87.01  ? 38  GLY   B O      1 
ATOM   3691  N  N      . ASP   B 2  39  ? -5.992  -82.603  24.972  1.00 83.55  ? 39  ASP   B N      1 
ATOM   3692  C  CA     . ASP   B 2  39  ? -5.159  -83.358  25.894  1.00 81.92  ? 39  ASP   B CA     1 
ATOM   3693  C  C      . ASP   B 2  39  ? -6.024  -83.949  27.003  1.00 83.03  ? 39  ASP   B C      1 
ATOM   3694  O  O      . ASP   B 2  39  ? -6.414  -85.119  26.945  1.00 77.29  ? 39  ASP   B O      1 
ATOM   3695  C  CB     . ASP   B 2  39  ? -4.095  -82.429  26.476  1.00 84.52  ? 39  ASP   B CB     1 
ATOM   3696  C  CG     . ASP   B 2  39  ? -2.797  -83.125  26.751  1.00 93.53  ? 39  ASP   B CG     1 
ATOM   3697  O  OD1    . ASP   B 2  39  ? -2.774  -84.368  26.705  1.00 92.60  ? 39  ASP   B OD1    1 
ATOM   3698  O  OD2    . ASP   B 2  39  ? -1.805  -82.422  27.039  1.00 101.14 ? 39  ASP   B OD2    1 
ATOM   3699  N  N      . SER   B 2  40  ? -6.339  -83.123  28.003  1.00 85.73  ? 40  SER   B N      1 
ATOM   3700  C  CA     . SER   B 2  40  ? -7.196  -83.442  29.138  1.00 78.05  ? 40  SER   B CA     1 
ATOM   3701  C  C      . SER   B 2  40  ? -8.662  -83.532  28.729  1.00 75.14  ? 40  SER   B C      1 
ATOM   3702  O  O      . SER   B 2  40  ? -9.074  -83.063  27.671  1.00 80.69  ? 40  SER   B O      1 
ATOM   3703  C  CB     . SER   B 2  40  ? -7.052  -82.383  30.232  1.00 73.50  ? 40  SER   B CB     1 
ATOM   3704  O  OG     . SER   B 2  40  ? -7.950  -82.617  31.303  1.00 75.27  ? 40  SER   B OG     1 
ATOM   3705  N  N      . ASP   B 2  41  ? -9.458  -84.148  29.592  1.00 77.05  ? 41  ASP   B N      1 
ATOM   3706  C  CA     . ASP   B 2  41  ? -10.902 -84.108  29.434  1.00 76.66  ? 41  ASP   B CA     1 
ATOM   3707  C  C      . ASP   B 2  41  ? -11.512 -82.880  30.080  1.00 78.57  ? 41  ASP   B C      1 
ATOM   3708  O  O      . ASP   B 2  41  ? -12.630 -82.491  29.715  1.00 75.58  ? 41  ASP   B O      1 
ATOM   3709  C  CB     . ASP   B 2  41  ? -11.541 -85.348  30.044  1.00 83.07  ? 41  ASP   B CB     1 
ATOM   3710  C  CG     . ASP   B 2  41  ? -11.439 -86.540  29.147  1.00 93.03  ? 41  ASP   B CG     1 
ATOM   3711  O  OD1    . ASP   B 2  41  ? -11.277 -86.347  27.918  1.00 88.65  ? 41  ASP   B OD1    1 
ATOM   3712  O  OD2    . ASP   B 2  41  ? -11.524 -87.668  29.680  1.00 103.15 ? 41  ASP   B OD2    1 
ATOM   3713  N  N      . LEU   B 2  42  ? -10.804 -82.277  31.042  1.00 75.10  ? 42  LEU   B N      1 
ATOM   3714  C  CA     . LEU   B 2  42  ? -11.206 -81.007  31.629  1.00 73.57  ? 42  LEU   B CA     1 
ATOM   3715  C  C      . LEU   B 2  42  ? -11.642 -80.083  30.503  1.00 71.68  ? 42  LEU   B C      1 
ATOM   3716  O  O      . LEU   B 2  42  ? -12.593 -79.312  30.660  1.00 80.54  ? 42  LEU   B O      1 
ATOM   3717  C  CB     . LEU   B 2  42  ? -10.056 -80.377  32.422  1.00 76.66  ? 42  LEU   B CB     1 
ATOM   3718  C  CG     . LEU   B 2  42  ? -9.575  -80.982  33.744  1.00 72.16  ? 42  LEU   B CG     1 
ATOM   3719  C  CD1    . LEU   B 2  42  ? -8.532  -80.074  34.362  1.00 75.61  ? 42  LEU   B CD1    1 
ATOM   3720  C  CD2    . LEU   B 2  42  ? -10.716 -81.190  34.701  1.00 74.19  ? 42  LEU   B CD2    1 
ATOM   3721  N  N      . GLN   B 2  43  ? -10.945 -80.174  29.358  1.00 67.12  ? 43  GLN   B N      1 
ATOM   3722  C  CA     . GLN   B 2  43  ? -11.245 -79.356  28.186  1.00 66.44  ? 43  GLN   B CA     1 
ATOM   3723  C  C      . GLN   B 2  43  ? -12.621 -79.595  27.592  1.00 66.06  ? 43  GLN   B C      1 
ATOM   3724  O  O      . GLN   B 2  43  ? -13.099 -78.737  26.846  1.00 63.70  ? 43  GLN   B O      1 
ATOM   3725  C  CB     . GLN   B 2  43  ? -10.218 -79.574  27.087  1.00 62.92  ? 43  GLN   B CB     1 
ATOM   3726  C  CG     . GLN   B 2  43  ? -8.839  -79.167  27.438  1.00 65.97  ? 43  GLN   B CG     1 
ATOM   3727  C  CD     . GLN   B 2  43  ? -7.861  -79.670  26.422  1.00 73.55  ? 43  GLN   B CD     1 
ATOM   3728  O  OE1    . GLN   B 2  43  ? -8.261  -80.071  25.336  1.00 71.61  ? 43  GLN   B OE1    1 
ATOM   3729  N  NE2    . GLN   B 2  43  ? -6.565  -79.612  26.741  1.00 80.17  ? 43  GLN   B NE2    1 
ATOM   3730  N  N      . LEU   B 2  44  ? -13.266 -80.722  27.863  1.00 65.06  ? 44  LEU   B N      1 
ATOM   3731  C  CA     . LEU   B 2  44  ? -14.610 -80.901  27.341  1.00 62.16  ? 44  LEU   B CA     1 
ATOM   3732  C  C      . LEU   B 2  44  ? -15.682 -81.029  28.410  1.00 62.86  ? 44  LEU   B C      1 
ATOM   3733  O  O      . LEU   B 2  44  ? -16.858 -81.148  28.062  1.00 67.38  ? 44  LEU   B O      1 
ATOM   3734  C  CB     . LEU   B 2  44  ? -14.659 -82.106  26.390  1.00 59.83  ? 44  LEU   B CB     1 
ATOM   3735  C  CG     . LEU   B 2  44  ? -13.853 -81.908  25.103  1.00 67.40  ? 44  LEU   B CG     1 
ATOM   3736  C  CD1    . LEU   B 2  44  ? -13.976 -83.079  24.167  1.00 68.05  ? 44  LEU   B CD1    1 
ATOM   3737  C  CD2    . LEU   B 2  44  ? -14.353 -80.683  24.398  1.00 71.92  ? 44  LEU   B CD2    1 
ATOM   3738  N  N      . GLU   B 2  45  ? -15.339 -80.965  29.693  1.00 63.03  ? 45  GLU   B N      1 
ATOM   3739  C  CA     . GLU   B 2  45  ? -16.362 -81.204  30.705  1.00 63.97  ? 45  GLU   B CA     1 
ATOM   3740  C  C      . GLU   B 2  45  ? -17.450 -80.146  30.655  1.00 67.62  ? 45  GLU   B C      1 
ATOM   3741  O  O      . GLU   B 2  45  ? -18.627 -80.447  30.873  1.00 67.36  ? 45  GLU   B O      1 
ATOM   3742  C  CB     . GLU   B 2  45  ? -15.766 -81.221  32.098  1.00 66.69  ? 45  GLU   B CB     1 
ATOM   3743  C  CG     . GLU   B 2  45  ? -16.565 -82.044  33.058  1.00 63.48  ? 45  GLU   B CG     1 
ATOM   3744  C  CD     . GLU   B 2  45  ? -15.905 -82.114  34.410  1.00 80.48  ? 45  GLU   B CD     1 
ATOM   3745  O  OE1    . GLU   B 2  45  ? -14.919 -82.878  34.555  1.00 85.69  ? 45  GLU   B OE1    1 
ATOM   3746  O  OE2    . GLU   B 2  45  ? -16.399 -81.413  35.330  1.00 74.83  ? 45  GLU   B OE2    1 
ATOM   3747  N  N      . ARG   B 2  46  ? -17.079 -78.892  30.418  1.00 66.20  ? 46  ARG   B N      1 
ATOM   3748  C  CA     . ARG   B 2  46  ? -18.055 -77.813  30.465  1.00 68.65  ? 46  ARG   B CA     1 
ATOM   3749  C  C      . ARG   B 2  46  ? -18.096 -77.078  29.128  1.00 67.34  ? 46  ARG   B C      1 
ATOM   3750  O  O      . ARG   B 2  46  ? -18.480 -75.906  29.051  1.00 61.21  ? 46  ARG   B O      1 
ATOM   3751  C  CB     . ARG   B 2  46  ? -17.734 -76.859  31.613  1.00 65.62  ? 46  ARG   B CB     1 
ATOM   3752  C  CG     . ARG   B 2  46  ? -18.047 -77.441  32.979  1.00 65.81  ? 46  ARG   B CG     1 
ATOM   3753  C  CD     . ARG   B 2  46  ? -17.698 -76.469  34.110  1.00 63.14  ? 46  ARG   B CD     1 
ATOM   3754  N  NE     . ARG   B 2  46  ? -18.722 -75.438  34.252  1.00 64.67  ? 46  ARG   B NE     1 
ATOM   3755  C  CZ     . ARG   B 2  46  ? -18.747 -74.517  35.206  1.00 57.80  ? 46  ARG   B CZ     1 
ATOM   3756  N  NH1    . ARG   B 2  46  ? -17.761 -74.390  36.072  1.00 62.92  ? 46  ARG   B NH1    1 
ATOM   3757  N  NH2    . ARG   B 2  46  ? -19.784 -73.691  35.283  1.00 68.05  ? 46  ARG   B NH2    1 
ATOM   3758  N  N      . ILE   B 2  47  ? -17.708 -77.778  28.060  1.00 67.08  ? 47  ILE   B N      1 
ATOM   3759  C  CA     . ILE   B 2  47  ? -17.521 -77.144  26.765  1.00 63.35  ? 47  ILE   B CA     1 
ATOM   3760  C  C      . ILE   B 2  47  ? -18.838 -76.588  26.236  1.00 65.41  ? 47  ILE   B C      1 
ATOM   3761  O  O      . ILE   B 2  47  ? -18.840 -75.660  25.419  1.00 62.61  ? 47  ILE   B O      1 
ATOM   3762  C  CB     . ILE   B 2  47  ? -16.897 -78.160  25.784  1.00 61.50  ? 47  ILE   B CB     1 
ATOM   3763  C  CG1    . ILE   B 2  47  ? -16.285 -77.459  24.574  1.00 59.87  ? 47  ILE   B CG1    1 
ATOM   3764  C  CG2    . ILE   B 2  47  ? -17.942 -79.149  25.312  1.00 63.33  ? 47  ILE   B CG2    1 
ATOM   3765  C  CD1    . ILE   B 2  47  ? -15.042 -76.680  24.895  1.00 59.29  ? 47  ILE   B CD1    1 
ATOM   3766  N  N      . ASN   B 2  48  ? -19.971 -77.116  26.701  1.00 66.37  ? 48  ASN   B N      1 
ATOM   3767  C  CA     . ASN   B 2  48  ? -21.263 -76.691  26.181  1.00 62.83  ? 48  ASN   B CA     1 
ATOM   3768  C  C      . ASN   B 2  48  ? -21.681 -75.326  26.696  1.00 61.28  ? 48  ASN   B C      1 
ATOM   3769  O  O      . ASN   B 2  48  ? -22.617 -74.738  26.144  1.00 64.24  ? 48  ASN   B O      1 
ATOM   3770  C  CB     . ASN   B 2  48  ? -22.336 -77.697  26.565  1.00 63.37  ? 48  ASN   B CB     1 
ATOM   3771  C  CG     . ASN   B 2  48  ? -22.402 -77.900  28.059  1.00 75.54  ? 48  ASN   B CG     1 
ATOM   3772  O  OD1    . ASN   B 2  48  ? -21.457 -78.416  28.672  1.00 72.67  ? 48  ASN   B OD1    1 
ATOM   3773  N  ND2    . ASN   B 2  48  ? -23.530 -77.503  28.662  1.00 85.21  ? 48  ASN   B ND2    1 
ATOM   3774  N  N      . VAL   B 2  49  ? -21.042 -74.821  27.753  1.00 57.95  ? 49  VAL   B N      1 
ATOM   3775  C  CA     . VAL   B 2  49  ? -21.383 -73.485  28.234  1.00 58.71  ? 49  VAL   B CA     1 
ATOM   3776  C  C      . VAL   B 2  49  ? -21.253 -72.479  27.095  1.00 57.57  ? 49  VAL   B C      1 
ATOM   3777  O  O      . VAL   B 2  49  ? -22.117 -71.608  26.906  1.00 50.87  ? 49  VAL   B O      1 
ATOM   3778  C  CB     . VAL   B 2  49  ? -20.491 -73.102  29.430  1.00 51.98  ? 49  VAL   B CB     1 
ATOM   3779  C  CG1    . VAL   B 2  49  ? -20.505 -71.599  29.662  1.00 47.02  ? 49  VAL   B CG1    1 
ATOM   3780  C  CG2    . VAL   B 2  49  ? -20.911 -73.840  30.667  1.00 60.14  ? 49  VAL   B CG2    1 
ATOM   3781  N  N      . TYR   B 2  50  ? -20.178 -72.603  26.298  1.00 56.01  ? 50  TYR   B N      1 
ATOM   3782  C  CA     . TYR   B 2  50  ? -19.894 -71.665  25.225  1.00 48.69  ? 50  TYR   B CA     1 
ATOM   3783  C  C      . TYR   B 2  50  ? -19.991 -72.250  23.826  1.00 52.68  ? 50  TYR   B C      1 
ATOM   3784  O  O      . TYR   B 2  50  ? -20.051 -71.474  22.872  1.00 54.37  ? 50  TYR   B O      1 
ATOM   3785  C  CB     . TYR   B 2  50  ? -18.499 -71.040  25.391  1.00 46.42  ? 50  TYR   B CB     1 
ATOM   3786  C  CG     . TYR   B 2  50  ? -18.456 -69.909  26.410  1.00 47.37  ? 50  TYR   B CG     1 
ATOM   3787  C  CD1    . TYR   B 2  50  ? -18.952 -68.650  26.090  1.00 47.94  ? 50  TYR   B CD1    1 
ATOM   3788  C  CD2    . TYR   B 2  50  ? -17.860 -70.074  27.647  1.00 40.18  ? 50  TYR   B CD2    1 
ATOM   3789  C  CE1    . TYR   B 2  50  ? -18.914 -67.615  26.987  1.00 45.19  ? 50  TYR   B CE1    1 
ATOM   3790  C  CE2    . TYR   B 2  50  ? -17.822 -69.043  28.556  1.00 40.80  ? 50  TYR   B CE2    1 
ATOM   3791  C  CZ     . TYR   B 2  50  ? -18.347 -67.811  28.223  1.00 45.66  ? 50  TYR   B CZ     1 
ATOM   3792  O  OH     . TYR   B 2  50  ? -18.312 -66.762  29.120  1.00 42.55  ? 50  TYR   B OH     1 
ATOM   3793  N  N      . TYR   B 2  51  ? -20.016 -73.573  23.661  1.00 56.30  ? 51  TYR   B N      1 
ATOM   3794  C  CA     . TYR   B 2  51  ? -20.057 -74.175  22.330  1.00 57.62  ? 51  TYR   B CA     1 
ATOM   3795  C  C      . TYR   B 2  51  ? -21.289 -75.066  22.210  1.00 63.71  ? 51  TYR   B C      1 
ATOM   3796  O  O      . TYR   B 2  51  ? -21.568 -75.867  23.112  1.00 60.05  ? 51  TYR   B O      1 
ATOM   3797  C  CB     . TYR   B 2  51  ? -18.806 -75.017  22.054  1.00 55.10  ? 51  TYR   B CB     1 
ATOM   3798  C  CG     . TYR   B 2  51  ? -17.512 -74.240  21.985  1.00 50.72  ? 51  TYR   B CG     1 
ATOM   3799  C  CD1    . TYR   B 2  51  ? -16.829 -73.909  23.148  1.00 52.93  ? 51  TYR   B CD1    1 
ATOM   3800  C  CD2    . TYR   B 2  51  ? -16.963 -73.842  20.780  1.00 54.61  ? 51  TYR   B CD2    1 
ATOM   3801  C  CE1    . TYR   B 2  51  ? -15.629 -73.190  23.121  1.00 54.07  ? 51  TYR   B CE1    1 
ATOM   3802  C  CE2    . TYR   B 2  51  ? -15.754 -73.117  20.740  1.00 58.10  ? 51  TYR   B CE2    1 
ATOM   3803  C  CZ     . TYR   B 2  51  ? -15.095 -72.797  21.920  1.00 54.88  ? 51  TYR   B CZ     1 
ATOM   3804  O  OH     . TYR   B 2  51  ? -13.910 -72.092  21.917  1.00 50.85  ? 51  TYR   B OH     1 
ATOM   3805  N  N      . ASN   B 2  52  ? -22.029 -74.921  21.108  1.00 67.02  ? 52  ASN   B N      1 
ATOM   3806  C  CA     . ASN   B 2  52  ? -22.969 -75.951  20.678  1.00 65.03  ? 52  ASN   B CA     1 
ATOM   3807  C  C      . ASN   B 2  52  ? -22.216 -77.086  19.992  1.00 75.38  ? 52  ASN   B C      1 
ATOM   3808  O  O      . ASN   B 2  52  ? -21.139 -76.885  19.423  1.00 71.86  ? 52  ASN   B O      1 
ATOM   3809  C  CB     . ASN   B 2  52  ? -24.021 -75.376  19.729  1.00 60.86  ? 52  ASN   B CB     1 
ATOM   3810  C  CG     . ASN   B 2  52  ? -25.197 -74.756  20.450  1.00 65.66  ? 52  ASN   B CG     1 
ATOM   3811  O  OD1    . ASN   B 2  52  ? -25.590 -75.219  21.507  1.00 78.03  ? 52  ASN   B OD1    1 
ATOM   3812  N  ND2    . ASN   B 2  52  ? -25.764 -73.696  19.882  1.00 65.49  ? 52  ASN   B ND2    1 
ATOM   3813  N  N      . GLU   B 2  53  ? -22.791 -78.288  20.059  1.00 87.70  ? 53  GLU   B N      1 
ATOM   3814  C  CA     . GLU   B 2  53  ? -22.179 -79.506  19.529  1.00 88.49  ? 53  GLU   B CA     1 
ATOM   3815  C  C      . GLU   B 2  53  ? -22.913 -79.932  18.263  1.00 83.91  ? 53  GLU   B C      1 
ATOM   3816  O  O      . GLU   B 2  53  ? -24.140 -80.077  18.260  1.00 75.19  ? 53  GLU   B O      1 
ATOM   3817  C  CB     . GLU   B 2  53  ? -22.175 -80.625  20.588  1.00 89.73  ? 53  GLU   B CB     1 
ATOM   3818  C  CG     . GLU   B 2  53  ? -21.174 -81.772  20.357  1.00 91.43  ? 53  GLU   B CG     1 
ATOM   3819  C  CD     . GLU   B 2  53  ? -21.114 -82.760  21.530  1.00 97.09  ? 53  GLU   B CD     1 
ATOM   3820  O  OE1    . GLU   B 2  53  ? -21.730 -82.480  22.584  1.00 97.88  ? 53  GLU   B OE1    1 
ATOM   3821  O  OE2    . GLU   B 2  53  ? -20.466 -83.825  21.399  1.00 103.06 ? 53  GLU   B OE2    1 
ATOM   3822  N  N      . ALA   B 2  54  ? -22.156 -80.115  17.190  1.00 91.49  ? 54  ALA   B N      1 
ATOM   3823  C  CA     . ALA   B 2  54  ? -22.696 -80.436  15.880  1.00 107.61 ? 54  ALA   B CA     1 
ATOM   3824  C  C      . ALA   B 2  54  ? -22.467 -81.902  15.530  1.00 119.34 ? 54  ALA   B C      1 
ATOM   3825  O  O      . ALA   B 2  54  ? -21.501 -82.530  15.983  1.00 116.37 ? 54  ALA   B O      1 
ATOM   3826  C  CB     . ALA   B 2  54  ? -22.062 -79.555  14.801  1.00 112.28 ? 54  ALA   B CB     1 
ATOM   3827  N  N      . THR   B 2  55  ? -23.377 -82.440  14.716  1.00 126.45 ? 55  THR   B N      1 
ATOM   3828  C  CA     . THR   B 2  55  ? -23.212 -83.786  14.193  1.00 129.60 ? 55  THR   B CA     1 
ATOM   3829  C  C      . THR   B 2  55  ? -21.842 -83.913  13.538  1.00 126.37 ? 55  THR   B C      1 
ATOM   3830  O  O      . THR   B 2  55  ? -21.267 -82.934  13.051  1.00 121.11 ? 55  THR   B O      1 
ATOM   3831  C  CB     . THR   B 2  55  ? -24.338 -84.108  13.204  1.00 133.03 ? 55  THR   B CB     1 
ATOM   3832  O  OG1    . THR   B 2  55  ? -24.452 -83.051  12.243  1.00 131.77 ? 55  THR   B OG1    1 
ATOM   3833  C  CG2    . THR   B 2  55  ? -25.667 -84.253  13.944  1.00 128.16 ? 55  THR   B CG2    1 
ATOM   3834  N  N      . GLY   B 2  56  ? -21.303 -85.126  13.547  1.00 126.85 ? 56  GLY   B N      1 
ATOM   3835  C  CA     . GLY   B 2  56  ? -19.887 -85.260  13.292  1.00 120.72 ? 56  GLY   B CA     1 
ATOM   3836  C  C      . GLY   B 2  56  ? -19.028 -84.827  14.452  1.00 114.01 ? 56  GLY   B C      1 
ATOM   3837  O  O      . GLY   B 2  56  ? -17.818 -84.660  14.277  1.00 114.94 ? 56  GLY   B O      1 
ATOM   3838  N  N      . ASN   B 2  57  ? -19.628 -84.638  15.628  1.00 115.40 ? 57  ASN   B N      1 
ATOM   3839  C  CA     . ASN   B 2  57  ? -18.947 -84.205  16.852  1.00 118.15 ? 57  ASN   B CA     1 
ATOM   3840  C  C      . ASN   B 2  57  ? -17.984 -83.043  16.578  1.00 112.23 ? 57  ASN   B C      1 
ATOM   3841  O  O      . ASN   B 2  57  ? -16.786 -83.089  16.878  1.00 106.38 ? 57  ASN   B O      1 
ATOM   3842  C  CB     . ASN   B 2  57  ? -18.249 -85.388  17.539  1.00 122.01 ? 57  ASN   B CB     1 
ATOM   3843  C  CG     . ASN   B 2  57  ? -19.230 -86.298  18.298  1.00 120.62 ? 57  ASN   B CG     1 
ATOM   3844  O  OD1    . ASN   B 2  57  ? -19.530 -87.413  17.864  1.00 120.74 ? 57  ASN   B OD1    1 
ATOM   3845  N  ND2    . ASN   B 2  57  ? -19.716 -85.822  19.442  1.00 115.94 ? 57  ASN   B ND2    1 
ATOM   3846  N  N      . LYS   B 2  58  ? -18.549 -81.987  15.994  1.00 107.54 ? 58  LYS   B N      1 
ATOM   3847  C  CA     . LYS   B 2  58  ? -17.915 -80.683  15.852  1.00 96.52  ? 58  LYS   B CA     1 
ATOM   3848  C  C      . LYS   B 2  58  ? -18.478 -79.718  16.890  1.00 92.19  ? 58  LYS   B C      1 
ATOM   3849  O  O      . LYS   B 2  58  ? -19.587 -79.898  17.400  1.00 94.60  ? 58  LYS   B O      1 
ATOM   3850  C  CB     . LYS   B 2  58  ? -18.129 -80.115  14.444  1.00 89.06  ? 58  LYS   B CB     1 
ATOM   3851  C  CG     . LYS   B 2  58  ? -17.300 -80.788  13.379  1.00 89.91  ? 58  LYS   B CG     1 
ATOM   3852  C  CD     . LYS   B 2  58  ? -16.028 -79.999  13.106  1.00 87.59  ? 58  LYS   B CD     1 
ATOM   3853  C  CE     . LYS   B 2  58  ? -15.262 -80.552  11.905  1.00 87.66  ? 58  LYS   B CE     1 
ATOM   3854  N  NZ     . LYS   B 2  58  ? -14.857 -81.974  12.128  1.00 96.48  ? 58  LYS   B NZ     1 
ATOM   3855  N  N      . TYR   B 2  59  ? -17.702 -78.681  17.201  1.00 84.97  ? 59  TYR   B N      1 
ATOM   3856  C  CA     . TYR   B 2  59  ? -18.103 -77.699  18.201  1.00 81.84  ? 59  TYR   B CA     1 
ATOM   3857  C  C      . TYR   B 2  59  ? -18.279 -76.330  17.559  1.00 78.79  ? 59  TYR   B C      1 
ATOM   3858  O  O      . TYR   B 2  59  ? -17.376 -75.842  16.868  1.00 82.48  ? 59  TYR   B O      1 
ATOM   3859  C  CB     . TYR   B 2  59  ? -17.088 -77.634  19.330  1.00 78.18  ? 59  TYR   B CB     1 
ATOM   3860  C  CG     . TYR   B 2  59  ? -17.079 -78.904  20.123  1.00 79.40  ? 59  TYR   B CG     1 
ATOM   3861  C  CD1    . TYR   B 2  59  ? -16.319 -79.991  19.727  1.00 81.46  ? 59  TYR   B CD1    1 
ATOM   3862  C  CD2    . TYR   B 2  59  ? -17.904 -79.047  21.220  1.00 80.11  ? 59  TYR   B CD2    1 
ATOM   3863  C  CE1    . TYR   B 2  59  ? -16.334 -81.155  20.453  1.00 84.35  ? 59  TYR   B CE1    1 
ATOM   3864  C  CE2    . TYR   B 2  59  ? -17.935 -80.203  21.944  1.00 81.83  ? 59  TYR   B CE2    1 
ATOM   3865  C  CZ     . TYR   B 2  59  ? -17.153 -81.253  21.563  1.00 84.25  ? 59  TYR   B CZ     1 
ATOM   3866  O  OH     . TYR   B 2  59  ? -17.200 -82.404  22.309  1.00 93.09  ? 59  TYR   B OH     1 
ATOM   3867  N  N      . VAL   B 2  60  ? -19.430 -75.709  17.802  1.00 71.48  ? 60  VAL   B N      1 
ATOM   3868  C  CA     . VAL   B 2  60  ? -19.836 -74.478  17.133  1.00 69.26  ? 60  VAL   B CA     1 
ATOM   3869  C  C      . VAL   B 2  60  ? -20.108 -73.395  18.172  1.00 63.13  ? 60  VAL   B C      1 
ATOM   3870  O  O      . VAL   B 2  60  ? -21.038 -73.526  18.976  1.00 59.70  ? 60  VAL   B O      1 
ATOM   3871  C  CB     . VAL   B 2  60  ? -21.070 -74.687  16.242  1.00 68.55  ? 60  VAL   B CB     1 
ATOM   3872  C  CG1    . VAL   B 2  60  ? -21.318 -73.443  15.422  1.00 67.16  ? 60  VAL   B CG1    1 
ATOM   3873  C  CG2    . VAL   B 2  60  ? -20.850 -75.883  15.332  1.00 68.94  ? 60  VAL   B CG2    1 
ATOM   3874  N  N      . PRO   B 2  61  ? -19.348 -72.299  18.178  1.00 56.72  ? 61  PRO   B N      1 
ATOM   3875  C  CA     . PRO   B 2  61  ? -19.545 -71.282  19.210  1.00 54.30  ? 61  PRO   B CA     1 
ATOM   3876  C  C      . PRO   B 2  61  ? -20.976 -70.774  19.209  1.00 53.30  ? 61  PRO   B C      1 
ATOM   3877  O  O      . PRO   B 2  61  ? -21.597 -70.589  18.161  1.00 57.09  ? 61  PRO   B O      1 
ATOM   3878  C  CB     . PRO   B 2  61  ? -18.536 -70.192  18.832  1.00 45.77  ? 61  PRO   B CB     1 
ATOM   3879  C  CG     . PRO   B 2  61  ? -17.489 -70.921  18.068  1.00 49.57  ? 61  PRO   B CG     1 
ATOM   3880  C  CD     . PRO   B 2  61  ? -18.230 -71.959  17.286  1.00 56.23  ? 61  PRO   B CD     1 
ATOM   3881  N  N      . ARG   B 2  62  ? -21.514 -70.590  20.410  1.00 50.42  ? 62  ARG   B N      1 
ATOM   3882  C  CA     . ARG   B 2  62  ? -22.848 -70.033  20.564  1.00 50.46  ? 62  ARG   B CA     1 
ATOM   3883  C  C      . ARG   B 2  62  ? -22.729 -68.510  20.444  1.00 50.59  ? 62  ARG   B C      1 
ATOM   3884  O  O      . ARG   B 2  62  ? -22.965 -67.740  21.383  1.00 51.79  ? 62  ARG   B O      1 
ATOM   3885  C  CB     . ARG   B 2  62  ? -23.460 -70.499  21.879  1.00 53.62  ? 62  ARG   B CB     1 
ATOM   3886  C  CG     . ARG   B 2  62  ? -24.984 -70.500  21.863  1.00 58.35  ? 62  ARG   B CG     1 
ATOM   3887  C  CD     . ARG   B 2  62  ? -25.569 -71.047  23.129  1.00 56.36  ? 62  ARG   B CD     1 
ATOM   3888  N  NE     . ARG   B 2  62  ? -25.294 -72.471  23.272  1.00 62.18  ? 62  ARG   B NE     1 
ATOM   3889  C  CZ     . ARG   B 2  62  ? -24.313 -72.959  24.014  1.00 60.62  ? 62  ARG   B CZ     1 
ATOM   3890  N  NH1    . ARG   B 2  62  ? -23.443 -72.161  24.607  1.00 62.96  ? 62  ARG   B NH1    1 
ATOM   3891  N  NH2    . ARG   B 2  62  ? -24.211 -74.277  24.180  1.00 52.65  ? 62  ARG   B NH2    1 
ATOM   3892  N  N      . ALA   B 2  63  ? -22.325 -68.079  19.244  1.00 48.68  ? 63  ALA   B N      1 
ATOM   3893  C  CA     . ALA   B 2  63  ? -21.972 -66.687  18.974  1.00 48.41  ? 63  ALA   B CA     1 
ATOM   3894  C  C      . ALA   B 2  63  ? -22.826 -66.110  17.855  1.00 50.24  ? 63  ALA   B C      1 
ATOM   3895  O  O      . ALA   B 2  63  ? -22.940 -66.697  16.772  1.00 47.64  ? 63  ALA   B O      1 
ATOM   3896  C  CB     . ALA   B 2  63  ? -20.498 -66.541  18.594  1.00 47.63  ? 63  ALA   B CB     1 
ATOM   3897  N  N      . ILE   B 2  64  ? -23.388 -64.943  18.120  1.00 43.07  ? 64  ILE   B N      1 
ATOM   3898  C  CA     . ILE   B 2  64  ? -24.136 -64.175  17.148  1.00 42.95  ? 64  ILE   B CA     1 
ATOM   3899  C  C      . ILE   B 2  64  ? -23.278 -62.981  16.782  1.00 45.20  ? 64  ILE   B C      1 
ATOM   3900  O  O      . ILE   B 2  64  ? -22.887 -62.211  17.666  1.00 43.01  ? 64  ILE   B O      1 
ATOM   3901  C  CB     . ILE   B 2  64  ? -25.471 -63.720  17.732  1.00 42.18  ? 64  ILE   B CB     1 
ATOM   3902  C  CG1    . ILE   B 2  64  ? -26.266 -64.943  18.185  1.00 43.62  ? 64  ILE   B CG1    1 
ATOM   3903  C  CG2    . ILE   B 2  64  ? -26.194 -62.861  16.733  1.00 39.81  ? 64  ILE   B CG2    1 
ATOM   3904  C  CD1    . ILE   B 2  64  ? -27.463 -64.624  19.041  1.00 44.80  ? 64  ILE   B CD1    1 
ATOM   3905  N  N      . LEU   B 2  65  ? -22.967 -62.835  15.491  1.00 46.73  ? 65  LEU   B N      1 
ATOM   3906  C  CA     . LEU   B 2  65  ? -22.105 -61.763  14.993  1.00 43.88  ? 65  LEU   B CA     1 
ATOM   3907  C  C      . LEU   B 2  65  ? -22.940 -60.681  14.327  1.00 49.44  ? 65  LEU   B C      1 
ATOM   3908  O  O      . LEU   B 2  65  ? -23.628 -60.948  13.338  1.00 51.59  ? 65  LEU   B O      1 
ATOM   3909  C  CB     . LEU   B 2  65  ? -21.072 -62.313  14.017  1.00 44.78  ? 65  LEU   B CB     1 
ATOM   3910  C  CG     . LEU   B 2  65  ? -20.007 -63.197  14.647  1.00 47.67  ? 65  LEU   B CG     1 
ATOM   3911  C  CD1    . LEU   B 2  65  ? -20.456 -64.617  14.669  1.00 49.55  ? 65  LEU   B CD1    1 
ATOM   3912  C  CD2    . LEU   B 2  65  ? -18.753 -63.086  13.804  1.00 42.44  ? 65  LEU   B CD2    1 
ATOM   3913  N  N      . VAL   B 2  66  ? -22.824 -59.453  14.837  1.00 47.86  ? 66  VAL   B N      1 
ATOM   3914  C  CA     . VAL   B 2  66  ? -23.755 -58.367  14.559  1.00 40.40  ? 66  VAL   B CA     1 
ATOM   3915  C  C      . VAL   B 2  66  ? -22.995 -57.107  14.183  1.00 40.14  ? 66  VAL   B C      1 
ATOM   3916  O  O      . VAL   B 2  66  ? -22.058 -56.708  14.879  1.00 43.18  ? 66  VAL   B O      1 
ATOM   3917  C  CB     . VAL   B 2  66  ? -24.627 -58.083  15.784  1.00 45.09  ? 66  VAL   B CB     1 
ATOM   3918  C  CG1    . VAL   B 2  66  ? -25.496 -56.942  15.487  1.00 45.48  ? 66  VAL   B CG1    1 
ATOM   3919  C  CG2    . VAL   B 2  66  ? -25.423 -59.319  16.169  1.00 43.31  ? 66  VAL   B CG2    1 
ATOM   3920  N  N      . ASP   B 2  67  ? -23.422 -56.453  13.113  1.00 46.09  ? 67  ASP   B N      1 
ATOM   3921  C  CA     . ASP   B 2  67  ? -22.768 -55.208  12.727  1.00 43.87  ? 67  ASP   B CA     1 
ATOM   3922  C  C      . ASP   B 2  67  ? -23.665 -54.502  11.709  1.00 40.86  ? 67  ASP   B C      1 
ATOM   3923  O  O      . ASP   B 2  67  ? -24.492 -55.137  11.055  1.00 41.31  ? 67  ASP   B O      1 
ATOM   3924  C  CB     . ASP   B 2  67  ? -21.362 -55.482  12.171  1.00 37.35  ? 67  ASP   B CB     1 
ATOM   3925  C  CG     . ASP   B 2  67  ? -20.446 -54.254  12.219  1.00 43.28  ? 67  ASP   B CG     1 
ATOM   3926  O  OD1    . ASP   B 2  67  ? -20.922 -53.125  12.569  1.00 38.46  ? 67  ASP   B OD1    1 
ATOM   3927  O  OD2    . ASP   B 2  67  ? -19.239 -54.440  11.896  1.00 43.28  ? 67  ASP   B OD2    1 
ATOM   3928  N  N      . LEU   B 2  68  ? -23.536 -53.187  11.615  1.00 38.16  ? 68  LEU   B N      1 
ATOM   3929  C  CA     . LEU   B 2  68  ? -24.340 -52.416  10.670  1.00 40.71  ? 68  LEU   B CA     1 
ATOM   3930  C  C      . LEU   B 2  68  ? -23.634 -52.195  9.327   1.00 51.23  ? 68  LEU   B C      1 
ATOM   3931  O  O      . LEU   B 2  68  ? -24.196 -51.557  8.431   1.00 54.71  ? 68  LEU   B O      1 
ATOM   3932  C  CB     . LEU   B 2  68  ? -24.717 -51.073  11.301  1.00 34.95  ? 68  LEU   B CB     1 
ATOM   3933  C  CG     . LEU   B 2  68  ? -25.922 -51.238  12.220  1.00 36.77  ? 68  LEU   B CG     1 
ATOM   3934  C  CD1    . LEU   B 2  68  ? -26.369 -49.941  12.841  1.00 36.32  ? 68  LEU   B CD1    1 
ATOM   3935  C  CD2    . LEU   B 2  68  ? -27.052 -51.864  11.446  1.00 37.41  ? 68  LEU   B CD2    1 
ATOM   3936  N  N      . GLU   B 2  69  ? -22.436 -52.751  9.163   1.00 49.97  ? 69  GLU   B N      1 
ATOM   3937  C  CA     . GLU   B 2  69  ? -21.466 -52.506  8.132   1.00 47.76  ? 69  GLU   B CA     1 
ATOM   3938  C  C      . GLU   B 2  69  ? -20.883 -53.883  7.876   1.00 52.08  ? 69  GLU   B C      1 
ATOM   3939  O  O      . GLU   B 2  69  ? -20.675 -54.636  8.834   1.00 54.18  ? 69  GLU   B O      1 
ATOM   3940  C  CB     . GLU   B 2  69  ? -20.394 -51.538  8.649   1.00 46.86  ? 69  GLU   B CB     1 
ATOM   3941  C  CG     . GLU   B 2  69  ? -19.319 -51.097  7.707   1.00 51.89  ? 69  GLU   B CG     1 
ATOM   3942  C  CD     . GLU   B 2  69  ? -18.811 -49.710  8.080   1.00 72.15  ? 69  GLU   B CD     1 
ATOM   3943  O  OE1    . GLU   B 2  69  ? -19.412 -48.696  7.654   1.00 75.52  ? 69  GLU   B OE1    1 
ATOM   3944  O  OE2    . GLU   B 2  69  ? -17.823 -49.628  8.839   1.00 86.05  ? 69  GLU   B OE2    1 
ATOM   3945  N  N      . PRO   B 2  70  ? -20.615 -54.255  6.622   1.00 54.72  ? 70  PRO   B N      1 
ATOM   3946  C  CA     . PRO   B 2  70  ? -20.090 -55.603  6.351   1.00 55.58  ? 70  PRO   B CA     1 
ATOM   3947  C  C      . PRO   B 2  70  ? -18.590 -55.720  6.494   1.00 59.47  ? 70  PRO   B C      1 
ATOM   3948  O  O      . PRO   B 2  70  ? -18.079 -56.848  6.489   1.00 65.18  ? 70  PRO   B O      1 
ATOM   3949  C  CB     . PRO   B 2  70  ? -20.510 -55.864  4.899   1.00 57.63  ? 70  PRO   B CB     1 
ATOM   3950  C  CG     . PRO   B 2  70  ? -21.111 -54.579  4.403   1.00 59.42  ? 70  PRO   B CG     1 
ATOM   3951  C  CD     . PRO   B 2  70  ? -20.770 -53.494  5.385   1.00 58.11  ? 70  PRO   B CD     1 
ATOM   3952  N  N      . GLY   B 2  71  ? -17.878 -54.601  6.625   1.00 53.45  ? 71  GLY   B N      1 
ATOM   3953  C  CA     . GLY   B 2  71  ? -16.429 -54.582  6.777   1.00 59.40  ? 71  GLY   B CA     1 
ATOM   3954  C  C      . GLY   B 2  71  ? -15.804 -55.547  7.774   1.00 64.14  ? 71  GLY   B C      1 
ATOM   3955  O  O      . GLY   B 2  71  ? -15.307 -56.612  7.382   1.00 61.58  ? 71  GLY   B O      1 
ATOM   3956  N  N      . THR   B 2  72  ? -15.799 -55.175  9.064   1.00 70.88  ? 72  THR   B N      1 
ATOM   3957  C  CA     . THR   B 2  72  ? -15.189 -56.024  10.093  1.00 70.47  ? 72  THR   B CA     1 
ATOM   3958  C  C      . THR   B 2  72  ? -15.738 -57.446  10.044  1.00 65.22  ? 72  THR   B C      1 
ATOM   3959  O  O      . THR   B 2  72  ? -14.982 -58.408  10.224  1.00 64.13  ? 72  THR   B O      1 
ATOM   3960  C  CB     . THR   B 2  72  ? -15.381 -55.430  11.513  1.00 63.84  ? 72  THR   B CB     1 
ATOM   3961  O  OG1    . THR   B 2  72  ? -14.744 -54.145  11.617  1.00 61.44  ? 72  THR   B OG1    1 
ATOM   3962  C  CG2    . THR   B 2  72  ? -14.789 -56.356  12.597  1.00 56.40  ? 72  THR   B CG2    1 
ATOM   3963  N  N      . MET   B 2  73  ? -17.032 -57.614  9.792   1.00 59.63  ? 73  MET   B N      1 
ATOM   3964  C  CA     . MET   B 2  73  ? -17.530 -58.979  9.790   1.00 65.40  ? 73  MET   B CA     1 
ATOM   3965  C  C      . MET   B 2  73  ? -17.101 -59.794  8.571   1.00 66.42  ? 73  MET   B C      1 
ATOM   3966  O  O      . MET   B 2  73  ? -17.083 -61.027  8.655   1.00 68.33  ? 73  MET   B O      1 
ATOM   3967  C  CB     . MET   B 2  73  ? -19.041 -58.999  9.921   1.00 70.66  ? 73  MET   B CB     1 
ATOM   3968  C  CG     . MET   B 2  73  ? -19.508 -59.113  11.360  1.00 57.43  ? 73  MET   B CG     1 
ATOM   3969  S  SD     . MET   B 2  73  ? -21.295 -58.995  11.362  1.00 62.83  ? 73  MET   B SD     1 
ATOM   3970  C  CE     . MET   B 2  73  ? -21.653 -60.210  10.078  1.00 57.04  ? 73  MET   B CE     1 
ATOM   3971  N  N      . ASP   B 2  74  ? -16.735 -59.169  7.450   1.00 62.83  ? 74  ASP   B N      1 
ATOM   3972  C  CA     . ASP   B 2  74  ? -16.055 -59.950  6.420   1.00 61.15  ? 74  ASP   B CA     1 
ATOM   3973  C  C      . ASP   B 2  74  ? -14.669 -60.378  6.877   1.00 64.26  ? 74  ASP   B C      1 
ATOM   3974  O  O      . ASP   B 2  74  ? -14.251 -61.511  6.621   1.00 61.49  ? 74  ASP   B O      1 
ATOM   3975  C  CB     . ASP   B 2  74  ? -15.955 -59.173  5.119   1.00 65.37  ? 74  ASP   B CB     1 
ATOM   3976  C  CG     . ASP   B 2  74  ? -17.183 -59.310  4.286   1.00 66.86  ? 74  ASP   B CG     1 
ATOM   3977  O  OD1    . ASP   B 2  74  ? -17.761 -60.421  4.287   1.00 68.54  ? 74  ASP   B OD1    1 
ATOM   3978  O  OD2    . ASP   B 2  74  ? -17.559 -58.320  3.626   1.00 65.48  ? 74  ASP   B OD2    1 
ATOM   3979  N  N      . SER   B 2  75  ? -13.932 -59.479  7.535   1.00 66.52  ? 75  SER   B N      1 
ATOM   3980  C  CA     . SER   B 2  75  ? -12.657 -59.849  8.137   1.00 62.47  ? 75  SER   B CA     1 
ATOM   3981  C  C      . SER   B 2  75  ? -12.818 -61.074  9.019   1.00 64.15  ? 75  SER   B C      1 
ATOM   3982  O  O      . SER   B 2  75  ? -12.189 -62.113  8.801   1.00 67.06  ? 75  SER   B O      1 
ATOM   3983  C  CB     . SER   B 2  75  ? -12.107 -58.693  8.967   1.00 64.39  ? 75  SER   B CB     1 
ATOM   3984  O  OG     . SER   B 2  75  ? -11.837 -57.562  8.165   1.00 82.94  ? 75  SER   B OG     1 
ATOM   3985  N  N      . VAL   B 2  76  ? -13.664 -60.958  10.036  1.00 61.04  ? 76  VAL   B N      1 
ATOM   3986  C  CA     . VAL   B 2  76  ? -13.792 -62.036  11.001  1.00 61.45  ? 76  VAL   B CA     1 
ATOM   3987  C  C      . VAL   B 2  76  ? -13.954 -63.368  10.287  1.00 63.98  ? 76  VAL   B C      1 
ATOM   3988  O  O      . VAL   B 2  76  ? -13.366 -64.376  10.696  1.00 69.51  ? 76  VAL   B O      1 
ATOM   3989  C  CB     . VAL   B 2  76  ? -14.944 -61.730  11.971  1.00 58.56  ? 76  VAL   B CB     1 
ATOM   3990  C  CG1    . VAL   B 2  76  ? -15.233 -62.913  12.864  1.00 57.72  ? 76  VAL   B CG1    1 
ATOM   3991  C  CG2    . VAL   B 2  76  ? -14.540 -60.553  12.818  1.00 55.09  ? 76  VAL   B CG2    1 
ATOM   3992  N  N      . ARG   B 2  77  ? -14.702 -63.388  9.178   1.00 60.83  ? 77  ARG   B N      1 
ATOM   3993  C  CA     . ARG   B 2  77  ? -14.860 -64.637  8.432   1.00 64.36  ? 77  ARG   B CA     1 
ATOM   3994  C  C      . ARG   B 2  77  ? -13.561 -65.064  7.762   1.00 65.51  ? 77  ARG   B C      1 
ATOM   3995  O  O      . ARG   B 2  77  ? -13.220 -66.252  7.761   1.00 66.62  ? 77  ARG   B O      1 
ATOM   3996  C  CB     . ARG   B 2  77  ? -15.959 -64.497  7.397   1.00 57.68  ? 77  ARG   B CB     1 
ATOM   3997  C  CG     . ARG   B 2  77  ? -16.434 -65.801  6.810   1.00 54.23  ? 77  ARG   B CG     1 
ATOM   3998  C  CD     . ARG   B 2  77  ? -17.913 -65.650  6.673   1.00 60.44  ? 77  ARG   B CD     1 
ATOM   3999  N  NE     . ARG   B 2  77  ? -18.197 -64.307  6.190   1.00 63.30  ? 77  ARG   B NE     1 
ATOM   4000  C  CZ     . ARG   B 2  77  ? -19.409 -63.779  6.115   1.00 62.97  ? 77  ARG   B CZ     1 
ATOM   4001  N  NH1    . ARG   B 2  77  ? -20.471 -64.429  6.569   1.00 60.86  ? 77  ARG   B NH1    1 
ATOM   4002  N  NH2    . ARG   B 2  77  ? -19.554 -62.553  5.613   1.00 61.20  ? 77  ARG   B NH2    1 
ATOM   4003  N  N      . SER   B 2  78  ? -12.829 -64.112  7.186   1.00 68.55  ? 78  SER   B N      1 
ATOM   4004  C  CA     . SER   B 2  78  ? -11.547 -64.390  6.549   1.00 68.96  ? 78  SER   B CA     1 
ATOM   4005  C  C      . SER   B 2  78  ? -10.495 -64.884  7.536   1.00 68.44  ? 78  SER   B C      1 
ATOM   4006  O  O      . SER   B 2  78  ? -9.502  -65.492  7.118   1.00 69.02  ? 78  SER   B O      1 
ATOM   4007  C  CB     . SER   B 2  78  ? -11.035 -63.119  5.869   1.00 68.15  ? 78  SER   B CB     1 
ATOM   4008  O  OG     . SER   B 2  78  ? -11.855 -62.745  4.776   1.00 72.72  ? 78  SER   B OG     1 
ATOM   4009  N  N      . GLY   B 2  79  ? -10.689 -64.628  8.825   1.00 64.69  ? 79  GLY   B N      1 
ATOM   4010  C  CA     . GLY   B 2  79  ? -9.632  -64.768  9.792   1.00 67.60  ? 79  GLY   B CA     1 
ATOM   4011  C  C      . GLY   B 2  79  ? -9.416  -66.196  10.224  1.00 66.92  ? 79  GLY   B C      1 
ATOM   4012  O  O      . GLY   B 2  79  ? -10.074 -67.137  9.767   1.00 65.28  ? 79  GLY   B O      1 
ATOM   4013  N  N      . PRO   B 2  80  ? -8.498  -66.357  11.182  1.00 73.92  ? 80  PRO   B N      1 
ATOM   4014  C  CA     . PRO   B 2  80  ? -7.971  -67.704  11.497  1.00 82.08  ? 80  PRO   B CA     1 
ATOM   4015  C  C      . PRO   B 2  80  ? -8.998  -68.697  12.039  1.00 80.37  ? 80  PRO   B C      1 
ATOM   4016  O  O      . PRO   B 2  80  ? -8.920  -69.900  11.731  1.00 73.59  ? 80  PRO   B O      1 
ATOM   4017  C  CB     . PRO   B 2  80  ? -6.867  -67.398  12.521  1.00 73.06  ? 80  PRO   B CB     1 
ATOM   4018  C  CG     . PRO   B 2  80  ? -7.264  -66.071  13.134  1.00 65.72  ? 80  PRO   B CG     1 
ATOM   4019  C  CD     . PRO   B 2  80  ? -7.914  -65.303  12.033  1.00 66.00  ? 80  PRO   B CD     1 
ATOM   4020  N  N      . PHE   B 2  81  ? -9.935  -68.231  12.865  1.00 72.43  ? 81  PHE   B N      1 
ATOM   4021  C  CA     . PHE   B 2  81  ? -11.017 -69.050  13.388  1.00 66.33  ? 81  PHE   B CA     1 
ATOM   4022  C  C      . PHE   B 2  81  ? -12.365 -68.658  12.794  1.00 64.49  ? 81  PHE   B C      1 
ATOM   4023  O  O      . PHE   B 2  81  ? -13.407 -69.034  13.336  1.00 57.08  ? 81  PHE   B O      1 
ATOM   4024  C  CB     . PHE   B 2  81  ? -11.042 -68.955  14.916  1.00 74.44  ? 81  PHE   B CB     1 
ATOM   4025  C  CG     . PHE   B 2  81  ? -10.170 -69.972  15.612  1.00 70.86  ? 81  PHE   B CG     1 
ATOM   4026  C  CD1    . PHE   B 2  81  ? -8.800  -69.787  15.707  1.00 68.08  ? 81  PHE   B CD1    1 
ATOM   4027  C  CD2    . PHE   B 2  81  ? -10.735 -71.093  16.215  1.00 70.05  ? 81  PHE   B CD2    1 
ATOM   4028  C  CE1    . PHE   B 2  81  ? -7.996  -70.723  16.358  1.00 74.42  ? 81  PHE   B CE1    1 
ATOM   4029  C  CE2    . PHE   B 2  81  ? -9.938  -72.038  16.864  1.00 70.51  ? 81  PHE   B CE2    1 
ATOM   4030  C  CZ     . PHE   B 2  81  ? -8.565  -71.851  16.934  1.00 72.18  ? 81  PHE   B CZ     1 
ATOM   4031  N  N      . GLY   B 2  82  ? -12.360 -67.909  11.686  1.00 66.89  ? 82  GLY   B N      1 
ATOM   4032  C  CA     . GLY   B 2  82  ? -13.611 -67.447  11.107  1.00 61.14  ? 82  GLY   B CA     1 
ATOM   4033  C  C      . GLY   B 2  82  ? -14.538 -68.582  10.715  1.00 63.28  ? 82  GLY   B C      1 
ATOM   4034  O  O      . GLY   B 2  82  ? -15.736 -68.558  11.014  1.00 63.82  ? 82  GLY   B O      1 
ATOM   4035  N  N      . GLN   B 2  83  ? -13.999 -69.595  10.047  1.00 62.57  ? 83  GLN   B N      1 
ATOM   4036  C  CA     . GLN   B 2  83  ? -14.828 -70.701  9.597   1.00 62.96  ? 83  GLN   B CA     1 
ATOM   4037  C  C      . GLN   B 2  83  ? -15.496 -71.438  10.748  1.00 65.86  ? 83  GLN   B C      1 
ATOM   4038  O  O      . GLN   B 2  83  ? -16.450 -72.187  10.521  1.00 69.42  ? 83  GLN   B O      1 
ATOM   4039  C  CB     . GLN   B 2  83  ? -13.981 -71.665  8.775   1.00 77.39  ? 83  GLN   B CB     1 
ATOM   4040  C  CG     . GLN   B 2  83  ? -13.215 -70.975  7.657   1.00 88.07  ? 83  GLN   B CG     1 
ATOM   4041  C  CD     . GLN   B 2  83  ? -14.142 -70.250  6.700   1.00 86.14  ? 83  GLN   B CD     1 
ATOM   4042  O  OE1    . GLN   B 2  83  ? -15.007 -70.866  6.087   1.00 95.29  ? 83  GLN   B OE1    1 
ATOM   4043  N  NE2    . GLN   B 2  83  ? -13.978 -68.936  6.584   1.00 79.00  ? 83  GLN   B NE2    1 
ATOM   4044  N  N      . ILE   B 2  84  ? -15.025 -71.260  11.979  1.00 66.36  ? 84  ILE   B N      1 
ATOM   4045  C  CA     . ILE   B 2  84  ? -15.678 -71.966  13.073  1.00 63.15  ? 84  ILE   B CA     1 
ATOM   4046  C  C      . ILE   B 2  84  ? -17.078 -71.427  13.287  1.00 58.56  ? 84  ILE   B C      1 
ATOM   4047  O  O      . ILE   B 2  84  ? -17.978 -72.180  13.668  1.00 57.53  ? 84  ILE   B O      1 
ATOM   4048  C  CB     . ILE   B 2  84  ? -14.840 -71.898  14.369  1.00 65.30  ? 84  ILE   B CB     1 
ATOM   4049  C  CG1    . ILE   B 2  84  ? -15.299 -72.971  15.354  1.00 63.75  ? 84  ILE   B CG1    1 
ATOM   4050  C  CG2    . ILE   B 2  84  ? -14.948 -70.545  15.034  1.00 59.55  ? 84  ILE   B CG2    1 
ATOM   4051  C  CD1    . ILE   B 2  84  ? -14.315 -73.212  16.456  1.00 66.51  ? 84  ILE   B CD1    1 
ATOM   4052  N  N      . PHE   B 2  85  ? -17.295 -70.137  13.031  1.00 61.51  ? 85  PHE   B N      1 
ATOM   4053  C  CA     . PHE   B 2  85  ? -18.571 -69.514  13.363  1.00 59.68  ? 85  PHE   B CA     1 
ATOM   4054  C  C      . PHE   B 2  85  ? -19.699 -69.998  12.467  1.00 62.92  ? 85  PHE   B C      1 
ATOM   4055  O  O      . PHE   B 2  85  ? -19.514 -70.218  11.265  1.00 65.79  ? 85  PHE   B O      1 
ATOM   4056  C  CB     . PHE   B 2  85  ? -18.468 -67.992  13.299  1.00 48.88  ? 85  PHE   B CB     1 
ATOM   4057  C  CG     . PHE   B 2  85  ? -17.572 -67.418  14.345  1.00 50.32  ? 85  PHE   B CG     1 
ATOM   4058  C  CD1    . PHE   B 2  85  ? -18.049 -67.225  15.636  1.00 45.66  ? 85  PHE   B CD1    1 
ATOM   4059  C  CD2    . PHE   B 2  85  ? -16.258 -67.090  14.061  1.00 54.60  ? 85  PHE   B CD2    1 
ATOM   4060  C  CE1    . PHE   B 2  85  ? -17.239 -66.719  16.618  1.00 43.80  ? 85  PHE   B CE1    1 
ATOM   4061  C  CE2    . PHE   B 2  85  ? -15.436 -66.566  15.049  1.00 53.43  ? 85  PHE   B CE2    1 
ATOM   4062  C  CZ     . PHE   B 2  85  ? -15.927 -66.386  16.331  1.00 46.33  ? 85  PHE   B CZ     1 
ATOM   4063  N  N      . ARG   B 2  86  ? -20.874 -70.161  13.079  1.00 55.33  ? 86  ARG   B N      1 
ATOM   4064  C  CA     . ARG   B 2  86  ? -22.074 -70.609  12.390  1.00 53.49  ? 86  ARG   B CA     1 
ATOM   4065  C  C      . ARG   B 2  86  ? -22.555 -69.574  11.380  1.00 57.39  ? 86  ARG   B C      1 
ATOM   4066  O  O      . ARG   B 2  86  ? -23.011 -68.495  11.784  1.00 53.84  ? 86  ARG   B O      1 
ATOM   4067  C  CB     . ARG   B 2  86  ? -23.163 -70.884  13.398  1.00 57.03  ? 86  ARG   B CB     1 
ATOM   4068  C  CG     . ARG   B 2  86  ? -24.522 -71.008  12.756  1.00 60.14  ? 86  ARG   B CG     1 
ATOM   4069  C  CD     . ARG   B 2  86  ? -25.571 -71.382  13.764  1.00 61.75  ? 86  ARG   B CD     1 
ATOM   4070  N  NE     . ARG   B 2  86  ? -26.843 -71.598  13.097  1.00 66.28  ? 86  ARG   B NE     1 
ATOM   4071  C  CZ     . ARG   B 2  86  ? -27.320 -72.803  12.824  1.00 73.42  ? 86  ARG   B CZ     1 
ATOM   4072  N  NH1    . ARG   B 2  86  ? -26.647 -73.898  13.148  1.00 72.01  ? 86  ARG   B NH1    1 
ATOM   4073  N  NH2    . ARG   B 2  86  ? -28.487 -72.912  12.196  1.00 73.81  ? 86  ARG   B NH2    1 
ATOM   4074  N  N      . PRO   B 2  87  ? -22.530 -69.875  10.073  1.00 57.24  ? 87  PRO   B N      1 
ATOM   4075  C  CA     . PRO   B 2  87  ? -22.780 -68.820  9.079   1.00 52.69  ? 87  PRO   B CA     1 
ATOM   4076  C  C      . PRO   B 2  87  ? -24.125 -68.138  9.251   1.00 56.97  ? 87  PRO   B C      1 
ATOM   4077  O  O      . PRO   B 2  87  ? -24.208 -66.909  9.124   1.00 57.61  ? 87  PRO   B O      1 
ATOM   4078  C  CB     . PRO   B 2  87  ? -22.680 -69.577  7.750   1.00 48.66  ? 87  PRO   B CB     1 
ATOM   4079  C  CG     . PRO   B 2  87  ? -22.998 -70.975  8.108   1.00 50.36  ? 87  PRO   B CG     1 
ATOM   4080  C  CD     . PRO   B 2  87  ? -22.367 -71.189  9.434   1.00 54.83  ? 87  PRO   B CD     1 
ATOM   4081  N  N      . ASP   B 2  88  ? -25.185 -68.883  9.566   1.00 53.06  ? 88  ASP   B N      1 
ATOM   4082  C  CA     . ASP   B 2  88  ? -26.453 -68.201  9.781   1.00 52.93  ? 88  ASP   B CA     1 
ATOM   4083  C  C      . ASP   B 2  88  ? -26.396 -67.142  10.871  1.00 55.87  ? 88  ASP   B C      1 
ATOM   4084  O  O      . ASP   B 2  88  ? -27.373 -66.399  11.026  1.00 55.26  ? 88  ASP   B O      1 
ATOM   4085  C  CB     . ASP   B 2  88  ? -27.553 -69.189  10.134  1.00 61.69  ? 88  ASP   B CB     1 
ATOM   4086  C  CG     . ASP   B 2  88  ? -27.970 -70.006  8.963   1.00 71.39  ? 88  ASP   B CG     1 
ATOM   4087  O  OD1    . ASP   B 2  88  ? -28.457 -69.400  7.981   1.00 74.90  ? 88  ASP   B OD1    1 
ATOM   4088  O  OD2    . ASP   B 2  88  ? -27.831 -71.244  9.032   1.00 73.63  ? 88  ASP   B OD2    1 
ATOM   4089  N  N      . ASN   B 2  89  ? -25.307 -67.052  11.641  1.00 55.30  ? 89  ASN   B N      1 
ATOM   4090  C  CA     . ASN   B 2  89  ? -25.237 -66.097  12.743  1.00 56.71  ? 89  ASN   B CA     1 
ATOM   4091  C  C      . ASN   B 2  89  ? -24.479 -64.824  12.402  1.00 55.10  ? 89  ASN   B C      1 
ATOM   4092  O  O      . ASN   B 2  89  ? -24.204 -64.020  13.305  1.00 52.47  ? 89  ASN   B O      1 
ATOM   4093  C  CB     . ASN   B 2  89  ? -24.615 -66.733  13.990  1.00 53.71  ? 89  ASN   B CB     1 
ATOM   4094  C  CG     . ASN   B 2  89  ? -25.473 -67.807  14.595  1.00 54.38  ? 89  ASN   B CG     1 
ATOM   4095  O  OD1    . ASN   B 2  89  ? -26.421 -68.295  13.983  1.00 57.76  ? 89  ASN   B OD1    1 
ATOM   4096  N  ND2    . ASN   B 2  89  ? -25.156 -68.167  15.832  1.00 57.75  ? 89  ASN   B ND2    1 
ATOM   4097  N  N      . PHE   B 2  90  ? -24.128 -64.622  11.137  1.00 52.65  ? 90  PHE   B N      1 
ATOM   4098  C  CA     . PHE   B 2  90  ? -23.565 -63.348  10.701  1.00 50.29  ? 90  PHE   B CA     1 
ATOM   4099  C  C      . PHE   B 2  90  ? -24.737 -62.465  10.282  1.00 49.65  ? 90  PHE   B C      1 
ATOM   4100  O  O      . PHE   B 2  90  ? -25.182 -62.490  9.143   1.00 54.61  ? 90  PHE   B O      1 
ATOM   4101  C  CB     . PHE   B 2  90  ? -22.570 -63.569  9.575   1.00 49.27  ? 90  PHE   B CB     1 
ATOM   4102  C  CG     . PHE   B 2  90  ? -21.279 -64.228  10.006  1.00 54.97  ? 90  PHE   B CG     1 
ATOM   4103  C  CD1    . PHE   B 2  90  ? -21.237 -65.578  10.305  1.00 55.07  ? 90  PHE   B CD1    1 
ATOM   4104  C  CD2    . PHE   B 2  90  ? -20.093 -63.505  10.035  1.00 56.06  ? 90  PHE   B CD2    1 
ATOM   4105  C  CE1    . PHE   B 2  90  ? -20.044 -66.186  10.663  1.00 55.40  ? 90  PHE   B CE1    1 
ATOM   4106  C  CE2    . PHE   B 2  90  ? -18.902 -64.103  10.387  1.00 52.67  ? 90  PHE   B CE2    1 
ATOM   4107  C  CZ     . PHE   B 2  90  ? -18.876 -65.444  10.697  1.00 58.83  ? 90  PHE   B CZ     1 
ATOM   4108  N  N      . VAL   B 2  91  ? -25.277 -61.701  11.222  1.00 47.36  ? 91  VAL   B N      1 
ATOM   4109  C  CA     . VAL   B 2  91  ? -26.408 -60.815  10.961  1.00 49.07  ? 91  VAL   B CA     1 
ATOM   4110  C  C      . VAL   B 2  91  ? -25.861 -59.411  10.760  1.00 56.94  ? 91  VAL   B C      1 
ATOM   4111  O  O      . VAL   B 2  91  ? -25.301 -58.822  11.695  1.00 57.71  ? 91  VAL   B O      1 
ATOM   4112  C  CB     . VAL   B 2  91  ? -27.432 -60.838  12.104  1.00 45.77  ? 91  VAL   B CB     1 
ATOM   4113  C  CG1    . VAL   B 2  91  ? -28.533 -59.880  11.815  1.00 46.75  ? 91  VAL   B CG1    1 
ATOM   4114  C  CG2    . VAL   B 2  91  ? -28.007 -62.198  12.249  1.00 52.55  ? 91  VAL   B CG2    1 
ATOM   4115  N  N      . PHE   B 2  92  ? -26.024 -58.854  9.557   1.00 54.41  ? 92  PHE   B N      1 
ATOM   4116  C  CA     . PHE   B 2  92  ? -25.504 -57.513  9.337   1.00 56.31  ? 92  PHE   B CA     1 
ATOM   4117  C  C      . PHE   B 2  92  ? -26.365 -56.754  8.338   1.00 56.90  ? 92  PHE   B C      1 
ATOM   4118  O  O      . PHE   B 2  92  ? -27.077 -57.345  7.526   1.00 60.87  ? 92  PHE   B O      1 
ATOM   4119  C  CB     . PHE   B 2  92  ? -24.051 -57.532  8.847   1.00 52.34  ? 92  PHE   B CB     1 
ATOM   4120  C  CG     . PHE   B 2  92  ? -23.839 -58.314  7.585   1.00 63.60  ? 92  PHE   B CG     1 
ATOM   4121  C  CD1    . PHE   B 2  92  ? -23.526 -59.673  7.625   1.00 68.21  ? 92  PHE   B CD1    1 
ATOM   4122  C  CD2    . PHE   B 2  92  ? -23.944 -57.683  6.345   1.00 63.71  ? 92  PHE   B CD2    1 
ATOM   4123  C  CE1    . PHE   B 2  92  ? -23.314 -60.392  6.448   1.00 69.89  ? 92  PHE   B CE1    1 
ATOM   4124  C  CE2    . PHE   B 2  92  ? -23.746 -58.391  5.173   1.00 67.06  ? 92  PHE   B CE2    1 
ATOM   4125  C  CZ     . PHE   B 2  92  ? -23.428 -59.752  5.221   1.00 70.32  ? 92  PHE   B CZ     1 
ATOM   4126  N  N      . GLY   B 2  93  ? -26.295 -55.424  8.432   1.00 54.40  ? 93  GLY   B N      1 
ATOM   4127  C  CA     . GLY   B 2  93  ? -26.756 -54.526  7.398   1.00 55.39  ? 93  GLY   B CA     1 
ATOM   4128  C  C      . GLY   B 2  93  ? -25.602 -53.975  6.581   1.00 60.02  ? 93  GLY   B C      1 
ATOM   4129  O  O      . GLY   B 2  93  ? -24.482 -54.501  6.603   1.00 59.67  ? 93  GLY   B O      1 
ATOM   4130  N  N      . GLN   B 2  94  ? -25.875 -52.872  5.868   1.00 61.14  ? 94  GLN   B N      1 
ATOM   4131  C  CA     . GLN   B 2  94  ? -24.919 -52.277  4.932   1.00 54.55  ? 94  GLN   B CA     1 
ATOM   4132  C  C      . GLN   B 2  94  ? -24.658 -50.791  5.102   1.00 53.89  ? 94  GLN   B C      1 
ATOM   4133  O  O      . GLN   B 2  94  ? -23.612 -50.324  4.641   1.00 57.14  ? 94  GLN   B O      1 
ATOM   4134  C  CB     . GLN   B 2  94  ? -25.378 -52.495  3.488   1.00 55.41  ? 94  GLN   B CB     1 
ATOM   4135  C  CG     . GLN   B 2  94  ? -25.315 -53.908  2.984   1.00 62.61  ? 94  GLN   B CG     1 
ATOM   4136  C  CD     . GLN   B 2  94  ? -23.893 -54.282  2.642   1.00 67.78  ? 94  GLN   B CD     1 
ATOM   4137  O  OE1    . GLN   B 2  94  ? -23.072 -53.404  2.348   1.00 69.89  ? 94  GLN   B OE1    1 
ATOM   4138  N  NE2    . GLN   B 2  94  ? -23.600 -55.583  2.617   1.00 68.55  ? 94  GLN   B NE2    1 
ATOM   4139  N  N      . SER   B 2  95  ? -25.568 -50.026  5.701   1.00 58.28  ? 95  SER   B N      1 
ATOM   4140  C  CA     . SER   B 2  95  ? -25.385 -48.580  5.749   1.00 56.81  ? 95  SER   B CA     1 
ATOM   4141  C  C      . SER   B 2  95  ? -24.147 -48.212  6.540   1.00 59.02  ? 95  SER   B C      1 
ATOM   4142  O  O      . SER   B 2  95  ? -23.376 -47.337  6.136   1.00 62.75  ? 95  SER   B O      1 
ATOM   4143  C  CB     . SER   B 2  95  ? -26.603 -47.910  6.386   1.00 62.61  ? 95  SER   B CB     1 
ATOM   4144  O  OG     . SER   B 2  95  ? -27.744 -47.998  5.551   1.00 72.76  ? 95  SER   B OG     1 
ATOM   4145  N  N      . GLY   B 2  96  ? -23.938 -48.876  7.663   1.00 55.87  ? 96  GLY   B N      1 
ATOM   4146  C  CA     . GLY   B 2  96  ? -23.092 -48.344  8.701   1.00 47.53  ? 96  GLY   B CA     1 
ATOM   4147  C  C      . GLY   B 2  96  ? -23.892 -47.519  9.691   1.00 43.70  ? 96  GLY   B C      1 
ATOM   4148  O  O      . GLY   B 2  96  ? -24.986 -47.037  9.409   1.00 52.25  ? 96  GLY   B O      1 
ATOM   4149  N  N      . ALA   B 2  97  ? -23.334 -47.390  10.885  1.00 39.05  ? 97  ALA   B N      1 
ATOM   4150  C  CA     . ALA   B 2  97  ? -23.867 -46.548  11.944  1.00 36.11  ? 97  ALA   B CA     1 
ATOM   4151  C  C      . ALA   B 2  97  ? -23.064 -45.271  12.128  1.00 33.92  ? 97  ALA   B C      1 
ATOM   4152  O  O      . ALA   B 2  97  ? -23.385 -44.474  13.016  1.00 31.23  ? 97  ALA   B O      1 
ATOM   4153  C  CB     . ALA   B 2  97  ? -23.900 -47.328  13.268  1.00 35.11  ? 97  ALA   B CB     1 
ATOM   4154  N  N      . GLY   B 2  98  ? -21.998 -45.093  11.351  1.00 32.76  ? 98  GLY   B N      1 
ATOM   4155  C  CA     . GLY   B 2  98  ? -21.161 -43.914  11.384  1.00 31.92  ? 98  GLY   B CA     1 
ATOM   4156  C  C      . GLY   B 2  98  ? -20.786 -43.308  12.728  1.00 34.87  ? 98  GLY   B C      1 
ATOM   4157  O  O      . GLY   B 2  98  ? -21.020 -42.112  12.939  1.00 38.32  ? 98  GLY   B O      1 
ATOM   4158  N  N      . ASN   B 2  99  ? -20.168 -44.078  13.629  1.00 33.19  ? 99  ASN   B N      1 
ATOM   4159  C  CA     . ASN   B 2  99  ? -19.721 -43.540  14.922  1.00 32.57  ? 99  ASN   B CA     1 
ATOM   4160  C  C      . ASN   B 2  99  ? -20.790 -42.681  15.592  1.00 32.19  ? 99  ASN   B C      1 
ATOM   4161  O  O      . ASN   B 2  99  ? -20.491 -41.698  16.273  1.00 31.12  ? 99  ASN   B O      1 
ATOM   4162  C  CB     . ASN   B 2  99  ? -18.429 -42.748  14.765  1.00 29.87  ? 99  ASN   B CB     1 
ATOM   4163  C  CG     . ASN   B 2  99  ? -17.246 -43.628  14.441  1.00 38.53  ? 99  ASN   B CG     1 
ATOM   4164  O  OD1    . ASN   B 2  99  ? -16.910 -44.539  15.189  1.00 36.89  ? 99  ASN   B OD1    1 
ATOM   4165  N  ND2    . ASN   B 2  99  ? -16.587 -43.341  13.327  1.00 47.04  ? 99  ASN   B ND2    1 
ATOM   4166  N  N      . ASN   B 2  100 ? -22.048 -43.064  15.414  1.00 31.77  ? 100 ASN   B N      1 
ATOM   4167  C  CA     . ASN   B 2  100 ? -23.193 -42.276  15.843  1.00 32.55  ? 100 ASN   B CA     1 
ATOM   4168  C  C      . ASN   B 2  100 ? -24.099 -43.139  16.696  1.00 38.31  ? 100 ASN   B C      1 
ATOM   4169  O  O      . ASN   B 2  100 ? -24.683 -44.103  16.190  1.00 39.79  ? 100 ASN   B O      1 
ATOM   4170  C  CB     . ASN   B 2  100 ? -23.974 -41.763  14.643  1.00 32.99  ? 100 ASN   B CB     1 
ATOM   4171  C  CG     . ASN   B 2  100 ? -25.010 -40.760  15.033  1.00 37.77  ? 100 ASN   B CG     1 
ATOM   4172  O  OD1    . ASN   B 2  100 ? -25.644 -40.903  16.063  1.00 38.68  ? 100 ASN   B OD1    1 
ATOM   4173  N  ND2    . ASN   B 2  100 ? -25.235 -39.768  14.189  1.00 44.23  ? 100 ASN   B ND2    1 
ATOM   4174  N  N      . TRP   B 2  101 ? -24.253 -42.776  17.974  1.00 36.62  ? 101 TRP   B N      1 
ATOM   4175  C  CA     . TRP   B 2  101 ? -25.087 -43.576  18.868  1.00 33.28  ? 101 TRP   B CA     1 
ATOM   4176  C  C      . TRP   B 2  101 ? -26.551 -43.549  18.458  1.00 38.35  ? 101 TRP   B C      1 
ATOM   4177  O  O      . TRP   B 2  101 ? -27.248 -44.556  18.603  1.00 43.73  ? 101 TRP   B O      1 
ATOM   4178  C  CB     . TRP   B 2  101 ? -24.945 -43.098  20.306  1.00 35.03  ? 101 TRP   B CB     1 
ATOM   4179  C  CG     . TRP   B 2  101 ? -25.485 -44.072  21.343  1.00 41.15  ? 101 TRP   B CG     1 
ATOM   4180  C  CD1    . TRP   B 2  101 ? -24.814 -45.120  21.901  1.00 39.88  ? 101 TRP   B CD1    1 
ATOM   4181  C  CD2    . TRP   B 2  101 ? -26.780 -44.045  21.980  1.00 42.95  ? 101 TRP   B CD2    1 
ATOM   4182  N  NE1    . TRP   B 2  101 ? -25.610 -45.762  22.811  1.00 39.51  ? 101 TRP   B NE1    1 
ATOM   4183  C  CE2    . TRP   B 2  101 ? -26.817 -45.122  22.888  1.00 41.47  ? 101 TRP   B CE2    1 
ATOM   4184  C  CE3    . TRP   B 2  101 ? -27.912 -43.227  21.856  1.00 39.82  ? 101 TRP   B CE3    1 
ATOM   4185  C  CZ2    . TRP   B 2  101 ? -27.936 -45.408  23.667  1.00 41.07  ? 101 TRP   B CZ2    1 
ATOM   4186  C  CZ3    . TRP   B 2  101 ? -29.029 -43.512  22.630  1.00 38.66  ? 101 TRP   B CZ3    1 
ATOM   4187  C  CH2    . TRP   B 2  101 ? -29.030 -44.592  23.524  1.00 44.20  ? 101 TRP   B CH2    1 
ATOM   4188  N  N      . ALA   B 2  102 ? -27.049 -42.427  17.941  1.00 36.47  ? 102 ALA   B N      1 
ATOM   4189  C  CA     . ALA   B 2  102 ? -28.442 -42.414  17.512  1.00 33.63  ? 102 ALA   B CA     1 
ATOM   4190  C  C      . ALA   B 2  102 ? -28.651 -43.236  16.243  1.00 34.22  ? 102 ALA   B C      1 
ATOM   4191  O  O      . ALA   B 2  102 ? -29.719 -43.817  16.047  1.00 35.92  ? 102 ALA   B O      1 
ATOM   4192  C  CB     . ALA   B 2  102 ? -28.927 -40.979  17.328  1.00 31.58  ? 102 ALA   B CB     1 
ATOM   4193  N  N      . LYS   B 2  103 ? -27.656 -43.334  15.376  1.00 37.36  ? 103 LYS   B N      1 
ATOM   4194  C  CA     . LYS   B 2  103 ? -27.879 -44.173  14.202  1.00 38.53  ? 103 LYS   B CA     1 
ATOM   4195  C  C      . LYS   B 2  103 ? -28.040 -45.644  14.588  1.00 40.91  ? 103 LYS   B C      1 
ATOM   4196  O  O      . LYS   B 2  103 ? -28.696 -46.399  13.863  1.00 40.92  ? 103 LYS   B O      1 
ATOM   4197  C  CB     . LYS   B 2  103 ? -26.747 -44.004  13.184  1.00 34.65  ? 103 LYS   B CB     1 
ATOM   4198  C  CG     . LYS   B 2  103 ? -26.959 -42.831  12.242  1.00 37.12  ? 103 LYS   B CG     1 
ATOM   4199  C  CD     . LYS   B 2  103 ? -25.857 -42.707  11.218  1.00 34.98  ? 103 LYS   B CD     1 
ATOM   4200  C  CE     . LYS   B 2  103 ? -26.224 -41.693  10.170  1.00 44.22  ? 103 LYS   B CE     1 
ATOM   4201  N  NZ     . LYS   B 2  103 ? -25.542 -41.958  8.873   1.00 60.71  ? 103 LYS   B NZ     1 
ATOM   4202  N  N      . GLY   B 2  104 ? -27.462 -46.067  15.720  1.00 40.73  ? 104 GLY   B N      1 
ATOM   4203  C  CA     . GLY   B 2  104 ? -27.402 -47.468  16.100  1.00 37.96  ? 104 GLY   B CA     1 
ATOM   4204  C  C      . GLY   B 2  104 ? -28.556 -47.891  16.982  1.00 37.84  ? 104 GLY   B C      1 
ATOM   4205  O  O      . GLY   B 2  104 ? -29.064 -49.010  16.899  1.00 39.83  ? 104 GLY   B O      1 
ATOM   4206  N  N      . HIS   B 2  105 ? -28.980 -46.982  17.833  1.00 34.20  ? 105 HIS   B N      1 
ATOM   4207  C  CA     . HIS   B 2  105 ? -30.057 -47.224  18.775  1.00 36.80  ? 105 HIS   B CA     1 
ATOM   4208  C  C      . HIS   B 2  105 ? -31.421 -46.936  18.169  1.00 39.03  ? 105 HIS   B C      1 
ATOM   4209  O  O      . HIS   B 2  105 ? -32.395 -47.636  18.474  1.00 40.58  ? 105 HIS   B O      1 
ATOM   4210  C  CB     . HIS   B 2  105 ? -29.830 -46.349  20.008  1.00 39.09  ? 105 HIS   B CB     1 
ATOM   4211  C  CG     . HIS   B 2  105 ? -30.447 -46.868  21.267  1.00 42.22  ? 105 HIS   B CG     1 
ATOM   4212  N  ND1    . HIS   B 2  105 ? -29.906 -47.908  21.991  1.00 43.74  ? 105 HIS   B ND1    1 
ATOM   4213  C  CD2    . HIS   B 2  105 ? -31.521 -46.437  21.970  1.00 42.58  ? 105 HIS   B CD2    1 
ATOM   4214  C  CE1    . HIS   B 2  105 ? -30.643 -48.120  23.066  1.00 42.97  ? 105 HIS   B CE1    1 
ATOM   4215  N  NE2    . HIS   B 2  105 ? -31.629 -47.237  23.078  1.00 42.14  ? 105 HIS   B NE2    1 
ATOM   4216  N  N      . TYR   B 2  106 ? -31.510 -45.927  17.295  1.00 41.26  ? 106 TYR   B N      1 
ATOM   4217  C  CA     . TYR   B 2  106 ? -32.815 -45.397  16.907  1.00 38.23  ? 106 TYR   B CA     1 
ATOM   4218  C  C      . TYR   B 2  106 ? -33.155 -45.495  15.429  1.00 37.85  ? 106 TYR   B C      1 
ATOM   4219  O  O      . TYR   B 2  106 ? -34.319 -45.686  15.103  1.00 42.38  ? 106 TYR   B O      1 
ATOM   4220  C  CB     . TYR   B 2  106 ? -32.967 -43.948  17.324  1.00 32.84  ? 106 TYR   B CB     1 
ATOM   4221  C  CG     . TYR   B 2  106 ? -33.043 -43.746  18.802  1.00 34.85  ? 106 TYR   B CG     1 
ATOM   4222  C  CD1    . TYR   B 2  106 ? -33.994 -44.397  19.555  1.00 35.77  ? 106 TYR   B CD1    1 
ATOM   4223  C  CD2    . TYR   B 2  106 ? -32.296 -42.746  19.413  1.00 39.29  ? 106 TYR   B CD2    1 
ATOM   4224  C  CE1    . TYR   B 2  106 ? -34.103 -44.169  20.893  1.00 37.00  ? 106 TYR   B CE1    1 
ATOM   4225  C  CE2    . TYR   B 2  106 ? -32.412 -42.483  20.750  1.00 37.83  ? 106 TYR   B CE2    1 
ATOM   4226  C  CZ     . TYR   B 2  106 ? -33.317 -43.194  21.485  1.00 38.67  ? 106 TYR   B CZ     1 
ATOM   4227  O  OH     . TYR   B 2  106 ? -33.425 -42.918  22.819  1.00 43.15  ? 106 TYR   B OH     1 
ATOM   4228  N  N      . THR   B 2  107 ? -32.209 -45.339  14.509  1.00 42.05  ? 107 THR   B N      1 
ATOM   4229  C  CA     . THR   B 2  107 ? -32.609 -45.489  13.111  1.00 41.40  ? 107 THR   B CA     1 
ATOM   4230  C  C      . THR   B 2  107 ? -31.935 -46.683  12.430  1.00 42.57  ? 107 THR   B C      1 
ATOM   4231  O  O      . THR   B 2  107 ? -32.548 -47.747  12.320  1.00 47.18  ? 107 THR   B O      1 
ATOM   4232  C  CB     . THR   B 2  107 ? -32.366 -44.184  12.365  1.00 40.28  ? 107 THR   B CB     1 
ATOM   4233  O  OG1    . THR   B 2  107 ? -30.981 -43.850  12.437  1.00 45.75  ? 107 THR   B OG1    1 
ATOM   4234  C  CG2    . THR   B 2  107 ? -33.179 -43.061  12.991  1.00 38.36  ? 107 THR   B CG2    1 
ATOM   4235  N  N      . GLU   B 2  108 ? -30.693 -46.557  11.977  1.00 37.78  ? 108 GLU   B N      1 
ATOM   4236  C  CA     . GLU   B 2  108 ? -30.124 -47.653  11.203  1.00 40.72  ? 108 GLU   B CA     1 
ATOM   4237  C  C      . GLU   B 2  108 ? -30.214 -48.967  11.960  1.00 40.35  ? 108 GLU   B C      1 
ATOM   4238  O  O      . GLU   B 2  108 ? -30.335 -50.043  11.355  1.00 41.72  ? 108 GLU   B O      1 
ATOM   4239  C  CB     . GLU   B 2  108 ? -28.665 -47.379  10.868  1.00 39.55  ? 108 GLU   B CB     1 
ATOM   4240  C  CG     . GLU   B 2  108 ? -28.423 -46.042  10.317  1.00 40.71  ? 108 GLU   B CG     1 
ATOM   4241  C  CD     . GLU   B 2  108 ? -29.025 -45.853  8.965   1.00 53.37  ? 108 GLU   B CD     1 
ATOM   4242  O  OE1    . GLU   B 2  108 ? -29.316 -46.872  8.306   1.00 53.19  ? 108 GLU   B OE1    1 
ATOM   4243  O  OE2    . GLU   B 2  108 ? -29.194 -44.670  8.576   1.00 60.10  ? 108 GLU   B OE2    1 
ATOM   4244  N  N      . GLY   B 2  109 ? -30.135 -48.900  13.286  1.00 42.18  ? 109 GLY   B N      1 
ATOM   4245  C  CA     . GLY   B 2  109 ? -30.088 -50.115  14.081  1.00 47.46  ? 109 GLY   B CA     1 
ATOM   4246  C  C      . GLY   B 2  109 ? -31.453 -50.711  14.353  1.00 51.11  ? 109 GLY   B C      1 
ATOM   4247  O  O      . GLY   B 2  109 ? -31.571 -51.919  14.582  1.00 49.24  ? 109 GLY   B O      1 
ATOM   4248  N  N      . ALA   B 2  110 ? -32.503 -49.883  14.333  1.00 52.27  ? 110 ALA   B N      1 
ATOM   4249  C  CA     . ALA   B 2  110 ? -33.852 -50.412  14.465  1.00 45.45  ? 110 ALA   B CA     1 
ATOM   4250  C  C      . ALA   B 2  110 ? -34.194 -51.352  13.304  1.00 48.94  ? 110 ALA   B C      1 
ATOM   4251  O  O      . ALA   B 2  110 ? -34.822 -52.400  13.515  1.00 47.93  ? 110 ALA   B O      1 
ATOM   4252  C  CB     . ALA   B 2  110 ? -34.840 -49.254  14.569  1.00 45.66  ? 110 ALA   B CB     1 
ATOM   4253  N  N      . GLU   B 2  111 ? -33.746 -51.020  12.074  1.00 49.70  ? 111 GLU   B N      1 
ATOM   4254  C  CA     . GLU   B 2  111 ? -34.083 -51.857  10.919  1.00 46.96  ? 111 GLU   B CA     1 
ATOM   4255  C  C      . GLU   B 2  111 ? -33.578 -53.281  11.112  1.00 49.24  ? 111 GLU   B C      1 
ATOM   4256  O  O      . GLU   B 2  111 ? -34.230 -54.241  10.684  1.00 56.05  ? 111 GLU   B O      1 
ATOM   4257  C  CB     . GLU   B 2  111 ? -33.547 -51.273  9.586   1.00 40.10  ? 111 GLU   B CB     1 
ATOM   4258  C  CG     . GLU   B 2  111 ? -34.142 -49.891  9.129   1.00 54.07  ? 111 GLU   B CG     1 
ATOM   4259  C  CD     . GLU   B 2  111 ? -33.545 -49.293  7.798   1.00 72.95  ? 111 GLU   B CD     1 
ATOM   4260  O  OE1    . GLU   B 2  111 ? -33.360 -50.053  6.813   1.00 68.08  ? 111 GLU   B OE1    1 
ATOM   4261  O  OE2    . GLU   B 2  111 ? -33.302 -48.051  7.716   1.00 73.32  ? 111 GLU   B OE2    1 
ATOM   4262  N  N      . LEU   B 2  112 ? -32.456 -53.450  11.799  1.00 50.09  ? 112 LEU   B N      1 
ATOM   4263  C  CA     . LEU   B 2  112 ? -31.799 -54.741  11.810  1.00 49.29  ? 112 LEU   B CA     1 
ATOM   4264  C  C      . LEU   B 2  112 ? -32.003 -55.531  13.095  1.00 50.53  ? 112 LEU   B C      1 
ATOM   4265  O  O      . LEU   B 2  112 ? -31.637 -56.706  13.136  1.00 53.50  ? 112 LEU   B O      1 
ATOM   4266  C  CB     . LEU   B 2  112 ? -30.304 -54.545  11.538  1.00 46.19  ? 112 LEU   B CB     1 
ATOM   4267  C  CG     . LEU   B 2  112 ? -29.443 -55.789  11.382  1.00 45.66  ? 112 LEU   B CG     1 
ATOM   4268  C  CD1    . LEU   B 2  112 ? -29.732 -56.453  10.079  1.00 44.38  ? 112 LEU   B CD1    1 
ATOM   4269  C  CD2    . LEU   B 2  112 ? -27.983 -55.387  11.439  1.00 48.77  ? 112 LEU   B CD2    1 
ATOM   4270  N  N      . VAL   B 2  113 ? -32.603 -54.958  14.133  1.00 48.51  ? 113 VAL   B N      1 
ATOM   4271  C  CA     . VAL   B 2  113 ? -32.509 -55.643  15.420  1.00 52.84  ? 113 VAL   B CA     1 
ATOM   4272  C  C      . VAL   B 2  113 ? -33.411 -56.878  15.453  1.00 54.83  ? 113 VAL   B C      1 
ATOM   4273  O  O      . VAL   B 2  113 ? -33.053 -57.902  16.049  1.00 51.59  ? 113 VAL   B O      1 
ATOM   4274  C  CB     . VAL   B 2  113 ? -32.807 -54.687  16.589  1.00 44.34  ? 113 VAL   B CB     1 
ATOM   4275  C  CG1    . VAL   B 2  113 ? -34.253 -54.252  16.570  1.00 50.95  ? 113 VAL   B CG1    1 
ATOM   4276  C  CG2    . VAL   B 2  113 ? -32.457 -55.349  17.878  1.00 40.16  ? 113 VAL   B CG2    1 
ATOM   4277  N  N      . ASP   B 2  114 ? -34.591 -56.823  14.819  1.00 57.05  ? 114 ASP   B N      1 
ATOM   4278  C  CA     . ASP   B 2  114 ? -35.445 -58.006  14.865  1.00 49.59  ? 114 ASP   B CA     1 
ATOM   4279  C  C      . ASP   B 2  114 ? -34.756 -59.190  14.211  1.00 50.79  ? 114 ASP   B C      1 
ATOM   4280  O  O      . ASP   B 2  114 ? -34.963 -60.331  14.627  1.00 54.38  ? 114 ASP   B O      1 
ATOM   4281  C  CB     . ASP   B 2  114 ? -36.796 -57.775  14.193  1.00 48.59  ? 114 ASP   B CB     1 
ATOM   4282  C  CG     . ASP   B 2  114 ? -37.706 -56.877  14.994  1.00 61.72  ? 114 ASP   B CG     1 
ATOM   4283  O  OD1    . ASP   B 2  114 ? -37.448 -56.673  16.203  1.00 60.41  ? 114 ASP   B OD1    1 
ATOM   4284  O  OD2    . ASP   B 2  114 ? -38.734 -56.437  14.424  1.00 74.18  ? 114 ASP   B OD2    1 
ATOM   4285  N  N      . SER   B 2  115 ? -33.933 -58.954  13.187  1.00 47.29  ? 115 SER   B N      1 
ATOM   4286  C  CA     . SER   B 2  115 ? -33.257 -60.091  12.574  1.00 46.71  ? 115 SER   B CA     1 
ATOM   4287  C  C      . SER   B 2  115 ? -32.153 -60.618  13.465  1.00 47.74  ? 115 SER   B C      1 
ATOM   4288  O  O      . SER   B 2  115 ? -31.865 -61.818  13.436  1.00 48.48  ? 115 SER   B O      1 
ATOM   4289  C  CB     . SER   B 2  115 ? -32.715 -59.731  11.195  1.00 41.27  ? 115 SER   B CB     1 
ATOM   4290  O  OG     . SER   B 2  115 ? -32.094 -58.472  11.215  1.00 55.27  ? 115 SER   B OG     1 
ATOM   4291  N  N      . VAL   B 2  116 ? -31.534 -59.750  14.271  1.00 49.42  ? 116 VAL   B N      1 
ATOM   4292  C  CA     . VAL   B 2  116 ? -30.580 -60.242  15.261  1.00 48.73  ? 116 VAL   B CA     1 
ATOM   4293  C  C      . VAL   B 2  116 ? -31.322 -61.041  16.314  1.00 46.40  ? 116 VAL   B C      1 
ATOM   4294  O  O      . VAL   B 2  116 ? -30.960 -62.182  16.617  1.00 46.98  ? 116 VAL   B O      1 
ATOM   4295  C  CB     . VAL   B 2  116 ? -29.769 -59.091  15.897  1.00 50.46  ? 116 VAL   B CB     1 
ATOM   4296  C  CG1    . VAL   B 2  116 ? -28.776 -59.623  16.942  1.00 38.24  ? 116 VAL   B CG1    1 
ATOM   4297  C  CG2    . VAL   B 2  116 ? -29.025 -58.267  14.854  1.00 49.47  ? 116 VAL   B CG2    1 
ATOM   4298  N  N      . LEU   B 2  117 ? -32.407 -60.465  16.851  1.00 47.75  ? 117 LEU   B N      1 
ATOM   4299  C  CA     . LEU   B 2  117 ? -33.194 -61.137  17.881  1.00 48.13  ? 117 LEU   B CA     1 
ATOM   4300  C  C      . LEU   B 2  117 ? -33.666 -62.518  17.430  1.00 54.13  ? 117 LEU   B C      1 
ATOM   4301  O  O      . LEU   B 2  117 ? -33.776 -63.441  18.256  1.00 50.81  ? 117 LEU   B O      1 
ATOM   4302  C  CB     . LEU   B 2  117 ? -34.372 -60.256  18.272  1.00 41.50  ? 117 LEU   B CB     1 
ATOM   4303  C  CG     . LEU   B 2  117 ? -33.935 -58.998  19.026  1.00 50.64  ? 117 LEU   B CG     1 
ATOM   4304  C  CD1    . LEU   B 2  117 ? -35.073 -58.032  19.155  1.00 54.96  ? 117 LEU   B CD1    1 
ATOM   4305  C  CD2    . LEU   B 2  117 ? -33.387 -59.313  20.411  1.00 49.07  ? 117 LEU   B CD2    1 
ATOM   4306  N  N      . ASP   B 2  118 ? -33.922 -62.688  16.123  1.00 51.88  ? 118 ASP   B N      1 
ATOM   4307  C  CA     . ASP   B 2  118 ? -34.329 -63.990  15.607  1.00 47.55  ? 118 ASP   B CA     1 
ATOM   4308  C  C      . ASP   B 2  118 ? -33.196 -65.003  15.739  1.00 53.45  ? 118 ASP   B C      1 
ATOM   4309  O  O      . ASP   B 2  118 ? -33.422 -66.168  16.106  1.00 51.74  ? 118 ASP   B O      1 
ATOM   4310  C  CB     . ASP   B 2  118 ? -34.755 -63.869  14.149  1.00 43.92  ? 118 ASP   B CB     1 
ATOM   4311  C  CG     . ASP   B 2  118 ? -36.053 -63.111  13.974  1.00 53.03  ? 118 ASP   B CG     1 
ATOM   4312  O  OD1    . ASP   B 2  118 ? -36.762 -62.850  14.974  1.00 51.98  ? 118 ASP   B OD1    1 
ATOM   4313  O  OD2    . ASP   B 2  118 ? -36.361 -62.759  12.814  1.00 59.74  ? 118 ASP   B OD2    1 
ATOM   4314  N  N      . VAL   B 2  119 ? -31.966 -64.582  15.428  1.00 48.70  ? 119 VAL   B N      1 
ATOM   4315  C  CA     . VAL   B 2  119 ? -30.845 -65.494  15.585  1.00 48.90  ? 119 VAL   B CA     1 
ATOM   4316  C  C      . VAL   B 2  119 ? -30.609 -65.774  17.064  1.00 53.17  ? 119 VAL   B C      1 
ATOM   4317  O  O      . VAL   B 2  119 ? -30.177 -66.873  17.438  1.00 51.53  ? 119 VAL   B O      1 
ATOM   4318  C  CB     . VAL   B 2  119 ? -29.586 -64.920  14.920  1.00 43.28  ? 119 VAL   B CB     1 
ATOM   4319  C  CG1    . VAL   B 2  119 ? -28.396 -65.879  15.136  1.00 48.08  ? 119 VAL   B CG1    1 
ATOM   4320  C  CG2    . VAL   B 2  119 ? -29.849 -64.629  13.476  1.00 38.39  ? 119 VAL   B CG2    1 
ATOM   4321  N  N      . VAL   B 2  120 ? -30.874 -64.783  17.925  1.00 50.72  ? 120 VAL   B N      1 
ATOM   4322  C  CA     . VAL   B 2  120 ? -30.784 -64.993  19.363  1.00 49.10  ? 120 VAL   B CA     1 
ATOM   4323  C  C      . VAL   B 2  120 ? -31.767 -66.070  19.786  1.00 52.14  ? 120 VAL   B C      1 
ATOM   4324  O  O      . VAL   B 2  120 ? -31.379 -67.147  20.249  1.00 51.62  ? 120 VAL   B O      1 
ATOM   4325  C  CB     . VAL   B 2  120 ? -31.048 -63.681  20.115  1.00 49.91  ? 120 VAL   B CB     1 
ATOM   4326  C  CG1    . VAL   B 2  120 ? -31.262 -63.981  21.602  1.00 55.64  ? 120 VAL   B CG1    1 
ATOM   4327  C  CG2    . VAL   B 2  120 ? -29.917 -62.701  19.907  1.00 42.97  ? 120 VAL   B CG2    1 
ATOM   4328  N  N      . ARG   B 2  121 ? -33.060 -65.787  19.605  1.00 52.81  ? 121 ARG   B N      1 
ATOM   4329  C  CA     . ARG   B 2  121 ? -34.124 -66.731  19.941  1.00 54.76  ? 121 ARG   B CA     1 
ATOM   4330  C  C      . ARG   B 2  121 ? -33.857 -68.144  19.414  1.00 54.57  ? 121 ARG   B C      1 
ATOM   4331  O  O      . ARG   B 2  121 ? -34.157 -69.134  20.092  1.00 52.26  ? 121 ARG   B O      1 
ATOM   4332  C  CB     . ARG   B 2  121 ? -35.437 -66.209  19.380  1.00 52.31  ? 121 ARG   B CB     1 
ATOM   4333  C  CG     . ARG   B 2  121 ? -36.660 -66.880  19.911  1.00 49.52  ? 121 ARG   B CG     1 
ATOM   4334  C  CD     . ARG   B 2  121 ? -37.819 -66.253  19.219  1.00 55.70  ? 121 ARG   B CD     1 
ATOM   4335  N  NE     . ARG   B 2  121 ? -37.975 -64.868  19.650  1.00 56.17  ? 121 ARG   B NE     1 
ATOM   4336  C  CZ     . ARG   B 2  121 ? -37.716 -63.820  18.879  1.00 54.14  ? 121 ARG   B CZ     1 
ATOM   4337  N  NH1    . ARG   B 2  121 ? -37.300 -63.965  17.634  1.00 56.76  ? 121 ARG   B NH1    1 
ATOM   4338  N  NH2    . ARG   B 2  121 ? -37.879 -62.594  19.368  1.00 51.62  ? 121 ARG   B NH2    1 
ATOM   4339  N  N      . LYS   B 2  122 ? -33.321 -68.272  18.195  1.00 55.41  ? 122 LYS   B N      1 
ATOM   4340  C  CA     . LYS   B 2  122 ? -32.989 -69.611  17.709  1.00 60.83  ? 122 LYS   B CA     1 
ATOM   4341  C  C      . LYS   B 2  122 ? -32.008 -70.287  18.657  1.00 58.16  ? 122 LYS   B C      1 
ATOM   4342  O  O      . LYS   B 2  122 ? -32.285 -71.369  19.185  1.00 62.28  ? 122 LYS   B O      1 
ATOM   4343  C  CB     . LYS   B 2  122 ? -32.431 -69.557  16.284  1.00 54.49  ? 122 LYS   B CB     1 
ATOM   4344  N  N      . GLU   B 2  123 ? -30.881 -69.630  18.935  1.00 56.09  ? 123 GLU   B N      1 
ATOM   4345  C  CA     . GLU   B 2  123 ? -29.912 -70.179  19.879  1.00 56.47  ? 123 GLU   B CA     1 
ATOM   4346  C  C      . GLU   B 2  123 ? -30.522 -70.431  21.257  1.00 59.64  ? 123 GLU   B C      1 
ATOM   4347  O  O      . GLU   B 2  123 ? -30.200 -71.433  21.908  1.00 58.90  ? 123 GLU   B O      1 
ATOM   4348  C  CB     . GLU   B 2  123 ? -28.713 -69.244  19.990  1.00 46.95  ? 123 GLU   B CB     1 
ATOM   4349  C  CG     . GLU   B 2  123 ? -27.928 -69.111  18.708  1.00 53.08  ? 123 GLU   B CG     1 
ATOM   4350  C  CD     . GLU   B 2  123 ? -26.956 -70.253  18.558  1.00 57.44  ? 123 GLU   B CD     1 
ATOM   4351  O  OE1    . GLU   B 2  123 ? -26.994 -71.145  19.445  1.00 66.11  ? 123 GLU   B OE1    1 
ATOM   4352  O  OE2    . GLU   B 2  123 ? -26.153 -70.257  17.592  1.00 49.86  ? 123 GLU   B OE2    1 
ATOM   4353  N  N      . SER   B 2  124 ? -31.377 -69.519  21.732  1.00 58.45  ? 124 SER   B N      1 
ATOM   4354  C  CA     . SER   B 2  124 ? -31.966 -69.665  23.060  1.00 55.05  ? 124 SER   B CA     1 
ATOM   4355  C  C      . SER   B 2  124 ? -32.772 -70.947  23.153  1.00 59.51  ? 124 SER   B C      1 
ATOM   4356  O  O      . SER   B 2  124 ? -32.609 -71.728  24.097  1.00 56.62  ? 124 SER   B O      1 
ATOM   4357  C  CB     . SER   B 2  124 ? -32.850 -68.460  23.389  1.00 55.10  ? 124 SER   B CB     1 
ATOM   4358  O  OG     . SER   B 2  124 ? -32.076 -67.346  23.819  1.00 59.94  ? 124 SER   B OG     1 
ATOM   4359  N  N      . GLU   B 2  125 ? -33.650 -71.178  22.170  1.00 62.53  ? 125 GLU   B N      1 
ATOM   4360  C  CA     . GLU   B 2  125 ? -34.515 -72.356  22.181  1.00 65.09  ? 125 GLU   B CA     1 
ATOM   4361  C  C      . GLU   B 2  125 ? -33.708 -73.636  22.320  1.00 62.64  ? 125 GLU   B C      1 
ATOM   4362  O  O      . GLU   B 2  125 ? -33.998 -74.475  23.179  1.00 66.33  ? 125 GLU   B O      1 
ATOM   4363  C  CB     . GLU   B 2  125 ? -35.379 -72.372  20.918  1.00 67.88  ? 125 GLU   B CB     1 
ATOM   4364  C  CG     . GLU   B 2  125 ? -36.419 -71.247  20.889  1.00 73.64  ? 125 GLU   B CG     1 
ATOM   4365  C  CD     . GLU   B 2  125 ? -37.040 -71.001  19.509  1.00 82.50  ? 125 GLU   B CD     1 
ATOM   4366  O  OE1    . GLU   B 2  125 ? -36.593 -71.626  18.505  1.00 67.28  ? 125 GLU   B OE1    1 
ATOM   4367  O  OE2    . GLU   B 2  125 ? -37.997 -70.184  19.446  1.00 83.51  ? 125 GLU   B OE2    1 
ATOM   4368  N  N      . SER   B 2  126 ? -32.678 -73.793  21.493  1.00 54.14  ? 126 SER   B N      1 
ATOM   4369  C  CA     . SER   B 2  126 ? -31.783 -74.931  21.631  1.00 53.67  ? 126 SER   B CA     1 
ATOM   4370  C  C      . SER   B 2  126 ? -31.333 -75.193  23.071  1.00 58.56  ? 126 SER   B C      1 
ATOM   4371  O  O      . SER   B 2  126 ? -30.959 -76.322  23.398  1.00 60.98  ? 126 SER   B O      1 
ATOM   4372  C  CB     . SER   B 2  126 ? -30.560 -74.726  20.757  1.00 52.51  ? 126 SER   B CB     1 
ATOM   4373  O  OG     . SER   B 2  126 ? -29.533 -75.617  21.153  1.00 68.13  ? 126 SER   B OG     1 
ATOM   4374  N  N      . CYS   B 2  127 ? -31.360 -74.192  23.941  1.00 50.21  ? 127 CYS   B N      1 
ATOM   4375  C  CA     . CYS   B 2  127 ? -30.603 -74.293  25.177  1.00 54.51  ? 127 CYS   B CA     1 
ATOM   4376  C  C      . CYS   B 2  127 ? -31.339 -75.070  26.254  1.00 64.11  ? 127 CYS   B C      1 
ATOM   4377  O  O      . CYS   B 2  127 ? -32.563 -74.978  26.405  1.00 61.61  ? 127 CYS   B O      1 
ATOM   4378  C  CB     . CYS   B 2  127 ? -30.259 -72.914  25.741  1.00 60.76  ? 127 CYS   B CB     1 
ATOM   4379  S  SG     . CYS   B 2  127 ? -29.067 -71.990  24.814  1.00 62.42  ? 127 CYS   B SG     1 
ATOM   4380  N  N      . ASP   B 2  128 ? -30.546 -75.787  27.055  1.00 64.84  ? 128 ASP   B N      1 
ATOM   4381  C  CA     . ASP   B 2  128 ? -31.055 -76.631  28.125  1.00 59.44  ? 128 ASP   B CA     1 
ATOM   4382  C  C      . ASP   B 2  128 ? -31.423 -75.810  29.365  1.00 65.93  ? 128 ASP   B C      1 
ATOM   4383  O  O      . ASP   B 2  128 ? -32.576 -75.822  29.811  1.00 65.92  ? 128 ASP   B O      1 
ATOM   4384  C  CB     . ASP   B 2  128 ? -30.005 -77.696  28.435  1.00 62.34  ? 128 ASP   B CB     1 
ATOM   4385  C  CG     . ASP   B 2  128 ? -30.462 -78.670  29.480  1.00 77.84  ? 128 ASP   B CG     1 
ATOM   4386  O  OD1    . ASP   B 2  128 ? -31.686 -78.810  29.670  1.00 85.89  ? 128 ASP   B OD1    1 
ATOM   4387  O  OD2    . ASP   B 2  128 ? -29.588 -79.273  30.135  1.00 79.24  ? 128 ASP   B OD2    1 
ATOM   4388  N  N      . CYS   B 2  129 ? -30.444 -75.119  29.957  1.00 60.08  ? 129 CYS   B N      1 
ATOM   4389  C  CA     . CYS   B 2  129 ? -30.663 -74.094  30.988  1.00 54.11  ? 129 CYS   B CA     1 
ATOM   4390  C  C      . CYS   B 2  129 ? -29.819 -72.888  30.596  1.00 59.42  ? 129 CYS   B C      1 
ATOM   4391  O  O      . CYS   B 2  129 ? -28.676 -72.739  31.036  1.00 58.92  ? 129 CYS   B O      1 
ATOM   4392  C  CB     . CYS   B 2  129 ? -30.330 -74.560  32.406  1.00 54.60  ? 129 CYS   B CB     1 
ATOM   4393  S  SG     . CYS   B 2  129 ? -30.990 -73.446  33.707  1.00 63.53  ? 129 CYS   B SG     1 
ATOM   4394  N  N      . LEU   B 2  130 ? -30.385 -72.039  29.756  1.00 56.72  ? 130 LEU   B N      1 
ATOM   4395  C  CA     . LEU   B 2  130 ? -29.723 -70.807  29.383  1.00 54.43  ? 130 LEU   B CA     1 
ATOM   4396  C  C      . LEU   B 2  130 ? -29.382 -70.006  30.623  1.00 51.76  ? 130 LEU   B C      1 
ATOM   4397  O  O      . LEU   B 2  130 ? -30.274 -69.663  31.404  1.00 54.76  ? 130 LEU   B O      1 
ATOM   4398  C  CB     . LEU   B 2  130 ? -30.638 -70.012  28.469  1.00 55.75  ? 130 LEU   B CB     1 
ATOM   4399  C  CG     . LEU   B 2  130 ? -30.202 -68.600  28.152  1.00 48.54  ? 130 LEU   B CG     1 
ATOM   4400  C  CD1    . LEU   B 2  130 ? -29.150 -68.659  27.081  1.00 47.59  ? 130 LEU   B CD1    1 
ATOM   4401  C  CD2    . LEU   B 2  130 ? -31.410 -67.833  27.704  1.00 46.92  ? 130 LEU   B CD2    1 
ATOM   4402  N  N      . GLN   B 2  131 ? -28.087 -69.724  30.813  1.00 51.36  ? 131 GLN   B N      1 
ATOM   4403  C  CA     . GLN   B 2  131 ? -27.666 -68.844  31.903  1.00 47.01  ? 131 GLN   B CA     1 
ATOM   4404  C  C      . GLN   B 2  131 ? -28.016 -67.410  31.585  1.00 45.74  ? 131 GLN   B C      1 
ATOM   4405  O  O      . GLN   B 2  131 ? -28.509 -66.671  32.444  1.00 48.30  ? 131 GLN   B O      1 
ATOM   4406  C  CB     . GLN   B 2  131 ? -26.163 -68.935  32.128  1.00 47.03  ? 131 GLN   B CB     1 
ATOM   4407  C  CG     . GLN   B 2  131 ? -25.639 -70.274  32.507  1.00 48.37  ? 131 GLN   B CG     1 
ATOM   4408  C  CD     . GLN   B 2  131 ? -24.194 -70.216  32.917  1.00 45.26  ? 131 GLN   B CD     1 
ATOM   4409  O  OE1    . GLN   B 2  131 ? -23.764 -69.311  33.636  1.00 41.82  ? 131 GLN   B OE1    1 
ATOM   4410  N  NE2    . GLN   B 2  131 ? -23.419 -71.171  32.432  1.00 51.19  ? 131 GLN   B NE2    1 
ATOM   4411  N  N      . GLY   B 2  132 ? -27.736 -66.997  30.370  1.00 44.17  ? 132 GLY   B N      1 
ATOM   4412  C  CA     . GLY   B 2  132 ? -27.949 -65.636  29.951  1.00 46.75  ? 132 GLY   B CA     1 
ATOM   4413  C  C      . GLY   B 2  132 ? -27.000 -65.271  28.817  1.00 48.90  ? 132 GLY   B C      1 
ATOM   4414  O  O      . GLY   B 2  132 ? -26.614 -66.123  28.012  1.00 50.12  ? 132 GLY   B O      1 
ATOM   4415  N  N      . PHE   B 2  133 ? -26.652 -63.985  28.776  1.00 45.56  ? 133 PHE   B N      1 
ATOM   4416  C  CA     . PHE   B 2  133 ? -25.964 -63.420  27.631  1.00 41.86  ? 133 PHE   B CA     1 
ATOM   4417  C  C      . PHE   B 2  133 ? -24.725 -62.665  28.080  1.00 43.56  ? 133 PHE   B C      1 
ATOM   4418  O  O      . PHE   B 2  133 ? -24.666 -62.101  29.178  1.00 39.55  ? 133 PHE   B O      1 
ATOM   4419  C  CB     . PHE   B 2  133 ? -26.888 -62.499  26.843  1.00 37.90  ? 133 PHE   B CB     1 
ATOM   4420  C  CG     . PHE   B 2  133 ? -28.243 -63.096  26.562  1.00 41.35  ? 133 PHE   B CG     1 
ATOM   4421  C  CD1    . PHE   B 2  133 ? -29.277 -62.963  27.461  1.00 38.30  ? 133 PHE   B CD1    1 
ATOM   4422  C  CD2    . PHE   B 2  133 ? -28.458 -63.842  25.416  1.00 46.91  ? 133 PHE   B CD2    1 
ATOM   4423  C  CE1    . PHE   B 2  133 ? -30.502 -63.539  27.213  1.00 38.89  ? 133 PHE   B CE1    1 
ATOM   4424  C  CE2    . PHE   B 2  133 ? -29.696 -64.416  25.159  1.00 46.56  ? 133 PHE   B CE2    1 
ATOM   4425  C  CZ     . PHE   B 2  133 ? -30.710 -64.270  26.059  1.00 42.63  ? 133 PHE   B CZ     1 
ATOM   4426  N  N      . GLN   B 2  134 ? -23.722 -62.684  27.218  1.00 45.05  ? 134 GLN   B N      1 
ATOM   4427  C  CA     . GLN   B 2  134 ? -22.594 -61.784  27.350  1.00 42.85  ? 134 GLN   B CA     1 
ATOM   4428  C  C      . GLN   B 2  134 ? -22.362 -61.127  26.002  1.00 40.70  ? 134 GLN   B C      1 
ATOM   4429  O  O      . GLN   B 2  134 ? -22.415 -61.779  24.952  1.00 41.80  ? 134 GLN   B O      1 
ATOM   4430  C  CB     . GLN   B 2  134 ? -21.333 -62.494  27.786  1.00 44.59  ? 134 GLN   B CB     1 
ATOM   4431  C  CG     . GLN   B 2  134 ? -20.751 -63.342  26.698  1.00 45.86  ? 134 GLN   B CG     1 
ATOM   4432  C  CD     . GLN   B 2  134 ? -19.443 -63.952  27.088  1.00 48.88  ? 134 GLN   B CD     1 
ATOM   4433  O  OE1    . GLN   B 2  134 ? -19.227 -64.300  28.262  1.00 41.91  ? 134 GLN   B OE1    1 
ATOM   4434  N  NE2    . GLN   B 2  134 ? -18.534 -64.059  26.109  1.00 48.08  ? 134 GLN   B NE2    1 
ATOM   4435  N  N      . LEU   B 2  135 ? -22.132 -59.830  26.045  1.00 37.08  ? 135 LEU   B N      1 
ATOM   4436  C  CA     . LEU   B 2  135 ? -21.964 -59.015  24.861  1.00 39.10  ? 135 LEU   B CA     1 
ATOM   4437  C  C      . LEU   B 2  135 ? -20.600 -58.351  24.908  1.00 39.57  ? 135 LEU   B C      1 
ATOM   4438  O  O      . LEU   B 2  135 ? -20.227 -57.777  25.938  1.00 37.58  ? 135 LEU   B O      1 
ATOM   4439  C  CB     . LEU   B 2  135 ? -23.057 -57.947  24.791  1.00 41.03  ? 135 LEU   B CB     1 
ATOM   4440  C  CG     . LEU   B 2  135 ? -22.809 -56.881  23.738  1.00 37.50  ? 135 LEU   B CG     1 
ATOM   4441  C  CD1    . LEU   B 2  135 ? -23.300 -57.341  22.377  1.00 35.62  ? 135 LEU   B CD1    1 
ATOM   4442  C  CD2    . LEU   B 2  135 ? -23.434 -55.582  24.195  1.00 35.02  ? 135 LEU   B CD2    1 
ATOM   4443  N  N      . THR   B 2  136 ? -19.861 -58.432  23.808  1.00 35.54  ? 136 THR   B N      1 
ATOM   4444  C  CA     . THR   B 2  136 ? -18.695 -57.590  23.614  1.00 35.46  ? 136 THR   B CA     1 
ATOM   4445  C  C      . THR   B 2  136 ? -19.125 -56.437  22.725  1.00 33.88  ? 136 THR   B C      1 
ATOM   4446  O  O      . THR   B 2  136 ? -19.910 -56.635  21.795  1.00 35.67  ? 136 THR   B O      1 
ATOM   4447  C  CB     . THR   B 2  136 ? -17.533 -58.348  22.953  1.00 39.36  ? 136 THR   B CB     1 
ATOM   4448  O  OG1    . THR   B 2  136 ? -17.933 -58.845  21.667  1.00 41.14  ? 136 THR   B OG1    1 
ATOM   4449  C  CG2    . THR   B 2  136 ? -17.117 -59.532  23.810  1.00 35.05  ? 136 THR   B CG2    1 
ATOM   4450  N  N      . HIS   B 2  137 ? -18.604 -55.245  23.002  1.00 31.42  ? 137 HIS   B N      1 
ATOM   4451  C  CA     . HIS   B 2  137 ? -18.873 -54.049  22.208  1.00 34.74  ? 137 HIS   B CA     1 
ATOM   4452  C  C      . HIS   B 2  137 ? -18.008 -52.920  22.749  1.00 32.55  ? 137 HIS   B C      1 
ATOM   4453  O  O      . HIS   B 2  137 ? -17.308 -53.085  23.750  1.00 34.81  ? 137 HIS   B O      1 
ATOM   4454  C  CB     . HIS   B 2  137 ? -20.351 -53.679  22.261  1.00 35.14  ? 137 HIS   B CB     1 
ATOM   4455  C  CG     . HIS   B 2  137 ? -20.801 -53.243  23.621  1.00 35.25  ? 137 HIS   B CG     1 
ATOM   4456  N  ND1    . HIS   B 2  137 ? -21.873 -52.404  23.827  1.00 35.09  ? 137 HIS   B ND1    1 
ATOM   4457  C  CD2    . HIS   B 2  137 ? -20.290 -53.504  24.847  1.00 35.78  ? 137 HIS   B CD2    1 
ATOM   4458  C  CE1    . HIS   B 2  137 ? -22.004 -52.172  25.119  1.00 30.77  ? 137 HIS   B CE1    1 
ATOM   4459  N  NE2    . HIS   B 2  137 ? -21.060 -52.833  25.759  1.00 31.56  ? 137 HIS   B NE2    1 
ATOM   4460  N  N      . SER   B 2  138 ? -18.059 -51.768  22.081  1.00 33.54  ? 138 SER   B N      1 
ATOM   4461  C  CA     . SER   B 2  138 ? -17.418 -50.558  22.583  1.00 33.62  ? 138 SER   B CA     1 
ATOM   4462  C  C      . SER   B 2  138 ? -18.451 -49.459  22.693  1.00 35.34  ? 138 SER   B C      1 
ATOM   4463  O  O      . SER   B 2  138 ? -19.396 -49.412  21.907  1.00 42.77  ? 138 SER   B O      1 
ATOM   4464  C  CB     . SER   B 2  138 ? -16.289 -50.063  21.699  1.00 29.25  ? 138 SER   B CB     1 
ATOM   4465  O  OG     . SER   B 2  138 ? -16.752 -49.932  20.378  1.00 37.95  ? 138 SER   B OG     1 
ATOM   4466  N  N      . LEU   B 2  139 ? -18.258 -48.570  23.660  1.00 30.52  ? 139 LEU   B N      1 
ATOM   4467  C  CA     . LEU   B 2  139 ? -19.238 -47.540  23.941  1.00 29.19  ? 139 LEU   B CA     1 
ATOM   4468  C  C      . LEU   B 2  139 ? -18.987 -46.243  23.168  1.00 34.64  ? 139 LEU   B C      1 
ATOM   4469  O  O      . LEU   B 2  139 ? -19.778 -45.309  23.284  1.00 34.70  ? 139 LEU   B O      1 
ATOM   4470  C  CB     . LEU   B 2  139 ? -19.260 -47.243  25.440  1.00 32.13  ? 139 LEU   B CB     1 
ATOM   4471  C  CG     . LEU   B 2  139 ? -19.371 -48.450  26.368  1.00 34.39  ? 139 LEU   B CG     1 
ATOM   4472  C  CD1    . LEU   B 2  139 ? -19.413 -48.027  27.838  1.00 35.86  ? 139 LEU   B CD1    1 
ATOM   4473  C  CD2    . LEU   B 2  139 ? -20.560 -49.294  25.989  1.00 34.54  ? 139 LEU   B CD2    1 
ATOM   4474  N  N      . GLY   B 2  140 ? -17.929 -46.144  22.376  1.00 31.91  ? 140 GLY   B N      1 
ATOM   4475  C  CA     . GLY   B 2  140 ? -17.641 -44.857  21.762  1.00 31.21  ? 140 GLY   B CA     1 
ATOM   4476  C  C      . GLY   B 2  140 ? -17.976 -44.693  20.289  1.00 32.81  ? 140 GLY   B C      1 
ATOM   4477  O  O      . GLY   B 2  140 ? -17.922 -43.578  19.764  1.00 33.91  ? 140 GLY   B O      1 
ATOM   4478  N  N      . GLY   B 2  141 ? -18.291 -45.785  19.601  1.00 30.38  ? 141 GLY   B N      1 
ATOM   4479  C  CA     . GLY   B 2  141 ? -18.747 -45.738  18.230  1.00 28.81  ? 141 GLY   B CA     1 
ATOM   4480  C  C      . GLY   B 2  141 ? -20.255 -45.786  18.143  1.00 32.43  ? 141 GLY   B C      1 
ATOM   4481  O  O      . GLY   B 2  141 ? -20.972 -45.412  19.074  1.00 33.91  ? 141 GLY   B O      1 
ATOM   4482  N  N      . GLY   B 2  142 ? -20.756 -46.274  17.022  1.00 33.22  ? 142 GLY   B N      1 
ATOM   4483  C  CA     . GLY   B 2  142 ? -22.192 -46.252  16.841  1.00 32.67  ? 142 GLY   B CA     1 
ATOM   4484  C  C      . GLY   B 2  142 ? -22.915 -47.584  16.864  1.00 35.95  ? 142 GLY   B C      1 
ATOM   4485  O  O      . GLY   B 2  142 ? -23.959 -47.697  17.520  1.00 38.54  ? 142 GLY   B O      1 
ATOM   4486  N  N      . THR   B 2  143 ? -22.421 -48.583  16.131  1.00 31.88  ? 143 THR   B N      1 
ATOM   4487  C  CA     . THR   B 2  143 ? -23.103 -49.868  16.135  1.00 31.21  ? 143 THR   B CA     1 
ATOM   4488  C  C      . THR   B 2  143 ? -23.057 -50.457  17.536  1.00 31.40  ? 143 THR   B C      1 
ATOM   4489  O  O      . THR   B 2  143 ? -24.019 -50.344  18.288  1.00 37.07  ? 143 THR   B O      1 
ATOM   4490  C  CB     . THR   B 2  143 ? -22.494 -50.825  15.110  1.00 34.38  ? 143 THR   B CB     1 
ATOM   4491  O  OG1    . THR   B 2  143 ? -22.757 -50.326  13.803  1.00 41.64  ? 143 THR   B OG1    1 
ATOM   4492  C  CG2    . THR   B 2  143 ? -23.107 -52.174  15.197  1.00 34.66  ? 143 THR   B CG2    1 
ATOM   4493  N  N      . GLY   B 2  144 ? -21.951 -51.062  17.916  1.00 33.07  ? 144 GLY   B N      1 
ATOM   4494  C  CA     . GLY   B 2  144 ? -21.896 -51.714  19.215  1.00 35.16  ? 144 GLY   B CA     1 
ATOM   4495  C  C      . GLY   B 2  144 ? -22.314 -50.814  20.355  1.00 32.67  ? 144 GLY   B C      1 
ATOM   4496  O  O      . GLY   B 2  144 ? -22.801 -51.287  21.383  1.00 30.75  ? 144 GLY   B O      1 
ATOM   4497  N  N      . SER   B 2  145 ? -22.139 -49.509  20.197  1.00 33.65  ? 145 SER   B N      1 
ATOM   4498  C  CA     . SER   B 2  145 ? -22.510 -48.607  21.275  1.00 34.51  ? 145 SER   B CA     1 
ATOM   4499  C  C      . SER   B 2  145 ? -24.014 -48.442  21.367  1.00 37.55  ? 145 SER   B C      1 
ATOM   4500  O  O      . SER   B 2  145 ? -24.625 -48.767  22.391  1.00 40.96  ? 145 SER   B O      1 
ATOM   4501  C  CB     . SER   B 2  145 ? -21.867 -47.258  21.078  1.00 35.78  ? 145 SER   B CB     1 
ATOM   4502  O  OG     . SER   B 2  145 ? -21.987 -46.571  22.294  1.00 37.07  ? 145 SER   B OG     1 
ATOM   4503  N  N      . GLY   B 2  146 ? -24.624 -47.917  20.308  1.00 38.90  ? 146 GLY   B N      1 
ATOM   4504  C  CA     . GLY   B 2  146 ? -26.047 -47.664  20.252  1.00 37.58  ? 146 GLY   B CA     1 
ATOM   4505  C  C      . GLY   B 2  146 ? -26.880 -48.879  19.912  1.00 35.48  ? 146 GLY   B C      1 
ATOM   4506  O  O      . GLY   B 2  146 ? -27.817 -49.188  20.640  1.00 39.73  ? 146 GLY   B O      1 
ATOM   4507  N  N      . MET   B 2  147 ? -26.581 -49.588  18.827  1.00 34.40  ? 147 MET   B N      1 
ATOM   4508  C  CA     . MET   B 2  147 ? -27.342 -50.811  18.587  1.00 39.25  ? 147 MET   B CA     1 
ATOM   4509  C  C      . MET   B 2  147 ? -27.128 -51.812  19.718  1.00 39.47  ? 147 MET   B C      1 
ATOM   4510  O  O      . MET   B 2  147 ? -28.066 -52.497  20.142  1.00 41.11  ? 147 MET   B O      1 
ATOM   4511  C  CB     . MET   B 2  147 ? -26.987 -51.451  17.241  1.00 35.17  ? 147 MET   B CB     1 
ATOM   4512  C  CG     . MET   B 2  147 ? -28.094 -52.377  16.814  1.00 33.48  ? 147 MET   B CG     1 
ATOM   4513  S  SD     . MET   B 2  147 ? -27.866 -53.370  15.358  1.00 46.60  ? 147 MET   B SD     1 
ATOM   4514  C  CE     . MET   B 2  147 ? -26.527 -54.373  15.893  1.00 50.90  ? 147 MET   B CE     1 
ATOM   4515  N  N      . GLY   B 2  148 ? -25.907 -51.902  20.226  1.00 37.83  ? 148 GLY   B N      1 
ATOM   4516  C  CA     . GLY   B 2  148 ? -25.612 -52.778  21.342  1.00 37.13  ? 148 GLY   B CA     1 
ATOM   4517  C  C      . GLY   B 2  148 ? -26.553 -52.574  22.507  1.00 41.14  ? 148 GLY   B C      1 
ATOM   4518  O  O      . GLY   B 2  148 ? -27.265 -53.496  22.903  1.00 41.76  ? 148 GLY   B O      1 
ATOM   4519  N  N      . THR   B 2  149 ? -26.561 -51.370  23.076  1.00 40.19  ? 149 THR   B N      1 
ATOM   4520  C  CA     . THR   B 2  149 ? -27.484 -51.098  24.165  1.00 39.18  ? 149 THR   B CA     1 
ATOM   4521  C  C      . THR   B 2  149 ? -28.940 -51.312  23.747  1.00 42.74  ? 149 THR   B C      1 
ATOM   4522  O  O      . THR   B 2  149 ? -29.771 -51.699  24.578  1.00 49.24  ? 149 THR   B O      1 
ATOM   4523  C  CB     . THR   B 2  149 ? -27.268 -49.677  24.674  1.00 35.18  ? 149 THR   B CB     1 
ATOM   4524  O  OG1    . THR   B 2  149 ? -27.335 -48.777  23.572  1.00 37.93  ? 149 THR   B OG1    1 
ATOM   4525  C  CG2    . THR   B 2  149 ? -25.963 -49.528  25.390  1.00 31.15  ? 149 THR   B CG2    1 
ATOM   4526  N  N      . LEU   B 2  150 ? -29.276 -51.076  22.483  1.00 33.22  ? 150 LEU   B N      1 
ATOM   4527  C  CA     . LEU   B 2  150 ? -30.633 -51.348  22.034  1.00 35.12  ? 150 LEU   B CA     1 
ATOM   4528  C  C      . LEU   B 2  150 ? -30.957 -52.833  22.147  1.00 39.40  ? 150 LEU   B C      1 
ATOM   4529  O  O      . LEU   B 2  150 ? -31.993 -53.214  22.698  1.00 44.98  ? 150 LEU   B O      1 
ATOM   4530  C  CB     . LEU   B 2  150 ? -30.813 -50.878  20.593  1.00 38.31  ? 150 LEU   B CB     1 
ATOM   4531  C  CG     . LEU   B 2  150 ? -32.142 -51.247  19.944  1.00 34.98  ? 150 LEU   B CG     1 
ATOM   4532  C  CD1    . LEU   B 2  150 ? -33.269 -50.307  20.363  1.00 32.90  ? 150 LEU   B CD1    1 
ATOM   4533  C  CD2    . LEU   B 2  150 ? -31.977 -51.351  18.450  1.00 35.40  ? 150 LEU   B CD2    1 
ATOM   4534  N  N      . LEU   B 2  151 ? -30.102 -53.685  21.585  1.00 38.40  ? 151 LEU   B N      1 
ATOM   4535  C  CA     . LEU   B 2  151 ? -30.251 -55.131  21.734  1.00 36.33  ? 151 LEU   B CA     1 
ATOM   4536  C  C      . LEU   B 2  151 ? -30.433 -55.529  23.190  1.00 40.15  ? 151 LEU   B C      1 
ATOM   4537  O  O      . LEU   B 2  151 ? -31.360 -56.261  23.541  1.00 44.95  ? 151 LEU   B O      1 
ATOM   4538  C  CB     . LEU   B 2  151 ? -29.011 -55.820  21.188  1.00 35.52  ? 151 LEU   B CB     1 
ATOM   4539  C  CG     . LEU   B 2  151 ? -28.963 -56.294  19.765  1.00 39.07  ? 151 LEU   B CG     1 
ATOM   4540  C  CD1    . LEU   B 2  151 ? -27.520 -56.304  19.327  1.00 36.32  ? 151 LEU   B CD1    1 
ATOM   4541  C  CD2    . LEU   B 2  151 ? -29.542 -57.692  19.727  1.00 42.76  ? 151 LEU   B CD2    1 
ATOM   4542  N  N      . ILE   B 2  152 ? -29.510 -55.097  24.044  1.00 38.08  ? 152 ILE   B N      1 
ATOM   4543  C  CA     . ILE   B 2  152 ? -29.578 -55.418  25.462  1.00 40.88  ? 152 ILE   B CA     1 
ATOM   4544  C  C      . ILE   B 2  152 ? -30.955 -55.041  25.994  1.00 40.98  ? 152 ILE   B C      1 
ATOM   4545  O  O      . ILE   B 2  152 ? -31.576 -55.788  26.757  1.00 41.78  ? 152 ILE   B O      1 
ATOM   4546  C  CB     . ILE   B 2  152 ? -28.428 -54.700  26.211  1.00 42.02  ? 152 ILE   B CB     1 
ATOM   4547  C  CG1    . ILE   B 2  152 ? -27.090 -55.320  25.820  1.00 36.31  ? 152 ILE   B CG1    1 
ATOM   4548  C  CG2    . ILE   B 2  152 ? -28.556 -54.797  27.727  1.00 33.27  ? 152 ILE   B CG2    1 
ATOM   4549  C  CD1    . ILE   B 2  152 ? -25.906 -54.491  26.204  1.00 36.28  ? 152 ILE   B CD1    1 
ATOM   4550  N  N      . SER   B 2  153 ? -31.474 -53.893  25.562  1.00 42.93  ? 153 SER   B N      1 
ATOM   4551  C  CA     . SER   B 2  153 ? -32.774 -53.443  26.040  1.00 43.79  ? 153 SER   B CA     1 
ATOM   4552  C  C      . SER   B 2  153 ? -33.891 -54.338  25.549  1.00 44.62  ? 153 SER   B C      1 
ATOM   4553  O  O      . SER   B 2  153 ? -34.943 -54.416  26.191  1.00 43.88  ? 153 SER   B O      1 
ATOM   4554  C  CB     . SER   B 2  153 ? -33.042 -52.008  25.602  1.00 42.11  ? 153 SER   B CB     1 
ATOM   4555  O  OG     . SER   B 2  153 ? -34.075 -51.451  26.389  1.00 48.23  ? 153 SER   B OG     1 
ATOM   4556  N  N      . LYS   B 2  154 ? -33.683 -55.028  24.437  1.00 42.59  ? 154 LYS   B N      1 
ATOM   4557  C  CA     . LYS   B 2  154 ? -34.722 -55.915  23.958  1.00 44.02  ? 154 LYS   B CA     1 
ATOM   4558  C  C      . LYS   B 2  154 ? -34.553 -57.314  24.528  1.00 44.01  ? 154 LYS   B C      1 
ATOM   4559  O  O      . LYS   B 2  154 ? -35.540 -57.985  24.839  1.00 46.72  ? 154 LYS   B O      1 
ATOM   4560  C  CB     . LYS   B 2  154 ? -34.729 -55.943  22.430  1.00 43.77  ? 154 LYS   B CB     1 
ATOM   4561  C  CG     . LYS   B 2  154 ? -35.148 -54.610  21.792  1.00 48.48  ? 154 LYS   B CG     1 
ATOM   4562  C  CD     . LYS   B 2  154 ? -35.789 -54.775  20.394  1.00 55.24  ? 154 LYS   B CD     1 
ATOM   4563  C  CE     . LYS   B 2  154 ? -36.854 -53.719  20.116  1.00 50.43  ? 154 LYS   B CE     1 
ATOM   4564  N  NZ     . LYS   B 2  154 ? -36.346 -52.357  20.477  1.00 52.57  ? 154 LYS   B NZ     1 
ATOM   4565  N  N      . ILE   B 2  155 ? -33.316 -57.773  24.687  1.00 44.95  ? 155 ILE   B N      1 
ATOM   4566  C  CA     . ILE   B 2  155 ? -33.106 -59.087  25.283  1.00 45.16  ? 155 ILE   B CA     1 
ATOM   4567  C  C      . ILE   B 2  155 ? -33.691 -59.130  26.689  1.00 43.43  ? 155 ILE   B C      1 
ATOM   4568  O  O      . ILE   B 2  155 ? -34.281 -60.139  27.097  1.00 40.15  ? 155 ILE   B O      1 
ATOM   4569  C  CB     . ILE   B 2  155 ? -31.609 -59.450  25.253  1.00 40.11  ? 155 ILE   B CB     1 
ATOM   4570  C  CG1    . ILE   B 2  155 ? -31.144 -59.504  23.802  1.00 39.69  ? 155 ILE   B CG1    1 
ATOM   4571  C  CG2    . ILE   B 2  155 ? -31.339 -60.759  25.975  1.00 40.85  ? 155 ILE   B CG2    1 
ATOM   4572  C  CD1    . ILE   B 2  155 ? -29.738 -59.932  23.662  1.00 45.86  ? 155 ILE   B CD1    1 
ATOM   4573  N  N      . ARG   B 2  156 ? -33.568 -58.025  27.440  1.00 40.93  ? 156 ARG   B N      1 
ATOM   4574  C  CA     . ARG   B 2  156 ? -34.102 -57.988  28.795  1.00 38.10  ? 156 ARG   B CA     1 
ATOM   4575  C  C      . ARG   B 2  156 ? -35.609 -58.093  28.807  1.00 46.97  ? 156 ARG   B C      1 
ATOM   4576  O  O      . ARG   B 2  156 ? -36.181 -58.602  29.780  1.00 46.32  ? 156 ARG   B O      1 
ATOM   4577  C  CB     . ARG   B 2  156 ? -33.710 -56.715  29.514  1.00 37.29  ? 156 ARG   B CB     1 
ATOM   4578  C  CG     . ARG   B 2  156 ? -34.071 -56.723  30.993  1.00 40.76  ? 156 ARG   B CG     1 
ATOM   4579  C  CD     . ARG   B 2  156 ? -33.598 -55.447  31.629  1.00 44.19  ? 156 ARG   B CD     1 
ATOM   4580  N  NE     . ARG   B 2  156 ? -33.743 -55.351  33.078  1.00 43.55  ? 156 ARG   B NE     1 
ATOM   4581  C  CZ     . ARG   B 2  156 ? -33.814 -54.186  33.704  1.00 44.23  ? 156 ARG   B CZ     1 
ATOM   4582  N  NH1    . ARG   B 2  156 ? -33.882 -53.054  33.026  1.00 51.19  ? 156 ARG   B NH1    1 
ATOM   4583  N  NH2    . ARG   B 2  156 ? -33.789 -54.149  35.034  1.00 42.28  ? 156 ARG   B NH2    1 
ATOM   4584  N  N      . GLU   B 2  157 ? -36.273 -57.586  27.762  1.00 49.68  ? 157 GLU   B N      1 
ATOM   4585  C  CA     . GLU   B 2  157 ? -37.735 -57.655  27.683  1.00 48.02  ? 157 GLU   B CA     1 
ATOM   4586  C  C      . GLU   B 2  157 ? -38.198 -59.061  27.343  1.00 44.49  ? 157 GLU   B C      1 
ATOM   4587  O  O      . GLU   B 2  157 ? -39.175 -59.557  27.912  1.00 49.07  ? 157 GLU   B O      1 
ATOM   4588  C  CB     . GLU   B 2  157 ? -38.249 -56.696  26.617  1.00 50.83  ? 157 GLU   B CB     1 
ATOM   4589  C  CG     . GLU   B 2  157 ? -39.716 -56.326  26.697  1.00 59.06  ? 157 GLU   B CG     1 
ATOM   4590  C  CD     . GLU   B 2  157 ? -40.121 -55.430  25.527  1.00 72.69  ? 157 GLU   B CD     1 
ATOM   4591  O  OE1    . GLU   B 2  157 ? -39.372 -55.440  24.511  1.00 66.39  ? 157 GLU   B OE1    1 
ATOM   4592  O  OE2    . GLU   B 2  157 ? -41.138 -54.690  25.636  1.00 75.62  ? 157 GLU   B OE2    1 
ATOM   4593  N  N      . GLU   B 2  158 ? -37.503 -59.710  26.418  1.00 41.01  ? 158 GLU   B N      1 
ATOM   4594  C  CA     . GLU   B 2  158 ? -37.860 -61.056  26.009  1.00 42.40  ? 158 GLU   B CA     1 
ATOM   4595  C  C      . GLU   B 2  158 ? -37.369 -62.102  27.007  1.00 49.49  ? 158 GLU   B C      1 
ATOM   4596  O  O      . GLU   B 2  158 ? -38.012 -63.148  27.155  1.00 52.33  ? 158 GLU   B O      1 
ATOM   4597  C  CB     . GLU   B 2  158 ? -37.307 -61.322  24.609  1.00 39.07  ? 158 GLU   B CB     1 
ATOM   4598  C  CG     . GLU   B 2  158 ? -37.832 -62.582  23.951  1.00 50.68  ? 158 GLU   B CG     1 
ATOM   4599  C  CD     . GLU   B 2  158 ? -37.507 -62.659  22.447  1.00 62.04  ? 158 GLU   B CD     1 
ATOM   4600  O  OE1    . GLU   B 2  158 ? -37.349 -61.587  21.815  1.00 64.41  ? 158 GLU   B OE1    1 
ATOM   4601  O  OE2    . GLU   B 2  158 ? -37.382 -63.788  21.900  1.00 60.06  ? 158 GLU   B OE2    1 
ATOM   4602  N  N      . TYR   B 2  159 ? -36.251 -61.845  27.698  1.00 45.25  ? 159 TYR   B N      1 
ATOM   4603  C  CA     . TYR   B 2  159 ? -35.656 -62.801  28.637  1.00 42.66  ? 159 TYR   B CA     1 
ATOM   4604  C  C      . TYR   B 2  159 ? -35.423 -62.105  29.969  1.00 44.67  ? 159 TYR   B C      1 
ATOM   4605  O  O      . TYR   B 2  159 ? -34.308 -62.072  30.496  1.00 48.94  ? 159 TYR   B O      1 
ATOM   4606  C  CB     . TYR   B 2  159 ? -34.356 -63.383  28.090  1.00 34.98  ? 159 TYR   B CB     1 
ATOM   4607  C  CG     . TYR   B 2  159 ? -34.453 -63.946  26.699  1.00 43.93  ? 159 TYR   B CG     1 
ATOM   4608  C  CD1    . TYR   B 2  159 ? -34.333 -63.120  25.591  1.00 46.37  ? 159 TYR   B CD1    1 
ATOM   4609  C  CD2    . TYR   B 2  159 ? -34.604 -65.313  26.484  1.00 43.68  ? 159 TYR   B CD2    1 
ATOM   4610  C  CE1    . TYR   B 2  159 ? -34.402 -63.633  24.310  1.00 46.92  ? 159 TYR   B CE1    1 
ATOM   4611  C  CE2    . TYR   B 2  159 ? -34.664 -65.836  25.205  1.00 41.59  ? 159 TYR   B CE2    1 
ATOM   4612  C  CZ     . TYR   B 2  159 ? -34.563 -64.991  24.122  1.00 47.76  ? 159 TYR   B CZ     1 
ATOM   4613  O  OH     . TYR   B 2  159 ? -34.625 -65.489  22.840  1.00 52.58  ? 159 TYR   B OH     1 
ATOM   4614  N  N      . PRO   B 2  160 ? -36.472 -61.539  30.554  1.00 41.88  ? 160 PRO   B N      1 
ATOM   4615  C  CA     . PRO   B 2  160 ? -36.280 -60.599  31.671  1.00 43.75  ? 160 PRO   B CA     1 
ATOM   4616  C  C      . PRO   B 2  160 ? -35.536 -61.179  32.856  1.00 41.60  ? 160 PRO   B C      1 
ATOM   4617  O  O      . PRO   B 2  160 ? -35.071 -60.402  33.708  1.00 38.21  ? 160 PRO   B O      1 
ATOM   4618  C  CB     . PRO   B 2  160 ? -37.709 -60.223  32.053  1.00 39.56  ? 160 PRO   B CB     1 
ATOM   4619  C  CG     . PRO   B 2  160 ? -38.490 -61.411  31.627  1.00 49.26  ? 160 PRO   B CG     1 
ATOM   4620  C  CD     . PRO   B 2  160 ? -37.873 -61.907  30.358  1.00 41.12  ? 160 PRO   B CD     1 
ATOM   4621  N  N      . ASP   B 2  161 ? -35.393 -62.502  32.931  1.00 40.42  ? 161 ASP   B N      1 
ATOM   4622  C  CA     . ASP   B 2  161 ? -34.876 -63.163  34.124  1.00 45.14  ? 161 ASP   B CA     1 
ATOM   4623  C  C      . ASP   B 2  161 ? -33.604 -63.962  33.861  1.00 43.98  ? 161 ASP   B C      1 
ATOM   4624  O  O      . ASP   B 2  161 ? -33.201 -64.748  34.719  1.00 49.16  ? 161 ASP   B O      1 
ATOM   4625  C  CB     . ASP   B 2  161 ? -35.935 -64.102  34.682  1.00 44.59  ? 161 ASP   B CB     1 
ATOM   4626  C  CG     . ASP   B 2  161 ? -36.197 -65.243  33.744  1.00 56.14  ? 161 ASP   B CG     1 
ATOM   4627  O  OD1    . ASP   B 2  161 ? -35.908 -65.087  32.536  1.00 55.77  ? 161 ASP   B OD1    1 
ATOM   4628  O  OD2    . ASP   B 2  161 ? -36.695 -66.290  34.197  1.00 71.55  ? 161 ASP   B OD2    1 
ATOM   4629  N  N      . ARG   B 2  162 ? -32.994 -63.824  32.690  1.00 42.72  ? 162 ARG   B N      1 
ATOM   4630  C  CA     . ARG   B 2  162 ? -31.658 -64.339  32.431  1.00 44.10  ? 162 ARG   B CA     1 
ATOM   4631  C  C      . ARG   B 2  162 ? -30.609 -63.272  32.798  1.00 40.67  ? 162 ARG   B C      1 
ATOM   4632  O  O      . ARG   B 2  162 ? -30.926 -62.123  33.117  1.00 38.65  ? 162 ARG   B O      1 
ATOM   4633  C  CB     . ARG   B 2  162 ? -31.533 -64.792  30.964  1.00 40.16  ? 162 ARG   B CB     1 
ATOM   4634  C  CG     . ARG   B 2  162 ? -32.429 -65.990  30.576  1.00 42.79  ? 162 ARG   B CG     1 
ATOM   4635  C  CD     . ARG   B 2  162 ? -32.331 -67.112  31.618  1.00 58.90  ? 162 ARG   B CD     1 
ATOM   4636  N  NE     . ARG   B 2  162 ? -32.727 -68.445  31.155  1.00 70.74  ? 162 ARG   B NE     1 
ATOM   4637  C  CZ     . ARG   B 2  162 ? -33.931 -68.984  31.333  1.00 67.97  ? 162 ARG   B CZ     1 
ATOM   4638  N  NH1    . ARG   B 2  162 ? -34.905 -68.316  31.925  1.00 70.38  ? 162 ARG   B NH1    1 
ATOM   4639  N  NH2    . ARG   B 2  162 ? -34.156 -70.228  30.922  1.00 63.07  ? 162 ARG   B NH2    1 
ATOM   4640  N  N      . ILE   B 2  163 ? -29.355 -63.656  32.782  1.00 38.30  ? 163 ILE   B N      1 
ATOM   4641  C  CA     . ILE   B 2  163 ? -28.298 -62.726  33.178  1.00 42.75  ? 163 ILE   B CA     1 
ATOM   4642  C  C      . ILE   B 2  163 ? -27.740 -61.988  31.971  1.00 41.50  ? 163 ILE   B C      1 
ATOM   4643  O  O      . ILE   B 2  163 ? -27.520 -62.576  30.899  1.00 38.46  ? 163 ILE   B O      1 
ATOM   4644  C  CB     . ILE   B 2  163 ? -27.183 -63.451  33.955  1.00 42.09  ? 163 ILE   B CB     1 
ATOM   4645  C  CG1    . ILE   B 2  163 ? -27.754 -63.971  35.273  1.00 38.75  ? 163 ILE   B CG1    1 
ATOM   4646  C  CG2    . ILE   B 2  163 ? -25.999 -62.533  34.173  1.00 34.21  ? 163 ILE   B CG2    1 
ATOM   4647  C  CD1    . ILE   B 2  163 ? -27.929 -62.864  36.296  1.00 33.39  ? 163 ILE   B CD1    1 
ATOM   4648  N  N      . MET   B 2  164 ? -27.497 -60.688  32.154  1.00 37.31  ? 164 MET   B N      1 
ATOM   4649  C  CA     . MET   B 2  164 ? -26.967 -59.829  31.102  1.00 37.38  ? 164 MET   B CA     1 
ATOM   4650  C  C      . MET   B 2  164 ? -25.564 -59.361  31.481  1.00 37.74  ? 164 MET   B C      1 
ATOM   4651  O  O      . MET   B 2  164 ? -25.383 -58.632  32.462  1.00 33.83  ? 164 MET   B O      1 
ATOM   4652  C  CB     . MET   B 2  164 ? -27.911 -58.655  30.826  1.00 37.48  ? 164 MET   B CB     1 
ATOM   4653  C  CG     . MET   B 2  164 ? -27.492 -57.734  29.657  1.00 43.51  ? 164 MET   B CG     1 
ATOM   4654  S  SD     . MET   B 2  164 ? -27.074 -58.481  28.030  1.00 42.44  ? 164 MET   B SD     1 
ATOM   4655  C  CE     . MET   B 2  164 ? -28.661 -59.180  27.567  1.00 42.90  ? 164 MET   B CE     1 
ATOM   4656  N  N      . ASN   B 2  165 ? -24.585 -59.783  30.678  1.00 41.56  ? 165 ASN   B N      1 
ATOM   4657  C  CA     . ASN   B 2  165 ? -23.161 -59.568  30.906  1.00 42.49  ? 165 ASN   B CA     1 
ATOM   4658  C  C      . ASN   B 2  165 ? -22.570 -58.822  29.709  1.00 43.67  ? 165 ASN   B C      1 
ATOM   4659  O  O      . ASN   B 2  165 ? -22.789 -59.231  28.558  1.00 40.31  ? 165 ASN   B O      1 
ATOM   4660  C  CB     . ASN   B 2  165 ? -22.452 -60.912  31.038  1.00 41.60  ? 165 ASN   B CB     1 
ATOM   4661  C  CG     . ASN   B 2  165 ? -21.014 -60.765  31.387  1.00 42.92  ? 165 ASN   B CG     1 
ATOM   4662  O  OD1    . ASN   B 2  165 ? -20.693 -60.259  32.465  1.00 46.67  ? 165 ASN   B OD1    1 
ATOM   4663  N  ND2    . ASN   B 2  165 ? -20.127 -61.135  30.465  1.00 41.75  ? 165 ASN   B ND2    1 
ATOM   4664  N  N      . THR   B 2  166 ? -21.816 -57.740  29.961  1.00 36.65  ? 166 THR   B N      1 
ATOM   4665  C  CA     . THR   B 2  166 ? -21.072 -57.109  28.876  1.00 39.22  ? 166 THR   B CA     1 
ATOM   4666  C  C      . THR   B 2  166 ? -19.606 -56.943  29.230  1.00 39.91  ? 166 THR   B C      1 
ATOM   4667  O  O      . THR   B 2  166 ? -19.240 -56.813  30.401  1.00 36.27  ? 166 THR   B O      1 
ATOM   4668  C  CB     . THR   B 2  166 ? -21.573 -55.717  28.481  1.00 40.25  ? 166 THR   B CB     1 
ATOM   4669  O  OG1    . THR   B 2  166 ? -21.159 -54.758  29.465  1.00 41.99  ? 166 THR   B OG1    1 
ATOM   4670  C  CG2    . THR   B 2  166 ? -23.069 -55.707  28.351  1.00 43.60  ? 166 THR   B CG2    1 
ATOM   4671  N  N      . PHE   B 2  167 ? -18.786 -56.936  28.171  1.00 40.25  ? 167 PHE   B N      1 
ATOM   4672  C  CA     . PHE   B 2  167 ? -17.423 -56.412  28.160  1.00 35.56  ? 167 PHE   B CA     1 
ATOM   4673  C  C      . PHE   B 2  167 ? -17.463 -55.123  27.338  1.00 33.28  ? 167 PHE   B C      1 
ATOM   4674  O  O      . PHE   B 2  167 ? -17.626 -55.171  26.117  1.00 36.58  ? 167 PHE   B O      1 
ATOM   4675  C  CB     . PHE   B 2  167 ? -16.472 -57.416  27.521  1.00 37.90  ? 167 PHE   B CB     1 
ATOM   4676  C  CG     . PHE   B 2  167 ? -16.358 -58.705  28.263  1.00 41.64  ? 167 PHE   B CG     1 
ATOM   4677  C  CD1    . PHE   B 2  167 ? -17.256 -59.738  28.010  1.00 40.98  ? 167 PHE   B CD1    1 
ATOM   4678  C  CD2    . PHE   B 2  167 ? -15.352 -58.898  29.200  1.00 36.14  ? 167 PHE   B CD2    1 
ATOM   4679  C  CE1    . PHE   B 2  167 ? -17.155 -60.937  28.680  1.00 43.21  ? 167 PHE   B CE1    1 
ATOM   4680  C  CE2    . PHE   B 2  167 ? -15.234 -60.084  29.865  1.00 36.75  ? 167 PHE   B CE2    1 
ATOM   4681  C  CZ     . PHE   B 2  167 ? -16.136 -61.107  29.616  1.00 46.49  ? 167 PHE   B CZ     1 
ATOM   4682  N  N      . SER   B 2  168 ? -17.337 -53.974  27.984  1.00 33.42  ? 168 SER   B N      1 
ATOM   4683  C  CA     . SER   B 2  168 ? -17.565 -52.691  27.325  1.00 34.23  ? 168 SER   B CA     1 
ATOM   4684  C  C      . SER   B 2  168 ? -16.257 -51.914  27.268  1.00 35.90  ? 168 SER   B C      1 
ATOM   4685  O  O      . SER   B 2  168 ? -15.749 -51.499  28.315  1.00 39.03  ? 168 SER   B O      1 
ATOM   4686  C  CB     . SER   B 2  168 ? -18.635 -51.872  28.073  1.00 35.01  ? 168 SER   B CB     1 
ATOM   4687  O  OG     . SER   B 2  168 ? -19.867 -52.570  28.174  1.00 36.41  ? 168 SER   B OG     1 
ATOM   4688  N  N      . VAL   B 2  169 ? -15.743 -51.665  26.060  1.00 29.50  ? 169 VAL   B N      1 
ATOM   4689  C  CA     . VAL   B 2  169 ? -14.537 -50.847  25.890  1.00 32.09  ? 169 VAL   B CA     1 
ATOM   4690  C  C      . VAL   B 2  169 ? -14.851 -49.366  26.091  1.00 31.24  ? 169 VAL   B C      1 
ATOM   4691  O  O      . VAL   B 2  169 ? -15.595 -48.778  25.304  1.00 36.33  ? 169 VAL   B O      1 
ATOM   4692  C  CB     . VAL   B 2  169 ? -13.911 -51.079  24.513  1.00 28.37  ? 169 VAL   B CB     1 
ATOM   4693  C  CG1    . VAL   B 2  169 ? -12.702 -50.225  24.360  1.00 27.45  ? 169 VAL   B CG1    1 
ATOM   4694  C  CG2    . VAL   B 2  169 ? -13.574 -52.535  24.364  1.00 32.34  ? 169 VAL   B CG2    1 
ATOM   4695  N  N      . MET   B 2  170 ? -14.236 -48.738  27.113  1.00 31.82  ? 170 MET   B N      1 
ATOM   4696  C  CA     . MET   B 2  170 ? -14.413 -47.288  27.294  1.00 37.38  ? 170 MET   B CA     1 
ATOM   4697  C  C      . MET   B 2  170 ? -13.508 -46.511  26.347  1.00 39.74  ? 170 MET   B C      1 
ATOM   4698  O  O      . MET   B 2  170 ? -12.324 -46.839  26.216  1.00 38.37  ? 170 MET   B O      1 
ATOM   4699  C  CB     . MET   B 2  170 ? -14.105 -46.823  28.721  1.00 42.14  ? 170 MET   B CB     1 
ATOM   4700  C  CG     . MET   B 2  170 ? -14.395 -47.856  29.736  1.00 47.15  ? 170 MET   B CG     1 
ATOM   4701  S  SD     . MET   B 2  170 ? -16.160 -48.093  29.669  1.00 59.62  ? 170 MET   B SD     1 
ATOM   4702  C  CE     . MET   B 2  170 ? -16.687 -46.749  30.706  1.00 52.26  ? 170 MET   B CE     1 
ATOM   4703  N  N      . PRO   B 2  171 ? -14.010 -45.458  25.717  1.00 38.95  ? 171 PRO   B N      1 
ATOM   4704  C  CA     . PRO   B 2  171 ? -13.164 -44.652  24.845  1.00 35.53  ? 171 PRO   B CA     1 
ATOM   4705  C  C      . PRO   B 2  171 ? -12.125 -43.875  25.624  1.00 40.14  ? 171 PRO   B C      1 
ATOM   4706  O  O      . PRO   B 2  171 ? -12.342 -43.465  26.763  1.00 42.14  ? 171 PRO   B O      1 
ATOM   4707  C  CB     . PRO   B 2  171 ? -14.160 -43.710  24.182  1.00 35.12  ? 171 PRO   B CB     1 
ATOM   4708  C  CG     . PRO   B 2  171 ? -15.227 -43.559  25.194  1.00 36.82  ? 171 PRO   B CG     1 
ATOM   4709  C  CD     . PRO   B 2  171 ? -15.359 -44.885  25.863  1.00 39.40  ? 171 PRO   B CD     1 
ATOM   4710  N  N      . SER   B 2  172 ? -10.979 -43.662  24.977  1.00 47.11  ? 172 SER   B N      1 
ATOM   4711  C  CA     . SER   B 2  172 ? -9.941  -42.791  25.500  1.00 41.19  ? 172 SER   B CA     1 
ATOM   4712  C  C      . SER   B 2  172 ? -9.420  -41.876  24.402  1.00 43.46  ? 172 SER   B C      1 
ATOM   4713  O  O      . SER   B 2  172 ? -9.177  -42.343  23.275  1.00 50.63  ? 172 SER   B O      1 
ATOM   4714  C  CB     . SER   B 2  172 ? -8.784  -43.593  26.074  1.00 41.51  ? 172 SER   B CB     1 
ATOM   4715  O  OG     . SER   B 2  172 ? -7.868  -42.697  26.650  1.00 46.07  ? 172 SER   B OG     1 
ATOM   4716  N  N      . PRO   B 2  173 ? -9.230  -40.594  24.679  1.00 40.90  ? 173 PRO   B N      1 
ATOM   4717  C  CA     . PRO   B 2  173 ? -8.528  -39.746  23.700  1.00 35.47  ? 173 PRO   B CA     1 
ATOM   4718  C  C      . PRO   B 2  173 ? -7.203  -40.324  23.266  1.00 37.24  ? 173 PRO   B C      1 
ATOM   4719  O  O      . PRO   B 2  173 ? -6.876  -40.258  22.082  1.00 41.66  ? 173 PRO   B O      1 
ATOM   4720  C  CB     . PRO   B 2  173 ? -8.352  -38.427  24.441  1.00 30.50  ? 173 PRO   B CB     1 
ATOM   4721  C  CG     . PRO   B 2  173 ? -9.484  -38.410  25.426  1.00 40.36  ? 173 PRO   B CG     1 
ATOM   4722  C  CD     . PRO   B 2  173 ? -9.732  -39.839  25.832  1.00 43.29  ? 173 PRO   B CD     1 
ATOM   4723  N  N      . LYS   B 2  174 ? -6.446  -40.935  24.183  1.00 40.78  ? 174 LYS   B N      1 
ATOM   4724  C  CA     . LYS   B 2  174 ? -5.209  -41.606  23.797  1.00 37.98  ? 174 LYS   B CA     1 
ATOM   4725  C  C      . LYS   B 2  174 ? -5.427  -42.621  22.690  1.00 38.51  ? 174 LYS   B C      1 
ATOM   4726  O  O      . LYS   B 2  174 ? -4.469  -42.967  21.996  1.00 45.07  ? 174 LYS   B O      1 
ATOM   4727  C  CB     . LYS   B 2  174 ? -4.554  -42.324  24.978  1.00 41.45  ? 174 LYS   B CB     1 
ATOM   4728  C  CG     . LYS   B 2  174 ? -4.346  -41.521  26.260  1.00 44.06  ? 174 LYS   B CG     1 
ATOM   4729  C  CD     . LYS   B 2  174 ? -3.454  -42.323  27.186  1.00 47.05  ? 174 LYS   B CD     1 
ATOM   4730  C  CE     . LYS   B 2  174 ? -3.577  -41.850  28.613  1.00 51.46  ? 174 LYS   B CE     1 
ATOM   4731  N  NZ     . LYS   B 2  174 ? -2.541  -42.413  29.537  1.00 53.19  ? 174 LYS   B NZ     1 
ATOM   4732  N  N      . VAL   B 2  175 ? -6.643  -43.129  22.512  1.00 39.97  ? 175 VAL   B N      1 
ATOM   4733  C  CA     . VAL   B 2  175 ? -6.892  -44.078  21.428  1.00 43.08  ? 175 VAL   B CA     1 
ATOM   4734  C  C      . VAL   B 2  175 ? -8.319  -43.853  20.936  1.00 44.69  ? 175 VAL   B C      1 
ATOM   4735  O  O      . VAL   B 2  175 ? -9.222  -44.635  21.254  1.00 54.43  ? 175 VAL   B O      1 
ATOM   4736  C  CB     . VAL   B 2  175 ? -6.687  -45.541  21.887  1.00 38.95  ? 175 VAL   B CB     1 
ATOM   4737  C  CG1    . VAL   B 2  175 ? -6.810  -46.506  20.734  1.00 35.59  ? 175 VAL   B CG1    1 
ATOM   4738  C  CG2    . VAL   B 2  175 ? -5.381  -45.719  22.615  1.00 45.71  ? 175 VAL   B CG2    1 
ATOM   4739  N  N      . SER   B 2  176 ? -8.561  -42.786  20.178  1.00 40.41  ? 176 SER   B N      1 
ATOM   4740  C  CA     . SER   B 2  176 ? -9.926  -42.446  19.818  1.00 41.17  ? 176 SER   B CA     1 
ATOM   4741  C  C      . SER   B 2  176 ? -10.067 -42.281  18.319  1.00 36.94  ? 176 SER   B C      1 
ATOM   4742  O  O      . SER   B 2  176 ? -9.158  -41.777  17.663  1.00 41.81  ? 176 SER   B O      1 
ATOM   4743  C  CB     . SER   B 2  176 ? -10.379 -41.169  20.494  1.00 43.91  ? 176 SER   B CB     1 
ATOM   4744  O  OG     . SER   B 2  176 ? -9.885  -40.077  19.786  1.00 47.77  ? 176 SER   B OG     1 
ATOM   4745  N  N      . ASP   B 2  177 ? -11.233 -42.693  17.795  1.00 36.70  ? 177 ASP   B N      1 
ATOM   4746  C  CA     . ASP   B 2  177 ? -11.595 -42.501  16.389  1.00 41.61  ? 177 ASP   B CA     1 
ATOM   4747  C  C      . ASP   B 2  177 ? -12.277 -41.174  16.089  1.00 45.02  ? 177 ASP   B C      1 
ATOM   4748  O  O      . ASP   B 2  177 ? -12.165 -40.687  14.958  1.00 44.55  ? 177 ASP   B O      1 
ATOM   4749  C  CB     . ASP   B 2  177 ? -12.564 -43.580  15.871  1.00 49.01  ? 177 ASP   B CB     1 
ATOM   4750  C  CG     . ASP   B 2  177 ? -12.017 -44.986  15.976  1.00 53.82  ? 177 ASP   B CG     1 
ATOM   4751  O  OD1    . ASP   B 2  177 ? -10.830 -45.093  16.385  1.00 47.89  ? 177 ASP   B OD1    1 
ATOM   4752  O  OD2    . ASP   B 2  177 ? -12.754 -45.951  15.550  1.00 49.99  ? 177 ASP   B OD2    1 
ATOM   4753  N  N      . THR   B 2  178 ? -13.035 -40.603  17.027  1.00 41.56  ? 178 THR   B N      1 
ATOM   4754  C  CA     . THR   B 2  178 ? -13.826 -39.425  16.696  1.00 40.71  ? 178 THR   B CA     1 
ATOM   4755  C  C      . THR   B 2  178 ? -14.097 -38.634  17.959  1.00 35.78  ? 178 THR   B C      1 
ATOM   4756  O  O      . THR   B 2  178 ? -13.982 -39.151  19.062  1.00 37.94  ? 178 THR   B O      1 
ATOM   4757  C  CB     . THR   B 2  178 ? -15.146 -39.793  15.990  1.00 41.45  ? 178 THR   B CB     1 
ATOM   4758  O  OG1    . THR   B 2  178 ? -15.831 -40.818  16.723  1.00 41.20  ? 178 THR   B OG1    1 
ATOM   4759  C  CG2    . THR   B 2  178 ? -14.898 -40.270  14.565  1.00 44.25  ? 178 THR   B CG2    1 
ATOM   4760  N  N      . VAL   B 2  179 ? -14.449 -37.360  17.778  1.00 34.35  ? 179 VAL   B N      1 
ATOM   4761  C  CA     . VAL   B 2  179 ? -14.611 -36.448  18.904  1.00 35.74  ? 179 VAL   B CA     1 
ATOM   4762  C  C      . VAL   B 2  179 ? -15.864 -36.732  19.698  1.00 42.78  ? 179 VAL   B C      1 
ATOM   4763  O  O      . VAL   B 2  179 ? -15.955 -36.336  20.874  1.00 40.55  ? 179 VAL   B O      1 
ATOM   4764  C  CB     . VAL   B 2  179 ? -14.692 -34.990  18.446  1.00 38.58  ? 179 VAL   B CB     1 
ATOM   4765  C  CG1    . VAL   B 2  179 ? -13.330 -34.458  18.163  1.00 43.27  ? 179 VAL   B CG1    1 
ATOM   4766  C  CG2    . VAL   B 2  179 ? -15.549 -34.911  17.222  1.00 40.41  ? 179 VAL   B CG2    1 
ATOM   4767  N  N      . VAL   B 2  180 ? -16.845 -37.391  19.072  1.00 41.94  ? 180 VAL   B N      1 
ATOM   4768  C  CA     . VAL   B 2  180 ? -18.133 -37.631  19.712  1.00 36.85  ? 180 VAL   B CA     1 
ATOM   4769  C  C      . VAL   B 2  180 ? -18.134 -38.838  20.635  1.00 40.82  ? 180 VAL   B C      1 
ATOM   4770  O  O      . VAL   B 2  180 ? -19.176 -39.145  21.230  1.00 41.95  ? 180 VAL   B O      1 
ATOM   4771  C  CB     . VAL   B 2  180 ? -19.192 -37.789  18.614  1.00 32.64  ? 180 VAL   B CB     1 
ATOM   4772  C  CG1    . VAL   B 2  180 ? -19.434 -36.448  17.986  1.00 33.43  ? 180 VAL   B CG1    1 
ATOM   4773  C  CG2    . VAL   B 2  180 ? -18.703 -38.789  17.597  1.00 30.58  ? 180 VAL   B CG2    1 
ATOM   4774  N  N      . GLU   B 2  181 ? -17.002 -39.527  20.791  1.00 37.48  ? 181 GLU   B N      1 
ATOM   4775  C  CA     . GLU   B 2  181 ? -17.007 -40.755  21.573  1.00 33.55  ? 181 GLU   B CA     1 
ATOM   4776  C  C      . GLU   B 2  181 ? -17.484 -40.525  22.996  1.00 32.97  ? 181 GLU   B C      1 
ATOM   4777  O  O      . GLU   B 2  181 ? -18.096 -41.451  23.551  1.00 35.57  ? 181 GLU   B O      1 
ATOM   4778  C  CB     . GLU   B 2  181 ? -15.610 -41.368  21.569  1.00 35.08  ? 181 GLU   B CB     1 
ATOM   4779  C  CG     . GLU   B 2  181 ? -15.101 -41.642  20.174  1.00 41.64  ? 181 GLU   B CG     1 
ATOM   4780  C  CD     . GLU   B 2  181 ? -13.729 -42.285  20.139  1.00 42.32  ? 181 GLU   B CD     1 
ATOM   4781  O  OE1    . GLU   B 2  181 ? -13.016 -42.213  21.172  1.00 43.14  ? 181 GLU   B OE1    1 
ATOM   4782  O  OE2    . GLU   B 2  181 ? -13.322 -42.724  19.035  1.00 41.76  ? 181 GLU   B OE2    1 
ATOM   4783  N  N      . PRO   B 2  182 ? -17.249 -39.369  23.632  1.00 30.10  ? 182 PRO   B N      1 
ATOM   4784  C  CA     . PRO   B 2  182 ? -17.826 -39.150  24.965  1.00 31.51  ? 182 PRO   B CA     1 
ATOM   4785  C  C      . PRO   B 2  182 ? -19.346 -39.078  24.964  1.00 34.92  ? 182 PRO   B C      1 
ATOM   4786  O  O      . PRO   B 2  182 ? -19.969 -39.537  25.927  1.00 37.58  ? 182 PRO   B O      1 
ATOM   4787  C  CB     . PRO   B 2  182 ? -17.201 -37.817  25.402  1.00 33.08  ? 182 PRO   B CB     1 
ATOM   4788  C  CG     . PRO   B 2  182 ? -16.002 -37.698  24.620  1.00 32.97  ? 182 PRO   B CG     1 
ATOM   4789  C  CD     . PRO   B 2  182 ? -16.326 -38.283  23.280  1.00 31.06  ? 182 PRO   B CD     1 
ATOM   4790  N  N      . TYR   B 2  183 ? -19.962 -38.486  23.933  1.00 38.68  ? 183 TYR   B N      1 
ATOM   4791  C  CA     . TYR   B 2  183 ? -21.420 -38.530  23.803  1.00 34.07  ? 183 TYR   B CA     1 
ATOM   4792  C  C      . TYR   B 2  183 ? -21.906 -39.968  23.753  1.00 32.34  ? 183 TYR   B C      1 
ATOM   4793  O  O      . TYR   B 2  183 ? -22.806 -40.362  24.498  1.00 30.93  ? 183 TYR   B O      1 
ATOM   4794  C  CB     . TYR   B 2  183 ? -21.876 -37.785  22.542  1.00 30.64  ? 183 TYR   B CB     1 
ATOM   4795  C  CG     . TYR   B 2  183 ? -21.857 -36.282  22.610  1.00 30.26  ? 183 TYR   B CG     1 
ATOM   4796  C  CD1    . TYR   B 2  183 ? -21.918 -35.619  23.817  1.00 37.71  ? 183 TYR   B CD1    1 
ATOM   4797  C  CD2    . TYR   B 2  183 ? -21.799 -35.517  21.452  1.00 36.95  ? 183 TYR   B CD2    1 
ATOM   4798  C  CE1    . TYR   B 2  183 ? -21.910 -34.219  23.881  1.00 42.08  ? 183 TYR   B CE1    1 
ATOM   4799  C  CE2    . TYR   B 2  183 ? -21.789 -34.109  21.490  1.00 31.70  ? 183 TYR   B CE2    1 
ATOM   4800  C  CZ     . TYR   B 2  183 ? -21.848 -33.468  22.701  1.00 38.56  ? 183 TYR   B CZ     1 
ATOM   4801  O  OH     . TYR   B 2  183 ? -21.836 -32.088  22.752  1.00 35.43  ? 183 TYR   B OH     1 
ATOM   4802  N  N      . ASN   B 2  184 ? -21.313 -40.773  22.875  1.00 32.29  ? 184 ASN   B N      1 
ATOM   4803  C  CA     . ASN   B 2  184 ? -21.764 -42.147  22.728  1.00 34.48  ? 184 ASN   B CA     1 
ATOM   4804  C  C      . ASN   B 2  184 ? -21.623 -42.914  24.040  1.00 37.15  ? 184 ASN   B C      1 
ATOM   4805  O  O      . ASN   B 2  184 ? -22.518 -43.670  24.431  1.00 38.62  ? 184 ASN   B O      1 
ATOM   4806  C  CB     . ASN   B 2  184 ? -20.968 -42.816  21.617  1.00 37.35  ? 184 ASN   B CB     1 
ATOM   4807  C  CG     . ASN   B 2  184 ? -21.207 -42.163  20.276  1.00 40.89  ? 184 ASN   B CG     1 
ATOM   4808  O  OD1    . ASN   B 2  184 ? -22.144 -41.366  20.146  1.00 43.81  ? 184 ASN   B OD1    1 
ATOM   4809  N  ND2    . ASN   B 2  184 ? -20.366 -42.484  19.268  1.00 29.65  ? 184 ASN   B ND2    1 
ATOM   4810  N  N      . ALA   B 2  185 ? -20.511 -42.724  24.744  1.00 35.08  ? 185 ALA   B N      1 
ATOM   4811  C  CA     . ALA   B 2  185 ? -20.280 -43.485  25.964  1.00 33.12  ? 185 ALA   B CA     1 
ATOM   4812  C  C      . ALA   B 2  185 ? -21.267 -43.096  27.058  1.00 36.66  ? 185 ALA   B C      1 
ATOM   4813  O  O      . ALA   B 2  185 ? -21.784 -43.968  27.768  1.00 41.11  ? 185 ALA   B O      1 
ATOM   4814  C  CB     . ALA   B 2  185 ? -18.837 -43.288  26.422  1.00 34.77  ? 185 ALA   B CB     1 
ATOM   4815  N  N      . THR   B 2  186 ? -21.558 -41.797  27.205  1.00 33.87  ? 186 THR   B N      1 
ATOM   4816  C  CA     . THR   B 2  186 ? -22.478 -41.371  28.261  1.00 34.64  ? 186 THR   B CA     1 
ATOM   4817  C  C      . THR   B 2  186 ? -23.894 -41.862  28.007  1.00 38.40  ? 186 THR   B C      1 
ATOM   4818  O  O      . THR   B 2  186 ? -24.648 -42.124  28.951  1.00 41.40  ? 186 THR   B O      1 
ATOM   4819  C  CB     . THR   B 2  186 ? -22.519 -39.866  28.374  1.00 29.49  ? 186 THR   B CB     1 
ATOM   4820  O  OG1    . THR   B 2  186 ? -21.201 -39.367  28.576  1.00 33.07  ? 186 THR   B OG1    1 
ATOM   4821  C  CG2    . THR   B 2  186 ? -23.385 -39.499  29.539  1.00 33.02  ? 186 THR   B CG2    1 
ATOM   4822  N  N      . LEU   B 2  187 ? -24.284 -41.945  26.742  1.00 35.42  ? 187 LEU   B N      1 
ATOM   4823  C  CA     . LEU   B 2  187 ? -25.579 -42.507  26.408  1.00 38.56  ? 187 LEU   B CA     1 
ATOM   4824  C  C      . LEU   B 2  187 ? -25.610 -43.987  26.769  1.00 41.67  ? 187 LEU   B C      1 
ATOM   4825  O  O      . LEU   B 2  187 ? -26.513 -44.437  27.483  1.00 48.30  ? 187 LEU   B O      1 
ATOM   4826  C  CB     . LEU   B 2  187 ? -25.876 -42.271  24.918  1.00 36.60  ? 187 LEU   B CB     1 
ATOM   4827  C  CG     . LEU   B 2  187 ? -26.005 -40.778  24.542  1.00 36.90  ? 187 LEU   B CG     1 
ATOM   4828  C  CD1    . LEU   B 2  187 ? -26.020 -40.526  23.033  1.00 34.41  ? 187 LEU   B CD1    1 
ATOM   4829  C  CD2    . LEU   B 2  187 ? -27.235 -40.117  25.194  1.00 30.83  ? 187 LEU   B CD2    1 
ATOM   4830  N  N      . SER   B 2  188 ? -24.589 -44.745  26.351  1.00 37.44  ? 188 SER   B N      1 
ATOM   4831  C  CA     . SER   B 2  188 ? -24.568 -46.183  26.614  1.00 34.37  ? 188 SER   B CA     1 
ATOM   4832  C  C      . SER   B 2  188 ? -24.508 -46.487  28.102  1.00 37.36  ? 188 SER   B C      1 
ATOM   4833  O  O      . SER   B 2  188 ? -25.213 -47.380  28.588  1.00 36.05  ? 188 SER   B O      1 
ATOM   4834  C  CB     . SER   B 2  188 ? -23.380 -46.832  25.912  1.00 35.12  ? 188 SER   B CB     1 
ATOM   4835  O  OG     . SER   B 2  188 ? -23.498 -46.752  24.509  1.00 37.67  ? 188 SER   B OG     1 
ATOM   4836  N  N      . VAL   B 2  189 ? -23.650 -45.778  28.841  1.00 39.89  ? 189 VAL   B N      1 
ATOM   4837  C  CA     . VAL   B 2  189 ? -23.467 -46.105  30.249  1.00 36.34  ? 189 VAL   B CA     1 
ATOM   4838  C  C      . VAL   B 2  189 ? -24.783 -45.942  30.975  1.00 36.21  ? 189 VAL   B C      1 
ATOM   4839  O  O      . VAL   B 2  189 ? -25.107 -46.699  31.896  1.00 34.73  ? 189 VAL   B O      1 
ATOM   4840  C  CB     . VAL   B 2  189 ? -22.375 -45.223  30.863  1.00 36.09  ? 189 VAL   B CB     1 
ATOM   4841  C  CG1    . VAL   B 2  189 ? -22.478 -45.254  32.391  1.00 39.14  ? 189 VAL   B CG1    1 
ATOM   4842  C  CG2    . VAL   B 2  189 ? -20.989 -45.633  30.340  1.00 36.77  ? 189 VAL   B CG2    1 
ATOM   4843  N  N      . HIS   B 2  190 ? -25.574 -44.965  30.544  1.00 40.34  ? 190 HIS   B N      1 
ATOM   4844  C  CA     . HIS   B 2  190 ? -26.942 -44.811  31.017  1.00 45.62  ? 190 HIS   B CA     1 
ATOM   4845  C  C      . HIS   B 2  190 ? -27.726 -46.104  30.839  1.00 43.19  ? 190 HIS   B C      1 
ATOM   4846  O  O      . HIS   B 2  190 ? -28.374 -46.599  31.769  1.00 45.97  ? 190 HIS   B O      1 
ATOM   4847  C  CB     . HIS   B 2  190 ? -27.586 -43.657  30.251  1.00 45.16  ? 190 HIS   B CB     1 
ATOM   4848  C  CG     . HIS   B 2  190 ? -28.949 -43.297  30.739  1.00 49.85  ? 190 HIS   B CG     1 
ATOM   4849  N  ND1    . HIS   B 2  190 ? -29.708 -44.148  31.518  1.00 48.86  ? 190 HIS   B ND1    1 
ATOM   4850  C  CD2    . HIS   B 2  190 ? -29.674 -42.165  30.593  1.00 49.45  ? 190 HIS   B CD2    1 
ATOM   4851  C  CE1    . HIS   B 2  190 ? -30.854 -43.562  31.810  1.00 58.91  ? 190 HIS   B CE1    1 
ATOM   4852  N  NE2    . HIS   B 2  190 ? -30.856 -42.356  31.266  1.00 60.62  ? 190 HIS   B NE2    1 
ATOM   4853  N  N      . GLN   B 2  191 ? -27.684 -46.648  29.629  1.00 37.85  ? 191 GLN   B N      1 
ATOM   4854  C  CA     . GLN   B 2  191 ? -28.258 -47.955  29.358  1.00 39.82  ? 191 GLN   B CA     1 
ATOM   4855  C  C      . GLN   B 2  191 ? -27.711 -49.022  30.302  1.00 40.37  ? 191 GLN   B C      1 
ATOM   4856  O  O      . GLN   B 2  191 ? -28.474 -49.803  30.880  1.00 36.05  ? 191 GLN   B O      1 
ATOM   4857  C  CB     . GLN   B 2  191 ? -27.967 -48.305  27.908  1.00 37.79  ? 191 GLN   B CB     1 
ATOM   4858  C  CG     . GLN   B 2  191 ? -28.496 -47.240  27.037  1.00 37.56  ? 191 GLN   B CG     1 
ATOM   4859  C  CD     . GLN   B 2  191 ? -29.961 -47.333  26.972  1.00 36.81  ? 191 GLN   B CD     1 
ATOM   4860  O  OE1    . GLN   B 2  191 ? -30.500 -48.410  26.748  1.00 45.36  ? 191 GLN   B OE1    1 
ATOM   4861  N  NE2    . GLN   B 2  191 ? -30.634 -46.243  27.260  1.00 37.69  ? 191 GLN   B NE2    1 
ATOM   4862  N  N      . LEU   B 2  192 ? -26.386 -49.065  30.471  1.00 39.21  ? 192 LEU   B N      1 
ATOM   4863  C  CA     . LEU   B 2  192 ? -25.765 -50.167  31.190  1.00 34.53  ? 192 LEU   B CA     1 
ATOM   4864  C  C      . LEU   B 2  192 ? -26.083 -50.104  32.677  1.00 39.75  ? 192 LEU   B C      1 
ATOM   4865  O  O      . LEU   B 2  192 ? -26.251 -51.146  33.326  1.00 39.83  ? 192 LEU   B O      1 
ATOM   4866  C  CB     . LEU   B 2  192 ? -24.259 -50.153  30.946  1.00 33.25  ? 192 LEU   B CB     1 
ATOM   4867  C  CG     . LEU   B 2  192 ? -23.807 -50.312  29.490  1.00 33.03  ? 192 LEU   B CG     1 
ATOM   4868  C  CD1    . LEU   B 2  192 ? -22.323 -50.232  29.425  1.00 28.57  ? 192 LEU   B CD1    1 
ATOM   4869  C  CD2    . LEU   B 2  192 ? -24.290 -51.612  28.858  1.00 34.24  ? 192 LEU   B CD2    1 
ATOM   4870  N  N      . VAL   B 2  193 ? -26.185 -48.893  33.239  1.00 41.37  ? 193 VAL   B N      1 
ATOM   4871  C  CA     . VAL   B 2  193 ? -26.593 -48.786  34.641  1.00 43.61  ? 193 VAL   B CA     1 
ATOM   4872  C  C      . VAL   B 2  193 ? -27.893 -49.536  34.875  1.00 43.13  ? 193 VAL   B C      1 
ATOM   4873  O  O      . VAL   B 2  193 ? -28.118 -50.087  35.957  1.00 43.71  ? 193 VAL   B O      1 
ATOM   4874  C  CB     . VAL   B 2  193 ? -26.712 -47.306  35.075  1.00 41.82  ? 193 VAL   B CB     1 
ATOM   4875  C  CG1    . VAL   B 2  193 ? -27.526 -47.210  36.322  1.00 46.17  ? 193 VAL   B CG1    1 
ATOM   4876  C  CG2    . VAL   B 2  193 ? -25.365 -46.743  35.400  1.00 41.34  ? 193 VAL   B CG2    1 
ATOM   4877  N  N      . GLU   B 2  194 ? -28.749 -49.594  33.858  1.00 44.01  ? 194 GLU   B N      1 
ATOM   4878  C  CA     . GLU   B 2  194 ? -30.111 -50.084  33.968  1.00 43.27  ? 194 GLU   B CA     1 
ATOM   4879  C  C      . GLU   B 2  194 ? -30.290 -51.531  33.517  1.00 46.35  ? 194 GLU   B C      1 
ATOM   4880  O  O      . GLU   B 2  194 ? -31.121 -52.242  34.093  1.00 50.42  ? 194 GLU   B O      1 
ATOM   4881  C  CB     . GLU   B 2  194 ? -31.041 -49.189  33.141  1.00 50.13  ? 194 GLU   B CB     1 
ATOM   4882  C  CG     . GLU   B 2  194 ? -30.960 -47.727  33.516  1.00 55.01  ? 194 GLU   B CG     1 
ATOM   4883  C  CD     . GLU   B 2  194 ? -32.011 -47.338  34.514  1.00 67.35  ? 194 GLU   B CD     1 
ATOM   4884  O  OE1    . GLU   B 2  194 ? -33.180 -47.746  34.304  1.00 73.63  ? 194 GLU   B OE1    1 
ATOM   4885  O  OE2    . GLU   B 2  194 ? -31.659 -46.657  35.511  1.00 66.34  ? 194 GLU   B OE2    1 
ATOM   4886  N  N      . ASN   B 2  195 ? -29.564 -52.005  32.505  1.00 41.58  ? 195 ASN   B N      1 
ATOM   4887  C  CA     . ASN   B 2  195 ? -29.935 -53.263  31.867  1.00 39.53  ? 195 ASN   B CA     1 
ATOM   4888  C  C      . ASN   B 2  195 ? -28.837 -54.308  31.839  1.00 40.52  ? 195 ASN   B C      1 
ATOM   4889  O  O      . ASN   B 2  195 ? -28.984 -55.310  31.128  1.00 42.54  ? 195 ASN   B O      1 
ATOM   4890  C  CB     . ASN   B 2  195 ? -30.415 -53.015  30.440  1.00 39.71  ? 195 ASN   B CB     1 
ATOM   4891  C  CG     . ASN   B 2  195 ? -31.602 -52.141  30.398  1.00 42.90  ? 195 ASN   B CG     1 
ATOM   4892  O  OD1    . ASN   B 2  195 ? -32.453 -52.244  31.265  1.00 44.59  ? 195 ASN   B OD1    1 
ATOM   4893  N  ND2    . ASN   B 2  195 ? -31.685 -51.265  29.391  1.00 46.13  ? 195 ASN   B ND2    1 
ATOM   4894  N  N      . THR   B 2  196 ? -27.744 -54.129  32.562  1.00 37.43  ? 196 THR   B N      1 
ATOM   4895  C  CA     . THR   B 2  196 ? -26.823 -55.240  32.717  1.00 36.64  ? 196 THR   B CA     1 
ATOM   4896  C  C      . THR   B 2  196 ? -26.683 -55.566  34.196  1.00 41.12  ? 196 THR   B C      1 
ATOM   4897  O  O      . THR   B 2  196 ? -26.783 -54.676  35.055  1.00 35.63  ? 196 THR   B O      1 
ATOM   4898  C  CB     . THR   B 2  196 ? -25.455 -54.966  32.093  1.00 34.88  ? 196 THR   B CB     1 
ATOM   4899  O  OG1    . THR   B 2  196 ? -24.881 -53.804  32.686  1.00 40.34  ? 196 THR   B OG1    1 
ATOM   4900  C  CG2    . THR   B 2  196 ? -25.584 -54.743  30.661  1.00 35.46  ? 196 THR   B CG2    1 
ATOM   4901  N  N      . ASP   B 2  197 ? -26.520 -56.870  34.468  1.00 37.97  ? 197 ASP   B N      1 
ATOM   4902  C  CA     . ASP   B 2  197 ? -26.134 -57.338  35.793  1.00 36.58  ? 197 ASP   B CA     1 
ATOM   4903  C  C      . ASP   B 2  197 ? -24.630 -57.116  36.035  1.00 36.11  ? 197 ASP   B C      1 
ATOM   4904  O  O      . ASP   B 2  197 ? -24.229 -56.591  37.077  1.00 35.32  ? 197 ASP   B O      1 
ATOM   4905  C  CB     . ASP   B 2  197 ? -26.495 -58.812  35.906  1.00 41.01  ? 197 ASP   B CB     1 
ATOM   4906  C  CG     . ASP   B 2  197 ? -27.944 -59.093  35.540  1.00 41.75  ? 197 ASP   B CG     1 
ATOM   4907  O  OD1    . ASP   B 2  197 ? -28.836 -58.568  36.232  1.00 44.91  ? 197 ASP   B OD1    1 
ATOM   4908  O  OD2    . ASP   B 2  197 ? -28.181 -59.863  34.565  1.00 42.46  ? 197 ASP   B OD2    1 
ATOM   4909  N  N      . GLU   B 2  198 ? -23.784 -57.485  35.065  1.00 35.72  ? 198 GLU   B N      1 
ATOM   4910  C  CA     . GLU   B 2  198 ? -22.330 -57.360  35.152  1.00 38.43  ? 198 GLU   B CA     1 
ATOM   4911  C  C      . GLU   B 2  198 ? -21.815 -56.754  33.864  1.00 39.27  ? 198 GLU   B C      1 
ATOM   4912  O  O      . GLU   B 2  198 ? -22.109 -57.281  32.784  1.00 40.87  ? 198 GLU   B O      1 
ATOM   4913  C  CB     . GLU   B 2  198 ? -21.643 -58.726  35.305  1.00 40.07  ? 198 GLU   B CB     1 
ATOM   4914  C  CG     . GLU   B 2  198 ? -22.235 -59.616  36.338  1.00 37.60  ? 198 GLU   B CG     1 
ATOM   4915  C  CD     . GLU   B 2  198 ? -22.204 -61.052  35.888  1.00 45.17  ? 198 GLU   B CD     1 
ATOM   4916  O  OE1    . GLU   B 2  198 ? -21.726 -61.344  34.753  1.00 42.03  ? 198 GLU   B OE1    1 
ATOM   4917  O  OE2    . GLU   B 2  198 ? -22.709 -61.890  36.661  1.00 51.68  ? 198 GLU   B OE2    1 
ATOM   4918  N  N      . THR   B 2  199 ? -21.031 -55.678  33.964  1.00 35.02  ? 199 THR   B N      1 
ATOM   4919  C  CA     . THR   B 2  199 ? -20.204 -55.271  32.837  1.00 37.02  ? 199 THR   B CA     1 
ATOM   4920  C  C      . THR   B 2  199 ? -18.793 -55.060  33.349  1.00 37.09  ? 199 THR   B C      1 
ATOM   4921  O  O      . THR   B 2  199 ? -18.591 -54.577  34.467  1.00 36.80  ? 199 THR   B O      1 
ATOM   4922  C  CB     . THR   B 2  199 ? -20.721 -54.003  32.074  1.00 35.99  ? 199 THR   B CB     1 
ATOM   4923  O  OG1    . THR   B 2  199 ? -20.315 -52.806  32.738  1.00 41.57  ? 199 THR   B OG1    1 
ATOM   4924  C  CG2    . THR   B 2  199 ? -22.217 -54.001  31.928  1.00 36.99  ? 199 THR   B CG2    1 
ATOM   4925  N  N      . TYR   B 2  200 ? -17.841 -55.486  32.525  1.00 34.53  ? 200 TYR   B N      1 
ATOM   4926  C  CA     . TYR   B 2  200 ? -16.413 -55.386  32.770  1.00 36.94  ? 200 TYR   B CA     1 
ATOM   4927  C  C      . TYR   B 2  200 ? -15.900 -54.183  32.001  1.00 39.21  ? 200 TYR   B C      1 
ATOM   4928  O  O      . TYR   B 2  200 ? -15.935 -54.186  30.770  1.00 37.92  ? 200 TYR   B O      1 
ATOM   4929  C  CB     . TYR   B 2  200 ? -15.688 -56.632  32.261  1.00 38.00  ? 200 TYR   B CB     1 
ATOM   4930  C  CG     . TYR   B 2  200 ? -16.026 -57.960  32.909  1.00 41.41  ? 200 TYR   B CG     1 
ATOM   4931  C  CD1    . TYR   B 2  200 ? -15.494 -58.335  34.150  1.00 39.29  ? 200 TYR   B CD1    1 
ATOM   4932  C  CD2    . TYR   B 2  200 ? -16.903 -58.834  32.288  1.00 39.09  ? 200 TYR   B CD2    1 
ATOM   4933  C  CE1    . TYR   B 2  200 ? -15.801 -59.567  34.714  1.00 38.21  ? 200 TYR   B CE1    1 
ATOM   4934  C  CE2    . TYR   B 2  200 ? -17.231 -60.044  32.858  1.00 40.71  ? 200 TYR   B CE2    1 
ATOM   4935  C  CZ     . TYR   B 2  200 ? -16.681 -60.415  34.063  1.00 41.32  ? 200 TYR   B CZ     1 
ATOM   4936  O  OH     . TYR   B 2  200 ? -17.027 -61.654  34.581  1.00 45.38  ? 200 TYR   B OH     1 
ATOM   4937  N  N      . CYS   B 2  201 ? -15.398 -53.184  32.715  1.00 39.17  ? 201 CYS   B N      1 
ATOM   4938  C  CA     . CYS   B 2  201 ? -15.015 -51.904  32.126  1.00 36.10  ? 201 CYS   B CA     1 
ATOM   4939  C  C      . CYS   B 2  201 ? -13.608 -52.010  31.578  1.00 34.61  ? 201 CYS   B C      1 
ATOM   4940  O  O      . CYS   B 2  201 ? -12.639 -51.795  32.293  1.00 44.71  ? 201 CYS   B O      1 
ATOM   4941  C  CB     . CYS   B 2  201 ? -15.093 -50.805  33.167  1.00 35.71  ? 201 CYS   B CB     1 
ATOM   4942  S  SG     . CYS   B 2  201 ? -16.709 -50.721  33.888  1.00 50.41  ? 201 CYS   B SG     1 
ATOM   4943  N  N      . ILE   B 2  202 ? -13.487 -52.318  30.293  1.00 31.07  ? 202 ILE   B N      1 
ATOM   4944  C  CA     . ILE   B 2  202 ? -12.187 -52.384  29.641  1.00 33.33  ? 202 ILE   B CA     1 
ATOM   4945  C  C      . ILE   B 2  202 ? -11.881 -50.991  29.106  1.00 35.55  ? 202 ILE   B C      1 
ATOM   4946  O  O      . ILE   B 2  202 ? -12.338 -50.595  28.035  1.00 37.69  ? 202 ILE   B O      1 
ATOM   4947  C  CB     . ILE   B 2  202 ? -12.154 -53.439  28.539  1.00 33.00  ? 202 ILE   B CB     1 
ATOM   4948  C  CG1    . ILE   B 2  202 ? -12.307 -54.826  29.145  1.00 32.88  ? 202 ILE   B CG1    1 
ATOM   4949  C  CG2    . ILE   B 2  202 ? -10.875 -53.338  27.741  1.00 32.74  ? 202 ILE   B CG2    1 
ATOM   4950  C  CD1    . ILE   B 2  202 ? -13.432 -55.606  28.560  1.00 32.19  ? 202 ILE   B CD1    1 
ATOM   4951  N  N      . ASP   B 2  203 ? -11.094 -50.245  29.857  1.00 35.71  ? 203 ASP   B N      1 
ATOM   4952  C  CA     . ASP   B 2  203 ? -10.733 -48.899  29.455  1.00 35.90  ? 203 ASP   B CA     1 
ATOM   4953  C  C      . ASP   B 2  203 ? -9.644  -48.981  28.393  1.00 41.03  ? 203 ASP   B C      1 
ATOM   4954  O  O      . ASP   B 2  203 ? -8.629  -49.662  28.583  1.00 42.30  ? 203 ASP   B O      1 
ATOM   4955  C  CB     . ASP   B 2  203 ? -10.287 -48.102  30.675  1.00 40.45  ? 203 ASP   B CB     1 
ATOM   4956  C  CG     . ASP   B 2  203 ? -9.991  -46.648  30.357  1.00 49.54  ? 203 ASP   B CG     1 
ATOM   4957  O  OD1    . ASP   B 2  203 ? -9.860  -46.295  29.153  1.00 46.31  ? 203 ASP   B OD1    1 
ATOM   4958  O  OD2    . ASP   B 2  203 ? -9.954  -45.846  31.325  1.00 48.56  ? 203 ASP   B OD2    1 
ATOM   4959  N  N      . ASN   B 2  204 ? -9.882  -48.343  27.243  1.00 40.55  ? 204 ASN   B N      1 
ATOM   4960  C  CA     . ASN   B 2  204 ? -8.839  -48.257  26.232  1.00 37.33  ? 204 ASN   B CA     1 
ATOM   4961  C  C      . ASN   B 2  204 ? -7.705  -47.352  26.676  1.00 40.39  ? 204 ASN   B C      1 
ATOM   4962  O  O      . ASN   B 2  204 ? -6.602  -47.428  26.120  1.00 42.17  ? 204 ASN   B O      1 
ATOM   4963  C  CB     . ASN   B 2  204 ? -9.392  -47.755  24.900  1.00 34.61  ? 204 ASN   B CB     1 
ATOM   4964  C  CG     . ASN   B 2  204 ? -9.672  -48.867  23.940  1.00 34.03  ? 204 ASN   B CG     1 
ATOM   4965  O  OD1    . ASN   B 2  204 ? -9.376  -50.017  24.210  1.00 39.91  ? 204 ASN   B OD1    1 
ATOM   4966  N  ND2    . ASN   B 2  204 ? -10.145 -48.522  22.775  1.00 32.62  ? 204 ASN   B ND2    1 
ATOM   4967  N  N      . GLU   B 2  205 ? -7.953  -46.477  27.647  1.00 39.59  ? 205 GLU   B N      1 
ATOM   4968  C  CA     . GLU   B 2  205 ? -6.856  -45.685  28.181  1.00 45.17  ? 205 GLU   B CA     1 
ATOM   4969  C  C      . GLU   B 2  205 ? -5.882  -46.575  28.935  1.00 47.36  ? 205 GLU   B C      1 
ATOM   4970  O  O      . GLU   B 2  205 ? -4.666  -46.476  28.746  1.00 49.10  ? 205 GLU   B O      1 
ATOM   4971  C  CB     . GLU   B 2  205 ? -7.393  -44.579  29.077  1.00 43.77  ? 205 GLU   B CB     1 
ATOM   4972  C  CG     . GLU   B 2  205 ? -6.326  -43.867  29.871  1.00 51.67  ? 205 GLU   B CG     1 
ATOM   4973  C  CD     . GLU   B 2  205 ? -6.496  -42.365  29.821  1.00 53.77  ? 205 GLU   B CD     1 
ATOM   4974  O  OE1    . GLU   B 2  205 ? -7.295  -41.909  28.986  1.00 55.00  ? 205 GLU   B OE1    1 
ATOM   4975  O  OE2    . GLU   B 2  205 ? -5.872  -41.643  30.630  1.00 54.67  ? 205 GLU   B OE2    1 
ATOM   4976  N  N      . ALA   B 2  206 ? -6.403  -47.482  29.759  1.00 42.04  ? 206 ALA   B N      1 
ATOM   4977  C  CA     . ALA   B 2  206 ? -5.538  -48.407  30.476  1.00 47.11  ? 206 ALA   B CA     1 
ATOM   4978  C  C      . ALA   B 2  206 ? -4.797  -49.334  29.514  1.00 45.35  ? 206 ALA   B C      1 
ATOM   4979  O  O      . ALA   B 2  206 ? -3.578  -49.514  29.622  1.00 45.05  ? 206 ALA   B O      1 
ATOM   4980  C  CB     . ALA   B 2  206 ? -6.357  -49.202  31.493  1.00 45.44  ? 206 ALA   B CB     1 
ATOM   4981  N  N      . LEU   B 2  207 ? -5.508  -49.933  28.564  1.00 41.36  ? 207 LEU   B N      1 
ATOM   4982  C  CA     . LEU   B 2  207 ? -4.815  -50.809  27.631  1.00 42.32  ? 207 LEU   B CA     1 
ATOM   4983  C  C      . LEU   B 2  207 ? -3.677  -50.076  26.948  1.00 45.00  ? 207 LEU   B C      1 
ATOM   4984  O  O      . LEU   B 2  207 ? -2.679  -50.700  26.572  1.00 45.93  ? 207 LEU   B O      1 
ATOM   4985  C  CB     . LEU   B 2  207 ? -5.773  -51.357  26.583  1.00 39.88  ? 207 LEU   B CB     1 
ATOM   4986  C  CG     . LEU   B 2  207 ? -7.019  -51.999  27.160  1.00 37.40  ? 207 LEU   B CG     1 
ATOM   4987  C  CD1    . LEU   B 2  207 ? -7.839  -52.525  26.022  1.00 40.49  ? 207 LEU   B CD1    1 
ATOM   4988  C  CD2    . LEU   B 2  207 ? -6.688  -53.077  28.148  1.00 39.84  ? 207 LEU   B CD2    1 
ATOM   4989  N  N      . TYR   B 2  208 ? -3.815  -48.755  26.765  1.00 48.06  ? 208 TYR   B N      1 
ATOM   4990  C  CA     . TYR   B 2  208 ? -2.786  -47.996  26.055  1.00 49.17  ? 208 TYR   B CA     1 
ATOM   4991  C  C      . TYR   B 2  208 ? -1.571  -47.791  26.940  1.00 48.45  ? 208 TYR   B C      1 
ATOM   4992  O  O      . TYR   B 2  208 ? -0.437  -48.080  26.542  1.00 50.36  ? 208 TYR   B O      1 
ATOM   4993  C  CB     . TYR   B 2  208 ? -3.333  -46.644  25.572  1.00 48.79  ? 208 TYR   B CB     1 
ATOM   4994  C  CG     . TYR   B 2  208 ? -2.313  -45.897  24.731  1.00 46.40  ? 208 TYR   B CG     1 
ATOM   4995  C  CD1    . TYR   B 2  208 ? -2.154  -46.185  23.384  1.00 43.16  ? 208 TYR   B CD1    1 
ATOM   4996  C  CD2    . TYR   B 2  208 ? -1.470  -44.943  25.300  1.00 47.24  ? 208 TYR   B CD2    1 
ATOM   4997  C  CE1    . TYR   B 2  208 ? -1.200  -45.534  22.616  1.00 52.53  ? 208 TYR   B CE1    1 
ATOM   4998  C  CE2    . TYR   B 2  208 ? -0.506  -44.279  24.539  1.00 46.88  ? 208 TYR   B CE2    1 
ATOM   4999  C  CZ     . TYR   B 2  208 ? -0.375  -44.577  23.195  1.00 51.76  ? 208 TYR   B CZ     1 
ATOM   5000  O  OH     . TYR   B 2  208 ? 0.578   -43.941  22.418  1.00 48.69  ? 208 TYR   B OH     1 
ATOM   5001  N  N      . ASP   B 2  209 ? -1.802  -47.306  28.154  1.00 43.59  ? 209 ASP   B N      1 
ATOM   5002  C  CA     . ASP   B 2  209 ? -0.745  -47.161  29.139  1.00 45.33  ? 209 ASP   B CA     1 
ATOM   5003  C  C      . ASP   B 2  209 ? -0.006  -48.476  29.375  1.00 48.77  ? 209 ASP   B C      1 
ATOM   5004  O  O      . ASP   B 2  209 ? 1.225   -48.517  29.395  1.00 50.38  ? 209 ASP   B O      1 
ATOM   5005  C  CB     . ASP   B 2  209 ? -1.386  -46.639  30.407  1.00 49.98  ? 209 ASP   B CB     1 
ATOM   5006  C  CG     . ASP   B 2  209 ? -1.806  -45.211  30.250  1.00 56.81  ? 209 ASP   B CG     1 
ATOM   5007  O  OD1    . ASP   B 2  209 ? -1.382  -44.631  29.224  1.00 52.45  ? 209 ASP   B OD1    1 
ATOM   5008  O  OD2    . ASP   B 2  209 ? -2.620  -44.705  31.068  1.00 61.83  ? 209 ASP   B OD2    1 
ATOM   5009  N  N      . ILE   B 2  210 ? -0.743  -49.569  29.551  1.00 49.30  ? 210 ILE   B N      1 
ATOM   5010  C  CA     . ILE   B 2  210 ? -0.088  -50.856  29.764  1.00 48.86  ? 210 ILE   B CA     1 
ATOM   5011  C  C      . ILE   B 2  210 ? 0.725   -51.241  28.538  1.00 51.72  ? 210 ILE   B C      1 
ATOM   5012  O  O      . ILE   B 2  210 ? 1.795   -51.843  28.654  1.00 61.52  ? 210 ILE   B O      1 
ATOM   5013  C  CB     . ILE   B 2  210 ? -1.125  -51.937  30.122  1.00 45.92  ? 210 ILE   B CB     1 
ATOM   5014  C  CG1    . ILE   B 2  210 ? -1.773  -51.617  31.457  1.00 43.29  ? 210 ILE   B CG1    1 
ATOM   5015  C  CG2    . ILE   B 2  210 ? -0.511  -53.305  30.149  1.00 40.85  ? 210 ILE   B CG2    1 
ATOM   5016  C  CD1    . ILE   B 2  210 ? -2.774  -52.632  31.849  1.00 49.23  ? 210 ILE   B CD1    1 
ATOM   5017  N  N      . CYS   B 2  211 ? 0.240   -50.915  27.343  1.00 46.53  ? 211 CYS   B N      1 
ATOM   5018  C  CA     . CYS   B 2  211 ? 1.033   -51.232  26.162  1.00 49.42  ? 211 CYS   B CA     1 
ATOM   5019  C  C      . CYS   B 2  211 ? 2.214   -50.295  26.019  1.00 55.93  ? 211 CYS   B C      1 
ATOM   5020  O  O      . CYS   B 2  211 ? 3.280   -50.703  25.557  1.00 58.76  ? 211 CYS   B O      1 
ATOM   5021  C  CB     . CYS   B 2  211 ? 0.174   -51.185  24.912  1.00 40.62  ? 211 CYS   B CB     1 
ATOM   5022  S  SG     . CYS   B 2  211 ? -0.748  -52.657  24.648  1.00 49.93  ? 211 CYS   B SG     1 
ATOM   5023  N  N      . PHE   B 2  212 ? 2.037   -49.033  26.390  1.00 54.27  ? 212 PHE   B N      1 
ATOM   5024  C  CA     . PHE   B 2  212 ? 3.112   -48.055  26.261  1.00 54.80  ? 212 PHE   B CA     1 
ATOM   5025  C  C      . PHE   B 2  212 ? 4.138   -48.281  27.362  1.00 56.45  ? 212 PHE   B C      1 
ATOM   5026  O  O      . PHE   B 2  212 ? 5.242   -48.768  27.109  1.00 62.47  ? 212 PHE   B O      1 
ATOM   5027  C  CB     . PHE   B 2  212 ? 2.537   -46.636  26.331  1.00 54.94  ? 212 PHE   B CB     1 
ATOM   5028  C  CG     . PHE   B 2  212 ? 3.561   -45.547  26.145  1.00 65.89  ? 212 PHE   B CG     1 
ATOM   5029  C  CD1    . PHE   B 2  212 ? 4.476   -45.607  25.091  1.00 71.04  ? 212 PHE   B CD1    1 
ATOM   5030  C  CD2    . PHE   B 2  212 ? 3.636   -44.480  27.035  1.00 65.83  ? 212 PHE   B CD2    1 
ATOM   5031  C  CE1    . PHE   B 2  212 ? 5.427   -44.603  24.906  1.00 64.03  ? 212 PHE   B CE1    1 
ATOM   5032  C  CE2    . PHE   B 2  212 ? 4.593   -43.469  26.854  1.00 70.36  ? 212 PHE   B CE2    1 
ATOM   5033  C  CZ     . PHE   B 2  212 ? 5.485   -43.533  25.789  1.00 66.54  ? 212 PHE   B CZ     1 
ATOM   5034  N  N      . ARG   B 2  213 ? 3.763   -47.955  28.596  1.00 56.09  ? 213 ARG   B N      1 
ATOM   5035  C  CA     . ARG   B 2  213 ? 4.639   -48.038  29.757  1.00 57.91  ? 213 ARG   B CA     1 
ATOM   5036  C  C      . ARG   B 2  213 ? 5.122   -49.459  30.025  1.00 57.37  ? 213 ARG   B C      1 
ATOM   5037  O  O      . ARG   B 2  213 ? 6.271   -49.814  29.758  1.00 62.51  ? 213 ARG   B O      1 
ATOM   5038  C  CB     . ARG   B 2  213 ? 3.895   -47.519  30.973  1.00 48.85  ? 213 ARG   B CB     1 
ATOM   5039  C  CG     . ARG   B 2  213 ? 3.656   -46.027  30.923  1.00 58.39  ? 213 ARG   B CG     1 
ATOM   5040  C  CD     . ARG   B 2  213 ? 2.623   -45.642  31.951  1.00 59.15  ? 213 ARG   B CD     1 
ATOM   5041  N  NE     . ARG   B 2  213 ? 1.975   -44.367  31.680  1.00 54.60  ? 213 ARG   B NE     1 
ATOM   5042  C  CZ     . ARG   B 2  213 ? 0.926   -43.928  32.361  1.00 59.36  ? 213 ARG   B CZ     1 
ATOM   5043  N  NH1    . ARG   B 2  213 ? 0.405   -44.633  33.352  1.00 71.39  ? 213 ARG   B NH1    1 
ATOM   5044  N  NH2    . ARG   B 2  213 ? 0.371   -42.766  32.029  1.00 61.98  ? 213 ARG   B NH2    1 
ATOM   5045  N  N      . THR   B 2  214 ? 4.239   -50.298  30.525  1.00 57.38  ? 214 THR   B N      1 
ATOM   5046  C  CA     . THR   B 2  214 ? 4.698   -51.562  31.079  1.00 64.81  ? 214 THR   B CA     1 
ATOM   5047  C  C      . THR   B 2  214 ? 5.308   -52.481  30.010  1.00 63.26  ? 214 THR   B C      1 
ATOM   5048  O  O      . THR   B 2  214 ? 6.364   -53.074  30.239  1.00 71.11  ? 214 THR   B O      1 
ATOM   5049  C  CB     . THR   B 2  214 ? 3.548   -52.225  31.836  1.00 62.41  ? 214 THR   B CB     1 
ATOM   5050  O  OG1    . THR   B 2  214 ? 3.028   -51.289  32.801  1.00 59.67  ? 214 THR   B OG1    1 
ATOM   5051  C  CG2    . THR   B 2  214 ? 4.041   -53.467  32.568  1.00 54.40  ? 214 THR   B CG2    1 
ATOM   5052  N  N      . LEU   B 2  215 ? 4.695   -52.619  28.841  1.00 57.27  ? 215 LEU   B N      1 
ATOM   5053  C  CA     . LEU   B 2  215 ? 5.243   -53.564  27.871  1.00 60.22  ? 215 LEU   B CA     1 
ATOM   5054  C  C      . LEU   B 2  215 ? 6.197   -52.917  26.895  1.00 64.99  ? 215 LEU   B C      1 
ATOM   5055  O  O      . LEU   B 2  215 ? 6.581   -53.553  25.905  1.00 57.00  ? 215 LEU   B O      1 
ATOM   5056  C  CB     . LEU   B 2  215 ? 4.139   -54.257  27.086  1.00 64.35  ? 215 LEU   B CB     1 
ATOM   5057  C  CG     . LEU   B 2  215 ? 3.162   -54.878  28.052  1.00 65.78  ? 215 LEU   B CG     1 
ATOM   5058  C  CD1    . LEU   B 2  215 ? 2.103   -55.685  27.299  1.00 62.64  ? 215 LEU   B CD1    1 
ATOM   5059  C  CD2    . LEU   B 2  215 ? 3.952   -55.692  29.063  1.00 69.72  ? 215 LEU   B CD2    1 
ATOM   5060  N  N      . LYS   B 2  216 ? 6.561   -51.665  27.144  1.00 67.48  ? 216 LYS   B N      1 
ATOM   5061  C  CA     . LYS   B 2  216 ? 7.467   -50.902  26.295  1.00 65.03  ? 216 LYS   B CA     1 
ATOM   5062  C  C      . LYS   B 2  216 ? 7.129   -51.125  24.823  1.00 64.41  ? 216 LYS   B C      1 
ATOM   5063  O  O      . LYS   B 2  216 ? 7.904   -51.684  24.047  1.00 67.92  ? 216 LYS   B O      1 
ATOM   5064  C  CB     . LYS   B 2  216 ? 8.922   -51.263  26.601  1.00 66.18  ? 216 LYS   B CB     1 
ATOM   5065  C  CG     . LYS   B 2  216 ? 9.278   -51.138  28.088  1.00 60.38  ? 216 LYS   B CG     1 
ATOM   5066  C  CD     . LYS   B 2  216 ? 8.997   -49.746  28.616  1.00 58.40  ? 216 LYS   B CD     1 
ATOM   5067  C  CE     . LYS   B 2  216 ? 9.305   -49.643  30.095  1.00 66.56  ? 216 LYS   B CE     1 
ATOM   5068  N  NZ     . LYS   B 2  216 ? 8.935   -48.293  30.648  1.00 72.81  ? 216 LYS   B NZ     1 
ATOM   5069  N  N      . LEU   B 2  217 ? 5.919   -50.720  24.454  1.00 68.05  ? 217 LEU   B N      1 
ATOM   5070  C  CA     . LEU   B 2  217 ? 5.528   -50.659  23.051  1.00 70.38  ? 217 LEU   B CA     1 
ATOM   5071  C  C      . LEU   B 2  217 ? 5.381   -49.194  22.662  1.00 68.51  ? 217 LEU   B C      1 
ATOM   5072  O  O      . LEU   B 2  217 ? 4.577   -48.450  23.238  1.00 61.69  ? 217 LEU   B O      1 
ATOM   5073  C  CB     . LEU   B 2  217 ? 4.258   -51.455  22.744  1.00 60.24  ? 217 LEU   B CB     1 
ATOM   5074  C  CG     . LEU   B 2  217 ? 4.328   -52.957  23.039  1.00 58.80  ? 217 LEU   B CG     1 
ATOM   5075  C  CD1    . LEU   B 2  217 ? 3.030   -53.636  22.676  1.00 57.29  ? 217 LEU   B CD1    1 
ATOM   5076  C  CD2    . LEU   B 2  217 ? 5.485   -53.606  22.322  1.00 59.42  ? 217 LEU   B CD2    1 
ATOM   5077  N  N      . THR   B 2  218 ? 6.196   -48.791  21.701  1.00 74.13  ? 218 THR   B N      1 
ATOM   5078  C  CA     . THR   B 2  218 ? 6.246   -47.401  21.284  1.00 80.23  ? 218 THR   B CA     1 
ATOM   5079  C  C      . THR   B 2  218 ? 4.918   -46.936  20.686  1.00 71.48  ? 218 THR   B C      1 
ATOM   5080  O  O      . THR   B 2  218 ? 4.365   -45.904  21.091  1.00 65.71  ? 218 THR   B O      1 
ATOM   5081  C  CB     . THR   B 2  218 ? 7.399   -47.241  20.293  1.00 89.07  ? 218 THR   B CB     1 
ATOM   5082  O  OG1    . THR   B 2  218 ? 7.446   -45.887  19.827  1.00 93.31  ? 218 THR   B OG1    1 
ATOM   5083  C  CG2    . THR   B 2  218 ? 7.263   -48.235  19.107  1.00 77.77  ? 218 THR   B CG2    1 
ATOM   5084  N  N      . THR   B 2  219 ? 4.409   -47.658  19.694  1.00 66.84  ? 219 THR   B N      1 
ATOM   5085  C  CA     . THR   B 2  219 ? 3.205   -47.236  18.986  1.00 64.73  ? 219 THR   B CA     1 
ATOM   5086  C  C      . THR   B 2  219 ? 2.222   -48.392  18.927  1.00 60.46  ? 219 THR   B C      1 
ATOM   5087  O  O      . THR   B 2  219 ? 2.212   -49.178  17.963  1.00 55.08  ? 219 THR   B O      1 
ATOM   5088  C  CB     . THR   B 2  219 ? 3.529   -46.708  17.597  1.00 66.08  ? 219 THR   B CB     1 
ATOM   5089  O  OG1    . THR   B 2  219 ? 4.166   -45.426  17.734  1.00 67.49  ? 219 THR   B OG1    1 
ATOM   5090  C  CG2    . THR   B 2  219 ? 2.233   -46.542  16.794  1.00 64.11  ? 219 THR   B CG2    1 
ATOM   5091  N  N      . PRO   B 2  220 ? 1.359   -48.506  19.941  1.00 63.71  ? 220 PRO   B N      1 
ATOM   5092  C  CA     . PRO   B 2  220 ? 0.513   -49.694  20.086  1.00 49.93  ? 220 PRO   B CA     1 
ATOM   5093  C  C      . PRO   B 2  220 ? -0.655  -49.655  19.126  1.00 52.59  ? 220 PRO   B C      1 
ATOM   5094  O  O      . PRO   B 2  220 ? -1.265  -48.610  18.897  1.00 54.29  ? 220 PRO   B O      1 
ATOM   5095  C  CB     . PRO   B 2  220 ? 0.029   -49.604  21.536  1.00 45.42  ? 220 PRO   B CB     1 
ATOM   5096  C  CG     . PRO   B 2  220 ? 0.774   -48.379  22.141  1.00 48.81  ? 220 PRO   B CG     1 
ATOM   5097  C  CD     . PRO   B 2  220 ? 1.080   -47.510  20.989  1.00 57.89  ? 220 PRO   B CD     1 
ATOM   5098  N  N      . THR   B 2  221 ? -0.954  -50.811  18.563  1.00 49.40  ? 221 THR   B N      1 
ATOM   5099  C  CA     . THR   B 2  221 ? -2.069  -51.010  17.660  1.00 43.93  ? 221 THR   B CA     1 
ATOM   5100  C  C      . THR   B 2  221 ? -3.273  -51.554  18.425  1.00 46.90  ? 221 THR   B C      1 
ATOM   5101  O  O      . THR   B 2  221 ? -3.184  -51.933  19.590  1.00 53.42  ? 221 THR   B O      1 
ATOM   5102  C  CB     . THR   B 2  221 ? -1.643  -51.981  16.575  1.00 47.80  ? 221 THR   B CB     1 
ATOM   5103  O  OG1    . THR   B 2  221 ? -1.625  -53.305  17.125  1.00 47.41  ? 221 THR   B OG1    1 
ATOM   5104  C  CG2    . THR   B 2  221 ? -0.248  -51.635  16.160  1.00 51.99  ? 221 THR   B CG2    1 
ATOM   5105  N  N      . TYR   B 2  222 ? -4.422  -51.604  17.761  1.00 45.43  ? 222 TYR   B N      1 
ATOM   5106  C  CA     . TYR   B 2  222 ? -5.554  -52.259  18.402  1.00 42.29  ? 222 TYR   B CA     1 
ATOM   5107  C  C      . TYR   B 2  222 ? -5.211  -53.719  18.672  1.00 50.36  ? 222 TYR   B C      1 
ATOM   5108  O  O      . TYR   B 2  222 ? -5.676  -54.297  19.663  1.00 52.66  ? 222 TYR   B O      1 
ATOM   5109  C  CB     . TYR   B 2  222 ? -6.819  -52.140  17.532  1.00 35.85  ? 222 TYR   B CB     1 
ATOM   5110  C  CG     . TYR   B 2  222 ? -7.452  -50.760  17.567  1.00 30.59  ? 222 TYR   B CG     1 
ATOM   5111  C  CD1    . TYR   B 2  222 ? -7.591  -50.049  18.755  1.00 31.70  ? 222 TYR   B CD1    1 
ATOM   5112  C  CD2    . TYR   B 2  222 ? -7.870  -50.155  16.408  1.00 26.85  ? 222 TYR   B CD2    1 
ATOM   5113  C  CE1    . TYR   B 2  222 ? -8.123  -48.789  18.777  1.00 26.58  ? 222 TYR   B CE1    1 
ATOM   5114  C  CE2    . TYR   B 2  222 ? -8.422  -48.886  16.422  1.00 25.32  ? 222 TYR   B CE2    1 
ATOM   5115  C  CZ     . TYR   B 2  222 ? -8.542  -48.209  17.604  1.00 27.09  ? 222 TYR   B CZ     1 
ATOM   5116  O  OH     . TYR   B 2  222 ? -9.080  -46.935  17.610  1.00 33.31  ? 222 TYR   B OH     1 
ATOM   5117  N  N      . GLY   B 2  223 ? -4.360  -54.315  17.824  1.00 46.87  ? 223 GLY   B N      1 
ATOM   5118  C  CA     . GLY   B 2  223 ? -3.963  -55.701  18.029  1.00 53.14  ? 223 GLY   B CA     1 
ATOM   5119  C  C      . GLY   B 2  223 ? -3.218  -55.914  19.333  1.00 58.27  ? 223 GLY   B C      1 
ATOM   5120  O  O      . GLY   B 2  223 ? -3.385  -56.938  19.998  1.00 60.21  ? 223 GLY   B O      1 
ATOM   5121  N  N      . ASP   B 2  224 ? -2.390  -54.947  19.719  1.00 56.65  ? 224 ASP   B N      1 
ATOM   5122  C  CA     . ASP   B 2  224 ? -1.685  -55.044  20.990  1.00 58.11  ? 224 ASP   B CA     1 
ATOM   5123  C  C      . ASP   B 2  224 ? -2.640  -54.838  22.148  1.00 49.60  ? 224 ASP   B C      1 
ATOM   5124  O  O      . ASP   B 2  224 ? -2.499  -55.480  23.197  1.00 51.05  ? 224 ASP   B O      1 
ATOM   5125  C  CB     . ASP   B 2  224 ? -0.556  -54.012  21.030  1.00 58.26  ? 224 ASP   B CB     1 
ATOM   5126  C  CG     . ASP   B 2  224 ? 0.556   -54.341  20.053  1.00 56.30  ? 224 ASP   B CG     1 
ATOM   5127  O  OD1    . ASP   B 2  224 ? 0.925   -55.528  19.962  1.00 58.00  ? 224 ASP   B OD1    1 
ATOM   5128  O  OD2    . ASP   B 2  224 ? 1.019   -53.420  19.345  1.00 55.09  ? 224 ASP   B OD2    1 
ATOM   5129  N  N      . LEU   B 2  225 ? -3.609  -53.939  21.975  1.00 49.78  ? 225 LEU   B N      1 
ATOM   5130  C  CA     . LEU   B 2  225 ? -4.639  -53.744  22.993  1.00 55.56  ? 225 LEU   B CA     1 
ATOM   5131  C  C      . LEU   B 2  225 ? -5.568  -54.953  23.105  1.00 55.32  ? 225 LEU   B C      1 
ATOM   5132  O  O      . LEU   B 2  225 ? -5.975  -55.326  24.214  1.00 48.04  ? 225 LEU   B O      1 
ATOM   5133  C  CB     . LEU   B 2  225 ? -5.464  -52.486  22.696  1.00 48.86  ? 225 LEU   B CB     1 
ATOM   5134  C  CG     . LEU   B 2  225 ? -4.854  -51.135  22.391  1.00 44.97  ? 225 LEU   B CG     1 
ATOM   5135  C  CD1    . LEU   B 2  225 ? -5.930  -50.077  22.499  1.00 42.21  ? 225 LEU   B CD1    1 
ATOM   5136  C  CD2    . LEU   B 2  225 ? -3.787  -50.862  23.401  1.00 46.52  ? 225 LEU   B CD2    1 
ATOM   5137  N  N      . ASN   B 2  226 ? -5.937  -55.559  21.968  1.00 47.75  ? 226 ASN   B N      1 
ATOM   5138  C  CA     . ASN   B 2  226 ? -6.902  -56.644  22.013  1.00 44.16  ? 226 ASN   B CA     1 
ATOM   5139  C  C      . ASN   B 2  226 ? -6.274  -57.913  22.563  1.00 47.27  ? 226 ASN   B C      1 
ATOM   5140  O  O      . ASN   B 2  226 ? -6.962  -58.726  23.186  1.00 46.91  ? 226 ASN   B O      1 
ATOM   5141  C  CB     . ASN   B 2  226 ? -7.482  -56.869  20.627  1.00 47.55  ? 226 ASN   B CB     1 
ATOM   5142  C  CG     . ASN   B 2  226 ? -8.295  -55.689  20.144  1.00 48.20  ? 226 ASN   B CG     1 
ATOM   5143  O  OD1    . ASN   B 2  226 ? -8.581  -54.767  20.905  1.00 48.96  ? 226 ASN   B OD1    1 
ATOM   5144  N  ND2    . ASN   B 2  226 ? -8.652  -55.699  18.864  1.00 52.77  ? 226 ASN   B ND2    1 
ATOM   5145  N  N      . HIS   B 2  227 ? -4.966  -58.087  22.365  1.00 53.06  ? 227 HIS   B N      1 
ATOM   5146  C  CA     . HIS   B 2  227 ? -4.227  -59.136  23.066  1.00 52.52  ? 227 HIS   B CA     1 
ATOM   5147  C  C      . HIS   B 2  227 ? -4.450  -59.053  24.576  1.00 49.42  ? 227 HIS   B C      1 
ATOM   5148  O  O      . HIS   B 2  227 ? -4.786  -60.049  25.220  1.00 49.87  ? 227 HIS   B O      1 
ATOM   5149  C  CB     . HIS   B 2  227 ? -2.739  -59.024  22.727  1.00 58.63  ? 227 HIS   B CB     1 
ATOM   5150  C  CG     . HIS   B 2  227 ? -1.853  -59.926  23.536  1.00 67.49  ? 227 HIS   B CG     1 
ATOM   5151  N  ND1    . HIS   B 2  227 ? -1.796  -61.291  23.340  1.00 68.17  ? 227 HIS   B ND1    1 
ATOM   5152  C  CD2    . HIS   B 2  227 ? -0.979  -59.653  24.536  1.00 64.28  ? 227 HIS   B CD2    1 
ATOM   5153  C  CE1    . HIS   B 2  227 ? -0.933  -61.820  24.190  1.00 68.14  ? 227 HIS   B CE1    1 
ATOM   5154  N  NE2    . HIS   B 2  227 ? -0.424  -60.848  24.927  1.00 67.80  ? 227 HIS   B NE2    1 
ATOM   5155  N  N      . LEU   B 2  228 ? -4.265  -57.868  25.162  1.00 45.87  ? 228 LEU   B N      1 
ATOM   5156  C  CA     . LEU   B 2  228 ? -4.600  -57.708  26.568  1.00 42.99  ? 228 LEU   B CA     1 
ATOM   5157  C  C      . LEU   B 2  228 ? -6.056  -58.056  26.834  1.00 43.98  ? 228 LEU   B C      1 
ATOM   5158  O  O      . LEU   B 2  228 ? -6.389  -58.578  27.902  1.00 41.76  ? 228 LEU   B O      1 
ATOM   5159  C  CB     . LEU   B 2  228 ? -4.321  -56.282  27.050  1.00 44.60  ? 228 LEU   B CB     1 
ATOM   5160  C  CG     . LEU   B 2  228 ? -2.929  -55.680  27.212  1.00 45.92  ? 228 LEU   B CG     1 
ATOM   5161  C  CD1    . LEU   B 2  228 ? -3.084  -54.343  27.920  1.00 40.67  ? 228 LEU   B CD1    1 
ATOM   5162  C  CD2    . LEU   B 2  228 ? -1.990  -56.593  27.989  1.00 38.01  ? 228 LEU   B CD2    1 
ATOM   5163  N  N      . VAL   B 2  229 ? -6.952  -57.736  25.897  1.00 46.67  ? 229 VAL   B N      1 
ATOM   5164  C  CA     . VAL   B 2  229 ? -8.372  -57.908  26.186  1.00 42.53  ? 229 VAL   B CA     1 
ATOM   5165  C  C      . VAL   B 2  229 ? -8.739  -59.376  26.180  1.00 44.75  ? 229 VAL   B C      1 
ATOM   5166  O  O      . VAL   B 2  229 ? -9.449  -59.854  27.079  1.00 45.04  ? 229 VAL   B O      1 
ATOM   5167  C  CB     . VAL   B 2  229 ? -9.238  -57.088  25.219  1.00 40.56  ? 229 VAL   B CB     1 
ATOM   5168  C  CG1    . VAL   B 2  229 ? -10.693 -57.349  25.492  1.00 38.55  ? 229 VAL   B CG1    1 
ATOM   5169  C  CG2    . VAL   B 2  229 ? -8.975  -55.606  25.436  1.00 42.85  ? 229 VAL   B CG2    1 
ATOM   5170  N  N      . SER   B 2  230 ? -8.235  -60.121  25.194  1.00 41.24  ? 230 SER   B N      1 
ATOM   5171  C  CA     . SER   B 2  230 ? -8.532  -61.543  25.125  1.00 43.04  ? 230 SER   B CA     1 
ATOM   5172  C  C      . SER   B 2  230 ? -7.881  -62.319  26.267  1.00 41.91  ? 230 SER   B C      1 
ATOM   5173  O  O      . SER   B 2  230 ? -8.400  -63.364  26.670  1.00 41.72  ? 230 SER   B O      1 
ATOM   5174  C  CB     . SER   B 2  230 ? -8.124  -62.068  23.754  1.00 46.96  ? 230 SER   B CB     1 
ATOM   5175  O  OG     . SER   B 2  230 ? -6.738  -62.273  23.696  1.00 54.44  ? 230 SER   B OG     1 
ATOM   5176  N  N      . ALA   B 2  231 ? -6.788  -61.794  26.832  1.00 46.71  ? 231 ALA   B N      1 
ATOM   5177  C  CA     . ALA   B 2  231 ? -6.188  -62.349  28.049  1.00 43.94  ? 231 ALA   B CA     1 
ATOM   5178  C  C      . ALA   B 2  231 ? -7.101  -62.178  29.254  1.00 45.39  ? 231 ALA   B C      1 
ATOM   5179  O  O      . ALA   B 2  231 ? -7.323  -63.129  30.011  1.00 46.22  ? 231 ALA   B O      1 
ATOM   5180  C  CB     . ALA   B 2  231 ? -4.846  -61.676  28.332  1.00 38.96  ? 231 ALA   B CB     1 
ATOM   5181  N  N      . THR   B 2  232 ? -7.598  -60.953  29.476  1.00 43.22  ? 232 THR   B N      1 
ATOM   5182  C  CA     . THR   B 2  232 ? -8.552  -60.728  30.552  1.00 38.62  ? 232 THR   B CA     1 
ATOM   5183  C  C      . THR   B 2  232 ? -9.835  -61.502  30.288  1.00 46.30  ? 232 THR   B C      1 
ATOM   5184  O  O      . THR   B 2  232 ? -10.373 -62.162  31.192  1.00 44.07  ? 232 THR   B O      1 
ATOM   5185  C  CB     . THR   B 2  232 ? -8.858  -59.233  30.709  1.00 40.08  ? 232 THR   B CB     1 
ATOM   5186  O  OG1    . THR   B 2  232 ? -7.643  -58.503  30.867  1.00 44.29  ? 232 THR   B OG1    1 
ATOM   5187  C  CG2    . THR   B 2  232 ? -9.722  -58.957  31.971  1.00 37.26  ? 232 THR   B CG2    1 
ATOM   5188  N  N      . MET   B 2  233 ? -10.334 -61.457  29.050  1.00 44.09  ? 233 MET   B N      1 
ATOM   5189  C  CA     . MET   B 2  233 ? -11.586 -62.156  28.774  1.00 47.52  ? 233 MET   B CA     1 
ATOM   5190  C  C      . MET   B 2  233 ? -11.471 -63.644  29.046  1.00 44.62  ? 233 MET   B C      1 
ATOM   5191  O  O      . MET   B 2  233 ? -12.422 -64.264  29.523  1.00 42.21  ? 233 MET   B O      1 
ATOM   5192  C  CB     . MET   B 2  233 ? -12.041 -61.907  27.347  1.00 46.45  ? 233 MET   B CB     1 
ATOM   5193  C  CG     . MET   B 2  233 ? -12.642 -60.554  27.206  1.00 44.06  ? 233 MET   B CG     1 
ATOM   5194  S  SD     . MET   B 2  233 ? -13.352 -60.346  25.600  1.00 47.00  ? 233 MET   B SD     1 
ATOM   5195  C  CE     . MET   B 2  233 ? -14.625 -61.593  25.602  1.00 45.03  ? 233 MET   B CE     1 
ATOM   5196  N  N      . SER   B 2  234 ? -10.319 -64.238  28.756  1.00 46.34  ? 234 SER   B N      1 
ATOM   5197  C  CA     . SER   B 2  234 ? -10.131 -65.638  29.110  1.00 48.06  ? 234 SER   B CA     1 
ATOM   5198  C  C      . SER   B 2  234 ? -10.139 -65.820  30.620  1.00 47.46  ? 234 SER   B C      1 
ATOM   5199  O  O      . SER   B 2  234 ? -10.793 -66.727  31.146  1.00 48.27  ? 234 SER   B O      1 
ATOM   5200  C  CB     . SER   B 2  234 ? -8.830  -66.160  28.524  1.00 44.33  ? 234 SER   B CB     1 
ATOM   5201  O  OG     . SER   B 2  234 ? -8.615  -67.476  28.962  1.00 49.64  ? 234 SER   B OG     1 
ATOM   5202  N  N      . GLY   B 2  235 ? -9.421  -64.964  31.333  1.00 45.60  ? 235 GLY   B N      1 
ATOM   5203  C  CA     . GLY   B 2  235 ? -9.300  -65.082  32.772  1.00 43.45  ? 235 GLY   B CA     1 
ATOM   5204  C  C      . GLY   B 2  235 ? -10.616 -65.044  33.514  1.00 46.38  ? 235 GLY   B C      1 
ATOM   5205  O  O      . GLY   B 2  235 ? -10.907 -65.945  34.302  1.00 43.90  ? 235 GLY   B O      1 
ATOM   5206  N  N      . VAL   B 2  236 ? -11.421 -64.004  33.272  1.00 51.15  ? 236 VAL   B N      1 
ATOM   5207  C  CA     . VAL   B 2  236 ? -12.680 -63.839  33.997  1.00 46.24  ? 236 VAL   B CA     1 
ATOM   5208  C  C      . VAL   B 2  236 ? -13.689 -64.907  33.584  1.00 47.97  ? 236 VAL   B C      1 
ATOM   5209  O  O      . VAL   B 2  236 ? -14.619 -65.222  34.342  1.00 55.96  ? 236 VAL   B O      1 
ATOM   5210  C  CB     . VAL   B 2  236 ? -13.250 -62.414  33.789  1.00 43.62  ? 236 VAL   B CB     1 
ATOM   5211  C  CG1    . VAL   B 2  236 ? -12.263 -61.368  34.257  1.00 42.24  ? 236 VAL   B CG1    1 
ATOM   5212  C  CG2    . VAL   B 2  236 ? -13.617 -62.169  32.333  1.00 47.37  ? 236 VAL   B CG2    1 
ATOM   5213  N  N      . THR   B 2  237 ? -13.525 -65.480  32.400  1.00 42.54  ? 237 THR   B N      1 
ATOM   5214  C  CA     . THR   B 2  237 ? -14.364 -66.586  31.982  1.00 47.38  ? 237 THR   B CA     1 
ATOM   5215  C  C      . THR   B 2  237 ? -13.994 -67.897  32.669  1.00 51.51  ? 237 THR   B C      1 
ATOM   5216  O  O      . THR   B 2  237 ? -14.811 -68.818  32.664  1.00 51.37  ? 237 THR   B O      1 
ATOM   5217  C  CB     . THR   B 2  237 ? -14.245 -66.812  30.477  1.00 48.48  ? 237 THR   B CB     1 
ATOM   5218  O  OG1    . THR   B 2  237 ? -14.311 -65.568  29.798  1.00 54.49  ? 237 THR   B OG1    1 
ATOM   5219  C  CG2    . THR   B 2  237 ? -15.387 -67.616  30.021  1.00 50.81  ? 237 THR   B CG2    1 
ATOM   5220  N  N      . THR   B 2  238 ? -12.791 -68.001  33.252  1.00 48.69  ? 238 THR   B N      1 
ATOM   5221  C  CA     . THR   B 2  238 ? -12.211 -69.306  33.568  1.00 49.64  ? 238 THR   B CA     1 
ATOM   5222  C  C      . THR   B 2  238 ? -13.170 -70.145  34.419  1.00 55.48  ? 238 THR   B C      1 
ATOM   5223  O  O      . THR   B 2  238 ? -13.564 -71.253  34.028  1.00 53.48  ? 238 THR   B O      1 
ATOM   5224  C  CB     . THR   B 2  238 ? -10.862 -69.133  34.283  1.00 51.00  ? 238 THR   B CB     1 
ATOM   5225  O  OG1    . THR   B 2  238 ? -9.974  -68.379  33.461  1.00 54.95  ? 238 THR   B OG1    1 
ATOM   5226  C  CG2    . THR   B 2  238 ? -10.193 -70.476  34.453  1.00 46.79  ? 238 THR   B CG2    1 
ATOM   5227  N  N      . CYS   B 2  239 ? -13.574 -69.621  35.588  1.00 48.47  ? 239 CYS   B N      1 
ATOM   5228  C  CA     . CYS   B 2  239 ? -14.465 -70.362  36.476  1.00 47.27  ? 239 CYS   B CA     1 
ATOM   5229  C  C      . CYS   B 2  239 ? -15.839 -70.685  35.901  1.00 56.58  ? 239 CYS   B C      1 
ATOM   5230  O  O      . CYS   B 2  239 ? -16.656 -71.305  36.592  1.00 66.07  ? 239 CYS   B O      1 
ATOM   5231  C  CB     . CYS   B 2  239 ? -14.664 -69.631  37.797  1.00 48.85  ? 239 CYS   B CB     1 
ATOM   5232  S  SG     . CYS   B 2  239 ? -13.181 -69.479  38.751  1.00 61.03  ? 239 CYS   B SG     1 
ATOM   5233  N  N      . LEU   B 2  240 ? -16.126 -70.255  34.674  1.00 50.09  ? 240 LEU   B N      1 
ATOM   5234  C  CA     . LEU   B 2  240 ? -17.305 -70.731  33.964  1.00 50.62  ? 240 LEU   B CA     1 
ATOM   5235  C  C      . LEU   B 2  240 ? -16.985 -71.859  32.994  1.00 53.74  ? 240 LEU   B C      1 
ATOM   5236  O  O      . LEU   B 2  240 ? -17.850 -72.692  32.724  1.00 58.91  ? 240 LEU   B O      1 
ATOM   5237  C  CB     . LEU   B 2  240 ? -17.989 -69.588  33.192  1.00 48.82  ? 240 LEU   B CB     1 
ATOM   5238  C  CG     . LEU   B 2  240 ? -18.324 -68.239  33.834  1.00 42.40  ? 240 LEU   B CG     1 
ATOM   5239  C  CD1    . LEU   B 2  240 ? -18.842 -67.330  32.780  1.00 36.05  ? 240 LEU   B CD1    1 
ATOM   5240  C  CD2    . LEU   B 2  240 ? -19.362 -68.382  34.913  1.00 42.25  ? 240 LEU   B CD2    1 
ATOM   5241  N  N      . ARG   B 2  241 ? -15.769 -71.912  32.464  1.00 53.97  ? 241 ARG   B N      1 
ATOM   5242  C  CA     . ARG   B 2  241 ? -15.459 -72.851  31.402  1.00 54.70  ? 241 ARG   B CA     1 
ATOM   5243  C  C      . ARG   B 2  241 ? -14.846 -74.137  31.908  1.00 61.79  ? 241 ARG   B C      1 
ATOM   5244  O  O      . ARG   B 2  241 ? -14.882 -75.144  31.188  1.00 68.11  ? 241 ARG   B O      1 
ATOM   5245  C  CB     . ARG   B 2  241 ? -14.510 -72.212  30.384  1.00 55.51  ? 241 ARG   B CB     1 
ATOM   5246  C  CG     . ARG   B 2  241 ? -15.030 -70.914  29.817  1.00 50.25  ? 241 ARG   B CG     1 
ATOM   5247  C  CD     . ARG   B 2  241 ? -14.189 -70.425  28.665  1.00 50.16  ? 241 ARG   B CD     1 
ATOM   5248  N  NE     . ARG   B 2  241 ? -13.095 -69.604  29.156  1.00 54.89  ? 241 ARG   B NE     1 
ATOM   5249  C  CZ     . ARG   B 2  241 ? -11.829 -69.992  29.150  1.00 55.27  ? 241 ARG   B CZ     1 
ATOM   5250  N  NH1    . ARG   B 2  241 ? -11.473 -71.167  28.656  1.00 53.41  ? 241 ARG   B NH1    1 
ATOM   5251  N  NH2    . ARG   B 2  241 ? -10.899 -69.183  29.651  1.00 49.19  ? 241 ARG   B NH2    1 
ATOM   5252  N  N      . PHE   B 2  242 ? -14.288 -74.135  33.111  1.00 63.02  ? 242 PHE   B N      1 
ATOM   5253  C  CA     . PHE   B 2  242 ? -13.642 -75.324  33.629  1.00 61.72  ? 242 PHE   B CA     1 
ATOM   5254  C  C      . PHE   B 2  242 ? -14.256 -75.784  34.939  1.00 63.79  ? 242 PHE   B C      1 
ATOM   5255  O  O      . PHE   B 2  242 ? -14.844 -74.988  35.678  1.00 60.61  ? 242 PHE   B O      1 
ATOM   5256  C  CB     . PHE   B 2  242 ? -12.141 -75.095  33.814  1.00 54.82  ? 242 PHE   B CB     1 
ATOM   5257  C  CG     . PHE   B 2  242 ? -11.430 -74.856  32.527  1.00 63.78  ? 242 PHE   B CG     1 
ATOM   5258  C  CD1    . PHE   B 2  242 ? -11.130 -75.926  31.692  1.00 64.09  ? 242 PHE   B CD1    1 
ATOM   5259  C  CD2    . PHE   B 2  242 ? -11.027 -73.588  32.162  1.00 58.25  ? 242 PHE   B CD2    1 
ATOM   5260  C  CE1    . PHE   B 2  242 ? -10.482 -75.734  30.514  1.00 56.28  ? 242 PHE   B CE1    1 
ATOM   5261  C  CE2    . PHE   B 2  242 ? -10.366 -73.388  30.983  1.00 56.84  ? 242 PHE   B CE2    1 
ATOM   5262  C  CZ     . PHE   B 2  242 ? -10.093 -74.460  30.156  1.00 59.79  ? 242 PHE   B CZ     1 
ATOM   5263  N  N      . PRO   B 2  243 ? -14.139 -77.076  35.247  1.00 73.16  ? 243 PRO   B N      1 
ATOM   5264  C  CA     . PRO   B 2  243 ? -14.660 -77.599  36.512  1.00 71.67  ? 243 PRO   B CA     1 
ATOM   5265  C  C      . PRO   B 2  243 ? -13.767 -77.212  37.677  1.00 71.36  ? 243 PRO   B C      1 
ATOM   5266  O  O      . PRO   B 2  243 ? -12.549 -77.052  37.533  1.00 65.64  ? 243 PRO   B O      1 
ATOM   5267  C  CB     . PRO   B 2  243 ? -14.635 -79.117  36.297  1.00 71.77  ? 243 PRO   B CB     1 
ATOM   5268  C  CG     . PRO   B 2  243 ? -13.532 -79.322  35.303  1.00 64.33  ? 243 PRO   B CG     1 
ATOM   5269  C  CD     . PRO   B 2  243 ? -13.578 -78.141  34.391  1.00 71.38  ? 243 PRO   B CD     1 
ATOM   5270  N  N      . GLY   B 2  244 ? -14.383 -77.091  38.847  1.00 72.45  ? 244 GLY   B N      1 
ATOM   5271  C  CA     . GLY   B 2  244 ? -13.591 -76.791  40.021  1.00 75.16  ? 244 GLY   B CA     1 
ATOM   5272  C  C      . GLY   B 2  244 ? -14.409 -76.896  41.283  1.00 78.00  ? 244 GLY   B C      1 
ATOM   5273  O  O      . GLY   B 2  244 ? -15.557 -77.350  41.269  1.00 70.06  ? 244 GLY   B O      1 
ATOM   5274  N  N      . GLN   B 2  245 ? -13.788 -76.472  42.391  1.00 79.03  ? 245 GLN   B N      1 
ATOM   5275  C  CA     . GLN   B 2  245 ? -14.531 -76.405  43.640  1.00 79.05  ? 245 GLN   B CA     1 
ATOM   5276  C  C      . GLN   B 2  245 ? -15.705 -75.451  43.495  1.00 81.21  ? 245 GLN   B C      1 
ATOM   5277  O  O      . GLN   B 2  245 ? -16.807 -75.735  43.979  1.00 81.92  ? 245 GLN   B O      1 
ATOM   5278  C  CB     . GLN   B 2  245 ? -13.606 -76.014  44.805  1.00 76.25  ? 245 GLN   B CB     1 
ATOM   5279  C  CG     . GLN   B 2  245 ? -14.200 -76.312  46.217  1.00 79.28  ? 245 GLN   B CG     1 
ATOM   5280  C  CD     . GLN   B 2  245 ? -13.279 -75.959  47.407  1.00 83.73  ? 245 GLN   B CD     1 
ATOM   5281  O  OE1    . GLN   B 2  245 ? -12.479 -75.027  47.339  1.00 99.75  ? 245 GLN   B OE1    1 
ATOM   5282  N  NE2    . GLN   B 2  245 ? -13.410 -76.709  48.509  1.00 67.34  ? 245 GLN   B NE2    1 
ATOM   5283  N  N      . LEU   B 2  246 ? -15.511 -74.352  42.756  1.00 85.81  ? 246 LEU   B N      1 
ATOM   5284  C  CA     . LEU   B 2  246 ? -16.555 -73.333  42.656  1.00 82.17  ? 246 LEU   B CA     1 
ATOM   5285  C  C      . LEU   B 2  246 ? -17.760 -73.816  41.861  1.00 79.83  ? 246 LEU   B C      1 
ATOM   5286  O  O      . LEU   B 2  246 ? -18.890 -73.781  42.368  1.00 77.31  ? 246 LEU   B O      1 
ATOM   5287  C  CB     . LEU   B 2  246 ? -16.006 -72.055  42.035  1.00 72.51  ? 246 LEU   B CB     1 
ATOM   5288  C  CG     . LEU   B 2  246 ? -15.757 -71.023  43.121  1.00 70.56  ? 246 LEU   B CG     1 
ATOM   5289  C  CD1    . LEU   B 2  246 ? -15.407 -69.692  42.482  1.00 60.67  ? 246 LEU   B CD1    1 
ATOM   5290  C  CD2    . LEU   B 2  246 ? -16.954 -70.933  44.081  1.00 70.20  ? 246 LEU   B CD2    1 
ATOM   5291  N  N      . ASN   B 2  247 ? -17.552 -74.232  40.599  1.00 74.74  ? 247 ASN   B N      1 
ATOM   5292  C  CA     . ASN   B 2  247 ? -18.709 -74.522  39.765  1.00 68.57  ? 247 ASN   B CA     1 
ATOM   5293  C  C      . ASN   B 2  247 ? -19.461 -73.212  39.531  1.00 71.58  ? 247 ASN   B C      1 
ATOM   5294  O  O      . ASN   B 2  247 ? -20.580 -73.043  40.037  1.00 73.38  ? 247 ASN   B O      1 
ATOM   5295  C  CB     . ASN   B 2  247 ? -19.594 -75.557  40.480  1.00 84.19  ? 247 ASN   B CB     1 
ATOM   5296  C  CG     . ASN   B 2  247 ? -20.702 -76.133  39.599  1.00 88.80  ? 247 ASN   B CG     1 
ATOM   5297  O  OD1    . ASN   B 2  247 ? -20.493 -76.437  38.425  1.00 78.96  ? 247 ASN   B OD1    1 
ATOM   5298  N  ND2    . ASN   B 2  247 ? -21.902 -76.273  40.176  1.00 86.64  ? 247 ASN   B ND2    1 
ATOM   5299  N  N      . ALA   B 2  248 ? -18.847 -72.257  38.820  1.00 67.04  ? 248 ALA   B N      1 
ATOM   5300  C  CA     . ALA   B 2  248 ? -19.335 -70.875  38.823  1.00 59.42  ? 248 ALA   B CA     1 
ATOM   5301  C  C      . ALA   B 2  248 ? -20.293 -70.636  37.669  1.00 51.66  ? 248 ALA   B C      1 
ATOM   5302  O  O      . ALA   B 2  248 ? -20.225 -71.309  36.639  1.00 48.12  ? 248 ALA   B O      1 
ATOM   5303  C  CB     . ALA   B 2  248 ? -18.183 -69.866  38.746  1.00 48.57  ? 248 ALA   B CB     1 
ATOM   5304  N  N      . ASP   B 2  249 ? -21.197 -69.673  37.854  1.00 48.16  ? 249 ASP   B N      1 
ATOM   5305  C  CA     . ASP   B 2  249 ? -22.074 -69.254  36.772  1.00 47.74  ? 249 ASP   B CA     1 
ATOM   5306  C  C      . ASP   B 2  249 ? -22.310 -67.753  36.875  1.00 45.87  ? 249 ASP   B C      1 
ATOM   5307  O  O      . ASP   B 2  249 ? -21.948 -67.107  37.869  1.00 45.73  ? 249 ASP   B O      1 
ATOM   5308  C  CB     . ASP   B 2  249 ? -23.396 -70.046  36.766  1.00 44.01  ? 249 ASP   B CB     1 
ATOM   5309  C  CG     . ASP   B 2  249 ? -24.279 -69.741  37.959  1.00 50.00  ? 249 ASP   B CG     1 
ATOM   5310  O  OD1    . ASP   B 2  249 ? -24.473 -68.546  38.257  1.00 50.46  ? 249 ASP   B OD1    1 
ATOM   5311  O  OD2    . ASP   B 2  249 ? -24.789 -70.691  38.603  1.00 54.91  ? 249 ASP   B OD2    1 
ATOM   5312  N  N      . LEU   B 2  250 ? -22.926 -67.205  35.821  1.00 40.02  ? 250 LEU   B N      1 
ATOM   5313  C  CA     . LEU   B 2  250 ? -23.154 -65.765  35.746  1.00 38.24  ? 250 LEU   B CA     1 
ATOM   5314  C  C      . LEU   B 2  250 ? -23.997 -65.258  36.918  1.00 44.47  ? 250 LEU   B C      1 
ATOM   5315  O  O      . LEU   B 2  250 ? -23.723 -64.184  37.470  1.00 44.23  ? 250 LEU   B O      1 
ATOM   5316  C  CB     . LEU   B 2  250 ? -23.812 -65.427  34.411  1.00 40.12  ? 250 LEU   B CB     1 
ATOM   5317  C  CG     . LEU   B 2  250 ? -22.864 -65.565  33.218  1.00 41.47  ? 250 LEU   B CG     1 
ATOM   5318  C  CD1    . LEU   B 2  250 ? -23.610 -65.432  31.935  1.00 37.89  ? 250 LEU   B CD1    1 
ATOM   5319  C  CD2    . LEU   B 2  250 ? -21.815 -64.483  33.312  1.00 44.91  ? 250 LEU   B CD2    1 
ATOM   5320  N  N      . ARG   B 2  251 ? -25.020 -66.011  37.329  1.00 43.40  ? 251 ARG   B N      1 
ATOM   5321  C  CA     . ARG   B 2  251 ? -25.906 -65.480  38.358  1.00 40.48  ? 251 ARG   B CA     1 
ATOM   5322  C  C      . ARG   B 2  251 ? -25.189 -65.411  39.695  1.00 38.58  ? 251 ARG   B C      1 
ATOM   5323  O  O      . ARG   B 2  251 ? -25.218 -64.377  40.367  1.00 41.02  ? 251 ARG   B O      1 
ATOM   5324  C  CB     . ARG   B 2  251 ? -27.185 -66.311  38.472  1.00 43.88  ? 251 ARG   B CB     1 
ATOM   5325  C  CG     . ARG   B 2  251 ? -28.172 -65.785  39.507  1.00 35.36  ? 251 ARG   B CG     1 
ATOM   5326  C  CD     . ARG   B 2  251 ? -29.526 -66.426  39.310  1.00 33.86  ? 251 ARG   B CD     1 
ATOM   5327  N  NE     . ARG   B 2  251 ? -30.356 -65.582  38.482  1.00 42.42  ? 251 ARG   B NE     1 
ATOM   5328  C  CZ     . ARG   B 2  251 ? -30.630 -65.842  37.215  1.00 46.12  ? 251 ARG   B CZ     1 
ATOM   5329  N  NH1    . ARG   B 2  251 ? -30.302 -67.007  36.672  1.00 42.47  ? 251 ARG   B NH1    1 
ATOM   5330  N  NH2    . ARG   B 2  251 ? -31.238 -64.905  36.476  1.00 42.14  ? 251 ARG   B NH2    1 
ATOM   5331  N  N      . LYS   B 2  252 ? -24.530 -66.498  40.107  1.00 42.51  ? 252 LYS   B N      1 
ATOM   5332  C  CA     . LYS   B 2  252 ? -23.825 -66.428  41.383  1.00 44.77  ? 252 LYS   B CA     1 
ATOM   5333  C  C      . LYS   B 2  252 ? -22.770 -65.346  41.318  1.00 43.15  ? 252 LYS   B C      1 
ATOM   5334  O  O      . LYS   B 2  252 ? -22.596 -64.582  42.280  1.00 38.87  ? 252 LYS   B O      1 
ATOM   5335  C  CB     . LYS   B 2  252 ? -23.232 -67.793  41.798  1.00 38.38  ? 252 LYS   B CB     1 
ATOM   5336  C  CG     . LYS   B 2  252 ? -24.285 -68.686  42.502  1.00 44.86  ? 252 LYS   B CG     1 
ATOM   5337  C  CD     . LYS   B 2  252 ? -23.874 -70.106  42.949  1.00 47.13  ? 252 LYS   B CD     1 
ATOM   5338  C  CE     . LYS   B 2  252 ? -23.861 -71.134  41.812  1.00 53.13  ? 252 LYS   B CE     1 
ATOM   5339  N  NZ     . LYS   B 2  252 ? -23.748 -72.553  42.304  1.00 48.47  ? 252 LYS   B NZ     1 
ATOM   5340  N  N      . LEU   B 2  253 ? -22.117 -65.206  40.158  1.00 36.01  ? 253 LEU   B N      1 
ATOM   5341  C  CA     . LEU   B 2  253 ? -21.128 -64.150  40.030  1.00 37.94  ? 253 LEU   B CA     1 
ATOM   5342  C  C      . LEU   B 2  253 ? -21.740 -62.793  40.377  1.00 41.81  ? 253 LEU   B C      1 
ATOM   5343  O  O      . LEU   B 2  253 ? -21.206 -62.055  41.217  1.00 39.12  ? 253 LEU   B O      1 
ATOM   5344  C  CB     . LEU   B 2  253 ? -20.522 -64.154  38.632  1.00 37.49  ? 253 LEU   B CB     1 
ATOM   5345  C  CG     . LEU   B 2  253 ? -19.633 -62.927  38.416  1.00 38.63  ? 253 LEU   B CG     1 
ATOM   5346  C  CD1    . LEU   B 2  253 ? -18.390 -63.014  39.244  1.00 34.39  ? 253 LEU   B CD1    1 
ATOM   5347  C  CD2    . LEU   B 2  253 ? -19.276 -62.811  36.970  1.00 38.93  ? 253 LEU   B CD2    1 
ATOM   5348  N  N      . ALA   B 2  254 ? -22.897 -62.471  39.780  1.00 40.77  ? 254 ALA   B N      1 
ATOM   5349  C  CA     . ALA   B 2  254 ? -23.565 -61.197  40.046  1.00 36.73  ? 254 ALA   B CA     1 
ATOM   5350  C  C      . ALA   B 2  254 ? -24.054 -61.107  41.485  1.00 37.87  ? 254 ALA   B C      1 
ATOM   5351  O  O      . ALA   B 2  254 ? -23.974 -60.038  42.105  1.00 38.59  ? 254 ALA   B O      1 
ATOM   5352  C  CB     . ALA   B 2  254 ? -24.736 -61.005  39.080  1.00 37.09  ? 254 ALA   B CB     1 
ATOM   5353  N  N      . VAL   B 2  255 ? -24.576 -62.213  42.030  1.00 37.86  ? 255 VAL   B N      1 
ATOM   5354  C  CA     . VAL   B 2  255 ? -25.120 -62.186  43.391  1.00 41.24  ? 255 VAL   B CA     1 
ATOM   5355  C  C      . VAL   B 2  255 ? -24.043 -61.793  44.393  1.00 37.98  ? 255 VAL   B C      1 
ATOM   5356  O  O      . VAL   B 2  255 ? -24.267 -60.976  45.290  1.00 31.82  ? 255 VAL   B O      1 
ATOM   5357  C  CB     . VAL   B 2  255 ? -25.752 -63.547  43.733  1.00 39.97  ? 255 VAL   B CB     1 
ATOM   5358  C  CG1    . VAL   B 2  255 ? -26.307 -63.561  45.134  1.00 32.25  ? 255 VAL   B CG1    1 
ATOM   5359  C  CG2    . VAL   B 2  255 ? -26.855 -63.819  42.763  1.00 43.16  ? 255 VAL   B CG2    1 
ATOM   5360  N  N      . ASN   B 2  256 ? -22.850 -62.336  44.228  1.00 40.72  ? 256 ASN   B N      1 
ATOM   5361  C  CA     . ASN   B 2  256 ? -21.778 -62.115  45.178  1.00 37.56  ? 256 ASN   B CA     1 
ATOM   5362  C  C      . ASN   B 2  256 ? -20.976 -60.858  44.905  1.00 36.61  ? 256 ASN   B C      1 
ATOM   5363  O  O      . ASN   B 2  256 ? -20.377 -60.318  45.840  1.00 35.77  ? 256 ASN   B O      1 
ATOM   5364  C  CB     . ASN   B 2  256 ? -20.860 -63.332  45.187  1.00 41.07  ? 256 ASN   B CB     1 
ATOM   5365  C  CG     . ASN   B 2  256 ? -21.534 -64.542  45.780  1.00 43.94  ? 256 ASN   B CG     1 
ATOM   5366  O  OD1    . ASN   B 2  256 ? -21.818 -64.571  46.973  1.00 47.48  ? 256 ASN   B OD1    1 
ATOM   5367  N  ND2    . ASN   B 2  256 ? -21.831 -65.534  44.942  1.00 40.06  ? 256 ASN   B ND2    1 
ATOM   5368  N  N      . MET   B 2  257 ? -20.966 -60.360  43.665  1.00 37.43  ? 257 MET   B N      1 
ATOM   5369  C  CA     . MET   B 2  257 ? -20.154 -59.186  43.333  1.00 35.33  ? 257 MET   B CA     1 
ATOM   5370  C  C      . MET   B 2  257 ? -20.890 -57.854  43.478  1.00 38.25  ? 257 MET   B C      1 
ATOM   5371  O  O      . MET   B 2  257 ? -20.259 -56.831  43.784  1.00 39.50  ? 257 MET   B O      1 
ATOM   5372  C  CB     . MET   B 2  257 ? -19.601 -59.319  41.924  1.00 29.73  ? 257 MET   B CB     1 
ATOM   5373  C  CG     . MET   B 2  257 ? -18.555 -60.409  41.791  1.00 33.69  ? 257 MET   B CG     1 
ATOM   5374  S  SD     . MET   B 2  257 ? -17.083 -59.988  42.758  1.00 45.94  ? 257 MET   B SD     1 
ATOM   5375  C  CE     . MET   B 2  257 ? -16.472 -58.522  41.926  1.00 39.02  ? 257 MET   B CE     1 
ATOM   5376  N  N      . VAL   B 2  258 ? -22.210 -57.852  43.360  1.00 37.83  ? 258 VAL   B N      1 
ATOM   5377  C  CA     . VAL   B 2  258 ? -22.977 -56.626  43.204  1.00 32.62  ? 258 VAL   B CA     1 
ATOM   5378  C  C      . VAL   B 2  258 ? -23.818 -56.311  44.439  1.00 35.71  ? 258 VAL   B C      1 
ATOM   5379  O  O      . VAL   B 2  258 ? -24.994 -56.687  44.473  1.00 36.94  ? 258 VAL   B O      1 
ATOM   5380  C  CB     . VAL   B 2  258 ? -23.856 -56.784  41.972  1.00 30.35  ? 258 VAL   B CB     1 
ATOM   5381  C  CG1    . VAL   B 2  258 ? -24.596 -55.498  41.664  1.00 35.54  ? 258 VAL   B CG1    1 
ATOM   5382  C  CG2    . VAL   B 2  258 ? -23.001 -57.284  40.840  1.00 31.64  ? 258 VAL   B CG2    1 
ATOM   5383  N  N      . PRO   B 2  259 ? -23.296 -55.609  45.458  1.00 33.52  ? 259 PRO   B N      1 
ATOM   5384  C  CA     . PRO   B 2  259 ? -24.120 -55.341  46.652  1.00 33.71  ? 259 PRO   B CA     1 
ATOM   5385  C  C      . PRO   B 2  259 ? -25.328 -54.473  46.385  1.00 38.57  ? 259 PRO   B C      1 
ATOM   5386  O  O      . PRO   B 2  259 ? -26.395 -54.664  46.990  1.00 33.78  ? 259 PRO   B O      1 
ATOM   5387  C  CB     . PRO   B 2  259 ? -23.140 -54.640  47.593  1.00 33.91  ? 259 PRO   B CB     1 
ATOM   5388  C  CG     . PRO   B 2  259 ? -22.194 -54.004  46.731  1.00 37.33  ? 259 PRO   B CG     1 
ATOM   5389  C  CD     . PRO   B 2  259 ? -22.003 -54.927  45.539  1.00 36.56  ? 259 PRO   B CD     1 
ATOM   5390  N  N      . PHE   B 2  260 ? -25.175 -53.495  45.507  1.00 42.48  ? 260 PHE   B N      1 
ATOM   5391  C  CA     . PHE   B 2  260 ? -26.250 -52.611  45.101  1.00 38.94  ? 260 PHE   B CA     1 
ATOM   5392  C  C      . PHE   B 2  260 ? -26.312 -52.678  43.590  1.00 39.28  ? 260 PHE   B C      1 
ATOM   5393  O  O      . PHE   B 2  260 ? -25.301 -52.978  42.949  1.00 38.67  ? 260 PHE   B O      1 
ATOM   5394  C  CB     . PHE   B 2  260 ? -25.992 -51.194  45.603  1.00 36.76  ? 260 PHE   B CB     1 
ATOM   5395  C  CG     . PHE   B 2  260 ? -25.535 -51.185  47.011  1.00 39.15  ? 260 PHE   B CG     1 
ATOM   5396  C  CD1    . PHE   B 2  260 ? -26.428 -51.386  48.037  1.00 38.89  ? 260 PHE   B CD1    1 
ATOM   5397  C  CD2    . PHE   B 2  260 ? -24.202 -51.015  47.312  1.00 45.61  ? 260 PHE   B CD2    1 
ATOM   5398  C  CE1    . PHE   B 2  260 ? -26.005 -51.418  49.342  1.00 43.40  ? 260 PHE   B CE1    1 
ATOM   5399  C  CE2    . PHE   B 2  260 ? -23.764 -51.028  48.625  1.00 47.78  ? 260 PHE   B CE2    1 
ATOM   5400  C  CZ     . PHE   B 2  260 ? -24.666 -51.228  49.641  1.00 46.66  ? 260 PHE   B CZ     1 
ATOM   5401  N  N      . PRO   B 2  261 ? -27.476 -52.470  42.998  1.00 40.97  ? 261 PRO   B N      1 
ATOM   5402  C  CA     . PRO   B 2  261 ? -27.702 -53.039  41.663  1.00 32.70  ? 261 PRO   B CA     1 
ATOM   5403  C  C      . PRO   B 2  261 ? -27.056 -52.185  40.599  1.00 31.52  ? 261 PRO   B C      1 
ATOM   5404  O  O      . PRO   B 2  261 ? -26.484 -52.701  39.640  1.00 33.92  ? 261 PRO   B O      1 
ATOM   5405  C  CB     . PRO   B 2  261 ? -29.221 -53.076  41.535  1.00 26.10  ? 261 PRO   B CB     1 
ATOM   5406  C  CG     . PRO   B 2  261 ? -29.759 -52.452  42.774  1.00 33.95  ? 261 PRO   B CG     1 
ATOM   5407  C  CD     . PRO   B 2  261 ? -28.657 -51.793  43.530  1.00 34.72  ? 261 PRO   B CD     1 
ATOM   5408  N  N      . ARG   B 2  262 ? -27.075 -50.871  40.780  1.00 32.49  ? 262 ARG   B N      1 
ATOM   5409  C  CA     . ARG   B 2  262 ? -26.425 -50.047  39.772  1.00 37.05  ? 262 ARG   B CA     1 
ATOM   5410  C  C      . ARG   B 2  262 ? -24.913 -50.190  39.817  1.00 33.79  ? 262 ARG   B C      1 
ATOM   5411  O  O      . ARG   B 2  262 ? -24.261 -50.031  38.784  1.00 36.51  ? 262 ARG   B O      1 
ATOM   5412  C  CB     . ARG   B 2  262 ? -26.834 -48.575  39.915  1.00 41.78  ? 262 ARG   B CB     1 
ATOM   5413  C  CG     . ARG   B 2  262 ? -28.344 -48.372  39.925  1.00 43.03  ? 262 ARG   B CG     1 
ATOM   5414  C  CD     . ARG   B 2  262 ? -28.748 -46.979  40.331  1.00 39.12  ? 262 ARG   B CD     1 
ATOM   5415  N  NE     . ARG   B 2  262 ? -28.652 -46.067  39.203  1.00 47.42  ? 262 ARG   B NE     1 
ATOM   5416  C  CZ     . ARG   B 2  262 ? -27.985 -44.924  39.209  1.00 50.39  ? 262 ARG   B CZ     1 
ATOM   5417  N  NH1    . ARG   B 2  262 ? -27.278 -44.545  40.263  1.00 53.24  ? 262 ARG   B NH1    1 
ATOM   5418  N  NH2    . ARG   B 2  262 ? -28.044 -44.135  38.138  1.00 48.09  ? 262 ARG   B NH2    1 
ATOM   5419  N  N      . LEU   B 2  263 ? -24.338 -50.522  40.972  1.00 35.80  ? 263 LEU   B N      1 
ATOM   5420  C  CA     . LEU   B 2  263 ? -22.884 -50.589  41.114  1.00 34.00  ? 263 LEU   B CA     1 
ATOM   5421  C  C      . LEU   B 2  263 ? -22.365 -51.950  40.656  1.00 35.41  ? 263 LEU   B C      1 
ATOM   5422  O  O      . LEU   B 2  263 ? -21.917 -52.768  41.452  1.00 42.02  ? 263 LEU   B O      1 
ATOM   5423  C  CB     . LEU   B 2  263 ? -22.484 -50.315  42.549  1.00 31.01  ? 263 LEU   B CB     1 
ATOM   5424  C  CG     . LEU   B 2  263 ? -23.199 -49.101  43.082  1.00 37.30  ? 263 LEU   B CG     1 
ATOM   5425  C  CD1    . LEU   B 2  263 ? -22.586 -48.605  44.377  1.00 45.22  ? 263 LEU   B CD1    1 
ATOM   5426  C  CD2    . LEU   B 2  263 ? -23.123 -48.049  42.026  1.00 43.25  ? 263 LEU   B CD2    1 
ATOM   5427  N  N      . HIS   B 2  264 ? -22.401 -52.176  39.340  1.00 29.46  ? 264 HIS   B N      1 
ATOM   5428  C  CA     . HIS   B 2  264 ? -22.067 -53.480  38.781  1.00 28.42  ? 264 HIS   B CA     1 
ATOM   5429  C  C      . HIS   B 2  264 ? -21.050 -53.349  37.651  1.00 38.98  ? 264 HIS   B C      1 
ATOM   5430  O  O      . HIS   B 2  264 ? -21.043 -54.141  36.684  1.00 36.06  ? 264 HIS   B O      1 
ATOM   5431  C  CB     . HIS   B 2  264 ? -23.337 -54.200  38.346  1.00 29.11  ? 264 HIS   B CB     1 
ATOM   5432  C  CG     . HIS   B 2  264 ? -24.113 -53.477  37.285  1.00 39.42  ? 264 HIS   B CG     1 
ATOM   5433  N  ND1    . HIS   B 2  264 ? -25.147 -52.613  37.578  1.00 36.18  ? 264 HIS   B ND1    1 
ATOM   5434  C  CD2    . HIS   B 2  264 ? -24.055 -53.541  35.927  1.00 39.60  ? 264 HIS   B CD2    1 
ATOM   5435  C  CE1    . HIS   B 2  264 ? -25.658 -52.140  36.451  1.00 39.59  ? 264 HIS   B CE1    1 
ATOM   5436  N  NE2    . HIS   B 2  264 ? -25.016 -52.689  35.435  1.00 36.59  ? 264 HIS   B NE2    1 
ATOM   5437  N  N      . PHE   B 2  265 ? -20.159 -52.360  37.785  1.00 42.96  ? 265 PHE   B N      1 
ATOM   5438  C  CA     . PHE   B 2  265 ? -19.073 -52.110  36.843  1.00 37.78  ? 265 PHE   B CA     1 
ATOM   5439  C  C      . PHE   B 2  265 ? -17.772 -52.516  37.512  1.00 36.53  ? 265 PHE   B C      1 
ATOM   5440  O  O      . PHE   B 2  265 ? -17.404 -51.949  38.547  1.00 38.77  ? 265 PHE   B O      1 
ATOM   5441  C  CB     . PHE   B 2  265 ? -19.054 -50.643  36.402  1.00 39.27  ? 265 PHE   B CB     1 
ATOM   5442  C  CG     . PHE   B 2  265 ? -20.304 -50.240  35.676  1.00 37.68  ? 265 PHE   B CG     1 
ATOM   5443  C  CD1    . PHE   B 2  265 ? -20.399 -50.387  34.310  1.00 34.84  ? 265 PHE   B CD1    1 
ATOM   5444  C  CD2    . PHE   B 2  265 ? -21.412 -49.797  36.373  1.00 37.80  ? 265 PHE   B CD2    1 
ATOM   5445  C  CE1    . PHE   B 2  265 ? -21.557 -50.062  33.654  1.00 35.48  ? 265 PHE   B CE1    1 
ATOM   5446  C  CE2    . PHE   B 2  265 ? -22.576 -49.484  35.713  1.00 37.22  ? 265 PHE   B CE2    1 
ATOM   5447  C  CZ     . PHE   B 2  265 ? -22.647 -49.610  34.360  1.00 36.36  ? 265 PHE   B CZ     1 
ATOM   5448  N  N      . PHE   B 2  266 ? -17.093 -53.495  36.909  1.00 33.10  ? 266 PHE   B N      1 
ATOM   5449  C  CA     . PHE   B 2  266 ? -15.925 -54.176  37.445  1.00 31.28  ? 266 PHE   B CA     1 
ATOM   5450  C  C      . PHE   B 2  266 ? -14.615 -53.717  36.797  1.00 38.93  ? 266 PHE   B C      1 
ATOM   5451  O  O      . PHE   B 2  266 ? -14.559 -53.446  35.593  1.00 42.27  ? 266 PHE   B O      1 
ATOM   5452  C  CB     . PHE   B 2  266 ? -16.058 -55.677  37.231  1.00 30.30  ? 266 PHE   B CB     1 
ATOM   5453  C  CG     . PHE   B 2  266 ? -17.320 -56.275  37.788  1.00 33.49  ? 266 PHE   B CG     1 
ATOM   5454  C  CD1    . PHE   B 2  266 ? -17.988 -55.666  38.823  1.00 32.60  ? 266 PHE   B CD1    1 
ATOM   5455  C  CD2    . PHE   B 2  266 ? -17.768 -57.516  37.358  1.00 30.69  ? 266 PHE   B CD2    1 
ATOM   5456  C  CE1    . PHE   B 2  266 ? -19.100 -56.245  39.373  1.00 31.20  ? 266 PHE   B CE1    1 
ATOM   5457  C  CE2    . PHE   B 2  266 ? -18.883 -58.082  37.908  1.00 28.69  ? 266 PHE   B CE2    1 
ATOM   5458  C  CZ     . PHE   B 2  266 ? -19.545 -57.443  38.910  1.00 26.81  ? 266 PHE   B CZ     1 
ATOM   5459  N  N      . MET   B 2  267 ? -13.540 -53.687  37.609  1.00 37.22  ? 267 MET   B N      1 
ATOM   5460  C  CA     . MET   B 2  267 ? -12.185 -53.404  37.138  1.00 34.09  ? 267 MET   B CA     1 
ATOM   5461  C  C      . MET   B 2  267 ? -11.457 -54.716  36.845  1.00 35.48  ? 267 MET   B C      1 
ATOM   5462  O  O      . MET   B 2  267 ? -11.072 -55.413  37.786  1.00 36.71  ? 267 MET   B O      1 
ATOM   5463  C  CB     . MET   B 2  267 ? -11.429 -52.628  38.198  1.00 35.36  ? 267 MET   B CB     1 
ATOM   5464  C  CG     . MET   B 2  267 ? -11.352 -51.143  38.009  1.00 46.07  ? 267 MET   B CG     1 
ATOM   5465  S  SD     . MET   B 2  267 ? -10.261 -50.432  39.255  1.00 57.54  ? 267 MET   B SD     1 
ATOM   5466  C  CE     . MET   B 2  267 ? -9.020  -51.732  39.331  1.00 44.67  ? 267 MET   B CE     1 
ATOM   5467  N  N      . PRO   B 2  268 ? -11.244 -55.097  35.591  1.00 34.93  ? 268 PRO   B N      1 
ATOM   5468  C  CA     . PRO   B 2  268 ? -10.446 -56.297  35.315  1.00 34.57  ? 268 PRO   B CA     1 
ATOM   5469  C  C      . PRO   B 2  268 ? -8.957  -56.051  35.487  1.00 43.28  ? 268 PRO   B C      1 
ATOM   5470  O  O      . PRO   B 2  268 ? -8.441  -54.962  35.221  1.00 43.32  ? 268 PRO   B O      1 
ATOM   5471  C  CB     . PRO   B 2  268 ? -10.762 -56.609  33.847  1.00 33.76  ? 268 PRO   B CB     1 
ATOM   5472  C  CG     . PRO   B 2  268 ? -11.940 -55.736  33.515  1.00 37.58  ? 268 PRO   B CG     1 
ATOM   5473  C  CD     . PRO   B 2  268 ? -11.841 -54.545  34.369  1.00 36.01  ? 268 PRO   B CD     1 
ATOM   5474  N  N      . GLY   B 2  269 ? -8.262  -57.097  35.925  1.00 47.68  ? 269 GLY   B N      1 
ATOM   5475  C  CA     . GLY   B 2  269 ? -6.813  -57.074  36.032  1.00 51.45  ? 269 GLY   B CA     1 
ATOM   5476  C  C      . GLY   B 2  269 ? -6.151  -58.362  35.565  1.00 52.38  ? 269 GLY   B C      1 
ATOM   5477  O  O      . GLY   B 2  269 ? -6.659  -59.462  35.806  1.00 54.47  ? 269 GLY   B O      1 
ATOM   5478  N  N      . PHE   B 2  270 ? -5.022  -58.263  34.893  1.00 47.32  ? 270 PHE   B N      1 
ATOM   5479  C  CA     . PHE   B 2  270 ? -4.319  -59.463  34.486  1.00 48.86  ? 270 PHE   B CA     1 
ATOM   5480  C  C      . PHE   B 2  270 ? -2.882  -59.401  34.972  1.00 53.98  ? 270 PHE   B C      1 
ATOM   5481  O  O      . PHE   B 2  270 ? -2.260  -58.336  34.940  1.00 58.03  ? 270 PHE   B O      1 
ATOM   5482  C  CB     . PHE   B 2  270 ? -4.320  -59.608  32.995  1.00 47.32  ? 270 PHE   B CB     1 
ATOM   5483  C  CG     . PHE   B 2  270 ? -3.856  -60.940  32.532  1.00 52.61  ? 270 PHE   B CG     1 
ATOM   5484  C  CD1    . PHE   B 2  270 ? -4.728  -62.021  32.515  1.00 55.55  ? 270 PHE   B CD1    1 
ATOM   5485  C  CD2    . PHE   B 2  270 ? -2.528  -61.145  32.194  1.00 52.60  ? 270 PHE   B CD2    1 
ATOM   5486  C  CE1    . PHE   B 2  270 ? -4.298  -63.276  32.085  1.00 62.24  ? 270 PHE   B CE1    1 
ATOM   5487  C  CE2    . PHE   B 2  270 ? -2.075  -62.396  31.770  1.00 54.84  ? 270 PHE   B CE2    1 
ATOM   5488  C  CZ     . PHE   B 2  270 ? -2.954  -63.463  31.712  1.00 60.11  ? 270 PHE   B CZ     1 
ATOM   5489  N  N      . ALA   B 2  271 ? -2.347  -60.544  35.409  1.00 51.98  ? 271 ALA   B N      1 
ATOM   5490  C  CA     . ALA   B 2  271 ? -0.915  -60.660  35.696  1.00 52.30  ? 271 ALA   B CA     1 
ATOM   5491  C  C      . ALA   B 2  271 ? -0.475  -62.070  35.335  1.00 51.10  ? 271 ALA   B C      1 
ATOM   5492  O  O      . ALA   B 2  271 ? -1.195  -63.032  35.626  1.00 52.03  ? 271 ALA   B O      1 
ATOM   5493  C  CB     . ALA   B 2  271 ? -0.559  -60.364  37.160  1.00 49.35  ? 271 ALA   B CB     1 
ATOM   5494  N  N      . PRO   B 2  272 ? 0.698   -62.229  34.705  1.00 55.97  ? 272 PRO   B N      1 
ATOM   5495  C  CA     . PRO   B 2  272 ? 1.695   -61.198  34.358  1.00 54.82  ? 272 PRO   B CA     1 
ATOM   5496  C  C      . PRO   B 2  272 ? 1.343   -60.495  33.066  1.00 56.29  ? 272 PRO   B C      1 
ATOM   5497  O  O      . PRO   B 2  272 ? 0.924   -61.180  32.145  1.00 57.57  ? 272 PRO   B O      1 
ATOM   5498  C  CB     . PRO   B 2  272 ? 2.974   -62.016  34.181  1.00 51.72  ? 272 PRO   B CB     1 
ATOM   5499  C  CG     . PRO   B 2  272 ? 2.462   -63.304  33.575  1.00 54.91  ? 272 PRO   B CG     1 
ATOM   5500  C  CD     . PRO   B 2  272 ? 1.143   -63.571  34.278  1.00 51.79  ? 272 PRO   B CD     1 
ATOM   5501  N  N      . LEU   B 2  273 ? 1.511   -59.180  32.932  1.00 59.68  ? 273 LEU   B N      1 
ATOM   5502  C  CA     . LEU   B 2  273 ? 1.311   -58.536  31.635  1.00 59.49  ? 273 LEU   B CA     1 
ATOM   5503  C  C      . LEU   B 2  273 ? 2.354   -59.024  30.632  1.00 64.01  ? 273 LEU   B C      1 
ATOM   5504  O  O      . LEU   B 2  273 ? 3.555   -59.040  30.919  1.00 64.51  ? 273 LEU   B O      1 
ATOM   5505  C  CB     . LEU   B 2  273 ? 1.376   -57.019  31.777  1.00 54.10  ? 273 LEU   B CB     1 
ATOM   5506  C  CG     . LEU   B 2  273 ? 0.232   -56.466  32.625  1.00 59.34  ? 273 LEU   B CG     1 
ATOM   5507  C  CD1    . LEU   B 2  273 ? 0.415   -54.973  33.012  1.00 50.52  ? 273 LEU   B CD1    1 
ATOM   5508  C  CD2    . LEU   B 2  273 ? -1.070  -56.704  31.884  1.00 52.68  ? 273 LEU   B CD2    1 
ATOM   5509  N  N      . THR   B 2  274 ? 1.887   -59.424  29.451  1.00 67.52  ? 274 THR   B N      1 
ATOM   5510  C  CA     . THR   B 2  274 ? 2.712   -60.049  28.425  1.00 69.39  ? 274 THR   B CA     1 
ATOM   5511  C  C      . THR   B 2  274 ? 2.425   -59.351  27.110  1.00 69.89  ? 274 THR   B C      1 
ATOM   5512  O  O      . THR   B 2  274 ? 1.276   -58.992  26.850  1.00 70.12  ? 274 THR   B O      1 
ATOM   5513  C  CB     . THR   B 2  274 ? 2.388   -61.544  28.282  1.00 74.50  ? 274 THR   B CB     1 
ATOM   5514  O  OG1    . THR   B 2  274 ? 1.041   -61.693  27.812  1.00 73.87  ? 274 THR   B OG1    1 
ATOM   5515  C  CG2    . THR   B 2  274 ? 2.499   -62.250  29.645  1.00 65.48  ? 274 THR   B CG2    1 
ATOM   5516  N  N      . SER   B 2  275 ? 3.455   -59.156  26.282  1.00 79.73  ? 275 SER   B N      1 
ATOM   5517  C  CA     . SER   B 2  275 ? 3.286   -58.527  24.974  1.00 74.54  ? 275 SER   B CA     1 
ATOM   5518  C  C      . SER   B 2  275 ? 3.350   -59.582  23.875  1.00 74.41  ? 275 SER   B C      1 
ATOM   5519  O  O      . SER   B 2  275 ? 4.040   -60.597  24.011  1.00 82.33  ? 275 SER   B O      1 
ATOM   5520  C  CB     . SER   B 2  275 ? 4.329   -57.429  24.738  1.00 63.34  ? 275 SER   B CB     1 
ATOM   5521  O  OG     . SER   B 2  275 ? 5.644   -57.924  24.863  1.00 76.73  ? 275 SER   B OG     1 
ATOM   5522  N  N      . ARG   B 2  276 ? 2.605   -59.333  22.787  1.00 76.05  ? 276 ARG   B N      1 
ATOM   5523  C  CA     . ARG   B 2  276 ? 2.346   -60.354  21.764  1.00 82.15  ? 276 ARG   B CA     1 
ATOM   5524  C  C      . ARG   B 2  276 ? 3.624   -60.905  21.142  1.00 82.82  ? 276 ARG   B C      1 
ATOM   5525  O  O      . ARG   B 2  276 ? 4.544   -60.157  20.799  1.00 88.08  ? 276 ARG   B O      1 
ATOM   5526  C  CB     . ARG   B 2  276 ? 1.431   -59.792  20.661  1.00 72.90  ? 276 ARG   B CB     1 
ATOM   5527  C  CG     . ARG   B 2  276 ? 0.017   -60.370  20.677  1.00 77.53  ? 276 ARG   B CG     1 
ATOM   5528  C  CD     . ARG   B 2  276 ? -0.758  -60.148  19.382  1.00 75.56  ? 276 ARG   B CD     1 
ATOM   5529  N  NE     . ARG   B 2  276 ? -0.849  -58.728  19.059  1.00 75.69  ? 276 ARG   B NE     1 
ATOM   5530  C  CZ     . ARG   B 2  276 ? -0.001  -58.076  18.280  1.00 73.53  ? 276 ARG   B CZ     1 
ATOM   5531  N  NH1    . ARG   B 2  276 ? 0.955   -58.708  17.621  1.00 83.59  ? 276 ARG   B NH1    1 
ATOM   5532  N  NH2    . ARG   B 2  276 ? -0.119  -56.756  18.156  1.00 66.67  ? 276 ARG   B NH2    1 
ATOM   5533  N  N      . GLY   B 2  277 ? 3.669   -62.228  20.990  1.00 80.00  ? 277 GLY   B N      1 
ATOM   5534  C  CA     . GLY   B 2  277 ? 4.820   -62.892  20.408  1.00 89.61  ? 277 GLY   B CA     1 
ATOM   5535  C  C      . GLY   B 2  277 ? 5.933   -63.207  21.391  1.00 100.55 ? 277 GLY   B C      1 
ATOM   5536  O  O      . GLY   B 2  277 ? 6.187   -64.379  21.695  1.00 104.56 ? 277 GLY   B O      1 
ATOM   5537  N  N      . SER   B 2  278 ? 6.610   -62.177  21.898  1.00 101.33 ? 278 SER   B N      1 
ATOM   5538  C  CA     . SER   B 2  278 ? 7.706   -62.410  22.829  1.00 110.92 ? 278 SER   B CA     1 
ATOM   5539  C  C      . SER   B 2  278 ? 7.183   -63.088  24.092  1.00 116.49 ? 278 SER   B C      1 
ATOM   5540  O  O      . SER   B 2  278 ? 6.330   -62.542  24.802  1.00 106.49 ? 278 SER   B O      1 
ATOM   5541  C  CB     . SER   B 2  278 ? 8.425   -61.101  23.176  1.00 110.95 ? 278 SER   B CB     1 
ATOM   5542  O  OG     . SER   B 2  278 ? 7.514   -60.049  23.430  1.00 109.59 ? 278 SER   B OG     1 
ATOM   5543  N  N      . GLN   B 2  279 ? 7.674   -64.302  24.338  1.00 119.37 ? 279 GLN   B N      1 
ATOM   5544  C  CA     . GLN   B 2  279 ? 7.478   -65.004  25.598  1.00 113.23 ? 279 GLN   B CA     1 
ATOM   5545  C  C      . GLN   B 2  279 ? 8.725   -64.824  26.454  1.00 108.06 ? 279 GLN   B C      1 
ATOM   5546  O  O      . GLN   B 2  279 ? 9.849   -64.953  25.957  1.00 106.07 ? 279 GLN   B O      1 
ATOM   5547  C  CB     . GLN   B 2  279 ? 7.207   -66.495  25.364  1.00 108.53 ? 279 GLN   B CB     1 
ATOM   5548  C  CG     . GLN   B 2  279 ? 7.232   -67.356  26.639  1.00 104.72 ? 279 GLN   B CG     1 
ATOM   5549  C  CD     . GLN   B 2  279 ? 7.253   -68.859  26.357  1.00 102.63 ? 279 GLN   B CD     1 
ATOM   5550  O  OE1    . GLN   B 2  279 ? 8.067   -69.599  26.919  1.00 100.05 ? 279 GLN   B OE1    1 
ATOM   5551  N  NE2    . GLN   B 2  279 ? 6.356   -69.313  25.484  1.00 102.30 ? 279 GLN   B NE2    1 
ATOM   5552  N  N      . GLN   B 2  280 ? 8.529   -64.486  27.720  1.00 108.13 ? 280 GLN   B N      1 
ATOM   5553  C  CA     . GLN   B 2  280 ? 9.586   -64.628  28.708  1.00 105.76 ? 280 GLN   B CA     1 
ATOM   5554  C  C      . GLN   B 2  280 ? 9.347   -65.910  29.499  1.00 98.15  ? 280 GLN   B C      1 
ATOM   5555  O  O      . GLN   B 2  280 ? 8.208   -66.364  29.655  1.00 88.44  ? 280 GLN   B O      1 
ATOM   5556  C  CB     . GLN   B 2  280 ? 9.684   -63.400  29.620  1.00 114.29 ? 280 GLN   B CB     1 
ATOM   5557  C  CG     . GLN   B 2  280 ? 10.272  -62.137  28.936  1.00 119.44 ? 280 GLN   B CG     1 
ATOM   5558  C  CD     . GLN   B 2  280 ? 9.387   -61.545  27.837  1.00 126.88 ? 280 GLN   B CD     1 
ATOM   5559  O  OE1    . GLN   B 2  280 ? 8.157   -61.573  27.927  1.00 132.56 ? 280 GLN   B OE1    1 
ATOM   5560  N  NE2    . GLN   B 2  280 ? 10.018  -60.988  26.799  1.00 123.85 ? 280 GLN   B NE2    1 
ATOM   5561  N  N      . TYR   B 2  281 ? 10.449  -66.503  29.969  1.00 94.83  ? 281 TYR   B N      1 
ATOM   5562  C  CA     . TYR   B 2  281 ? 10.515  -67.935  30.239  1.00 86.17  ? 281 TYR   B CA     1 
ATOM   5563  C  C      . TYR   B 2  281 ? 10.509  -68.323  31.713  1.00 82.55  ? 281 TYR   B C      1 
ATOM   5564  O  O      . TYR   B 2  281 ? 10.388  -69.520  32.009  1.00 81.22  ? 281 TYR   B O      1 
ATOM   5565  C  CB     . TYR   B 2  281 ? 11.763  -68.536  29.562  1.00 86.25  ? 281 TYR   B CB     1 
ATOM   5566  C  CG     . TYR   B 2  281 ? 11.996  -68.048  28.139  1.00 85.41  ? 281 TYR   B CG     1 
ATOM   5567  C  CD1    . TYR   B 2  281 ? 11.306  -68.622  27.070  1.00 85.23  ? 281 TYR   B CD1    1 
ATOM   5568  C  CD2    . TYR   B 2  281 ? 12.884  -67.013  27.867  1.00 76.80  ? 281 TYR   B CD2    1 
ATOM   5569  C  CE1    . TYR   B 2  281 ? 11.499  -68.190  25.774  1.00 83.28  ? 281 TYR   B CE1    1 
ATOM   5570  C  CE2    . TYR   B 2  281 ? 13.082  -66.569  26.573  1.00 82.07  ? 281 TYR   B CE2    1 
ATOM   5571  C  CZ     . TYR   B 2  281 ? 12.384  -67.162  25.528  1.00 89.34  ? 281 TYR   B CZ     1 
ATOM   5572  O  OH     . TYR   B 2  281 ? 12.574  -66.735  24.230  1.00 87.96  ? 281 TYR   B OH     1 
ATOM   5573  N  N      . ARG   B 2  282 ? 10.628  -67.374  32.642  1.00 77.36  ? 282 ARG   B N      1 
ATOM   5574  C  CA     . ARG   B 2  282 ? 10.512  -67.682  34.065  1.00 69.64  ? 282 ARG   B CA     1 
ATOM   5575  C  C      . ARG   B 2  282 ? 9.080   -67.458  34.518  1.00 72.33  ? 282 ARG   B C      1 
ATOM   5576  O  O      . ARG   B 2  282 ? 8.512   -66.384  34.288  1.00 73.94  ? 282 ARG   B O      1 
ATOM   5577  C  CB     . ARG   B 2  282 ? 11.452  -66.819  34.906  1.00 75.03  ? 282 ARG   B CB     1 
ATOM   5578  N  N      . ALA   B 2  283 ? 8.496   -68.466  35.158  1.00 70.16  ? 283 ALA   B N      1 
ATOM   5579  C  CA     . ALA   B 2  283 ? 7.168   -68.280  35.710  1.00 60.16  ? 283 ALA   B CA     1 
ATOM   5580  C  C      . ALA   B 2  283 ? 7.236   -67.353  36.915  1.00 57.05  ? 283 ALA   B C      1 
ATOM   5581  O  O      . ALA   B 2  283 ? 8.297   -67.135  37.511  1.00 53.59  ? 283 ALA   B O      1 
ATOM   5582  C  CB     . ALA   B 2  283 ? 6.544   -69.615  36.103  1.00 56.13  ? 283 ALA   B CB     1 
ATOM   5583  N  N      . LEU   B 2  284 ? 6.093   -66.771  37.252  1.00 58.11  ? 284 LEU   B N      1 
ATOM   5584  C  CA     . LEU   B 2  284 ? 6.069   -65.975  38.461  1.00 57.44  ? 284 LEU   B CA     1 
ATOM   5585  C  C      . LEU   B 2  284 ? 5.920   -66.879  39.667  1.00 60.13  ? 284 LEU   B C      1 
ATOM   5586  O  O      . LEU   B 2  284 ? 5.498   -68.035  39.570  1.00 63.37  ? 284 LEU   B O      1 
ATOM   5587  C  CB     . LEU   B 2  284 ? 4.944   -64.946  38.436  1.00 57.10  ? 284 LEU   B CB     1 
ATOM   5588  C  CG     . LEU   B 2  284 ? 5.125   -63.860  37.382  1.00 58.27  ? 284 LEU   B CG     1 
ATOM   5589  C  CD1    . LEU   B 2  284 ? 4.908   -64.491  36.006  1.00 64.68  ? 284 LEU   B CD1    1 
ATOM   5590  C  CD2    . LEU   B 2  284 ? 4.210   -62.643  37.599  1.00 47.88  ? 284 LEU   B CD2    1 
ATOM   5591  N  N      . THR   B 2  285 ? 6.326   -66.351  40.807  1.00 57.79  ? 285 THR   B N      1 
ATOM   5592  C  CA     . THR   B 2  285 ? 6.035   -66.973  42.080  1.00 58.24  ? 285 THR   B CA     1 
ATOM   5593  C  C      . THR   B 2  285 ? 4.721   -66.416  42.617  1.00 57.67  ? 285 THR   B C      1 
ATOM   5594  O  O      . THR   B 2  285 ? 4.457   -65.212  42.516  1.00 55.87  ? 285 THR   B O      1 
ATOM   5595  C  CB     . THR   B 2  285 ? 7.182   -66.729  43.057  1.00 56.35  ? 285 THR   B CB     1 
ATOM   5596  O  OG1    . THR   B 2  285 ? 7.209   -65.346  43.431  1.00 59.32  ? 285 THR   B OG1    1 
ATOM   5597  C  CG2    . THR   B 2  285 ? 8.485   -67.082  42.402  1.00 57.90  ? 285 THR   B CG2    1 
ATOM   5598  N  N      . VAL   B 2  286 ? 3.888   -67.303  43.155  1.00 55.59  ? 286 VAL   B N      1 
ATOM   5599  C  CA     . VAL   B 2  286 ? 2.567   -66.938  43.659  1.00 55.89  ? 286 VAL   B CA     1 
ATOM   5600  C  C      . VAL   B 2  286 ? 2.622   -65.587  44.363  1.00 57.02  ? 286 VAL   B C      1 
ATOM   5601  O  O      . VAL   B 2  286 ? 1.743   -64.744  44.137  1.00 60.49  ? 286 VAL   B O      1 
ATOM   5602  C  CB     . VAL   B 2  286 ? 2.004   -68.019  44.588  1.00 57.12  ? 286 VAL   B CB     1 
ATOM   5603  C  CG1    . VAL   B 2  286 ? 0.708   -67.542  45.209  1.00 53.29  ? 286 VAL   B CG1    1 
ATOM   5604  C  CG2    . VAL   B 2  286 ? 1.780   -69.305  43.798  1.00 62.50  ? 286 VAL   B CG2    1 
ATOM   5605  N  N      . PRO   B 2  287 ? 3.614   -65.325  45.207  1.00 54.94  ? 287 PRO   B N      1 
ATOM   5606  C  CA     . PRO   B 2  287 ? 3.770   -63.955  45.716  1.00 60.00  ? 287 PRO   B CA     1 
ATOM   5607  C  C      . PRO   B 2  287 ? 3.779   -62.907  44.622  1.00 59.56  ? 287 PRO   B C      1 
ATOM   5608  O  O      . PRO   B 2  287 ? 3.199   -61.831  44.813  1.00 60.30  ? 287 PRO   B O      1 
ATOM   5609  C  CB     . PRO   B 2  287 ? 5.103   -64.018  46.470  1.00 54.28  ? 287 PRO   B CB     1 
ATOM   5610  C  CG     . PRO   B 2  287 ? 5.172   -65.428  46.915  1.00 54.46  ? 287 PRO   B CG     1 
ATOM   5611  C  CD     . PRO   B 2  287 ? 4.585   -66.246  45.809  1.00 53.86  ? 287 PRO   B CD     1 
ATOM   5612  N  N      . GLU   B 2  288 ? 4.405   -63.192  43.476  1.00 58.98  ? 288 GLU   B N      1 
ATOM   5613  C  CA     . GLU   B 2  288 ? 4.456   -62.201  42.402  1.00 57.66  ? 288 GLU   B CA     1 
ATOM   5614  C  C      . GLU   B 2  288 ? 3.086   -62.003  41.770  1.00 56.47  ? 288 GLU   B C      1 
ATOM   5615  O  O      . GLU   B 2  288 ? 2.604   -60.868  41.649  1.00 55.08  ? 288 GLU   B O      1 
ATOM   5616  C  CB     . GLU   B 2  288 ? 5.489   -62.606  41.348  1.00 57.69  ? 288 GLU   B CB     1 
ATOM   5617  C  CG     . GLU   B 2  288 ? 6.897   -62.247  41.798  1.00 66.91  ? 288 GLU   B CG     1 
ATOM   5618  C  CD     . GLU   B 2  288 ? 8.032   -62.985  41.089  1.00 67.17  ? 288 GLU   B CD     1 
ATOM   5619  O  OE1    . GLU   B 2  288 ? 7.817   -64.038  40.420  1.00 61.13  ? 288 GLU   B OE1    1 
ATOM   5620  O  OE2    . GLU   B 2  288 ? 9.173   -62.508  41.284  1.00 61.83  ? 288 GLU   B OE2    1 
ATOM   5621  N  N      . LEU   B 2  289 ? 2.437   -63.100  41.375  1.00 54.44  ? 289 LEU   B N      1 
ATOM   5622  C  CA     . LEU   B 2  289 ? 1.109   -62.990  40.788  1.00 53.26  ? 289 LEU   B CA     1 
ATOM   5623  C  C      . LEU   B 2  289 ? 0.229   -62.072  41.625  1.00 51.64  ? 289 LEU   B C      1 
ATOM   5624  O  O      . LEU   B 2  289 ? -0.429  -61.177  41.093  1.00 53.94  ? 289 LEU   B O      1 
ATOM   5625  C  CB     . LEU   B 2  289 ? 0.476   -64.375  40.661  1.00 49.49  ? 289 LEU   B CB     1 
ATOM   5626  C  CG     . LEU   B 2  289 ? 0.989   -65.287  39.540  1.00 46.80  ? 289 LEU   B CG     1 
ATOM   5627  C  CD1    . LEU   B 2  289 ? 0.310   -66.638  39.610  1.00 49.39  ? 289 LEU   B CD1    1 
ATOM   5628  C  CD2    . LEU   B 2  289 ? 0.905   -64.681  38.158  1.00 48.48  ? 289 LEU   B CD2    1 
ATOM   5629  N  N      . THR   B 2  290 ? 0.250   -62.254  42.945  1.00 51.27  ? 290 THR   B N      1 
ATOM   5630  C  CA     . THR   B 2  290 ? -0.634  -61.520  43.844  1.00 54.61  ? 290 THR   B CA     1 
ATOM   5631  C  C      . THR   B 2  290 ? -0.382  -60.013  43.805  1.00 54.65  ? 290 THR   B C      1 
ATOM   5632  O  O      . THR   B 2  290 ? -1.306  -59.233  43.575  1.00 58.09  ? 290 THR   B O      1 
ATOM   5633  C  CB     . THR   B 2  290 ? -0.489  -62.078  45.271  1.00 59.18  ? 290 THR   B CB     1 
ATOM   5634  O  OG1    . THR   B 2  290 ? -0.881  -63.462  45.297  1.00 51.70  ? 290 THR   B OG1    1 
ATOM   5635  C  CG2    . THR   B 2  290 ? -1.326  -61.295  46.265  1.00 62.14  ? 290 THR   B CG2    1 
ATOM   5636  N  N      . GLN   B 2  291 ? 0.846   -59.568  44.061  1.00 57.36  ? 291 GLN   B N      1 
ATOM   5637  C  CA     . GLN   B 2  291 ? 1.045   -58.124  44.064  1.00 61.24  ? 291 GLN   B CA     1 
ATOM   5638  C  C      . GLN   B 2  291 ? 0.946   -57.486  42.690  1.00 65.76  ? 291 GLN   B C      1 
ATOM   5639  O  O      . GLN   B 2  291 ? 0.680   -56.282  42.615  1.00 70.52  ? 291 GLN   B O      1 
ATOM   5640  C  CB     . GLN   B 2  291 ? 2.363   -57.716  44.718  1.00 71.50  ? 291 GLN   B CB     1 
ATOM   5641  C  CG     . GLN   B 2  291 ? 2.532   -56.184  44.628  1.00 88.16  ? 291 GLN   B CG     1 
ATOM   5642  C  CD     . GLN   B 2  291 ? 1.552   -55.355  45.491  1.00 93.19  ? 291 GLN   B CD     1 
ATOM   5643  O  OE1    . GLN   B 2  291 ? 1.112   -55.772  46.573  1.00 94.31  ? 291 GLN   B OE1    1 
ATOM   5644  N  NE2    . GLN   B 2  291 ? 1.171   -54.190  44.965  1.00 89.06  ? 291 GLN   B NE2    1 
ATOM   5645  N  N      . GLN   B 2  292 ? 1.132   -58.238  41.609  1.00 60.64  ? 292 GLN   B N      1 
ATOM   5646  C  CA     . GLN   B 2  292 ? 0.884   -57.649  40.297  1.00 56.51  ? 292 GLN   B CA     1 
ATOM   5647  C  C      . GLN   B 2  292 ? -0.612  -57.474  40.059  1.00 56.87  ? 292 GLN   B C      1 
ATOM   5648  O  O      . GLN   B 2  292 ? -1.081  -56.361  39.786  1.00 58.87  ? 292 GLN   B O      1 
ATOM   5649  C  CB     . GLN   B 2  292 ? 1.519   -58.501  39.203  1.00 50.15  ? 292 GLN   B CB     1 
ATOM   5650  C  CG     . GLN   B 2  292 ? 3.015   -58.661  39.425  1.00 51.34  ? 292 GLN   B CG     1 
ATOM   5651  C  CD     . GLN   B 2  292 ? 3.767   -59.074  38.188  1.00 55.99  ? 292 GLN   B CD     1 
ATOM   5652  O  OE1    . GLN   B 2  292 ? 3.287   -58.911  37.067  1.00 68.98  ? 292 GLN   B OE1    1 
ATOM   5653  N  NE2    . GLN   B 2  292 ? 4.939   -59.651  38.382  1.00 51.00  ? 292 GLN   B NE2    1 
ATOM   5654  N  N      . MET   B 2  293 ? -1.385  -58.556  40.220  1.00 57.08  ? 293 MET   B N      1 
ATOM   5655  C  CA     . MET   B 2  293 ? -2.822  -58.516  39.966  1.00 55.66  ? 293 MET   B CA     1 
ATOM   5656  C  C      . MET   B 2  293 ? -3.515  -57.423  40.772  1.00 58.75  ? 293 MET   B C      1 
ATOM   5657  O  O      . MET   B 2  293 ? -4.523  -56.863  40.320  1.00 61.39  ? 293 MET   B O      1 
ATOM   5658  C  CB     . MET   B 2  293 ? -3.446  -59.869  40.282  1.00 49.69  ? 293 MET   B CB     1 
ATOM   5659  C  CG     . MET   B 2  293 ? -3.845  -60.002  41.732  1.00 56.94  ? 293 MET   B CG     1 
ATOM   5660  S  SD     . MET   B 2  293 ? -4.512  -61.651  42.021  1.00 72.92  ? 293 MET   B SD     1 
ATOM   5661  C  CE     . MET   B 2  293 ? -5.492  -61.881  40.535  1.00 49.36  ? 293 MET   B CE     1 
ATOM   5662  N  N      . PHE   B 2  294 ? -3.009  -57.102  41.957  1.00 53.44  ? 294 PHE   B N      1 
ATOM   5663  C  CA     . PHE   B 2  294 ? -3.566  -55.967  42.669  1.00 52.52  ? 294 PHE   B CA     1 
ATOM   5664  C  C      . PHE   B 2  294 ? -2.915  -54.656  42.310  1.00 55.23  ? 294 PHE   B C      1 
ATOM   5665  O  O      . PHE   B 2  294 ? -3.362  -53.619  42.808  1.00 62.60  ? 294 PHE   B O      1 
ATOM   5666  C  CB     . PHE   B 2  294 ? -3.452  -56.146  44.168  1.00 58.17  ? 294 PHE   B CB     1 
ATOM   5667  C  CG     . PHE   B 2  294 ? -4.492  -57.028  44.739  1.00 57.57  ? 294 PHE   B CG     1 
ATOM   5668  C  CD1    . PHE   B 2  294 ? -4.353  -58.395  44.698  1.00 60.37  ? 294 PHE   B CD1    1 
ATOM   5669  C  CD2    . PHE   B 2  294 ? -5.632  -56.486  45.296  1.00 56.93  ? 294 PHE   B CD2    1 
ATOM   5670  C  CE1    . PHE   B 2  294 ? -5.318  -59.205  45.232  1.00 64.24  ? 294 PHE   B CE1    1 
ATOM   5671  C  CE2    . PHE   B 2  294 ? -6.606  -57.290  45.826  1.00 54.44  ? 294 PHE   B CE2    1 
ATOM   5672  C  CZ     . PHE   B 2  294 ? -6.452  -58.651  45.797  1.00 58.97  ? 294 PHE   B CZ     1 
ATOM   5673  N  N      . ASP   B 2  295 ? -1.873  -54.681  41.487  1.00 57.02  ? 295 ASP   B N      1 
ATOM   5674  C  CA     . ASP   B 2  295 ? -1.141  -53.473  41.131  1.00 62.48  ? 295 ASP   B CA     1 
ATOM   5675  C  C      . ASP   B 2  295 ? -1.908  -52.710  40.066  1.00 57.23  ? 295 ASP   B C      1 
ATOM   5676  O  O      . ASP   B 2  295 ? -2.351  -53.302  39.077  1.00 53.07  ? 295 ASP   B O      1 
ATOM   5677  C  CB     . ASP   B 2  295 ? 0.250   -53.831  40.610  1.00 62.50  ? 295 ASP   B CB     1 
ATOM   5678  C  CG     . ASP   B 2  295 ? 1.126   -52.617  40.409  1.00 65.15  ? 295 ASP   B CG     1 
ATOM   5679  O  OD1    . ASP   B 2  295 ? 0.705   -51.495  40.788  1.00 62.99  ? 295 ASP   B OD1    1 
ATOM   5680  O  OD2    . ASP   B 2  295 ? 2.244   -52.804  39.882  1.00 67.87  ? 295 ASP   B OD2    1 
ATOM   5681  N  N      . SER   B 2  296 ? -2.052  -51.393  40.256  1.00 56.06  ? 296 SER   B N      1 
ATOM   5682  C  CA     . SER   B 2  296 ? -2.873  -50.628  39.324  1.00 52.69  ? 296 SER   B CA     1 
ATOM   5683  C  C      . SER   B 2  296 ? -2.301  -50.684  37.913  1.00 49.36  ? 296 SER   B C      1 
ATOM   5684  O  O      . SER   B 2  296 ? -3.046  -50.543  36.941  1.00 52.93  ? 296 SER   B O      1 
ATOM   5685  C  CB     . SER   B 2  296 ? -3.013  -49.186  39.797  1.00 50.56  ? 296 SER   B CB     1 
ATOM   5686  O  OG     . SER   B 2  296 ? -1.899  -48.418  39.390  1.00 65.73  ? 296 SER   B OG     1 
ATOM   5687  N  N      . LYS   B 2  297 ? -0.987  -50.892  37.785  1.00 46.23  ? 297 LYS   B N      1 
ATOM   5688  C  CA     . LYS   B 2  297 ? -0.334  -51.115  36.498  1.00 51.23  ? 297 LYS   B CA     1 
ATOM   5689  C  C      . LYS   B 2  297 ? -0.854  -52.360  35.773  1.00 53.98  ? 297 LYS   B C      1 
ATOM   5690  O  O      . LYS   B 2  297 ? -0.511  -52.576  34.602  1.00 48.40  ? 297 LYS   B O      1 
ATOM   5691  C  CB     . LYS   B 2  297 ? 1.166   -51.268  36.715  1.00 53.50  ? 297 LYS   B CB     1 
ATOM   5692  C  CG     . LYS   B 2  297 ? 1.889   -50.043  37.216  1.00 51.98  ? 297 LYS   B CG     1 
ATOM   5693  C  CD     . LYS   B 2  297 ? 3.388   -50.323  37.207  1.00 54.12  ? 297 LYS   B CD     1 
ATOM   5694  C  CE     . LYS   B 2  297 ? 4.023   -49.923  38.524  1.00 59.84  ? 297 LYS   B CE     1 
ATOM   5695  N  NZ     . LYS   B 2  297 ? 3.894   -48.452  38.735  1.00 64.81  ? 297 LYS   B NZ     1 
ATOM   5696  N  N      . ASN   B 2  298 ? -1.624  -53.204  36.460  1.00 57.23  ? 298 ASN   B N      1 
ATOM   5697  C  CA     . ASN   B 2  298 ? -2.221  -54.411  35.902  1.00 53.06  ? 298 ASN   B CA     1 
ATOM   5698  C  C      . ASN   B 2  298 ? -3.734  -54.278  35.772  1.00 55.08  ? 298 ASN   B C      1 
ATOM   5699  O  O      . ASN   B 2  298 ? -4.401  -55.235  35.354  1.00 53.22  ? 298 ASN   B O      1 
ATOM   5700  C  CB     . ASN   B 2  298 ? -1.894  -55.623  36.786  1.00 52.26  ? 298 ASN   B CB     1 
ATOM   5701  C  CG     . ASN   B 2  298 ? -0.437  -56.025  36.732  1.00 53.25  ? 298 ASN   B CG     1 
ATOM   5702  O  OD1    . ASN   B 2  298 ? 0.451   -55.248  37.096  1.00 53.94  ? 298 ASN   B OD1    1 
ATOM   5703  N  ND2    . ASN   B 2  298 ? -0.183  -57.262  36.330  1.00 54.76  ? 298 ASN   B ND2    1 
ATOM   5704  N  N      . MET   B 2  299 ? -4.287  -53.117  36.134  1.00 49.24  ? 299 MET   B N      1 
ATOM   5705  C  CA     . MET   B 2  299 ? -5.705  -52.832  35.984  1.00 45.39  ? 299 MET   B CA     1 
ATOM   5706  C  C      . MET   B 2  299 ? -6.020  -52.466  34.535  1.00 47.11  ? 299 MET   B C      1 
ATOM   5707  O  O      . MET   B 2  299 ? -5.309  -51.661  33.930  1.00 50.03  ? 299 MET   B O      1 
ATOM   5708  C  CB     . MET   B 2  299 ? -6.097  -51.690  36.922  1.00 48.62  ? 299 MET   B CB     1 
ATOM   5709  C  CG     . MET   B 2  299 ? -5.948  -52.028  38.417  1.00 52.04  ? 299 MET   B CG     1 
ATOM   5710  S  SD     . MET   B 2  299 ? -6.606  -53.670  38.822  1.00 57.89  ? 299 MET   B SD     1 
ATOM   5711  C  CE     . MET   B 2  299 ? -6.206  -53.830  40.558  1.00 54.06  ? 299 MET   B CE     1 
ATOM   5712  N  N      . MET   B 2  300 ? -7.090  -53.053  33.980  1.00 44.42  ? 300 MET   B N      1 
ATOM   5713  C  CA     . MET   B 2  300 ? -7.546  -52.732  32.628  1.00 42.68  ? 300 MET   B CA     1 
ATOM   5714  C  C      . MET   B 2  300 ? -8.553  -51.582  32.562  1.00 43.72  ? 300 MET   B C      1 
ATOM   5715  O  O      . MET   B 2  300 ? -9.115  -51.345  31.491  1.00 46.45  ? 300 MET   B O      1 
ATOM   5716  C  CB     . MET   B 2  300 ? -8.198  -53.939  31.965  1.00 42.00  ? 300 MET   B CB     1 
ATOM   5717  C  CG     . MET   B 2  300 ? -7.405  -55.204  32.017  1.00 48.69  ? 300 MET   B CG     1 
ATOM   5718  S  SD     . MET   B 2  300 ? -5.990  -55.106  30.938  1.00 59.29  ? 300 MET   B SD     1 
ATOM   5719  C  CE     . MET   B 2  300 ? -5.064  -56.552  31.414  1.00 48.37  ? 300 MET   B CE     1 
ATOM   5720  N  N      . ALA   B 2  301 ? -8.832  -50.898  33.669  1.00 44.27  ? 301 ALA   B N      1 
ATOM   5721  C  CA     . ALA   B 2  301 ? -9.671  -49.706  33.697  1.00 42.29  ? 301 ALA   B CA     1 
ATOM   5722  C  C      . ALA   B 2  301 ? -8.891  -48.636  34.442  1.00 48.01  ? 301 ALA   B C      1 
ATOM   5723  O  O      . ALA   B 2  301 ? -8.546  -48.811  35.622  1.00 43.99  ? 301 ALA   B O      1 
ATOM   5724  C  CB     . ALA   B 2  301 ? -11.024 -49.966  34.370  1.00 35.34  ? 301 ALA   B CB     1 
ATOM   5725  N  N      . ALA   B 2  302 ? -8.594  -47.543  33.748  1.00 41.24  ? 302 ALA   B N      1 
ATOM   5726  C  CA     . ALA   B 2  302 ? -7.572  -46.617  34.213  1.00 34.65  ? 302 ALA   B CA     1 
ATOM   5727  C  C      . ALA   B 2  302 ? -8.124  -45.879  35.423  1.00 42.84  ? 302 ALA   B C      1 
ATOM   5728  O  O      . ALA   B 2  302 ? -8.576  -44.734  35.340  1.00 47.38  ? 302 ALA   B O      1 
ATOM   5729  C  CB     . ALA   B 2  302 ? -7.155  -45.669  33.109  1.00 39.80  ? 302 ALA   B CB     1 
ATOM   5730  N  N      . CYS   B 2  303 ? -8.075  -46.570  36.571  1.00 47.89  ? 303 CYS   B N      1 
ATOM   5731  C  CA     . CYS   B 2  303 ? -8.404  -46.026  37.883  1.00 46.28  ? 303 CYS   B CA     1 
ATOM   5732  C  C      . CYS   B 2  303 ? -7.332  -46.437  38.877  1.00 50.82  ? 303 CYS   B C      1 
ATOM   5733  O  O      . CYS   B 2  303 ? -6.648  -47.443  38.704  1.00 55.61  ? 303 CYS   B O      1 
ATOM   5734  C  CB     . CYS   B 2  303 ? -9.753  -46.520  38.379  1.00 50.15  ? 303 CYS   B CB     1 
ATOM   5735  S  SG     . CYS   B 2  303 ? -11.046 -46.187  37.205  1.00 60.71  ? 303 CYS   B SG     1 
ATOM   5736  N  N      . ASP   B 2  304 ? -7.209  -45.641  39.925  1.00 53.23  ? 304 ASP   B N      1 
ATOM   5737  C  CA     . ASP   B 2  304 ? -6.295  -45.906  41.010  1.00 56.11  ? 304 ASP   B CA     1 
ATOM   5738  C  C      . ASP   B 2  304 ? -7.073  -46.626  42.095  1.00 62.01  ? 304 ASP   B C      1 
ATOM   5739  O  O      . ASP   B 2  304 ? -7.998  -46.026  42.678  1.00 58.98  ? 304 ASP   B O      1 
ATOM   5740  C  CB     . ASP   B 2  304 ? -5.738  -44.599  41.553  1.00 62.86  ? 304 ASP   B CB     1 
ATOM   5741  C  CG     . ASP   B 2  304 ? -4.596  -44.800  42.532  1.00 67.55  ? 304 ASP   B CG     1 
ATOM   5742  O  OD1    . ASP   B 2  304 ? -4.513  -45.875  43.171  1.00 68.94  ? 304 ASP   B OD1    1 
ATOM   5743  O  OD2    . ASP   B 2  304 ? -3.828  -43.835  42.718  1.00 69.50  ? 304 ASP   B OD2    1 
ATOM   5744  N  N      . PRO   B 2  305 ? -6.760  -47.884  42.405  1.00 53.41  ? 305 PRO   B N      1 
ATOM   5745  C  CA     . PRO   B 2  305 ? -7.570  -48.607  43.384  1.00 46.35  ? 305 PRO   B CA     1 
ATOM   5746  C  C      . PRO   B 2  305 ? -7.453  -48.022  44.759  1.00 56.99  ? 305 PRO   B C      1 
ATOM   5747  O  O      . PRO   B 2  305 ? -8.365  -48.227  45.570  1.00 57.05  ? 305 PRO   B O      1 
ATOM   5748  C  CB     . PRO   B 2  305 ? -7.007  -50.024  43.325  1.00 44.86  ? 305 PRO   B CB     1 
ATOM   5749  C  CG     . PRO   B 2  305 ? -6.258  -50.085  42.035  1.00 50.98  ? 305 PRO   B CG     1 
ATOM   5750  C  CD     . PRO   B 2  305 ? -5.710  -48.722  41.826  1.00 51.05  ? 305 PRO   B CD     1 
ATOM   5751  N  N      . ARG   B 2  306 ? -6.350  -47.303  45.036  1.00 61.13  ? 306 ARG   B N      1 
ATOM   5752  C  CA     . ARG   B 2  306 ? -6.078  -46.595  46.289  1.00 59.44  ? 306 ARG   B CA     1 
ATOM   5753  C  C      . ARG   B 2  306 ? -6.881  -45.310  46.434  1.00 58.26  ? 306 ARG   B C      1 
ATOM   5754  O  O      . ARG   B 2  306 ? -6.918  -44.734  47.526  1.00 53.45  ? 306 ARG   B O      1 
ATOM   5755  C  CB     . ARG   B 2  306 ? -4.586  -46.277  46.390  1.00 56.62  ? 306 ARG   B CB     1 
ATOM   5756  C  CG     . ARG   B 2  306 ? -3.746  -47.462  46.779  1.00 59.51  ? 306 ARG   B CG     1 
ATOM   5757  C  CD     . ARG   B 2  306 ? -2.291  -47.099  47.004  1.00 60.93  ? 306 ARG   B CD     1 
ATOM   5758  N  NE     . ARG   B 2  306 ? -1.591  -48.242  47.571  1.00 59.96  ? 306 ARG   B NE     1 
ATOM   5759  C  CZ     . ARG   B 2  306 ? -1.171  -48.302  48.826  1.00 66.00  ? 306 ARG   B CZ     1 
ATOM   5760  N  NH1    . ARG   B 2  306 ? -1.319  -47.280  49.653  1.00 78.49  ? 306 ARG   B NH1    1 
ATOM   5761  N  NH2    . ARG   B 2  306 ? -0.611  -49.423  49.273  1.00 68.30  ? 306 ARG   B NH2    1 
ATOM   5762  N  N      . HIS   B 2  307 ? -7.495  -44.837  45.359  1.00 61.83  ? 307 HIS   B N      1 
ATOM   5763  C  CA     . HIS   B 2  307 ? -8.441  -43.740  45.405  1.00 55.98  ? 307 HIS   B CA     1 
ATOM   5764  C  C      . HIS   B 2  307 ? -9.837  -44.224  45.749  1.00 61.44  ? 307 HIS   B C      1 
ATOM   5765  O  O      . HIS   B 2  307 ? -10.768 -43.416  45.765  1.00 65.45  ? 307 HIS   B O      1 
ATOM   5766  C  CB     . HIS   B 2  307 ? -8.454  -43.038  44.053  1.00 62.93  ? 307 HIS   B CB     1 
ATOM   5767  C  CG     . HIS   B 2  307 ? -7.126  -42.474  43.652  1.00 70.15  ? 307 HIS   B CG     1 
ATOM   5768  N  ND1    . HIS   B 2  307 ? -6.920  -41.853  42.439  1.00 71.92  ? 307 HIS   B ND1    1 
ATOM   5769  C  CD2    . HIS   B 2  307 ? -5.941  -42.423  44.306  1.00 67.11  ? 307 HIS   B CD2    1 
ATOM   5770  C  CE1    . HIS   B 2  307 ? -5.659  -41.467  42.354  1.00 73.69  ? 307 HIS   B CE1    1 
ATOM   5771  N  NE2    . HIS   B 2  307 ? -5.045  -41.798  43.475  1.00 70.58  ? 307 HIS   B NE2    1 
ATOM   5772  N  N      . GLY   B 2  308 ? -10.001 -45.521  46.019  1.00 60.63  ? 308 GLY   B N      1 
ATOM   5773  C  CA     . GLY   B 2  308 ? -11.286 -46.086  46.370  1.00 58.22  ? 308 GLY   B CA     1 
ATOM   5774  C  C      . GLY   B 2  308 ? -11.166 -47.278  47.297  1.00 59.20  ? 308 GLY   B C      1 
ATOM   5775  O  O      . GLY   B 2  308 ? -10.070 -47.697  47.673  1.00 65.37  ? 308 GLY   B O      1 
ATOM   5776  N  N      . ARG   B 2  309 ? -12.320 -47.833  47.654  1.00 51.69  ? 309 ARG   B N      1 
ATOM   5777  C  CA     . ARG   B 2  309 ? -12.406 -49.046  48.452  1.00 50.52  ? 309 ARG   B CA     1 
ATOM   5778  C  C      . ARG   B 2  309 ? -13.002 -50.173  47.610  1.00 49.43  ? 309 ARG   B C      1 
ATOM   5779  O  O      . ARG   B 2  309 ? -13.831 -49.938  46.729  1.00 46.32  ? 309 ARG   B O      1 
ATOM   5780  C  CB     . ARG   B 2  309 ? -13.228 -48.782  49.717  1.00 52.16  ? 309 ARG   B CB     1 
ATOM   5781  C  CG     . ARG   B 2  309 ? -12.468 -47.934  50.730  1.00 57.73  ? 309 ARG   B CG     1 
ATOM   5782  C  CD     . ARG   B 2  309 ? -13.322 -47.396  51.862  1.00 57.98  ? 309 ARG   B CD     1 
ATOM   5783  N  NE     . ARG   B 2  309 ? -13.913 -48.426  52.705  1.00 59.73  ? 309 ARG   B NE     1 
ATOM   5784  C  CZ     . ARG   B 2  309 ? -13.423 -48.833  53.868  1.00 58.79  ? 309 ARG   B CZ     1 
ATOM   5785  N  NH1    . ARG   B 2  309 ? -12.268 -48.378  54.327  1.00 57.48  ? 309 ARG   B NH1    1 
ATOM   5786  N  NH2    . ARG   B 2  309 ? -14.124 -49.701  54.602  1.00 54.60  ? 309 ARG   B NH2    1 
ATOM   5787  N  N      . TYR   B 2  310 ? -12.550 -51.397  47.858  1.00 49.03  ? 310 TYR   B N      1 
ATOM   5788  C  CA     . TYR   B 2  310 ? -13.102 -52.573  47.198  1.00 43.46  ? 310 TYR   B CA     1 
ATOM   5789  C  C      . TYR   B 2  310 ? -14.368 -53.020  47.914  1.00 43.44  ? 310 TYR   B C      1 
ATOM   5790  O  O      . TYR   B 2  310 ? -14.321 -53.453  49.070  1.00 47.41  ? 310 TYR   B O      1 
ATOM   5791  C  CB     . TYR   B 2  310 ? -12.067 -53.692  47.177  1.00 45.75  ? 310 TYR   B CB     1 
ATOM   5792  C  CG     . TYR   B 2  310 ? -10.960 -53.524  46.174  1.00 43.55  ? 310 TYR   B CG     1 
ATOM   5793  C  CD1    . TYR   B 2  310 ? -11.189 -53.744  44.829  1.00 41.56  ? 310 TYR   B CD1    1 
ATOM   5794  C  CD2    . TYR   B 2  310 ? -9.708  -53.100  46.562  1.00 44.32  ? 310 TYR   B CD2    1 
ATOM   5795  C  CE1    . TYR   B 2  310 ? -10.180 -53.596  43.897  1.00 43.68  ? 310 TYR   B CE1    1 
ATOM   5796  C  CE2    . TYR   B 2  310 ? -8.701  -52.931  45.645  1.00 51.80  ? 310 TYR   B CE2    1 
ATOM   5797  C  CZ     . TYR   B 2  310 ? -8.937  -53.180  44.304  1.00 52.52  ? 310 TYR   B CZ     1 
ATOM   5798  O  OH     . TYR   B 2  310 ? -7.923  -53.018  43.376  1.00 52.18  ? 310 TYR   B OH     1 
ATOM   5799  N  N      . LEU   B 2  311 ? -15.502 -52.912  47.232  1.00 41.61  ? 311 LEU   B N      1 
ATOM   5800  C  CA     . LEU   B 2  311 ? -16.715 -53.523  47.751  1.00 41.11  ? 311 LEU   B CA     1 
ATOM   5801  C  C      . LEU   B 2  311 ? -16.611 -55.046  47.745  1.00 40.71  ? 311 LEU   B C      1 
ATOM   5802  O  O      . LEU   B 2  311 ? -16.922 -55.698  48.746  1.00 44.09  ? 311 LEU   B O      1 
ATOM   5803  C  CB     . LEU   B 2  311 ? -17.921 -53.075  46.941  1.00 37.67  ? 311 LEU   B CB     1 
ATOM   5804  C  CG     . LEU   B 2  311 ? -18.146 -51.596  46.925  1.00 34.31  ? 311 LEU   B CG     1 
ATOM   5805  C  CD1    . LEU   B 2  311 ? -19.346 -51.359  46.070  1.00 33.80  ? 311 LEU   B CD1    1 
ATOM   5806  C  CD2    . LEU   B 2  311 ? -18.397 -51.233  48.329  1.00 40.77  ? 311 LEU   B CD2    1 
ATOM   5807  N  N      . THR   B 2  312 ? -16.214 -55.633  46.617  1.00 34.13  ? 312 THR   B N      1 
ATOM   5808  C  CA     . THR   B 2  312 ? -15.989 -57.070  46.547  1.00 37.71  ? 312 THR   B CA     1 
ATOM   5809  C  C      . THR   B 2  312 ? -14.873 -57.329  45.556  1.00 40.53  ? 312 THR   B C      1 
ATOM   5810  O  O      . THR   B 2  312 ? -14.631 -56.532  44.650  1.00 41.04  ? 312 THR   B O      1 
ATOM   5811  C  CB     . THR   B 2  312 ? -17.198 -57.858  46.065  1.00 41.51  ? 312 THR   B CB     1 
ATOM   5812  O  OG1    . THR   B 2  312 ? -17.587 -57.364  44.776  1.00 45.33  ? 312 THR   B OG1    1 
ATOM   5813  C  CG2    . THR   B 2  312 ? -18.350 -57.705  47.018  1.00 37.02  ? 312 THR   B CG2    1 
ATOM   5814  N  N      . VAL   B 2  313 ? -14.216 -58.470  45.714  1.00 37.74  ? 313 VAL   B N      1 
ATOM   5815  C  CA     . VAL   B 2  313 ? -13.108 -58.822  44.848  1.00 38.52  ? 313 VAL   B CA     1 
ATOM   5816  C  C      . VAL   B 2  313 ? -13.273 -60.289  44.488  1.00 41.28  ? 313 VAL   B C      1 
ATOM   5817  O  O      . VAL   B 2  313 ? -13.896 -61.060  45.225  1.00 41.26  ? 313 VAL   B O      1 
ATOM   5818  C  CB     . VAL   B 2  313 ? -11.733 -58.547  45.508  1.00 37.68  ? 313 VAL   B CB     1 
ATOM   5819  C  CG1    . VAL   B 2  313 ? -10.605 -58.938  44.566  1.00 38.21  ? 313 VAL   B CG1    1 
ATOM   5820  C  CG2    . VAL   B 2  313 ? -11.605 -57.103  45.973  1.00 36.83  ? 313 VAL   B CG2    1 
ATOM   5821  N  N      . ALA   B 2  314 ? -12.746 -60.662  43.323  1.00 36.83  ? 314 ALA   B N      1 
ATOM   5822  C  CA     . ALA   B 2  314 ? -12.765 -62.045  42.867  1.00 39.84  ? 314 ALA   B CA     1 
ATOM   5823  C  C      . ALA   B 2  314 ? -11.521 -62.256  42.030  1.00 49.23  ? 314 ALA   B C      1 
ATOM   5824  O  O      . ALA   B 2  314 ? -11.327 -61.539  41.043  1.00 53.00  ? 314 ALA   B O      1 
ATOM   5825  C  CB     . ALA   B 2  314 ? -14.002 -62.354  42.041  1.00 40.34  ? 314 ALA   B CB     1 
ATOM   5826  N  N      . ALA   B 2  315 ? -10.689 -63.222  42.426  1.00 50.01  ? 315 ALA   B N      1 
ATOM   5827  C  CA     . ALA   B 2  315 ? -9.419  -63.505  41.778  1.00 43.41  ? 315 ALA   B CA     1 
ATOM   5828  C  C      . ALA   B 2  315 ? -9.359  -64.977  41.412  1.00 47.52  ? 315 ALA   B C      1 
ATOM   5829  O  O      . ALA   B 2  315 ? -9.960  -65.829  42.071  1.00 48.11  ? 315 ALA   B O      1 
ATOM   5830  C  CB     . ALA   B 2  315 ? -8.231  -63.141  42.668  1.00 44.39  ? 315 ALA   B CB     1 
ATOM   5831  N  N      . ILE   B 2  316 ? -8.608  -65.261  40.355  1.00 47.15  ? 316 ILE   B N      1 
ATOM   5832  C  CA     . ILE   B 2  316 ? -8.578  -66.560  39.694  1.00 41.47  ? 316 ILE   B CA     1 
ATOM   5833  C  C      . ILE   B 2  316 ? -7.139  -66.866  39.354  1.00 43.40  ? 316 ILE   B C      1 
ATOM   5834  O  O      . ILE   B 2  316 ? -6.505  -66.097  38.627  1.00 45.66  ? 316 ILE   B O      1 
ATOM   5835  C  CB     . ILE   B 2  316 ? -9.436  -66.576  38.422  1.00 41.64  ? 316 ILE   B CB     1 
ATOM   5836  C  CG1    . ILE   B 2  316 ? -9.285  -67.900  37.701  1.00 46.08  ? 316 ILE   B CG1    1 
ATOM   5837  C  CG2    . ILE   B 2  316 ? -9.073  -65.441  37.527  1.00 48.69  ? 316 ILE   B CG2    1 
ATOM   5838  C  CD1    . ILE   B 2  316 ? -9.796  -69.042  38.516  1.00 55.38  ? 316 ILE   B CD1    1 
ATOM   5839  N  N      . PHE   B 2  317 ? -6.611  -67.966  39.887  1.00 46.06  ? 317 PHE   B N      1 
ATOM   5840  C  CA     . PHE   B 2  317 ? -5.212  -68.316  39.687  1.00 46.70  ? 317 PHE   B CA     1 
ATOM   5841  C  C      . PHE   B 2  317 ? -5.134  -69.523  38.762  1.00 49.85  ? 317 PHE   B C      1 
ATOM   5842  O  O      . PHE   B 2  317 ? -5.711  -70.578  39.055  1.00 53.13  ? 317 PHE   B O      1 
ATOM   5843  C  CB     . PHE   B 2  317 ? -4.504  -68.617  41.006  1.00 44.06  ? 317 PHE   B CB     1 
ATOM   5844  C  CG     . PHE   B 2  317 ? -4.258  -67.403  41.872  1.00 46.92  ? 317 PHE   B CG     1 
ATOM   5845  C  CD1    . PHE   B 2  317 ? -5.273  -66.859  42.645  1.00 43.93  ? 317 PHE   B CD1    1 
ATOM   5846  C  CD2    . PHE   B 2  317 ? -3.039  -66.760  41.845  1.00 44.38  ? 317 PHE   B CD2    1 
ATOM   5847  C  CE1    . PHE   B 2  317 ? -5.054  -65.765  43.439  1.00 42.65  ? 317 PHE   B CE1    1 
ATOM   5848  C  CE2    . PHE   B 2  317 ? -2.821  -65.645  42.622  1.00 46.58  ? 317 PHE   B CE2    1 
ATOM   5849  C  CZ     . PHE   B 2  317 ? -3.834  -65.138  43.414  1.00 45.82  ? 317 PHE   B CZ     1 
ATOM   5850  N  N      . ARG   B 2  318 ? -4.420  -69.375  37.652  1.00 45.32  ? 318 ARG   B N      1 
ATOM   5851  C  CA     . ARG   B 2  318 ? -4.302  -70.436  36.663  1.00 50.70  ? 318 ARG   B CA     1 
ATOM   5852  C  C      . ARG   B 2  318 ? -2.870  -70.942  36.604  1.00 56.59  ? 318 ARG   B C      1 
ATOM   5853  O  O      . ARG   B 2  318 ? -1.924  -70.150  36.611  1.00 56.40  ? 318 ARG   B O      1 
ATOM   5854  C  CB     . ARG   B 2  318 ? -4.765  -69.944  35.284  1.00 54.11  ? 318 ARG   B CB     1 
ATOM   5855  C  CG     . ARG   B 2  318 ? -6.264  -69.660  35.214  1.00 52.85  ? 318 ARG   B CG     1 
ATOM   5856  C  CD     . ARG   B 2  318 ? -6.668  -69.399  33.804  1.00 47.46  ? 318 ARG   B CD     1 
ATOM   5857  N  NE     . ARG   B 2  318 ? -6.554  -70.612  33.012  1.00 50.40  ? 318 ARG   B NE     1 
ATOM   5858  C  CZ     . ARG   B 2  318 ? -7.097  -70.773  31.814  1.00 51.30  ? 318 ARG   B CZ     1 
ATOM   5859  N  NH1    . ARG   B 2  318 ? -7.794  -69.815  31.240  1.00 48.86  ? 318 ARG   B NH1    1 
ATOM   5860  N  NH2    . ARG   B 2  318 ? -6.912  -71.917  31.166  1.00 53.21  ? 318 ARG   B NH2    1 
ATOM   5861  N  N      . GLY   B 2  319 ? -2.720  -72.260  36.538  1.00 54.80  ? 319 GLY   B N      1 
ATOM   5862  C  CA     . GLY   B 2  319 ? -1.429  -72.922  36.559  1.00 59.54  ? 319 GLY   B CA     1 
ATOM   5863  C  C      . GLY   B 2  319 ? -1.375  -74.027  37.586  1.00 59.04  ? 319 GLY   B C      1 
ATOM   5864  O  O      . GLY   B 2  319 ? -2.355  -74.342  38.253  1.00 60.98  ? 319 GLY   B O      1 
ATOM   5865  N  N      . ARG   B 2  320 ? -0.196  -74.635  37.701  1.00 63.58  ? 320 ARG   B N      1 
ATOM   5866  C  CA     . ARG   B 2  320 ? 0.075   -75.608  38.756  1.00 65.14  ? 320 ARG   B CA     1 
ATOM   5867  C  C      . ARG   B 2  320 ? 0.826   -74.890  39.866  1.00 60.36  ? 320 ARG   B C      1 
ATOM   5868  O  O      . ARG   B 2  320 ? 1.936   -74.394  39.638  1.00 57.63  ? 320 ARG   B O      1 
ATOM   5869  C  CB     . ARG   B 2  320 ? 0.913   -76.770  38.241  1.00 68.34  ? 320 ARG   B CB     1 
ATOM   5870  C  CG     . ARG   B 2  320 ? 0.662   -78.071  38.992  1.00 80.63  ? 320 ARG   B CG     1 
ATOM   5871  C  CD     . ARG   B 2  320 ? 0.981   -79.272  38.113  1.00 97.64  ? 320 ARG   B CD     1 
ATOM   5872  N  NE     . ARG   B 2  320 ? 2.432   -79.464  38.035  1.00 103.96 ? 320 ARG   B NE     1 
ATOM   5873  C  CZ     . ARG   B 2  320 ? 3.097   -79.855  36.951  1.00 99.99  ? 320 ARG   B CZ     1 
ATOM   5874  N  NH1    . ARG   B 2  320 ? 2.473   -80.147  35.823  1.00 106.70 ? 320 ARG   B NH1    1 
ATOM   5875  N  NH2    . ARG   B 2  320 ? 4.425   -79.976  37.004  1.00 99.81  ? 320 ARG   B NH2    1 
ATOM   5876  N  N      . MET   B 2  321 ? 0.223   -74.823  41.050  1.00 51.91  ? 321 MET   B N      1 
ATOM   5877  C  CA     . MET   B 2  321 ? 0.823   -74.089  42.151  1.00 50.71  ? 321 MET   B CA     1 
ATOM   5878  C  C      . MET   B 2  321 ? 0.128   -74.487  43.451  1.00 60.61  ? 321 MET   B C      1 
ATOM   5879  O  O      . MET   B 2  321 ? -0.925  -75.131  43.454  1.00 56.94  ? 321 MET   B O      1 
ATOM   5880  C  CB     . MET   B 2  321 ? 0.700   -72.586  41.956  1.00 53.22  ? 321 MET   B CB     1 
ATOM   5881  C  CG     . MET   B 2  321 ? -0.727  -72.132  42.205  1.00 60.86  ? 321 MET   B CG     1 
ATOM   5882  S  SD     . MET   B 2  321 ? -1.116  -70.476  41.639  1.00 75.50  ? 321 MET   B SD     1 
ATOM   5883  C  CE     . MET   B 2  321 ? -1.261  -70.806  39.877  1.00 58.01  ? 321 MET   B CE     1 
ATOM   5884  N  N      . SER   B 2  322 ? 0.734   -74.069  44.562  1.00 67.81  ? 322 SER   B N      1 
ATOM   5885  C  CA     . SER   B 2  322 ? 0.249   -74.385  45.900  1.00 60.97  ? 322 SER   B CA     1 
ATOM   5886  C  C      . SER   B 2  322 ? -0.993  -73.572  46.225  1.00 62.66  ? 322 SER   B C      1 
ATOM   5887  O  O      . SER   B 2  322 ? -0.913  -72.353  46.398  1.00 60.29  ? 322 SER   B O      1 
ATOM   5888  C  CB     . SER   B 2  322 ? 1.336   -74.093  46.926  1.00 68.89  ? 322 SER   B CB     1 
ATOM   5889  O  OG     . SER   B 2  322 ? 0.804   -74.146  48.238  1.00 69.73  ? 322 SER   B OG     1 
ATOM   5890  N  N      . MET   B 2  323 ? -2.141  -74.238  46.347  1.00 67.10  ? 323 MET   B N      1 
ATOM   5891  C  CA     . MET   B 2  323 ? -3.296  -73.545  46.899  1.00 67.21  ? 323 MET   B CA     1 
ATOM   5892  C  C      . MET   B 2  323 ? -2.996  -73.021  48.296  1.00 74.45  ? 323 MET   B C      1 
ATOM   5893  O  O      . MET   B 2  323 ? -3.510  -71.967  48.685  1.00 71.37  ? 323 MET   B O      1 
ATOM   5894  C  CB     . MET   B 2  323 ? -4.510  -74.463  46.905  1.00 69.02  ? 323 MET   B CB     1 
ATOM   5895  C  CG     . MET   B 2  323 ? -5.030  -74.691  45.504  1.00 82.07  ? 323 MET   B CG     1 
ATOM   5896  S  SD     . MET   B 2  323 ? -5.792  -76.296  45.221  1.00 104.86 ? 323 MET   B SD     1 
ATOM   5897  C  CE     . MET   B 2  323 ? -7.450  -75.977  45.816  1.00 77.70  ? 323 MET   B CE     1 
ATOM   5898  N  N      . LYS   B 2  324 ? -2.146  -73.724  49.053  1.00 75.25  ? 324 LYS   B N      1 
ATOM   5899  C  CA     . LYS   B 2  324 ? -1.694  -73.208  50.342  1.00 68.14  ? 324 LYS   B CA     1 
ATOM   5900  C  C      . LYS   B 2  324 ? -1.063  -71.833  50.178  1.00 64.32  ? 324 LYS   B C      1 
ATOM   5901  O  O      . LYS   B 2  324 ? -1.399  -70.887  50.895  1.00 64.97  ? 324 LYS   B O      1 
ATOM   5902  C  CB     . LYS   B 2  324 ? -0.695  -74.182  50.968  1.00 68.49  ? 324 LYS   B CB     1 
ATOM   5903  C  CG     . LYS   B 2  324 ? -0.141  -73.779  52.339  1.00 68.05  ? 324 LYS   B CG     1 
ATOM   5904  C  CD     . LYS   B 2  324 ? 1.241   -74.398  52.517  1.00 71.01  ? 324 LYS   B CD     1 
ATOM   5905  C  CE     . LYS   B 2  324 ? 1.963   -73.937  53.757  1.00 82.83  ? 324 LYS   B CE     1 
ATOM   5906  N  NZ     . LYS   B 2  324 ? 1.331   -74.538  54.974  1.00 82.94  ? 324 LYS   B NZ     1 
ATOM   5907  N  N      . GLU   B 2  325 ? -0.153  -71.702  49.218  1.00 66.51  ? 325 GLU   B N      1 
ATOM   5908  C  CA     . GLU   B 2  325 ? 0.559   -70.441  49.059  1.00 70.17  ? 325 GLU   B CA     1 
ATOM   5909  C  C      . GLU   B 2  325 ? -0.343  -69.345  48.504  1.00 68.30  ? 325 GLU   B C      1 
ATOM   5910  O  O      . GLU   B 2  325 ? -0.234  -68.179  48.907  1.00 60.78  ? 325 GLU   B O      1 
ATOM   5911  C  CB     . GLU   B 2  325 ? 1.762   -70.637  48.156  1.00 63.10  ? 325 GLU   B CB     1 
ATOM   5912  C  CG     . GLU   B 2  325 ? 2.819   -69.630  48.434  1.00 61.65  ? 325 GLU   B CG     1 
ATOM   5913  C  CD     . GLU   B 2  325 ? 4.012   -69.881  47.593  1.00 71.99  ? 325 GLU   B CD     1 
ATOM   5914  O  OE1    . GLU   B 2  325 ? 4.063   -70.976  46.991  1.00 80.45  ? 325 GLU   B OE1    1 
ATOM   5915  O  OE2    . GLU   B 2  325 ? 4.908   -69.013  47.555  1.00 80.11  ? 325 GLU   B OE2    1 
ATOM   5916  N  N      . VAL   B 2  326 ? -1.216  -69.686  47.551  1.00 64.74  ? 326 VAL   B N      1 
ATOM   5917  C  CA     . VAL   B 2  326 ? -2.229  -68.729  47.120  1.00 58.07  ? 326 VAL   B CA     1 
ATOM   5918  C  C      . VAL   B 2  326 ? -2.980  -68.206  48.337  1.00 64.45  ? 326 VAL   B C      1 
ATOM   5919  O  O      . VAL   B 2  326 ? -2.976  -67.004  48.628  1.00 58.77  ? 326 VAL   B O      1 
ATOM   5920  C  CB     . VAL   B 2  326 ? -3.183  -69.371  46.102  1.00 54.80  ? 326 VAL   B CB     1 
ATOM   5921  C  CG1    . VAL   B 2  326 ? -4.178  -68.345  45.601  1.00 56.62  ? 326 VAL   B CG1    1 
ATOM   5922  C  CG2    . VAL   B 2  326 ? -2.417  -69.951  44.955  1.00 52.72  ? 326 VAL   B CG2    1 
ATOM   5923  N  N      . ASP   B 2  327 ? -3.599  -69.124  49.091  1.00 70.53  ? 327 ASP   B N      1 
ATOM   5924  C  CA     . ASP   B 2  327 ? -4.357  -68.746  50.280  1.00 62.16  ? 327 ASP   B CA     1 
ATOM   5925  C  C      . ASP   B 2  327 ? -3.543  -67.804  51.143  1.00 60.12  ? 327 ASP   B C      1 
ATOM   5926  O  O      . ASP   B 2  327 ? -4.029  -66.757  51.582  1.00 62.25  ? 327 ASP   B O      1 
ATOM   5927  C  CB     . ASP   B 2  327 ? -4.733  -69.988  51.087  1.00 61.27  ? 327 ASP   B CB     1 
ATOM   5928  C  CG     . ASP   B 2  327 ? -5.939  -70.716  50.523  1.00 83.33  ? 327 ASP   B CG     1 
ATOM   5929  O  OD1    . ASP   B 2  327 ? -6.726  -70.063  49.799  1.00 90.77  ? 327 ASP   B OD1    1 
ATOM   5930  O  OD2    . ASP   B 2  327 ? -6.118  -71.929  50.833  1.00 78.77  ? 327 ASP   B OD2    1 
ATOM   5931  N  N      . GLU   B 2  328 ? -2.285  -68.162  51.388  1.00 60.36  ? 328 GLU   B N      1 
ATOM   5932  C  CA     . GLU   B 2  328 ? -1.479  -67.347  52.284  1.00 66.23  ? 328 GLU   B CA     1 
ATOM   5933  C  C      . GLU   B 2  328 ? -1.178  -65.995  51.667  1.00 61.97  ? 328 GLU   B C      1 
ATOM   5934  O  O      . GLU   B 2  328 ? -1.085  -64.988  52.381  1.00 58.64  ? 328 GLU   B O      1 
ATOM   5935  C  CB     . GLU   B 2  328 ? -0.188  -68.088  52.653  1.00 70.46  ? 328 GLU   B CB     1 
ATOM   5936  C  CG     . GLU   B 2  328 ? -0.421  -69.534  53.107  1.00 72.96  ? 328 GLU   B CG     1 
ATOM   5937  C  CD     . GLU   B 2  328 ? 0.828   -70.218  53.662  1.00 83.29  ? 328 GLU   B CD     1 
ATOM   5938  O  OE1    . GLU   B 2  328 ? 1.874   -69.540  53.842  1.00 76.35  ? 328 GLU   B OE1    1 
ATOM   5939  O  OE2    . GLU   B 2  328 ? 0.748   -71.443  53.924  1.00 83.27  ? 328 GLU   B OE2    1 
ATOM   5940  N  N      . GLN   B 2  329 ? -1.054  -65.956  50.344  1.00 59.62  ? 329 GLN   B N      1 
ATOM   5941  C  CA     . GLN   B 2  329 ? -0.670  -64.733  49.665  1.00 62.80  ? 329 GLN   B CA     1 
ATOM   5942  C  C      . GLN   B 2  329 ? -1.860  -63.816  49.467  1.00 61.59  ? 329 GLN   B C      1 
ATOM   5943  O  O      . GLN   B 2  329 ? -1.712  -62.590  49.514  1.00 61.91  ? 329 GLN   B O      1 
ATOM   5944  C  CB     . GLN   B 2  329 ? -0.020  -65.067  48.322  1.00 61.12  ? 329 GLN   B CB     1 
ATOM   5945  C  CG     . GLN   B 2  329 ? 1.474   -65.330  48.415  1.00 55.80  ? 329 GLN   B CG     1 
ATOM   5946  C  CD     . GLN   B 2  329 ? 2.172   -64.245  49.182  1.00 60.35  ? 329 GLN   B CD     1 
ATOM   5947  O  OE1    . GLN   B 2  329 ? 1.741   -63.094  49.163  1.00 67.34  ? 329 GLN   B OE1    1 
ATOM   5948  N  NE2    . GLN   B 2  329 ? 3.254   -64.592  49.859  1.00 57.46  ? 329 GLN   B NE2    1 
ATOM   5949  N  N      . MET   B 2  330 ? -3.043  -64.394  49.263  1.00 62.18  ? 330 MET   B N      1 
ATOM   5950  C  CA     . MET   B 2  330 ? -4.250  -63.586  49.130  1.00 60.38  ? 330 MET   B CA     1 
ATOM   5951  C  C      . MET   B 2  330 ? -4.668  -63.033  50.480  1.00 60.22  ? 330 MET   B C      1 
ATOM   5952  O  O      . MET   B 2  330 ? -5.018  -61.854  50.592  1.00 61.52  ? 330 MET   B O      1 
ATOM   5953  C  CB     . MET   B 2  330 ? -5.386  -64.414  48.533  1.00 62.84  ? 330 MET   B CB     1 
ATOM   5954  C  CG     . MET   B 2  330 ? -5.319  -64.621  47.020  1.00 58.53  ? 330 MET   B CG     1 
ATOM   5955  S  SD     . MET   B 2  330 ? -5.261  -63.062  46.161  1.00 54.57  ? 330 MET   B SD     1 
ATOM   5956  C  CE     . MET   B 2  330 ? -6.768  -62.317  46.750  1.00 61.98  ? 330 MET   B CE     1 
ATOM   5957  N  N      . LEU   B 2  331 ? -4.634  -63.876  51.518  1.00 61.77  ? 331 LEU   B N      1 
ATOM   5958  C  CA     . LEU   B 2  331 ? -4.828  -63.393  52.883  1.00 65.50  ? 331 LEU   B CA     1 
ATOM   5959  C  C      . LEU   B 2  331 ? -3.826  -62.297  53.232  1.00 64.20  ? 331 LEU   B C      1 
ATOM   5960  O  O      . LEU   B 2  331 ? -4.140  -61.369  53.990  1.00 57.56  ? 331 LEU   B O      1 
ATOM   5961  C  CB     . LEU   B 2  331 ? -4.706  -64.558  53.869  1.00 62.69  ? 331 LEU   B CB     1 
ATOM   5962  C  CG     . LEU   B 2  331 ? -5.957  -65.413  54.073  1.00 58.70  ? 331 LEU   B CG     1 
ATOM   5963  C  CD1    . LEU   B 2  331 ? -5.698  -66.542  55.050  1.00 56.30  ? 331 LEU   B CD1    1 
ATOM   5964  C  CD2    . LEU   B 2  331 ? -7.116  -64.553  54.524  1.00 66.70  ? 331 LEU   B CD2    1 
ATOM   5965  N  N      . ASN   B 2  332 ? -2.625  -62.381  52.664  1.00 67.12  ? 332 ASN   B N      1 
ATOM   5966  C  CA     . ASN   B 2  332 ? -1.559  -61.463  53.021  1.00 66.80  ? 332 ASN   B CA     1 
ATOM   5967  C  C      . ASN   B 2  332 ? -1.774  -60.068  52.445  1.00 69.29  ? 332 ASN   B C      1 
ATOM   5968  O  O      . ASN   B 2  332 ? -1.347  -59.084  53.061  1.00 65.23  ? 332 ASN   B O      1 
ATOM   5969  C  CB     . ASN   B 2  332 ? -0.228  -62.025  52.554  1.00 67.04  ? 332 ASN   B CB     1 
ATOM   5970  C  CG     . ASN   B 2  332 ? 0.846   -60.985  52.549  1.00 85.94  ? 332 ASN   B CG     1 
ATOM   5971  O  OD1    . ASN   B 2  332 ? 1.335   -60.576  53.608  1.00 93.95  ? 332 ASN   B OD1    1 
ATOM   5972  N  ND2    . ASN   B 2  332 ? 1.191   -60.499  51.358  1.00 89.13  ? 332 ASN   B ND2    1 
ATOM   5973  N  N      . VAL   B 2  333 ? -2.427  -59.953  51.280  1.00 69.92  ? 333 VAL   B N      1 
ATOM   5974  C  CA     . VAL   B 2  333 ? -2.637  -58.631  50.684  1.00 69.39  ? 333 VAL   B CA     1 
ATOM   5975  C  C      . VAL   B 2  333 ? -3.768  -57.890  51.402  1.00 65.59  ? 333 VAL   B C      1 
ATOM   5976  O  O      . VAL   B 2  333 ? -3.655  -56.691  51.689  1.00 60.49  ? 333 VAL   B O      1 
ATOM   5977  C  CB     . VAL   B 2  333 ? -2.911  -58.757  49.174  1.00 66.29  ? 333 VAL   B CB     1 
ATOM   5978  C  CG1    . VAL   B 2  333 ? -4.268  -59.373  48.936  1.00 65.08  ? 333 VAL   B CG1    1 
ATOM   5979  C  CG2    . VAL   B 2  333 ? -2.767  -57.417  48.466  1.00 68.17  ? 333 VAL   B CG2    1 
ATOM   5980  N  N      . GLN   B 2  334 ? -4.862  -58.597  51.715  1.00 63.41  ? 334 GLN   B N      1 
ATOM   5981  C  CA     . GLN   B 2  334 ? -5.957  -58.035  52.505  1.00 63.09  ? 334 GLN   B CA     1 
ATOM   5982  C  C      . GLN   B 2  334 ? -5.466  -57.470  53.839  1.00 72.40  ? 334 GLN   B C      1 
ATOM   5983  O  O      . GLN   B 2  334 ? -5.680  -56.289  54.145  1.00 71.34  ? 334 GLN   B O      1 
ATOM   5984  C  CB     . GLN   B 2  334 ? -7.036  -59.100  52.755  1.00 58.52  ? 334 GLN   B CB     1 
ATOM   5985  C  CG     . GLN   B 2  334 ? -7.463  -59.893  51.537  1.00 63.24  ? 334 GLN   B CG     1 
ATOM   5986  C  CD     . GLN   B 2  334 ? -8.482  -60.987  51.855  1.00 68.70  ? 334 GLN   B CD     1 
ATOM   5987  O  OE1    . GLN   B 2  334 ? -9.485  -60.742  52.520  1.00 76.30  ? 334 GLN   B OE1    1 
ATOM   5988  N  NE2    . GLN   B 2  334 ? -8.231  -62.200  51.360  1.00 63.59  ? 334 GLN   B NE2    1 
ATOM   5989  N  N      . ASN   B 2  335 ? -4.831  -58.318  54.666  1.00 75.07  ? 335 ASN   B N      1 
ATOM   5990  C  CA     . ASN   B 2  335 ? -4.441  -57.906  56.016  1.00 70.71  ? 335 ASN   B CA     1 
ATOM   5991  C  C      . ASN   B 2  335 ? -3.411  -56.783  55.995  1.00 65.98  ? 335 ASN   B C      1 
ATOM   5992  O  O      . ASN   B 2  335 ? -3.393  -55.946  56.906  1.00 64.30  ? 335 ASN   B O      1 
ATOM   5993  C  CB     . ASN   B 2  335 ? -3.914  -59.105  56.807  1.00 63.16  ? 335 ASN   B CB     1 
ATOM   5994  C  CG     . ASN   B 2  335 ? -4.988  -60.158  57.064  1.00 68.78  ? 335 ASN   B CG     1 
ATOM   5995  O  OD1    . ASN   B 2  335 ? -6.187  -59.863  57.063  1.00 67.52  ? 335 ASN   B OD1    1 
ATOM   5996  N  ND2    . ASN   B 2  335 ? -4.558  -61.396  57.282  1.00 70.54  ? 335 ASN   B ND2    1 
ATOM   5997  N  N      . LYS   B 2  336 ? -2.552  -56.753  54.972  1.00 65.46  ? 336 LYS   B N      1 
ATOM   5998  C  CA     . LYS   B 2  336 ? -1.624  -55.638  54.788  1.00 70.08  ? 336 LYS   B CA     1 
ATOM   5999  C  C      . LYS   B 2  336 ? -2.352  -54.351  54.418  1.00 67.22  ? 336 LYS   B C      1 
ATOM   6000  O  O      . LYS   B 2  336 ? -1.997  -53.269  54.893  1.00 68.21  ? 336 LYS   B O      1 
ATOM   6001  C  CB     . LYS   B 2  336 ? -0.607  -55.993  53.703  1.00 77.57  ? 336 LYS   B CB     1 
ATOM   6002  C  CG     . LYS   B 2  336 ? 0.479   -57.003  54.109  1.00 91.48  ? 336 LYS   B CG     1 
ATOM   6003  C  CD     . LYS   B 2  336 ? 1.669   -56.976  53.108  1.00 101.90 ? 336 LYS   B CD     1 
ATOM   6004  C  CE     . LYS   B 2  336 ? 2.670   -55.836  53.335  1.00 107.10 ? 336 LYS   B CE     1 
ATOM   6005  N  NZ     . LYS   B 2  336 ? 3.521   -55.597  52.118  1.00 100.95 ? 336 LYS   B NZ     1 
ATOM   6006  N  N      . ASN   B 2  337 ? -3.369  -54.448  53.574  1.00 70.37  ? 337 ASN   B N      1 
ATOM   6007  C  CA     . ASN   B 2  337 ? -4.028  -53.290  52.994  1.00 65.77  ? 337 ASN   B CA     1 
ATOM   6008  C  C      . ASN   B 2  337 ? -5.516  -53.322  53.287  1.00 59.02  ? 337 ASN   B C      1 
ATOM   6009  O  O      . ASN   B 2  337 ? -6.344  -53.045  52.422  1.00 60.99  ? 337 ASN   B O      1 
ATOM   6010  C  CB     . ASN   B 2  337 ? -3.758  -53.257  51.500  1.00 62.88  ? 337 ASN   B CB     1 
ATOM   6011  C  CG     . ASN   B 2  337 ? -2.303  -53.385  51.208  1.00 60.70  ? 337 ASN   B CG     1 
ATOM   6012  O  OD1    . ASN   B 2  337 ? -1.893  -54.318  50.540  1.00 66.68  ? 337 ASN   B OD1    1 
ATOM   6013  N  ND2    . ASN   B 2  337 ? -1.502  -52.479  51.745  1.00 59.61  ? 337 ASN   B ND2    1 
ATOM   6014  N  N      . SER   B 2  338 ? -5.850  -53.658  54.535  1.00 58.47  ? 338 SER   B N      1 
ATOM   6015  C  CA     . SER   B 2  338 ? -7.234  -53.860  54.940  1.00 57.25  ? 338 SER   B CA     1 
ATOM   6016  C  C      . SER   B 2  338 ? -8.028  -52.569  54.869  1.00 57.00  ? 338 SER   B C      1 
ATOM   6017  O  O      . SER   B 2  338 ? -9.251  -52.607  54.736  1.00 60.47  ? 338 SER   B O      1 
ATOM   6018  C  CB     . SER   B 2  338 ? -7.287  -54.427  56.367  1.00 69.46  ? 338 SER   B CB     1 
ATOM   6019  O  OG     . SER   B 2  338 ? -6.929  -53.451  57.352  1.00 65.07  ? 338 SER   B OG     1 
ATOM   6020  N  N      . SER   B 2  339 ? -7.366  -51.422  55.008  1.00 52.81  ? 339 SER   B N      1 
ATOM   6021  C  CA     . SER   B 2  339 ? -8.006  -50.148  54.707  1.00 54.79  ? 339 SER   B CA     1 
ATOM   6022  C  C      . SER   B 2  339 ? -8.792  -50.206  53.396  1.00 61.32  ? 339 SER   B C      1 
ATOM   6023  O  O      . SER   B 2  339 ? -10.004 -49.966  53.362  1.00 63.69  ? 339 SER   B O      1 
ATOM   6024  C  CB     . SER   B 2  339 ? -6.945  -49.059  54.630  1.00 57.22  ? 339 SER   B CB     1 
ATOM   6025  O  OG     . SER   B 2  339 ? -7.452  -47.916  53.975  1.00 58.41  ? 339 SER   B OG     1 
ATOM   6026  N  N      . TYR   B 2  340 ? -8.116  -50.532  52.300  1.00 59.46  ? 340 TYR   B N      1 
ATOM   6027  C  CA     . TYR   B 2  340 ? -8.713  -50.410  50.981  1.00 53.65  ? 340 TYR   B CA     1 
ATOM   6028  C  C      . TYR   B 2  340 ? -9.788  -51.446  50.684  1.00 58.68  ? 340 TYR   B C      1 
ATOM   6029  O  O      . TYR   B 2  340 ? -10.105 -51.679  49.511  1.00 58.66  ? 340 TYR   B O      1 
ATOM   6030  C  CB     . TYR   B 2  340 ? -7.623  -50.502  49.929  1.00 57.31  ? 340 TYR   B CB     1 
ATOM   6031  C  CG     . TYR   B 2  340 ? -6.653  -49.365  50.017  1.00 62.71  ? 340 TYR   B CG     1 
ATOM   6032  C  CD1    . TYR   B 2  340 ? -7.045  -48.072  49.728  1.00 62.77  ? 340 TYR   B CD1    1 
ATOM   6033  C  CD2    . TYR   B 2  340 ? -5.343  -49.581  50.393  1.00 65.69  ? 340 TYR   B CD2    1 
ATOM   6034  C  CE1    . TYR   B 2  340 ? -6.164  -47.020  49.825  1.00 64.53  ? 340 TYR   B CE1    1 
ATOM   6035  C  CE2    . TYR   B 2  340 ? -4.446  -48.532  50.479  1.00 66.01  ? 340 TYR   B CE2    1 
ATOM   6036  C  CZ     . TYR   B 2  340 ? -4.864  -47.256  50.197  1.00 63.81  ? 340 TYR   B CZ     1 
ATOM   6037  O  OH     . TYR   B 2  340 ? -3.975  -46.214  50.289  1.00 65.21  ? 340 TYR   B OH     1 
ATOM   6038  N  N      . PHE   B 2  341 ? -10.352 -52.079  51.721  1.00 54.35  ? 341 PHE   B N      1 
ATOM   6039  C  CA     . PHE   B 2  341 ? -11.506 -52.963  51.583  1.00 52.19  ? 341 PHE   B CA     1 
ATOM   6040  C  C      . PHE   B 2  341 ? -12.588 -52.494  52.536  1.00 50.85  ? 341 PHE   B C      1 
ATOM   6041  O  O      . PHE   B 2  341 ? -12.294 -52.129  53.674  1.00 57.06  ? 341 PHE   B O      1 
ATOM   6042  C  CB     . PHE   B 2  341 ? -11.172 -54.409  51.914  1.00 49.73  ? 341 PHE   B CB     1 
ATOM   6043  C  CG     . PHE   B 2  341 ? -10.175 -55.026  51.000  1.00 46.03  ? 341 PHE   B CG     1 
ATOM   6044  C  CD1    . PHE   B 2  341 ? -8.829  -54.816  51.187  1.00 46.86  ? 341 PHE   B CD1    1 
ATOM   6045  C  CD2    . PHE   B 2  341 ? -10.580 -55.809  49.951  1.00 45.43  ? 341 PHE   B CD2    1 
ATOM   6046  C  CE1    . PHE   B 2  341 ? -7.908  -55.390  50.345  1.00 51.18  ? 341 PHE   B CE1    1 
ATOM   6047  C  CE2    . PHE   B 2  341 ? -9.661  -56.374  49.102  1.00 46.44  ? 341 PHE   B CE2    1 
ATOM   6048  C  CZ     . PHE   B 2  341 ? -8.327  -56.168  49.297  1.00 47.78  ? 341 PHE   B CZ     1 
ATOM   6049  N  N      . VAL   B 2  342 ? -13.842 -52.512  52.100  1.00 53.79  ? 342 VAL   B N      1 
ATOM   6050  C  CA     . VAL   B 2  342 ? -14.889 -52.081  53.021  1.00 55.92  ? 342 VAL   B CA     1 
ATOM   6051  C  C      . VAL   B 2  342 ? -14.996 -53.062  54.186  1.00 55.08  ? 342 VAL   B C      1 
ATOM   6052  O  O      . VAL   B 2  342 ? -14.824 -54.284  54.042  1.00 54.51  ? 342 VAL   B O      1 
ATOM   6053  C  CB     . VAL   B 2  342 ? -16.232 -51.847  52.298  1.00 48.80  ? 342 VAL   B CB     1 
ATOM   6054  C  CG1    . VAL   B 2  342 ? -16.070 -50.778  51.257  1.00 44.76  ? 342 VAL   B CG1    1 
ATOM   6055  C  CG2    . VAL   B 2  342 ? -16.677 -53.111  51.587  1.00 52.21  ? 342 VAL   B CG2    1 
ATOM   6056  N  N      . GLU   B 2  343 ? -15.203 -52.501  55.366  1.00 55.60  ? 343 GLU   B N      1 
ATOM   6057  C  CA     . GLU   B 2  343 ? -15.405 -53.257  56.586  1.00 53.58  ? 343 GLU   B CA     1 
ATOM   6058  C  C      . GLU   B 2  343 ? -16.810 -53.834  56.680  1.00 54.15  ? 343 GLU   B C      1 
ATOM   6059  O  O      . GLU   B 2  343 ? -17.028 -54.804  57.413  1.00 58.90  ? 343 GLU   B O      1 
ATOM   6060  C  CB     . GLU   B 2  343 ? -15.108 -52.331  57.773  1.00 54.46  ? 343 GLU   B CB     1 
ATOM   6061  C  CG     . GLU   B 2  343 ? -16.045 -51.123  57.826  1.00 65.10  ? 343 GLU   B CG     1 
ATOM   6062  C  CD     . GLU   B 2  343 ? -15.795 -50.206  59.011  1.00 87.42  ? 343 GLU   B CD     1 
ATOM   6063  O  OE1    . GLU   B 2  343 ? -14.717 -50.324  59.655  1.00 81.04  ? 343 GLU   B OE1    1 
ATOM   6064  O  OE2    . GLU   B 2  343 ? -16.710 -49.397  59.318  1.00 96.63  ? 343 GLU   B OE2    1 
ATOM   6065  N  N      . TRP   B 2  344 ? -17.767 -53.284  55.951  1.00 50.31  ? 344 TRP   B N      1 
ATOM   6066  C  CA     . TRP   B 2  344 ? -19.144 -53.675  56.151  1.00 43.78  ? 344 TRP   B CA     1 
ATOM   6067  C  C      . TRP   B 2  344 ? -19.611 -54.739  55.169  1.00 50.12  ? 344 TRP   B C      1 
ATOM   6068  O  O      . TRP   B 2  344 ? -20.809 -55.028  55.109  1.00 52.11  ? 344 TRP   B O      1 
ATOM   6069  C  CB     . TRP   B 2  344 ? -20.041 -52.456  56.077  1.00 47.83  ? 344 TRP   B CB     1 
ATOM   6070  C  CG     . TRP   B 2  344 ? -19.698 -51.470  55.018  1.00 47.35  ? 344 TRP   B CG     1 
ATOM   6071  C  CD1    . TRP   B 2  344 ? -18.831 -50.431  55.113  1.00 50.99  ? 344 TRP   B CD1    1 
ATOM   6072  C  CD2    . TRP   B 2  344 ? -20.247 -51.419  53.701  1.00 49.04  ? 344 TRP   B CD2    1 
ATOM   6073  N  NE1    . TRP   B 2  344 ? -18.811 -49.724  53.934  1.00 51.82  ? 344 TRP   B NE1    1 
ATOM   6074  C  CE2    . TRP   B 2  344 ? -19.673 -50.316  53.052  1.00 45.61  ? 344 TRP   B CE2    1 
ATOM   6075  C  CE3    . TRP   B 2  344 ? -21.172 -52.206  53.004  1.00 50.96  ? 344 TRP   B CE3    1 
ATOM   6076  C  CZ2    . TRP   B 2  344 ? -19.990 -49.980  51.748  1.00 47.08  ? 344 TRP   B CZ2    1 
ATOM   6077  C  CZ3    . TRP   B 2  344 ? -21.488 -51.869  51.701  1.00 46.16  ? 344 TRP   B CZ3    1 
ATOM   6078  C  CH2    . TRP   B 2  344 ? -20.903 -50.765  51.091  1.00 44.94  ? 344 TRP   B CH2    1 
ATOM   6079  N  N      . ILE   B 2  345 ? -18.711 -55.331  54.399  1.00 46.15  ? 345 ILE   B N      1 
ATOM   6080  C  CA     . ILE   B 2  345 ? -18.968 -56.593  53.720  1.00 41.10  ? 345 ILE   B CA     1 
ATOM   6081  C  C      . ILE   B 2  345 ? -17.896 -57.579  54.167  1.00 44.08  ? 345 ILE   B C      1 
ATOM   6082  O  O      . ILE   B 2  345 ? -16.764 -57.554  53.679  1.00 44.20  ? 345 ILE   B O      1 
ATOM   6083  C  CB     . ILE   B 2  345 ? -18.975 -56.439  52.190  1.00 44.83  ? 345 ILE   B CB     1 
ATOM   6084  C  CG1    . ILE   B 2  345 ? -20.041 -55.443  51.755  1.00 44.95  ? 345 ILE   B CG1    1 
ATOM   6085  C  CG2    . ILE   B 2  345 ? -19.155 -57.803  51.518  1.00 37.78  ? 345 ILE   B CG2    1 
ATOM   6086  C  CD1    . ILE   B 2  345 ? -20.022 -55.232  50.302  1.00 43.38  ? 345 ILE   B CD1    1 
ATOM   6087  N  N      . PRO   B 2  346 ? -18.207 -58.432  55.130  1.00 40.51  ? 346 PRO   B N      1 
ATOM   6088  C  CA     . PRO   B 2  346 ? -17.214 -59.374  55.629  1.00 31.00  ? 346 PRO   B CA     1 
ATOM   6089  C  C      . PRO   B 2  346 ? -16.736 -60.344  54.566  1.00 33.35  ? 346 PRO   B C      1 
ATOM   6090  O  O      . PRO   B 2  346 ? -17.521 -60.903  53.803  1.00 37.05  ? 346 PRO   B O      1 
ATOM   6091  C  CB     . PRO   B 2  346 ? -17.956 -60.085  56.754  1.00 32.53  ? 346 PRO   B CB     1 
ATOM   6092  C  CG     . PRO   B 2  346 ? -18.954 -59.069  57.202  1.00 36.49  ? 346 PRO   B CG     1 
ATOM   6093  C  CD     . PRO   B 2  346 ? -19.408 -58.396  55.974  1.00 41.06  ? 346 PRO   B CD     1 
ATOM   6094  N  N      . ASN   B 2  347 ? -15.422 -60.545  54.545  1.00 34.31  ? 347 ASN   B N      1 
ATOM   6095  C  CA     . ASN   B 2  347 ? -14.775 -61.575  53.743  1.00 33.79  ? 347 ASN   B CA     1 
ATOM   6096  C  C      . ASN   B 2  347 ? -15.162 -61.426  52.286  1.00 32.62  ? 347 ASN   B C      1 
ATOM   6097  O  O      . ASN   B 2  347 ? -15.569 -62.379  51.634  1.00 39.43  ? 347 ASN   B O      1 
ATOM   6098  C  CB     . ASN   B 2  347 ? -15.093 -62.988  54.258  1.00 31.28  ? 347 ASN   B CB     1 
ATOM   6099  C  CG     . ASN   B 2  347 ? -15.229 -63.051  55.774  1.00 32.57  ? 347 ASN   B CG     1 
ATOM   6100  O  OD1    . ASN   B 2  347 ? -14.296 -62.727  56.496  1.00 38.76  ? 347 ASN   B OD1    1 
ATOM   6101  N  ND2    . ASN   B 2  347 ? -16.383 -63.502  56.259  1.00 34.83  ? 347 ASN   B ND2    1 
ATOM   6102  N  N      . ASN   B 2  348 ? -14.976 -60.210  51.764  1.00 40.19  ? 348 ASN   B N      1 
ATOM   6103  C  CA     . ASN   B 2  348 ? -15.444 -59.781  50.446  1.00 35.89  ? 348 ASN   B CA     1 
ATOM   6104  C  C      . ASN   B 2  348 ? -14.495 -60.139  49.311  1.00 38.66  ? 348 ASN   B C      1 
ATOM   6105  O  O      . ASN   B 2  348 ? -14.828 -59.866  48.155  1.00 43.01  ? 348 ASN   B O      1 
ATOM   6106  C  CB     . ASN   B 2  348 ? -15.723 -58.271  50.479  1.00 35.00  ? 348 ASN   B CB     1 
ATOM   6107  C  CG     . ASN   B 2  348 ? -14.483 -57.438  50.691  1.00 43.59  ? 348 ASN   B CG     1 
ATOM   6108  O  OD1    . ASN   B 2  348 ? -13.800 -57.577  51.694  1.00 54.87  ? 348 ASN   B OD1    1 
ATOM   6109  N  ND2    . ASN   B 2  348 ? -14.256 -56.488  49.815  1.00 45.19  ? 348 ASN   B ND2    1 
ATOM   6110  N  N      . VAL   B 2  349 ? -13.349 -60.764  49.607  1.00 41.53  ? 349 VAL   B N      1 
ATOM   6111  C  CA     . VAL   B 2  349 ? -12.434 -61.324  48.613  1.00 35.74  ? 349 VAL   B CA     1 
ATOM   6112  C  C      . VAL   B 2  349 ? -12.582 -62.834  48.602  1.00 37.73  ? 349 VAL   B C      1 
ATOM   6113  O  O      . VAL   B 2  349 ? -12.570 -63.468  49.658  1.00 45.46  ? 349 VAL   B O      1 
ATOM   6114  C  CB     . VAL   B 2  349 ? -10.971 -60.958  48.889  1.00 41.41  ? 349 VAL   B CB     1 
ATOM   6115  C  CG1    . VAL   B 2  349 ? -10.122 -61.455  47.750  1.00 46.89  ? 349 VAL   B CG1    1 
ATOM   6116  C  CG2    . VAL   B 2  349 ? -10.793 -59.463  49.024  1.00 42.26  ? 349 VAL   B CG2    1 
ATOM   6117  N  N      . LYS   B 2  350 ? -12.700 -63.400  47.407  1.00 37.48  ? 350 LYS   B N      1 
ATOM   6118  C  CA     . LYS   B 2  350 ? -12.883 -64.821  47.156  1.00 38.47  ? 350 LYS   B CA     1 
ATOM   6119  C  C      . LYS   B 2  350 ? -11.917 -65.229  46.060  1.00 41.33  ? 350 LYS   B C      1 
ATOM   6120  O  O      . LYS   B 2  350 ? -11.694 -64.466  45.119  1.00 39.08  ? 350 LYS   B O      1 
ATOM   6121  C  CB     . LYS   B 2  350 ? -14.317 -65.143  46.741  1.00 37.23  ? 350 LYS   B CB     1 
ATOM   6122  C  CG     . LYS   B 2  350 ? -15.339 -64.915  47.852  1.00 41.79  ? 350 LYS   B CG     1 
ATOM   6123  C  CD     . LYS   B 2  350 ? -15.481 -66.202  48.695  1.00 55.53  ? 350 LYS   B CD     1 
ATOM   6124  C  CE     . LYS   B 2  350 ? -16.084 -66.010  50.070  1.00 50.86  ? 350 LYS   B CE     1 
ATOM   6125  N  NZ     . LYS   B 2  350 ? -15.466 -64.899  50.800  1.00 43.95  ? 350 LYS   B NZ     1 
ATOM   6126  N  N      . THR   B 2  351 ? -11.324 -66.417  46.203  1.00 44.79  ? 351 THR   B N      1 
ATOM   6127  C  CA     . THR   B 2  351 ? -10.263 -66.887  45.329  1.00 38.21  ? 351 THR   B CA     1 
ATOM   6128  C  C      . THR   B 2  351 ? -10.624 -68.245  44.744  1.00 45.16  ? 351 THR   B C      1 
ATOM   6129  O  O      . THR   B 2  351 ? -11.350 -69.033  45.355  1.00 46.91  ? 351 THR   B O      1 
ATOM   6130  C  CB     . THR   B 2  351 ? -8.963  -67.015  46.064  1.00 35.38  ? 351 THR   B CB     1 
ATOM   6131  O  OG1    . THR   B 2  351 ? -8.676  -65.789  46.728  1.00 36.94  ? 351 THR   B OG1    1 
ATOM   6132  C  CG2    . THR   B 2  351 ? -7.854  -67.274  45.062  1.00 47.97  ? 351 THR   B CG2    1 
ATOM   6133  N  N      . ALA   B 2  352 ? -10.119 -68.512  43.546  1.00 39.99  ? 352 ALA   B N      1 
ATOM   6134  C  CA     . ALA   B 2  352 ? -10.432 -69.748  42.854  1.00 39.01  ? 352 ALA   B CA     1 
ATOM   6135  C  C      . ALA   B 2  352 ? -9.186  -70.156  42.098  1.00 42.80  ? 352 ALA   B C      1 
ATOM   6136  O  O      . ALA   B 2  352 ? -8.277  -69.351  41.896  1.00 45.48  ? 352 ALA   B O      1 
ATOM   6137  C  CB     . ALA   B 2  352 ? -11.637 -69.582  41.923  1.00 41.91  ? 352 ALA   B CB     1 
ATOM   6138  N  N      . VAL   B 2  353 ? -9.132  -71.411  41.685  1.00 44.59  ? 353 VAL   B N      1 
ATOM   6139  C  CA     . VAL   B 2  353 ? -7.940  -71.923  41.021  1.00 51.44  ? 353 VAL   B CA     1 
ATOM   6140  C  C      . VAL   B 2  353 ? -8.317  -72.922  39.937  1.00 49.81  ? 353 VAL   B C      1 
ATOM   6141  O  O      . VAL   B 2  353 ? -9.241  -73.722  40.099  1.00 55.75  ? 353 VAL   B O      1 
ATOM   6142  C  CB     . VAL   B 2  353 ? -6.969  -72.553  42.027  1.00 50.20  ? 353 VAL   B CB     1 
ATOM   6143  C  CG1    . VAL   B 2  353 ? -7.383  -73.974  42.284  1.00 62.89  ? 353 VAL   B CG1    1 
ATOM   6144  C  CG2    . VAL   B 2  353 ? -5.578  -72.534  41.446  1.00 52.44  ? 353 VAL   B CG2    1 
ATOM   6145  N  N      . CYS   B 2  354 ? -7.599  -72.867  38.829  1.00 43.73  ? 354 CYS   B N      1 
ATOM   6146  C  CA     . CYS   B 2  354 ? -7.782  -73.779  37.712  1.00 47.81  ? 354 CYS   B CA     1 
ATOM   6147  C  C      . CYS   B 2  354 ? -6.434  -74.370  37.339  1.00 53.60  ? 354 CYS   B C      1 
ATOM   6148  O  O      . CYS   B 2  354 ? -5.436  -73.652  37.241  1.00 54.98  ? 354 CYS   B O      1 
ATOM   6149  C  CB     . CYS   B 2  354 ? -8.406  -73.067  36.509  1.00 47.94  ? 354 CYS   B CB     1 
ATOM   6150  S  SG     . CYS   B 2  354 ? -8.663  -74.103  35.046  1.00 61.56  ? 354 CYS   B SG     1 
ATOM   6151  N  N      . ASP   B 2  355 ? -6.410  -75.683  37.129  1.00 53.64  ? 355 ASP   B N      1 
ATOM   6152  C  CA     . ASP   B 2  355 ? -5.159  -76.352  36.801  1.00 51.85  ? 355 ASP   B CA     1 
ATOM   6153  C  C      . ASP   B 2  355 ? -4.587  -75.858  35.479  1.00 58.60  ? 355 ASP   B C      1 
ATOM   6154  O  O      . ASP   B 2  355 ? -3.399  -75.532  35.396  1.00 59.70  ? 355 ASP   B O      1 
ATOM   6155  C  CB     . ASP   B 2  355 ? -5.399  -77.848  36.768  1.00 53.83  ? 355 ASP   B CB     1 
ATOM   6156  C  CG     . ASP   B 2  355 ? -5.520  -78.431  38.148  1.00 62.09  ? 355 ASP   B CG     1 
ATOM   6157  O  OD1    . ASP   B 2  355 ? -4.749  -78.012  39.043  1.00 51.50  ? 355 ASP   B OD1    1 
ATOM   6158  O  OD2    . ASP   B 2  355 ? -6.438  -79.250  38.354  1.00 74.53  ? 355 ASP   B OD2    1 
ATOM   6159  N  N      . ILE   B 2  356 ? -5.413  -75.772  34.442  1.00 56.28  ? 356 ILE   B N      1 
ATOM   6160  C  CA     . ILE   B 2  356 ? -4.891  -75.424  33.112  1.00 55.58  ? 356 ILE   B CA     1 
ATOM   6161  C  C      . ILE   B 2  356 ? -4.506  -73.949  33.078  1.00 56.27  ? 356 ILE   B C      1 
ATOM   6162  O  O      . ILE   B 2  356 ? -5.355  -73.091  33.376  1.00 57.41  ? 356 ILE   B O      1 
ATOM   6163  C  CB     . ILE   B 2  356 ? -5.930  -75.733  32.028  1.00 58.19  ? 356 ILE   B CB     1 
ATOM   6164  C  CG1    . ILE   B 2  356 ? -6.366  -77.198  32.067  1.00 57.10  ? 356 ILE   B CG1    1 
ATOM   6165  C  CG2    . ILE   B 2  356 ? -5.366  -75.404  30.651  1.00 61.21  ? 356 ILE   B CG2    1 
ATOM   6166  C  CD1    . ILE   B 2  356 ? -7.845  -77.369  32.137  1.00 58.11  ? 356 ILE   B CD1    1 
ATOM   6167  N  N      . PRO   B 2  357 ? -3.276  -73.597  32.696  1.00 57.55  ? 357 PRO   B N      1 
ATOM   6168  C  CA     . PRO   B 2  357 ? -2.953  -72.190  32.443  1.00 54.10  ? 357 PRO   B CA     1 
ATOM   6169  C  C      . PRO   B 2  357 ? -3.337  -71.812  31.024  1.00 55.59  ? 357 PRO   B C      1 
ATOM   6170  O  O      . PRO   B 2  357 ? -3.725  -72.676  30.224  1.00 59.00  ? 357 PRO   B O      1 
ATOM   6171  C  CB     . PRO   B 2  357 ? -1.429  -72.131  32.642  1.00 51.72  ? 357 PRO   B CB     1 
ATOM   6172  C  CG     . PRO   B 2  357 ? -0.939  -73.534  32.453  1.00 54.66  ? 357 PRO   B CG     1 
ATOM   6173  C  CD     . PRO   B 2  357 ? -2.147  -74.462  32.316  1.00 58.92  ? 357 PRO   B CD     1 
ATOM   6174  N  N      . PRO   B 2  358 ? -3.261  -70.538  30.673  1.00 53.12  ? 358 PRO   B N      1 
ATOM   6175  C  CA     . PRO   B 2  358 ? -3.533  -70.134  29.294  1.00 51.98  ? 358 PRO   B CA     1 
ATOM   6176  C  C      . PRO   B 2  358 ? -2.300  -70.285  28.419  1.00 58.49  ? 358 PRO   B C      1 
ATOM   6177  O  O      . PRO   B 2  358 ? -1.164  -70.205  28.890  1.00 58.33  ? 358 PRO   B O      1 
ATOM   6178  C  CB     . PRO   B 2  358 ? -3.915  -68.662  29.436  1.00 56.27  ? 358 PRO   B CB     1 
ATOM   6179  C  CG     . PRO   B 2  358 ? -3.168  -68.218  30.685  1.00 53.61  ? 358 PRO   B CG     1 
ATOM   6180  C  CD     . PRO   B 2  358 ? -3.175  -69.388  31.592  1.00 55.06  ? 358 PRO   B CD     1 
ATOM   6181  N  N      . ARG   B 2  359 ? -2.550  -70.508  27.123  1.00 60.21  ? 359 ARG   B N      1 
ATOM   6182  C  CA     . ARG   B 2  359 ? -1.493  -70.541  26.117  1.00 58.60  ? 359 ARG   B CA     1 
ATOM   6183  C  C      . ARG   B 2  359 ? -0.422  -69.497  26.405  1.00 63.31  ? 359 ARG   B C      1 
ATOM   6184  O  O      . ARG   B 2  359 ? -0.672  -68.291  26.327  1.00 61.40  ? 359 ARG   B O      1 
ATOM   6185  C  CB     . ARG   B 2  359 ? -2.083  -70.334  24.712  1.00 71.53  ? 359 ARG   B CB     1 
ATOM   6186  C  CG     . ARG   B 2  359 ? -1.155  -70.612  23.504  1.00 72.56  ? 359 ARG   B CG     1 
ATOM   6187  C  CD     . ARG   B 2  359 ? -0.360  -71.919  23.641  1.00 93.28  ? 359 ARG   B CD     1 
ATOM   6188  N  NE     . ARG   B 2  359 ? -1.071  -72.988  24.346  1.00 100.08 ? 359 ARG   B NE     1 
ATOM   6189  C  CZ     . ARG   B 2  359 ? -1.650  -74.036  23.768  1.00 97.85  ? 359 ARG   B CZ     1 
ATOM   6190  N  NH1    . ARG   B 2  359 ? -1.584  -74.231  22.456  1.00 97.02  ? 359 ARG   B NH1    1 
ATOM   6191  N  NH2    . ARG   B 2  359 ? -2.307  -74.914  24.525  1.00 90.44  ? 359 ARG   B NH2    1 
ATOM   6192  N  N      . GLY   B 2  360 ? 0.769   -69.951  26.765  1.00 65.42  ? 360 GLY   B N      1 
ATOM   6193  C  CA     . GLY   B 2  360 ? 1.911   -69.078  26.838  1.00 60.04  ? 360 GLY   B CA     1 
ATOM   6194  C  C      . GLY   B 2  360 ? 2.377   -68.737  28.228  1.00 62.00  ? 360 GLY   B C      1 
ATOM   6195  O  O      . GLY   B 2  360 ? 3.416   -68.088  28.365  1.00 69.79  ? 360 GLY   B O      1 
ATOM   6196  N  N      . LEU   B 2  361 ? 1.661   -69.138  29.263  1.00 58.87  ? 361 LEU   B N      1 
ATOM   6197  C  CA     . LEU   B 2  361 ? 2.126   -68.866  30.613  1.00 57.73  ? 361 LEU   B CA     1 
ATOM   6198  C  C      . LEU   B 2  361 ? 2.070   -70.154  31.412  1.00 57.23  ? 361 LEU   B C      1 
ATOM   6199  O  O      . LEU   B 2  361 ? 1.192   -70.991  31.181  1.00 60.81  ? 361 LEU   B O      1 
ATOM   6200  C  CB     . LEU   B 2  361 ? 1.285   -67.778  31.273  1.00 56.74  ? 361 LEU   B CB     1 
ATOM   6201  C  CG     . LEU   B 2  361 ? 1.370   -66.430  30.555  1.00 55.42  ? 361 LEU   B CG     1 
ATOM   6202  C  CD1    . LEU   B 2  361 ? 0.547   -65.367  31.261  1.00 63.34  ? 361 LEU   B CD1    1 
ATOM   6203  C  CD2    . LEU   B 2  361 ? 2.798   -65.979  30.420  1.00 62.88  ? 361 LEU   B CD2    1 
ATOM   6204  N  N      . LYS   B 2  362 ? 3.023   -70.339  32.328  1.00 59.70  ? 362 LYS   B N      1 
ATOM   6205  C  CA     . LYS   B 2  362 ? 2.914   -71.475  33.244  1.00 67.32  ? 362 LYS   B CA     1 
ATOM   6206  C  C      . LYS   B 2  362 ? 2.070   -71.158  34.462  1.00 64.68  ? 362 LYS   B C      1 
ATOM   6207  O  O      . LYS   B 2  362 ? 1.598   -72.086  35.128  1.00 66.22  ? 362 LYS   B O      1 
ATOM   6208  C  CB     . LYS   B 2  362 ? 4.291   -71.987  33.701  1.00 66.60  ? 362 LYS   B CB     1 
ATOM   6209  C  CG     . LYS   B 2  362 ? 4.909   -73.042  32.745  1.00 70.86  ? 362 LYS   B CG     1 
ATOM   6210  C  CD     . LYS   B 2  362 ? 6.173   -73.719  33.302  1.00 78.02  ? 362 LYS   B CD     1 
ATOM   6211  C  CE     . LYS   B 2  362 ? 7.269   -73.798  32.247  1.00 88.24  ? 362 LYS   B CE     1 
ATOM   6212  N  NZ     . LYS   B 2  362 ? 6.701   -74.143  30.907  1.00 92.83  ? 362 LYS   B NZ     1 
ATOM   6213  N  N      . MET   B 2  363 ? 1.869   -69.876  34.754  1.00 63.26  ? 363 MET   B N      1 
ATOM   6214  C  CA     . MET   B 2  363 ? 0.972   -69.434  35.808  1.00 60.92  ? 363 MET   B CA     1 
ATOM   6215  C  C      . MET   B 2  363 ? 0.556   -67.997  35.570  1.00 55.22  ? 363 MET   B C      1 
ATOM   6216  O  O      . MET   B 2  363 ? 1.355   -67.173  35.112  1.00 56.12  ? 363 MET   B O      1 
ATOM   6217  C  CB     . MET   B 2  363 ? 1.601   -69.560  37.192  1.00 61.42  ? 363 MET   B CB     1 
ATOM   6218  C  CG     . MET   B 2  363 ? 1.932   -70.956  37.617  1.00 61.41  ? 363 MET   B CG     1 
ATOM   6219  S  SD     . MET   B 2  363 ? 2.195   -70.730  39.354  1.00 71.35  ? 363 MET   B SD     1 
ATOM   6220  C  CE     . MET   B 2  363 ? 3.039   -69.156  39.258  1.00 59.52  ? 363 MET   B CE     1 
ATOM   6221  N  N      . SER   B 2  364 ? -0.696  -67.708  35.921  1.00 49.00  ? 364 SER   B N      1 
ATOM   6222  C  CA     . SER   B 2  364 ? -1.272  -66.384  35.734  1.00 53.21  ? 364 SER   B CA     1 
ATOM   6223  C  C      . SER   B 2  364 ? -2.449  -66.197  36.681  1.00 51.47  ? 364 SER   B C      1 
ATOM   6224  O  O      . SER   B 2  364 ? -3.068  -67.162  37.145  1.00 52.26  ? 364 SER   B O      1 
ATOM   6225  C  CB     . SER   B 2  364 ? -1.690  -66.154  34.271  1.00 58.16  ? 364 SER   B CB     1 
ATOM   6226  O  OG     . SER   B 2  364 ? -2.551  -67.172  33.784  1.00 60.89  ? 364 SER   B OG     1 
ATOM   6227  N  N      . ALA   B 2  365 ? -2.730  -64.928  36.973  1.00 48.39  ? 365 ALA   B N      1 
ATOM   6228  C  CA     . ALA   B 2  365 ? -3.821  -64.513  37.845  1.00 48.29  ? 365 ALA   B CA     1 
ATOM   6229  C  C      . ALA   B 2  365 ? -4.675  -63.478  37.125  1.00 52.88  ? 365 ALA   B C      1 
ATOM   6230  O  O      . ALA   B 2  365 ? -4.144  -62.468  36.644  1.00 54.86  ? 365 ALA   B O      1 
ATOM   6231  C  CB     . ALA   B 2  365 ? -3.293  -63.912  39.145  1.00 48.86  ? 365 ALA   B CB     1 
ATOM   6232  N  N      . THR   B 2  366 ? -5.990  -63.720  37.056  1.00 46.09  ? 366 THR   B N      1 
ATOM   6233  C  CA     . THR   B 2  366 ? -6.947  -62.722  36.592  1.00 44.24  ? 366 THR   B CA     1 
ATOM   6234  C  C      . THR   B 2  366 ? -7.715  -62.174  37.783  1.00 48.69  ? 366 THR   B C      1 
ATOM   6235  O  O      . THR   B 2  366 ? -8.020  -62.910  38.728  1.00 50.83  ? 366 THR   B O      1 
ATOM   6236  C  CB     . THR   B 2  366 ? -7.942  -63.279  35.589  1.00 44.56  ? 366 THR   B CB     1 
ATOM   6237  O  OG1    . THR   B 2  366 ? -7.236  -63.836  34.476  1.00 50.56  ? 366 THR   B OG1    1 
ATOM   6238  C  CG2    . THR   B 2  366 ? -8.822  -62.141  35.109  1.00 43.13  ? 366 THR   B CG2    1 
ATOM   6239  N  N      . PHE   B 2  367 ? -8.031  -60.883  37.730  1.00 47.51  ? 367 PHE   B N      1 
ATOM   6240  C  CA     . PHE   B 2  367 ? -8.567  -60.159  38.872  1.00 43.00  ? 367 PHE   B CA     1 
ATOM   6241  C  C      . PHE   B 2  367 ? -9.833  -59.429  38.452  1.00 46.20  ? 367 PHE   B C      1 
ATOM   6242  O  O      . PHE   B 2  367 ? -9.840  -58.751  37.421  1.00 44.03  ? 367 PHE   B O      1 
ATOM   6243  C  CB     . PHE   B 2  367 ? -7.512  -59.199  39.395  1.00 42.80  ? 367 PHE   B CB     1 
ATOM   6244  C  CG     . PHE   B 2  367 ? -8.046  -58.101  40.222  1.00 41.56  ? 367 PHE   B CG     1 
ATOM   6245  C  CD1    . PHE   B 2  367 ? -8.423  -56.916  39.653  1.00 44.84  ? 367 PHE   B CD1    1 
ATOM   6246  C  CD2    . PHE   B 2  367 ? -8.125  -58.231  41.577  1.00 43.03  ? 367 PHE   B CD2    1 
ATOM   6247  C  CE1    . PHE   B 2  367 ? -8.903  -55.891  40.436  1.00 47.14  ? 367 PHE   B CE1    1 
ATOM   6248  C  CE2    . PHE   B 2  367 ? -8.586  -57.210  42.357  1.00 47.21  ? 367 PHE   B CE2    1 
ATOM   6249  C  CZ     . PHE   B 2  367 ? -8.981  -56.038  41.789  1.00 44.95  ? 367 PHE   B CZ     1 
ATOM   6250  N  N      . ILE   B 2  368 ? -10.904 -59.593  39.231  1.00 40.45  ? 368 ILE   B N      1 
ATOM   6251  C  CA     . ILE   B 2  368 ? -12.172 -58.918  39.000  1.00 33.68  ? 368 ILE   B CA     1 
ATOM   6252  C  C      . ILE   B 2  368 ? -12.486 -58.093  40.238  1.00 38.59  ? 368 ILE   B C      1 
ATOM   6253  O  O      . ILE   B 2  368 ? -12.859 -58.653  41.276  1.00 43.98  ? 368 ILE   B O      1 
ATOM   6254  C  CB     . ILE   B 2  368 ? -13.302 -59.906  38.716  1.00 37.43  ? 368 ILE   B CB     1 
ATOM   6255  C  CG1    . ILE   B 2  368 ? -12.928 -60.865  37.609  1.00 38.95  ? 368 ILE   B CG1    1 
ATOM   6256  C  CG2    . ILE   B 2  368 ? -14.578 -59.182  38.315  1.00 37.93  ? 368 ILE   B CG2    1 
ATOM   6257  C  CD1    . ILE   B 2  368 ? -13.927 -61.974  37.483  1.00 37.84  ? 368 ILE   B CD1    1 
ATOM   6258  N  N      . GLY   B 2  369 ? -12.378 -56.771  40.130  1.00 36.58  ? 369 GLY   B N      1 
ATOM   6259  C  CA     . GLY   B 2  369 ? -12.601 -55.865  41.253  1.00 35.53  ? 369 GLY   B CA     1 
ATOM   6260  C  C      . GLY   B 2  369 ? -13.796 -54.955  41.051  1.00 39.68  ? 369 GLY   B C      1 
ATOM   6261  O  O      . GLY   B 2  369 ? -13.916 -54.271  40.031  1.00 40.52  ? 369 GLY   B O      1 
ATOM   6262  N  N      . ASN   B 2  370 ? -14.682 -54.938  42.049  1.00 39.68  ? 370 ASN   B N      1 
ATOM   6263  C  CA     . ASN   B 2  370 ? -15.750 -53.956  42.158  1.00 33.59  ? 370 ASN   B CA     1 
ATOM   6264  C  C      . ASN   B 2  370 ? -15.317 -52.923  43.194  1.00 37.61  ? 370 ASN   B C      1 
ATOM   6265  O  O      . ASN   B 2  370 ? -15.752 -52.927  44.342  1.00 35.92  ? 370 ASN   B O      1 
ATOM   6266  C  CB     . ASN   B 2  370 ? -17.055 -54.639  42.520  1.00 33.01  ? 370 ASN   B CB     1 
ATOM   6267  C  CG     . ASN   B 2  370 ? -18.264 -53.736  42.346  1.00 41.25  ? 370 ASN   B CG     1 
ATOM   6268  O  OD1    . ASN   B 2  370 ? -18.152 -52.504  42.260  1.00 40.27  ? 370 ASN   B OD1    1 
ATOM   6269  N  ND2    . ASN   B 2  370 ? -19.435 -54.357  42.226  1.00 39.56  ? 370 ASN   B ND2    1 
ATOM   6270  N  N      . SER   B 2  371 ? -14.412 -52.046  42.754  1.00 40.60  ? 371 SER   B N      1 
ATOM   6271  C  CA     . SER   B 2  371 ? -13.913 -50.905  43.508  1.00 40.09  ? 371 SER   B CA     1 
ATOM   6272  C  C      . SER   B 2  371 ? -14.788 -49.666  43.328  1.00 43.20  ? 371 SER   B C      1 
ATOM   6273  O  O      . SER   B 2  371 ? -15.275 -49.382  42.231  1.00 45.92  ? 371 SER   B O      1 
ATOM   6274  C  CB     . SER   B 2  371 ? -12.497 -50.568  43.051  1.00 40.22  ? 371 SER   B CB     1 
ATOM   6275  O  OG     . SER   B 2  371 ? -12.133 -49.295  43.558  1.00 45.18  ? 371 SER   B OG     1 
ATOM   6276  N  N      . THR   B 2  372 ? -14.948 -48.893  44.401  1.00 44.85  ? 372 THR   B N      1 
ATOM   6277  C  CA     . THR   B 2  372 ? -15.578 -47.591  44.220  1.00 47.00  ? 372 THR   B CA     1 
ATOM   6278  C  C      . THR   B 2  372 ? -14.675 -46.637  43.451  1.00 48.02  ? 372 THR   B C      1 
ATOM   6279  O  O      . THR   B 2  372 ? -15.082 -45.511  43.161  1.00 53.60  ? 372 THR   B O      1 
ATOM   6280  C  CB     . THR   B 2  372 ? -15.958 -46.941  45.559  1.00 47.41  ? 372 THR   B CB     1 
ATOM   6281  O  OG1    . THR   B 2  372 ? -14.788 -46.702  46.340  1.00 47.87  ? 372 THR   B OG1    1 
ATOM   6282  C  CG2    . THR   B 2  372 ? -16.863 -47.861  46.345  1.00 46.01  ? 372 THR   B CG2    1 
ATOM   6283  N  N      . ALA   B 2  373 ? -13.457 -47.044  43.124  1.00 42.11  ? 373 ALA   B N      1 
ATOM   6284  C  CA     . ALA   B 2  373 ? -12.612 -46.139  42.371  1.00 42.97  ? 373 ALA   B CA     1 
ATOM   6285  C  C      . ALA   B 2  373 ? -12.977 -46.096  40.892  1.00 42.35  ? 373 ALA   B C      1 
ATOM   6286  O  O      . ALA   B 2  373 ? -12.491 -45.213  40.178  1.00 42.42  ? 373 ALA   B O      1 
ATOM   6287  C  CB     . ALA   B 2  373 ? -11.149 -46.530  42.564  1.00 48.85  ? 373 ALA   B CB     1 
ATOM   6288  N  N      . ILE   B 2  374 ? -13.818 -47.016  40.408  1.00 44.36  ? 374 ILE   B N      1 
ATOM   6289  C  CA     . ILE   B 2  374 ? -14.263 -46.930  39.020  1.00 37.25  ? 374 ILE   B CA     1 
ATOM   6290  C  C      . ILE   B 2  374 ? -14.950 -45.609  38.737  1.00 39.25  ? 374 ILE   B C      1 
ATOM   6291  O  O      . ILE   B 2  374 ? -14.983 -45.166  37.586  1.00 37.88  ? 374 ILE   B O      1 
ATOM   6292  C  CB     . ILE   B 2  374 ? -15.189 -48.090  38.657  1.00 31.96  ? 374 ILE   B CB     1 
ATOM   6293  C  CG1    . ILE   B 2  374 ? -15.332 -48.182  37.136  1.00 35.39  ? 374 ILE   B CG1    1 
ATOM   6294  C  CG2    . ILE   B 2  374 ? -16.531 -47.859  39.269  1.00 36.42  ? 374 ILE   B CG2    1 
ATOM   6295  C  CD1    . ILE   B 2  374 ? -14.296 -48.976  36.418  1.00 32.80  ? 374 ILE   B CD1    1 
ATOM   6296  N  N      . GLN   B 2  375 ? -15.495 -44.948  39.752  1.00 36.51  ? 375 GLN   B N      1 
ATOM   6297  C  CA     . GLN   B 2  375 ? -16.067 -43.643  39.482  1.00 39.49  ? 375 GLN   B CA     1 
ATOM   6298  C  C      . GLN   B 2  375 ? -15.080 -42.771  38.726  1.00 42.60  ? 375 GLN   B C      1 
ATOM   6299  O  O      . GLN   B 2  375 ? -15.457 -42.080  37.781  1.00 43.34  ? 375 GLN   B O      1 
ATOM   6300  C  CB     . GLN   B 2  375 ? -16.486 -42.951  40.765  1.00 47.07  ? 375 GLN   B CB     1 
ATOM   6301  C  CG     . GLN   B 2  375 ? -15.354 -42.671  41.698  1.00 48.68  ? 375 GLN   B CG     1 
ATOM   6302  C  CD     . GLN   B 2  375 ? -15.755 -41.713  42.791  1.00 56.62  ? 375 GLN   B CD     1 
ATOM   6303  O  OE1    . GLN   B 2  375 ? -16.087 -40.553  42.528  1.00 63.41  ? 375 GLN   B OE1    1 
ATOM   6304  N  NE2    . GLN   B 2  375 ? -15.744 -42.190  44.022  1.00 58.41  ? 375 GLN   B NE2    1 
ATOM   6305  N  N      . GLU   B 2  376 ? -13.803 -42.801  39.115  1.00 43.70  ? 376 GLU   B N      1 
ATOM   6306  C  CA     . GLU   B 2  376 ? -12.787 -42.057  38.380  1.00 39.62  ? 376 GLU   B CA     1 
ATOM   6307  C  C      . GLU   B 2  376 ? -12.985 -42.209  36.879  1.00 41.35  ? 376 GLU   B C      1 
ATOM   6308  O  O      . GLU   B 2  376 ? -12.843 -41.236  36.130  1.00 41.24  ? 376 GLU   B O      1 
ATOM   6309  C  CB     . GLU   B 2  376 ? -11.368 -42.485  38.775  1.00 34.72  ? 376 GLU   B CB     1 
ATOM   6310  C  CG     . GLU   B 2  376 ? -10.933 -41.946  40.132  1.00 46.50  ? 376 GLU   B CG     1 
ATOM   6311  C  CD     . GLU   B 2  376 ? -9.455  -42.204  40.488  1.00 60.78  ? 376 GLU   B CD     1 
ATOM   6312  O  OE1    . GLU   B 2  376 ? -8.760  -42.975  39.780  1.00 61.88  ? 376 GLU   B OE1    1 
ATOM   6313  O  OE2    . GLU   B 2  376 ? -8.992  -41.618  41.495  1.00 58.00  ? 376 GLU   B OE2    1 
ATOM   6314  N  N      . LEU   B 2  377 ? -13.317 -43.421  36.431  1.00 39.60  ? 377 LEU   B N      1 
ATOM   6315  C  CA     . LEU   B 2  377 ? -13.565 -43.636  35.011  1.00 42.41  ? 377 LEU   B CA     1 
ATOM   6316  C  C      . LEU   B 2  377 ? -14.701 -42.737  34.524  1.00 45.80  ? 377 LEU   B C      1 
ATOM   6317  O  O      . LEU   B 2  377 ? -14.525 -41.920  33.608  1.00 42.08  ? 377 LEU   B O      1 
ATOM   6318  C  CB     . LEU   B 2  377 ? -13.882 -45.115  34.749  1.00 35.51  ? 377 LEU   B CB     1 
ATOM   6319  C  CG     . LEU   B 2  377 ? -13.847 -45.580  33.291  1.00 37.36  ? 377 LEU   B CG     1 
ATOM   6320  C  CD1    . LEU   B 2  377 ? -14.043 -47.050  33.184  1.00 40.16  ? 377 LEU   B CD1    1 
ATOM   6321  C  CD2    . LEU   B 2  377 ? -14.896 -44.895  32.477  1.00 44.68  ? 377 LEU   B CD2    1 
ATOM   6322  N  N      . PHE   B 2  378 ? -15.883 -42.884  35.137  1.00 43.09  ? 378 PHE   B N      1 
ATOM   6323  C  CA     . PHE   B 2  378 ? -17.070 -42.161  34.697  1.00 38.29  ? 378 PHE   B CA     1 
ATOM   6324  C  C      . PHE   B 2  378 ? -16.914 -40.658  34.863  1.00 39.06  ? 378 PHE   B C      1 
ATOM   6325  O  O      . PHE   B 2  378 ? -17.392 -39.890  34.031  1.00 45.38  ? 378 PHE   B O      1 
ATOM   6326  C  CB     . PHE   B 2  378 ? -18.278 -42.662  35.467  1.00 34.04  ? 378 PHE   B CB     1 
ATOM   6327  C  CG     . PHE   B 2  378 ? -18.549 -44.113  35.256  1.00 37.47  ? 378 PHE   B CG     1 
ATOM   6328  C  CD1    . PHE   B 2  378 ? -18.823 -44.597  33.985  1.00 42.97  ? 378 PHE   B CD1    1 
ATOM   6329  C  CD2    . PHE   B 2  378 ? -18.544 -44.996  36.309  1.00 34.13  ? 378 PHE   B CD2    1 
ATOM   6330  C  CE1    . PHE   B 2  378 ? -19.093 -45.945  33.774  1.00 41.78  ? 378 PHE   B CE1    1 
ATOM   6331  C  CE2    . PHE   B 2  378 ? -18.810 -46.343  36.109  1.00 38.62  ? 378 PHE   B CE2    1 
ATOM   6332  C  CZ     . PHE   B 2  378 ? -19.079 -46.823  34.842  1.00 40.79  ? 378 PHE   B CZ     1 
ATOM   6333  N  N      . LYS   B 2  379 ? -16.270 -40.209  35.933  1.00 40.07  ? 379 LYS   B N      1 
ATOM   6334  C  CA     . LYS   B 2  379 ? -15.959 -38.789  36.038  1.00 41.88  ? 379 LYS   B CA     1 
ATOM   6335  C  C      . LYS   B 2  379 ? -15.204 -38.336  34.804  1.00 39.32  ? 379 LYS   B C      1 
ATOM   6336  O  O      . LYS   B 2  379 ? -15.465 -37.261  34.266  1.00 40.23  ? 379 LYS   B O      1 
ATOM   6337  C  CB     . LYS   B 2  379 ? -15.125 -38.514  37.295  1.00 46.59  ? 379 LYS   B CB     1 
ATOM   6338  C  CG     . LYS   B 2  379 ? -15.901 -38.537  38.613  1.00 53.30  ? 379 LYS   B CG     1 
ATOM   6339  C  CD     . LYS   B 2  379 ? -15.016 -38.115  39.806  1.00 65.08  ? 379 LYS   B CD     1 
ATOM   6340  C  CE     . LYS   B 2  379 ? -15.817 -37.992  41.119  1.00 74.87  ? 379 LYS   B CE     1 
ATOM   6341  N  NZ     . LYS   B 2  379 ? -15.145 -37.172  42.178  1.00 87.56  ? 379 LYS   B NZ     1 
ATOM   6342  N  N      . ARG   B 2  380 ? -14.268 -39.156  34.331  1.00 38.26  ? 380 ARG   B N      1 
ATOM   6343  C  CA     . ARG   B 2  380 ? -13.471 -38.749  33.184  1.00 37.69  ? 380 ARG   B CA     1 
ATOM   6344  C  C      . ARG   B 2  380 ? -14.355 -38.601  31.959  1.00 40.15  ? 380 ARG   B C      1 
ATOM   6345  O  O      . ARG   B 2  380 ? -14.232 -37.645  31.191  1.00 40.12  ? 380 ARG   B O      1 
ATOM   6346  C  CB     . ARG   B 2  380 ? -12.355 -39.761  32.939  1.00 33.17  ? 380 ARG   B CB     1 
ATOM   6347  C  CG     . ARG   B 2  380 ? -11.494 -39.465  31.740  1.00 33.60  ? 380 ARG   B CG     1 
ATOM   6348  C  CD     . ARG   B 2  380 ? -10.521 -40.577  31.528  1.00 42.02  ? 380 ARG   B CD     1 
ATOM   6349  N  NE     . ARG   B 2  380 ? -11.047 -41.618  30.652  1.00 52.11  ? 380 ARG   B NE     1 
ATOM   6350  C  CZ     . ARG   B 2  380 ? -10.808 -42.914  30.832  1.00 58.17  ? 380 ARG   B CZ     1 
ATOM   6351  N  NH1    . ARG   B 2  380 ? -10.183 -43.361  31.920  1.00 52.37  ? 380 ARG   B NH1    1 
ATOM   6352  N  NH2    . ARG   B 2  380 ? -11.247 -43.790  29.928  1.00 52.34  ? 380 ARG   B NH2    1 
ATOM   6353  N  N      . ILE   B 2  381 ? -15.293 -39.518  31.784  1.00 43.58  ? 381 ILE   B N      1 
ATOM   6354  C  CA     . ILE   B 2  381 ? -16.126 -39.453  30.604  1.00 39.02  ? 381 ILE   B CA     1 
ATOM   6355  C  C      . ILE   B 2  381 ? -17.164 -38.356  30.759  1.00 44.20  ? 381 ILE   B C      1 
ATOM   6356  O  O      . ILE   B 2  381 ? -17.558 -37.726  29.774  1.00 47.91  ? 381 ILE   B O      1 
ATOM   6357  C  CB     . ILE   B 2  381 ? -16.733 -40.836  30.361  1.00 36.30  ? 381 ILE   B CB     1 
ATOM   6358  C  CG1    . ILE   B 2  381 ? -15.584 -41.788  30.017  1.00 37.78  ? 381 ILE   B CG1    1 
ATOM   6359  C  CG2    . ILE   B 2  381 ? -17.749 -40.761  29.267  1.00 38.01  ? 381 ILE   B CG2    1 
ATOM   6360  C  CD1    . ILE   B 2  381 ? -15.972 -43.173  29.606  1.00 35.88  ? 381 ILE   B CD1    1 
ATOM   6361  N  N      . SER   B 2  382 ? -17.588 -38.063  31.986  1.00 39.41  ? 382 SER   B N      1 
ATOM   6362  C  CA     . SER   B 2  382 ? -18.560 -36.996  32.182  1.00 38.05  ? 382 SER   B CA     1 
ATOM   6363  C  C      . SER   B 2  382 ? -17.949 -35.621  31.917  1.00 41.21  ? 382 SER   B C      1 
ATOM   6364  O  O      . SER   B 2  382 ? -18.614 -34.740  31.365  1.00 42.93  ? 382 SER   B O      1 
ATOM   6365  C  CB     . SER   B 2  382 ? -19.142 -37.067  33.592  1.00 39.07  ? 382 SER   B CB     1 
ATOM   6366  O  OG     . SER   B 2  382 ? -20.406 -36.426  33.656  1.00 46.32  ? 382 SER   B OG     1 
ATOM   6367  N  N      . GLU   B 2  383 ? -16.696 -35.403  32.315  1.00 41.89  ? 383 GLU   B N      1 
ATOM   6368  C  CA     . GLU   B 2  383 ? -16.045 -34.138  31.997  1.00 39.78  ? 383 GLU   B CA     1 
ATOM   6369  C  C      . GLU   B 2  383 ? -15.933 -33.938  30.493  1.00 41.33  ? 383 GLU   B C      1 
ATOM   6370  O  O      . GLU   B 2  383 ? -16.360 -32.905  29.963  1.00 41.13  ? 383 GLU   B O      1 
ATOM   6371  C  CB     . GLU   B 2  383 ? -14.664 -34.072  32.639  1.00 43.56  ? 383 GLU   B CB     1 
ATOM   6372  C  CG     . GLU   B 2  383 ? -14.662 -34.079  34.130  1.00 53.62  ? 383 GLU   B CG     1 
ATOM   6373  C  CD     . GLU   B 2  383 ? -13.251 -34.045  34.694  1.00 75.86  ? 383 GLU   B CD     1 
ATOM   6374  O  OE1    . GLU   B 2  383 ? -12.397 -33.339  34.097  1.00 80.74  ? 383 GLU   B OE1    1 
ATOM   6375  O  OE2    . GLU   B 2  383 ? -13.010 -34.687  35.751  1.00 80.44  ? 383 GLU   B OE2    1 
ATOM   6376  N  N      . GLN   B 2  384 ? -15.322 -34.902  29.793  1.00 36.24  ? 384 GLN   B N      1 
ATOM   6377  C  CA     . GLN   B 2  384 ? -15.221 -34.815  28.341  1.00 37.59  ? 384 GLN   B CA     1 
ATOM   6378  C  C      . GLN   B 2  384 ? -16.593 -34.574  27.724  1.00 39.43  ? 384 GLN   B C      1 
ATOM   6379  O  O      . GLN   B 2  384 ? -16.729 -33.837  26.743  1.00 38.30  ? 384 GLN   B O      1 
ATOM   6380  C  CB     . GLN   B 2  384 ? -14.605 -36.101  27.789  1.00 37.14  ? 384 GLN   B CB     1 
ATOM   6381  C  CG     . GLN   B 2  384 ? -13.374 -36.557  28.578  1.00 44.71  ? 384 GLN   B CG     1 
ATOM   6382  C  CD     . GLN   B 2  384 ? -12.821 -37.904  28.136  1.00 47.72  ? 384 GLN   B CD     1 
ATOM   6383  O  OE1    . GLN   B 2  384 ? -13.479 -38.644  27.415  1.00 54.39  ? 384 GLN   B OE1    1 
ATOM   6384  N  NE2    . GLN   B 2  384 ? -11.625 -38.243  28.606  1.00 44.60  ? 384 GLN   B NE2    1 
ATOM   6385  N  N      . PHE   B 2  385 ? -17.624 -35.176  28.299  1.00 37.29  ? 385 PHE   B N      1 
ATOM   6386  C  CA     . PHE   B 2  385 ? -18.969 -34.976  27.799  1.00 35.78  ? 385 PHE   B CA     1 
ATOM   6387  C  C      . PHE   B 2  385 ? -19.368 -33.510  27.874  1.00 34.94  ? 385 PHE   B C      1 
ATOM   6388  O  O      . PHE   B 2  385 ? -19.721 -32.893  26.869  1.00 39.10  ? 385 PHE   B O      1 
ATOM   6389  C  CB     . PHE   B 2  385 ? -19.932 -35.847  28.596  1.00 37.23  ? 385 PHE   B CB     1 
ATOM   6390  C  CG     . PHE   B 2  385 ? -21.366 -35.688  28.197  1.00 37.38  ? 385 PHE   B CG     1 
ATOM   6391  C  CD1    . PHE   B 2  385 ? -22.130 -34.636  28.683  1.00 35.32  ? 385 PHE   B CD1    1 
ATOM   6392  C  CD2    . PHE   B 2  385 ? -21.952 -36.602  27.332  1.00 31.47  ? 385 PHE   B CD2    1 
ATOM   6393  C  CE1    . PHE   B 2  385 ? -23.446 -34.509  28.326  1.00 39.42  ? 385 PHE   B CE1    1 
ATOM   6394  C  CE2    . PHE   B 2  385 ? -23.261 -36.471  26.966  1.00 34.48  ? 385 PHE   B CE2    1 
ATOM   6395  C  CZ     . PHE   B 2  385 ? -24.015 -35.422  27.461  1.00 38.50  ? 385 PHE   B CZ     1 
ATOM   6396  N  N      . THR   B 2  386 ? -19.348 -32.937  29.062  1.00 34.79  ? 386 THR   B N      1 
ATOM   6397  C  CA     . THR   B 2  386 ? -19.905 -31.602  29.181  1.00 37.25  ? 386 THR   B CA     1 
ATOM   6398  C  C      . THR   B 2  386 ? -19.004 -30.552  28.564  1.00 35.31  ? 386 THR   B C      1 
ATOM   6399  O  O      . THR   B 2  386 ? -19.485 -29.470  28.224  1.00 38.16  ? 386 THR   B O      1 
ATOM   6400  C  CB     . THR   B 2  386 ? -20.169 -31.258  30.634  1.00 35.26  ? 386 THR   B CB     1 
ATOM   6401  O  OG1    . THR   B 2  386 ? -18.919 -31.162  31.294  1.00 38.68  ? 386 THR   B OG1    1 
ATOM   6402  C  CG2    . THR   B 2  386 ? -20.947 -32.376  31.304  1.00 44.27  ? 386 THR   B CG2    1 
ATOM   6403  N  N      . ALA   B 2  387 ? -17.714 -30.829  28.401  1.00 34.43  ? 387 ALA   B N      1 
ATOM   6404  C  CA     . ALA   B 2  387 ? -16.882 -29.863  27.697  1.00 35.16  ? 387 ALA   B CA     1 
ATOM   6405  C  C      . ALA   B 2  387 ? -17.518 -29.482  26.375  1.00 39.71  ? 387 ALA   B C      1 
ATOM   6406  O  O      . ALA   B 2  387 ? -17.545 -28.305  26.001  1.00 44.75  ? 387 ALA   B O      1 
ATOM   6407  C  CB     . ALA   B 2  387 ? -15.492 -30.422  27.470  1.00 29.81  ? 387 ALA   B CB     1 
ATOM   6408  N  N      . MET   B 2  388 ? -18.065 -30.472  25.673  1.00 34.93  ? 388 MET   B N      1 
ATOM   6409  C  CA     . MET   B 2  388 ? -18.756 -30.252  24.418  1.00 30.87  ? 388 MET   B CA     1 
ATOM   6410  C  C      . MET   B 2  388 ? -20.204 -29.829  24.631  1.00 39.95  ? 388 MET   B C      1 
ATOM   6411  O  O      . MET   B 2  388 ? -20.655 -28.855  24.022  1.00 43.23  ? 388 MET   B O      1 
ATOM   6412  C  CB     . MET   B 2  388 ? -18.689 -31.520  23.600  1.00 30.27  ? 388 MET   B CB     1 
ATOM   6413  C  CG     . MET   B 2  388 ? -17.291 -31.866  23.202  1.00 30.80  ? 388 MET   B CG     1 
ATOM   6414  S  SD     . MET   B 2  388 ? -17.220 -33.420  22.297  1.00 39.11  ? 388 MET   B SD     1 
ATOM   6415  C  CE     . MET   B 2  388 ? -17.979 -34.578  23.432  1.00 34.94  ? 388 MET   B CE     1 
ATOM   6416  N  N      . PHE   B 2  389 ? -20.938 -30.519  25.517  1.00 41.10  ? 389 PHE   B N      1 
ATOM   6417  C  CA     . PHE   B 2  389 ? -22.376 -30.283  25.658  1.00 37.10  ? 389 PHE   B CA     1 
ATOM   6418  C  C      . PHE   B 2  389 ? -22.682 -28.875  26.140  1.00 36.04  ? 389 PHE   B C      1 
ATOM   6419  O  O      . PHE   B 2  389 ? -23.722 -28.306  25.763  1.00 37.16  ? 389 PHE   B O      1 
ATOM   6420  C  CB     . PHE   B 2  389 ? -22.973 -31.292  26.637  1.00 38.50  ? 389 PHE   B CB     1 
ATOM   6421  C  CG     . PHE   B 2  389 ? -24.486 -31.422  26.577  1.00 33.86  ? 389 PHE   B CG     1 
ATOM   6422  C  CD1    . PHE   B 2  389 ? -25.100 -31.959  25.472  1.00 38.22  ? 389 PHE   B CD1    1 
ATOM   6423  C  CD2    . PHE   B 2  389 ? -25.279 -31.063  27.653  1.00 35.14  ? 389 PHE   B CD2    1 
ATOM   6424  C  CE1    . PHE   B 2  389 ? -26.484 -32.114  25.442  1.00 42.84  ? 389 PHE   B CE1    1 
ATOM   6425  C  CE2    . PHE   B 2  389 ? -26.650 -31.216  27.624  1.00 34.06  ? 389 PHE   B CE2    1 
ATOM   6426  C  CZ     . PHE   B 2  389 ? -27.257 -31.738  26.522  1.00 34.64  ? 389 PHE   B CZ     1 
ATOM   6427  N  N      . ARG   B 2  390 ? -21.825 -28.303  27.000  1.00 32.38  ? 390 ARG   B N      1 
ATOM   6428  C  CA     . ARG   B 2  390 ? -22.139 -26.967  27.496  1.00 34.62  ? 390 ARG   B CA     1 
ATOM   6429  C  C      . ARG   B 2  390 ? -22.144 -25.955  26.356  1.00 37.54  ? 390 ARG   B C      1 
ATOM   6430  O  O      . ARG   B 2  390 ? -22.602 -24.821  26.527  1.00 40.54  ? 390 ARG   B O      1 
ATOM   6431  C  CB     . ARG   B 2  390 ? -21.148 -26.521  28.570  1.00 32.92  ? 390 ARG   B CB     1 
ATOM   6432  C  CG     . ARG   B 2  390 ? -19.775 -26.284  27.986  1.00 46.50  ? 390 ARG   B CG     1 
ATOM   6433  C  CD     . ARG   B 2  390 ? -18.688 -25.844  28.959  1.00 52.49  ? 390 ARG   B CD     1 
ATOM   6434  N  NE     . ARG   B 2  390 ? -17.394 -25.948  28.282  1.00 52.35  ? 390 ARG   B NE     1 
ATOM   6435  C  CZ     . ARG   B 2  390 ? -16.216 -25.713  28.851  1.00 64.22  ? 390 ARG   B CZ     1 
ATOM   6436  N  NH1    . ARG   B 2  390 ? -16.119 -25.258  30.096  1.00 67.08  ? 390 ARG   B NH1    1 
ATOM   6437  N  NH2    . ARG   B 2  390 ? -15.106 -25.935  28.150  1.00 57.58  ? 390 ARG   B NH2    1 
ATOM   6438  N  N      . ARG   B 2  391 ? -21.644 -26.354  25.195  1.00 35.86  ? 391 ARG   B N      1 
ATOM   6439  C  CA     . ARG   B 2  391 ? -21.653 -25.548  23.993  1.00 30.38  ? 391 ARG   B CA     1 
ATOM   6440  C  C      . ARG   B 2  391 ? -22.462 -26.255  22.917  1.00 31.45  ? 391 ARG   B C      1 
ATOM   6441  O  O      . ARG   B 2  391 ? -22.314 -25.977  21.727  1.00 34.84  ? 391 ARG   B O      1 
ATOM   6442  C  CB     . ARG   B 2  391 ? -20.213 -25.303  23.547  1.00 36.77  ? 391 ARG   B CB     1 
ATOM   6443  C  CG     . ARG   B 2  391 ? -19.398 -24.355  24.451  1.00 31.95  ? 391 ARG   B CG     1 
ATOM   6444  C  CD     . ARG   B 2  391 ? -20.076 -23.062  24.634  1.00 33.76  ? 391 ARG   B CD     1 
ATOM   6445  N  NE     . ARG   B 2  391 ? -19.605 -22.126  23.626  1.00 34.62  ? 391 ARG   B NE     1 
ATOM   6446  C  CZ     . ARG   B 2  391 ? -18.367 -21.667  23.547  1.00 38.05  ? 391 ARG   B CZ     1 
ATOM   6447  N  NH1    . ARG   B 2  391 ? -17.457 -21.976  24.451  1.00 42.66  ? 391 ARG   B NH1    1 
ATOM   6448  N  NH2    . ARG   B 2  391 ? -18.032 -20.880  22.532  1.00 38.30  ? 391 ARG   B NH2    1 
ATOM   6449  N  N      . LYS   B 2  392 ? -23.291 -27.204  23.324  1.00 33.21  ? 392 LYS   B N      1 
ATOM   6450  C  CA     . LYS   B 2  392 ? -24.109 -27.966  22.396  1.00 34.89  ? 392 LYS   B CA     1 
ATOM   6451  C  C      . LYS   B 2  392 ? -23.336 -28.361  21.138  1.00 31.00  ? 392 LYS   B C      1 
ATOM   6452  O  O      . LYS   B 2  392 ? -23.924 -28.427  20.065  1.00 31.48  ? 392 LYS   B O      1 
ATOM   6453  C  CB     . LYS   B 2  392 ? -25.361 -27.160  22.048  1.00 33.99  ? 392 LYS   B CB     1 
ATOM   6454  C  CG     . LYS   B 2  392 ? -26.486 -27.264  23.102  1.00 45.48  ? 392 LYS   B CG     1 
ATOM   6455  C  CD     . LYS   B 2  392 ? -27.161 -25.909  23.445  1.00 55.72  ? 392 LYS   B CD     1 
ATOM   6456  C  CE     . LYS   B 2  392 ? -28.363 -25.591  22.509  1.00 61.47  ? 392 LYS   B CE     1 
ATOM   6457  N  NZ     . LYS   B 2  392 ? -29.364 -24.572  22.997  1.00 54.15  ? 392 LYS   B NZ     1 
ATOM   6458  N  N      . ALA   B 2  393 ? -22.042 -28.677  21.267  1.00 30.67  ? 393 ALA   B N      1 
ATOM   6459  C  CA     . ALA   B 2  393 ? -21.184 -29.008  20.134  1.00 29.54  ? 393 ALA   B CA     1 
ATOM   6460  C  C      . ALA   B 2  393 ? -21.467 -30.400  19.570  1.00 26.56  ? 393 ALA   B C      1 
ATOM   6461  O  O      . ALA   B 2  393 ? -21.849 -31.318  20.285  1.00 35.51  ? 393 ALA   B O      1 
ATOM   6462  C  CB     . ALA   B 2  393 ? -19.704 -28.917  20.525  1.00 29.33  ? 393 ALA   B CB     1 
ATOM   6463  N  N      . PHE   B 2  394 ? -21.246 -30.550  18.269  1.00 26.93  ? 394 PHE   B N      1 
ATOM   6464  C  CA     . PHE   B 2  394 ? -21.499 -31.778  17.517  1.00 28.62  ? 394 PHE   B CA     1 
ATOM   6465  C  C      . PHE   B 2  394 ? -22.871 -32.356  17.761  1.00 28.58  ? 394 PHE   B C      1 
ATOM   6466  O  O      . PHE   B 2  394 ? -23.169 -33.438  17.262  1.00 28.58  ? 394 PHE   B O      1 
ATOM   6467  C  CB     . PHE   B 2  394 ? -20.442 -32.829  17.809  1.00 28.41  ? 394 PHE   B CB     1 
ATOM   6468  C  CG     . PHE   B 2  394 ? -19.091 -32.363  17.478  1.00 31.06  ? 394 PHE   B CG     1 
ATOM   6469  C  CD1    . PHE   B 2  394 ? -18.659 -32.375  16.162  1.00 29.68  ? 394 PHE   B CD1    1 
ATOM   6470  C  CD2    . PHE   B 2  394 ? -18.287 -31.797  18.447  1.00 30.34  ? 394 PHE   B CD2    1 
ATOM   6471  C  CE1    . PHE   B 2  394 ? -17.426 -31.891  15.836  1.00 32.91  ? 394 PHE   B CE1    1 
ATOM   6472  C  CE2    . PHE   B 2  394 ? -17.055 -31.297  18.117  1.00 27.02  ? 394 PHE   B CE2    1 
ATOM   6473  C  CZ     . PHE   B 2  394 ? -16.623 -31.344  16.823  1.00 31.33  ? 394 PHE   B CZ     1 
ATOM   6474  N  N      . LEU   B 2  395 ? -23.728 -31.627  18.470  1.00 28.31  ? 395 LEU   B N      1 
ATOM   6475  C  CA     . LEU   B 2  395 ? -25.037 -32.165  18.791  1.00 29.38  ? 395 LEU   B CA     1 
ATOM   6476  C  C      . LEU   B 2  395 ? -25.896 -32.381  17.541  1.00 29.67  ? 395 LEU   B C      1 
ATOM   6477  O  O      . LEU   B 2  395 ? -26.791 -33.235  17.557  1.00 27.19  ? 395 LEU   B O      1 
ATOM   6478  C  CB     . LEU   B 2  395 ? -25.725 -31.238  19.800  1.00 27.98  ? 395 LEU   B CB     1 
ATOM   6479  C  CG     . LEU   B 2  395 ? -26.595 -31.967  20.824  1.00 33.54  ? 395 LEU   B CG     1 
ATOM   6480  C  CD1    . LEU   B 2  395 ? -25.736 -33.036  21.469  1.00 34.38  ? 395 LEU   B CD1    1 
ATOM   6481  C  CD2    . LEU   B 2  395 ? -27.110 -31.022  21.889  1.00 40.56  ? 395 LEU   B CD2    1 
ATOM   6482  N  N      . HIS   B 2  396 ? -25.623 -31.650  16.448  1.00 30.26  ? 396 HIS   B N      1 
ATOM   6483  C  CA     . HIS   B 2  396 ? -26.463 -31.763  15.261  1.00 27.90  ? 396 HIS   B CA     1 
ATOM   6484  C  C      . HIS   B 2  396 ? -26.447 -33.175  14.724  1.00 31.52  ? 396 HIS   B C      1 
ATOM   6485  O  O      . HIS   B 2  396 ? -27.490 -33.681  14.297  1.00 34.71  ? 396 HIS   B O      1 
ATOM   6486  C  CB     . HIS   B 2  396 ? -26.056 -30.744  14.170  1.00 34.26  ? 396 HIS   B CB     1 
ATOM   6487  C  CG     . HIS   B 2  396 ? -24.758 -31.038  13.450  1.00 35.61  ? 396 HIS   B CG     1 
ATOM   6488  N  ND1    . HIS   B 2  396 ? -24.706 -31.689  12.229  1.00 37.10  ? 396 HIS   B ND1    1 
ATOM   6489  C  CD2    . HIS   B 2  396 ? -23.475 -30.708  13.750  1.00 30.84  ? 396 HIS   B CD2    1 
ATOM   6490  C  CE1    . HIS   B 2  396 ? -23.446 -31.792  11.839  1.00 34.24  ? 396 HIS   B CE1    1 
ATOM   6491  N  NE2    . HIS   B 2  396 ? -22.682 -31.197  12.738  1.00 33.08  ? 396 HIS   B NE2    1 
ATOM   6492  N  N      . TRP   B 2  397 ? -25.297 -33.846  14.771  1.00 30.05  ? 397 TRP   B N      1 
ATOM   6493  C  CA     . TRP   B 2  397 ? -25.256 -35.197  14.246  1.00 30.71  ? 397 TRP   B CA     1 
ATOM   6494  C  C      . TRP   B 2  397 ? -26.297 -36.080  14.912  1.00 35.07  ? 397 TRP   B C      1 
ATOM   6495  O  O      . TRP   B 2  397 ? -26.625 -37.142  14.375  1.00 39.11  ? 397 TRP   B O      1 
ATOM   6496  C  CB     . TRP   B 2  397 ? -23.884 -35.823  14.427  1.00 28.51  ? 397 TRP   B CB     1 
ATOM   6497  C  CG     . TRP   B 2  397 ? -22.695 -35.159  13.737  1.00 34.74  ? 397 TRP   B CG     1 
ATOM   6498  C  CD1    . TRP   B 2  397 ? -21.543 -34.687  14.341  1.00 36.71  ? 397 TRP   B CD1    1 
ATOM   6499  C  CD2    . TRP   B 2  397 ? -22.509 -34.949  12.331  1.00 35.99  ? 397 TRP   B CD2    1 
ATOM   6500  N  NE1    . TRP   B 2  397 ? -20.669 -34.208  13.394  1.00 37.29  ? 397 TRP   B NE1    1 
ATOM   6501  C  CE2    . TRP   B 2  397 ? -21.244 -34.344  12.156  1.00 42.24  ? 397 TRP   B CE2    1 
ATOM   6502  C  CE3    . TRP   B 2  397 ? -23.279 -35.217  11.204  1.00 33.84  ? 397 TRP   B CE3    1 
ATOM   6503  C  CZ2    . TRP   B 2  397 ? -20.754 -34.000  10.900  1.00 44.52  ? 397 TRP   B CZ2    1 
ATOM   6504  C  CZ3    . TRP   B 2  397 ? -22.785 -34.872  9.967   1.00 34.47  ? 397 TRP   B CZ3    1 
ATOM   6505  C  CH2    . TRP   B 2  397 ? -21.539 -34.276  9.821   1.00 39.50  ? 397 TRP   B CH2    1 
ATOM   6506  N  N      . TYR   B 2  398 ? -26.828 -35.664  16.060  1.00 29.97  ? 398 TYR   B N      1 
ATOM   6507  C  CA     . TYR   B 2  398 ? -27.755 -36.471  16.835  1.00 32.31  ? 398 TYR   B CA     1 
ATOM   6508  C  C      . TYR   B 2  398 ? -29.181 -35.954  16.774  1.00 34.54  ? 398 TYR   B C      1 
ATOM   6509  O  O      . TYR   B 2  398 ? -30.121 -36.733  16.567  1.00 35.67  ? 398 TYR   B O      1 
ATOM   6510  C  CB     . TYR   B 2  398 ? -27.308 -36.542  18.307  1.00 37.15  ? 398 TYR   B CB     1 
ATOM   6511  C  CG     . TYR   B 2  398 ? -25.934 -37.124  18.537  1.00 34.21  ? 398 TYR   B CG     1 
ATOM   6512  C  CD1    . TYR   B 2  398 ? -24.812 -36.331  18.488  1.00 34.14  ? 398 TYR   B CD1    1 
ATOM   6513  C  CD2    . TYR   B 2  398 ? -25.761 -38.471  18.764  1.00 34.57  ? 398 TYR   B CD2    1 
ATOM   6514  C  CE1    . TYR   B 2  398 ? -23.549 -36.861  18.689  1.00 36.67  ? 398 TYR   B CE1    1 
ATOM   6515  C  CE2    . TYR   B 2  398 ? -24.507 -39.013  18.966  1.00 36.31  ? 398 TYR   B CE2    1 
ATOM   6516  C  CZ     . TYR   B 2  398 ? -23.399 -38.205  18.928  1.00 36.51  ? 398 TYR   B CZ     1 
ATOM   6517  O  OH     . TYR   B 2  398 ? -22.141 -38.733  19.126  1.00 35.44  ? 398 TYR   B OH     1 
ATOM   6518  N  N      . THR   B 2  399 ? -29.379 -34.652  16.994  1.00 36.38  ? 399 THR   B N      1 
ATOM   6519  C  CA     . THR   B 2  399 ? -30.703 -34.082  16.781  1.00 35.33  ? 399 THR   B CA     1 
ATOM   6520  C  C      . THR   B 2  399 ? -31.186 -34.371  15.379  1.00 32.98  ? 399 THR   B C      1 
ATOM   6521  O  O      . THR   B 2  399 ? -32.391 -34.405  15.134  1.00 33.89  ? 399 THR   B O      1 
ATOM   6522  C  CB     . THR   B 2  399 ? -30.679 -32.585  17.019  1.00 34.81  ? 399 THR   B CB     1 
ATOM   6523  O  OG1    . THR   B 2  399 ? -29.696 -31.997  16.159  1.00 39.32  ? 399 THR   B OG1    1 
ATOM   6524  C  CG2    . THR   B 2  399 ? -30.355 -32.294  18.448  1.00 32.24  ? 399 THR   B CG2    1 
ATOM   6525  N  N      . GLY   B 2  400 ? -30.252 -34.608  14.460  1.00 35.37  ? 400 GLY   B N      1 
ATOM   6526  C  CA     . GLY   B 2  400 ? -30.581 -34.964  13.097  1.00 34.55  ? 400 GLY   B CA     1 
ATOM   6527  C  C      . GLY   B 2  400 ? -31.240 -36.302  12.954  1.00 29.36  ? 400 GLY   B C      1 
ATOM   6528  O  O      . GLY   B 2  400 ? -31.875 -36.543  11.939  1.00 38.59  ? 400 GLY   B O      1 
ATOM   6529  N  N      . GLU   B 2  401 ? -31.125 -37.169  13.953  1.00 29.28  ? 401 GLU   B N      1 
ATOM   6530  C  CA     . GLU   B 2  401 ? -31.680 -38.513  13.894  1.00 34.49  ? 401 GLU   B CA     1 
ATOM   6531  C  C      . GLU   B 2  401 ? -32.874 -38.687  14.824  1.00 40.26  ? 401 GLU   B C      1 
ATOM   6532  O  O      . GLU   B 2  401 ? -33.192 -39.811  15.214  1.00 42.62  ? 401 GLU   B O      1 
ATOM   6533  C  CB     . GLU   B 2  401 ? -30.609 -39.550  14.221  1.00 35.79  ? 401 GLU   B CB     1 
ATOM   6534  C  CG     . GLU   B 2  401 ? -29.411 -39.405  13.347  1.00 41.22  ? 401 GLU   B CG     1 
ATOM   6535  C  CD     . GLU   B 2  401 ? -29.572 -40.126  12.045  1.00 46.19  ? 401 GLU   B CD     1 
ATOM   6536  O  OE1    . GLU   B 2  401 ? -30.409 -41.048  11.972  1.00 51.00  ? 401 GLU   B OE1    1 
ATOM   6537  O  OE2    . GLU   B 2  401 ? -28.920 -39.721  11.069  1.00 44.46  ? 401 GLU   B OE2    1 
ATOM   6538  N  N      . GLY   B 2  402 ? -33.542 -37.609  15.195  1.00 37.71  ? 402 GLY   B N      1 
ATOM   6539  C  CA     . GLY   B 2  402 ? -34.639 -37.693  16.125  1.00 34.36  ? 402 GLY   B CA     1 
ATOM   6540  C  C      . GLY   B 2  402 ? -34.279 -37.354  17.553  1.00 38.48  ? 402 GLY   B C      1 
ATOM   6541  O  O      . GLY   B 2  402 ? -35.186 -37.110  18.359  1.00 40.73  ? 402 GLY   B O      1 
ATOM   6542  N  N      . MET   B 2  403 ? -32.994 -37.306  17.898  1.00 37.10  ? 403 MET   B N      1 
ATOM   6543  C  CA     . MET   B 2  403 ? -32.707 -37.181  19.312  1.00 34.92  ? 403 MET   B CA     1 
ATOM   6544  C  C      . MET   B 2  403 ? -32.971 -35.767  19.797  1.00 37.61  ? 403 MET   B C      1 
ATOM   6545  O  O      . MET   B 2  403 ? -33.186 -34.836  19.024  1.00 43.75  ? 403 MET   B O      1 
ATOM   6546  C  CB     . MET   B 2  403 ? -31.286 -37.592  19.632  1.00 34.47  ? 403 MET   B CB     1 
ATOM   6547  C  CG     . MET   B 2  403 ? -31.164 -39.098  19.758  1.00 38.56  ? 403 MET   B CG     1 
ATOM   6548  S  SD     . MET   B 2  403 ? -29.626 -39.651  20.471  1.00 40.34  ? 403 MET   B SD     1 
ATOM   6549  C  CE     . MET   B 2  403 ? -29.962 -39.217  22.148  1.00 30.22  ? 403 MET   B CE     1 
ATOM   6550  N  N      . ASP   B 2  404 ? -32.941 -35.616  21.111  1.00 39.23  ? 404 ASP   B N      1 
ATOM   6551  C  CA     . ASP   B 2  404 ? -33.361 -34.389  21.761  1.00 35.96  ? 404 ASP   B CA     1 
ATOM   6552  C  C      . ASP   B 2  404 ? -32.342 -33.997  22.818  1.00 42.62  ? 404 ASP   B C      1 
ATOM   6553  O  O      . ASP   B 2  404 ? -31.798 -34.859  23.511  1.00 47.60  ? 404 ASP   B O      1 
ATOM   6554  C  CB     . ASP   B 2  404 ? -34.755 -34.606  22.330  1.00 46.89  ? 404 ASP   B CB     1 
ATOM   6555  C  CG     . ASP   B 2  404 ? -35.440 -33.327  22.700  1.00 58.46  ? 404 ASP   B CG     1 
ATOM   6556  O  OD1    . ASP   B 2  404 ? -34.743 -32.386  23.134  1.00 60.83  ? 404 ASP   B OD1    1 
ATOM   6557  O  OD2    . ASP   B 2  404 ? -36.664 -33.228  22.427  1.00 69.11  ? 404 ASP   B OD2    1 
ATOM   6558  N  N      . GLU   B 2  405 ? -32.038 -32.699  22.900  1.00 44.01  ? 405 GLU   B N      1 
ATOM   6559  C  CA     . GLU   B 2  405 ? -31.089 -32.220  23.902  1.00 41.57  ? 405 GLU   B CA     1 
ATOM   6560  C  C      . GLU   B 2  405 ? -31.434 -32.818  25.262  1.00 44.11  ? 405 GLU   B C      1 
ATOM   6561  O  O      . GLU   B 2  405 ? -30.551 -33.206  26.041  1.00 42.87  ? 405 GLU   B O      1 
ATOM   6562  C  CB     . GLU   B 2  405 ? -31.121 -30.685  23.962  1.00 40.13  ? 405 GLU   B CB     1 
ATOM   6563  C  CG     . GLU   B 2  405 ? -30.198 -29.970  22.992  1.00 48.67  ? 405 GLU   B CG     1 
ATOM   6564  C  CD     . GLU   B 2  405 ? -30.174 -28.443  23.175  1.00 62.75  ? 405 GLU   B CD     1 
ATOM   6565  O  OE1    . GLU   B 2  405 ? -30.414 -27.929  24.308  1.00 52.11  ? 405 GLU   B OE1    1 
ATOM   6566  O  OE2    . GLU   B 2  405 ? -29.939 -27.761  22.146  1.00 60.36  ? 405 GLU   B OE2    1 
ATOM   6567  N  N      . MET   B 2  406 ? -32.735 -32.931  25.535  1.00 44.91  ? 406 MET   B N      1 
ATOM   6568  C  CA     . MET   B 2  406 ? -33.216 -33.425  26.812  1.00 45.88  ? 406 MET   B CA     1 
ATOM   6569  C  C      . MET   B 2  406 ? -32.606 -34.784  27.114  1.00 50.52  ? 406 MET   B C      1 
ATOM   6570  O  O      . MET   B 2  406 ? -32.044 -35.009  28.193  1.00 55.17  ? 406 MET   B O      1 
ATOM   6571  C  CB     . MET   B 2  406 ? -34.740 -33.500  26.754  1.00 54.73  ? 406 MET   B CB     1 
ATOM   6572  C  CG     . MET   B 2  406 ? -35.412 -34.105  27.961  1.00 64.98  ? 406 MET   B CG     1 
ATOM   6573  S  SD     . MET   B 2  406 ? -35.741 -32.797  29.163  1.00 91.96  ? 406 MET   B SD     1 
ATOM   6574  C  CE     . MET   B 2  406 ? -34.359 -32.971  30.325  1.00 71.88  ? 406 MET   B CE     1 
ATOM   6575  N  N      . GLU   B 2  407 ? -32.673 -35.697  26.147  1.00 45.55  ? 407 GLU   B N      1 
ATOM   6576  C  CA     . GLU   B 2  407 ? -32.117 -37.030  26.333  1.00 41.35  ? 407 GLU   B CA     1 
ATOM   6577  C  C      . GLU   B 2  407 ? -30.659 -36.975  26.772  1.00 41.63  ? 407 GLU   B C      1 
ATOM   6578  O  O      . GLU   B 2  407 ? -30.206 -37.818  27.554  1.00 41.89  ? 407 GLU   B O      1 
ATOM   6579  C  CB     . GLU   B 2  407 ? -32.276 -37.821  25.043  1.00 33.75  ? 407 GLU   B CB     1 
ATOM   6580  C  CG     . GLU   B 2  407 ? -31.819 -39.233  25.143  1.00 33.92  ? 407 GLU   B CG     1 
ATOM   6581  C  CD     . GLU   B 2  407 ? -32.557 -40.118  24.193  1.00 38.11  ? 407 GLU   B CD     1 
ATOM   6582  O  OE1    . GLU   B 2  407 ? -33.512 -39.631  23.549  1.00 41.40  ? 407 GLU   B OE1    1 
ATOM   6583  O  OE2    . GLU   B 2  407 ? -32.173 -41.297  24.081  1.00 41.63  ? 407 GLU   B OE2    1 
ATOM   6584  N  N      . PHE   B 2  408 ? -29.916 -35.985  26.295  1.00 43.26  ? 408 PHE   B N      1 
ATOM   6585  C  CA     . PHE   B 2  408 ? -28.510 -35.889  26.657  1.00 43.89  ? 408 PHE   B CA     1 
ATOM   6586  C  C      . PHE   B 2  408 ? -28.363 -35.469  28.099  1.00 42.38  ? 408 PHE   B C      1 
ATOM   6587  O  O      . PHE   B 2  408 ? -27.519 -36.011  28.820  1.00 44.27  ? 408 PHE   B O      1 
ATOM   6588  C  CB     . PHE   B 2  408 ? -27.791 -34.914  25.717  1.00 42.73  ? 408 PHE   B CB     1 
ATOM   6589  C  CG     . PHE   B 2  408 ? -27.322 -35.538  24.421  1.00 38.40  ? 408 PHE   B CG     1 
ATOM   6590  C  CD1    . PHE   B 2  408 ? -28.227 -35.860  23.421  1.00 36.57  ? 408 PHE   B CD1    1 
ATOM   6591  C  CD2    . PHE   B 2  408 ? -25.969 -35.724  24.173  1.00 41.89  ? 408 PHE   B CD2    1 
ATOM   6592  C  CE1    . PHE   B 2  408 ? -27.803 -36.426  22.221  1.00 38.99  ? 408 PHE   B CE1    1 
ATOM   6593  C  CE2    . PHE   B 2  408 ? -25.530 -36.272  22.964  1.00 39.50  ? 408 PHE   B CE2    1 
ATOM   6594  C  CZ     . PHE   B 2  408 ? -26.451 -36.622  21.988  1.00 38.25  ? 408 PHE   B CZ     1 
ATOM   6595  N  N      . THR   B 2  409 ? -29.191 -34.511  28.534  1.00 44.95  ? 409 THR   B N      1 
ATOM   6596  C  CA     . THR   B 2  409 ? -29.189 -34.069  29.928  1.00 44.41  ? 409 THR   B CA     1 
ATOM   6597  C  C      . THR   B 2  409 ? -29.466 -35.224  30.880  1.00 44.21  ? 409 THR   B C      1 
ATOM   6598  O  O      . THR   B 2  409 ? -28.809 -35.355  31.919  1.00 47.67  ? 409 THR   B O      1 
ATOM   6599  C  CB     . THR   B 2  409 ? -30.228 -32.969  30.116  1.00 41.42  ? 409 THR   B CB     1 
ATOM   6600  O  OG1    . THR   B 2  409 ? -29.800 -31.782  29.437  1.00 37.42  ? 409 THR   B OG1    1 
ATOM   6601  C  CG2    . THR   B 2  409 ? -30.452 -32.692  31.590  1.00 50.43  ? 409 THR   B CG2    1 
ATOM   6602  N  N      . GLU   B 2  410 ? -30.432 -36.074  30.531  1.00 42.78  ? 410 GLU   B N      1 
ATOM   6603  C  CA     . GLU   B 2  410 ? -30.788 -37.219  31.360  1.00 43.91  ? 410 GLU   B CA     1 
ATOM   6604  C  C      . GLU   B 2  410 ? -29.625 -38.189  31.522  1.00 48.16  ? 410 GLU   B C      1 
ATOM   6605  O  O      . GLU   B 2  410 ? -29.386 -38.705  32.622  1.00 48.37  ? 410 GLU   B O      1 
ATOM   6606  C  CB     . GLU   B 2  410 ? -31.972 -37.935  30.737  1.00 43.79  ? 410 GLU   B CB     1 
ATOM   6607  C  CG     . GLU   B 2  410 ? -33.189 -37.078  30.766  1.00 56.75  ? 410 GLU   B CG     1 
ATOM   6608  C  CD     . GLU   B 2  410 ? -34.275 -37.639  29.917  1.00 67.00  ? 410 GLU   B CD     1 
ATOM   6609  O  OE1    . GLU   B 2  410 ? -34.061 -38.746  29.362  1.00 68.90  ? 410 GLU   B OE1    1 
ATOM   6610  O  OE2    . GLU   B 2  410 ? -35.314 -36.952  29.777  1.00 66.47  ? 410 GLU   B OE2    1 
ATOM   6611  N  N      . ALA   B 2  411 ? -28.928 -38.499  30.425  1.00 52.03  ? 411 ALA   B N      1 
ATOM   6612  C  CA     . ALA   B 2  411 ? -27.823 -39.442  30.496  1.00 42.89  ? 411 ALA   B CA     1 
ATOM   6613  C  C      . ALA   B 2  411 ? -26.690 -38.865  31.327  1.00 41.90  ? 411 ALA   B C      1 
ATOM   6614  O  O      . ALA   B 2  411 ? -26.287 -39.452  32.339  1.00 44.51  ? 411 ALA   B O      1 
ATOM   6615  C  CB     . ALA   B 2  411 ? -27.356 -39.800  29.091  1.00 39.45  ? 411 ALA   B CB     1 
ATOM   6616  N  N      . GLU   B 2  412 ? -26.156 -37.718  30.906  1.00 38.02  ? 412 GLU   B N      1 
ATOM   6617  C  CA     . GLU   B 2  412 ? -25.203 -36.960  31.711  1.00 44.53  ? 412 GLU   B CA     1 
ATOM   6618  C  C      . GLU   B 2  412 ? -25.577 -37.022  33.181  1.00 46.23  ? 412 GLU   B C      1 
ATOM   6619  O  O      . GLU   B 2  412 ? -24.733 -37.246  34.051  1.00 47.71  ? 412 GLU   B O      1 
ATOM   6620  C  CB     . GLU   B 2  412 ? -25.164 -35.500  31.266  1.00 45.40  ? 412 GLU   B CB     1 
ATOM   6621  C  CG     . GLU   B 2  412 ? -24.203 -34.594  32.037  1.00 46.48  ? 412 GLU   B CG     1 
ATOM   6622  C  CD     . GLU   B 2  412 ? -24.542 -33.120  31.805  1.00 60.51  ? 412 GLU   B CD     1 
ATOM   6623  O  OE1    . GLU   B 2  412 ? -25.730 -32.767  31.976  1.00 69.04  ? 412 GLU   B OE1    1 
ATOM   6624  O  OE2    . GLU   B 2  412 ? -23.654 -32.312  31.454  1.00 56.36  ? 412 GLU   B OE2    1 
ATOM   6625  N  N      . SER   B 2  413 ? -26.857 -36.839  33.458  1.00 46.16  ? 413 SER   B N      1 
ATOM   6626  C  CA     . SER   B 2  413 ? -27.311 -36.761  34.833  1.00 43.37  ? 413 SER   B CA     1 
ATOM   6627  C  C      . SER   B 2  413 ? -27.353 -38.141  35.483  1.00 45.39  ? 413 SER   B C      1 
ATOM   6628  O  O      . SER   B 2  413 ? -26.847 -38.321  36.595  1.00 45.71  ? 413 SER   B O      1 
ATOM   6629  C  CB     . SER   B 2  413 ? -28.672 -36.087  34.868  1.00 36.22  ? 413 SER   B CB     1 
ATOM   6630  O  OG     . SER   B 2  413 ? -28.992 -35.799  36.187  1.00 54.16  ? 413 SER   B OG     1 
ATOM   6631  N  N      . ASN   B 2  414 ? -27.949 -39.133  34.812  1.00 44.77  ? 414 ASN   B N      1 
ATOM   6632  C  CA     . ASN   B 2  414 ? -27.936 -40.477  35.373  1.00 41.56  ? 414 ASN   B CA     1 
ATOM   6633  C  C      . ASN   B 2  414 ? -26.516 -40.893  35.694  1.00 44.41  ? 414 ASN   B C      1 
ATOM   6634  O  O      . ASN   B 2  414 ? -26.270 -41.533  36.722  1.00 45.84  ? 414 ASN   B O      1 
ATOM   6635  C  CB     . ASN   B 2  414 ? -28.580 -41.489  34.420  1.00 49.86  ? 414 ASN   B CB     1 
ATOM   6636  C  CG     . ASN   B 2  414 ? -28.817 -42.870  35.085  1.00 55.22  ? 414 ASN   B CG     1 
ATOM   6637  O  OD1    . ASN   B 2  414 ? -28.660 -43.011  36.305  1.00 54.65  ? 414 ASN   B OD1    1 
ATOM   6638  N  ND2    . ASN   B 2  414 ? -29.206 -43.880  34.287  1.00 47.05  ? 414 ASN   B ND2    1 
ATOM   6639  N  N      . MET   B 2  415 ? -25.557 -40.504  34.842  1.00 47.74  ? 415 MET   B N      1 
ATOM   6640  C  CA     . MET   B 2  415 ? -24.166 -40.905  35.059  1.00 42.75  ? 415 MET   B CA     1 
ATOM   6641  C  C      . MET   B 2  415 ? -23.555 -40.178  36.244  1.00 46.82  ? 415 MET   B C      1 
ATOM   6642  O  O      . MET   B 2  415 ? -22.873 -40.789  37.073  1.00 48.36  ? 415 MET   B O      1 
ATOM   6643  C  CB     . MET   B 2  415 ? -23.321 -40.646  33.828  1.00 36.06  ? 415 MET   B CB     1 
ATOM   6644  C  CG     . MET   B 2  415 ? -22.034 -41.400  33.924  1.00 35.33  ? 415 MET   B CG     1 
ATOM   6645  S  SD     . MET   B 2  415 ? -20.946 -41.022  32.553  1.00 44.21  ? 415 MET   B SD     1 
ATOM   6646  C  CE     . MET   B 2  415 ? -21.133 -42.448  31.521  1.00 37.24  ? 415 MET   B CE     1 
ATOM   6647  N  N      . ASN   B 2  416 ? -23.773 -38.866  36.326  1.00 46.24  ? 416 ASN   B N      1 
ATOM   6648  C  CA     . ASN   B 2  416 ? -23.295 -38.097  37.463  1.00 39.51  ? 416 ASN   B CA     1 
ATOM   6649  C  C      . ASN   B 2  416 ? -23.860 -38.648  38.755  1.00 45.69  ? 416 ASN   B C      1 
ATOM   6650  O  O      . ASN   B 2  416 ? -23.183 -38.650  39.786  1.00 49.27  ? 416 ASN   B O      1 
ATOM   6651  C  CB     . ASN   B 2  416 ? -23.688 -36.643  37.277  1.00 41.37  ? 416 ASN   B CB     1 
ATOM   6652  C  CG     . ASN   B 2  416 ? -22.821 -35.948  36.268  1.00 49.12  ? 416 ASN   B CG     1 
ATOM   6653  O  OD1    . ASN   B 2  416 ? -21.703 -36.396  35.996  1.00 50.56  ? 416 ASN   B OD1    1 
ATOM   6654  N  ND2    . ASN   B 2  416 ? -23.340 -34.868  35.664  1.00 50.11  ? 416 ASN   B ND2    1 
ATOM   6655  N  N      . ASP   B 2  417 ? -25.106 -39.119  38.715  1.00 46.80  ? 417 ASP   B N      1 
ATOM   6656  C  CA     . ASP   B 2  417 ? -25.670 -39.864  39.834  1.00 47.52  ? 417 ASP   B CA     1 
ATOM   6657  C  C      . ASP   B 2  417 ? -24.810 -41.073  40.160  1.00 50.59  ? 417 ASP   B C      1 
ATOM   6658  O  O      . ASP   B 2  417 ? -24.326 -41.232  41.288  1.00 52.97  ? 417 ASP   B O      1 
ATOM   6659  C  CB     . ASP   B 2  417 ? -27.081 -40.314  39.489  1.00 47.78  ? 417 ASP   B CB     1 
ATOM   6660  C  CG     . ASP   B 2  417 ? -28.046 -39.165  39.400  1.00 49.86  ? 417 ASP   B CG     1 
ATOM   6661  O  OD1    . ASP   B 2  417 ? -27.620 -38.017  39.697  1.00 46.40  ? 417 ASP   B OD1    1 
ATOM   6662  O  OD2    . ASP   B 2  417 ? -29.216 -39.424  39.004  1.00 46.83  ? 417 ASP   B OD2    1 
ATOM   6663  N  N      . LEU   B 2  418 ? -24.627 -41.955  39.179  1.00 50.61  ? 418 LEU   B N      1 
ATOM   6664  C  CA     . LEU   B 2  418 ? -23.766 -43.117  39.346  1.00 48.28  ? 418 LEU   B CA     1 
ATOM   6665  C  C      . LEU   B 2  418 ? -22.477 -42.752  40.070  1.00 48.10  ? 418 LEU   B C      1 
ATOM   6666  O  O      . LEU   B 2  418 ? -22.051 -43.476  40.973  1.00 49.07  ? 418 LEU   B O      1 
ATOM   6667  C  CB     . LEU   B 2  418 ? -23.432 -43.727  37.994  1.00 43.98  ? 418 LEU   B CB     1 
ATOM   6668  C  CG     . LEU   B 2  418 ? -22.648 -45.016  38.118  1.00 40.90  ? 418 LEU   B CG     1 
ATOM   6669  C  CD1    . LEU   B 2  418 ? -23.583 -46.055  38.696  1.00 43.33  ? 418 LEU   B CD1    1 
ATOM   6670  C  CD2    . LEU   B 2  418 ? -22.038 -45.482  36.786  1.00 33.59  ? 418 LEU   B CD2    1 
ATOM   6671  N  N      . VAL   B 2  419 ? -21.847 -41.633  39.693  1.00 48.52  ? 419 VAL   B N      1 
ATOM   6672  C  CA     . VAL   B 2  419 ? -20.635 -41.221  40.398  1.00 48.67  ? 419 VAL   B CA     1 
ATOM   6673  C  C      . VAL   B 2  419 ? -20.949 -40.920  41.851  1.00 50.83  ? 419 VAL   B C      1 
ATOM   6674  O  O      . VAL   B 2  419 ? -20.211 -41.327  42.750  1.00 53.34  ? 419 VAL   B O      1 
ATOM   6675  C  CB     . VAL   B 2  419 ? -19.959 -40.018  39.720  1.00 45.32  ? 419 VAL   B CB     1 
ATOM   6676  C  CG1    . VAL   B 2  419 ? -18.797 -39.583  40.559  1.00 54.09  ? 419 VAL   B CG1    1 
ATOM   6677  C  CG2    . VAL   B 2  419 ? -19.445 -40.392  38.368  1.00 50.57  ? 419 VAL   B CG2    1 
ATOM   6678  N  N      . SER   B 2  420 ? -22.029 -40.185  42.109  1.00 53.25  ? 420 SER   B N      1 
ATOM   6679  C  CA     . SER   B 2  420 ? -22.393 -39.902  43.494  1.00 51.29  ? 420 SER   B CA     1 
ATOM   6680  C  C      . SER   B 2  420 ? -22.547 -41.189  44.278  1.00 52.09  ? 420 SER   B C      1 
ATOM   6681  O  O      . SER   B 2  420 ? -21.909 -41.380  45.319  1.00 52.53  ? 420 SER   B O      1 
ATOM   6682  C  CB     . SER   B 2  420 ? -23.680 -39.083  43.561  1.00 53.26  ? 420 SER   B CB     1 
ATOM   6683  O  OG     . SER   B 2  420 ? -23.574 -37.915  42.774  1.00 68.37  ? 420 SER   B OG     1 
ATOM   6684  N  N      . GLU   B 2  421 ? -23.393 -42.089  43.785  1.00 51.34  ? 421 GLU   B N      1 
ATOM   6685  C  CA     . GLU   B 2  421 ? -23.562 -43.376  44.436  1.00 49.87  ? 421 GLU   B CA     1 
ATOM   6686  C  C      . GLU   B 2  421 ? -22.198 -44.002  44.732  1.00 53.22  ? 421 GLU   B C      1 
ATOM   6687  O  O      . GLU   B 2  421 ? -21.848 -44.220  45.896  1.00 58.37  ? 421 GLU   B O      1 
ATOM   6688  C  CB     . GLU   B 2  421 ? -24.450 -44.272  43.564  1.00 47.97  ? 421 GLU   B CB     1 
ATOM   6689  C  CG     . GLU   B 2  421 ? -25.195 -45.368  44.333  1.00 59.54  ? 421 GLU   B CG     1 
ATOM   6690  C  CD     . GLU   B 2  421 ? -26.122 -46.213  43.449  1.00 61.14  ? 421 GLU   B CD     1 
ATOM   6691  O  OE1    . GLU   B 2  421 ? -26.703 -45.617  42.499  1.00 58.70  ? 421 GLU   B OE1    1 
ATOM   6692  O  OE2    . GLU   B 2  421 ? -26.273 -47.452  43.716  1.00 50.94  ? 421 GLU   B OE2    1 
ATOM   6693  N  N      . TYR   B 2  422 ? -21.375 -44.235  43.697  1.00 51.65  ? 422 TYR   B N      1 
ATOM   6694  C  CA     . TYR   B 2  422 ? -20.062 -44.843  43.933  1.00 49.09  ? 422 TYR   B CA     1 
ATOM   6695  C  C      . TYR   B 2  422 ? -19.268 -44.091  44.994  1.00 56.51  ? 422 TYR   B C      1 
ATOM   6696  O  O      . TYR   B 2  422 ? -18.362 -44.667  45.602  1.00 61.03  ? 422 TYR   B O      1 
ATOM   6697  C  CB     . TYR   B 2  422 ? -19.221 -44.909  42.649  1.00 44.67  ? 422 TYR   B CB     1 
ATOM   6698  C  CG     . TYR   B 2  422 ? -19.350 -46.210  41.878  1.00 44.74  ? 422 TYR   B CG     1 
ATOM   6699  C  CD1    . TYR   B 2  422 ? -18.973 -47.412  42.449  1.00 43.73  ? 422 TYR   B CD1    1 
ATOM   6700  C  CD2    . TYR   B 2  422 ? -19.823 -46.227  40.569  1.00 37.39  ? 422 TYR   B CD2    1 
ATOM   6701  C  CE1    . TYR   B 2  422 ? -19.095 -48.603  41.766  1.00 40.50  ? 422 TYR   B CE1    1 
ATOM   6702  C  CE2    . TYR   B 2  422 ? -19.950 -47.418  39.867  1.00 37.68  ? 422 TYR   B CE2    1 
ATOM   6703  C  CZ     . TYR   B 2  422 ? -19.581 -48.614  40.470  1.00 46.46  ? 422 TYR   B CZ     1 
ATOM   6704  O  OH     . TYR   B 2  422 ? -19.681 -49.837  39.793  1.00 47.10  ? 422 TYR   B OH     1 
ATOM   6705  N  N      . GLN   B 2  423 ? -19.582 -42.820  45.235  1.00 53.40  ? 423 GLN   B N      1 
ATOM   6706  C  CA     . GLN   B 2  423 ? -18.852 -42.043  46.224  1.00 55.79  ? 423 GLN   B CA     1 
ATOM   6707  C  C      . GLN   B 2  423 ? -19.430 -42.179  47.616  1.00 66.76  ? 423 GLN   B C      1 
ATOM   6708  O  O      . GLN   B 2  423 ? -18.712 -41.956  48.602  1.00 71.98  ? 423 GLN   B O      1 
ATOM   6709  C  CB     . GLN   B 2  423 ? -18.843 -40.561  45.855  1.00 63.71  ? 423 GLN   B CB     1 
ATOM   6710  C  CG     . GLN   B 2  423 ? -17.467 -40.015  45.481  1.00 72.38  ? 423 GLN   B CG     1 
ATOM   6711  C  CD     . GLN   B 2  423 ? -16.540 -39.931  46.689  1.00 75.13  ? 423 GLN   B CD     1 
ATOM   6712  O  OE1    . GLN   B 2  423 ? -17.001 -39.843  47.835  1.00 73.32  ? 423 GLN   B OE1    1 
ATOM   6713  N  NE2    . GLN   B 2  423 ? -15.225 -39.922  46.436  1.00 69.63  ? 423 GLN   B NE2    1 
ATOM   6714  N  N      . GLN   B 2  424 ? -20.714 -42.515  47.713  1.00 63.37  ? 424 GLN   B N      1 
ATOM   6715  C  CA     . GLN   B 2  424 ? -21.338 -42.728  49.010  1.00 54.77  ? 424 GLN   B CA     1 
ATOM   6716  C  C      . GLN   B 2  424 ? -20.613 -43.811  49.795  1.00 67.37  ? 424 GLN   B C      1 
ATOM   6717  O  O      . GLN   B 2  424 ? -20.210 -43.604  50.948  1.00 70.99  ? 424 GLN   B O      1 
ATOM   6718  C  CB     . GLN   B 2  424 ? -22.785 -43.125  48.800  1.00 54.02  ? 424 GLN   B CB     1 
ATOM   6719  C  CG     . GLN   B 2  424 ? -23.501 -43.432  50.052  1.00 63.77  ? 424 GLN   B CG     1 
ATOM   6720  C  CD     . GLN   B 2  424 ? -24.822 -44.090  49.789  1.00 71.08  ? 424 GLN   B CD     1 
ATOM   6721  O  OE1    . GLN   B 2  424 ? -25.228 -44.253  48.628  1.00 70.24  ? 424 GLN   B OE1    1 
ATOM   6722  N  NE2    . GLN   B 2  424 ? -25.543 -44.416  50.865  1.00 71.36  ? 424 GLN   B NE2    1 
ATOM   6723  N  N      . TYR   B 2  425 ? -20.431 -44.980  49.171  1.00 65.24  ? 425 TYR   B N      1 
ATOM   6724  C  CA     . TYR   B 2  425 ? -19.926 -46.165  49.851  1.00 58.72  ? 425 TYR   B CA     1 
ATOM   6725  C  C      . TYR   B 2  425 ? -18.429 -46.109  50.079  1.00 60.94  ? 425 TYR   B C      1 
ATOM   6726  O  O      . TYR   B 2  425 ? -17.911 -46.863  50.908  1.00 66.25  ? 425 TYR   B O      1 
ATOM   6727  C  CB     . TYR   B 2  425 ? -20.290 -47.393  49.033  1.00 53.01  ? 425 TYR   B CB     1 
ATOM   6728  C  CG     . TYR   B 2  425 ? -21.775 -47.464  48.806  1.00 58.31  ? 425 TYR   B CG     1 
ATOM   6729  C  CD1    . TYR   B 2  425 ? -22.650 -47.725  49.853  1.00 58.11  ? 425 TYR   B CD1    1 
ATOM   6730  C  CD2    . TYR   B 2  425 ? -22.318 -47.196  47.554  1.00 61.20  ? 425 TYR   B CD2    1 
ATOM   6731  C  CE1    . TYR   B 2  425 ? -24.032 -47.769  49.651  1.00 54.91  ? 425 TYR   B CE1    1 
ATOM   6732  C  CE2    . TYR   B 2  425 ? -23.693 -47.231  47.344  1.00 62.07  ? 425 TYR   B CE2    1 
ATOM   6733  C  CZ     . TYR   B 2  425 ? -24.546 -47.518  48.400  1.00 60.00  ? 425 TYR   B CZ     1 
ATOM   6734  O  OH     . TYR   B 2  425 ? -25.907 -47.555  48.179  1.00 60.66  ? 425 TYR   B OH     1 
ATOM   6735  N  N      . GLN   B 2  426 ? -17.728 -45.227  49.375  1.00 64.16  ? 426 GLN   B N      1 
ATOM   6736  C  CA     . GLN   B 2  426 ? -16.289 -45.098  49.543  1.00 68.32  ? 426 GLN   B CA     1 
ATOM   6737  C  C      . GLN   B 2  426 ? -15.954 -44.388  50.842  1.00 71.73  ? 426 GLN   B C      1 
ATOM   6738  O  O      . GLN   B 2  426 ? -14.778 -44.324  51.218  1.00 70.65  ? 426 GLN   B O      1 
ATOM   6739  C  CB     . GLN   B 2  426 ? -15.723 -44.357  48.329  1.00 68.17  ? 426 GLN   B CB     1 
ATOM   6740  C  CG     . GLN   B 2  426 ? -14.229 -44.379  48.127  1.00 74.36  ? 426 GLN   B CG     1 
ATOM   6741  C  CD     . GLN   B 2  426 ? -13.846 -43.490  46.967  1.00 75.97  ? 426 GLN   B CD     1 
ATOM   6742  O  OE1    . GLN   B 2  426 ? -14.441 -42.441  46.770  1.00 83.66  ? 426 GLN   B OE1    1 
ATOM   6743  N  NE2    . GLN   B 2  426 ? -12.960 -43.974  46.112  1.00 64.99  ? 426 GLN   B NE2    1 
ATOM   6744  N  N      . ASP   B 2  427 ? -16.980 -43.896  51.544  1.00 78.15  ? 427 ASP   B N      1 
ATOM   6745  C  CA     . ASP   B 2  427 ? -16.867 -43.194  52.818  1.00 81.42  ? 427 ASP   B CA     1 
ATOM   6746  C  C      . ASP   B 2  427 ? -17.472 -43.948  54.005  1.00 84.33  ? 427 ASP   B C      1 
ATOM   6747  O  O      . ASP   B 2  427 ? -16.964 -43.815  55.122  1.00 92.51  ? 427 ASP   B O      1 
ATOM   6748  C  CB     . ASP   B 2  427 ? -17.534 -41.815  52.707  1.00 81.98  ? 427 ASP   B CB     1 
ATOM   6749  C  CG     . ASP   B 2  427 ? -16.850 -40.910  51.683  1.00 86.36  ? 427 ASP   B CG     1 
ATOM   6750  O  OD1    . ASP   B 2  427 ? -15.800 -41.310  51.122  1.00 88.34  ? 427 ASP   B OD1    1 
ATOM   6751  O  OD2    . ASP   B 2  427 ? -17.363 -39.798  51.435  1.00 91.38  ? 427 ASP   B OD2    1 
ATOM   6752  N  N      . ALA   B 2  428 ? -18.534 -44.730  53.794  1.00 78.26  ? 428 ALA   B N      1 
ATOM   6753  C  CA     . ALA   B 2  428 ? -19.150 -45.561  54.841  1.00 74.38  ? 428 ALA   B CA     1 
ATOM   6754  C  C      . ALA   B 2  428 ? -18.134 -46.342  55.693  1.00 80.70  ? 428 ALA   B C      1 
ATOM   6755  O  O      . ALA   B 2  428 ? -18.398 -46.682  56.859  1.00 83.83  ? 428 ALA   B O      1 
ATOM   6756  C  CB     . ALA   B 2  428 ? -20.140 -46.523  54.204  1.00 68.61  ? 428 ALA   B CB     1 
ATOM   6757  N  N      . MET   C 1  1   ? -20.014 -51.075  -2.123  1.00 90.68  ? 1   MET   C N      1 
ATOM   6758  C  CA     . MET   C 1  1   ? -20.820 -49.973  -2.633  1.00 69.86  ? 1   MET   C CA     1 
ATOM   6759  C  C      . MET   C 1  1   ? -20.251 -48.706  -2.030  1.00 65.86  ? 1   MET   C C      1 
ATOM   6760  O  O      . MET   C 1  1   ? -19.033 -48.522  -2.037  1.00 67.31  ? 1   MET   C O      1 
ATOM   6761  C  CB     . MET   C 1  1   ? -22.313 -50.144  -2.296  1.00 63.57  ? 1   MET   C CB     1 
ATOM   6762  C  CG     . MET   C 1  1   ? -22.616 -50.420  -0.823  1.00 72.31  ? 1   MET   C CG     1 
ATOM   6763  S  SD     . MET   C 1  1   ? -24.192 -51.260  -0.454  1.00 72.05  ? 1   MET   C SD     1 
ATOM   6764  C  CE     . MET   C 1  1   ? -24.028 -52.753  -1.439  1.00 67.62  ? 1   MET   C CE     1 
ATOM   6765  N  N      . ARG   C 1  2   ? -21.136 -47.861  -1.493  1.00 62.04  ? 2   ARG   C N      1 
ATOM   6766  C  CA     . ARG   C 1  2   ? -20.789 -46.520  -1.010  1.00 58.54  ? 2   ARG   C CA     1 
ATOM   6767  C  C      . ARG   C 1  2   ? -20.343 -45.607  -2.163  1.00 52.45  ? 2   ARG   C C      1 
ATOM   6768  O  O      . ARG   C 1  2   ? -19.282 -44.993  -2.130  1.00 54.06  ? 2   ARG   C O      1 
ATOM   6769  C  CB     . ARG   C 1  2   ? -19.714 -46.602  0.077   1.00 66.20  ? 2   ARG   C CB     1 
ATOM   6770  C  CG     . ARG   C 1  2   ? -20.034 -47.614  1.171   1.00 80.98  ? 2   ARG   C CG     1 
ATOM   6771  C  CD     . ARG   C 1  2   ? -20.691 -46.958  2.401   1.00 80.82  ? 2   ARG   C CD     1 
ATOM   6772  N  NE     . ARG   C 1  2   ? -21.819 -46.108  2.027   1.00 75.72  ? 2   ARG   C NE     1 
ATOM   6773  C  CZ     . ARG   C 1  2   ? -23.094 -46.475  2.084   1.00 73.26  ? 2   ARG   C CZ     1 
ATOM   6774  N  NH1    . ARG   C 1  2   ? -23.446 -47.723  2.351   1.00 78.00  ? 2   ARG   C NH1    1 
ATOM   6775  N  NH2    . ARG   C 1  2   ? -24.042 -45.570  1.852   1.00 66.68  ? 2   ARG   C NH2    1 
ATOM   6776  N  N      . GLU   C 1  3   ? -21.187 -45.514  -3.186  1.00 47.89  ? 3   GLU   C N      1 
ATOM   6777  C  CA     . GLU   C 1  3   ? -20.846 -44.766  -4.389  1.00 46.95  ? 3   GLU   C CA     1 
ATOM   6778  C  C      . GLU   C 1  3   ? -20.984 -43.260  -4.168  1.00 42.74  ? 3   GLU   C C      1 
ATOM   6779  O  O      . GLU   C 1  3   ? -21.884 -42.793  -3.471  1.00 40.22  ? 3   GLU   C O      1 
ATOM   6780  C  CB     . GLU   C 1  3   ? -21.744 -45.172  -5.569  1.00 45.42  ? 3   GLU   C CB     1 
ATOM   6781  C  CG     . GLU   C 1  3   ? -21.723 -46.622  -6.009  1.00 42.49  ? 3   GLU   C CG     1 
ATOM   6782  C  CD     . GLU   C 1  3   ? -22.845 -47.420  -5.377  1.00 49.32  ? 3   GLU   C CD     1 
ATOM   6783  O  OE1    . GLU   C 1  3   ? -23.317 -47.009  -4.293  1.00 50.24  ? 3   GLU   C OE1    1 
ATOM   6784  O  OE2    . GLU   C 1  3   ? -23.285 -48.433  -5.973  1.00 48.45  ? 3   GLU   C OE2    1 
ATOM   6785  N  N      . CYS   C 1  4   ? -20.101 -42.501  -4.812  1.00 37.91  ? 4   CYS   C N      1 
ATOM   6786  C  CA     . CYS   C 1  4   ? -20.114 -41.046  -4.780  1.00 35.21  ? 4   CYS   C CA     1 
ATOM   6787  C  C      . CYS   C 1  4   ? -20.300 -40.556  -6.210  1.00 41.79  ? 4   CYS   C C      1 
ATOM   6788  O  O      . CYS   C 1  4   ? -19.630 -41.049  -7.125  1.00 45.54  ? 4   CYS   C O      1 
ATOM   6789  C  CB     . CYS   C 1  4   ? -18.797 -40.505  -4.213  1.00 42.05  ? 4   CYS   C CB     1 
ATOM   6790  S  SG     . CYS   C 1  4   ? -18.437 -40.852  -2.444  1.00 54.36  ? 4   CYS   C SG     1 
ATOM   6791  N  N      . ILE   C 1  5   ? -21.199 -39.597  -6.417  1.00 40.40  ? 5   ILE   C N      1 
ATOM   6792  C  CA     . ILE   C 1  5   ? -21.441 -39.037  -7.744  1.00 38.14  ? 5   ILE   C CA     1 
ATOM   6793  C  C      . ILE   C 1  5   ? -20.904 -37.614  -7.780  1.00 41.39  ? 5   ILE   C C      1 
ATOM   6794  O  O      . ILE   C 1  5   ? -21.200 -36.804  -6.892  1.00 42.72  ? 5   ILE   C O      1 
ATOM   6795  C  CB     . ILE   C 1  5   ? -22.928 -39.057  -8.120  1.00 37.32  ? 5   ILE   C CB     1 
ATOM   6796  C  CG1    . ILE   C 1  5   ? -23.420 -40.485  -8.261  1.00 36.92  ? 5   ILE   C CG1    1 
ATOM   6797  C  CG2    . ILE   C 1  5   ? -23.132 -38.314  -9.407  1.00 33.14  ? 5   ILE   C CG2    1 
ATOM   6798  C  CD1    . ILE   C 1  5   ? -24.916 -40.604  -8.143  1.00 34.29  ? 5   ILE   C CD1    1 
ATOM   6799  N  N      . SER   C 1  6   ? -20.125 -37.310  -8.809  1.00 35.41  ? 6   SER   C N      1 
ATOM   6800  C  CA     . SER   C 1  6   ? -19.478 -36.020  -8.940  1.00 34.35  ? 6   SER   C CA     1 
ATOM   6801  C  C      . SER   C 1  6   ? -20.258 -35.121  -9.902  1.00 38.36  ? 6   SER   C C      1 
ATOM   6802  O  O      . SER   C 1  6   ? -20.723 -35.562  -10.956 1.00 40.14  ? 6   SER   C O      1 
ATOM   6803  C  CB     . SER   C 1  6   ? -18.048 -36.220  -9.431  1.00 40.67  ? 6   SER   C CB     1 
ATOM   6804  O  OG     . SER   C 1  6   ? -17.273 -36.896  -8.461  1.00 46.78  ? 6   SER   C OG     1 
ATOM   6805  N  N      . ILE   C 1  7   ? -20.411 -33.856  -9.539  1.00 33.85  ? 7   ILE   C N      1 
ATOM   6806  C  CA     . ILE   C 1  7   ? -21.082 -32.898  -10.397 1.00 31.22  ? 7   ILE   C CA     1 
ATOM   6807  C  C      . ILE   C 1  7   ? -20.155 -31.707  -10.561 1.00 36.46  ? 7   ILE   C C      1 
ATOM   6808  O  O      . ILE   C 1  7   ? -19.832 -31.032  -9.575  1.00 35.01  ? 7   ILE   C O      1 
ATOM   6809  C  CB     . ILE   C 1  7   ? -22.435 -32.458  -9.834  1.00 29.28  ? 7   ILE   C CB     1 
ATOM   6810  C  CG1    . ILE   C 1  7   ? -23.293 -33.667  -9.500  1.00 35.08  ? 7   ILE   C CG1    1 
ATOM   6811  C  CG2    . ILE   C 1  7   ? -23.122 -31.560  -10.801 1.00 27.14  ? 7   ILE   C CG2    1 
ATOM   6812  C  CD1    . ILE   C 1  7   ? -24.649 -33.281  -8.921  1.00 34.49  ? 7   ILE   C CD1    1 
ATOM   6813  N  N      . HIS   C 1  8   ? -19.732 -31.459  -11.806 1.00 36.27  ? 8   HIS   C N      1 
ATOM   6814  C  CA     . HIS   C 1  8   ? -18.832 -30.388  -12.203 1.00 30.89  ? 8   HIS   C CA     1 
ATOM   6815  C  C      . HIS   C 1  8   ? -19.632 -29.339  -12.967 1.00 29.36  ? 8   HIS   C C      1 
ATOM   6816  O  O      . HIS   C 1  8   ? -20.211 -29.647  -14.010 1.00 32.40  ? 8   HIS   C O      1 
ATOM   6817  C  CB     . HIS   C 1  8   ? -17.712 -30.959  -13.075 1.00 37.50  ? 8   HIS   C CB     1 
ATOM   6818  C  CG     . HIS   C 1  8   ? -17.007 -32.144  -12.478 1.00 34.52  ? 8   HIS   C CG     1 
ATOM   6819  N  ND1    . HIS   C 1  8   ? -15.878 -32.031  -11.698 1.00 35.54  ? 8   HIS   C ND1    1 
ATOM   6820  C  CD2    . HIS   C 1  8   ? -17.288 -33.464  -12.535 1.00 35.32  ? 8   HIS   C CD2    1 
ATOM   6821  C  CE1    . HIS   C 1  8   ? -15.484 -33.230  -11.315 1.00 35.27  ? 8   HIS   C CE1    1 
ATOM   6822  N  NE2    . HIS   C 1  8   ? -16.326 -34.117  -11.807 1.00 34.87  ? 8   HIS   C NE2    1 
ATOM   6823  N  N      . VAL   C 1  9   ? -19.635 -28.103  -12.469 1.00 27.61  ? 9   VAL   C N      1 
ATOM   6824  C  CA     . VAL   C 1  9   ? -20.487 -27.023  -12.968 1.00 31.54  ? 9   VAL   C CA     1 
ATOM   6825  C  C      . VAL   C 1  9   ? -19.653 -25.818  -13.392 1.00 31.99  ? 9   VAL   C C      1 
ATOM   6826  O  O      . VAL   C 1  9   ? -18.801 -25.340  -12.630 1.00 35.03  ? 9   VAL   C O      1 
ATOM   6827  C  CB     . VAL   C 1  9   ? -21.544 -26.595  -11.925 1.00 32.10  ? 9   VAL   C CB     1 
ATOM   6828  C  CG1    . VAL   C 1  9   ? -22.399 -25.445  -12.473 1.00 29.34  ? 9   VAL   C CG1    1 
ATOM   6829  C  CG2    . VAL   C 1  9   ? -22.432 -27.764  -11.592 1.00 24.40  ? 9   VAL   C CG2    1 
ATOM   6830  N  N      . GLY   C 1  10  ? -19.950 -25.292  -14.585 1.00 33.45  ? 10  GLY   C N      1 
ATOM   6831  C  CA     . GLY   C 1  10  ? -19.174 -24.227  -15.189 1.00 33.59  ? 10  GLY   C CA     1 
ATOM   6832  C  C      . GLY   C 1  10  ? -17.776 -24.678  -15.611 1.00 33.74  ? 10  GLY   C C      1 
ATOM   6833  O  O      . GLY   C 1  10  ? -17.327 -25.809  -15.390 1.00 34.34  ? 10  GLY   C O      1 
ATOM   6834  N  N      . GLN   C 1  11  ? -17.069 -23.730  -16.214 1.00 28.31  ? 11  GLN   C N      1 
ATOM   6835  C  CA     . GLN   C 1  11  ? -15.704 -23.959  -16.645 1.00 25.70  ? 11  GLN   C CA     1 
ATOM   6836  C  C      . GLN   C 1  11  ? -14.828 -24.484  -15.508 1.00 31.46  ? 11  GLN   C C      1 
ATOM   6837  O  O      . GLN   C 1  11  ? -14.187 -25.530  -15.635 1.00 34.43  ? 11  GLN   C O      1 
ATOM   6838  C  CB     . GLN   C 1  11  ? -15.148 -22.663  -17.173 1.00 26.98  ? 11  GLN   C CB     1 
ATOM   6839  C  CG     . GLN   C 1  11  ? -13.756 -22.731  -17.635 1.00 28.20  ? 11  GLN   C CG     1 
ATOM   6840  C  CD     . GLN   C 1  11  ? -13.330 -21.371  -18.065 1.00 35.08  ? 11  GLN   C CD     1 
ATOM   6841  O  OE1    . GLN   C 1  11  ? -13.962 -20.744  -18.928 1.00 40.57  ? 11  GLN   C OE1    1 
ATOM   6842  N  NE2    . GLN   C 1  11  ? -12.257 -20.876  -17.459 1.00 35.90  ? 11  GLN   C NE2    1 
ATOM   6843  N  N      . ALA   C 1  12  ? -14.766 -23.760  -14.383 1.00 29.50  ? 12  ALA   C N      1 
ATOM   6844  C  CA     . ALA   C 1  12  ? -13.820 -24.125  -13.327 1.00 28.27  ? 12  ALA   C CA     1 
ATOM   6845  C  C      . ALA   C 1  12  ? -14.105 -25.517  -12.795 1.00 33.76  ? 12  ALA   C C      1 
ATOM   6846  O  O      . ALA   C 1  12  ? -13.186 -26.327  -12.615 1.00 34.33  ? 12  ALA   C O      1 
ATOM   6847  C  CB     . ALA   C 1  12  ? -13.858 -23.115  -12.188 1.00 30.86  ? 12  ALA   C CB     1 
ATOM   6848  N  N      . GLY   C 1  13  ? -15.379 -25.812  -12.526 1.00 32.78  ? 13  GLY   C N      1 
ATOM   6849  C  CA     . GLY   C 1  13  ? -15.731 -27.161  -12.149 1.00 28.34  ? 13  GLY   C CA     1 
ATOM   6850  C  C      . GLY   C 1  13  ? -15.368 -28.146  -13.236 1.00 31.55  ? 13  GLY   C C      1 
ATOM   6851  O  O      . GLY   C 1  13  ? -14.772 -29.188  -12.969 1.00 32.43  ? 13  GLY   C O      1 
ATOM   6852  N  N      . VAL   C 1  14  ? -15.718 -27.824  -14.484 1.00 29.35  ? 14  VAL   C N      1 
ATOM   6853  C  CA     . VAL   C 1  14  ? -15.480 -28.766  -15.574 1.00 29.88  ? 14  VAL   C CA     1 
ATOM   6854  C  C      . VAL   C 1  14  ? -13.991 -29.024  -15.737 1.00 32.84  ? 14  VAL   C C      1 
ATOM   6855  O  O      . VAL   C 1  14  ? -13.534 -30.170  -15.753 1.00 33.25  ? 14  VAL   C O      1 
ATOM   6856  C  CB     . VAL   C 1  14  ? -16.101 -28.253  -16.883 1.00 28.24  ? 14  VAL   C CB     1 
ATOM   6857  C  CG1    . VAL   C 1  14  ? -15.475 -28.985  -18.048 1.00 28.68  ? 14  VAL   C CG1    1 
ATOM   6858  C  CG2    . VAL   C 1  14  ? -17.595 -28.485  -16.868 1.00 31.05  ? 14  VAL   C CG2    1 
ATOM   6859  N  N      . GLN   C 1  15  ? -13.215 -27.953  -15.876 1.00 33.11  ? 15  GLN   C N      1 
ATOM   6860  C  CA     . GLN   C 1  15  ? -11.782 -28.083  -16.040 1.00 28.15  ? 15  GLN   C CA     1 
ATOM   6861  C  C      . GLN   C 1  15  ? -11.131 -28.673  -14.797 1.00 34.73  ? 15  GLN   C C      1 
ATOM   6862  O  O      . GLN   C 1  15  ? -10.189 -29.459  -14.905 1.00 35.95  ? 15  GLN   C O      1 
ATOM   6863  C  CB     . GLN   C 1  15  ? -11.211 -26.715  -16.398 1.00 30.91  ? 15  GLN   C CB     1 
ATOM   6864  C  CG     . GLN   C 1  15  ? -11.376 -26.433  -17.867 1.00 32.53  ? 15  GLN   C CG     1 
ATOM   6865  C  CD     . GLN   C 1  15  ? -11.019 -25.032  -18.325 1.00 35.64  ? 15  GLN   C CD     1 
ATOM   6866  O  OE1    . GLN   C 1  15  ? -10.669 -24.163  -17.527 1.00 39.79  ? 15  GLN   C OE1    1 
ATOM   6867  N  NE2    . GLN   C 1  15  ? -11.081 -24.816  -19.649 1.00 39.48  ? 15  GLN   C NE2    1 
ATOM   6868  N  N      . ILE   C 1  16  ? -11.626 -28.349  -13.604 1.00 32.98  ? 16  ILE   C N      1 
ATOM   6869  C  CA     . ILE   C 1  16  ? -11.060 -29.027  -12.440 1.00 35.33  ? 16  ILE   C CA     1 
ATOM   6870  C  C      . ILE   C 1  16  ? -11.432 -30.512  -12.419 1.00 34.48  ? 16  ILE   C C      1 
ATOM   6871  O  O      . ILE   C 1  16  ? -10.619 -31.354  -12.028 1.00 33.88  ? 16  ILE   C O      1 
ATOM   6872  C  CB     . ILE   C 1  16  ? -11.460 -28.285  -11.156 1.00 32.59  ? 16  ILE   C CB     1 
ATOM   6873  C  CG1    . ILE   C 1  16  ? -10.701 -26.965  -11.106 1.00 30.70  ? 16  ILE   C CG1    1 
ATOM   6874  C  CG2    . ILE   C 1  16  ? -11.183 -29.128  -9.925  1.00 31.34  ? 16  ILE   C CG2    1 
ATOM   6875  C  CD1    . ILE   C 1  16  ? -11.176 -26.034  -10.067 1.00 32.88  ? 16  ILE   C CD1    1 
ATOM   6876  N  N      . GLY   C 1  17  ? -12.639 -30.865  -12.857 1.00 36.70  ? 17  GLY   C N      1 
ATOM   6877  C  CA     . GLY   C 1  17  ? -12.981 -32.271  -12.992 1.00 33.74  ? 17  GLY   C CA     1 
ATOM   6878  C  C      . GLY   C 1  17  ? -12.098 -32.994  -13.996 1.00 37.92  ? 17  GLY   C C      1 
ATOM   6879  O  O      . GLY   C 1  17  ? -11.675 -34.129  -13.762 1.00 39.60  ? 17  GLY   C O      1 
ATOM   6880  N  N      . ASN   C 1  18  ? -11.809 -32.361  -15.131 1.00 32.37  ? 18  ASN   C N      1 
ATOM   6881  C  CA     . ASN   C 1  18  ? -10.829 -32.940  -16.042 1.00 33.98  ? 18  ASN   C CA     1 
ATOM   6882  C  C      . ASN   C 1  18  ? -9.541  -33.294  -15.318 1.00 33.73  ? 18  ASN   C C      1 
ATOM   6883  O  O      . ASN   C 1  18  ? -9.044  -34.412  -15.440 1.00 34.47  ? 18  ASN   C O      1 
ATOM   6884  C  CB     . ASN   C 1  18  ? -10.552 -31.982  -17.194 1.00 36.41  ? 18  ASN   C CB     1 
ATOM   6885  C  CG     . ASN   C 1  18  ? -11.573 -32.104  -18.297 1.00 46.48  ? 18  ASN   C CG     1 
ATOM   6886  O  OD1    . ASN   C 1  18  ? -12.084 -31.089  -18.798 1.00 50.99  ? 18  ASN   C OD1    1 
ATOM   6887  N  ND2    . ASN   C 1  18  ? -11.837 -33.356  -18.736 1.00 47.07  ? 18  ASN   C ND2    1 
ATOM   6888  N  N      . ALA   C 1  19  ? -8.993  -32.347  -14.554 1.00 33.76  ? 19  ALA   C N      1 
ATOM   6889  C  CA     . ALA   C 1  19  ? -7.765  -32.597  -13.801 1.00 38.08  ? 19  ALA   C CA     1 
ATOM   6890  C  C      . ALA   C 1  19  ? -7.911  -33.808  -12.882 1.00 41.95  ? 19  ALA   C C      1 
ATOM   6891  O  O      . ALA   C 1  19  ? -7.032  -34.687  -12.849 1.00 43.21  ? 19  ALA   C O      1 
ATOM   6892  C  CB     . ALA   C 1  19  ? -7.374  -31.358  -12.989 1.00 34.63  ? 19  ALA   C CB     1 
ATOM   6893  N  N      . CYS   C 1  20  ? -9.017  -33.867  -12.125 1.00 33.76  ? 20  CYS   C N      1 
ATOM   6894  C  CA     . CYS   C 1  20  ? -9.190  -34.921  -11.137 1.00 35.03  ? 20  CYS   C CA     1 
ATOM   6895  C  C      . CYS   C 1  20  ? -9.357  -36.281  -11.798 1.00 38.97  ? 20  CYS   C C      1 
ATOM   6896  O  O      . CYS   C 1  20  ? -8.768  -37.275  -11.349 1.00 36.40  ? 20  CYS   C O      1 
ATOM   6897  C  CB     . CYS   C 1  20  ? -10.390 -34.624  -10.265 1.00 34.08  ? 20  CYS   C CB     1 
ATOM   6898  S  SG     . CYS   C 1  20  ? -10.146 -33.244  -9.259  1.00 45.01  ? 20  CYS   C SG     1 
ATOM   6899  N  N      . TRP   C 1  21  ? -10.170 -36.362  -12.850 1.00 35.64  ? 21  TRP   C N      1 
ATOM   6900  C  CA     . TRP   C 1  21  ? -10.409 -37.685  -13.401 1.00 37.14  ? 21  TRP   C CA     1 
ATOM   6901  C  C      . TRP   C 1  21  ? -9.194  -38.191  -14.167 1.00 39.04  ? 21  TRP   C C      1 
ATOM   6902  O  O      . TRP   C 1  21  ? -8.914  -39.392  -14.146 1.00 41.01  ? 21  TRP   C O      1 
ATOM   6903  C  CB     . TRP   C 1  21  ? -11.669 -37.681  -14.254 1.00 35.81  ? 21  TRP   C CB     1 
ATOM   6904  C  CG     . TRP   C 1  21  ? -12.908 -37.580  -13.403 1.00 36.65  ? 21  TRP   C CG     1 
ATOM   6905  C  CD1    . TRP   C 1  21  ? -13.647 -36.455  -13.181 1.00 37.34  ? 21  TRP   C CD1    1 
ATOM   6906  C  CD2    . TRP   C 1  21  ? -13.542 -38.627  -12.654 1.00 36.83  ? 21  TRP   C CD2    1 
ATOM   6907  N  NE1    . TRP   C 1  21  ? -14.698 -36.731  -12.352 1.00 37.25  ? 21  TRP   C NE1    1 
ATOM   6908  C  CE2    . TRP   C 1  21  ? -14.660 -38.060  -12.013 1.00 39.50  ? 21  TRP   C CE2    1 
ATOM   6909  C  CE3    . TRP   C 1  21  ? -13.284 -39.990  -12.469 1.00 40.09  ? 21  TRP   C CE3    1 
ATOM   6910  C  CZ2    . TRP   C 1  21  ? -15.519 -38.812  -11.193 1.00 38.35  ? 21  TRP   C CZ2    1 
ATOM   6911  C  CZ3    . TRP   C 1  21  ? -14.138 -40.727  -11.642 1.00 38.05  ? 21  TRP   C CZ3    1 
ATOM   6912  C  CH2    . TRP   C 1  21  ? -15.232 -40.135  -11.021 1.00 35.50  ? 21  TRP   C CH2    1 
ATOM   6913  N  N      . GLU   C 1  22  ? -8.418  -37.311  -14.794 1.00 37.85  ? 22  GLU   C N      1 
ATOM   6914  C  CA     . GLU   C 1  22  ? -7.177  -37.801  -15.366 1.00 35.35  ? 22  GLU   C CA     1 
ATOM   6915  C  C      . GLU   C 1  22  ? -6.281  -38.345  -14.271 1.00 44.45  ? 22  GLU   C C      1 
ATOM   6916  O  O      . GLU   C 1  22  ? -5.575  -39.347  -14.472 1.00 47.75  ? 22  GLU   C O      1 
ATOM   6917  C  CB     . GLU   C 1  22  ? -6.470  -36.710  -16.162 1.00 41.59  ? 22  GLU   C CB     1 
ATOM   6918  C  CG     . GLU   C 1  22  ? -5.003  -37.025  -16.499 1.00 53.13  ? 22  GLU   C CG     1 
ATOM   6919  C  CD     . GLU   C 1  22  ? -4.382  -36.038  -17.501 1.00 52.11  ? 22  GLU   C CD     1 
ATOM   6920  O  OE1    . GLU   C 1  22  ? -4.656  -34.820  -17.414 1.00 52.28  ? 22  GLU   C OE1    1 
ATOM   6921  O  OE2    . GLU   C 1  22  ? -3.670  -36.506  -18.420 1.00 44.30  ? 22  GLU   C OE2    1 
ATOM   6922  N  N      . LEU   C 1  23  ? -6.341  -37.742  -13.083 1.00 42.19  ? 23  LEU   C N      1 
ATOM   6923  C  CA     . LEU   C 1  23  ? -5.465  -38.199  -12.021 1.00 36.83  ? 23  LEU   C CA     1 
ATOM   6924  C  C      . LEU   C 1  23  ? -5.983  -39.480  -11.400 1.00 41.14  ? 23  LEU   C C      1 
ATOM   6925  O  O      . LEU   C 1  23  ? -5.188  -40.370  -11.094 1.00 46.10  ? 23  LEU   C O      1 
ATOM   6926  C  CB     . LEU   C 1  23  ? -5.310  -37.114  -10.975 1.00 36.41  ? 23  LEU   C CB     1 
ATOM   6927  C  CG     . LEU   C 1  23  ? -4.444  -37.534  -9.804  1.00 37.76  ? 23  LEU   C CG     1 
ATOM   6928  C  CD1    . LEU   C 1  23  ? -3.096  -37.835  -10.353 1.00 38.49  ? 23  LEU   C CD1    1 
ATOM   6929  C  CD2    . LEU   C 1  23  ? -4.375  -36.380  -8.820  1.00 40.37  ? 23  LEU   C CD2    1 
ATOM   6930  N  N      . TYR   C 1  24  ? -7.304  -39.597  -11.207 1.00 38.25  ? 24  TYR   C N      1 
ATOM   6931  C  CA     . TYR   C 1  24  ? -7.877  -40.843  -10.697 1.00 38.59  ? 24  TYR   C CA     1 
ATOM   6932  C  C      . TYR   C 1  24  ? -7.493  -42.013  -11.585 1.00 43.92  ? 24  TYR   C C      1 
ATOM   6933  O  O      . TYR   C 1  24  ? -7.021  -43.055  -11.105 1.00 42.56  ? 24  TYR   C O      1 
ATOM   6934  C  CB     . TYR   C 1  24  ? -9.399  -40.748  -10.631 1.00 39.15  ? 24  TYR   C CB     1 
ATOM   6935  C  CG     . TYR   C 1  24  ? -9.918  -39.737  -9.647  1.00 42.06  ? 24  TYR   C CG     1 
ATOM   6936  C  CD1    . TYR   C 1  24  ? -9.094  -39.227  -8.648  1.00 40.12  ? 24  TYR   C CD1    1 
ATOM   6937  C  CD2    . TYR   C 1  24  ? -11.243 -39.311  -9.693  1.00 37.51  ? 24  TYR   C CD2    1 
ATOM   6938  C  CE1    . TYR   C 1  24  ? -9.567  -38.309  -7.739  1.00 36.35  ? 24  TYR   C CE1    1 
ATOM   6939  C  CE2    . TYR   C 1  24  ? -11.720 -38.402  -8.786  1.00 39.94  ? 24  TYR   C CE2    1 
ATOM   6940  C  CZ     . TYR   C 1  24  ? -10.874 -37.899  -7.817  1.00 40.52  ? 24  TYR   C CZ     1 
ATOM   6941  O  OH     . TYR   C 1  24  ? -11.348 -36.984  -6.920  1.00 46.19  ? 24  TYR   C OH     1 
ATOM   6942  N  N      . CYS   C 1  25  ? -7.737  -41.867  -12.890 1.00 41.39  ? 25  CYS   C N      1 
ATOM   6943  C  CA     . CYS   C 1  25  ? -7.327  -42.878  -13.851 1.00 42.19  ? 25  CYS   C CA     1 
ATOM   6944  C  C      . CYS   C 1  25  ? -5.865  -43.255  -13.665 1.00 47.61  ? 25  CYS   C C      1 
ATOM   6945  O  O      . CYS   C 1  25  ? -5.516  -44.439  -13.681 1.00 48.82  ? 25  CYS   C O      1 
ATOM   6946  C  CB     . CYS   C 1  25  ? -7.554  -42.361  -15.259 1.00 42.14  ? 25  CYS   C CB     1 
ATOM   6947  S  SG     . CYS   C 1  25  ? -9.272  -42.266  -15.667 1.00 50.85  ? 25  CYS   C SG     1 
ATOM   6948  N  N      . LEU   C 1  26  ? -4.985  -42.266  -13.504 1.00 44.05  ? 26  LEU   C N      1 
ATOM   6949  C  CA     . LEU   C 1  26  ? -3.590  -42.627  -13.301 1.00 43.25  ? 26  LEU   C CA     1 
ATOM   6950  C  C      . LEU   C 1  26  ? -3.385  -43.339  -11.975 1.00 42.63  ? 26  LEU   C C      1 
ATOM   6951  O  O      . LEU   C 1  26  ? -2.570  -44.256  -11.895 1.00 49.47  ? 26  LEU   C O      1 
ATOM   6952  C  CB     . LEU   C 1  26  ? -2.687  -41.402  -13.396 1.00 44.24  ? 26  LEU   C CB     1 
ATOM   6953  C  CG     . LEU   C 1  26  ? -2.650  -40.733  -14.771 1.00 42.48  ? 26  LEU   C CG     1 
ATOM   6954  C  CD1    . LEU   C 1  26  ? -1.781  -39.490  -14.728 1.00 49.53  ? 26  LEU   C CD1    1 
ATOM   6955  C  CD2    . LEU   C 1  26  ? -2.193  -41.669  -15.858 1.00 45.65  ? 26  LEU   C CD2    1 
ATOM   6956  N  N      . GLU   C 1  27  ? -4.112  -42.956  -10.933 1.00 43.11  ? 27  GLU   C N      1 
ATOM   6957  C  CA     . GLU   C 1  27  ? -3.916  -43.602  -9.635  1.00 46.36  ? 27  GLU   C CA     1 
ATOM   6958  C  C      . GLU   C 1  27  ? -4.434  -45.035  -9.632  1.00 45.00  ? 27  GLU   C C      1 
ATOM   6959  O  O      . GLU   C 1  27  ? -3.954  -45.858  -8.846  1.00 49.23  ? 27  GLU   C O      1 
ATOM   6960  C  CB     . GLU   C 1  27  ? -4.617  -42.814  -8.530  1.00 42.93  ? 27  GLU   C CB     1 
ATOM   6961  C  CG     . GLU   C 1  27  ? -4.024  -41.472  -8.293  1.00 43.69  ? 27  GLU   C CG     1 
ATOM   6962  C  CD     . GLU   C 1  27  ? -4.655  -40.762  -7.138  1.00 41.46  ? 27  GLU   C CD     1 
ATOM   6963  O  OE1    . GLU   C 1  27  ? -5.521  -41.378  -6.488  1.00 42.91  ? 27  GLU   C OE1    1 
ATOM   6964  O  OE2    . GLU   C 1  27  ? -4.312  -39.578  -6.911  1.00 41.06  ? 27  GLU   C OE2    1 
ATOM   6965  N  N      . HIS   C 1  28  ? -5.411  -45.348  -10.482 1.00 40.42  ? 28  HIS   C N      1 
ATOM   6966  C  CA     . HIS   C 1  28  ? -6.037  -46.662  -10.511 1.00 41.78  ? 28  HIS   C CA     1 
ATOM   6967  C  C      . HIS   C 1  28  ? -5.635  -47.483  -11.739 1.00 45.84  ? 28  HIS   C C      1 
ATOM   6968  O  O      . HIS   C 1  28  ? -6.177  -48.571  -11.960 1.00 47.26  ? 28  HIS   C O      1 
ATOM   6969  C  CB     . HIS   C 1  28  ? -7.560  -46.504  -10.447 1.00 39.88  ? 28  HIS   C CB     1 
ATOM   6970  C  CG     . HIS   C 1  28  ? -8.057  -45.876  -9.178  1.00 40.31  ? 28  HIS   C CG     1 
ATOM   6971  N  ND1    . HIS   C 1  28  ? -7.993  -46.513  -7.957  1.00 43.75  ? 28  HIS   C ND1    1 
ATOM   6972  C  CD2    . HIS   C 1  28  ? -8.638  -44.678  -8.941  1.00 40.21  ? 28  HIS   C CD2    1 
ATOM   6973  C  CE1    . HIS   C 1  28  ? -8.510  -45.736  -7.022  1.00 37.52  ? 28  HIS   C CE1    1 
ATOM   6974  N  NE2    . HIS   C 1  28  ? -8.908  -44.616  -7.593  1.00 41.08  ? 28  HIS   C NE2    1 
ATOM   6975  N  N      . GLY   C 1  29  ? -4.696  -46.997  -12.540 1.00 45.44  ? 29  GLY   C N      1 
ATOM   6976  C  CA     . GLY   C 1  29  ? -4.317  -47.725  -13.736 1.00 41.99  ? 29  GLY   C CA     1 
ATOM   6977  C  C      . GLY   C 1  29  ? -5.451  -47.948  -14.710 1.00 49.14  ? 29  GLY   C C      1 
ATOM   6978  O  O      . GLY   C 1  29  ? -5.566  -49.040  -15.282 1.00 60.12  ? 29  GLY   C O      1 
ATOM   6979  N  N      . ILE   C 1  30  ? -6.308  -46.957  -14.886 1.00 42.71  ? 30  ILE   C N      1 
ATOM   6980  C  CA     . ILE   C 1  30  ? -7.337  -46.998  -15.914 1.00 44.73  ? 30  ILE   C CA     1 
ATOM   6981  C  C      . ILE   C 1  30  ? -6.787  -46.293  -17.132 1.00 50.18  ? 30  ILE   C C      1 
ATOM   6982  O  O      . ILE   C 1  30  ? -6.089  -45.281  -17.011 1.00 48.56  ? 30  ILE   C O      1 
ATOM   6983  C  CB     . ILE   C 1  30  ? -8.643  -46.339  -15.435 1.00 45.10  ? 30  ILE   C CB     1 
ATOM   6984  C  CG1    . ILE   C 1  30  ? -9.155  -47.009  -14.169 1.00 45.74  ? 30  ILE   C CG1    1 
ATOM   6985  C  CG2    . ILE   C 1  30  ? -9.692  -46.380  -16.514 1.00 44.52  ? 30  ILE   C CG2    1 
ATOM   6986  C  CD1    . ILE   C 1  30  ? -10.472 -46.469  -13.712 1.00 40.35  ? 30  ILE   C CD1    1 
ATOM   6987  N  N      . GLN   C 1  31  ? -7.075  -46.836  -18.305 1.00 56.89  ? 31  GLN   C N      1 
ATOM   6988  C  CA     . GLN   C 1  31  ? -6.605  -46.221  -19.533 1.00 52.82  ? 31  GLN   C CA     1 
ATOM   6989  C  C      . GLN   C 1  31  ? -7.640  -45.262  -20.092 1.00 55.71  ? 31  GLN   C C      1 
ATOM   6990  O  O      . GLN   C 1  31  ? -8.816  -45.294  -19.717 1.00 57.16  ? 31  GLN   C O      1 
ATOM   6991  C  CB     . GLN   C 1  31  ? -6.283  -47.289  -20.564 1.00 56.73  ? 31  GLN   C CB     1 
ATOM   6992  C  CG     . GLN   C 1  31  ? -5.287  -48.312  -20.075 1.00 63.65  ? 31  GLN   C CG     1 
ATOM   6993  C  CD     . GLN   C 1  31  ? -5.385  -49.619  -20.839 1.00 72.73  ? 31  GLN   C CD     1 
ATOM   6994  O  OE1    . GLN   C 1  31  ? -6.020  -49.691  -21.908 1.00 71.74  ? 31  GLN   C OE1    1 
ATOM   6995  N  NE2    . GLN   C 1  31  ? -4.766  -50.669  -20.290 1.00 69.05  ? 31  GLN   C NE2    1 
ATOM   6996  N  N      . PRO   C 1  32  ? -7.229  -44.379  -20.994 1.00 52.82  ? 32  PRO   C N      1 
ATOM   6997  C  CA     . PRO   C 1  32  ? -8.185  -43.418  -21.549 1.00 55.69  ? 32  PRO   C CA     1 
ATOM   6998  C  C      . PRO   C 1  32  ? -9.367  -44.062  -22.258 1.00 59.54  ? 32  PRO   C C      1 
ATOM   6999  O  O      . PRO   C 1  32  ? -10.383 -43.386  -22.467 1.00 58.32  ? 32  PRO   C O      1 
ATOM   7000  C  CB     . PRO   C 1  32  ? -7.317  -42.593  -22.505 1.00 49.90  ? 32  PRO   C CB     1 
ATOM   7001  C  CG     . PRO   C 1  32  ? -5.974  -42.695  -21.925 1.00 46.24  ? 32  PRO   C CG     1 
ATOM   7002  C  CD     . PRO   C 1  32  ? -5.851  -44.071  -21.394 1.00 44.08  ? 32  PRO   C CD     1 
ATOM   7003  N  N      . ASP   C 1  33  ? -9.272  -45.335  -22.656 1.00 63.07  ? 33  ASP   C N      1 
ATOM   7004  C  CA     . ASP   C 1  33  ? -10.437 -46.054  -23.156 1.00 62.24  ? 33  ASP   C CA     1 
ATOM   7005  C  C      . ASP   C 1  33  ? -11.152 -46.822  -22.051 1.00 63.34  ? 33  ASP   C C      1 
ATOM   7006  O  O      . ASP   C 1  33  ? -11.796 -47.848  -22.320 1.00 70.70  ? 33  ASP   C O      1 
ATOM   7007  C  CB     . ASP   C 1  33  ? -10.057 -46.991  -24.311 1.00 63.66  ? 33  ASP   C CB     1 
ATOM   7008  C  CG     . ASP   C 1  33  ? -9.139  -48.129  -23.889 1.00 68.21  ? 33  ASP   C CG     1 
ATOM   7009  O  OD1    . ASP   C 1  33  ? -8.605  -48.118  -22.750 1.00 58.64  ? 33  ASP   C OD1    1 
ATOM   7010  O  OD2    . ASP   C 1  33  ? -8.983  -49.059  -24.718 1.00 73.76  ? 33  ASP   C OD2    1 
ATOM   7011  N  N      . GLY   C 1  34  ? -11.047 -46.355  -20.809 1.00 55.36  ? 34  GLY   C N      1 
ATOM   7012  C  CA     . GLY   C 1  34  ? -11.728 -46.974  -19.692 1.00 57.28  ? 34  GLY   C CA     1 
ATOM   7013  C  C      . GLY   C 1  34  ? -11.287 -48.376  -19.320 1.00 54.45  ? 34  GLY   C C      1 
ATOM   7014  O  O      . GLY   C 1  34  ? -11.850 -48.953  -18.385 1.00 52.49  ? 34  GLY   C O      1 
ATOM   7015  N  N      . GLN   C 1  35  ? -10.307 -48.952  -19.993 1.00 52.59  ? 35  GLN   C N      1 
ATOM   7016  C  CA     . GLN   C 1  35  ? -9.967  -50.336  -19.719 1.00 58.05  ? 35  GLN   C CA     1 
ATOM   7017  C  C      . GLN   C 1  35  ? -8.953  -50.409  -18.586 1.00 58.65  ? 35  GLN   C C      1 
ATOM   7018  O  O      . GLN   C 1  35  ? -7.981  -49.645  -18.550 1.00 57.78  ? 35  GLN   C O      1 
ATOM   7019  C  CB     . GLN   C 1  35  ? -9.443  -51.032  -20.977 1.00 58.43  ? 35  GLN   C CB     1 
ATOM   7020  C  CG     . GLN   C 1  35  ? -10.441 -51.025  -22.114 1.00 59.16  ? 35  GLN   C CG     1 
ATOM   7021  C  CD     . GLN   C 1  35  ? -11.537 -52.049  -21.912 1.00 62.88  ? 35  GLN   C CD     1 
ATOM   7022  O  OE1    . GLN   C 1  35  ? -11.333 -53.071  -21.261 1.00 66.28  ? 35  GLN   C OE1    1 
ATOM   7023  N  NE2    . GLN   C 1  35  ? -12.718 -51.764  -22.439 1.00 67.11  ? 35  GLN   C NE2    1 
ATOM   7024  N  N      . MET   C 1  36  ? -9.186  -51.339  -17.662 1.00 57.06  ? 36  MET   C N      1 
ATOM   7025  C  CA     . MET   C 1  36  ? -8.384  -51.471  -16.445 1.00 59.33  ? 36  MET   C CA     1 
ATOM   7026  C  C      . MET   C 1  36  ? -7.844  -52.894  -16.348 1.00 60.83  ? 36  MET   C C      1 
ATOM   7027  O  O      . MET   C 1  36  ? -8.552  -53.796  -15.869 1.00 66.20  ? 36  MET   C O      1 
ATOM   7028  C  CB     . MET   C 1  36  ? -9.234  -51.107  -15.230 1.00 58.09  ? 36  MET   C CB     1 
ATOM   7029  C  CG     . MET   C 1  36  ? -8.524  -51.021  -13.880 1.00 57.20  ? 36  MET   C CG     1 
ATOM   7030  S  SD     . MET   C 1  36  ? -9.716  -50.640  -12.555 1.00 55.70  ? 36  MET   C SD     1 
ATOM   7031  C  CE     . MET   C 1  36  ? -8.645  -50.487  -11.145 1.00 45.70  ? 36  MET   C CE     1 
ATOM   7032  N  N      . PRO   C 1  37  ? -6.613  -53.140  -16.801 1.00 57.03  ? 37  PRO   C N      1 
ATOM   7033  C  CA     . PRO   C 1  37  ? -6.091  -54.523  -16.825 1.00 53.59  ? 37  PRO   C CA     1 
ATOM   7034  C  C      . PRO   C 1  37  ? -6.153  -55.246  -15.492 1.00 59.79  ? 37  PRO   C C      1 
ATOM   7035  O  O      . PRO   C 1  37  ? -6.392  -56.460  -15.463 1.00 56.09  ? 37  PRO   C O      1 
ATOM   7036  C  CB     . PRO   C 1  37  ? -4.639  -54.332  -17.278 1.00 57.96  ? 37  PRO   C CB     1 
ATOM   7037  C  CG     . PRO   C 1  37  ? -4.656  -53.063  -18.064 1.00 61.64  ? 37  PRO   C CG     1 
ATOM   7038  C  CD     . PRO   C 1  37  ? -5.690  -52.177  -17.417 1.00 60.59  ? 37  PRO   C CD     1 
ATOM   7039  N  N      . SER   C 1  38  ? -5.937  -54.521  -14.388 1.00 64.18  ? 38  SER   C N      1 
ATOM   7040  C  CA     . SER   C 1  38  ? -5.926  -55.125  -13.058 1.00 57.04  ? 38  SER   C CA     1 
ATOM   7041  C  C      . SER   C 1  38  ? -7.314  -55.574  -12.620 1.00 61.03  ? 38  SER   C C      1 
ATOM   7042  O  O      . SER   C 1  38  ? -7.453  -56.622  -11.977 1.00 67.52  ? 38  SER   C O      1 
ATOM   7043  C  CB     . SER   C 1  38  ? -5.343  -54.144  -12.050 1.00 55.81  ? 38  SER   C CB     1 
ATOM   7044  O  OG     . SER   C 1  38  ? -5.741  -52.825  -12.351 1.00 66.88  ? 38  SER   C OG     1 
ATOM   7045  N  N      . ASP   C 1  39  ? -8.354  -54.805  -12.939 1.00 60.02  ? 39  ASP   C N      1 
ATOM   7046  C  CA     . ASP   C 1  39  ? -9.693  -55.266  -12.587 1.00 63.06  ? 39  ASP   C CA     1 
ATOM   7047  C  C      . ASP   C 1  39  ? -9.944  -56.598  -13.287 1.00 63.81  ? 39  ASP   C C      1 
ATOM   7048  O  O      . ASP   C 1  39  ? -10.112 -56.648  -14.513 1.00 65.69  ? 39  ASP   C O      1 
ATOM   7049  C  CB     . ASP   C 1  39  ? -10.768 -54.240  -12.964 1.00 53.88  ? 39  ASP   C CB     1 
ATOM   7050  C  CG     . ASP   C 1  39  ? -12.114 -54.522  -12.299 1.00 57.32  ? 39  ASP   C CG     1 
ATOM   7051  O  OD1    . ASP   C 1  39  ? -12.282 -55.491  -11.537 1.00 58.52  ? 39  ASP   C OD1    1 
ATOM   7052  O  OD2    . ASP   C 1  39  ? -13.051 -53.769  -12.565 1.00 63.55  ? 39  ASP   C OD2    1 
ATOM   7053  N  N      . LYS   C 1  40  ? -9.935  -57.684  -12.522 1.00 56.13  ? 40  LYS   C N      1 
ATOM   7054  C  CA     . LYS   C 1  40  ? -10.314 -58.975  -13.064 1.00 55.47  ? 40  LYS   C CA     1 
ATOM   7055  C  C      . LYS   C 1  40  ? -11.816 -59.246  -12.955 1.00 61.16  ? 40  LYS   C C      1 
ATOM   7056  O  O      . LYS   C 1  40  ? -12.284 -60.253  -13.501 1.00 67.32  ? 40  LYS   C O      1 
ATOM   7057  C  CB     . LYS   C 1  40  ? -9.531  -60.065  -12.350 1.00 47.88  ? 40  LYS   C CB     1 
ATOM   7058  C  CG     . LYS   C 1  40  ? -8.046  -59.824  -12.345 1.00 54.40  ? 40  LYS   C CG     1 
ATOM   7059  C  CD     . LYS   C 1  40  ? -7.465  -59.807  -13.752 1.00 60.37  ? 40  LYS   C CD     1 
ATOM   7060  C  CE     . LYS   C 1  40  ? -6.044  -59.241  -13.741 1.00 59.03  ? 40  LYS   C CE     1 
ATOM   7061  N  NZ     . LYS   C 1  40  ? -5.356  -59.280  -15.065 1.00 57.43  ? 40  LYS   C NZ     1 
ATOM   7062  N  N      . THR   C 1  41  ? -12.576 -58.373  -12.274 1.00 56.78  ? 41  THR   C N      1 
ATOM   7063  C  CA     . THR   C 1  41  ? -14.019 -58.534  -12.062 1.00 59.83  ? 41  THR   C CA     1 
ATOM   7064  C  C      . THR   C 1  41  ? -14.740 -57.745  -13.143 1.00 65.61  ? 41  THR   C C      1 
ATOM   7065  O  O      . THR   C 1  41  ? -15.038 -56.556  -12.976 1.00 63.42  ? 41  THR   C O      1 
ATOM   7066  C  CB     . THR   C 1  41  ? -14.444 -58.038  -10.686 1.00 62.48  ? 41  THR   C CB     1 
ATOM   7067  O  OG1    . THR   C 1  41  ? -14.187 -56.618  -10.568 1.00 63.44  ? 41  THR   C OG1    1 
ATOM   7068  C  CG2    . THR   C 1  41  ? -13.692 -58.801  -9.606  1.00 54.25  ? 41  THR   C CG2    1 
ATOM   7069  N  N      . ILE   C 1  42  ? -15.054 -58.427  -14.243 1.00 58.93  ? 42  ILE   C N      1 
ATOM   7070  C  CA     . ILE   C 1  42  ? -15.538 -57.778  -15.454 1.00 55.31  ? 42  ILE   C CA     1 
ATOM   7071  C  C      . ILE   C 1  42  ? -17.010 -57.429  -15.300 1.00 61.65  ? 42  ILE   C C      1 
ATOM   7072  O  O      . ILE   C 1  42  ? -17.807 -58.231  -14.800 1.00 63.01  ? 42  ILE   C O      1 
ATOM   7073  C  CB     . ILE   C 1  42  ? -15.316 -58.709  -16.648 1.00 61.24  ? 42  ILE   C CB     1 
ATOM   7074  C  CG1    . ILE   C 1  42  ? -13.867 -59.159  -16.650 1.00 62.77  ? 42  ILE   C CG1    1 
ATOM   7075  C  CG2    . ILE   C 1  42  ? -15.662 -58.010  -17.944 1.00 61.22  ? 42  ILE   C CG2    1 
ATOM   7076  C  CD1    . ILE   C 1  42  ? -13.515 -59.971  -17.824 1.00 64.43  ? 42  ILE   C CD1    1 
ATOM   7077  N  N      . GLY   C 1  43  ? -17.379 -56.223  -15.741 1.00 66.81  ? 43  GLY   C N      1 
ATOM   7078  C  CA     . GLY   C 1  43  ? -18.756 -55.753  -15.674 1.00 63.20  ? 43  GLY   C CA     1 
ATOM   7079  C  C      . GLY   C 1  43  ? -19.236 -55.237  -14.325 1.00 59.37  ? 43  GLY   C C      1 
ATOM   7080  O  O      . GLY   C 1  43  ? -20.289 -54.573  -14.277 1.00 55.33  ? 43  GLY   C O      1 
ATOM   7081  N  N      . GLY   C 1  44  ? -18.521 -55.530  -13.241 1.00 57.91  ? 44  GLY   C N      1 
ATOM   7082  C  CA     . GLY   C 1  44  ? -18.918 -55.083  -11.919 1.00 60.60  ? 44  GLY   C CA     1 
ATOM   7083  C  C      . GLY   C 1  44  ? -17.837 -55.287  -10.865 1.00 64.13  ? 44  GLY   C C      1 
ATOM   7084  O  O      . GLY   C 1  44  ? -16.642 -55.421  -11.163 1.00 66.17  ? 44  GLY   C O      1 
ATOM   7085  N  N      . GLY   C 1  45  ? -18.282 -55.307  -9.615  1.00 60.35  ? 45  GLY   C N      1 
ATOM   7086  C  CA     . GLY   C 1  45  ? -17.374 -55.445  -8.485  1.00 66.07  ? 45  GLY   C CA     1 
ATOM   7087  C  C      . GLY   C 1  45  ? -17.715 -54.472  -7.372  1.00 63.41  ? 45  GLY   C C      1 
ATOM   7088  O  O      . GLY   C 1  45  ? -18.507 -53.542  -7.591  1.00 58.63  ? 45  GLY   C O      1 
ATOM   7089  N  N      . ASP   C 1  46  ? -17.151 -54.676  -6.173  1.00 63.53  ? 46  ASP   C N      1 
ATOM   7090  C  CA     . ASP   C 1  46  ? -17.328 -53.728  -5.070  1.00 66.45  ? 46  ASP   C CA     1 
ATOM   7091  C  C      . ASP   C 1  46  ? -15.989 -53.249  -4.528  1.00 58.13  ? 46  ASP   C C      1 
ATOM   7092  O  O      . ASP   C 1  46  ? -15.933 -52.721  -3.417  1.00 62.61  ? 46  ASP   C O      1 
ATOM   7093  C  CB     . ASP   C 1  46  ? -18.198 -54.304  -3.937  1.00 66.85  ? 46  ASP   C CB     1 
ATOM   7094  C  CG     . ASP   C 1  46  ? -17.630 -55.586  -3.332  1.00 79.02  ? 46  ASP   C CG     1 
ATOM   7095  O  OD1    . ASP   C 1  46  ? -16.819 -56.284  -4.004  1.00 80.72  ? 46  ASP   C OD1    1 
ATOM   7096  O  OD2    . ASP   C 1  46  ? -18.021 -55.904  -2.183  1.00 79.74  ? 46  ASP   C OD2    1 
ATOM   7097  N  N      . ASP   C 1  47  ? -14.916 -53.427  -5.300  1.00 50.78  ? 47  ASP   C N      1 
ATOM   7098  C  CA     . ASP   C 1  47  ? -13.604 -52.871  -5.002  1.00 49.66  ? 47  ASP   C CA     1 
ATOM   7099  C  C      . ASP   C 1  47  ? -13.659 -51.400  -4.609  1.00 52.45  ? 47  ASP   C C      1 
ATOM   7100  O  O      . ASP   C 1  47  ? -14.576 -50.672  -4.999  1.00 52.91  ? 47  ASP   C O      1 
ATOM   7101  C  CB     . ASP   C 1  47  ? -12.711 -53.057  -6.217  1.00 50.16  ? 47  ASP   C CB     1 
ATOM   7102  C  CG     . ASP   C 1  47  ? -12.464 -54.492  -6.504  1.00 57.52  ? 47  ASP   C CG     1 
ATOM   7103  O  OD1    . ASP   C 1  47  ? -12.314 -55.220  -5.508  1.00 55.25  ? 47  ASP   C OD1    1 
ATOM   7104  O  OD2    . ASP   C 1  47  ? -12.502 -54.909  -7.690  1.00 63.87  ? 47  ASP   C OD2    1 
ATOM   7105  N  N      . SER   C 1  48  ? -12.661 -50.936  -3.862  1.00 54.97  ? 48  SER   C N      1 
ATOM   7106  C  CA     . SER   C 1  48  ? -12.731 -49.577  -3.353  1.00 50.71  ? 48  SER   C CA     1 
ATOM   7107  C  C      . SER   C 1  48  ? -12.898 -48.567  -4.475  1.00 46.38  ? 48  SER   C C      1 
ATOM   7108  O  O      . SER   C 1  48  ? -13.658 -47.607  -4.328  1.00 44.94  ? 48  SER   C O      1 
ATOM   7109  C  CB     . SER   C 1  48  ? -11.503 -49.269  -2.509  1.00 53.23  ? 48  SER   C CB     1 
ATOM   7110  O  OG     . SER   C 1  48  ? -11.766 -49.642  -1.168  1.00 58.26  ? 48  SER   C OG     1 
ATOM   7111  N  N      . PHE   C 1  49  ? -12.228 -48.782  -5.618  1.00 44.16  ? 49  PHE   C N      1 
ATOM   7112  C  CA     . PHE   C 1  49  ? -12.322 -47.826  -6.721  1.00 42.31  ? 49  PHE   C CA     1 
ATOM   7113  C  C      . PHE   C 1  49  ? -13.682 -47.805  -7.382  1.00 42.66  ? 49  PHE   C C      1 
ATOM   7114  O  O      . PHE   C 1  49  ? -13.924 -46.924  -8.213  1.00 43.69  ? 49  PHE   C O      1 
ATOM   7115  C  CB     . PHE   C 1  49  ? -11.277 -48.082  -7.806  1.00 37.74  ? 49  PHE   C CB     1 
ATOM   7116  C  CG     . PHE   C 1  49  ? -11.405 -49.423  -8.484  1.00 48.60  ? 49  PHE   C CG     1 
ATOM   7117  C  CD1    . PHE   C 1  49  ? -12.268 -49.610  -9.553  1.00 46.83  ? 49  PHE   C CD1    1 
ATOM   7118  C  CD2    . PHE   C 1  49  ? -10.610 -50.496  -8.080  1.00 48.85  ? 49  PHE   C CD2    1 
ATOM   7119  C  CE1    . PHE   C 1  49  ? -12.366 -50.848  -10.160 1.00 50.08  ? 49  PHE   C CE1    1 
ATOM   7120  C  CE2    . PHE   C 1  49  ? -10.706 -51.727  -8.695  1.00 45.31  ? 49  PHE   C CE2    1 
ATOM   7121  C  CZ     . PHE   C 1  49  ? -11.579 -51.903  -9.731  1.00 48.23  ? 49  PHE   C CZ     1 
ATOM   7122  N  N      . ASN   C 1  50  ? -14.564 -48.740  -7.053  1.00 40.67  ? 50  ASN   C N      1 
ATOM   7123  C  CA     . ASN   C 1  50  ? -15.876 -48.729  -7.676  1.00 44.01  ? 50  ASN   C CA     1 
ATOM   7124  C  C      . ASN   C 1  50  ? -16.760 -47.617  -7.139  1.00 45.27  ? 50  ASN   C C      1 
ATOM   7125  O  O      . ASN   C 1  50  ? -17.808 -47.331  -7.735  1.00 40.34  ? 50  ASN   C O      1 
ATOM   7126  C  CB     . ASN   C 1  50  ? -16.526 -50.099  -7.503  1.00 43.46  ? 50  ASN   C CB     1 
ATOM   7127  C  CG     . ASN   C 1  50  ? -16.030 -51.088  -8.532  1.00 54.93  ? 50  ASN   C CG     1 
ATOM   7128  O  OD1    . ASN   C 1  50  ? -15.543 -52.180  -8.201  1.00 55.30  ? 50  ASN   C OD1    1 
ATOM   7129  N  ND2    . ASN   C 1  50  ? -16.159 -50.711  -9.808  1.00 54.51  ? 50  ASN   C ND2    1 
ATOM   7130  N  N      . THR   C 1  51  ? -16.354 -46.973  -6.045  1.00 45.16  ? 51  THR   C N      1 
ATOM   7131  C  CA     . THR   C 1  51  ? -17.158 -45.895  -5.493  1.00 44.37  ? 51  THR   C CA     1 
ATOM   7132  C  C      . THR   C 1  51  ? -17.152 -44.686  -6.413  1.00 44.01  ? 51  THR   C C      1 
ATOM   7133  O  O      . THR   C 1  51  ? -18.072 -43.859  -6.341  1.00 42.52  ? 51  THR   C O      1 
ATOM   7134  C  CB     . THR   C 1  51  ? -16.663 -45.528  -4.089  1.00 40.79  ? 51  THR   C CB     1 
ATOM   7135  O  OG1    . THR   C 1  51  ? -15.268 -45.217  -4.124  1.00 41.60  ? 51  THR   C OG1    1 
ATOM   7136  C  CG2    . THR   C 1  51  ? -16.828 -46.702  -3.172  1.00 44.97  ? 51  THR   C CG2    1 
ATOM   7137  N  N      . PHE   C 1  52  ? -16.151 -44.587  -7.293  1.00 38.88  ? 52  PHE   C N      1 
ATOM   7138  C  CA     . PHE   C 1  52  ? -16.058 -43.510  -8.268  1.00 38.91  ? 52  PHE   C CA     1 
ATOM   7139  C  C      . PHE   C 1  52  ? -16.245 -43.979  -9.706  1.00 39.31  ? 52  PHE   C C      1 
ATOM   7140  O  O      . PHE   C 1  52  ? -16.797 -43.245  -10.516 1.00 42.89  ? 52  PHE   C O      1 
ATOM   7141  C  CB     . PHE   C 1  52  ? -14.705 -42.794  -8.137  1.00 39.33  ? 52  PHE   C CB     1 
ATOM   7142  C  CG     . PHE   C 1  52  ? -14.668 -41.790  -7.024  1.00 37.24  ? 52  PHE   C CG     1 
ATOM   7143  C  CD1    . PHE   C 1  52  ? -14.992 -42.159  -5.722  1.00 40.22  ? 52  PHE   C CD1    1 
ATOM   7144  C  CD2    . PHE   C 1  52  ? -14.320 -40.475  -7.274  1.00 40.93  ? 52  PHE   C CD2    1 
ATOM   7145  C  CE1    . PHE   C 1  52  ? -14.996 -41.226  -4.690  1.00 41.17  ? 52  PHE   C CE1    1 
ATOM   7146  C  CE2    . PHE   C 1  52  ? -14.310 -39.533  -6.247  1.00 39.68  ? 52  PHE   C CE2    1 
ATOM   7147  C  CZ     . PHE   C 1  52  ? -14.663 -39.908  -4.957  1.00 41.39  ? 52  PHE   C CZ     1 
ATOM   7148  N  N      . PHE   C 1  53  ? -15.836 -45.182  -10.049 1.00 40.14  ? 53  PHE   C N      1 
ATOM   7149  C  CA     . PHE   C 1  53  ? -15.997 -45.682  -11.400 1.00 39.30  ? 53  PHE   C CA     1 
ATOM   7150  C  C      . PHE   C 1  53  ? -17.006 -46.825  -11.402 1.00 47.02  ? 53  PHE   C C      1 
ATOM   7151  O  O      . PHE   C 1  53  ? -17.024 -47.652  -10.476 1.00 47.22  ? 53  PHE   C O      1 
ATOM   7152  C  CB     . PHE   C 1  53  ? -14.662 -46.175  -11.927 1.00 40.61  ? 53  PHE   C CB     1 
ATOM   7153  C  CG     . PHE   C 1  53  ? -13.637 -45.100  -12.066 1.00 41.64  ? 53  PHE   C CG     1 
ATOM   7154  C  CD1    . PHE   C 1  53  ? -12.820 -44.783  -10.994 1.00 38.91  ? 53  PHE   C CD1    1 
ATOM   7155  C  CD2    . PHE   C 1  53  ? -13.471 -44.418  -13.271 1.00 41.78  ? 53  PHE   C CD2    1 
ATOM   7156  C  CE1    . PHE   C 1  53  ? -11.855 -43.795  -11.114 1.00 43.51  ? 53  PHE   C CE1    1 
ATOM   7157  C  CE2    . PHE   C 1  53  ? -12.513 -43.431  -13.411 1.00 40.57  ? 53  PHE   C CE2    1 
ATOM   7158  C  CZ     . PHE   C 1  53  ? -11.700 -43.110  -12.332 1.00 44.56  ? 53  PHE   C CZ     1 
ATOM   7159  N  N      . SER   C 1  54  ? -17.845 -46.884  -12.432 1.00 41.63  ? 54  SER   C N      1 
ATOM   7160  C  CA     . SER   C 1  54  ? -18.656 -48.071  -12.642 1.00 41.34  ? 54  SER   C CA     1 
ATOM   7161  C  C      . SER   C 1  54  ? -18.102 -48.824  -13.842 1.00 47.79  ? 54  SER   C C      1 
ATOM   7162  O  O      . SER   C 1  54  ? -17.325 -48.274  -14.623 1.00 50.28  ? 54  SER   C O      1 
ATOM   7163  C  CB     . SER   C 1  54  ? -20.133 -47.716  -12.812 1.00 39.33  ? 54  SER   C CB     1 
ATOM   7164  O  OG     . SER   C 1  54  ? -20.344 -46.930  -13.958 1.00 48.05  ? 54  SER   C OG     1 
ATOM   7165  N  N      . GLU   C 1  55  ? -18.439 -50.112  -13.940 1.00 53.32  ? 55  GLU   C N      1 
ATOM   7166  C  CA     . GLU   C 1  55  ? -17.869 -51.000  -14.948 1.00 49.45  ? 55  GLU   C CA     1 
ATOM   7167  C  C      . GLU   C 1  55  ? -18.960 -51.428  -15.925 1.00 50.61  ? 55  GLU   C C      1 
ATOM   7168  O  O      . GLU   C 1  55  ? -20.065 -51.785  -15.503 1.00 53.24  ? 55  GLU   C O      1 
ATOM   7169  C  CB     . GLU   C 1  55  ? -17.220 -52.239  -14.307 1.00 49.34  ? 55  GLU   C CB     1 
ATOM   7170  C  CG     . GLU   C 1  55  ? -16.353 -52.023  -13.034 1.00 51.30  ? 55  GLU   C CG     1 
ATOM   7171  C  CD     . GLU   C 1  55  ? -15.629 -53.319  -12.591 1.00 60.43  ? 55  GLU   C CD     1 
ATOM   7172  O  OE1    . GLU   C 1  55  ? -15.409 -54.206  -13.448 1.00 57.93  ? 55  GLU   C OE1    1 
ATOM   7173  O  OE2    . GLU   C 1  55  ? -15.263 -53.474  -11.397 1.00 59.90  ? 55  GLU   C OE2    1 
ATOM   7174  N  N      . THR   C 1  56  ? -18.653 -51.385  -17.226 1.00 52.59  ? 56  THR   C N      1 
ATOM   7175  C  CA     . THR   C 1  56  ? -19.521 -51.947  -18.257 1.00 52.33  ? 56  THR   C CA     1 
ATOM   7176  C  C      . THR   C 1  56  ? -19.140 -53.394  -18.538 1.00 61.32  ? 56  THR   C C      1 
ATOM   7177  O  O      . THR   C 1  56  ? -18.007 -53.826  -18.296 1.00 61.61  ? 56  THR   C O      1 
ATOM   7178  C  CB     . THR   C 1  56  ? -19.455 -51.174  -19.582 1.00 54.05  ? 56  THR   C CB     1 
ATOM   7179  O  OG1    . THR   C 1  56  ? -18.168 -51.336  -20.193 1.00 53.19  ? 56  THR   C OG1    1 
ATOM   7180  C  CG2    . THR   C 1  56  ? -19.717 -49.711  -19.368 1.00 55.20  ? 56  THR   C CG2    1 
ATOM   7181  N  N      . GLY   C 1  57  ? -20.106 -54.146  -19.071 1.00 61.33  ? 57  GLY   C N      1 
ATOM   7182  C  CA     . GLY   C 1  57  ? -19.797 -55.485  -19.538 1.00 59.53  ? 57  GLY   C CA     1 
ATOM   7183  C  C      . GLY   C 1  57  ? -18.566 -55.514  -20.423 1.00 60.51  ? 57  GLY   C C      1 
ATOM   7184  O  O      . GLY   C 1  57  ? -17.754 -56.441  -20.345 1.00 62.96  ? 57  GLY   C O      1 
ATOM   7185  N  N      . ALA   C 1  58  ? -18.397 -54.485  -21.266 1.00 52.39  ? 58  ALA   C N      1 
ATOM   7186  C  CA     . ALA   C 1  58  ? -17.258 -54.423  -22.177 1.00 53.91  ? 58  ALA   C CA     1 
ATOM   7187  C  C      . ALA   C 1  58  ? -15.945 -54.167  -21.465 1.00 64.36  ? 58  ALA   C C      1 
ATOM   7188  O  O      . ALA   C 1  58  ? -14.908 -54.048  -22.141 1.00 65.35  ? 58  ALA   C O      1 
ATOM   7189  C  CB     . ALA   C 1  58  ? -17.484 -53.346  -23.240 1.00 54.74  ? 58  ALA   C CB     1 
ATOM   7190  N  N      . GLY   C 1  59  ? -15.968 -54.070  -20.134 1.00 63.20  ? 59  GLY   C N      1 
ATOM   7191  C  CA     . GLY   C 1  59  ? -14.767 -53.839  -19.357 1.00 60.18  ? 59  GLY   C CA     1 
ATOM   7192  C  C      . GLY   C 1  59  ? -14.343 -52.396  -19.224 1.00 56.54  ? 59  GLY   C C      1 
ATOM   7193  O  O      . GLY   C 1  59  ? -13.201 -52.140  -18.827 1.00 57.25  ? 59  GLY   C O      1 
ATOM   7194  N  N      . LYS   C 1  60  ? -15.221 -51.445  -19.535 1.00 55.31  ? 60  LYS   C N      1 
ATOM   7195  C  CA     . LYS   C 1  60  ? -14.907 -50.024  -19.431 1.00 57.63  ? 60  LYS   C CA     1 
ATOM   7196  C  C      . LYS   C 1  60  ? -15.331 -49.470  -18.072 1.00 56.32  ? 60  LYS   C C      1 
ATOM   7197  O  O      . LYS   C 1  60  ? -16.466 -49.677  -17.629 1.00 54.70  ? 60  LYS   C O      1 
ATOM   7198  C  CB     . LYS   C 1  60  ? -15.585 -49.245  -20.562 1.00 53.19  ? 60  LYS   C CB     1 
ATOM   7199  C  CG     . LYS   C 1  60  ? -15.572 -47.755  -20.359 1.00 54.02  ? 60  LYS   C CG     1 
ATOM   7200  C  CD     . LYS   C 1  60  ? -16.429 -47.051  -21.368 1.00 58.13  ? 60  LYS   C CD     1 
ATOM   7201  C  CE     . LYS   C 1  60  ? -15.782 -47.113  -22.741 1.00 64.97  ? 60  LYS   C CE     1 
ATOM   7202  N  NZ     . LYS   C 1  60  ? -16.563 -46.318  -23.721 1.00 68.27  ? 60  LYS   C NZ     1 
ATOM   7203  N  N      . HIS   C 1  61  ? -14.414 -48.772  -17.410 1.00 56.29  ? 61  HIS   C N      1 
ATOM   7204  C  CA     . HIS   C 1  61  ? -14.698 -48.130  -16.134 1.00 50.74  ? 61  HIS   C CA     1 
ATOM   7205  C  C      . HIS   C 1  61  ? -15.106 -46.694  -16.422 1.00 48.07  ? 61  HIS   C C      1 
ATOM   7206  O  O      . HIS   C 1  61  ? -14.393 -45.969  -17.126 1.00 50.37  ? 61  HIS   C O      1 
ATOM   7207  C  CB     . HIS   C 1  61  ? -13.473 -48.175  -15.236 1.00 49.52  ? 61  HIS   C CB     1 
ATOM   7208  C  CG     . HIS   C 1  61  ? -13.001 -49.563  -14.942 1.00 53.67  ? 61  HIS   C CG     1 
ATOM   7209  N  ND1    . HIS   C 1  61  ? -12.658 -50.452  -15.935 1.00 53.33  ? 61  HIS   C ND1    1 
ATOM   7210  C  CD2    . HIS   C 1  61  ? -12.800 -50.210  -13.771 1.00 54.05  ? 61  HIS   C CD2    1 
ATOM   7211  C  CE1    . HIS   C 1  61  ? -12.278 -51.591  -15.389 1.00 57.62  ? 61  HIS   C CE1    1 
ATOM   7212  N  NE2    . HIS   C 1  61  ? -12.350 -51.469  -14.076 1.00 50.77  ? 61  HIS   C NE2    1 
ATOM   7213  N  N      . VAL   C 1  62  ? -16.256 -46.287  -15.907 1.00 46.16  ? 62  VAL   C N      1 
ATOM   7214  C  CA     . VAL   C 1  62  ? -16.877 -45.036  -16.315 1.00 41.58  ? 62  VAL   C CA     1 
ATOM   7215  C  C      . VAL   C 1  62  ? -17.076 -44.154  -15.088 1.00 40.16  ? 62  VAL   C C      1 
ATOM   7216  O  O      . VAL   C 1  62  ? -17.735 -44.565  -14.131 1.00 38.00  ? 62  VAL   C O      1 
ATOM   7217  C  CB     . VAL   C 1  62  ? -18.210 -45.281  -17.034 1.00 40.11  ? 62  VAL   C CB     1 
ATOM   7218  C  CG1    . VAL   C 1  62  ? -18.713 -43.988  -17.670 1.00 39.93  ? 62  VAL   C CG1    1 
ATOM   7219  C  CG2    . VAL   C 1  62  ? -18.058 -46.415  -18.039 1.00 44.57  ? 62  VAL   C CG2    1 
ATOM   7220  N  N      . PRO   C 1  63  ? -16.510 -42.950  -15.060 1.00 38.45  ? 63  PRO   C N      1 
ATOM   7221  C  CA     . PRO   C 1  63  ? -16.782 -42.024  -13.960 1.00 37.74  ? 63  PRO   C CA     1 
ATOM   7222  C  C      . PRO   C 1  63  ? -18.241 -41.975  -13.542 1.00 40.40  ? 63  PRO   C C      1 
ATOM   7223  O  O      . PRO   C 1  63  ? -19.127 -42.035  -14.400 1.00 44.27  ? 63  PRO   C O      1 
ATOM   7224  C  CB     . PRO   C 1  63  ? -16.326 -40.672  -14.528 1.00 37.20  ? 63  PRO   C CB     1 
ATOM   7225  C  CG     . PRO   C 1  63  ? -15.285 -41.002  -15.532 1.00 36.80  ? 63  PRO   C CG     1 
ATOM   7226  C  CD     . PRO   C 1  63  ? -15.697 -42.330  -16.123 1.00 43.49  ? 63  PRO   C CD     1 
ATOM   7227  N  N      . ARG   C 1  64  ? -18.495 -41.901  -12.233 1.00 31.35  ? 64  ARG   C N      1 
ATOM   7228  C  CA     . ARG   C 1  64  ? -19.812 -41.573  -11.706 1.00 30.63  ? 64  ARG   C CA     1 
ATOM   7229  C  C      . ARG   C 1  64  ? -19.966 -40.059  -11.618 1.00 38.26  ? 64  ARG   C C      1 
ATOM   7230  O  O      . ARG   C 1  64  ? -20.265 -39.483  -10.571 1.00 47.27  ? 64  ARG   C O      1 
ATOM   7231  C  CB     . ARG   C 1  64  ? -20.038 -42.254  -10.359 1.00 35.30  ? 64  ARG   C CB     1 
ATOM   7232  C  CG     . ARG   C 1  64  ? -19.929 -43.766  -10.386 1.00 34.77  ? 64  ARG   C CG     1 
ATOM   7233  C  CD     . ARG   C 1  64  ? -20.264 -44.396  -9.059  1.00 35.23  ? 64  ARG   C CD     1 
ATOM   7234  N  NE     . ARG   C 1  64  ? -19.931 -45.814  -9.076  1.00 39.48  ? 64  ARG   C NE     1 
ATOM   7235  C  CZ     . ARG   C 1  64  ? -20.717 -46.753  -9.588  1.00 42.06  ? 64  ARG   C CZ     1 
ATOM   7236  N  NH1    . ARG   C 1  64  ? -21.963 -46.496  -9.945  1.00 45.84  ? 64  ARG   C NH1    1 
ATOM   7237  N  NH2    . ARG   C 1  64  ? -20.242 -47.982  -9.749  1.00 46.80  ? 64  ARG   C NH2    1 
ATOM   7238  N  N      . ALA   C 1  65  ? -19.767 -39.418  -12.764 1.00 36.45  ? 65  ALA   C N      1 
ATOM   7239  C  CA     . ALA   C 1  65  ? -19.649 -37.975  -12.835 1.00 36.26  ? 65  ALA   C CA     1 
ATOM   7240  C  C      . ALA   C 1  65  ? -20.611 -37.404  -13.863 1.00 37.85  ? 65  ALA   C C      1 
ATOM   7241  O  O      . ALA   C 1  65  ? -21.159 -38.109  -14.711 1.00 37.65  ? 65  ALA   C O      1 
ATOM   7242  C  CB     . ALA   C 1  65  ? -18.221 -37.557  -13.179 1.00 36.42  ? 65  ALA   C CB     1 
ATOM   7243  N  N      . VAL   C 1  66  ? -20.816 -36.101  -13.755 1.00 36.82  ? 66  VAL   C N      1 
ATOM   7244  C  CA     . VAL   C 1  66  ? -21.636 -35.353  -14.690 1.00 37.16  ? 66  VAL   C CA     1 
ATOM   7245  C  C      . VAL   C 1  66  ? -21.008 -33.992  -14.874 1.00 39.49  ? 66  VAL   C C      1 
ATOM   7246  O  O      . VAL   C 1  66  ? -20.533 -33.378  -13.914 1.00 39.49  ? 66  VAL   C O      1 
ATOM   7247  C  CB     . VAL   C 1  66  ? -23.089 -35.223  -14.220 1.00 35.85  ? 66  VAL   C CB     1 
ATOM   7248  C  CG1    . VAL   C 1  66  ? -23.875 -34.471  -15.254 1.00 39.23  ? 66  VAL   C CG1    1 
ATOM   7249  C  CG2    . VAL   C 1  66  ? -23.678 -36.611  -14.066 1.00 36.65  ? 66  VAL   C CG2    1 
ATOM   7250  N  N      . PHE   C 1  67  ? -20.970 -33.537  -16.118 1.00 35.99  ? 67  PHE   C N      1 
ATOM   7251  C  CA     . PHE   C 1  67  ? -20.415 -32.242  -16.449 1.00 34.56  ? 67  PHE   C CA     1 
ATOM   7252  C  C      . PHE   C 1  67  ? -21.541 -31.394  -16.986 1.00 31.50  ? 67  PHE   C C      1 
ATOM   7253  O  O      . PHE   C 1  67  ? -22.189 -31.779  -17.951 1.00 38.97  ? 67  PHE   C O      1 
ATOM   7254  C  CB     . PHE   C 1  67  ? -19.287 -32.378  -17.459 1.00 38.51  ? 67  PHE   C CB     1 
ATOM   7255  C  CG     . PHE   C 1  67  ? -18.038 -32.993  -16.884 1.00 35.32  ? 67  PHE   C CG     1 
ATOM   7256  C  CD1    . PHE   C 1  67  ? -18.050 -34.262  -16.368 1.00 32.96  ? 67  PHE   C CD1    1 
ATOM   7257  C  CD2    . PHE   C 1  67  ? -16.863 -32.282  -16.839 1.00 33.89  ? 67  PHE   C CD2    1 
ATOM   7258  C  CE1    . PHE   C 1  67  ? -16.908 -34.825  -15.828 1.00 37.64  ? 67  PHE   C CE1    1 
ATOM   7259  C  CE2    . PHE   C 1  67  ? -15.720 -32.847  -16.311 1.00 39.05  ? 67  PHE   C CE2    1 
ATOM   7260  C  CZ     . PHE   C 1  67  ? -15.744 -34.128  -15.798 1.00 35.43  ? 67  PHE   C CZ     1 
ATOM   7261  N  N      . VAL   C 1  68  ? -21.794 -30.268  -16.340 1.00 29.44  ? 68  VAL   C N      1 
ATOM   7262  C  CA     . VAL   C 1  68  ? -22.838 -29.357  -16.750 1.00 30.15  ? 68  VAL   C CA     1 
ATOM   7263  C  C      . VAL   C 1  68  ? -22.185 -28.005  -16.951 1.00 35.58  ? 68  VAL   C C      1 
ATOM   7264  O  O      . VAL   C 1  68  ? -21.477 -27.524  -16.060 1.00 33.63  ? 68  VAL   C O      1 
ATOM   7265  C  CB     . VAL   C 1  68  ? -23.947 -29.267  -15.706 1.00 31.53  ? 68  VAL   C CB     1 
ATOM   7266  C  CG1    . VAL   C 1  68  ? -25.201 -28.692  -16.320 1.00 34.43  ? 68  VAL   C CG1    1 
ATOM   7267  C  CG2    . VAL   C 1  68  ? -24.197 -30.633  -15.132 1.00 38.91  ? 68  VAL   C CG2    1 
ATOM   7268  N  N      . ASP   C 1  69  ? -22.355 -27.429  -18.142 1.00 34.26  ? 69  ASP   C N      1 
ATOM   7269  C  CA     . ASP   C 1  69  ? -22.034 -26.030  -18.376 1.00 35.85  ? 69  ASP   C CA     1 
ATOM   7270  C  C      . ASP   C 1  69  ? -23.143 -25.425  -19.225 1.00 38.99  ? 69  ASP   C C      1 
ATOM   7271  O  O      . ASP   C 1  69  ? -23.758 -26.110  -20.038 1.00 41.98  ? 69  ASP   C O      1 
ATOM   7272  C  CB     . ASP   C 1  69  ? -20.664 -25.850  -19.043 1.00 36.23  ? 69  ASP   C CB     1 
ATOM   7273  C  CG     . ASP   C 1  69  ? -20.172 -24.412  -18.976 1.00 38.51  ? 69  ASP   C CG     1 
ATOM   7274  O  OD1    . ASP   C 1  69  ? -20.918 -23.580  -18.383 1.00 32.25  ? 69  ASP   C OD1    1 
ATOM   7275  O  OD2    . ASP   C 1  69  ? -19.050 -24.131  -19.493 1.00 39.76  ? 69  ASP   C OD2    1 
ATOM   7276  N  N      . LEU   C 1  70  ? -23.427 -24.149  -19.012 1.00 34.07  ? 70  LEU   C N      1 
ATOM   7277  C  CA     . LEU   C 1  70  ? -24.470 -23.524  -19.798 1.00 31.20  ? 70  LEU   C CA     1 
ATOM   7278  C  C      . LEU   C 1  70  ? -24.002 -23.127  -21.195 1.00 43.79  ? 70  LEU   C C      1 
ATOM   7279  O  O      . LEU   C 1  70  ? -24.778 -22.512  -21.945 1.00 44.78  ? 70  LEU   C O      1 
ATOM   7280  C  CB     . LEU   C 1  70  ? -25.005 -22.300  -19.077 1.00 30.85  ? 70  LEU   C CB     1 
ATOM   7281  C  CG     . LEU   C 1  70  ? -25.814 -22.602  -17.847 1.00 27.52  ? 70  LEU   C CG     1 
ATOM   7282  C  CD1    . LEU   C 1  70  ? -26.574 -21.339  -17.415 1.00 32.53  ? 70  LEU   C CD1    1 
ATOM   7283  C  CD2    . LEU   C 1  70  ? -26.725 -23.771  -18.130 1.00 32.70  ? 70  LEU   C CD2    1 
ATOM   7284  N  N      . GLU   C 1  71  ? -22.758 -23.431  -21.553 1.00 41.76  ? 71  GLU   C N      1 
ATOM   7285  C  CA     . GLU   C 1  71  ? -22.264 -23.213  -22.903 1.00 41.79  ? 71  GLU   C CA     1 
ATOM   7286  C  C      . GLU   C 1  71  ? -21.299 -24.331  -23.251 1.00 46.35  ? 71  GLU   C C      1 
ATOM   7287  O  O      . GLU   C 1  71  ? -20.806 -25.046  -22.364 1.00 44.43  ? 71  GLU   C O      1 
ATOM   7288  C  CB     . GLU   C 1  71  ? -21.593 -21.839  -23.065 1.00 39.95  ? 71  GLU   C CB     1 
ATOM   7289  C  CG     . GLU   C 1  71  ? -20.407 -21.581  -22.161 1.00 38.23  ? 71  GLU   C CG     1 
ATOM   7290  C  CD     . GLU   C 1  71  ? -19.095 -21.613  -22.917 1.00 47.46  ? 71  GLU   C CD     1 
ATOM   7291  O  OE1    . GLU   C 1  71  ? -19.085 -22.250  -24.004 1.00 46.03  ? 71  GLU   C OE1    1 
ATOM   7292  O  OE2    . GLU   C 1  71  ? -18.077 -21.062  -22.413 1.00 48.54  ? 71  GLU   C OE2    1 
ATOM   7293  N  N      . PRO   C 1  72  ? -20.996 -24.498  -24.513 1.00 48.54  ? 72  PRO   C N      1 
ATOM   7294  C  CA     . PRO   C 1  72  ? -20.386 -25.749  -24.970 1.00 43.04  ? 72  PRO   C CA     1 
ATOM   7295  C  C      . PRO   C 1  72  ? -18.887 -25.683  -25.194 1.00 46.81  ? 72  PRO   C C      1 
ATOM   7296  O  O      . PRO   C 1  72  ? -18.275 -26.738  -25.388 1.00 49.44  ? 72  PRO   C O      1 
ATOM   7297  C  CB     . PRO   C 1  72  ? -21.116 -26.002  -26.280 1.00 42.40  ? 72  PRO   C CB     1 
ATOM   7298  C  CG     . PRO   C 1  72  ? -21.302 -24.613  -26.815 1.00 41.72  ? 72  PRO   C CG     1 
ATOM   7299  C  CD     . PRO   C 1  72  ? -21.633 -23.756  -25.611 1.00 44.39  ? 72  PRO   C CD     1 
ATOM   7300  N  N      . THR   C 1  73  ? -18.280 -24.489  -25.182 1.00 41.07  ? 73  THR   C N      1 
ATOM   7301  C  CA     . THR   C 1  73  ? -16.829 -24.385  -25.353 1.00 41.86  ? 73  THR   C CA     1 
ATOM   7302  C  C      . THR   C 1  73  ? -16.073 -25.366  -24.451 1.00 46.26  ? 73  THR   C C      1 
ATOM   7303  O  O      . THR   C 1  73  ? -15.256 -26.168  -24.916 1.00 45.63  ? 73  THR   C O      1 
ATOM   7304  C  CB     . THR   C 1  73  ? -16.371 -22.959  -25.061 1.00 43.96  ? 73  THR   C CB     1 
ATOM   7305  O  OG1    . THR   C 1  73  ? -17.221 -22.036  -25.722 1.00 47.22  ? 73  THR   C OG1    1 
ATOM   7306  C  CG2    . THR   C 1  73  ? -14.944 -22.729  -25.514 1.00 58.83  ? 73  THR   C CG2    1 
ATOM   7307  N  N      . VAL   C 1  74  ? -16.337 -25.315  -23.150 1.00 44.71  ? 74  VAL   C N      1 
ATOM   7308  C  CA     . VAL   C 1  74  ? -15.462 -25.993  -22.215 1.00 38.29  ? 74  VAL   C CA     1 
ATOM   7309  C  C      . VAL   C 1  74  ? -15.766 -27.484  -22.176 1.00 46.15  ? 74  VAL   C C      1 
ATOM   7310  O  O      . VAL   C 1  74  ? -14.861 -28.317  -22.031 1.00 46.89  ? 74  VAL   C O      1 
ATOM   7311  C  CB     . VAL   C 1  74  ? -15.591 -25.346  -20.830 1.00 36.48  ? 74  VAL   C CB     1 
ATOM   7312  C  CG1    . VAL   C 1  74  ? -14.432 -25.759  -19.945 1.00 35.39  ? 74  VAL   C CG1    1 
ATOM   7313  C  CG2    . VAL   C 1  74  ? -15.677 -23.827  -20.938 1.00 38.13  ? 74  VAL   C CG2    1 
ATOM   7314  N  N      . ILE   C 1  75  ? -17.040 -27.866  -22.291 1.00 47.63  ? 75  ILE   C N      1 
ATOM   7315  C  CA     . ILE   C 1  75  ? -17.319 -29.302  -22.299 1.00 45.48  ? 75  ILE   C CA     1 
ATOM   7316  C  C      . ILE   C 1  75  ? -17.121 -29.910  -23.681 1.00 50.16  ? 75  ILE   C C      1 
ATOM   7317  O  O      . ILE   C 1  75  ? -16.937 -31.129  -23.797 1.00 50.49  ? 75  ILE   C O      1 
ATOM   7318  C  CB     . ILE   C 1  75  ? -18.720 -29.543  -21.707 1.00 40.43  ? 75  ILE   C CB     1 
ATOM   7319  C  CG1    . ILE   C 1  75  ? -18.659 -29.394  -20.176 1.00 36.21  ? 75  ILE   C CG1    1 
ATOM   7320  C  CG2    . ILE   C 1  75  ? -19.212 -30.930  -22.056 1.00 38.13  ? 75  ILE   C CG2    1 
ATOM   7321  C  CD1    . ILE   C 1  75  ? -20.005 -29.315  -19.499 1.00 36.22  ? 75  ILE   C CD1    1 
ATOM   7322  N  N      . ASP   C 1  76  ? -17.089 -29.092  -24.735 1.00 48.79  ? 76  ASP   C N      1 
ATOM   7323  C  CA     . ASP   C 1  76  ? -16.655 -29.598  -26.030 1.00 45.14  ? 76  ASP   C CA     1 
ATOM   7324  C  C      . ASP   C 1  76  ? -15.205 -30.076  -26.011 1.00 45.93  ? 76  ASP   C C      1 
ATOM   7325  O  O      . ASP   C 1  76  ? -14.867 -31.002  -26.742 1.00 46.88  ? 76  ASP   C O      1 
ATOM   7326  C  CB     . ASP   C 1  76  ? -16.835 -28.531  -27.101 1.00 43.36  ? 76  ASP   C CB     1 
ATOM   7327  C  CG     . ASP   C 1  76  ? -18.248 -28.490  -27.633 1.00 52.45  ? 76  ASP   C CG     1 
ATOM   7328  O  OD1    . ASP   C 1  76  ? -18.982 -29.486  -27.388 1.00 55.97  ? 76  ASP   C OD1    1 
ATOM   7329  O  OD2    . ASP   C 1  76  ? -18.624 -27.470  -28.282 1.00 50.48  ? 76  ASP   C OD2    1 
ATOM   7330  N  N      . GLU   C 1  77  ? -14.319 -29.464  -25.218 1.00 47.73  ? 77  GLU   C N      1 
ATOM   7331  C  CA     . GLU   C 1  77  ? -12.934 -29.931  -25.261 1.00 47.54  ? 77  GLU   C CA     1 
ATOM   7332  C  C      . GLU   C 1  77  ? -12.804 -31.304  -24.616 1.00 48.73  ? 77  GLU   C C      1 
ATOM   7333  O  O      . GLU   C 1  77  ? -11.949 -32.099  -25.019 1.00 47.26  ? 77  GLU   C O      1 
ATOM   7334  C  CB     . GLU   C 1  77  ? -11.973 -28.932  -24.602 1.00 54.14  ? 77  GLU   C CB     1 
ATOM   7335  C  CG     . GLU   C 1  77  ? -11.939 -27.508  -25.197 1.00 56.93  ? 77  GLU   C CG     1 
ATOM   7336  C  CD     . GLU   C 1  77  ? -10.770 -26.643  -24.660 1.00 84.43  ? 77  GLU   C CD     1 
ATOM   7337  O  OE1    . GLU   C 1  77  ? -10.072 -27.057  -23.700 1.00 96.20  ? 77  GLU   C OE1    1 
ATOM   7338  O  OE2    . GLU   C 1  77  ? -10.579 -25.513  -25.163 1.00 90.16  ? 77  GLU   C OE2    1 
ATOM   7339  N  N      . VAL   C 1  78  ? -13.655 -31.605  -23.631 1.00 52.29  ? 78  VAL   C N      1 
ATOM   7340  C  CA     . VAL   C 1  78  ? -13.758 -32.968  -23.107 1.00 49.06  ? 78  VAL   C CA     1 
ATOM   7341  C  C      . VAL   C 1  78  ? -14.228 -33.927  -24.197 1.00 49.97  ? 78  VAL   C C      1 
ATOM   7342  O  O      . VAL   C 1  78  ? -13.581 -34.947  -24.472 1.00 53.48  ? 78  VAL   C O      1 
ATOM   7343  C  CB     . VAL   C 1  78  ? -14.704 -33.000  -21.892 1.00 42.03  ? 78  VAL   C CB     1 
ATOM   7344  C  CG1    . VAL   C 1  78  ? -14.828 -34.383  -21.350 1.00 36.47  ? 78  VAL   C CG1    1 
ATOM   7345  C  CG2    . VAL   C 1  78  ? -14.204 -32.073  -20.821 1.00 41.95  ? 78  VAL   C CG2    1 
ATOM   7346  N  N      . ARG   C 1  79  ? -15.365 -33.612  -24.832 1.00 46.55  ? 79  ARG   C N      1 
ATOM   7347  C  CA     . ARG   C 1  79  ? -15.972 -34.515  -25.805 1.00 47.95  ? 79  ARG   C CA     1 
ATOM   7348  C  C      . ARG   C 1  79  ? -14.985 -34.945  -26.884 1.00 54.92  ? 79  ARG   C C      1 
ATOM   7349  O  O      . ARG   C 1  79  ? -15.135 -36.038  -27.451 1.00 60.95  ? 79  ARG   C O      1 
ATOM   7350  C  CB     . ARG   C 1  79  ? -17.200 -33.856  -26.448 1.00 43.54  ? 79  ARG   C CB     1 
ATOM   7351  C  CG     . ARG   C 1  79  ? -18.429 -33.734  -25.514 1.00 45.54  ? 79  ARG   C CG     1 
ATOM   7352  C  CD     . ARG   C 1  79  ? -19.505 -32.808  -26.098 1.00 38.17  ? 79  ARG   C CD     1 
ATOM   7353  N  NE     . ARG   C 1  79  ? -20.684 -32.651  -25.250 1.00 37.61  ? 79  ARG   C NE     1 
ATOM   7354  C  CZ     . ARG   C 1  79  ? -21.341 -31.504  -25.121 1.00 39.64  ? 79  ARG   C CZ     1 
ATOM   7355  N  NH1    . ARG   C 1  79  ? -20.971 -30.421  -25.783 1.00 37.92  ? 79  ARG   C NH1    1 
ATOM   7356  N  NH2    . ARG   C 1  79  ? -22.386 -31.437  -24.303 1.00 37.87  ? 79  ARG   C NH2    1 
ATOM   7357  N  N      . THR   C 1  80  ? -13.956 -34.133  -27.151 1.00 53.28  ? 80  THR   C N      1 
ATOM   7358  C  CA     . THR   C 1  80  ? -12.986 -34.395  -28.210 1.00 51.50  ? 80  THR   C CA     1 
ATOM   7359  C  C      . THR   C 1  80  ? -11.559 -34.613  -27.725 1.00 52.84  ? 80  THR   C C      1 
ATOM   7360  O  O      . THR   C 1  80  ? -10.680 -34.859  -28.557 1.00 52.23  ? 80  THR   C O      1 
ATOM   7361  C  CB     . THR   C 1  80  ? -12.983 -33.240  -29.214 1.00 37.78  ? 80  THR   C CB     1 
ATOM   7362  O  OG1    . THR   C 1  80  ? -12.543 -32.058  -28.550 1.00 45.49  ? 80  THR   C OG1    1 
ATOM   7363  C  CG2    . THR   C 1  80  ? -14.350 -33.008  -29.756 1.00 38.04  ? 80  THR   C CG2    1 
ATOM   7364  N  N      . GLY   C 1  81  ? -11.297 -34.531  -26.419 1.00 55.13  ? 81  GLY   C N      1 
ATOM   7365  C  CA     . GLY   C 1  81  ? -9.951  -34.617  -25.892 1.00 53.48  ? 81  GLY   C CA     1 
ATOM   7366  C  C      . GLY   C 1  81  ? -9.547  -36.025  -25.491 1.00 55.66  ? 81  GLY   C C      1 
ATOM   7367  O  O      . GLY   C 1  81  ? -10.254 -37.008  -25.714 1.00 55.40  ? 81  GLY   C O      1 
ATOM   7368  N  N      . THR   C 1  82  ? -8.383  -36.101  -24.849 1.00 58.67  ? 82  THR   C N      1 
ATOM   7369  C  CA     . THR   C 1  82  ? -7.736  -37.384  -24.596 1.00 60.15  ? 82  THR   C CA     1 
ATOM   7370  C  C      . THR   C 1  82  ? -8.641  -38.402  -23.916 1.00 64.82  ? 82  THR   C C      1 
ATOM   7371  O  O      . THR   C 1  82  ? -8.459  -39.612  -24.107 1.00 68.28  ? 82  THR   C O      1 
ATOM   7372  C  CB     . THR   C 1  82  ? -6.491  -37.180  -23.738 1.00 65.13  ? 82  THR   C CB     1 
ATOM   7373  O  OG1    . THR   C 1  82  ? -5.676  -36.142  -24.299 1.00 62.83  ? 82  THR   C OG1    1 
ATOM   7374  C  CG2    . THR   C 1  82  ? -5.708  -38.476  -23.629 1.00 68.62  ? 82  THR   C CG2    1 
ATOM   7375  N  N      . TYR   C 1  83  ? -9.588  -37.955  -23.090 1.00 63.50  ? 83  TYR   C N      1 
ATOM   7376  C  CA     . TYR   C 1  83  ? -10.416 -38.879  -22.324 1.00 57.60  ? 83  TYR   C CA     1 
ATOM   7377  C  C      . TYR   C 1  83  ? -11.865 -38.888  -22.792 1.00 60.54  ? 83  TYR   C C      1 
ATOM   7378  O  O      . TYR   C 1  83  ? -12.765 -39.219  -22.018 1.00 57.07  ? 83  TYR   C O      1 
ATOM   7379  C  CB     . TYR   C 1  83  ? -10.335 -38.554  -20.840 1.00 40.94  ? 83  TYR   C CB     1 
ATOM   7380  C  CG     . TYR   C 1  83  ? -9.032  -38.944  -20.201 1.00 49.85  ? 83  TYR   C CG     1 
ATOM   7381  C  CD1    . TYR   C 1  83  ? -8.864  -40.204  -19.645 1.00 50.75  ? 83  TYR   C CD1    1 
ATOM   7382  C  CD2    . TYR   C 1  83  ? -7.962  -38.064  -20.164 1.00 54.15  ? 83  TYR   C CD2    1 
ATOM   7383  C  CE1    . TYR   C 1  83  ? -7.676  -40.574  -19.049 1.00 48.44  ? 83  TYR   C CE1    1 
ATOM   7384  C  CE2    . TYR   C 1  83  ? -6.766  -38.420  -19.569 1.00 55.94  ? 83  TYR   C CE2    1 
ATOM   7385  C  CZ     . TYR   C 1  83  ? -6.624  -39.678  -19.008 1.00 55.25  ? 83  TYR   C CZ     1 
ATOM   7386  O  OH     . TYR   C 1  83  ? -5.423  -40.038  -18.405 1.00 56.59  ? 83  TYR   C OH     1 
ATOM   7387  N  N      . ARG   C 1  84  ? -12.102 -38.544  -24.061 1.00 57.88  ? 84  ARG   C N      1 
ATOM   7388  C  CA     . ARG   C 1  84  ? -13.456 -38.606  -24.599 1.00 56.09  ? 84  ARG   C CA     1 
ATOM   7389  C  C      . ARG   C 1  84  ? -14.073 -39.997  -24.444 1.00 58.60  ? 84  ARG   C C      1 
ATOM   7390  O  O      . ARG   C 1  84  ? -15.277 -40.121  -24.187 1.00 58.36  ? 84  ARG   C O      1 
ATOM   7391  C  CB     . ARG   C 1  84  ? -13.449 -38.202  -26.066 1.00 60.06  ? 84  ARG   C CB     1 
ATOM   7392  C  CG     . ARG   C 1  84  ? -12.371 -38.914  -26.853 1.00 63.47  ? 84  ARG   C CG     1 
ATOM   7393  C  CD     . ARG   C 1  84  ? -12.343 -38.454  -28.296 1.00 62.44  ? 84  ARG   C CD     1 
ATOM   7394  N  NE     . ARG   C 1  84  ? -11.371 -39.230  -29.049 1.00 66.54  ? 84  ARG   C NE     1 
ATOM   7395  C  CZ     . ARG   C 1  84  ? -10.083 -38.920  -29.102 1.00 71.18  ? 84  ARG   C CZ     1 
ATOM   7396  N  NH1    . ARG   C 1  84  ? -9.613  -37.835  -28.512 1.00 67.50  ? 84  ARG   C NH1    1 
ATOM   7397  N  NH2    . ARG   C 1  84  ? -9.245  -39.723  -29.751 1.00 85.06  ? 84  ARG   C NH2    1 
ATOM   7398  N  N      . GLN   C 1  85  ? -13.275 -41.055  -24.607 1.00 56.49  ? 85  GLN   C N      1 
ATOM   7399  C  CA     . GLN   C 1  85  ? -13.813 -42.410  -24.488 1.00 57.65  ? 85  GLN   C CA     1 
ATOM   7400  C  C      . GLN   C 1  85  ? -14.298 -42.718  -23.082 1.00 54.23  ? 85  GLN   C C      1 
ATOM   7401  O  O      . GLN   C 1  85  ? -15.037 -43.689  -22.889 1.00 58.57  ? 85  GLN   C O      1 
ATOM   7402  C  CB     . GLN   C 1  85  ? -12.753 -43.448  -24.855 1.00 65.42  ? 85  GLN   C CB     1 
ATOM   7403  C  CG     . GLN   C 1  85  ? -11.992 -43.161  -26.136 1.00 70.44  ? 85  GLN   C CG     1 
ATOM   7404  C  CD     . GLN   C 1  85  ? -11.415 -44.413  -26.763 1.00 73.22  ? 85  GLN   C CD     1 
ATOM   7405  O  OE1    . GLN   C 1  85  ? -12.037 -45.474  -26.741 1.00 83.06  ? 85  GLN   C OE1    1 
ATOM   7406  N  NE2    . GLN   C 1  85  ? -10.199 -44.307  -27.283 1.00 74.21  ? 85  GLN   C NE2    1 
ATOM   7407  N  N      . LEU   C 1  86  ? -13.873 -41.933  -22.092 1.00 50.15  ? 86  LEU   C N      1 
ATOM   7408  C  CA     . LEU   C 1  86  ? -14.134 -42.277  -20.701 1.00 52.46  ? 86  LEU   C CA     1 
ATOM   7409  C  C      . LEU   C 1  86  ? -15.587 -42.079  -20.308 1.00 53.46  ? 86  LEU   C C      1 
ATOM   7410  O  O      . LEU   C 1  86  ? -16.047 -42.708  -19.349 1.00 56.27  ? 86  LEU   C O      1 
ATOM   7411  C  CB     . LEU   C 1  86  ? -13.256 -41.442  -19.780 1.00 50.59  ? 86  LEU   C CB     1 
ATOM   7412  C  CG     . LEU   C 1  86  ? -12.830 -42.055  -18.462 1.00 43.56  ? 86  LEU   C CG     1 
ATOM   7413  C  CD1    . LEU   C 1  86  ? -12.023 -43.296  -18.745 1.00 51.17  ? 86  LEU   C CD1    1 
ATOM   7414  C  CD2    . LEU   C 1  86  ? -12.001 -41.034  -17.730 1.00 42.30  ? 86  LEU   C CD2    1 
ATOM   7415  N  N      . PHE   C 1  87  ? -16.307 -41.217  -21.008 1.00 45.84  ? 87  PHE   C N      1 
ATOM   7416  C  CA     . PHE   C 1  87  ? -17.633 -40.793  -20.603 1.00 48.17  ? 87  PHE   C CA     1 
ATOM   7417  C  C      . PHE   C 1  87  ? -18.655 -41.209  -21.646 1.00 49.64  ? 87  PHE   C C      1 
ATOM   7418  O  O      . PHE   C 1  87  ? -18.401 -41.108  -22.844 1.00 61.75  ? 87  PHE   C O      1 
ATOM   7419  C  CB     . PHE   C 1  87  ? -17.679 -39.267  -20.438 1.00 53.85  ? 87  PHE   C CB     1 
ATOM   7420  C  CG     . PHE   C 1  87  ? -16.602 -38.709  -19.541 1.00 50.90  ? 87  PHE   C CG     1 
ATOM   7421  C  CD1    . PHE   C 1  87  ? -16.751 -38.725  -18.158 1.00 41.80  ? 87  PHE   C CD1    1 
ATOM   7422  C  CD2    . PHE   C 1  87  ? -15.416 -38.207  -20.086 1.00 53.02  ? 87  PHE   C CD2    1 
ATOM   7423  C  CE1    . PHE   C 1  87  ? -15.760 -38.226  -17.328 1.00 42.18  ? 87  PHE   C CE1    1 
ATOM   7424  C  CE2    . PHE   C 1  87  ? -14.412 -37.705  -19.255 1.00 51.95  ? 87  PHE   C CE2    1 
ATOM   7425  C  CZ     . PHE   C 1  87  ? -14.589 -37.720  -17.872 1.00 47.78  ? 87  PHE   C CZ     1 
ATOM   7426  N  N      . HIS   C 1  88  ? -19.806 -41.672  -21.197 1.00 47.47  ? 88  HIS   C N      1 
ATOM   7427  C  CA     . HIS   C 1  88  ? -20.957 -41.727  -22.079 1.00 49.16  ? 88  HIS   C CA     1 
ATOM   7428  C  C      . HIS   C 1  88  ? -21.370 -40.309  -22.446 1.00 45.48  ? 88  HIS   C C      1 
ATOM   7429  O  O      . HIS   C 1  88  ? -21.345 -39.423  -21.597 1.00 42.49  ? 88  HIS   C O      1 
ATOM   7430  C  CB     . HIS   C 1  88  ? -22.130 -42.443  -21.406 1.00 52.78  ? 88  HIS   C CB     1 
ATOM   7431  C  CG     . HIS   C 1  88  ? -23.394 -42.412  -22.208 1.00 58.05  ? 88  HIS   C CG     1 
ATOM   7432  N  ND1    . HIS   C 1  88  ? -23.631 -43.254  -23.273 1.00 66.17  ? 88  HIS   C ND1    1 
ATOM   7433  C  CD2    . HIS   C 1  88  ? -24.468 -41.587  -22.137 1.00 60.53  ? 88  HIS   C CD2    1 
ATOM   7434  C  CE1    . HIS   C 1  88  ? -24.810 -42.970  -23.802 1.00 67.44  ? 88  HIS   C CE1    1 
ATOM   7435  N  NE2    . HIS   C 1  88  ? -25.337 -41.960  -23.133 1.00 64.03  ? 88  HIS   C NE2    1 
ATOM   7436  N  N      . PRO   C 1  89  ? -21.758 -40.072  -23.692 1.00 45.77  ? 89  PRO   C N      1 
ATOM   7437  C  CA     . PRO   C 1  89  ? -22.163 -38.718  -24.089 1.00 48.98  ? 89  PRO   C CA     1 
ATOM   7438  C  C      . PRO   C 1  89  ? -23.105 -38.056  -23.109 1.00 46.78  ? 89  PRO   C C      1 
ATOM   7439  O  O      . PRO   C 1  89  ? -22.868 -36.913  -22.702 1.00 47.46  ? 89  PRO   C O      1 
ATOM   7440  C  CB     . PRO   C 1  89  ? -22.837 -38.955  -25.434 1.00 50.10  ? 89  PRO   C CB     1 
ATOM   7441  C  CG     . PRO   C 1  89  ? -22.155 -40.127  -25.955 1.00 51.62  ? 89  PRO   C CG     1 
ATOM   7442  C  CD     . PRO   C 1  89  ? -21.823 -41.011  -24.808 1.00 42.75  ? 89  PRO   C CD     1 
ATOM   7443  N  N      . GLU   C 1  90  ? -24.164 -38.757  -22.697 1.00 50.67  ? 90  GLU   C N      1 
ATOM   7444  C  CA     . GLU   C 1  90  ? -25.208 -38.148  -21.868 1.00 59.44  ? 90  GLU   C CA     1 
ATOM   7445  C  C      . GLU   C 1  90  ? -24.709 -37.634  -20.524 1.00 47.45  ? 90  GLU   C C      1 
ATOM   7446  O  O      . GLU   C 1  90  ? -25.456 -36.903  -19.865 1.00 41.25  ? 90  GLU   C O      1 
ATOM   7447  C  CB     . GLU   C 1  90  ? -26.359 -39.125  -21.628 1.00 58.39  ? 90  GLU   C CB     1 
ATOM   7448  C  CG     . GLU   C 1  90  ? -26.950 -39.733  -22.877 1.00 56.03  ? 90  GLU   C CG     1 
ATOM   7449  C  CD     . GLU   C 1  90  ? -28.259 -40.415  -22.578 1.00 67.53  ? 90  GLU   C CD     1 
ATOM   7450  O  OE1    . GLU   C 1  90  ? -28.303 -41.175  -21.583 1.00 67.98  ? 90  GLU   C OE1    1 
ATOM   7451  O  OE2    . GLU   C 1  90  ? -29.247 -40.163  -23.311 1.00 73.71  ? 90  GLU   C OE2    1 
ATOM   7452  N  N      . GLN   C 1  91  ? -23.490 -38.010  -20.108 1.00 42.48  ? 91  GLN   C N      1 
ATOM   7453  C  CA     . GLN   C 1  91  ? -22.828 -37.429  -18.944 1.00 37.90  ? 91  GLN   C CA     1 
ATOM   7454  C  C      . GLN   C 1  91  ? -22.380 -35.988  -19.165 1.00 43.58  ? 91  GLN   C C      1 
ATOM   7455  O  O      . GLN   C 1  91  ? -22.192 -35.265  -18.183 1.00 43.45  ? 91  GLN   C O      1 
ATOM   7456  C  CB     . GLN   C 1  91  ? -21.605 -38.267  -18.550 1.00 34.69  ? 91  GLN   C CB     1 
ATOM   7457  C  CG     . GLN   C 1  91  ? -21.881 -39.497  -17.743 1.00 40.47  ? 91  GLN   C CG     1 
ATOM   7458  C  CD     . GLN   C 1  91  ? -20.689 -40.436  -17.650 1.00 43.77  ? 91  GLN   C CD     1 
ATOM   7459  O  OE1    . GLN   C 1  91  ? -20.521 -41.312  -18.487 1.00 44.13  ? 91  GLN   C OE1    1 
ATOM   7460  N  NE2    . GLN   C 1  91  ? -19.840 -40.230  -16.646 1.00 39.25  ? 91  GLN   C NE2    1 
ATOM   7461  N  N      . LEU   C 1  92  ? -22.154 -35.561  -20.411 1.00 42.79  ? 92  LEU   C N      1 
ATOM   7462  C  CA     . LEU   C 1  92  ? -21.648 -34.223  -20.691 1.00 38.06  ? 92  LEU   C CA     1 
ATOM   7463  C  C      . LEU   C 1  92  ? -22.785 -33.387  -21.254 1.00 40.07  ? 92  LEU   C C      1 
ATOM   7464  O  O      . LEU   C 1  92  ? -23.209 -33.602  -22.395 1.00 47.72  ? 92  LEU   C O      1 
ATOM   7465  C  CB     . LEU   C 1  92  ? -20.474 -34.268  -21.656 1.00 37.07  ? 92  LEU   C CB     1 
ATOM   7466  C  CG     . LEU   C 1  92  ? -19.463 -35.379  -21.449 1.00 33.26  ? 92  LEU   C CG     1 
ATOM   7467  C  CD1    . LEU   C 1  92  ? -18.346 -35.137  -22.411 1.00 39.35  ? 92  LEU   C CD1    1 
ATOM   7468  C  CD2    . LEU   C 1  92  ? -18.933 -35.374  -20.059 1.00 39.79  ? 92  LEU   C CD2    1 
ATOM   7469  N  N      . ILE   C 1  93  ? -23.251 -32.420  -20.466 1.00 34.67  ? 93  ILE   C N      1 
ATOM   7470  C  CA     . ILE   C 1  93  ? -24.438 -31.621  -20.758 1.00 37.93  ? 93  ILE   C CA     1 
ATOM   7471  C  C      . ILE   C 1  93  ? -24.013 -30.189  -21.044 1.00 41.90  ? 93  ILE   C C      1 
ATOM   7472  O  O      . ILE   C 1  93  ? -23.199 -29.624  -20.302 1.00 40.77  ? 93  ILE   C O      1 
ATOM   7473  C  CB     . ILE   C 1  93  ? -25.426 -31.666  -19.582 1.00 36.06  ? 93  ILE   C CB     1 
ATOM   7474  C  CG1    . ILE   C 1  93  ? -25.584 -33.119  -19.108 1.00 42.00  ? 93  ILE   C CG1    1 
ATOM   7475  C  CG2    . ILE   C 1  93  ? -26.739 -30.932  -19.915 1.00 31.84  ? 93  ILE   C CG2    1 
ATOM   7476  C  CD1    . ILE   C 1  93  ? -26.526 -33.332  -17.905 1.00 43.34  ? 93  ILE   C CD1    1 
ATOM   7477  N  N      . THR   C 1  94  ? -24.557 -29.593  -22.112 1.00 37.76  ? 94  THR   C N      1 
ATOM   7478  C  CA     . THR   C 1  94  ? -24.284 -28.188  -22.365 1.00 36.12  ? 94  THR   C CA     1 
ATOM   7479  C  C      . THR   C 1  94  ? -25.543 -27.500  -22.863 1.00 37.97  ? 94  THR   C C      1 
ATOM   7480  O  O      . THR   C 1  94  ? -26.377 -28.115  -23.514 1.00 47.83  ? 94  THR   C O      1 
ATOM   7481  C  CB     . THR   C 1  94  ? -23.138 -27.984  -23.376 1.00 39.05  ? 94  THR   C CB     1 
ATOM   7482  O  OG1    . THR   C 1  94  ? -23.482 -28.583  -24.614 1.00 43.52  ? 94  THR   C OG1    1 
ATOM   7483  C  CG2    . THR   C 1  94  ? -21.883 -28.658  -22.902 1.00 40.47  ? 94  THR   C CG2    1 
ATOM   7484  N  N      . GLY   C 1  95  ? -25.686 -26.220  -22.526 1.00 44.40  ? 95  GLY   C N      1 
ATOM   7485  C  CA     . GLY   C 1  95  ? -26.590 -25.318  -23.212 1.00 35.83  ? 95  GLY   C CA     1 
ATOM   7486  C  C      . GLY   C 1  95  ? -25.855 -24.575  -24.309 1.00 42.44  ? 95  GLY   C C      1 
ATOM   7487  O  O      . GLY   C 1  95  ? -24.815 -25.013  -24.807 1.00 40.89  ? 95  GLY   C O      1 
ATOM   7488  N  N      . LYS   C 1  96  ? -26.404 -23.426  -24.692 1.00 50.29  ? 96  LYS   C N      1 
ATOM   7489  C  CA     . LYS   C 1  96  ? -25.847 -22.658  -25.802 1.00 44.23  ? 96  LYS   C CA     1 
ATOM   7490  C  C      . LYS   C 1  96  ? -25.417 -21.263  -25.422 1.00 48.50  ? 96  LYS   C C      1 
ATOM   7491  O  O      . LYS   C 1  96  ? -24.498 -20.732  -26.034 1.00 55.98  ? 96  LYS   C O      1 
ATOM   7492  C  CB     . LYS   C 1  96  ? -26.850 -22.531  -26.955 1.00 49.38  ? 96  LYS   C CB     1 
ATOM   7493  C  CG     . LYS   C 1  96  ? -27.093 -23.816  -27.743 1.00 59.93  ? 96  LYS   C CG     1 
ATOM   7494  C  CD     . LYS   C 1  96  ? -27.930 -23.548  -28.977 1.00 70.34  ? 96  LYS   C CD     1 
ATOM   7495  C  CE     . LYS   C 1  96  ? -28.282 -24.842  -29.657 1.00 77.32  ? 96  LYS   C CE     1 
ATOM   7496  N  NZ     . LYS   C 1  96  ? -27.041 -25.518  -30.107 1.00 79.39  ? 96  LYS   C NZ     1 
ATOM   7497  N  N      . GLU   C 1  97  ? -26.078 -20.648  -24.461 1.00 48.90  ? 97  GLU   C N      1 
ATOM   7498  C  CA     . GLU   C 1  97  ? -25.774 -19.307  -23.991 1.00 44.11  ? 97  GLU   C CA     1 
ATOM   7499  C  C      . GLU   C 1  97  ? -25.302 -19.485  -22.556 1.00 47.34  ? 97  GLU   C C      1 
ATOM   7500  O  O      . GLU   C 1  97  ? -25.990 -20.134  -21.764 1.00 50.15  ? 97  GLU   C O      1 
ATOM   7501  C  CB     . GLU   C 1  97  ? -27.031 -18.432  -24.099 1.00 40.96  ? 97  GLU   C CB     1 
ATOM   7502  C  CG     . GLU   C 1  97  ? -26.835 -16.936  -24.217 1.00 51.85  ? 97  GLU   C CG     1 
ATOM   7503  C  CD     . GLU   C 1  97  ? -28.139 -16.196  -24.558 1.00 63.48  ? 97  GLU   C CD     1 
ATOM   7504  O  OE1    . GLU   C 1  97  ? -29.218 -16.825  -24.466 1.00 63.42  ? 97  GLU   C OE1    1 
ATOM   7505  O  OE2    . GLU   C 1  97  ? -28.088 -14.991  -24.928 1.00 64.19  ? 97  GLU   C OE2    1 
ATOM   7506  N  N      . ASP   C 1  98  ? -24.118 -18.988  -22.219 1.00 42.43  ? 98  ASP   C N      1 
ATOM   7507  C  CA     . ASP   C 1  98  ? -23.706 -19.175  -20.835 1.00 34.36  ? 98  ASP   C CA     1 
ATOM   7508  C  C      . ASP   C 1  98  ? -24.454 -18.174  -19.946 1.00 37.52  ? 98  ASP   C C      1 
ATOM   7509  O  O      . ASP   C 1  98  ? -25.434 -17.541  -20.356 1.00 39.34  ? 98  ASP   C O      1 
ATOM   7510  C  CB     . ASP   C 1  98  ? -22.192 -19.116  -20.688 1.00 31.18  ? 98  ASP   C CB     1 
ATOM   7511  C  CG     . ASP   C 1  98  ? -21.598 -17.762  -21.039 1.00 39.80  ? 98  ASP   C CG     1 
ATOM   7512  O  OD1    . ASP   C 1  98  ? -22.228 -16.703  -20.784 1.00 38.62  ? 98  ASP   C OD1    1 
ATOM   7513  O  OD2    . ASP   C 1  98  ? -20.410 -17.763  -21.439 1.00 45.00  ? 98  ASP   C OD2    1 
ATOM   7514  N  N      . ALA   C 1  99  ? -24.027 -18.051  -18.696 1.00 33.97  ? 99  ALA   C N      1 
ATOM   7515  C  CA     . ALA   C 1  99  ? -24.720 -17.206  -17.745 1.00 34.76  ? 99  ALA   C CA     1 
ATOM   7516  C  C      . ALA   C 1  99  ? -24.188 -15.777  -17.738 1.00 35.93  ? 99  ALA   C C      1 
ATOM   7517  O  O      . ALA   C 1  99  ? -24.559 -14.986  -16.859 1.00 31.65  ? 99  ALA   C O      1 
ATOM   7518  C  CB     . ALA   C 1  99  ? -24.632 -17.835  -16.356 1.00 31.74  ? 99  ALA   C CB     1 
ATOM   7519  N  N      . ALA   C 1  100 ? -23.322 -15.441  -18.698 1.00 36.35  ? 100 ALA   C N      1 
ATOM   7520  C  CA     . ALA   C 1  100 ? -22.753 -14.096  -18.859 1.00 37.30  ? 100 ALA   C CA     1 
ATOM   7521  C  C      . ALA   C 1  100 ? -22.264 -13.503  -17.534 1.00 37.63  ? 100 ALA   C C      1 
ATOM   7522  O  O      . ALA   C 1  100 ? -22.512 -12.341  -17.218 1.00 37.28  ? 100 ALA   C O      1 
ATOM   7523  C  CB     . ALA   C 1  100 ? -23.767 -13.166  -19.528 1.00 38.12  ? 100 ALA   C CB     1 
ATOM   7524  N  N      . ASN   C 1  101 ? -21.537 -14.316  -16.767 1.00 37.78  ? 101 ASN   C N      1 
ATOM   7525  C  CA     . ASN   C 1  101 ? -21.024 -13.961  -15.443 1.00 29.44  ? 101 ASN   C CA     1 
ATOM   7526  C  C      . ASN   C 1  101 ? -22.114 -13.517  -14.489 1.00 32.85  ? 101 ASN   C C      1 
ATOM   7527  O  O      . ASN   C 1  101 ? -21.835 -12.803  -13.530 1.00 32.48  ? 101 ASN   C O      1 
ATOM   7528  C  CB     . ASN   C 1  101 ? -19.962 -12.859  -15.494 1.00 31.76  ? 101 ASN   C CB     1 
ATOM   7529  C  CG     . ASN   C 1  101 ? -18.785 -13.188  -16.375 1.00 36.96  ? 101 ASN   C CG     1 
ATOM   7530  O  OD1    . ASN   C 1  101 ? -18.267 -12.326  -17.062 1.00 39.73  ? 101 ASN   C OD1    1 
ATOM   7531  N  ND2    . ASN   C 1  101 ? -18.414 -14.450  -16.424 1.00 44.18  ? 101 ASN   C ND2    1 
ATOM   7532  N  N      . ASN   C 1  102 ? -23.370 -13.896  -14.712 1.00 36.06  ? 102 ASN   C N      1 
ATOM   7533  C  CA     . ASN   C 1  102 ? -24.484 -13.409  -13.899 1.00 32.98  ? 102 ASN   C CA     1 
ATOM   7534  C  C      . ASN   C 1  102 ? -25.127 -14.535  -13.091 1.00 37.96  ? 102 ASN   C C      1 
ATOM   7535  O  O      . ASN   C 1  102 ? -25.630 -15.515  -13.660 1.00 35.88  ? 102 ASN   C O      1 
ATOM   7536  C  CB     . ASN   C 1  102 ? -25.526 -12.717  -14.769 1.00 33.93  ? 102 ASN   C CB     1 
ATOM   7537  C  CG     . ASN   C 1  102 ? -26.630 -12.085  -13.946 1.00 38.60  ? 102 ASN   C CG     1 
ATOM   7538  O  OD1    . ASN   C 1  102 ? -26.870 -12.488  -12.808 1.00 39.25  ? 102 ASN   C OD1    1 
ATOM   7539  N  ND2    . ASN   C 1  102 ? -27.304 -11.090  -14.513 1.00 39.80  ? 102 ASN   C ND2    1 
ATOM   7540  N  N      . TYR   C 1  103 ? -25.137 -14.370  -11.761 1.00 36.58  ? 103 TYR   C N      1 
ATOM   7541  C  CA     . TYR   C 1  103 ? -25.775 -15.362  -10.906 1.00 32.41  ? 103 TYR   C CA     1 
ATOM   7542  C  C      . TYR   C 1  103 ? -27.240 -15.511  -11.260 1.00 36.28  ? 103 TYR   C C      1 
ATOM   7543  O  O      . TYR   C 1  103 ? -27.760 -16.633  -11.296 1.00 41.03  ? 103 TYR   C O      1 
ATOM   7544  C  CB     . TYR   C 1  103 ? -25.611 -14.993  -9.434  1.00 33.36  ? 103 TYR   C CB     1 
ATOM   7545  C  CG     . TYR   C 1  103 ? -26.440 -15.835  -8.469  1.00 36.68  ? 103 TYR   C CG     1 
ATOM   7546  C  CD1    . TYR   C 1  103 ? -27.736 -15.470  -8.118  1.00 31.59  ? 103 TYR   C CD1    1 
ATOM   7547  C  CD2    . TYR   C 1  103 ? -25.924 -17.016  -7.931  1.00 37.54  ? 103 TYR   C CD2    1 
ATOM   7548  C  CE1    . TYR   C 1  103 ? -28.464 -16.239  -7.260  1.00 35.80  ? 103 TYR   C CE1    1 
ATOM   7549  C  CE2    . TYR   C 1  103 ? -26.662 -17.795  -7.061  1.00 33.39  ? 103 TYR   C CE2    1 
ATOM   7550  C  CZ     . TYR   C 1  103 ? -27.927 -17.406  -6.736  1.00 34.59  ? 103 TYR   C CZ     1 
ATOM   7551  O  OH     . TYR   C 1  103 ? -28.682 -18.173  -5.890  1.00 32.18  ? 103 TYR   C OH     1 
ATOM   7552  N  N      . ALA   C 1  104 ? -27.916 -14.396  -11.560 1.00 33.28  ? 104 ALA   C N      1 
ATOM   7553  C  CA     . ALA   C 1  104 ? -29.346 -14.466  -11.830 1.00 32.87  ? 104 ALA   C CA     1 
ATOM   7554  C  C      . ALA   C 1  104 ? -29.643 -15.314  -13.046 1.00 34.87  ? 104 ALA   C C      1 
ATOM   7555  O  O      . ALA   C 1  104 ? -30.667 -15.995  -13.088 1.00 37.03  ? 104 ALA   C O      1 
ATOM   7556  C  CB     . ALA   C 1  104 ? -29.931 -13.077  -12.011 1.00 35.49  ? 104 ALA   C CB     1 
ATOM   7557  N  N      . ARG   C 1  105 ? -28.769 -15.296  -14.041 1.00 34.17  ? 105 ARG   C N      1 
ATOM   7558  C  CA     . ARG   C 1  105 ? -29.058 -16.051  -15.248 1.00 34.52  ? 105 ARG   C CA     1 
ATOM   7559  C  C      . ARG   C 1  105 ? -28.767 -17.515  -15.042 1.00 35.96  ? 105 ARG   C C      1 
ATOM   7560  O  O      . ARG   C 1  105 ? -29.489 -18.364  -15.558 1.00 38.79  ? 105 ARG   C O      1 
ATOM   7561  C  CB     . ARG   C 1  105 ? -28.237 -15.519  -16.419 1.00 38.86  ? 105 ARG   C CB     1 
ATOM   7562  C  CG     . ARG   C 1  105 ? -28.645 -14.146  -16.888 1.00 40.56  ? 105 ARG   C CG     1 
ATOM   7563  C  CD     . ARG   C 1  105 ? -27.648 -13.632  -17.899 1.00 45.88  ? 105 ARG   C CD     1 
ATOM   7564  N  NE     . ARG   C 1  105 ? -27.700 -14.376  -19.156 1.00 53.94  ? 105 ARG   C NE     1 
ATOM   7565  C  CZ     . ARG   C 1  105 ? -28.482 -14.075  -20.188 1.00 49.10  ? 105 ARG   C CZ     1 
ATOM   7566  N  NH1    . ARG   C 1  105 ? -29.356 -13.083  -20.131 1.00 43.53  ? 105 ARG   C NH1    1 
ATOM   7567  N  NH2    . ARG   C 1  105 ? -28.380 -14.786  -21.304 1.00 48.12  ? 105 ARG   C NH2    1 
ATOM   7568  N  N      . GLY   C 1  106 ? -27.694 -17.824  -14.317 1.00 37.06  ? 106 GLY   C N      1 
ATOM   7569  C  CA     . GLY   C 1  106 ? -27.377 -19.212  -14.061 1.00 34.99  ? 106 GLY   C CA     1 
ATOM   7570  C  C      . GLY   C 1  106 ? -28.425 -19.866  -13.188 1.00 38.02  ? 106 GLY   C C      1 
ATOM   7571  O  O      . GLY   C 1  106 ? -28.806 -21.018  -13.413 1.00 41.09  ? 106 GLY   C O      1 
ATOM   7572  N  N      . HIS   C 1  107 ? -28.934 -19.130  -12.202 1.00 32.88  ? 107 HIS   C N      1 
ATOM   7573  C  CA     . HIS   C 1  107 ? -29.940 -19.697  -11.309 1.00 40.10  ? 107 HIS   C CA     1 
ATOM   7574  C  C      . HIS   C 1  107 ? -31.324 -19.786  -11.962 1.00 44.63  ? 107 HIS   C C      1 
ATOM   7575  O  O      . HIS   C 1  107 ? -31.968 -20.844  -11.935 1.00 46.86  ? 107 HIS   C O      1 
ATOM   7576  C  CB     . HIS   C 1  107 ? -30.009 -18.879  -10.028 1.00 37.64  ? 107 HIS   C CB     1 
ATOM   7577  C  CG     . HIS   C 1  107 ? -30.883 -19.491  -8.987  1.00 40.25  ? 107 HIS   C CG     1 
ATOM   7578  N  ND1    . HIS   C 1  107 ? -32.246 -19.589  -9.137  1.00 43.57  ? 107 HIS   C ND1    1 
ATOM   7579  C  CD2    . HIS   C 1  107 ? -30.595 -20.043  -7.785  1.00 41.08  ? 107 HIS   C CD2    1 
ATOM   7580  C  CE1    . HIS   C 1  107 ? -32.764 -20.170  -8.067  1.00 47.72  ? 107 HIS   C CE1    1 
ATOM   7581  N  NE2    . HIS   C 1  107 ? -31.783 -20.454  -7.232  1.00 45.29  ? 107 HIS   C NE2    1 
ATOM   7582  N  N      . TYR   C 1  108 ? -31.795 -18.685  -12.547 1.00 43.76  ? 108 TYR   C N      1 
ATOM   7583  C  CA     . TYR   C 1  108 ? -33.141 -18.569  -13.094 1.00 40.19  ? 108 TYR   C CA     1 
ATOM   7584  C  C      . TYR   C 1  108 ? -33.145 -18.647  -14.619 1.00 40.31  ? 108 TYR   C C      1 
ATOM   7585  O  O      . TYR   C 1  108 ? -33.341 -19.723  -15.186 1.00 43.61  ? 108 TYR   C O      1 
ATOM   7586  C  CB     . TYR   C 1  108 ? -33.744 -17.247  -12.650 1.00 38.10  ? 108 TYR   C CB     1 
ATOM   7587  C  CG     . TYR   C 1  108 ? -33.822 -17.036  -11.148 1.00 52.84  ? 108 TYR   C CG     1 
ATOM   7588  C  CD1    . TYR   C 1  108 ? -34.917 -17.513  -10.394 1.00 54.88  ? 108 TYR   C CD1    1 
ATOM   7589  C  CD2    . TYR   C 1  108 ? -32.796 -16.375  -10.468 1.00 49.99  ? 108 TYR   C CD2    1 
ATOM   7590  C  CE1    . TYR   C 1  108 ? -34.999 -17.298  -9.019  1.00 43.78  ? 108 TYR   C CE1    1 
ATOM   7591  C  CE2    . TYR   C 1  108 ? -32.862 -16.164  -9.088  1.00 46.38  ? 108 TYR   C CE2    1 
ATOM   7592  C  CZ     . TYR   C 1  108 ? -33.964 -16.628  -8.376  1.00 48.84  ? 108 TYR   C CZ     1 
ATOM   7593  O  OH     . TYR   C 1  108 ? -34.018 -16.414  -7.021  1.00 51.71  ? 108 TYR   C OH     1 
ATOM   7594  N  N      . THR   C 1  109 ? -32.890 -17.511  -15.283 1.00 41.53  ? 109 THR   C N      1 
ATOM   7595  C  CA     . THR   C 1  109 ? -33.080 -17.298  -16.718 1.00 36.00  ? 109 THR   C CA     1 
ATOM   7596  C  C      . THR   C 1  109 ? -32.534 -18.421  -17.578 1.00 37.75  ? 109 THR   C C      1 
ATOM   7597  O  O      . THR   C 1  109 ? -33.306 -19.159  -18.188 1.00 50.50  ? 109 THR   C O      1 
ATOM   7598  C  CB     . THR   C 1  109 ? -32.436 -15.988  -17.155 1.00 39.56  ? 109 THR   C CB     1 
ATOM   7599  O  OG1    . THR   C 1  109 ? -33.072 -14.914  -16.459 1.00 41.87  ? 109 THR   C OG1    1 
ATOM   7600  C  CG2    . THR   C 1  109 ? -32.619 -15.781  -18.648 1.00 34.08  ? 109 THR   C CG2    1 
ATOM   7601  N  N      . ILE   C 1  110 ? -31.221 -18.569  -17.670 1.00 35.88  ? 110 ILE   C N      1 
ATOM   7602  C  CA     . ILE   C 1  110 ? -30.748 -19.657  -18.517 1.00 37.88  ? 110 ILE   C CA     1 
ATOM   7603  C  C      . ILE   C 1  110 ? -30.851 -20.995  -17.799 1.00 42.03  ? 110 ILE   C C      1 
ATOM   7604  O  O      . ILE   C 1  110 ? -31.139 -22.016  -18.434 1.00 45.49  ? 110 ILE   C O      1 
ATOM   7605  C  CB     . ILE   C 1  110 ? -29.311 -19.416  -19.010 1.00 36.98  ? 110 ILE   C CB     1 
ATOM   7606  C  CG1    . ILE   C 1  110 ? -29.187 -18.042  -19.685 1.00 37.61  ? 110 ILE   C CG1    1 
ATOM   7607  C  CG2    . ILE   C 1  110 ? -28.827 -20.588  -19.836 1.00 34.12  ? 110 ILE   C CG2    1 
ATOM   7608  C  CD1    . ILE   C 1  110 ? -30.273 -17.722  -20.681 1.00 36.77  ? 110 ILE   C CD1    1 
ATOM   7609  N  N      . GLY   C 1  111 ? -30.633 -21.014  -16.481 1.00 42.11  ? 111 GLY   C N      1 
ATOM   7610  C  CA     . GLY   C 1  111 ? -30.497 -22.276  -15.769 1.00 39.95  ? 111 GLY   C CA     1 
ATOM   7611  C  C      . GLY   C 1  111 ? -31.775 -23.094  -15.738 1.00 41.22  ? 111 GLY   C C      1 
ATOM   7612  O  O      . GLY   C 1  111 ? -31.755 -24.313  -15.947 1.00 37.54  ? 111 GLY   C O      1 
ATOM   7613  N  N      . LYS   C 1  112 ? -32.902 -22.439  -15.469 1.00 45.41  ? 112 LYS   C N      1 
ATOM   7614  C  CA     . LYS   C 1  112 ? -34.189 -23.120  -15.435 1.00 45.60  ? 112 LYS   C CA     1 
ATOM   7615  C  C      . LYS   C 1  112 ? -34.445 -23.923  -16.703 1.00 42.92  ? 112 LYS   C C      1 
ATOM   7616  O  O      . LYS   C 1  112 ? -35.215 -24.888  -16.679 1.00 36.92  ? 112 LYS   C O      1 
ATOM   7617  C  CB     . LYS   C 1  112 ? -35.289 -22.080  -15.221 1.00 47.54  ? 112 LYS   C CB     1 
ATOM   7618  C  CG     . LYS   C 1  112 ? -35.543 -21.169  -16.422 1.00 42.66  ? 112 LYS   C CG     1 
ATOM   7619  C  CD     . LYS   C 1  112 ? -36.584 -20.102  -16.061 1.00 46.97  ? 112 LYS   C CD     1 
ATOM   7620  C  CE     . LYS   C 1  112 ? -36.741 -19.043  -17.167 1.00 55.69  ? 112 LYS   C CE     1 
ATOM   7621  N  NZ     . LYS   C 1  112 ? -37.101 -19.661  -18.492 1.00 51.47  ? 112 LYS   C NZ     1 
ATOM   7622  N  N      . GLU   C 1  113 ? -33.793 -23.576  -17.799 1.00 40.70  ? 113 GLU   C N      1 
ATOM   7623  C  CA     . GLU   C 1  113 ? -34.047 -24.304  -19.023 1.00 40.48  ? 113 GLU   C CA     1 
ATOM   7624  C  C      . GLU   C 1  113 ? -33.325 -25.635  -19.101 1.00 41.90  ? 113 GLU   C C      1 
ATOM   7625  O  O      . GLU   C 1  113 ? -33.617 -26.412  -20.013 1.00 47.52  ? 113 GLU   C O      1 
ATOM   7626  C  CB     . GLU   C 1  113 ? -33.649 -23.455  -20.226 1.00 49.41  ? 113 GLU   C CB     1 
ATOM   7627  C  CG     . GLU   C 1  113 ? -34.390 -22.145  -20.282 1.00 57.12  ? 113 GLU   C CG     1 
ATOM   7628  C  CD     . GLU   C 1  113 ? -35.848 -22.346  -20.639 1.00 63.14  ? 113 GLU   C CD     1 
ATOM   7629  O  OE1    . GLU   C 1  113 ? -36.133 -23.046  -21.644 1.00 62.51  ? 113 GLU   C OE1    1 
ATOM   7630  O  OE2    . GLU   C 1  113 ? -36.706 -21.824  -19.881 1.00 59.83  ? 113 GLU   C OE2    1 
ATOM   7631  N  N      . ILE   C 1  114 ? -32.379 -25.920  -18.206 1.00 41.35  ? 114 ILE   C N      1 
ATOM   7632  C  CA     . ILE   C 1  114 ? -31.590 -27.146  -18.325 1.00 37.74  ? 114 ILE   C CA     1 
ATOM   7633  C  C      . ILE   C 1  114 ? -31.607 -27.962  -17.027 1.00 40.70  ? 114 ILE   C C      1 
ATOM   7634  O  O      . ILE   C 1  114 ? -31.127 -29.102  -16.995 1.00 38.29  ? 114 ILE   C O      1 
ATOM   7635  C  CB     . ILE   C 1  114 ? -30.155 -26.806  -18.745 1.00 31.78  ? 114 ILE   C CB     1 
ATOM   7636  C  CG1    . ILE   C 1  114 ? -29.439 -28.040  -19.290 1.00 37.06  ? 114 ILE   C CG1    1 
ATOM   7637  C  CG2    . ILE   C 1  114 ? -29.406 -26.212  -17.582 1.00 32.78  ? 114 ILE   C CG2    1 
ATOM   7638  C  CD1    . ILE   C 1  114 ? -28.208 -27.764  -20.188 1.00 32.22  ? 114 ILE   C CD1    1 
ATOM   7639  N  N      . ILE   C 1  115 ? -32.194 -27.408  -15.958 1.00 37.61  ? 115 ILE   C N      1 
ATOM   7640  C  CA     . ILE   C 1  115 ? -32.106 -28.038  -14.646 1.00 32.39  ? 115 ILE   C CA     1 
ATOM   7641  C  C      . ILE   C 1  115 ? -32.815 -29.383  -14.650 1.00 37.29  ? 115 ILE   C C      1 
ATOM   7642  O  O      . ILE   C 1  115 ? -32.314 -30.361  -14.086 1.00 39.70  ? 115 ILE   C O      1 
ATOM   7643  C  CB     . ILE   C 1  115 ? -32.685 -27.108  -13.568 1.00 40.63  ? 115 ILE   C CB     1 
ATOM   7644  C  CG1    . ILE   C 1  115 ? -32.592 -27.741  -12.171 1.00 39.58  ? 115 ILE   C CG1    1 
ATOM   7645  C  CG2    . ILE   C 1  115 ? -34.122 -26.785  -13.869 1.00 41.75  ? 115 ILE   C CG2    1 
ATOM   7646  C  CD1    . ILE   C 1  115 ? -31.222 -27.706  -11.576 1.00 32.98  ? 115 ILE   C CD1    1 
ATOM   7647  N  N      . ASP   C 1  116 ? -33.992 -29.468  -15.288 1.00 45.61  ? 116 ASP   C N      1 
ATOM   7648  C  CA     . ASP   C 1  116 ? -34.687 -30.759  -15.330 1.00 38.32  ? 116 ASP   C CA     1 
ATOM   7649  C  C      . ASP   C 1  116 ? -33.843 -31.786  -16.076 1.00 35.51  ? 116 ASP   C C      1 
ATOM   7650  O  O      . ASP   C 1  116 ? -33.724 -32.931  -15.645 1.00 38.16  ? 116 ASP   C O      1 
ATOM   7651  C  CB     . ASP   C 1  116 ? -36.079 -30.641  -15.966 1.00 29.23  ? 116 ASP   C CB     1 
ATOM   7652  C  CG     . ASP   C 1  116 ? -37.108 -29.912  -15.074 1.00 38.96  ? 116 ASP   C CG     1 
ATOM   7653  O  OD1    . ASP   C 1  116 ? -37.023 -29.926  -13.841 1.00 47.36  ? 116 ASP   C OD1    1 
ATOM   7654  O  OD2    . ASP   C 1  116 ? -38.082 -29.367  -15.613 1.00 53.01  ? 116 ASP   C OD2    1 
ATOM   7655  N  N      . LEU   C 1  117 ? -33.204 -31.385  -17.171 1.00 36.53  ? 117 LEU   C N      1 
ATOM   7656  C  CA     . LEU   C 1  117 ? -32.409 -32.356  -17.910 1.00 38.12  ? 117 LEU   C CA     1 
ATOM   7657  C  C      . LEU   C 1  117 ? -31.231 -32.814  -17.061 1.00 42.41  ? 117 LEU   C C      1 
ATOM   7658  O  O      . LEU   C 1  117 ? -30.944 -34.019  -16.970 1.00 40.89  ? 117 LEU   C O      1 
ATOM   7659  C  CB     . LEU   C 1  117 ? -31.916 -31.760  -19.231 1.00 34.94  ? 117 LEU   C CB     1 
ATOM   7660  C  CG     . LEU   C 1  117 ? -30.829 -32.628  -19.873 1.00 39.63  ? 117 LEU   C CG     1 
ATOM   7661  C  CD1    . LEU   C 1  117 ? -31.353 -34.016  -20.226 1.00 41.28  ? 117 LEU   C CD1    1 
ATOM   7662  C  CD2    . LEU   C 1  117 ? -30.202 -31.990  -21.058 1.00 48.01  ? 117 LEU   C CD2    1 
ATOM   7663  N  N      . VAL   C 1  118 ? -30.546 -31.859  -16.412 1.00 41.16  ? 118 VAL   C N      1 
ATOM   7664  C  CA     . VAL   C 1  118 ? -29.401 -32.203  -15.569 1.00 39.78  ? 118 VAL   C CA     1 
ATOM   7665  C  C      . VAL   C 1  118 ? -29.823 -33.162  -14.466 1.00 37.77  ? 118 VAL   C C      1 
ATOM   7666  O  O      . VAL   C 1  118 ? -29.171 -34.186  -14.248 1.00 35.98  ? 118 VAL   C O      1 
ATOM   7667  C  CB     . VAL   C 1  118 ? -28.736 -30.946  -14.983 1.00 37.14  ? 118 VAL   C CB     1 
ATOM   7668  C  CG1    . VAL   C 1  118 ? -27.783 -31.357  -13.871 1.00 31.74  ? 118 VAL   C CG1    1 
ATOM   7669  C  CG2    . VAL   C 1  118 ? -27.998 -30.167  -16.065 1.00 36.03  ? 118 VAL   C CG2    1 
ATOM   7670  N  N      . LEU   C 1  119 ? -30.929 -32.859  -13.761 1.00 34.52  ? 119 LEU   C N      1 
ATOM   7671  C  CA     . LEU   C 1  119 ? -31.368 -33.765  -12.702 1.00 35.20  ? 119 LEU   C CA     1 
ATOM   7672  C  C      . LEU   C 1  119 ? -31.738 -35.140  -13.244 1.00 40.61  ? 119 LEU   C C      1 
ATOM   7673  O  O      . LEU   C 1  119 ? -31.498 -36.148  -12.567 1.00 39.24  ? 119 LEU   C O      1 
ATOM   7674  C  CB     . LEU   C 1  119 ? -32.539 -33.191  -11.927 1.00 26.76  ? 119 LEU   C CB     1 
ATOM   7675  C  CG     . LEU   C 1  119 ? -32.199 -32.049  -10.990 1.00 30.10  ? 119 LEU   C CG     1 
ATOM   7676  C  CD1    . LEU   C 1  119 ? -33.456 -31.346  -10.558 1.00 41.82  ? 119 LEU   C CD1    1 
ATOM   7677  C  CD2    . LEU   C 1  119 ? -31.456 -32.516  -9.813  1.00 29.40  ? 119 LEU   C CD2    1 
ATOM   7678  N  N      . ASP   C 1  120 ? -32.296 -35.214  -14.461 1.00 40.94  ? 120 ASP   C N      1 
ATOM   7679  C  CA     . ASP   C 1  120 ? -32.621 -36.518  -15.039 1.00 42.82  ? 120 ASP   C CA     1 
ATOM   7680  C  C      . ASP   C 1  120 ? -31.367 -37.353  -15.273 1.00 44.63  ? 120 ASP   C C      1 
ATOM   7681  O  O      . ASP   C 1  120 ? -31.358 -38.559  -15.016 1.00 44.18  ? 120 ASP   C O      1 
ATOM   7682  C  CB     . ASP   C 1  120 ? -33.378 -36.377  -16.355 1.00 44.08  ? 120 ASP   C CB     1 
ATOM   7683  C  CG     . ASP   C 1  120 ? -34.796 -35.850  -16.169 1.00 59.79  ? 120 ASP   C CG     1 
ATOM   7684  O  OD1    . ASP   C 1  120 ? -35.343 -35.874  -15.033 1.00 62.86  ? 120 ASP   C OD1    1 
ATOM   7685  O  OD2    . ASP   C 1  120 ? -35.392 -35.467  -17.198 1.00 65.28  ? 120 ASP   C OD2    1 
ATOM   7686  N  N      . ARG   C 1  121 ? -30.303 -36.749  -15.781 1.00 43.40  ? 121 ARG   C N      1 
ATOM   7687  C  CA     . ARG   C 1  121 ? -29.083 -37.528  -15.933 1.00 43.08  ? 121 ARG   C CA     1 
ATOM   7688  C  C      . ARG   C 1  121 ? -28.499 -37.917  -14.585 1.00 45.85  ? 121 ARG   C C      1 
ATOM   7689  O  O      . ARG   C 1  121 ? -27.974 -39.025  -14.440 1.00 48.05  ? 121 ARG   C O      1 
ATOM   7690  C  CB     . ARG   C 1  121 ? -28.058 -36.753  -16.735 1.00 51.26  ? 121 ARG   C CB     1 
ATOM   7691  C  CG     . ARG   C 1  121 ? -28.627 -36.237  -17.978 1.00 52.16  ? 121 ARG   C CG     1 
ATOM   7692  C  CD     . ARG   C 1  121 ? -28.346 -37.273  -19.019 1.00 61.55  ? 121 ARG   C CD     1 
ATOM   7693  N  NE     . ARG   C 1  121 ? -29.279 -37.114  -20.116 1.00 62.43  ? 121 ARG   C NE     1 
ATOM   7694  C  CZ     . ARG   C 1  121 ? -28.975 -36.445  -21.209 1.00 58.87  ? 121 ARG   C CZ     1 
ATOM   7695  N  NH1    . ARG   C 1  121 ? -27.772 -35.908  -21.366 1.00 49.94  ? 121 ARG   C NH1    1 
ATOM   7696  N  NH2    . ARG   C 1  121 ? -29.901 -36.300  -22.152 1.00 60.75  ? 121 ARG   C NH2    1 
ATOM   7697  N  N      . ILE   C 1  122 ? -28.541 -37.015  -13.595 1.00 41.27  ? 122 ILE   C N      1 
ATOM   7698  C  CA     . ILE   C 1  122 ? -28.009 -37.368  -12.280 1.00 40.97  ? 122 ILE   C CA     1 
ATOM   7699  C  C      . ILE   C 1  122 ? -28.766 -38.564  -11.731 1.00 41.33  ? 122 ILE   C C      1 
ATOM   7700  O  O      . ILE   C 1  122 ? -28.178 -39.553  -11.283 1.00 39.71  ? 122 ILE   C O      1 
ATOM   7701  C  CB     . ILE   C 1  122 ? -28.084 -36.182  -11.304 1.00 38.65  ? 122 ILE   C CB     1 
ATOM   7702  C  CG1    . ILE   C 1  122 ? -27.141 -35.049  -11.709 1.00 34.38  ? 122 ILE   C CG1    1 
ATOM   7703  C  CG2    . ILE   C 1  122 ? -27.735 -36.668  -9.903  1.00 35.09  ? 122 ILE   C CG2    1 
ATOM   7704  C  CD1    . ILE   C 1  122 ? -27.191 -33.871  -10.763 1.00 30.28  ? 122 ILE   C CD1    1 
ATOM   7705  N  N      . ARG   C 1  123 ? -30.092 -38.491  -11.773 1.00 42.16  ? 123 ARG   C N      1 
ATOM   7706  C  CA     . ARG   C 1  123 ? -30.897 -39.645  -11.414 1.00 41.41  ? 123 ARG   C CA     1 
ATOM   7707  C  C      . ARG   C 1  123 ? -30.454 -40.911  -12.141 1.00 42.45  ? 123 ARG   C C      1 
ATOM   7708  O  O      . ARG   C 1  123 ? -30.447 -41.996  -11.551 1.00 43.23  ? 123 ARG   C O      1 
ATOM   7709  C  CB     . ARG   C 1  123 ? -32.356 -39.353  -11.695 1.00 34.77  ? 123 ARG   C CB     1 
ATOM   7710  C  CG     . ARG   C 1  123 ? -33.226 -40.509  -11.361 1.00 36.76  ? 123 ARG   C CG     1 
ATOM   7711  C  CD     . ARG   C 1  123 ? -33.286 -40.680  -9.874  1.00 48.77  ? 123 ARG   C CD     1 
ATOM   7712  N  NE     . ARG   C 1  123 ? -34.088 -39.657  -9.210  1.00 48.80  ? 123 ARG   C NE     1 
ATOM   7713  C  CZ     . ARG   C 1  123 ? -34.209 -39.590  -7.892  1.00 47.36  ? 123 ARG   C CZ     1 
ATOM   7714  N  NH1    . ARG   C 1  123 ? -33.644 -40.495  -7.109  1.00 38.73  ? 123 ARG   C NH1    1 
ATOM   7715  N  NH2    . ARG   C 1  123 ? -34.912 -38.596  -7.348  1.00 51.31  ? 123 ARG   C NH2    1 
ATOM   7716  N  N      . LYS   C 1  124 ? -30.082 -40.803  -13.419 1.00 39.36  ? 124 LYS   C N      1 
ATOM   7717  C  CA     . LYS   C 1  124 ? -29.690 -42.004  -14.146 1.00 37.75  ? 124 LYS   C CA     1 
ATOM   7718  C  C      . LYS   C 1  124 ? -28.465 -42.625  -13.515 1.00 41.53  ? 124 LYS   C C      1 
ATOM   7719  O  O      . LYS   C 1  124 ? -28.330 -43.851  -13.494 1.00 47.29  ? 124 LYS   C O      1 
ATOM   7720  C  CB     . LYS   C 1  124 ? -29.402 -41.696  -15.614 1.00 46.03  ? 124 LYS   C CB     1 
ATOM   7721  C  CG     . LYS   C 1  124 ? -30.636 -41.620  -16.555 1.00 59.85  ? 124 LYS   C CG     1 
ATOM   7722  C  CD     . LYS   C 1  124 ? -31.603 -42.810  -16.441 1.00 78.50  ? 124 LYS   C CD     1 
ATOM   7723  C  CE     . LYS   C 1  124 ? -32.904 -42.557  -17.231 1.00 89.56  ? 124 LYS   C CE     1 
ATOM   7724  N  NZ     . LYS   C 1  124 ? -33.913 -43.665  -17.114 1.00 100.15 ? 124 LYS   C NZ     1 
ATOM   7725  N  N      . LEU   C 1  125 ? -27.551 -41.789  -13.007 1.00 42.40  ? 125 LEU   C N      1 
ATOM   7726  C  CA     . LEU   C 1  125 ? -26.365 -42.285  -12.314 1.00 40.07  ? 125 LEU   C CA     1 
ATOM   7727  C  C      . LEU   C 1  125 ? -26.726 -42.855  -10.945 1.00 40.71  ? 125 LEU   C C      1 
ATOM   7728  O  O      . LEU   C 1  125 ? -26.245 -43.929  -10.553 1.00 41.58  ? 125 LEU   C O      1 
ATOM   7729  C  CB     . LEU   C 1  125 ? -25.332 -41.157  -12.193 1.00 35.89  ? 125 LEU   C CB     1 
ATOM   7730  C  CG     . LEU   C 1  125 ? -24.615 -40.648  -13.446 1.00 31.96  ? 125 LEU   C CG     1 
ATOM   7731  C  CD1    . LEU   C 1  125 ? -23.472 -39.693  -13.168 1.00 32.70  ? 125 LEU   C CD1    1 
ATOM   7732  C  CD2    . LEU   C 1  125 ? -24.044 -41.822  -14.110 1.00 34.66  ? 125 LEU   C CD2    1 
ATOM   7733  N  N      . ALA   C 1  126 ? -27.582 -42.153  -10.210 1.00 41.99  ? 126 ALA   C N      1 
ATOM   7734  C  CA     . ALA   C 1  126 ? -27.997 -42.640  -8.905  1.00 43.10  ? 126 ALA   C CA     1 
ATOM   7735  C  C      . ALA   C 1  126 ? -28.527 -44.060  -9.011  1.00 44.95  ? 126 ALA   C C      1 
ATOM   7736  O  O      . ALA   C 1  126 ? -28.250 -44.901  -8.150  1.00 45.41  ? 126 ALA   C O      1 
ATOM   7737  C  CB     . ALA   C 1  126 ? -29.048 -41.702  -8.306  1.00 37.42  ? 126 ALA   C CB     1 
ATOM   7738  N  N      . ASP   C 1  127 ? -29.263 -44.355  -10.080 1.00 46.53  ? 127 ASP   C N      1 
ATOM   7739  C  CA     . ASP   C 1  127 ? -29.962 -45.629  -10.170 1.00 48.63  ? 127 ASP   C CA     1 
ATOM   7740  C  C      . ASP   C 1  127 ? -29.020 -46.793  -10.417 1.00 51.11  ? 127 ASP   C C      1 
ATOM   7741  O  O      . ASP   C 1  127 ? -29.387 -47.936  -10.136 1.00 54.61  ? 127 ASP   C O      1 
ATOM   7742  C  CB     . ASP   C 1  127 ? -31.015 -45.579  -11.272 1.00 49.55  ? 127 ASP   C CB     1 
ATOM   7743  C  CG     . ASP   C 1  127 ? -32.265 -44.817  -10.843 1.00 58.70  ? 127 ASP   C CG     1 
ATOM   7744  O  OD1    . ASP   C 1  127 ? -32.378 -44.440  -9.636  1.00 50.19  ? 127 ASP   C OD1    1 
ATOM   7745  O  OD2    . ASP   C 1  127 ? -33.135 -44.603  -11.719 1.00 57.11  ? 127 ASP   C OD2    1 
ATOM   7746  N  N      . GLN   C 1  128 ? -27.821 -46.533  -10.919 1.00 44.87  ? 128 GLN   C N      1 
ATOM   7747  C  CA     . GLN   C 1  128 ? -26.850 -47.598  -11.064 1.00 46.35  ? 128 GLN   C CA     1 
ATOM   7748  C  C      . GLN   C 1  128 ? -26.162 -47.957  -9.754  1.00 50.23  ? 128 GLN   C C      1 
ATOM   7749  O  O      . GLN   C 1  128 ? -25.232 -48.771  -9.773  1.00 55.80  ? 128 GLN   C O      1 
ATOM   7750  C  CB     . GLN   C 1  128 ? -25.786 -47.184  -12.063 1.00 51.23  ? 128 GLN   C CB     1 
ATOM   7751  C  CG     . GLN   C 1  128 ? -26.300 -46.976  -13.464 1.00 61.72  ? 128 GLN   C CG     1 
ATOM   7752  C  CD     . GLN   C 1  128 ? -25.156 -46.788  -14.468 1.00 70.68  ? 128 GLN   C CD     1 
ATOM   7753  O  OE1    . GLN   C 1  128 ? -24.217 -46.021  -14.210 1.00 62.38  ? 128 GLN   C OE1    1 
ATOM   7754  N  NE2    . GLN   C 1  128 ? -25.257 -47.453  -15.641 1.00 64.12  ? 128 GLN   C NE2    1 
ATOM   7755  N  N      . CYS   C 1  129 ? -26.566 -47.352  -8.634  1.00 50.97  ? 129 CYS   C N      1 
ATOM   7756  C  CA     . CYS   C 1  129 ? -25.836 -47.400  -7.368  1.00 45.04  ? 129 CYS   C CA     1 
ATOM   7757  C  C      . CYS   C 1  129 ? -26.549 -48.332  -6.411  1.00 48.20  ? 129 CYS   C C      1 
ATOM   7758  O  O      . CYS   C 1  129 ? -27.758 -48.186  -6.192  1.00 50.04  ? 129 CYS   C O      1 
ATOM   7759  C  CB     . CYS   C 1  129 ? -25.741 -46.012  -6.720  1.00 43.32  ? 129 CYS   C CB     1 
ATOM   7760  S  SG     . CYS   C 1  129 ? -24.761 -44.760  -7.591  1.00 39.38  ? 129 CYS   C SG     1 
ATOM   7761  N  N      . THR   C 1  130 ? -25.803 -49.266  -5.815  1.00 46.81  ? 130 THR   C N      1 
ATOM   7762  C  CA     . THR   C 1  130 ? -26.443 -50.113  -4.816  1.00 48.06  ? 130 THR   C CA     1 
ATOM   7763  C  C      . THR   C 1  130 ? -26.545 -49.403  -3.471  1.00 49.90  ? 130 THR   C C      1 
ATOM   7764  O  O      . THR   C 1  130 ? -27.542 -49.567  -2.763  1.00 52.17  ? 130 THR   C O      1 
ATOM   7765  C  CB     . THR   C 1  130 ? -25.714 -51.446  -4.678  1.00 46.70  ? 130 THR   C CB     1 
ATOM   7766  O  OG1    . THR   C 1  130 ? -24.421 -51.242  -4.109  1.00 58.43  ? 130 THR   C OG1    1 
ATOM   7767  C  CG2    . THR   C 1  130 ? -25.551 -52.084  -6.018  1.00 52.31  ? 130 THR   C CG2    1 
ATOM   7768  N  N      . GLY   C 1  131 ? -25.554 -48.594  -3.107  1.00 48.70  ? 131 GLY   C N      1 
ATOM   7769  C  CA     . GLY   C 1  131 ? -25.662 -47.834  -1.876  1.00 49.48  ? 131 GLY   C CA     1 
ATOM   7770  C  C      . GLY   C 1  131 ? -25.097 -46.436  -1.970  1.00 44.44  ? 131 GLY   C C      1 
ATOM   7771  O  O      . GLY   C 1  131 ? -24.139 -46.116  -1.273  1.00 50.84  ? 131 GLY   C O      1 
ATOM   7772  N  N      . LEU   C 1  132 ? -25.679 -45.595  -2.821  1.00 45.50  ? 132 LEU   C N      1 
ATOM   7773  C  CA     . LEU   C 1  132 ? -25.170 -44.242  -3.012  1.00 39.64  ? 132 LEU   C CA     1 
ATOM   7774  C  C      . LEU   C 1  132 ? -25.057 -43.491  -1.698  1.00 41.58  ? 132 LEU   C C      1 
ATOM   7775  O  O      . LEU   C 1  132 ? -25.956 -43.518  -0.856  1.00 39.64  ? 132 LEU   C O      1 
ATOM   7776  C  CB     . LEU   C 1  132 ? -26.050 -43.447  -3.976  1.00 37.57  ? 132 LEU   C CB     1 
ATOM   7777  C  CG     . LEU   C 1  132 ? -25.795 -41.943  -3.894  1.00 35.61  ? 132 LEU   C CG     1 
ATOM   7778  C  CD1    . LEU   C 1  132 ? -24.468 -41.618  -4.492  1.00 40.38  ? 132 LEU   C CD1    1 
ATOM   7779  C  CD2    . LEU   C 1  132 ? -26.877 -41.168  -4.591  1.00 31.72  ? 132 LEU   C CD2    1 
ATOM   7780  N  N      . GLN   C 1  133 ? -23.938 -42.794  -1.560  1.00 45.41  ? 133 GLN   C N      1 
ATOM   7781  C  CA     . GLN   C 1  133 ? -23.494 -42.115  -0.355  1.00 44.92  ? 133 GLN   C CA     1 
ATOM   7782  C  C      . GLN   C 1  133 ? -23.776 -40.623  -0.402  1.00 40.85  ? 133 GLN   C C      1 
ATOM   7783  O  O      . GLN   C 1  133 ? -24.245 -40.039  0.579   1.00 42.85  ? 133 GLN   C O      1 
ATOM   7784  C  CB     . GLN   C 1  133 ? -21.990 -42.334  -0.187  1.00 47.33  ? 133 GLN   C CB     1 
ATOM   7785  C  CG     . GLN   C 1  133 ? -21.460 -42.274  1.210   1.00 49.87  ? 133 GLN   C CG     1 
ATOM   7786  C  CD     . GLN   C 1  133 ? -20.023 -42.726  1.253   1.00 52.73  ? 133 GLN   C CD     1 
ATOM   7787  O  OE1    . GLN   C 1  133 ? -19.422 -42.990  0.205   1.00 51.49  ? 133 GLN   C OE1    1 
ATOM   7788  N  NE2    . GLN   C 1  133 ? -19.455 -42.823  2.459   1.00 63.32  ? 133 GLN   C NE2    1 
ATOM   7789  N  N      . GLY   C 1  134 ? -23.479 -39.986  -1.526  1.00 35.90  ? 134 GLY   C N      1 
ATOM   7790  C  CA     . GLY   C 1  134 ? -23.692 -38.564  -1.631  1.00 37.74  ? 134 GLY   C CA     1 
ATOM   7791  C  C      . GLY   C 1  134 ? -23.108 -38.031  -2.920  1.00 37.88  ? 134 GLY   C C      1 
ATOM   7792  O  O      . GLY   C 1  134 ? -22.727 -38.787  -3.815  1.00 38.02  ? 134 GLY   C O      1 
ATOM   7793  N  N      . PHE   C 1  135 ? -23.035 -36.702  -2.973  1.00 38.74  ? 135 PHE   C N      1 
ATOM   7794  C  CA     . PHE   C 1  135 ? -22.615 -35.942  -4.141  1.00 35.77  ? 135 PHE   C CA     1 
ATOM   7795  C  C      . PHE   C 1  135 ? -21.390 -35.100  -3.820  1.00 37.77  ? 135 PHE   C C      1 
ATOM   7796  O  O      . PHE   C 1  135 ? -21.293 -34.542  -2.722  1.00 37.11  ? 135 PHE   C O      1 
ATOM   7797  C  CB     . PHE   C 1  135 ? -23.741 -35.043  -4.590  1.00 32.13  ? 135 PHE   C CB     1 
ATOM   7798  C  CG     . PHE   C 1  135 ? -25.004 -35.769  -4.818  1.00 32.81  ? 135 PHE   C CG     1 
ATOM   7799  C  CD1    . PHE   C 1  135 ? -25.281 -36.319  -6.050  1.00 37.06  ? 135 PHE   C CD1    1 
ATOM   7800  C  CD2    . PHE   C 1  135 ? -25.889 -35.966  -3.790  1.00 36.65  ? 135 PHE   C CD2    1 
ATOM   7801  C  CE1    . PHE   C 1  135 ? -26.442 -37.011  -6.270  1.00 35.82  ? 135 PHE   C CE1    1 
ATOM   7802  C  CE2    . PHE   C 1  135 ? -27.069 -36.672  -4.005  1.00 38.92  ? 135 PHE   C CE2    1 
ATOM   7803  C  CZ     . PHE   C 1  135 ? -27.341 -37.190  -5.247  1.00 36.08  ? 135 PHE   C CZ     1 
ATOM   7804  N  N      . LEU   C 1  136 ? -20.456 -35.011  -4.779  1.00 34.45  ? 136 LEU   C N      1 
ATOM   7805  C  CA     . LEU   C 1  136 ? -19.330 -34.080  -4.711  1.00 30.68  ? 136 LEU   C CA     1 
ATOM   7806  C  C      . LEU   C 1  136 ? -19.473 -33.052  -5.817  1.00 35.93  ? 136 LEU   C C      1 
ATOM   7807  O  O      . LEU   C 1  136 ? -19.268 -33.376  -6.989  1.00 39.81  ? 136 LEU   C O      1 
ATOM   7808  C  CB     . LEU   C 1  136 ? -17.989 -34.794  -4.830  1.00 33.52  ? 136 LEU   C CB     1 
ATOM   7809  C  CG     . LEU   C 1  136 ? -17.602 -35.768  -3.715  1.00 36.81  ? 136 LEU   C CG     1 
ATOM   7810  C  CD1    . LEU   C 1  136 ? -18.247 -37.153  -3.864  1.00 35.77  ? 136 LEU   C CD1    1 
ATOM   7811  C  CD2    . LEU   C 1  136 ? -16.089 -35.864  -3.670  1.00 32.57  ? 136 LEU   C CD2    1 
ATOM   7812  N  N      . VAL   C 1  137 ? -19.771 -31.810  -5.441  1.00 34.42  ? 137 VAL   C N      1 
ATOM   7813  C  CA     . VAL   C 1  137 ? -20.057 -30.735  -6.389  1.00 34.23  ? 137 VAL   C CA     1 
ATOM   7814  C  C      . VAL   C 1  137 ? -18.861 -29.801  -6.518  1.00 35.88  ? 137 VAL   C C      1 
ATOM   7815  O  O      . VAL   C 1  137 ? -18.465 -29.131  -5.551  1.00 35.48  ? 137 VAL   C O      1 
ATOM   7816  C  CB     . VAL   C 1  137 ? -21.299 -29.946  -5.966  1.00 37.68  ? 137 VAL   C CB     1 
ATOM   7817  C  CG1    . VAL   C 1  137 ? -21.615 -28.884  -7.019  1.00 32.08  ? 137 VAL   C CG1    1 
ATOM   7818  C  CG2    . VAL   C 1  137 ? -22.450 -30.912  -5.721  1.00 36.05  ? 137 VAL   C CG2    1 
ATOM   7819  N  N      . PHE   C 1  138 ? -18.318 -29.730  -7.728  1.00 33.00  ? 138 PHE   C N      1 
ATOM   7820  C  CA     . PHE   C 1  138 ? -17.240 -28.818  -8.089  1.00 30.47  ? 138 PHE   C CA     1 
ATOM   7821  C  C      . PHE   C 1  138 ? -17.805 -27.620  -8.836  1.00 30.59  ? 138 PHE   C C      1 
ATOM   7822  O  O      . PHE   C 1  138 ? -18.630 -27.767  -9.730  1.00 37.72  ? 138 PHE   C O      1 
ATOM   7823  C  CB     . PHE   C 1  138 ? -16.230 -29.530  -8.975  1.00 30.13  ? 138 PHE   C CB     1 
ATOM   7824  C  CG     . PHE   C 1  138 ? -15.624 -30.715  -8.329  1.00 32.71  ? 138 PHE   C CG     1 
ATOM   7825  C  CD1    . PHE   C 1  138 ? -16.377 -31.865  -8.134  1.00 35.61  ? 138 PHE   C CD1    1 
ATOM   7826  C  CD2    . PHE   C 1  138 ? -14.301 -30.702  -7.927  1.00 31.52  ? 138 PHE   C CD2    1 
ATOM   7827  C  CE1    . PHE   C 1  138 ? -15.824 -32.987  -7.533  1.00 39.35  ? 138 PHE   C CE1    1 
ATOM   7828  C  CE2    . PHE   C 1  138 ? -13.740 -31.807  -7.326  1.00 34.90  ? 138 PHE   C CE2    1 
ATOM   7829  C  CZ     . PHE   C 1  138 ? -14.505 -32.956  -7.124  1.00 36.81  ? 138 PHE   C CZ     1 
ATOM   7830  N  N      . HIS   C 1  139 ? -17.354 -26.430  -8.493  1.00 30.27  ? 139 HIS   C N      1 
ATOM   7831  C  CA     . HIS   C 1  139 ? -17.913 -25.255  -9.145  1.00 30.68  ? 139 HIS   C CA     1 
ATOM   7832  C  C      . HIS   C 1  139 ? -17.135 -24.060  -8.635  1.00 26.10  ? 139 HIS   C C      1 
ATOM   7833  O  O      . HIS   C 1  139 ? -16.435 -24.142  -7.626  1.00 26.82  ? 139 HIS   C O      1 
ATOM   7834  C  CB     . HIS   C 1  139 ? -19.396 -25.058  -8.821  1.00 33.58  ? 139 HIS   C CB     1 
ATOM   7835  C  CG     . HIS   C 1  139 ? -19.638 -24.731  -7.376  1.00 30.47  ? 139 HIS   C CG     1 
ATOM   7836  N  ND1    . HIS   C 1  139 ? -19.765 -23.437  -6.926  1.00 29.70  ? 139 HIS   C ND1    1 
ATOM   7837  C  CD2    . HIS   C 1  139 ? -19.725 -25.519  -6.283  1.00 27.45  ? 139 HIS   C CD2    1 
ATOM   7838  C  CE1    . HIS   C 1  139 ? -19.929 -23.440  -5.619  1.00 28.73  ? 139 HIS   C CE1    1 
ATOM   7839  N  NE2    . HIS   C 1  139 ? -19.898 -24.690  -5.206  1.00 30.69  ? 139 HIS   C NE2    1 
ATOM   7840  N  N      . SER   C 1  140 ? -17.287 -22.948  -9.320  1.00 27.60  ? 140 SER   C N      1 
ATOM   7841  C  CA     . SER   C 1  140 ? -16.659 -21.711  -8.903  1.00 32.21  ? 140 SER   C CA     1 
ATOM   7842  C  C      . SER   C 1  140 ? -17.657 -20.840  -8.134  1.00 30.16  ? 140 SER   C C      1 
ATOM   7843  O  O      . SER   C 1  140 ? -18.868 -20.947  -8.314  1.00 27.85  ? 140 SER   C O      1 
ATOM   7844  C  CB     . SER   C 1  140 ? -16.121 -20.965  -10.122 1.00 30.50  ? 140 SER   C CB     1 
ATOM   7845  O  OG     . SER   C 1  140 ? -17.204 -20.543  -10.932 1.00 31.37  ? 140 SER   C OG     1 
ATOM   7846  N  N      . PHE   C 1  141 ? -17.136 -19.999  -7.238  1.00 32.68  ? 141 PHE   C N      1 
ATOM   7847  C  CA     . PHE   C 1  141 ? -17.981 -18.979  -6.641  1.00 29.90  ? 141 PHE   C CA     1 
ATOM   7848  C  C      . PHE   C 1  141 ? -18.295 -17.897  -7.653  1.00 34.82  ? 141 PHE   C C      1 
ATOM   7849  O  O      . PHE   C 1  141 ? -19.390 -17.334  -7.632  1.00 34.76  ? 141 PHE   C O      1 
ATOM   7850  C  CB     . PHE   C 1  141 ? -17.292 -18.325  -5.443  1.00 30.49  ? 141 PHE   C CB     1 
ATOM   7851  C  CG     . PHE   C 1  141 ? -17.428 -19.082  -4.156  1.00 36.26  ? 141 PHE   C CG     1 
ATOM   7852  C  CD1    . PHE   C 1  141 ? -18.316 -20.125  -4.033  1.00 36.83  ? 141 PHE   C CD1    1 
ATOM   7853  C  CD2    . PHE   C 1  141 ? -16.667 -18.732  -3.048  1.00 38.30  ? 141 PHE   C CD2    1 
ATOM   7854  C  CE1    . PHE   C 1  141 ? -18.431 -20.815  -2.823  1.00 42.63  ? 141 PHE   C CE1    1 
ATOM   7855  C  CE2    . PHE   C 1  141 ? -16.789 -19.418  -1.839  1.00 35.26  ? 141 PHE   C CE2    1 
ATOM   7856  C  CZ     . PHE   C 1  141 ? -17.672 -20.453  -1.732  1.00 37.41  ? 141 PHE   C CZ     1 
ATOM   7857  N  N      . GLY   C 1  142 ? -17.347 -17.594  -8.540  1.00 30.90  ? 142 GLY   C N      1 
ATOM   7858  C  CA     . GLY   C 1  142 ? -17.354 -16.325  -9.244  1.00 31.07  ? 142 GLY   C CA     1 
ATOM   7859  C  C      . GLY   C 1  142 ? -18.109 -16.271  -10.552 1.00 35.10  ? 142 GLY   C C      1 
ATOM   7860  O  O      . GLY   C 1  142 ? -18.603 -15.201  -10.930 1.00 35.49  ? 142 GLY   C O      1 
ATOM   7861  N  N      . GLY   C 1  143 ? -18.195 -17.400  -11.265 1.00 29.90  ? 143 GLY   C N      1 
ATOM   7862  C  CA     . GLY   C 1  143 ? -18.932 -17.415  -12.502 1.00 27.29  ? 143 GLY   C CA     1 
ATOM   7863  C  C      . GLY   C 1  143 ? -20.427 -17.463  -12.279 1.00 29.20  ? 143 GLY   C C      1 
ATOM   7864  O  O      . GLY   C 1  143 ? -20.919 -17.901  -11.249 1.00 34.39  ? 143 GLY   C O      1 
ATOM   7865  N  N      . GLY   C 1  144 ? -21.173 -16.989  -13.274 1.00 36.04  ? 144 GLY   C N      1 
ATOM   7866  C  CA     . GLY   C 1  144 ? -22.621 -16.983  -13.171 1.00 29.39  ? 144 GLY   C CA     1 
ATOM   7867  C  C      . GLY   C 1  144 ? -23.245 -18.362  -13.227 1.00 30.03  ? 144 GLY   C C      1 
ATOM   7868  O  O      . GLY   C 1  144 ? -24.336 -18.565  -12.698 1.00 36.86  ? 144 GLY   C O      1 
ATOM   7869  N  N      . THR   C 1  145 ? -22.592 -19.320  -13.885 1.00 27.51  ? 145 THR   C N      1 
ATOM   7870  C  CA     . THR   C 1  145 ? -23.064 -20.694  -13.807 1.00 24.24  ? 145 THR   C CA     1 
ATOM   7871  C  C      . THR   C 1  145 ? -22.594 -21.348  -12.524 1.00 31.24  ? 145 THR   C C      1 
ATOM   7872  O  O      . THR   C 1  145 ? -23.410 -21.754  -11.693 1.00 30.26  ? 145 THR   C O      1 
ATOM   7873  C  CB     . THR   C 1  145 ? -22.608 -21.489  -15.017 1.00 27.20  ? 145 THR   C CB     1 
ATOM   7874  O  OG1    . THR   C 1  145 ? -23.005 -20.798  -16.201 1.00 37.03  ? 145 THR   C OG1    1 
ATOM   7875  C  CG2    . THR   C 1  145 ? -23.177 -22.861  -15.017 1.00 28.16  ? 145 THR   C CG2    1 
ATOM   7876  N  N      . GLY   C 1  146 ? -21.278 -21.450  -12.352 1.00 33.02  ? 146 GLY   C N      1 
ATOM   7877  C  CA     . GLY   C 1  146 ? -20.658 -21.787  -11.089 1.00 25.03  ? 146 GLY   C CA     1 
ATOM   7878  C  C      . GLY   C 1  146 ? -21.429 -21.326  -9.869  1.00 30.46  ? 146 GLY   C C      1 
ATOM   7879  O  O      . GLY   C 1  146 ? -21.595 -22.105  -8.919  1.00 33.26  ? 146 GLY   C O      1 
ATOM   7880  N  N      . SER   C 1  147 ? -21.919 -20.081  -9.865  1.00 29.12  ? 147 SER   C N      1 
ATOM   7881  C  CA     . SER   C 1  147 ? -22.669 -19.565  -8.716  1.00 34.36  ? 147 SER   C CA     1 
ATOM   7882  C  C      . SER   C 1  147 ? -24.172 -19.857  -8.816  1.00 36.99  ? 147 SER   C C      1 
ATOM   7883  O  O      . SER   C 1  147 ? -24.751 -20.548  -7.967  1.00 35.73  ? 147 SER   C O      1 
ATOM   7884  C  CB     . SER   C 1  147 ? -22.458 -18.059  -8.583  1.00 32.27  ? 147 SER   C CB     1 
ATOM   7885  O  OG     . SER   C 1  147 ? -22.993 -17.373  -9.692  1.00 30.34  ? 147 SER   C OG     1 
ATOM   7886  N  N      . GLY   C 1  148 ? -24.812 -19.325  -9.852  1.00 32.58  ? 148 GLY   C N      1 
ATOM   7887  C  CA     . GLY   C 1  148 ? -26.250 -19.464  -9.970  1.00 35.54  ? 148 GLY   C CA     1 
ATOM   7888  C  C      . GLY   C 1  148 ? -26.709 -20.883  -10.246 1.00 36.48  ? 148 GLY   C C      1 
ATOM   7889  O  O      . GLY   C 1  148 ? -27.672 -21.352  -9.643  1.00 39.89  ? 148 GLY   C O      1 
ATOM   7890  N  N      . PHE   C 1  149 ? -26.068 -21.585  -11.180 1.00 34.14  ? 149 PHE   C N      1 
ATOM   7891  C  CA     . PHE   C 1  149 ? -26.609 -22.900  -11.500 1.00 32.72  ? 149 PHE   C CA     1 
ATOM   7892  C  C      . PHE   C 1  149 ? -26.367 -23.869  -10.356 1.00 33.13  ? 149 PHE   C C      1 
ATOM   7893  O  O      . PHE   C 1  149 ? -27.280 -24.585  -9.938  1.00 32.48  ? 149 PHE   C O      1 
ATOM   7894  C  CB     . PHE   C 1  149 ? -26.029 -23.440  -12.799 1.00 31.44  ? 149 PHE   C CB     1 
ATOM   7895  C  CG     . PHE   C 1  149 ? -26.730 -24.680  -13.292 1.00 33.15  ? 149 PHE   C CG     1 
ATOM   7896  C  CD1    . PHE   C 1  149 ? -27.969 -24.595  -13.889 1.00 31.83  ? 149 PHE   C CD1    1 
ATOM   7897  C  CD2    . PHE   C 1  149 ? -26.151 -25.923  -13.169 1.00 33.18  ? 149 PHE   C CD2    1 
ATOM   7898  C  CE1    . PHE   C 1  149 ? -28.610 -25.727  -14.331 1.00 32.53  ? 149 PHE   C CE1    1 
ATOM   7899  C  CE2    . PHE   C 1  149 ? -26.807 -27.065  -13.620 1.00 31.58  ? 149 PHE   C CE2    1 
ATOM   7900  C  CZ     . PHE   C 1  149 ? -28.031 -26.959  -14.192 1.00 30.59  ? 149 PHE   C CZ     1 
ATOM   7901  N  N      . THR   C 1  150 ? -25.140 -23.897  -9.835  1.00 32.92  ? 150 THR   C N      1 
ATOM   7902  C  CA     . THR   C 1  150 ? -24.824 -24.709  -8.664  1.00 31.99  ? 150 THR   C CA     1 
ATOM   7903  C  C      . THR   C 1  150 ? -25.868 -24.564  -7.564  1.00 32.43  ? 150 THR   C C      1 
ATOM   7904  O  O      . THR   C 1  150 ? -26.314 -25.556  -6.979  1.00 32.45  ? 150 THR   C O      1 
ATOM   7905  C  CB     . THR   C 1  150 ? -23.446 -24.331  -8.122  1.00 32.20  ? 150 THR   C CB     1 
ATOM   7906  O  OG1    . THR   C 1  150 ? -22.457 -24.491  -9.147  1.00 28.14  ? 150 THR   C OG1    1 
ATOM   7907  C  CG2    . THR   C 1  150 ? -23.096 -25.165  -6.897  1.00 29.75  ? 150 THR   C CG2    1 
ATOM   7908  N  N      . SER   C 1  151 ? -26.254 -23.339  -7.240  1.00 29.90  ? 151 SER   C N      1 
ATOM   7909  C  CA     . SER   C 1  151 ? -27.143 -23.195  -6.101  1.00 31.95  ? 151 SER   C CA     1 
ATOM   7910  C  C      . SER   C 1  151 ? -28.536 -23.716  -6.424  1.00 34.64  ? 151 SER   C C      1 
ATOM   7911  O  O      . SER   C 1  151 ? -29.107 -24.475  -5.631  1.00 35.84  ? 151 SER   C O      1 
ATOM   7912  C  CB     . SER   C 1  151 ? -27.138 -21.752  -5.606  1.00 33.48  ? 151 SER   C CB     1 
ATOM   7913  O  OG     . SER   C 1  151 ? -27.499 -20.862  -6.621  1.00 38.58  ? 151 SER   C OG     1 
ATOM   7914  N  N      . LEU   C 1  152 ? -29.086 -23.353  -7.595  1.00 33.80  ? 152 LEU   C N      1 
ATOM   7915  C  CA     . LEU   C 1  152 ? -30.257 -24.027  -8.155  1.00 31.00  ? 152 LEU   C CA     1 
ATOM   7916  C  C      . LEU   C 1  152 ? -30.202 -25.537  -7.998  1.00 33.02  ? 152 LEU   C C      1 
ATOM   7917  O  O      . LEU   C 1  152 ? -31.114 -26.157  -7.446  1.00 38.11  ? 152 LEU   C O      1 
ATOM   7918  C  CB     . LEU   C 1  152 ? -30.400 -23.713  -9.641  1.00 37.01  ? 152 LEU   C CB     1 
ATOM   7919  C  CG     . LEU   C 1  152 ? -31.644 -24.419  -10.184 1.00 35.27  ? 152 LEU   C CG     1 
ATOM   7920  C  CD1    . LEU   C 1  152 ? -32.885 -23.927  -9.420  1.00 37.70  ? 152 LEU   C CD1    1 
ATOM   7921  C  CD2    . LEU   C 1  152 ? -31.784 -24.328  -11.690 1.00 28.85  ? 152 LEU   C CD2    1 
ATOM   7922  N  N      . LEU   C 1  153 ? -29.150 -26.142  -8.535  1.00 30.95  ? 153 LEU   C N      1 
ATOM   7923  C  CA     . LEU   C 1  153 ? -28.989 -27.583  -8.440  1.00 31.64  ? 153 LEU   C CA     1 
ATOM   7924  C  C      . LEU   C 1  153 ? -29.030 -28.056  -6.989  1.00 34.88  ? 153 LEU   C C      1 
ATOM   7925  O  O      . LEU   C 1  153 ? -29.766 -28.994  -6.651  1.00 34.00  ? 153 LEU   C O      1 
ATOM   7926  C  CB     . LEU   C 1  153 ? -27.690 -27.989  -9.146  1.00 29.91  ? 153 LEU   C CB     1 
ATOM   7927  C  CG     . LEU   C 1  153 ? -27.295 -29.458  -9.071  1.00 36.17  ? 153 LEU   C CG     1 
ATOM   7928  C  CD1    . LEU   C 1  153 ? -28.297 -30.270  -9.815  1.00 36.71  ? 153 LEU   C CD1    1 
ATOM   7929  C  CD2    . LEU   C 1  153 ? -25.960 -29.654  -9.731  1.00 32.57  ? 153 LEU   C CD2    1 
ATOM   7930  N  N      . MET   C 1  154 ? -28.263 -27.403  -6.108  1.00 32.87  ? 154 MET   C N      1 
ATOM   7931  C  CA     . MET   C 1  154 ? -28.196 -27.841  -4.714  1.00 34.34  ? 154 MET   C CA     1 
ATOM   7932  C  C      . MET   C 1  154 ? -29.584 -27.893  -4.072  1.00 34.83  ? 154 MET   C C      1 
ATOM   7933  O  O      . MET   C 1  154 ? -29.918 -28.854  -3.371  1.00 34.65  ? 154 MET   C O      1 
ATOM   7934  C  CB     . MET   C 1  154 ? -27.281 -26.918  -3.903  1.00 34.74  ? 154 MET   C CB     1 
ATOM   7935  C  CG     . MET   C 1  154 ? -25.778 -26.969  -4.135  1.00 33.29  ? 154 MET   C CG     1 
ATOM   7936  S  SD     . MET   C 1  154 ? -25.021 -28.574  -3.857  1.00 39.15  ? 154 MET   C SD     1 
ATOM   7937  C  CE     . MET   C 1  154 ? -24.346 -28.371  -2.215  1.00 40.60  ? 154 MET   C CE     1 
ATOM   7938  N  N      . GLU   C 1  155 ? -30.375 -26.826  -4.240  1.00 36.48  ? 155 GLU   C N      1 
ATOM   7939  C  CA     . GLU   C 1  155 ? -31.780 -26.824  -3.825  1.00 37.42  ? 155 GLU   C CA     1 
ATOM   7940  C  C      . GLU   C 1  155 ? -32.503 -28.045  -4.393  1.00 40.15  ? 155 GLU   C C      1 
ATOM   7941  O  O      . GLU   C 1  155 ? -33.149 -28.815  -3.674  1.00 36.95  ? 155 GLU   C O      1 
ATOM   7942  C  CB     . GLU   C 1  155 ? -32.433 -25.533  -4.319  1.00 28.87  ? 155 GLU   C CB     1 
ATOM   7943  C  CG     . GLU   C 1  155 ? -31.766 -24.336  -3.718  1.00 37.98  ? 155 GLU   C CG     1 
ATOM   7944  C  CD     . GLU   C 1  155 ? -32.363 -23.009  -4.135  1.00 45.46  ? 155 GLU   C CD     1 
ATOM   7945  O  OE1    . GLU   C 1  155 ? -32.364 -22.687  -5.337  1.00 40.26  ? 155 GLU   C OE1    1 
ATOM   7946  O  OE2    . GLU   C 1  155 ? -32.814 -22.262  -3.256  1.00 59.75  ? 155 GLU   C OE2    1 
ATOM   7947  N  N      . ARG   C 1  156 ? -32.368 -28.261  -5.696  1.00 37.68  ? 156 ARG   C N      1 
ATOM   7948  C  CA     . ARG   C 1  156 ? -33.067 -29.374  -6.306  1.00 38.10  ? 156 ARG   C CA     1 
ATOM   7949  C  C      . ARG   C 1  156 ? -32.574 -30.695  -5.740  1.00 40.40  ? 156 ARG   C C      1 
ATOM   7950  O  O      . ARG   C 1  156 ? -33.375 -31.592  -5.474  1.00 42.06  ? 156 ARG   C O      1 
ATOM   7951  C  CB     . ARG   C 1  156 ? -32.894 -29.314  -7.822  1.00 36.30  ? 156 ARG   C CB     1 
ATOM   7952  C  CG     . ARG   C 1  156 ? -33.682 -28.178  -8.444  1.00 38.53  ? 156 ARG   C CG     1 
ATOM   7953  C  CD     . ARG   C 1  156 ? -35.173 -28.411  -8.282  1.00 43.68  ? 156 ARG   C CD     1 
ATOM   7954  N  NE     . ARG   C 1  156 ? -35.583 -29.468  -9.195  1.00 46.94  ? 156 ARG   C NE     1 
ATOM   7955  C  CZ     . ARG   C 1  156 ? -35.912 -29.281  -10.464 1.00 41.28  ? 156 ARG   C CZ     1 
ATOM   7956  N  NH1    . ARG   C 1  156 ? -36.040 -28.064  -10.976 1.00 40.13  ? 156 ARG   C NH1    1 
ATOM   7957  N  NH2    . ARG   C 1  156 ? -36.098 -30.342  -11.242 1.00 38.57  ? 156 ARG   C NH2    1 
ATOM   7958  N  N      . LEU   C 1  157 ? -31.259 -30.833  -5.546  1.00 36.56  ? 157 LEU   C N      1 
ATOM   7959  C  CA     . LEU   C 1  157 ? -30.727 -32.070  -4.990  1.00 34.99  ? 157 LEU   C CA     1 
ATOM   7960  C  C      . LEU   C 1  157 ? -31.265 -32.324  -3.586  1.00 35.67  ? 157 LEU   C C      1 
ATOM   7961  O  O      . LEU   C 1  157 ? -31.587 -33.461  -3.234  1.00 35.06  ? 157 LEU   C O      1 
ATOM   7962  C  CB     . LEU   C 1  157 ? -29.209 -32.015  -4.975  1.00 36.06  ? 157 LEU   C CB     1 
ATOM   7963  C  CG     . LEU   C 1  157 ? -28.511 -32.068  -6.330  1.00 39.87  ? 157 LEU   C CG     1 
ATOM   7964  C  CD1    . LEU   C 1  157 ? -26.989 -32.242  -6.125  1.00 34.20  ? 157 LEU   C CD1    1 
ATOM   7965  C  CD2    . LEU   C 1  157 ? -29.105 -33.192  -7.193  1.00 41.71  ? 157 LEU   C CD2    1 
ATOM   7966  N  N      . SER   C 1  158 ? -31.365 -31.276  -2.768  1.00 34.32  ? 158 SER   C N      1 
ATOM   7967  C  CA     . SER   C 1  158 ? -31.946 -31.425  -1.444  1.00 35.19  ? 158 SER   C CA     1 
ATOM   7968  C  C      . SER   C 1  158 ? -33.346 -32.000  -1.517  1.00 42.15  ? 158 SER   C C      1 
ATOM   7969  O  O      . SER   C 1  158 ? -33.751 -32.783  -0.644  1.00 42.15  ? 158 SER   C O      1 
ATOM   7970  C  CB     . SER   C 1  158 ? -31.982 -30.080  -0.743  1.00 35.15  ? 158 SER   C CB     1 
ATOM   7971  O  OG     . SER   C 1  158 ? -30.715 -29.768  -0.233  1.00 43.73  ? 158 SER   C OG     1 
ATOM   7972  N  N      . VAL   C 1  159 ? -34.100 -31.595  -2.539  1.00 43.36  ? 159 VAL   C N      1 
ATOM   7973  C  CA     . VAL   C 1  159 ? -35.487 -32.014  -2.701  1.00 38.84  ? 159 VAL   C CA     1 
ATOM   7974  C  C      . VAL   C 1  159 ? -35.566 -33.464  -3.159  1.00 34.82  ? 159 VAL   C C      1 
ATOM   7975  O  O      . VAL   C 1  159 ? -36.402 -34.229  -2.677  1.00 36.56  ? 159 VAL   C O      1 
ATOM   7976  C  CB     . VAL   C 1  159 ? -36.194 -31.048  -3.671  1.00 39.19  ? 159 VAL   C CB     1 
ATOM   7977  C  CG1    . VAL   C 1  159 ? -37.464 -31.626  -4.194  1.00 44.14  ? 159 VAL   C CG1    1 
ATOM   7978  C  CG2    . VAL   C 1  159 ? -36.511 -29.761  -2.961  1.00 43.22  ? 159 VAL   C CG2    1 
ATOM   7979  N  N      . ASP   C 1  160 ? -34.703 -33.874  -4.083  1.00 36.97  ? 160 ASP   C N      1 
ATOM   7980  C  CA     . ASP   C 1  160 ? -34.861 -35.196  -4.671  1.00 39.31  ? 160 ASP   C CA     1 
ATOM   7981  C  C      . ASP   C 1  160 ? -34.087 -36.250  -3.912  1.00 41.63  ? 160 ASP   C C      1 
ATOM   7982  O  O      . ASP   C 1  160 ? -34.336 -37.445  -4.118  1.00 48.24  ? 160 ASP   C O      1 
ATOM   7983  C  CB     . ASP   C 1  160 ? -34.407 -35.279  -6.155  1.00 36.45  ? 160 ASP   C CB     1 
ATOM   7984  C  CG     . ASP   C 1  160 ? -35.110 -34.262  -7.089  1.00 44.27  ? 160 ASP   C CG     1 
ATOM   7985  O  OD1    . ASP   C 1  160 ? -35.925 -33.411  -6.663  1.00 44.99  ? 160 ASP   C OD1    1 
ATOM   7986  O  OD2    . ASP   C 1  160 ? -34.914 -34.395  -8.314  1.00 50.07  ? 160 ASP   C OD2    1 
ATOM   7987  N  N      . TYR   C 1  161 ? -33.135 -35.853  -3.069  1.00 38.55  ? 161 TYR   C N      1 
ATOM   7988  C  CA     . TYR   C 1  161 ? -32.377 -36.837  -2.306  1.00 38.15  ? 161 TYR   C CA     1 
ATOM   7989  C  C      . TYR   C 1  161 ? -32.306 -36.448  -0.831  1.00 44.82  ? 161 TYR   C C      1 
ATOM   7990  O  O      . TYR   C 1  161 ? -31.523 -37.032  -0.076  1.00 48.42  ? 161 TYR   C O      1 
ATOM   7991  C  CB     . TYR   C 1  161 ? -30.972 -37.018  -2.879  1.00 34.99  ? 161 TYR   C CB     1 
ATOM   7992  C  CG     . TYR   C 1  161 ? -30.910 -37.403  -4.349  1.00 37.06  ? 161 TYR   C CG     1 
ATOM   7993  C  CD1    . TYR   C 1  161 ? -31.002 -36.434  -5.343  1.00 35.38  ? 161 TYR   C CD1    1 
ATOM   7994  C  CD2    . TYR   C 1  161 ? -30.752 -38.725  -4.744  1.00 36.53  ? 161 TYR   C CD2    1 
ATOM   7995  C  CE1    . TYR   C 1  161 ? -30.937 -36.777  -6.679  1.00 36.16  ? 161 TYR   C CE1    1 
ATOM   7996  C  CE2    . TYR   C 1  161 ? -30.689 -39.079  -6.080  1.00 32.18  ? 161 TYR   C CE2    1 
ATOM   7997  C  CZ     . TYR   C 1  161 ? -30.785 -38.107  -7.043  1.00 38.15  ? 161 TYR   C CZ     1 
ATOM   7998  O  OH     . TYR   C 1  161 ? -30.716 -38.455  -8.379  1.00 41.98  ? 161 TYR   C OH     1 
ATOM   7999  N  N      . GLY   C 1  162 ? -33.100 -35.477  -0.402  1.00 45.03  ? 162 GLY   C N      1 
ATOM   8000  C  CA     . GLY   C 1  162 ? -33.246 -35.249  1.021   1.00 45.51  ? 162 GLY   C CA     1 
ATOM   8001  C  C      . GLY   C 1  162 ? -31.909 -34.946  1.637   1.00 52.22  ? 162 GLY   C C      1 
ATOM   8002  O  O      . GLY   C 1  162 ? -31.141 -34.130  1.119   1.00 57.58  ? 162 GLY   C O      1 
ATOM   8003  N  N      . LYS   C 1  163 ? -31.604 -35.629  2.740   1.00 55.86  ? 163 LYS   C N      1 
ATOM   8004  C  CA     . LYS   C 1  163 ? -30.472 -35.256  3.579   1.00 49.75  ? 163 LYS   C CA     1 
ATOM   8005  C  C      . LYS   C 1  163 ? -29.174 -35.957  3.194   1.00 55.84  ? 163 LYS   C C      1 
ATOM   8006  O  O      . LYS   C 1  163 ? -28.130 -35.642  3.789   1.00 55.75  ? 163 LYS   C O      1 
ATOM   8007  C  CB     . LYS   C 1  163 ? -30.797 -35.544  5.038   1.00 54.44  ? 163 LYS   C CB     1 
ATOM   8008  C  CG     . LYS   C 1  163 ? -31.616 -34.462  5.667   1.00 57.13  ? 163 LYS   C CG     1 
ATOM   8009  C  CD     . LYS   C 1  163 ? -30.860 -33.161  5.562   1.00 62.30  ? 163 LYS   C CD     1 
ATOM   8010  C  CE     . LYS   C 1  163 ? -31.315 -32.181  6.623   1.00 61.76  ? 163 LYS   C CE     1 
ATOM   8011  N  NZ     . LYS   C 1  163 ? -30.481 -30.961  6.543   1.00 68.09  ? 163 LYS   C NZ     1 
ATOM   8012  N  N      . LYS   C 1  164 ? -29.231 -36.912  2.246   1.00 51.59  ? 164 LYS   C N      1 
ATOM   8013  C  CA     . LYS   C 1  164 ? -28.080 -37.432  1.512   1.00 43.13  ? 164 LYS   C CA     1 
ATOM   8014  C  C      . LYS   C 1  164 ? -26.982 -36.393  1.311   1.00 44.78  ? 164 LYS   C C      1 
ATOM   8015  O  O      . LYS   C 1  164 ? -27.285 -35.268  0.887   1.00 48.58  ? 164 LYS   C O      1 
ATOM   8016  C  CB     . LYS   C 1  164 ? -28.563 -37.964  0.160   1.00 43.36  ? 164 LYS   C CB     1 
ATOM   8017  C  CG     . LYS   C 1  164 ? -27.484 -38.518  -0.725  1.00 41.90  ? 164 LYS   C CG     1 
ATOM   8018  C  CD     . LYS   C 1  164 ? -27.243 -39.999  -0.517  1.00 41.38  ? 164 LYS   C CD     1 
ATOM   8019  C  CE     . LYS   C 1  164 ? -28.431 -40.844  -0.879  1.00 39.34  ? 164 LYS   C CE     1 
ATOM   8020  N  NZ     . LYS   C 1  164 ? -28.063 -42.280  -0.628  1.00 45.00  ? 164 LYS   C NZ     1 
ATOM   8021  N  N      . SER   C 1  165 ? -25.717 -36.777  1.571   1.00 36.68  ? 165 SER   C N      1 
ATOM   8022  C  CA     . SER   C 1  165 ? -24.602 -35.828  1.645   1.00 34.47  ? 165 SER   C CA     1 
ATOM   8023  C  C      . SER   C 1  165 ? -24.336 -35.058  0.356   1.00 38.30  ? 165 SER   C C      1 
ATOM   8024  O  O      . SER   C 1  165 ? -24.310 -35.626  -0.741  1.00 43.79  ? 165 SER   C O      1 
ATOM   8025  C  CB     . SER   C 1  165 ? -23.310 -36.540  2.009   1.00 39.37  ? 165 SER   C CB     1 
ATOM   8026  O  OG     . SER   C 1  165 ? -23.087 -36.528  3.402   1.00 58.00  ? 165 SER   C OG     1 
ATOM   8027  N  N      . LYS   C 1  166 ? -24.056 -33.764  0.506   1.00 32.20  ? 166 LYS   C N      1 
ATOM   8028  C  CA     . LYS   C 1  166 ? -23.545 -32.948  -0.583  1.00 32.82  ? 166 LYS   C CA     1 
ATOM   8029  C  C      . LYS   C 1  166 ? -22.319 -32.163  -0.117  1.00 31.65  ? 166 LYS   C C      1 
ATOM   8030  O  O      . LYS   C 1  166 ? -22.434 -31.222  0.669   1.00 31.02  ? 166 LYS   C O      1 
ATOM   8031  C  CB     . LYS   C 1  166 ? -24.636 -32.041  -1.124  1.00 31.27  ? 166 LYS   C CB     1 
ATOM   8032  C  CG     . LYS   C 1  166 ? -25.836 -32.833  -1.628  1.00 32.52  ? 166 LYS   C CG     1 
ATOM   8033  C  CD     . LYS   C 1  166 ? -26.906 -31.917  -2.305  1.00 40.98  ? 166 LYS   C CD     1 
ATOM   8034  C  CE     . LYS   C 1  166 ? -27.969 -31.391  -1.321  1.00 41.96  ? 166 LYS   C CE     1 
ATOM   8035  N  NZ     . LYS   C 1  166 ? -28.623 -32.532  -0.565  1.00 47.74  ? 166 LYS   C NZ     1 
ATOM   8036  N  N      . LEU   C 1  167 ? -21.148 -32.557  -0.616  1.00 28.47  ? 167 LEU   C N      1 
ATOM   8037  C  CA     . LEU   C 1  167 ? -19.887 -31.861  -0.419  1.00 25.56  ? 167 LEU   C CA     1 
ATOM   8038  C  C      . LEU   C 1  167 ? -19.602 -30.930  -1.600  1.00 32.33  ? 167 LEU   C C      1 
ATOM   8039  O  O      . LEU   C 1  167 ? -19.899 -31.258  -2.752  1.00 36.07  ? 167 LEU   C O      1 
ATOM   8040  C  CB     . LEU   C 1  167 ? -18.737 -32.857  -0.281  1.00 28.64  ? 167 LEU   C CB     1 
ATOM   8041  C  CG     . LEU   C 1  167 ? -18.276 -33.414  1.088   1.00 41.45  ? 167 LEU   C CG     1 
ATOM   8042  C  CD1    . LEU   C 1  167 ? -19.287 -34.292  1.870   1.00 32.00  ? 167 LEU   C CD1    1 
ATOM   8043  C  CD2    . LEU   C 1  167 ? -16.919 -34.126  0.928   1.00 36.47  ? 167 LEU   C CD2    1 
ATOM   8044  N  N      . GLU   C 1  168 ? -18.997 -29.782  -1.307  1.00 30.67  ? 168 GLU   C N      1 
ATOM   8045  C  CA     . GLU   C 1  168 ? -18.592 -28.776  -2.281  1.00 32.25  ? 168 GLU   C CA     1 
ATOM   8046  C  C      . GLU   C 1  168 ? -17.074 -28.654  -2.362  1.00 34.06  ? 168 GLU   C C      1 
ATOM   8047  O  O      . GLU   C 1  168 ? -16.389 -28.580  -1.337  1.00 30.42  ? 168 GLU   C O      1 
ATOM   8048  C  CB     . GLU   C 1  168 ? -19.172 -27.402  -1.911  1.00 31.45  ? 168 GLU   C CB     1 
ATOM   8049  C  CG     . GLU   C 1  168 ? -20.484 -27.038  -2.508  1.00 29.75  ? 168 GLU   C CG     1 
ATOM   8050  C  CD     . GLU   C 1  168 ? -21.016 -25.746  -1.948  1.00 31.41  ? 168 GLU   C CD     1 
ATOM   8051  O  OE1    . GLU   C 1  168 ? -21.435 -25.780  -0.779  1.00 41.90  ? 168 GLU   C OE1    1 
ATOM   8052  O  OE2    . GLU   C 1  168 ? -20.983 -24.696  -2.602  1.00 30.76  ? 168 GLU   C OE2    1 
ATOM   8053  N  N      . PHE   C 1  169 ? -16.556 -28.593  -3.591  1.00 34.32  ? 169 PHE   C N      1 
ATOM   8054  C  CA     . PHE   C 1  169 ? -15.228 -28.047  -3.868  1.00 31.52  ? 169 PHE   C CA     1 
ATOM   8055  C  C      . PHE   C 1  169 ? -15.464 -26.726  -4.590  1.00 32.98  ? 169 PHE   C C      1 
ATOM   8056  O  O      . PHE   C 1  169 ? -15.720 -26.719  -5.795  1.00 35.03  ? 169 PHE   C O      1 
ATOM   8057  C  CB     . PHE   C 1  169 ? -14.400 -28.992  -4.719  1.00 30.19  ? 169 PHE   C CB     1 
ATOM   8058  C  CG     . PHE   C 1  169 ? -13.797 -30.118  -3.946  1.00 37.73  ? 169 PHE   C CG     1 
ATOM   8059  C  CD1    . PHE   C 1  169 ? -12.618 -29.944  -3.252  1.00 36.70  ? 169 PHE   C CD1    1 
ATOM   8060  C  CD2    . PHE   C 1  169 ? -14.431 -31.366  -3.894  1.00 41.18  ? 169 PHE   C CD2    1 
ATOM   8061  C  CE1    . PHE   C 1  169 ? -12.064 -31.000  -2.509  1.00 41.55  ? 169 PHE   C CE1    1 
ATOM   8062  C  CE2    . PHE   C 1  169 ? -13.886 -32.430  -3.154  1.00 43.77  ? 169 PHE   C CE2    1 
ATOM   8063  C  CZ     . PHE   C 1  169 ? -12.701 -32.246  -2.463  1.00 40.22  ? 169 PHE   C CZ     1 
ATOM   8064  N  N      . SER   C 1  170 ? -15.392 -25.605  -3.866  1.00 29.01  ? 170 SER   C N      1 
ATOM   8065  C  CA     . SER   C 1  170 ? -15.755 -24.305  -4.422  1.00 31.40  ? 170 SER   C CA     1 
ATOM   8066  C  C      . SER   C 1  170 ? -14.516 -23.454  -4.649  1.00 32.04  ? 170 SER   C C      1 
ATOM   8067  O  O      . SER   C 1  170 ? -13.684 -23.326  -3.743  1.00 32.17  ? 170 SER   C O      1 
ATOM   8068  C  CB     . SER   C 1  170 ? -16.728 -23.547  -3.511  1.00 33.28  ? 170 SER   C CB     1 
ATOM   8069  O  OG     . SER   C 1  170 ? -17.815 -24.344  -3.068  1.00 39.93  ? 170 SER   C OG     1 
ATOM   8070  N  N      . ILE   C 1  171 ? -14.420 -22.840  -5.837  1.00 26.94  ? 171 ILE   C N      1 
ATOM   8071  C  CA     . ILE   C 1  171 ? -13.315 -21.943  -6.171  1.00 26.60  ? 171 ILE   C CA     1 
ATOM   8072  C  C      . ILE   C 1  171 ? -13.667 -20.537  -5.730  1.00 29.28  ? 171 ILE   C C      1 
ATOM   8073  O  O      . ILE   C 1  171 ? -14.495 -19.878  -6.358  1.00 32.66  ? 171 ILE   C O      1 
ATOM   8074  C  CB     . ILE   C 1  171 ? -12.989 -21.941  -7.660  1.00 26.42  ? 171 ILE   C CB     1 
ATOM   8075  C  CG1    . ILE   C 1  171 ? -12.830 -23.359  -8.170  1.00 27.29  ? 171 ILE   C CG1    1 
ATOM   8076  C  CG2    . ILE   C 1  171 ? -11.724 -21.185  -7.879  1.00 24.77  ? 171 ILE   C CG2    1 
ATOM   8077  C  CD1    . ILE   C 1  171 ? -12.107 -24.228  -7.265  1.00 27.37  ? 171 ILE   C CD1    1 
ATOM   8078  N  N      . TYR   C 1  172 ? -12.995 -20.075  -4.688  1.00 30.49  ? 172 TYR   C N      1 
ATOM   8079  C  CA     . TYR   C 1  172 ? -13.067 -18.721  -4.154  1.00 28.30  ? 172 TYR   C CA     1 
ATOM   8080  C  C      . TYR   C 1  172 ? -12.217 -17.789  -5.015  1.00 32.04  ? 172 TYR   C C      1 
ATOM   8081  O  O      . TYR   C 1  172 ? -11.089 -18.142  -5.376  1.00 31.28  ? 172 TYR   C O      1 
ATOM   8082  C  CB     . TYR   C 1  172 ? -12.539 -18.733  -2.738  1.00 32.85  ? 172 TYR   C CB     1 
ATOM   8083  C  CG     . TYR   C 1  172 ? -12.501 -17.433  -2.004  1.00 33.81  ? 172 TYR   C CG     1 
ATOM   8084  C  CD1    . TYR   C 1  172 ? -11.459 -16.538  -2.207  1.00 30.66  ? 172 TYR   C CD1    1 
ATOM   8085  C  CD2    . TYR   C 1  172 ? -13.424 -17.168  -1.008  1.00 31.79  ? 172 TYR   C CD2    1 
ATOM   8086  C  CE1    . TYR   C 1  172 ? -11.381 -15.380  -1.508  1.00 33.31  ? 172 TYR   C CE1    1 
ATOM   8087  C  CE2    . TYR   C 1  172 ? -13.355 -16.007  -0.283  1.00 34.93  ? 172 TYR   C CE2    1 
ATOM   8088  C  CZ     . TYR   C 1  172 ? -12.330 -15.103  -0.535  1.00 37.68  ? 172 TYR   C CZ     1 
ATOM   8089  O  OH     . TYR   C 1  172 ? -12.259 -13.930  0.203   1.00 34.06  ? 172 TYR   C OH     1 
ATOM   8090  N  N      . PRO   C 1  173 ? -12.704 -16.598  -5.342  1.00 29.15  ? 173 PRO   C N      1 
ATOM   8091  C  CA     . PRO   C 1  173 ? -12.100 -15.833  -6.420  1.00 25.18  ? 173 PRO   C CA     1 
ATOM   8092  C  C      . PRO   C 1  173 ? -10.871 -15.061  -5.988  1.00 35.79  ? 173 PRO   C C      1 
ATOM   8093  O  O      . PRO   C 1  173 ? -10.739 -14.622  -4.841  1.00 40.48  ? 173 PRO   C O      1 
ATOM   8094  C  CB     . PRO   C 1  173 ? -13.230 -14.889  -6.820  1.00 25.56  ? 173 PRO   C CB     1 
ATOM   8095  C  CG     . PRO   C 1  173 ? -14.007 -14.734  -5.624  1.00 23.97  ? 173 PRO   C CG     1 
ATOM   8096  C  CD     . PRO   C 1  173 ? -14.011 -16.038  -4.958  1.00 32.38  ? 173 PRO   C CD     1 
ATOM   8097  N  N      . ALA   C 1  174 ? -9.957  -14.905  -6.944  1.00 36.26  ? 174 ALA   C N      1 
ATOM   8098  C  CA     . ALA   C 1  174 ? -8.771  -14.104  -6.763  1.00 35.58  ? 174 ALA   C CA     1 
ATOM   8099  C  C      . ALA   C 1  174 ? -8.621  -13.160  -7.943  1.00 48.13  ? 174 ALA   C C      1 
ATOM   8100  O  O      . ALA   C 1  174 ? -8.871  -13.551  -9.093  1.00 51.14  ? 174 ALA   C O      1 
ATOM   8101  C  CB     . ALA   C 1  174 ? -7.521  -14.973  -6.655  1.00 44.00  ? 174 ALA   C CB     1 
ATOM   8102  N  N      . PRO   C 1  175 ? -8.192  -11.921  -7.686  1.00 56.20  ? 175 PRO   C N      1 
ATOM   8103  C  CA     . PRO   C 1  175 ? -7.953  -10.965  -8.788  1.00 47.81  ? 175 PRO   C CA     1 
ATOM   8104  C  C      . PRO   C 1  175 ? -6.946  -11.422  -9.850  1.00 44.92  ? 175 PRO   C C      1 
ATOM   8105  O  O      . PRO   C 1  175 ? -7.162  -11.139  -11.032 1.00 41.04  ? 175 PRO   C O      1 
ATOM   8106  C  CB     . PRO   C 1  175 ? -7.462  -9.725   -8.039  1.00 48.22  ? 175 PRO   C CB     1 
ATOM   8107  C  CG     . PRO   C 1  175 ? -6.828  -10.277  -6.765  1.00 48.17  ? 175 PRO   C CG     1 
ATOM   8108  C  CD     . PRO   C 1  175 ? -7.715  -11.421  -6.381  1.00 50.41  ? 175 PRO   C CD     1 
ATOM   8109  N  N      . GLN   C 1  176 ? -5.860  -12.115  -9.475  1.00 49.70  ? 176 GLN   C N      1 
ATOM   8110  C  CA     . GLN   C 1  176 ? -4.860  -12.541  -10.460 1.00 51.68  ? 176 GLN   C CA     1 
ATOM   8111  C  C      . GLN   C 1  176 ? -5.476  -13.293  -11.633 1.00 53.81  ? 176 GLN   C C      1 
ATOM   8112  O  O      . GLN   C 1  176 ? -4.956  -13.220  -12.751 1.00 53.22  ? 176 GLN   C O      1 
ATOM   8113  C  CB     . GLN   C 1  176 ? -3.777  -13.432  -9.824  1.00 42.56  ? 176 GLN   C CB     1 
ATOM   8114  C  CG     . GLN   C 1  176 ? -2.810  -12.749  -8.856  1.00 39.03  ? 176 GLN   C CG     1 
ATOM   8115  C  CD     . GLN   C 1  176 ? -3.285  -12.705  -7.418  1.00 58.64  ? 176 GLN   C CD     1 
ATOM   8116  O  OE1    . GLN   C 1  176 ? -4.482  -12.831  -7.124  1.00 54.65  ? 176 GLN   C OE1    1 
ATOM   8117  N  NE2    . GLN   C 1  176 ? -2.327  -12.553  -6.494  1.00 65.30  ? 176 GLN   C NE2    1 
ATOM   8118  N  N      . VAL   C 1  177 ? -6.563  -14.033  -11.406 1.00 50.44  ? 177 VAL   C N      1 
ATOM   8119  C  CA     . VAL   C 1  177 ? -7.189  -14.828  -12.455 1.00 51.14  ? 177 VAL   C CA     1 
ATOM   8120  C  C      . VAL   C 1  177 ? -8.665  -14.520  -12.651 1.00 55.72  ? 177 VAL   C C      1 
ATOM   8121  O  O      . VAL   C 1  177 ? -9.286  -15.088  -13.559 1.00 57.62  ? 177 VAL   C O      1 
ATOM   8122  C  CB     . VAL   C 1  177 ? -6.984  -16.333  -12.204 1.00 53.97  ? 177 VAL   C CB     1 
ATOM   8123  C  CG1    . VAL   C 1  177 ? -5.562  -16.736  -12.539 1.00 47.24  ? 177 VAL   C CG1    1 
ATOM   8124  C  CG2    . VAL   C 1  177 ? -7.224  -16.618  -10.750 1.00 59.00  ? 177 VAL   C CG2    1 
ATOM   8125  N  N      . SER   C 1  178 ? -9.249  -13.625  -11.849 1.00 50.81  ? 178 SER   C N      1 
ATOM   8126  C  CA     . SER   C 1  178 ? -10.663 -13.287  -11.992 1.00 49.76  ? 178 SER   C CA     1 
ATOM   8127  C  C      . SER   C 1  178 ? -11.034 -12.953  -13.437 1.00 51.63  ? 178 SER   C C      1 
ATOM   8128  O  O      . SER   C 1  178 ? -10.287 -12.277  -14.149 1.00 54.31  ? 178 SER   C O      1 
ATOM   8129  C  CB     . SER   C 1  178 ? -10.990 -12.099  -11.091 1.00 49.37  ? 178 SER   C CB     1 
ATOM   8130  O  OG     . SER   C 1  178 ? -10.412 -10.934  -11.656 1.00 58.15  ? 178 SER   C OG     1 
ATOM   8131  N  N      . THR   C 1  179 ? -12.225 -13.395  -13.848 1.00 51.44  ? 179 THR   C N      1 
ATOM   8132  C  CA     . THR   C 1  179 ? -12.753 -13.131  -15.181 1.00 54.86  ? 179 THR   C CA     1 
ATOM   8133  C  C      . THR   C 1  179 ? -13.895 -12.112  -15.167 1.00 53.31  ? 179 THR   C C      1 
ATOM   8134  O  O      . THR   C 1  179 ? -14.606 -12.006  -16.176 1.00 53.81  ? 179 THR   C O      1 
ATOM   8135  C  CB     . THR   C 1  179 ? -13.248 -14.438  -15.849 1.00 53.70  ? 179 THR   C CB     1 
ATOM   8136  O  OG1    . THR   C 1  179 ? -14.424 -14.932  -15.205 1.00 40.95  ? 179 THR   C OG1    1 
ATOM   8137  C  CG2    . THR   C 1  179 ? -12.193 -15.553  -15.704 1.00 51.82  ? 179 THR   C CG2    1 
ATOM   8138  N  N      . ALA   C 1  180 ? -14.117 -11.385  -14.051 1.00 42.63  ? 180 ALA   C N      1 
ATOM   8139  C  CA     . ALA   C 1  180 ? -15.409 -10.724  -13.859 1.00 36.22  ? 180 ALA   C CA     1 
ATOM   8140  C  C      . ALA   C 1  180 ? -15.470 -9.770   -12.679 1.00 36.85  ? 180 ALA   C C      1 
ATOM   8141  O  O      . ALA   C 1  180 ? -15.145 -10.139  -11.548 1.00 38.58  ? 180 ALA   C O      1 
ATOM   8142  C  CB     . ALA   C 1  180 ? -16.502 -11.775  -13.693 1.00 33.54  ? 180 ALA   C CB     1 
ATOM   8143  N  N      . VAL   C 1  181 ? -15.916 -8.541   -12.917 1.00 33.38  ? 181 VAL   C N      1 
ATOM   8144  C  CA     . VAL   C 1  181 ? -15.881 -7.567   -11.837 1.00 34.88  ? 181 VAL   C CA     1 
ATOM   8145  C  C      . VAL   C 1  181 ? -16.986 -7.822   -10.808 1.00 34.20  ? 181 VAL   C C      1 
ATOM   8146  O  O      . VAL   C 1  181 ? -16.915 -7.297   -9.683  1.00 33.29  ? 181 VAL   C O      1 
ATOM   8147  C  CB     . VAL   C 1  181 ? -15.924 -6.139   -12.421 1.00 34.98  ? 181 VAL   C CB     1 
ATOM   8148  C  CG1    . VAL   C 1  181 ? -17.256 -5.858   -13.098 1.00 35.55  ? 181 VAL   C CG1    1 
ATOM   8149  C  CG2    . VAL   C 1  181 ? -15.666 -5.119   -11.362 1.00 32.70  ? 181 VAL   C CG2    1 
ATOM   8150  N  N      . VAL   C 1  182 ? -17.981 -8.644   -11.148 1.00 30.04  ? 182 VAL   C N      1 
ATOM   8151  C  CA     . VAL   C 1  182 ? -19.083 -8.938   -10.247 1.00 30.20  ? 182 VAL   C CA     1 
ATOM   8152  C  C      . VAL   C 1  182 ? -18.863 -10.252  -9.494  1.00 34.59  ? 182 VAL   C C      1 
ATOM   8153  O  O      . VAL   C 1  182 ? -19.812 -10.781  -8.895  1.00 33.24  ? 182 VAL   C O      1 
ATOM   8154  C  CB     . VAL   C 1  182 ? -20.443 -8.960   -10.984 1.00 30.07  ? 182 VAL   C CB     1 
ATOM   8155  C  CG1    . VAL   C 1  182 ? -20.787 -7.597   -11.546 1.00 33.60  ? 182 VAL   C CG1    1 
ATOM   8156  C  CG2    . VAL   C 1  182 ? -20.470 -10.014  -12.056 1.00 29.35  ? 182 VAL   C CG2    1 
ATOM   8157  N  N      . GLU   C 1  183 ? -17.649 -10.815  -9.520  1.00 31.24  ? 183 GLU   C N      1 
ATOM   8158  C  CA     . GLU   C 1  183 ? -17.471 -12.087  -8.828  1.00 30.86  ? 183 GLU   C CA     1 
ATOM   8159  C  C      . GLU   C 1  183 ? -17.895 -12.005  -7.373  1.00 30.54  ? 183 GLU   C C      1 
ATOM   8160  O  O      . GLU   C 1  183 ? -18.545 -12.958  -6.911  1.00 31.14  ? 183 GLU   C O      1 
ATOM   8161  C  CB     . GLU   C 1  183 ? -16.042 -12.627  -9.009  1.00 27.50  ? 183 GLU   C CB     1 
ATOM   8162  C  CG     . GLU   C 1  183 ? -15.889 -13.221  -10.411 1.00 32.43  ? 183 GLU   C CG     1 
ATOM   8163  C  CD     . GLU   C 1  183 ? -14.571 -13.933  -10.719 1.00 41.06  ? 183 GLU   C CD     1 
ATOM   8164  O  OE1    . GLU   C 1  183 ? -14.175 -14.872  -9.999  1.00 38.90  ? 183 GLU   C OE1    1 
ATOM   8165  O  OE2    . GLU   C 1  183 ? -13.920 -13.523  -11.719 1.00 38.65  ? 183 GLU   C OE2    1 
ATOM   8166  N  N      . PRO   C 1  184 ? -17.642 -10.916  -6.623  1.00 29.13  ? 184 PRO   C N      1 
ATOM   8167  C  CA     . PRO   C 1  184 ? -18.162 -10.856  -5.239  1.00 30.86  ? 184 PRO   C CA     1 
ATOM   8168  C  C      . PRO   C 1  184 ? -19.671 -11.041  -5.116  1.00 30.47  ? 184 PRO   C C      1 
ATOM   8169  O  O      . PRO   C 1  184 ? -20.120 -11.824  -4.267  1.00 29.07  ? 184 PRO   C O      1 
ATOM   8170  C  CB     . PRO   C 1  184 ? -17.704 -9.474   -4.758  1.00 27.19  ? 184 PRO   C CB     1 
ATOM   8171  C  CG     . PRO   C 1  184 ? -16.518 -9.209   -5.546  1.00 28.02  ? 184 PRO   C CG     1 
ATOM   8172  C  CD     . PRO   C 1  184 ? -16.759 -9.778   -6.903  1.00 26.19  ? 184 PRO   C CD     1 
ATOM   8173  N  N      . TYR   C 1  185 ? -20.467 -10.372  -5.950  1.00 29.40  ? 185 TYR   C N      1 
ATOM   8174  C  CA     . TYR   C 1  185 ? -21.913 -10.564  -5.893  1.00 30.40  ? 185 TYR   C CA     1 
ATOM   8175  C  C      . TYR   C 1  185 ? -22.293 -12.031  -6.099  1.00 27.27  ? 185 TYR   C C      1 
ATOM   8176  O  O      . TYR   C 1  185 ? -23.129 -12.578  -5.380  1.00 28.69  ? 185 TYR   C O      1 
ATOM   8177  C  CB     . TYR   C 1  185 ? -22.609 -9.703   -6.945  1.00 28.57  ? 185 TYR   C CB     1 
ATOM   8178  C  CG     . TYR   C 1  185 ? -22.703 -8.224   -6.668  1.00 30.32  ? 185 TYR   C CG     1 
ATOM   8179  C  CD1    . TYR   C 1  185 ? -22.326 -7.678   -5.446  1.00 31.74  ? 185 TYR   C CD1    1 
ATOM   8180  C  CD2    . TYR   C 1  185 ? -23.172 -7.365   -7.649  1.00 35.90  ? 185 TYR   C CD2    1 
ATOM   8181  C  CE1    . TYR   C 1  185 ? -22.408 -6.321   -5.226  1.00 32.02  ? 185 TYR   C CE1    1 
ATOM   8182  C  CE2    . TYR   C 1  185 ? -23.262 -6.010   -7.434  1.00 32.85  ? 185 TYR   C CE2    1 
ATOM   8183  C  CZ     . TYR   C 1  185 ? -22.885 -5.497   -6.231  1.00 32.79  ? 185 TYR   C CZ     1 
ATOM   8184  O  OH     . TYR   C 1  185 ? -22.999 -4.144   -6.054  1.00 37.03  ? 185 TYR   C OH     1 
ATOM   8185  N  N      . ASN   C 1  186 ? -21.744 -12.679  -7.112  1.00 26.94  ? 186 ASN   C N      1 
ATOM   8186  C  CA     . ASN   C 1  186 ? -22.135 -14.064  -7.292  1.00 28.72  ? 186 ASN   C CA     1 
ATOM   8187  C  C      . ASN   C 1  186 ? -21.705 -14.889  -6.085  1.00 34.31  ? 186 ASN   C C      1 
ATOM   8188  O  O      . ASN   C 1  186 ? -22.427 -15.798  -5.657  1.00 34.47  ? 186 ASN   C O      1 
ATOM   8189  C  CB     . ASN   C 1  186 ? -21.549 -14.640  -8.582  1.00 32.41  ? 186 ASN   C CB     1 
ATOM   8190  C  CG     . ASN   C 1  186 ? -21.923 -13.838  -9.815  1.00 35.18  ? 186 ASN   C CG     1 
ATOM   8191  O  OD1    . ASN   C 1  186 ? -22.903 -13.079  -9.819  1.00 32.15  ? 186 ASN   C OD1    1 
ATOM   8192  N  ND2    . ASN   C 1  186 ? -21.167 -14.046  -10.895 1.00 32.87  ? 186 ASN   C ND2    1 
ATOM   8193  N  N      . SER   C 1  187 ? -20.527 -14.586  -5.518  1.00 37.11  ? 187 SER   C N      1 
ATOM   8194  C  CA     . SER   C 1  187 ? -20.026 -15.345  -4.374  1.00 31.65  ? 187 SER   C CA     1 
ATOM   8195  C  C      . SER   C 1  187 ? -20.999 -15.286  -3.219  1.00 30.31  ? 187 SER   C C      1 
ATOM   8196  O  O      . SER   C 1  187 ? -21.421 -16.321  -2.700  1.00 33.38  ? 187 SER   C O      1 
ATOM   8197  C  CB     . SER   C 1  187 ? -18.653 -14.838  -3.934  1.00 31.89  ? 187 SER   C CB     1 
ATOM   8198  O  OG     . SER   C 1  187 ? -17.745 -14.835  -5.016  1.00 39.82  ? 187 SER   C OG     1 
ATOM   8199  N  N      . ILE   C 1  188 ? -21.364 -14.079  -2.791  1.00 28.53  ? 188 ILE   C N      1 
ATOM   8200  C  CA     . ILE   C 1  188 ? -22.276 -13.971  -1.661  1.00 28.16  ? 188 ILE   C CA     1 
ATOM   8201  C  C      . ILE   C 1  188 ? -23.611 -14.620  -1.985  1.00 30.36  ? 188 ILE   C C      1 
ATOM   8202  O  O      . ILE   C 1  188 ? -24.179 -15.343  -1.160  1.00 31.02  ? 188 ILE   C O      1 
ATOM   8203  C  CB     . ILE   C 1  188 ? -22.459 -12.513  -1.233  1.00 25.26  ? 188 ILE   C CB     1 
ATOM   8204  C  CG1    . ILE   C 1  188 ? -21.381 -12.114  -0.224  1.00 27.74  ? 188 ILE   C CG1    1 
ATOM   8205  C  CG2    . ILE   C 1  188 ? -23.824 -12.382  -0.647  1.00 28.57  ? 188 ILE   C CG2    1 
ATOM   8206  C  CD1    . ILE   C 1  188 ? -19.953 -12.213  -0.762  1.00 28.35  ? 188 ILE   C CD1    1 
ATOM   8207  N  N      . LEU   C 1  189 ? -24.140 -14.382  -3.187  1.00 33.71  ? 189 LEU   C N      1 
ATOM   8208  C  CA     . LEU   C 1  189 ? -25.455 -14.926  -3.508  1.00 33.34  ? 189 LEU   C CA     1 
ATOM   8209  C  C      . LEU   C 1  189 ? -25.456 -16.437  -3.351  1.00 34.51  ? 189 LEU   C C      1 
ATOM   8210  O  O      . LEU   C 1  189 ? -26.251 -16.994  -2.588  1.00 35.37  ? 189 LEU   C O      1 
ATOM   8211  C  CB     . LEU   C 1  189 ? -25.882 -14.518  -4.913  1.00 28.17  ? 189 LEU   C CB     1 
ATOM   8212  C  CG     . LEU   C 1  189 ? -26.224 -13.043  -5.023  1.00 28.41  ? 189 LEU   C CG     1 
ATOM   8213  C  CD1    . LEU   C 1  189 ? -26.584 -12.717  -6.448  1.00 32.27  ? 189 LEU   C CD1    1 
ATOM   8214  C  CD2    . LEU   C 1  189 ? -27.341 -12.646  -4.070  1.00 25.78  ? 189 LEU   C CD2    1 
ATOM   8215  N  N      . THR   C 1  190 ? -24.532 -17.114  -4.027  1.00 37.56  ? 190 THR   C N      1 
ATOM   8216  C  CA     . THR   C 1  190 ? -24.527 -18.570  -3.988  1.00 37.07  ? 190 THR   C CA     1 
ATOM   8217  C  C      . THR   C 1  190 ? -24.213 -19.079  -2.590  1.00 33.02  ? 190 THR   C C      1 
ATOM   8218  O  O      . THR   C 1  190 ? -24.810 -20.068  -2.144  1.00 36.34  ? 190 THR   C O      1 
ATOM   8219  C  CB     . THR   C 1  190 ? -23.544 -19.126  -5.017  1.00 33.79  ? 190 THR   C CB     1 
ATOM   8220  O  OG1    . THR   C 1  190 ? -23.823 -20.517  -5.225  1.00 36.97  ? 190 THR   C OG1    1 
ATOM   8221  C  CG2    . THR   C 1  190 ? -22.118 -18.952  -4.543  1.00 31.90  ? 190 THR   C CG2    1 
ATOM   8222  N  N      . THR   C 1  191 ? -23.304 -18.412  -1.868  1.00 31.52  ? 191 THR   C N      1 
ATOM   8223  C  CA     . THR   C 1  191 ? -22.973 -18.894  -0.527  1.00 34.69  ? 191 THR   C CA     1 
ATOM   8224  C  C      . THR   C 1  191 ? -24.190 -18.856  0.371   1.00 36.20  ? 191 THR   C C      1 
ATOM   8225  O  O      . THR   C 1  191 ? -24.428 -19.791  1.141   1.00 40.38  ? 191 THR   C O      1 
ATOM   8226  C  CB     . THR   C 1  191 ? -21.832 -18.100  0.106   1.00 30.39  ? 191 THR   C CB     1 
ATOM   8227  O  OG1    . THR   C 1  191 ? -20.591 -18.435  -0.533  1.00 33.88  ? 191 THR   C OG1    1 
ATOM   8228  C  CG2    . THR   C 1  191 ? -21.736 -18.444  1.563   1.00 28.77  ? 191 THR   C CG2    1 
ATOM   8229  N  N      . HIS   C 1  192 ? -24.985 -17.796  0.268   1.00 34.43  ? 192 HIS   C N      1 
ATOM   8230  C  CA     . HIS   C 1  192 ? -26.206 -17.723  1.049   1.00 31.30  ? 192 HIS   C CA     1 
ATOM   8231  C  C      . HIS   C 1  192 ? -27.189 -18.794  0.613   1.00 32.19  ? 192 HIS   C C      1 
ATOM   8232  O  O      . HIS   C 1  192 ? -27.737 -19.527  1.440   1.00 38.52  ? 192 HIS   C O      1 
ATOM   8233  C  CB     . HIS   C 1  192 ? -26.821 -16.346  0.895   1.00 32.17  ? 192 HIS   C CB     1 
ATOM   8234  C  CG     . HIS   C 1  192 ? -28.260 -16.299  1.255   1.00 31.92  ? 192 HIS   C CG     1 
ATOM   8235  N  ND1    . HIS   C 1  192 ? -28.707 -16.622  2.512   1.00 33.13  ? 192 HIS   C ND1    1 
ATOM   8236  C  CD2    . HIS   C 1  192 ? -29.350 -15.925  0.551   1.00 40.60  ? 192 HIS   C CD2    1 
ATOM   8237  C  CE1    . HIS   C 1  192 ? -30.017 -16.477  2.563   1.00 36.65  ? 192 HIS   C CE1    1 
ATOM   8238  N  NE2    . HIS   C 1  192 ? -30.434 -16.055  1.386   1.00 38.99  ? 192 HIS   C NE2    1 
ATOM   8239  N  N      . THR   C 1  193 ? -27.394 -18.922  -0.691  1.00 33.43  ? 193 THR   C N      1 
ATOM   8240  C  CA     . THR   C 1  193 ? -28.381 -19.850  -1.228  1.00 33.52  ? 193 THR   C CA     1 
ATOM   8241  C  C      . THR   C 1  193 ? -28.034 -21.312  -1.008  1.00 34.44  ? 193 THR   C C      1 
ATOM   8242  O  O      . THR   C 1  193 ? -28.924 -22.163  -1.100  1.00 35.49  ? 193 THR   C O      1 
ATOM   8243  C  CB     . THR   C 1  193 ? -28.552 -19.632  -2.725  1.00 32.50  ? 193 THR   C CB     1 
ATOM   8244  O  OG1    . THR   C 1  193 ? -28.812 -18.249  -2.983  1.00 36.83  ? 193 THR   C OG1    1 
ATOM   8245  C  CG2    . THR   C 1  193 ? -29.681 -20.498  -3.247  1.00 36.53  ? 193 THR   C CG2    1 
ATOM   8246  N  N      . THR   C 1  194 ? -26.765 -21.627  -0.787  1.00 35.73  ? 194 THR   C N      1 
ATOM   8247  C  CA     . THR   C 1  194 ? -26.316 -22.999  -0.646  1.00 32.69  ? 194 THR   C CA     1 
ATOM   8248  C  C      . THR   C 1  194 ? -26.155 -23.420  0.795   1.00 32.45  ? 194 THR   C C      1 
ATOM   8249  O  O      . THR   C 1  194 ? -26.341 -24.596  1.112   1.00 26.50  ? 194 THR   C O      1 
ATOM   8250  C  CB     . THR   C 1  194 ? -24.992 -23.158  -1.373  1.00 30.34  ? 194 THR   C CB     1 
ATOM   8251  O  OG1    . THR   C 1  194 ? -25.240 -22.939  -2.762  1.00 29.62  ? 194 THR   C OG1    1 
ATOM   8252  C  CG2    . THR   C 1  194 ? -24.370 -24.533  -1.116  1.00 28.98  ? 194 THR   C CG2    1 
ATOM   8253  N  N      . LEU   C 1  195 ? -25.880 -22.461  1.675   1.00 34.59  ? 195 LEU   C N      1 
ATOM   8254  C  CA     . LEU   C 1  195 ? -25.368 -22.783  2.994   1.00 27.67  ? 195 LEU   C CA     1 
ATOM   8255  C  C      . LEU   C 1  195 ? -26.182 -23.899  3.619   1.00 31.84  ? 195 LEU   C C      1 
ATOM   8256  O  O      . LEU   C 1  195 ? -25.616 -24.885  4.099   1.00 38.11  ? 195 LEU   C O      1 
ATOM   8257  C  CB     . LEU   C 1  195 ? -25.363 -21.524  3.836   1.00 24.56  ? 195 LEU   C CB     1 
ATOM   8258  C  CG     . LEU   C 1  195 ? -24.513 -21.504  5.091   1.00 27.61  ? 195 LEU   C CG     1 
ATOM   8259  C  CD1    . LEU   C 1  195 ? -23.111 -21.977  4.802   1.00 29.79  ? 195 LEU   C CD1    1 
ATOM   8260  C  CD2    . LEU   C 1  195 ? -24.495 -20.071  5.603   1.00 26.67  ? 195 LEU   C CD2    1 
ATOM   8261  N  N      . GLU   C 1  196 ? -27.520 -23.805  3.526   1.00 36.57  ? 196 GLU   C N      1 
ATOM   8262  C  CA     . GLU   C 1  196 ? -28.443 -24.852  3.982   1.00 26.99  ? 196 GLU   C CA     1 
ATOM   8263  C  C      . GLU   C 1  196 ? -28.330 -26.176  3.266   1.00 27.14  ? 196 GLU   C C      1 
ATOM   8264  O  O      . GLU   C 1  196 ? -28.936 -27.133  3.728   1.00 34.12  ? 196 GLU   C O      1 
ATOM   8265  C  CB     . GLU   C 1  196 ? -29.890 -24.433  3.812   1.00 27.81  ? 196 GLU   C CB     1 
ATOM   8266  C  CG     . GLU   C 1  196 ? -30.540 -23.813  4.993   1.00 37.24  ? 196 GLU   C CG     1 
ATOM   8267  C  CD     . GLU   C 1  196 ? -31.976 -23.436  4.696   1.00 55.84  ? 196 GLU   C CD     1 
ATOM   8268  O  OE1    . GLU   C 1  196 ? -32.405 -23.591  3.517   1.00 49.59  ? 196 GLU   C OE1    1 
ATOM   8269  O  OE2    . GLU   C 1  196 ? -32.699 -23.124  5.674   1.00 63.22  ? 196 GLU   C OE2    1 
ATOM   8270  N  N      . HIS   C 1  197 ? -27.674 -26.261  2.120   1.00 29.49  ? 197 HIS   C N      1 
ATOM   8271  C  CA     . HIS   C 1  197 ? -27.769 -27.480  1.326   1.00 28.74  ? 197 HIS   C CA     1 
ATOM   8272  C  C      . HIS   C 1  197 ? -26.439 -28.190  1.195   1.00 33.82  ? 197 HIS   C C      1 
ATOM   8273  O  O      . HIS   C 1  197 ? -26.362 -29.221  0.519   1.00 42.10  ? 197 HIS   C O      1 
ATOM   8274  C  CB     . HIS   C 1  197 ? -28.338 -27.177  -0.064  1.00 29.09  ? 197 HIS   C CB     1 
ATOM   8275  C  CG     . HIS   C 1  197 ? -29.703 -26.578  -0.021  1.00 32.71  ? 197 HIS   C CG     1 
ATOM   8276  N  ND1    . HIS   C 1  197 ? -30.849 -27.339  0.060   1.00 37.60  ? 197 HIS   C ND1    1 
ATOM   8277  C  CD2    . HIS   C 1  197 ? -30.102 -25.290  0.016   1.00 30.47  ? 197 HIS   C CD2    1 
ATOM   8278  C  CE1    . HIS   C 1  197 ? -31.895 -26.542  0.144   1.00 37.00  ? 197 HIS   C CE1    1 
ATOM   8279  N  NE2    . HIS   C 1  197 ? -31.469 -25.293  0.120   1.00 38.64  ? 197 HIS   C NE2    1 
ATOM   8280  N  N      . SER   C 1  198 ? -25.395 -27.670  1.821   1.00 26.67  ? 198 SER   C N      1 
ATOM   8281  C  CA     . SER   C 1  198 ? -24.090 -28.279  1.777   1.00 25.66  ? 198 SER   C CA     1 
ATOM   8282  C  C      . SER   C 1  198 ? -23.752 -28.792  3.162   1.00 31.32  ? 198 SER   C C      1 
ATOM   8283  O  O      . SER   C 1  198 ? -23.924 -28.087  4.158   1.00 36.10  ? 198 SER   C O      1 
ATOM   8284  C  CB     . SER   C 1  198 ? -23.041 -27.298  1.294   1.00 34.77  ? 198 SER   C CB     1 
ATOM   8285  O  OG     . SER   C 1  198 ? -21.924 -28.005  0.766   1.00 38.64  ? 198 SER   C OG     1 
ATOM   8286  N  N      . ASP   C 1  199 ? -23.280 -30.033  3.204   1.00 32.67  ? 199 ASP   C N      1 
ATOM   8287  C  CA     . ASP   C 1  199 ? -22.882 -30.705  4.424   1.00 28.92  ? 199 ASP   C CA     1 
ATOM   8288  C  C      . ASP   C 1  199 ? -21.457 -30.352  4.806   1.00 33.01  ? 199 ASP   C C      1 
ATOM   8289  O  O      . ASP   C 1  199 ? -21.090 -30.395  5.992   1.00 32.44  ? 199 ASP   C O      1 
ATOM   8290  C  CB     . ASP   C 1  199 ? -23.031 -32.202  4.202   1.00 26.96  ? 199 ASP   C CB     1 
ATOM   8291  C  CG     . ASP   C 1  199 ? -24.451 -32.607  4.092   1.00 30.14  ? 199 ASP   C CG     1 
ATOM   8292  O  OD1    . ASP   C 1  199 ? -25.202 -32.373  5.054   1.00 31.10  ? 199 ASP   C OD1    1 
ATOM   8293  O  OD2    . ASP   C 1  199 ? -24.849 -33.076  3.008   1.00 43.45  ? 199 ASP   C OD2    1 
ATOM   8294  N  N      . CYS   C 1  200 ? -20.650 -30.005  3.813   1.00 32.75  ? 200 CYS   C N      1 
ATOM   8295  C  CA     . CYS   C 1  200 ? -19.242 -29.751  4.031   1.00 33.26  ? 200 CYS   C CA     1 
ATOM   8296  C  C      . CYS   C 1  200 ? -18.674 -29.154  2.752   1.00 33.23  ? 200 CYS   C C      1 
ATOM   8297  O  O      . CYS   C 1  200 ? -18.903 -29.702  1.676   1.00 35.17  ? 200 CYS   C O      1 
ATOM   8298  C  CB     . CYS   C 1  200 ? -18.552 -31.056  4.411   1.00 32.41  ? 200 CYS   C CB     1 
ATOM   8299  S  SG     . CYS   C 1  200 ? -16.811 -30.923  4.532   1.00 42.07  ? 200 CYS   C SG     1 
ATOM   8300  N  N      . ALA   C 1  201 ? -17.952 -28.040  2.833   1.00 33.65  ? 201 ALA   C N      1 
ATOM   8301  C  CA     . ALA   C 1  201 ? -17.465 -27.350  1.644   1.00 28.35  ? 201 ALA   C CA     1 
ATOM   8302  C  C      . ALA   C 1  201 ? -15.977 -27.022  1.785   1.00 33.44  ? 201 ALA   C C      1 
ATOM   8303  O  O      . ALA   C 1  201 ? -15.587 -26.206  2.637   1.00 37.33  ? 201 ALA   C O      1 
ATOM   8304  C  CB     . ALA   C 1  201 ? -18.292 -26.092  1.412   1.00 29.83  ? 201 ALA   C CB     1 
ATOM   8305  N  N      . PHE   C 1  202 ? -15.147 -27.656  0.950   1.00 29.12  ? 202 PHE   C N      1 
ATOM   8306  C  CA     . PHE   C 1  202 ? -13.718 -27.355  0.867   1.00 28.36  ? 202 PHE   C CA     1 
ATOM   8307  C  C      . PHE   C 1  202 ? -13.515 -26.212  -0.129  1.00 34.25  ? 202 PHE   C C      1 
ATOM   8308  O  O      . PHE   C 1  202 ? -13.672 -26.408  -1.335  1.00 32.75  ? 202 PHE   C O      1 
ATOM   8309  C  CB     . PHE   C 1  202 ? -12.956 -28.591  0.432   1.00 23.53  ? 202 PHE   C CB     1 
ATOM   8310  C  CG     . PHE   C 1  202 ? -13.121 -29.753  1.347   1.00 28.74  ? 202 PHE   C CG     1 
ATOM   8311  C  CD1    . PHE   C 1  202 ? -12.394 -29.847  2.516   1.00 32.30  ? 202 PHE   C CD1    1 
ATOM   8312  C  CD2    . PHE   C 1  202 ? -14.035 -30.756  1.054   1.00 32.50  ? 202 PHE   C CD2    1 
ATOM   8313  C  CE1    . PHE   C 1  202 ? -12.554 -30.955  3.363   1.00 34.78  ? 202 PHE   C CE1    1 
ATOM   8314  C  CE2    . PHE   C 1  202 ? -14.223 -31.858  1.911   1.00 30.22  ? 202 PHE   C CE2    1 
ATOM   8315  C  CZ     . PHE   C 1  202 ? -13.482 -31.961  3.055   1.00 29.33  ? 202 PHE   C CZ     1 
ATOM   8316  N  N      . MET   C 1  203 ? -13.177 -25.010  0.379   1.00 33.20  ? 203 MET   C N      1 
ATOM   8317  C  CA     . MET   C 1  203 ? -12.921 -23.834  -0.455  1.00 30.55  ? 203 MET   C CA     1 
ATOM   8318  C  C      . MET   C 1  203 ? -11.476 -23.782  -0.929  1.00 31.05  ? 203 MET   C C      1 
ATOM   8319  O  O      . MET   C 1  203 ? -10.555 -23.943  -0.130  1.00 38.37  ? 203 MET   C O      1 
ATOM   8320  C  CB     . MET   C 1  203 ? -13.214 -22.555  0.319   1.00 32.16  ? 203 MET   C CB     1 
ATOM   8321  C  CG     . MET   C 1  203 ? -14.657 -22.329  0.582   1.00 38.87  ? 203 MET   C CG     1 
ATOM   8322  S  SD     . MET   C 1  203 ? -14.981 -20.608  1.052   1.00 44.81  ? 203 MET   C SD     1 
ATOM   8323  C  CE     . MET   C 1  203 ? -14.288 -20.594  2.691   1.00 40.06  ? 203 MET   C CE     1 
ATOM   8324  N  N      . VAL   C 1  204 ? -11.268 -23.519  -2.215  1.00 32.04  ? 204 VAL   C N      1 
ATOM   8325  C  CA     . VAL   C 1  204 ? -9.936  -23.287  -2.768  1.00 32.17  ? 204 VAL   C CA     1 
ATOM   8326  C  C      . VAL   C 1  204 ? -9.826  -21.834  -3.200  1.00 34.60  ? 204 VAL   C C      1 
ATOM   8327  O  O      . VAL   C 1  204 ? -10.665 -21.337  -3.961  1.00 34.52  ? 204 VAL   C O      1 
ATOM   8328  C  CB     . VAL   C 1  204 ? -9.642  -24.224  -3.943  1.00 31.19  ? 204 VAL   C CB     1 
ATOM   8329  C  CG1    . VAL   C 1  204 ? -8.223  -24.095  -4.358  1.00 32.22  ? 204 VAL   C CG1    1 
ATOM   8330  C  CG2    . VAL   C 1  204 ? -9.915  -25.631  -3.525  1.00 33.75  ? 204 VAL   C CG2    1 
ATOM   8331  N  N      . ASP   C 1  205 ? -8.796  -21.159  -2.715  1.00 30.35  ? 205 ASP   C N      1 
ATOM   8332  C  CA     . ASP   C 1  205 ? -8.595  -19.739  -2.957  1.00 31.37  ? 205 ASP   C CA     1 
ATOM   8333  C  C      . ASP   C 1  205 ? -7.609  -19.582  -4.103  1.00 39.53  ? 205 ASP   C C      1 
ATOM   8334  O  O      . ASP   C 1  205 ? -6.407  -19.806  -3.928  1.00 39.20  ? 205 ASP   C O      1 
ATOM   8335  C  CB     . ASP   C 1  205 ? -8.079  -19.051  -1.700  1.00 33.55  ? 205 ASP   C CB     1 
ATOM   8336  C  CG     . ASP   C 1  205 ? -7.701  -17.612  -1.932  1.00 37.02  ? 205 ASP   C CG     1 
ATOM   8337  O  OD1    . ASP   C 1  205 ? -7.819  -17.115  -3.072  1.00 38.25  ? 205 ASP   C OD1    1 
ATOM   8338  O  OD2    . ASP   C 1  205 ? -7.309  -16.954  -0.945  1.00 39.65  ? 205 ASP   C OD2    1 
ATOM   8339  N  N      . ASN   C 1  206 ? -8.110  -19.164  -5.268  1.00 35.56  ? 206 ASN   C N      1 
ATOM   8340  C  CA     . ASN   C 1  206 ? -7.253  -19.105  -6.440  1.00 35.06  ? 206 ASN   C CA     1 
ATOM   8341  C  C      . ASN   C 1  206 ? -5.946  -18.370  -6.169  1.00 38.33  ? 206 ASN   C C      1 
ATOM   8342  O  O      . ASN   C 1  206 ? -4.918  -18.688  -6.780  1.00 42.13  ? 206 ASN   C O      1 
ATOM   8343  C  CB     . ASN   C 1  206 ? -7.995  -18.460  -7.592  1.00 34.10  ? 206 ASN   C CB     1 
ATOM   8344  C  CG     . ASN   C 1  206 ? -8.529  -19.466  -8.529  1.00 34.51  ? 206 ASN   C CG     1 
ATOM   8345  O  OD1    . ASN   C 1  206 ? -8.208  -20.641  -8.426  1.00 38.17  ? 206 ASN   C OD1    1 
ATOM   8346  N  ND2    . ASN   C 1  206 ? -9.379  -19.039  -9.425  1.00 30.94  ? 206 ASN   C ND2    1 
ATOM   8347  N  N      . GLU   C 1  207 ? -5.942  -17.403  -5.255  1.00 35.84  ? 207 GLU   C N      1 
ATOM   8348  C  CA     . GLU   C 1  207 ? -4.683  -16.706  -5.017  1.00 42.05  ? 207 GLU   C CA     1 
ATOM   8349  C  C      . GLU   C 1  207 ? -3.707  -17.576  -4.238  1.00 41.00  ? 207 GLU   C C      1 
ATOM   8350  O  O      . GLU   C 1  207 ? -2.516  -17.603  -4.558  1.00 39.22  ? 207 GLU   C O      1 
ATOM   8351  C  CB     . GLU   C 1  207 ? -4.926  -15.381  -4.305  1.00 40.06  ? 207 GLU   C CB     1 
ATOM   8352  C  CG     . GLU   C 1  207 ? -3.798  -14.429  -4.471  1.00 40.16  ? 207 GLU   C CG     1 
ATOM   8353  C  CD     . GLU   C 1  207 ? -3.908  -13.283  -3.543  1.00 49.22  ? 207 GLU   C CD     1 
ATOM   8354  O  OE1    . GLU   C 1  207 ? -4.978  -12.662  -3.573  1.00 57.55  ? 207 GLU   C OE1    1 
ATOM   8355  O  OE2    . GLU   C 1  207 ? -2.944  -12.961  -2.830  1.00 57.54  ? 207 GLU   C OE2    1 
ATOM   8356  N  N      . ALA   C 1  208 ? -4.188  -18.305  -3.231  1.00 37.38  ? 208 ALA   C N      1 
ATOM   8357  C  CA     . ALA   C 1  208 ? -3.336  -19.275  -2.553  1.00 36.62  ? 208 ALA   C CA     1 
ATOM   8358  C  C      . ALA   C 1  208 ? -2.700  -20.225  -3.561  1.00 35.26  ? 208 ALA   C C      1 
ATOM   8359  O  O      . ALA   C 1  208 ? -1.477  -20.357  -3.641  1.00 36.16  ? 208 ALA   C O      1 
ATOM   8360  C  CB     . ALA   C 1  208 ? -4.151  -20.044  -1.507  1.00 31.38  ? 208 ALA   C CB     1 
ATOM   8361  N  N      . ILE   C 1  209 ? -3.533  -20.883  -4.356  1.00 37.82  ? 209 ILE   C N      1 
ATOM   8362  C  CA     . ILE   C 1  209 ? -3.052  -21.820  -5.365  1.00 39.71  ? 209 ILE   C CA     1 
ATOM   8363  C  C      . ILE   C 1  209 ? -2.087  -21.122  -6.328  1.00 39.72  ? 209 ILE   C C      1 
ATOM   8364  O  O      . ILE   C 1  209 ? -1.011  -21.641  -6.643  1.00 37.10  ? 209 ILE   C O      1 
ATOM   8365  C  CB     . ILE   C 1  209 ? -4.262  -22.444  -6.086  1.00 35.95  ? 209 ILE   C CB     1 
ATOM   8366  C  CG1    . ILE   C 1  209 ? -5.177  -23.049  -5.040  1.00 38.87  ? 209 ILE   C CG1    1 
ATOM   8367  C  CG2    . ILE   C 1  209 ? -3.865  -23.562  -6.999  1.00 38.84  ? 209 ILE   C CG2    1 
ATOM   8368  C  CD1    . ILE   C 1  209 ? -4.516  -24.089  -4.157  1.00 38.61  ? 209 ILE   C CD1    1 
ATOM   8369  N  N      . TYR   C 1  210 ? -2.459  -19.933  -6.810  1.00 38.09  ? 210 TYR   C N      1 
ATOM   8370  C  CA     . TYR   C 1  210 ? -1.573  -19.162  -7.677  1.00 38.45  ? 210 TYR   C CA     1 
ATOM   8371  C  C      . TYR   C 1  210 ? -0.236  -18.884  -7.011  1.00 41.97  ? 210 TYR   C C      1 
ATOM   8372  O  O      . TYR   C 1  210 ? 0.823   -19.076  -7.612  1.00 44.12  ? 210 TYR   C O      1 
ATOM   8373  C  CB     . TYR   C 1  210 ? -2.235  -17.857  -8.044  1.00 39.25  ? 210 TYR   C CB     1 
ATOM   8374  C  CG     . TYR   C 1  210 ? -1.575  -17.108  -9.156  1.00 42.30  ? 210 TYR   C CG     1 
ATOM   8375  C  CD1    . TYR   C 1  210 ? -1.954  -17.329  -10.467 1.00 42.46  ? 210 TYR   C CD1    1 
ATOM   8376  C  CD2    . TYR   C 1  210 ? -0.645  -16.103  -8.894  1.00 45.27  ? 210 TYR   C CD2    1 
ATOM   8377  C  CE1    . TYR   C 1  210 ? -1.390  -16.620  -11.497 1.00 50.23  ? 210 TYR   C CE1    1 
ATOM   8378  C  CE2    . TYR   C 1  210 ? -0.068  -15.374  -9.932  1.00 49.18  ? 210 TYR   C CE2    1 
ATOM   8379  C  CZ     . TYR   C 1  210 ? -0.450  -15.644  -11.233 1.00 51.73  ? 210 TYR   C CZ     1 
ATOM   8380  O  OH     . TYR   C 1  210 ? 0.079   -14.958  -12.299 1.00 59.63  ? 210 TYR   C OH     1 
ATOM   8381  N  N      . ASP   C 1  211 ? -0.264  -18.396  -5.774  1.00 42.77  ? 211 ASP   C N      1 
ATOM   8382  C  CA     . ASP   C 1  211 ? 0.977   -18.129  -5.060  1.00 40.57  ? 211 ASP   C CA     1 
ATOM   8383  C  C      . ASP   C 1  211 ? 1.812   -19.394  -4.936  1.00 40.64  ? 211 ASP   C C      1 
ATOM   8384  O  O      . ASP   C 1  211 ? 2.973   -19.412  -5.343  1.00 50.13  ? 211 ASP   C O      1 
ATOM   8385  C  CB     . ASP   C 1  211 ? 0.665   -17.545  -3.687  1.00 50.78  ? 211 ASP   C CB     1 
ATOM   8386  C  CG     . ASP   C 1  211 ? 0.254   -16.082  -3.753  1.00 52.09  ? 211 ASP   C CG     1 
ATOM   8387  O  OD1    . ASP   C 1  211 ? 0.476   -15.445  -4.822  1.00 49.05  ? 211 ASP   C OD1    1 
ATOM   8388  O  OD2    . ASP   C 1  211 ? -0.326  -15.597  -2.742  1.00 45.88  ? 211 ASP   C OD2    1 
ATOM   8389  N  N      . ILE   C 1  212 ? 1.232   -20.471  -4.399  1.00 37.96  ? 212 ILE   C N      1 
ATOM   8390  C  CA     . ILE   C 1  212 ? 1.950   -21.749  -4.287  1.00 41.70  ? 212 ILE   C CA     1 
ATOM   8391  C  C      . ILE   C 1  212 ? 2.655   -22.119  -5.593  1.00 40.15  ? 212 ILE   C C      1 
ATOM   8392  O  O      . ILE   C 1  212 ? 3.826   -22.511  -5.594  1.00 39.22  ? 212 ILE   C O      1 
ATOM   8393  C  CB     . ILE   C 1  212 ? 0.995   -22.873  -3.836  1.00 37.75  ? 212 ILE   C CB     1 
ATOM   8394  C  CG1    . ILE   C 1  212 ? 0.510   -22.636  -2.412  1.00 32.29  ? 212 ILE   C CG1    1 
ATOM   8395  C  CG2    . ILE   C 1  212 ? 1.644   -24.241  -3.994  1.00 32.89  ? 212 ILE   C CG2    1 
ATOM   8396  C  CD1    . ILE   C 1  212 ? -0.615  -23.524  -2.054  1.00 28.01  ? 212 ILE   C CD1    1 
ATOM   8397  N  N      . CYS   C 1  213 ? 1.958   -22.018  -6.725  1.00 37.79  ? 213 CYS   C N      1 
ATOM   8398  C  CA     . CYS   C 1  213 ? 2.579   -22.407  -7.991  1.00 42.27  ? 213 CYS   C CA     1 
ATOM   8399  C  C      . CYS   C 1  213 ? 3.788   -21.537  -8.296  1.00 49.27  ? 213 CYS   C C      1 
ATOM   8400  O  O      . CYS   C 1  213 ? 4.875   -22.041  -8.607  1.00 52.79  ? 213 CYS   C O      1 
ATOM   8401  C  CB     . CYS   C 1  213 ? 1.573   -22.314  -9.128  1.00 38.23  ? 213 CYS   C CB     1 
ATOM   8402  S  SG     . CYS   C 1  213 ? 0.457   -23.695  -9.192  1.00 55.03  ? 213 CYS   C SG     1 
ATOM   8403  N  N      . ARG   C 1  214 ? 3.604   -20.216  -8.239  1.00 43.71  ? 214 ARG   C N      1 
ATOM   8404  C  CA     . ARG   C 1  214 ? 4.718   -19.299  -8.411  1.00 43.27  ? 214 ARG   C CA     1 
ATOM   8405  C  C      . ARG   C 1  214 ? 5.869   -19.664  -7.483  1.00 44.68  ? 214 ARG   C C      1 
ATOM   8406  O  O      . ARG   C 1  214 ? 7.007   -19.837  -7.920  1.00 46.75  ? 214 ARG   C O      1 
ATOM   8407  C  CB     . ARG   C 1  214 ? 4.229   -17.865  -8.169  1.00 43.99  ? 214 ARG   C CB     1 
ATOM   8408  C  CG     . ARG   C 1  214 ? 3.537   -17.237  -9.382  1.00 49.19  ? 214 ARG   C CG     1 
ATOM   8409  C  CD     . ARG   C 1  214 ? 3.666   -15.722  -9.410  1.00 53.38  ? 214 ARG   C CD     1 
ATOM   8410  N  NE     . ARG   C 1  214 ? 3.033   -15.134  -8.238  1.00 61.59  ? 214 ARG   C NE     1 
ATOM   8411  C  CZ     . ARG   C 1  214 ? 2.778   -13.841  -8.089  1.00 70.41  ? 214 ARG   C CZ     1 
ATOM   8412  N  NH1    . ARG   C 1  214 ? 3.144   -12.953  -9.002  1.00 74.49  ? 214 ARG   C NH1    1 
ATOM   8413  N  NH2    . ARG   C 1  214 ? 2.115   -13.433  -7.011  1.00 64.44  ? 214 ARG   C NH2    1 
ATOM   8414  N  N      . ARG   C 1  215 ? 5.576   -19.817  -6.195  1.00 43.91  ? 215 ARG   C N      1 
ATOM   8415  C  CA     . ARG   C 1  215 ? 6.624   -19.949  -5.187  1.00 44.46  ? 215 ARG   C CA     1 
ATOM   8416  C  C      . ARG   C 1  215 ? 7.322   -21.305  -5.220  1.00 50.03  ? 215 ARG   C C      1 
ATOM   8417  O  O      . ARG   C 1  215 ? 8.535   -21.369  -5.006  1.00 51.04  ? 215 ARG   C O      1 
ATOM   8418  C  CB     . ARG   C 1  215 ? 6.042   -19.699  -3.801  1.00 42.66  ? 215 ARG   C CB     1 
ATOM   8419  C  CG     . ARG   C 1  215 ? 7.027   -19.240  -2.773  1.00 49.46  ? 215 ARG   C CG     1 
ATOM   8420  C  CD     . ARG   C 1  215 ? 6.412   -19.208  -1.356  1.00 59.81  ? 215 ARG   C CD     1 
ATOM   8421  N  NE     . ARG   C 1  215 ? 5.183   -18.418  -1.268  1.00 70.28  ? 215 ARG   C NE     1 
ATOM   8422  C  CZ     . ARG   C 1  215 ? 3.957   -18.897  -1.058  1.00 59.05  ? 215 ARG   C CZ     1 
ATOM   8423  N  NH1    . ARG   C 1  215 ? 3.728   -20.199  -0.918  1.00 49.90  ? 215 ARG   C NH1    1 
ATOM   8424  N  NH2    . ARG   C 1  215 ? 2.938   -18.043  -0.960  1.00 52.22  ? 215 ARG   C NH2    1 
ATOM   8425  N  N      . ASN   C 1  216 ? 6.589   -22.406  -5.416  1.00 47.98  ? 216 ASN   C N      1 
ATOM   8426  C  CA     . ASN   C 1  216 ? 7.204   -23.707  -5.177  1.00 42.20  ? 216 ASN   C CA     1 
ATOM   8427  C  C      . ASN   C 1  216 ? 7.482   -24.458  -6.464  1.00 46.89  ? 216 ASN   C C      1 
ATOM   8428  O  O      . ASN   C 1  216 ? 8.117   -25.520  -6.430  1.00 53.80  ? 216 ASN   C O      1 
ATOM   8429  C  CB     . ASN   C 1  216 ? 6.330   -24.615  -4.295  1.00 38.08  ? 216 ASN   C CB     1 
ATOM   8430  C  CG     . ASN   C 1  216 ? 5.966   -24.005  -2.956  1.00 39.00  ? 216 ASN   C CG     1 
ATOM   8431  O  OD1    . ASN   C 1  216 ? 6.161   -22.818  -2.691  1.00 46.13  ? 216 ASN   C OD1    1 
ATOM   8432  N  ND2    . ASN   C 1  216 ? 5.489   -24.848  -2.076  1.00 41.16  ? 216 ASN   C ND2    1 
ATOM   8433  N  N      . LEU   C 1  217 ? 7.021   -23.945  -7.593  1.00 42.09  ? 217 LEU   C N      1 
ATOM   8434  C  CA     . LEU   C 1  217 ? 7.194   -24.638  -8.857  1.00 47.27  ? 217 LEU   C CA     1 
ATOM   8435  C  C      . LEU   C 1  217 ? 7.851   -23.717  -9.881  1.00 54.03  ? 217 LEU   C C      1 
ATOM   8436  O  O      . LEU   C 1  217 ? 7.786   -23.988  -11.082 1.00 60.33  ? 217 LEU   C O      1 
ATOM   8437  C  CB     . LEU   C 1  217 ? 5.830   -25.144  -9.339  1.00 52.08  ? 217 LEU   C CB     1 
ATOM   8438  C  CG     . LEU   C 1  217 ? 5.092   -26.199  -8.492  1.00 45.29  ? 217 LEU   C CG     1 
ATOM   8439  C  CD1    . LEU   C 1  217 ? 3.747   -26.523  -9.081  1.00 45.56  ? 217 LEU   C CD1    1 
ATOM   8440  C  CD2    . LEU   C 1  217 ? 5.880   -27.471  -8.369  1.00 47.40  ? 217 LEU   C CD2    1 
ATOM   8441  N  N      . ASP   C 1  218 ? 8.581   -22.700  -9.409  1.00 53.88  ? 218 ASP   C N      1 
ATOM   8442  C  CA     . ASP   C 1  218 ? 8.436   -21.347  -9.939  1.00 60.05  ? 218 ASP   C CA     1 
ATOM   8443  C  C      . ASP   C 1  218 ? 7.820   -21.351  -11.334 1.00 56.77  ? 218 ASP   C C      1 
ATOM   8444  O  O      . ASP   C 1  218 ? 8.514   -21.527  -12.335 1.00 61.32  ? 218 ASP   C O      1 
ATOM   8445  C  CB     . ASP   C 1  218 ? 9.759   -20.541  -9.883  1.00 70.15  ? 218 ASP   C CB     1 
ATOM   8446  C  CG     . ASP   C 1  218 ? 10.806  -21.005  -10.877 1.00 81.86  ? 218 ASP   C CG     1 
ATOM   8447  O  OD1    . ASP   C 1  218 ? 10.683  -22.140  -11.379 1.00 80.89  ? 218 ASP   C OD1    1 
ATOM   8448  O  OD2    . ASP   C 1  218 ? 11.725  -20.198  -11.194 1.00 87.27  ? 218 ASP   C OD2    1 
ATOM   8449  N  N      . ILE   C 1  219 ? 6.499   -21.193  -11.387 1.00 52.00  ? 219 ILE   C N      1 
ATOM   8450  C  CA     . ILE   C 1  219 ? 5.770   -20.876  -12.608 1.00 50.10  ? 219 ILE   C CA     1 
ATOM   8451  C  C      . ILE   C 1  219 ? 5.532   -19.372  -12.614 1.00 56.37  ? 219 ILE   C C      1 
ATOM   8452  O  O      . ILE   C 1  219 ? 4.762   -18.864  -11.795 1.00 55.50  ? 219 ILE   C O      1 
ATOM   8453  C  CB     . ILE   C 1  219 ? 4.446   -21.644  -12.691 1.00 48.65  ? 219 ILE   C CB     1 
ATOM   8454  C  CG1    . ILE   C 1  219 ? 4.712   -23.137  -12.895 1.00 53.29  ? 219 ILE   C CG1    1 
ATOM   8455  C  CG2    . ILE   C 1  219 ? 3.539   -21.061  -13.771 1.00 45.44  ? 219 ILE   C CG2    1 
ATOM   8456  C  CD1    . ILE   C 1  219 ? 3.754   -24.067  -12.186 1.00 53.52  ? 219 ILE   C CD1    1 
ATOM   8457  N  N      . GLU   C 1  220 ? 6.183   -18.652  -13.537 1.00 58.89  ? 220 GLU   C N      1 
ATOM   8458  C  CA     . GLU   C 1  220 ? 6.089   -17.192  -13.542 1.00 54.85  ? 220 GLU   C CA     1 
ATOM   8459  C  C      . GLU   C 1  220 ? 4.643   -16.726  -13.514 1.00 51.65  ? 220 GLU   C C      1 
ATOM   8460  O  O      . GLU   C 1  220 ? 4.238   -15.957  -12.638 1.00 57.71  ? 220 GLU   C O      1 
ATOM   8461  C  CB     . GLU   C 1  220 ? 6.788   -16.622  -14.770 1.00 68.00  ? 220 GLU   C CB     1 
ATOM   8462  C  CG     . GLU   C 1  220 ? 8.273   -16.822  -14.808 1.00 83.54  ? 220 GLU   C CG     1 
ATOM   8463  C  CD     . GLU   C 1  220 ? 8.966   -15.644  -15.447 1.00 93.81  ? 220 GLU   C CD     1 
ATOM   8464  O  OE1    . GLU   C 1  220 ? 8.454   -15.157  -16.480 1.00 91.35  ? 220 GLU   C OE1    1 
ATOM   8465  O  OE2    . GLU   C 1  220 ? 10.013  -15.203  -14.916 1.00 103.44 ? 220 GLU   C OE2    1 
ATOM   8466  N  N      . ARG   C 1  221 ? 3.853   -17.166  -14.481 1.00 53.65  ? 221 ARG   C N      1 
ATOM   8467  C  CA     . ARG   C 1  221 ? 2.443   -16.798  -14.583 1.00 54.56  ? 221 ARG   C CA     1 
ATOM   8468  C  C      . ARG   C 1  221 ? 1.652   -18.081  -14.730 1.00 51.35  ? 221 ARG   C C      1 
ATOM   8469  O  O      . ARG   C 1  221 ? 1.283   -18.481  -15.842 1.00 52.77  ? 221 ARG   C O      1 
ATOM   8470  C  CB     . ARG   C 1  221 ? 2.206   -15.833  -15.740 1.00 54.36  ? 221 ARG   C CB     1 
ATOM   8471  C  CG     . ARG   C 1  221 ? 0.812   -15.280  -15.863 1.00 51.74  ? 221 ARG   C CG     1 
ATOM   8472  C  CD     . ARG   C 1  221 ? 0.919   -14.196  -16.919 1.00 76.64  ? 221 ARG   C CD     1 
ATOM   8473  N  NE     . ARG   C 1  221 ? 0.246   -14.511  -18.174 1.00 83.29  ? 221 ARG   C NE     1 
ATOM   8474  C  CZ     . ARG   C 1  221 ? -0.778  -13.835  -18.673 1.00 79.31  ? 221 ARG   C CZ     1 
ATOM   8475  N  NH1    . ARG   C 1  221 ? -1.299  -12.799  -18.035 1.00 78.82  ? 221 ARG   C NH1    1 
ATOM   8476  N  NH2    . ARG   C 1  221 ? -1.266  -14.185  -19.859 1.00 75.82  ? 221 ARG   C NH2    1 
ATOM   8477  N  N      . PRO   C 1  222 ? 1.368   -18.748  -13.618 1.00 52.35  ? 222 PRO   C N      1 
ATOM   8478  C  CA     . PRO   C 1  222 ? 0.729   -20.067  -13.686 1.00 49.16  ? 222 PRO   C CA     1 
ATOM   8479  C  C      . PRO   C 1  222 ? -0.574  -19.970  -14.448 1.00 42.68  ? 222 PRO   C C      1 
ATOM   8480  O  O      . PRO   C 1  222 ? -1.254  -18.948  -14.407 1.00 43.15  ? 222 PRO   C O      1 
ATOM   8481  C  CB     . PRO   C 1  222 ? 0.491   -20.425  -12.214 1.00 47.88  ? 222 PRO   C CB     1 
ATOM   8482  C  CG     . PRO   C 1  222 ? 1.440   -19.533  -11.435 1.00 47.61  ? 222 PRO   C CG     1 
ATOM   8483  C  CD     . PRO   C 1  222 ? 1.529   -18.263  -12.237 1.00 49.87  ? 222 PRO   C CD     1 
ATOM   8484  N  N      . THR   C 1  223 ? -0.911  -21.034  -15.159 1.00 43.13  ? 223 THR   C N      1 
ATOM   8485  C  CA     . THR   C 1  223 ? -2.162  -21.071  -15.899 1.00 43.26  ? 223 THR   C CA     1 
ATOM   8486  C  C      . THR   C 1  223 ? -3.239  -21.795  -15.105 1.00 43.09  ? 223 THR   C C      1 
ATOM   8487  O  O      . THR   C 1  223 ? -2.997  -22.334  -14.019 1.00 41.49  ? 223 THR   C O      1 
ATOM   8488  C  CB     . THR   C 1  223 ? -1.976  -21.760  -17.238 1.00 44.13  ? 223 THR   C CB     1 
ATOM   8489  O  OG1    . THR   C 1  223 ? -1.441  -23.073  -17.022 1.00 45.27  ? 223 THR   C OG1    1 
ATOM   8490  C  CG2    . THR   C 1  223 ? -1.047  -20.951  -18.095 1.00 45.80  ? 223 THR   C CG2    1 
ATOM   8491  N  N      . TYR   C 1  224 ? -4.454  -21.804  -15.665 1.00 43.93  ? 224 TYR   C N      1 
ATOM   8492  C  CA     . TYR   C 1  224 ? -5.501  -22.634  -15.082 1.00 37.80  ? 224 TYR   C CA     1 
ATOM   8493  C  C      . TYR   C 1  224 ? -5.093  -24.096  -15.110 1.00 41.81  ? 224 TYR   C C      1 
ATOM   8494  O  O      . TYR   C 1  224 ? -5.450  -24.871  -14.214 1.00 37.19  ? 224 TYR   C O      1 
ATOM   8495  C  CB     . TYR   C 1  224 ? -6.793  -22.478  -15.848 1.00 32.32  ? 224 TYR   C CB     1 
ATOM   8496  C  CG     . TYR   C 1  224 ? -7.505  -21.184  -15.644 1.00 34.20  ? 224 TYR   C CG     1 
ATOM   8497  C  CD1    . TYR   C 1  224 ? -7.466  -20.517  -14.439 1.00 31.14  ? 224 TYR   C CD1    1 
ATOM   8498  C  CD2    . TYR   C 1  224 ? -8.288  -20.663  -16.663 1.00 38.26  ? 224 TYR   C CD2    1 
ATOM   8499  C  CE1    . TYR   C 1  224 ? -8.167  -19.335  -14.275 1.00 38.75  ? 224 TYR   C CE1    1 
ATOM   8500  C  CE2    . TYR   C 1  224 ? -8.984  -19.505  -16.512 1.00 37.35  ? 224 TYR   C CE2    1 
ATOM   8501  C  CZ     . TYR   C 1  224 ? -8.926  -18.842  -15.330 1.00 40.23  ? 224 TYR   C CZ     1 
ATOM   8502  O  OH     . TYR   C 1  224 ? -9.636  -17.671  -15.237 1.00 50.55  ? 224 TYR   C OH     1 
ATOM   8503  N  N      . THR   C 1  225 ? -4.345  -24.490  -16.139 1.00 44.96  ? 225 THR   C N      1 
ATOM   8504  C  CA     . THR   C 1  225 ? -3.858  -25.855  -16.185 1.00 41.54  ? 225 THR   C CA     1 
ATOM   8505  C  C      . THR   C 1  225 ? -2.884  -26.107  -15.060 1.00 43.07  ? 225 THR   C C      1 
ATOM   8506  O  O      . THR   C 1  225 ? -2.837  -27.213  -14.516 1.00 48.95  ? 225 THR   C O      1 
ATOM   8507  C  CB     . THR   C 1  225 ? -3.191  -26.136  -17.514 1.00 47.38  ? 225 THR   C CB     1 
ATOM   8508  O  OG1    . THR   C 1  225 ? -4.028  -25.651  -18.578 1.00 51.88  ? 225 THR   C OG1    1 
ATOM   8509  C  CG2    . THR   C 1  225 ? -2.977  -27.639  -17.641 1.00 44.05  ? 225 THR   C CG2    1 
ATOM   8510  N  N      . ASN   C 1  226 ? -2.092  -25.090  -14.700 1.00 41.40  ? 226 ASN   C N      1 
ATOM   8511  C  CA     . ASN   C 1  226 ? -1.158  -25.226  -13.584 1.00 43.05  ? 226 ASN   C CA     1 
ATOM   8512  C  C      . ASN   C 1  226 ? -1.897  -25.425  -12.271 1.00 43.06  ? 226 ASN   C C      1 
ATOM   8513  O  O      . ASN   C 1  226 ? -1.574  -26.335  -11.497 1.00 39.44  ? 226 ASN   C O      1 
ATOM   8514  C  CB     . ASN   C 1  226 ? -0.258  -23.994  -13.482 1.00 45.91  ? 226 ASN   C CB     1 
ATOM   8515  C  CG     . ASN   C 1  226 ? 0.803   -23.955  -14.546 1.00 46.66  ? 226 ASN   C CG     1 
ATOM   8516  O  OD1    . ASN   C 1  226 ? 0.987   -22.939  -15.218 1.00 45.57  ? 226 ASN   C OD1    1 
ATOM   8517  N  ND2    . ASN   C 1  226 ? 1.494   -25.071  -14.725 1.00 42.66  ? 226 ASN   C ND2    1 
ATOM   8518  N  N      . LEU   C 1  227 ? -2.885  -24.558  -11.997 1.00 44.25  ? 227 LEU   C N      1 
ATOM   8519  C  CA     . LEU   C 1  227 ? -3.603  -24.601  -10.723 1.00 39.69  ? 227 LEU   C CA     1 
ATOM   8520  C  C      . LEU   C 1  227 ? -4.445  -25.848  -10.614 1.00 40.86  ? 227 LEU   C C      1 
ATOM   8521  O  O      . LEU   C 1  227 ? -4.532  -26.455  -9.539  1.00 39.37  ? 227 LEU   C O      1 
ATOM   8522  C  CB     . LEU   C 1  227 ? -4.513  -23.394  -10.566 1.00 35.35  ? 227 LEU   C CB     1 
ATOM   8523  C  CG     . LEU   C 1  227 ? -3.960  -22.031  -10.917 1.00 39.99  ? 227 LEU   C CG     1 
ATOM   8524  C  CD1    . LEU   C 1  227 ? -5.109  -21.068  -10.945 1.00 41.22  ? 227 LEU   C CD1    1 
ATOM   8525  C  CD2    . LEU   C 1  227 ? -2.918  -21.620  -9.910  1.00 38.54  ? 227 LEU   C CD2    1 
ATOM   8526  N  N      . ASN   C 1  228 ? -5.106  -26.219  -11.711 1.00 41.62  ? 228 ASN   C N      1 
ATOM   8527  C  CA     . ASN   C 1  228 ? -5.958  -27.394  -11.680 1.00 40.49  ? 228 ASN   C CA     1 
ATOM   8528  C  C      . ASN   C 1  228 ? -5.154  -28.646  -11.379 1.00 43.80  ? 228 ASN   C C      1 
ATOM   8529  O  O      . ASN   C 1  228 ? -5.639  -29.556  -10.691 1.00 43.29  ? 228 ASN   C O      1 
ATOM   8530  C  CB     . ASN   C 1  228 ? -6.702  -27.508  -12.999 1.00 40.48  ? 228 ASN   C CB     1 
ATOM   8531  C  CG     . ASN   C 1  228 ? -7.774  -26.468  -13.130 1.00 40.22  ? 228 ASN   C CG     1 
ATOM   8532  O  OD1    . ASN   C 1  228 ? -8.129  -25.832  -12.145 1.00 42.77  ? 228 ASN   C OD1    1 
ATOM   8533  N  ND2    . ASN   C 1  228 ? -8.288  -26.267  -14.343 1.00 38.95  ? 228 ASN   C ND2    1 
ATOM   8534  N  N      . ARG   C 1  229 ? -3.913  -28.701  -11.842 1.00 43.85  ? 229 ARG   C N      1 
ATOM   8535  C  CA     . ARG   C 1  229 ? -3.151  -29.902  -11.562 1.00 43.76  ? 229 ARG   C CA     1 
ATOM   8536  C  C      . ARG   C 1  229 ? -2.744  -29.955  -10.103 1.00 42.20  ? 229 ARG   C C      1 
ATOM   8537  O  O      . ARG   C 1  229 ? -2.490  -31.040  -9.583  1.00 50.29  ? 229 ARG   C O      1 
ATOM   8538  C  CB     . ARG   C 1  229 ? -1.942  -29.977  -12.482 1.00 45.39  ? 229 ARG   C CB     1 
ATOM   8539  C  CG     . ARG   C 1  229 ? -2.257  -30.321  -13.945 1.00 43.55  ? 229 ARG   C CG     1 
ATOM   8540  C  CD     . ARG   C 1  229 ? -1.051  -30.976  -14.523 1.00 54.92  ? 229 ARG   C CD     1 
ATOM   8541  N  NE     . ARG   C 1  229 ? -1.162  -31.352  -15.921 1.00 64.89  ? 229 ARG   C NE     1 
ATOM   8542  C  CZ     . ARG   C 1  229 ? -0.426  -30.794  -16.872 1.00 77.91  ? 229 ARG   C CZ     1 
ATOM   8543  N  NH1    . ARG   C 1  229 ? 0.455   -29.840  -16.593 1.00 78.39  ? 229 ARG   C NH1    1 
ATOM   8544  N  NH2    . ARG   C 1  229 ? -0.566  -31.209  -18.130 1.00 82.68  ? 229 ARG   C NH2    1 
ATOM   8545  N  N      . LEU   C 1  230 ? -2.706  -28.819  -9.422  1.00 42.80  ? 230 LEU   C N      1 
ATOM   8546  C  CA     . LEU   C 1  230 ? -2.466  -28.817  -7.985  1.00 43.69  ? 230 LEU   C CA     1 
ATOM   8547  C  C      . LEU   C 1  230 ? -3.748  -29.021  -7.199  1.00 44.92  ? 230 LEU   C C      1 
ATOM   8548  O  O      . LEU   C 1  230 ? -3.757  -29.762  -6.209  1.00 41.27  ? 230 LEU   C O      1 
ATOM   8549  C  CB     . LEU   C 1  230 ? -1.790  -27.509  -7.562  1.00 42.69  ? 230 LEU   C CB     1 
ATOM   8550  C  CG     . LEU   C 1  230 ? -1.571  -27.212  -6.076  1.00 42.51  ? 230 LEU   C CG     1 
ATOM   8551  C  CD1    . LEU   C 1  230 ? -1.078  -28.417  -5.256  1.00 35.19  ? 230 LEU   C CD1    1 
ATOM   8552  C  CD2    . LEU   C 1  230 ? -0.569  -26.091  -6.002  1.00 38.09  ? 230 LEU   C CD2    1 
ATOM   8553  N  N      . ILE   C 1  231 ? -4.834  -28.377  -7.630  1.00 43.13  ? 231 ILE   C N      1 
ATOM   8554  C  CA     . ILE   C 1  231 ? -6.104  -28.568  -6.949  1.00 38.11  ? 231 ILE   C CA     1 
ATOM   8555  C  C      . ILE   C 1  231 ? -6.441  -30.041  -6.933  1.00 42.71  ? 231 ILE   C C      1 
ATOM   8556  O  O      . ILE   C 1  231 ? -7.012  -30.560  -5.965  1.00 45.09  ? 231 ILE   C O      1 
ATOM   8557  C  CB     . ILE   C 1  231 ? -7.210  -27.765  -7.643  1.00 36.39  ? 231 ILE   C CB     1 
ATOM   8558  C  CG1    . ILE   C 1  231 ? -6.892  -26.301  -7.607  1.00 35.86  ? 231 ILE   C CG1    1 
ATOM   8559  C  CG2    . ILE   C 1  231 ? -8.543  -27.925  -6.926  1.00 30.85  ? 231 ILE   C CG2    1 
ATOM   8560  C  CD1    . ILE   C 1  231 ? -7.857  -25.576  -8.386  1.00 36.74  ? 231 ILE   C CD1    1 
ATOM   8561  N  N      . SER   C 1  232 ? -6.092  -30.746  -7.997  1.00 39.06  ? 232 SER   C N      1 
ATOM   8562  C  CA     . SER   C 1  232 ? -6.546  -32.119  -8.073  1.00 39.93  ? 232 SER   C CA     1 
ATOM   8563  C  C      . SER   C 1  232 ? -5.760  -33.011  -7.135  1.00 42.86  ? 232 SER   C C      1 
ATOM   8564  O  O      . SER   C 1  232 ? -6.303  -33.994  -6.618  1.00 44.63  ? 232 SER   C O      1 
ATOM   8565  C  CB     . SER   C 1  232 ? -6.468  -32.608  -9.510  1.00 45.74  ? 232 SER   C CB     1 
ATOM   8566  O  OG     . SER   C 1  232 ? -5.162  -32.449  -10.013 1.00 59.70  ? 232 SER   C OG     1 
ATOM   8567  N  N      . GLN   C 1  233 ? -4.492  -32.689  -6.887  1.00 41.61  ? 233 GLN   C N      1 
ATOM   8568  C  CA     . GLN   C 1  233 ? -3.750  -33.482  -5.916  1.00 44.76  ? 233 GLN   C CA     1 
ATOM   8569  C  C      . GLN   C 1  233 ? -4.452  -33.437  -4.570  1.00 40.90  ? 233 GLN   C C      1 
ATOM   8570  O  O      . GLN   C 1  233 ? -4.594  -34.462  -3.897  1.00 41.87  ? 233 GLN   C O      1 
ATOM   8571  C  CB     . GLN   C 1  233 ? -2.308  -32.981  -5.825  1.00 44.02  ? 233 GLN   C CB     1 
ATOM   8572  C  CG     . GLN   C 1  233 ? -1.474  -33.356  -7.043  1.00 41.12  ? 233 GLN   C CG     1 
ATOM   8573  C  CD     . GLN   C 1  233 ? -1.243  -34.842  -7.145  1.00 43.86  ? 233 GLN   C CD     1 
ATOM   8574  O  OE1    . GLN   C 1  233 ? -0.960  -35.490  -6.149  1.00 54.56  ? 233 GLN   C OE1    1 
ATOM   8575  N  NE2    . GLN   C 1  233 ? -1.420  -35.401  -8.335  1.00 45.27  ? 233 GLN   C NE2    1 
ATOM   8576  N  N      . ILE   C 1  234 ? -4.967  -32.264  -4.206  1.00 38.74  ? 234 ILE   C N      1 
ATOM   8577  C  CA     . ILE   C 1  234 ? -5.657  -32.090  -2.930  1.00 42.25  ? 234 ILE   C CA     1 
ATOM   8578  C  C      . ILE   C 1  234 ? -7.016  -32.786  -2.956  1.00 42.64  ? 234 ILE   C C      1 
ATOM   8579  O  O      . ILE   C 1  234 ? -7.382  -33.513  -2.020  1.00 36.74  ? 234 ILE   C O      1 
ATOM   8580  C  CB     . ILE   C 1  234 ? -5.794  -30.588  -2.631  1.00 36.18  ? 234 ILE   C CB     1 
ATOM   8581  C  CG1    . ILE   C 1  234 ? -4.412  -30.016  -2.376  1.00 37.53  ? 234 ILE   C CG1    1 
ATOM   8582  C  CG2    . ILE   C 1  234 ? -6.732  -30.354  -1.459  1.00 29.57  ? 234 ILE   C CG2    1 
ATOM   8583  C  CD1    . ILE   C 1  234 ? -4.178  -28.694  -3.035  1.00 40.07  ? 234 ILE   C CD1    1 
ATOM   8584  N  N      . VAL   C 1  235 ? -7.787  -32.562  -4.028  1.00 39.05  ? 235 VAL   C N      1 
ATOM   8585  C  CA     . VAL   C 1  235 ? -9.025  -33.307  -4.213  1.00 37.02  ? 235 VAL   C CA     1 
ATOM   8586  C  C      . VAL   C 1  235 ? -8.758  -34.795  -4.091  1.00 39.07  ? 235 VAL   C C      1 
ATOM   8587  O  O      . VAL   C 1  235 ? -9.544  -35.535  -3.492  1.00 40.83  ? 235 VAL   C O      1 
ATOM   8588  C  CB     . VAL   C 1  235 ? -9.671  -32.966  -5.565  1.00 37.32  ? 235 VAL   C CB     1 
ATOM   8589  C  CG1    . VAL   C 1  235 ? -10.805 -33.901  -5.807  1.00 37.63  ? 235 VAL   C CG1    1 
ATOM   8590  C  CG2    . VAL   C 1  235 ? -10.200 -31.552  -5.569  1.00 37.97  ? 235 VAL   C CG2    1 
ATOM   8591  N  N      . SER   C 1  236 ? -7.627  -35.256  -4.623  1.00 38.91  ? 236 SER   C N      1 
ATOM   8592  C  CA     . SER   C 1  236 ? -7.339  -36.683  -4.585  1.00 37.55  ? 236 SER   C CA     1 
ATOM   8593  C  C      . SER   C 1  236 ? -7.083  -37.169  -3.163  1.00 37.13  ? 236 SER   C C      1 
ATOM   8594  O  O      . SER   C 1  236 ? -7.585  -38.227  -2.775  1.00 39.83  ? 236 SER   C O      1 
ATOM   8595  C  CB     . SER   C 1  236 ? -6.153  -37.007  -5.484  1.00 38.40  ? 236 SER   C CB     1 
ATOM   8596  O  OG     . SER   C 1  236 ? -5.900  -38.400  -5.468  1.00 38.10  ? 236 SER   C OG     1 
ATOM   8597  N  N      . SER   C 1  237 ? -6.311  -36.417  -2.369  1.00 36.81  ? 237 SER   C N      1 
ATOM   8598  C  CA     . SER   C 1  237 ? -6.058  -36.816  -0.982  1.00 38.76  ? 237 SER   C CA     1 
ATOM   8599  C  C      . SER   C 1  237 ? -7.345  -36.912  -0.179  1.00 35.88  ? 237 SER   C C      1 
ATOM   8600  O  O      . SER   C 1  237 ? -7.490  -37.790  0.673   1.00 37.07  ? 237 SER   C O      1 
ATOM   8601  C  CB     . SER   C 1  237 ? -5.110  -35.831  -0.301  1.00 44.34  ? 237 SER   C CB     1 
ATOM   8602  O  OG     . SER   C 1  237 ? -3.892  -35.704  -1.011  1.00 45.67  ? 237 SER   C OG     1 
ATOM   8603  N  N      . ILE   C 1  238 ? -8.284  -36.003  -0.420  1.00 38.92  ? 238 ILE   C N      1 
ATOM   8604  C  CA     . ILE   C 1  238 ? -9.526  -36.030  0.337   1.00 38.32  ? 238 ILE   C CA     1 
ATOM   8605  C  C      . ILE   C 1  238 ? -10.368 -37.245  -0.041  1.00 36.11  ? 238 ILE   C C      1 
ATOM   8606  O  O      . ILE   C 1  238 ? -10.907 -37.939  0.828   1.00 37.35  ? 238 ILE   C O      1 
ATOM   8607  C  CB     . ILE   C 1  238 ? -10.261 -34.690  0.164   1.00 34.41  ? 238 ILE   C CB     1 
ATOM   8608  C  CG1    . ILE   C 1  238 ? -9.354  -33.572  0.692   1.00 33.71  ? 238 ILE   C CG1    1 
ATOM   8609  C  CG2    . ILE   C 1  238 ? -11.600 -34.716  0.846   1.00 36.89  ? 238 ILE   C CG2    1 
ATOM   8610  C  CD1    . ILE   C 1  238 ? -9.936  -32.202  0.678   1.00 31.65  ? 238 ILE   C CD1    1 
ATOM   8611  N  N      . THR   C 1  239 ? -10.444 -37.566  -1.319  1.00 35.76  ? 239 THR   C N      1 
ATOM   8612  C  CA     . THR   C 1  239 ? -11.201 -38.741  -1.725  1.00 37.89  ? 239 THR   C CA     1 
ATOM   8613  C  C      . THR   C 1  239 ? -10.391 -40.023  -1.687  1.00 40.12  ? 239 THR   C C      1 
ATOM   8614  O  O      . THR   C 1  239 ? -10.968 -41.099  -1.835  1.00 42.30  ? 239 THR   C O      1 
ATOM   8615  C  CB     . THR   C 1  239 ? -11.711 -38.561  -3.136  1.00 34.66  ? 239 THR   C CB     1 
ATOM   8616  O  OG1    . THR   C 1  239 ? -10.576 -38.424  -3.983  1.00 38.22  ? 239 THR   C OG1    1 
ATOM   8617  C  CG2    . THR   C 1  239 ? -12.534 -37.309  -3.242  1.00 34.64  ? 239 THR   C CG2    1 
ATOM   8618  N  N      . ALA   C 1  240 ? -9.075  -39.940  -1.511  1.00 37.55  ? 240 ALA   C N      1 
ATOM   8619  C  CA     . ALA   C 1  240 ? -8.255  -41.138  -1.551  1.00 39.38  ? 240 ALA   C CA     1 
ATOM   8620  C  C      . ALA   C 1  240 ? -8.773  -42.200  -0.603  1.00 44.44  ? 240 ALA   C C      1 
ATOM   8621  O  O      . ALA   C 1  240 ? -8.590  -43.393  -0.853  1.00 45.99  ? 240 ALA   C O      1 
ATOM   8622  C  CB     . ALA   C 1  240 ? -6.803  -40.793  -1.215  1.00 45.21  ? 240 ALA   C CB     1 
ATOM   8623  N  N      . SER   C 1  241 ? -9.407  -41.785  0.493   1.00 47.55  ? 241 SER   C N      1 
ATOM   8624  C  CA     . SER   C 1  241 ? -9.981  -42.689  1.486   1.00 48.94  ? 241 SER   C CA     1 
ATOM   8625  C  C      . SER   C 1  241 ? -11.277 -43.346  1.025   1.00 49.24  ? 241 SER   C C      1 
ATOM   8626  O  O      . SER   C 1  241 ? -11.639 -44.412  1.530   1.00 52.58  ? 241 SER   C O      1 
ATOM   8627  C  CB     . SER   C 1  241 ? -10.208 -41.916  2.784   1.00 53.93  ? 241 SER   C CB     1 
ATOM   8628  O  OG     . SER   C 1  241 ? -10.693 -40.605  2.518   1.00 55.32  ? 241 SER   C OG     1 
ATOM   8629  N  N      . LEU   C 1  242 ? -11.978 -42.730  0.081   1.00 45.21  ? 242 LEU   C N      1 
ATOM   8630  C  CA     . LEU   C 1  242 ? -13.123 -43.349  -0.567  1.00 42.10  ? 242 LEU   C CA     1 
ATOM   8631  C  C      . LEU   C 1  242 ? -12.732 -44.333  -1.657  1.00 42.68  ? 242 LEU   C C      1 
ATOM   8632  O  O      . LEU   C 1  242 ? -13.450 -45.304  -1.895  1.00 46.82  ? 242 LEU   C O      1 
ATOM   8633  C  CB     . LEU   C 1  242 ? -13.987 -42.260  -1.180  1.00 45.84  ? 242 LEU   C CB     1 
ATOM   8634  C  CG     . LEU   C 1  242 ? -14.582 -41.327  -0.162  1.00 44.37  ? 242 LEU   C CG     1 
ATOM   8635  C  CD1    . LEU   C 1  242 ? -15.293 -40.214  -0.845  1.00 36.76  ? 242 LEU   C CD1    1 
ATOM   8636  C  CD2    . LEU   C 1  242 ? -15.579 -42.209  0.548   1.00 54.40  ? 242 LEU   C CD2    1 
ATOM   8637  N  N      . ARG   C 1  243 ? -11.640 -44.079  -2.364  1.00 43.84  ? 243 ARG   C N      1 
ATOM   8638  C  CA     . ARG   C 1  243 ? -11.304 -44.861  -3.544  1.00 42.20  ? 243 ARG   C CA     1 
ATOM   8639  C  C      . ARG   C 1  243 ? -10.365 -46.017  -3.253  1.00 48.92  ? 243 ARG   C C      1 
ATOM   8640  O  O      . ARG   C 1  243 ? -10.355 -46.998  -4.005  1.00 49.21  ? 243 ARG   C O      1 
ATOM   8641  C  CB     . ARG   C 1  243 ? -10.701 -43.947  -4.614  1.00 38.85  ? 243 ARG   C CB     1 
ATOM   8642  C  CG     . ARG   C 1  243 ? -11.570 -42.730  -4.899  1.00 39.74  ? 243 ARG   C CG     1 
ATOM   8643  C  CD     . ARG   C 1  243 ? -10.995 -41.771  -5.938  1.00 39.32  ? 243 ARG   C CD     1 
ATOM   8644  N  NE     . ARG   C 1  243 ? -9.926  -40.903  -5.452  1.00 40.81  ? 243 ARG   C NE     1 
ATOM   8645  C  CZ     . ARG   C 1  243 ? -8.630  -41.074  -5.673  1.00 38.21  ? 243 ARG   C CZ     1 
ATOM   8646  N  NH1    . ARG   C 1  243 ? -8.175  -42.099  -6.365  1.00 38.14  ? 243 ARG   C NH1    1 
ATOM   8647  N  NH2    . ARG   C 1  243 ? -7.768  -40.188  -5.189  1.00 39.63  ? 243 ARG   C NH2    1 
ATOM   8648  N  N      . PHE   C 1  244 ? -9.617  -45.946  -2.159  1.00 49.55  ? 244 PHE   C N      1 
ATOM   8649  C  CA     . PHE   C 1  244 ? -8.574  -46.903  -1.855  1.00 46.10  ? 244 PHE   C CA     1 
ATOM   8650  C  C      . PHE   C 1  244 ? -8.897  -47.678  -0.593  1.00 57.42  ? 244 PHE   C C      1 
ATOM   8651  O  O      . PHE   C 1  244 ? -9.241  -47.096  0.442   1.00 60.17  ? 244 PHE   C O      1 
ATOM   8652  C  CB     . PHE   C 1  244 ? -7.255  -46.196  -1.704  1.00 46.27  ? 244 PHE   C CB     1 
ATOM   8653  C  CG     . PHE   C 1  244 ? -6.664  -45.808  -2.989  1.00 46.94  ? 244 PHE   C CG     1 
ATOM   8654  C  CD1    . PHE   C 1  244 ? -6.110  -46.764  -3.813  1.00 49.90  ? 244 PHE   C CD1    1 
ATOM   8655  C  CD2    . PHE   C 1  244 ? -6.671  -44.502  -3.394  1.00 45.07  ? 244 PHE   C CD2    1 
ATOM   8656  C  CE1    . PHE   C 1  244 ? -5.548  -46.413  -5.009  1.00 43.46  ? 244 PHE   C CE1    1 
ATOM   8657  C  CE2    . PHE   C 1  244 ? -6.118  -44.151  -4.593  1.00 43.57  ? 244 PHE   C CE2    1 
ATOM   8658  C  CZ     . PHE   C 1  244 ? -5.557  -45.105  -5.400  1.00 42.47  ? 244 PHE   C CZ     1 
ATOM   8659  N  N      . ASP   C 1  245 ? -8.774  -48.992  -0.689  1.00 58.76  ? 245 ASP   C N      1 
ATOM   8660  C  CA     . ASP   C 1  245 ? -8.903  -49.855  0.461   1.00 67.45  ? 245 ASP   C CA     1 
ATOM   8661  C  C      . ASP   C 1  245 ? -7.682  -49.634  1.348   1.00 76.01  ? 245 ASP   C C      1 
ATOM   8662  O  O      . ASP   C 1  245 ? -6.600  -49.279  0.864   1.00 77.54  ? 245 ASP   C O      1 
ATOM   8663  C  CB     . ASP   C 1  245 ? -8.998  -51.310  -0.004  1.00 79.94  ? 245 ASP   C CB     1 
ATOM   8664  C  CG     . ASP   C 1  245 ? -10.444 -51.860  0.017   1.00 90.72  ? 245 ASP   C CG     1 
ATOM   8665  O  OD1    . ASP   C 1  245 ? -11.270 -51.448  0.874   1.00 86.84  ? 245 ASP   C OD1    1 
ATOM   8666  O  OD2    . ASP   C 1  245 ? -10.760 -52.681  -0.886  1.00 90.33  ? 245 ASP   C OD2    1 
ATOM   8667  N  N      . GLY   C 1  246 ? -7.859  -49.813  2.654   1.00 73.89  ? 246 GLY   C N      1 
ATOM   8668  C  CA     . GLY   C 1  246 ? -6.696  -49.747  3.516   1.00 66.84  ? 246 GLY   C CA     1 
ATOM   8669  C  C      . GLY   C 1  246 ? -6.922  -50.025  4.987   1.00 78.51  ? 246 GLY   C C      1 
ATOM   8670  O  O      . GLY   C 1  246 ? -7.989  -49.707  5.530   1.00 86.44  ? 246 GLY   C O      1 
ATOM   8671  N  N      . ALA   C 1  247 ? -5.908  -50.606  5.644   1.00 78.34  ? 247 ALA   C N      1 
ATOM   8672  C  CA     . ALA   C 1  247 ? -5.960  -50.819  7.090   1.00 78.26  ? 247 ALA   C CA     1 
ATOM   8673  C  C      . ALA   C 1  247 ? -5.962  -49.488  7.842   1.00 78.32  ? 247 ALA   C C      1 
ATOM   8674  O  O      . ALA   C 1  247 ? -6.949  -49.123  8.497   1.00 67.27  ? 247 ALA   C O      1 
ATOM   8675  C  CB     . ALA   C 1  247 ? -4.779  -51.689  7.525   1.00 69.83  ? 247 ALA   C CB     1 
ATOM   8676  N  N      . LEU   C 1  248 ? -4.858  -48.739  7.738   1.00 79.92  ? 248 LEU   C N      1 
ATOM   8677  C  CA     . LEU   C 1  248 ? -4.707  -47.439  8.385   1.00 73.29  ? 248 LEU   C CA     1 
ATOM   8678  C  C      . LEU   C 1  248 ? -5.519  -46.345  7.702   1.00 69.58  ? 248 LEU   C C      1 
ATOM   8679  O  O      . LEU   C 1  248 ? -5.230  -45.153  7.880   1.00 64.15  ? 248 LEU   C O      1 
ATOM   8680  C  CB     . LEU   C 1  248 ? -3.227  -47.040  8.426   1.00 66.38  ? 248 LEU   C CB     1 
ATOM   8681  C  CG     . LEU   C 1  248 ? -2.333  -47.884  9.338   1.00 74.26  ? 248 LEU   C CG     1 
ATOM   8682  C  CD1    . LEU   C 1  248 ? -0.914  -47.324  9.439   1.00 62.47  ? 248 LEU   C CD1    1 
ATOM   8683  C  CD2    . LEU   C 1  248 ? -2.974  -47.944  10.723  1.00 75.75  ? 248 LEU   C CD2    1 
ATOM   8684  N  N      . ASN   C 1  249 ? -6.554  -46.733  6.954   1.00 70.17  ? 249 ASN   C N      1 
ATOM   8685  C  CA     . ASN   C 1  249 ? -7.299  -45.821  6.093   1.00 66.00  ? 249 ASN   C CA     1 
ATOM   8686  C  C      . ASN   C 1  249 ? -8.594  -45.391  6.777   1.00 63.28  ? 249 ASN   C C      1 
ATOM   8687  O  O      . ASN   C 1  249 ? -9.409  -46.233  7.163   1.00 70.53  ? 249 ASN   C O      1 
ATOM   8688  C  CB     . ASN   C 1  249 ? -7.595  -46.483  4.750   1.00 71.06  ? 249 ASN   C CB     1 
ATOM   8689  C  CG     . ASN   C 1  249 ? -8.455  -45.628  3.866   1.00 70.13  ? 249 ASN   C CG     1 
ATOM   8690  O  OD1    . ASN   C 1  249 ? -7.986  -44.632  3.310   1.00 66.12  ? 249 ASN   C OD1    1 
ATOM   8691  N  ND2    . ASN   C 1  249 ? -9.731  -45.991  3.747   1.00 71.11  ? 249 ASN   C ND2    1 
ATOM   8692  N  N      . VAL   C 1  250 ? -8.786  -44.083  6.892   1.00 61.99  ? 250 VAL   C N      1 
ATOM   8693  C  CA     . VAL   C 1  250 ? -9.895  -43.480  7.623   1.00 60.42  ? 250 VAL   C CA     1 
ATOM   8694  C  C      . VAL   C 1  250 ? -10.880 -42.906  6.608   1.00 57.57  ? 250 VAL   C C      1 
ATOM   8695  O  O      . VAL   C 1  250 ? -10.473 -42.238  5.653   1.00 54.98  ? 250 VAL   C O      1 
ATOM   8696  C  CB     . VAL   C 1  250 ? -9.371  -42.391  8.575   1.00 53.67  ? 250 VAL   C CB     1 
ATOM   8697  C  CG1    . VAL   C 1  250 ? -10.501 -41.643  9.282   1.00 53.18  ? 250 VAL   C CG1    1 
ATOM   8698  C  CG2    . VAL   C 1  250 ? -8.365  -42.977  9.544   1.00 48.83  ? 250 VAL   C CG2    1 
ATOM   8699  N  N      . ASP   C 1  251 ? -12.172 -43.159  6.814   1.00 60.49  ? 251 ASP   C N      1 
ATOM   8700  C  CA     . ASP   C 1  251 ? -13.185 -42.755  5.843   1.00 63.58  ? 251 ASP   C CA     1 
ATOM   8701  C  C      . ASP   C 1  251 ? -13.427 -41.244  5.872   1.00 59.24  ? 251 ASP   C C      1 
ATOM   8702  O  O      . ASP   C 1  251 ? -13.592 -40.648  6.939   1.00 59.57  ? 251 ASP   C O      1 
ATOM   8703  C  CB     . ASP   C 1  251 ? -14.487 -43.515  6.116   1.00 62.29  ? 251 ASP   C CB     1 
ATOM   8704  C  CG     . ASP   C 1  251 ? -15.194 -43.935  4.834   1.00 76.98  ? 251 ASP   C CG     1 
ATOM   8705  O  OD1    . ASP   C 1  251 ? -14.504 -44.478  3.923   1.00 71.87  ? 251 ASP   C OD1    1 
ATOM   8706  O  OD2    . ASP   C 1  251 ? -16.437 -43.720  4.748   1.00 73.93  ? 251 ASP   C OD2    1 
ATOM   8707  N  N      . LEU   C 1  252 ? -13.486 -40.617  4.688   1.00 54.52  ? 252 LEU   C N      1 
ATOM   8708  C  CA     . LEU   C 1  252 ? -13.701 -39.169  4.657   1.00 57.73  ? 252 LEU   C CA     1 
ATOM   8709  C  C      . LEU   C 1  252 ? -14.941 -38.730  5.436   1.00 62.32  ? 252 LEU   C C      1 
ATOM   8710  O  O      . LEU   C 1  252 ? -15.080 -37.541  5.763   1.00 61.50  ? 252 LEU   C O      1 
ATOM   8711  C  CB     . LEU   C 1  252 ? -13.793 -38.652  3.219   1.00 50.94  ? 252 LEU   C CB     1 
ATOM   8712  C  CG     . LEU   C 1  252 ? -14.194 -37.168  3.143   1.00 46.77  ? 252 LEU   C CG     1 
ATOM   8713  C  CD1    . LEU   C 1  252 ? -13.349 -36.239  4.053   1.00 38.80  ? 252 LEU   C CD1    1 
ATOM   8714  C  CD2    . LEU   C 1  252 ? -14.121 -36.698  1.695   1.00 41.54  ? 252 LEU   C CD2    1 
ATOM   8715  N  N      . THR   C 1  253 ? -15.847 -39.655  5.740   1.00 63.05  ? 253 THR   C N      1 
ATOM   8716  C  CA     . THR   C 1  253 ? -17.011 -39.330  6.546   1.00 59.78  ? 253 THR   C CA     1 
ATOM   8717  C  C      . THR   C 1  253 ? -16.702 -39.366  8.036   1.00 58.14  ? 253 THR   C C      1 
ATOM   8718  O  O      . THR   C 1  253 ? -17.379 -38.692  8.817   1.00 56.36  ? 253 THR   C O      1 
ATOM   8719  C  CB     . THR   C 1  253 ? -18.147 -40.284  6.177   1.00 60.44  ? 253 THR   C CB     1 
ATOM   8720  O  OG1    . THR   C 1  253 ? -17.672 -41.637  6.239   1.00 60.56  ? 253 THR   C OG1    1 
ATOM   8721  C  CG2    . THR   C 1  253 ? -18.650 -39.987  4.754   1.00 53.75  ? 253 THR   C CG2    1 
ATOM   8722  N  N      . GLU   C 1  254 ? -15.677 -40.121  8.437   1.00 58.18  ? 254 GLU   C N      1 
ATOM   8723  C  CA     . GLU   C 1  254 ? -15.193 -40.073  9.816   1.00 60.06  ? 254 GLU   C CA     1 
ATOM   8724  C  C      . GLU   C 1  254 ? -14.562 -38.722  10.132  1.00 58.50  ? 254 GLU   C C      1 
ATOM   8725  O  O      . GLU   C 1  254 ? -14.667 -38.207  11.262  1.00 50.50  ? 254 GLU   C O      1 
ATOM   8726  C  CB     . GLU   C 1  254 ? -14.178 -41.198  10.042  1.00 50.75  ? 254 GLU   C CB     1 
ATOM   8727  C  CG     . GLU   C 1  254 ? -14.011 -41.642  11.483  1.00 47.85  ? 254 GLU   C CG     1 
ATOM   8728  C  CD     . GLU   C 1  254 ? -13.486 -43.042  11.566  1.00 52.90  ? 254 GLU   C CD     1 
ATOM   8729  O  OE1    . GLU   C 1  254 ? -14.065 -43.900  10.877  1.00 57.79  ? 254 GLU   C OE1    1 
ATOM   8730  O  OE2    . GLU   C 1  254 ? -12.505 -43.296  12.296  1.00 52.11  ? 254 GLU   C OE2    1 
ATOM   8731  N  N      . PHE   C 1  255 ? -13.876 -38.151  9.144   1.00 53.51  ? 255 PHE   C N      1 
ATOM   8732  C  CA     . PHE   C 1  255 ? -13.301 -36.831  9.319   1.00 51.72  ? 255 PHE   C CA     1 
ATOM   8733  C  C      . PHE   C 1  255 ? -14.386 -35.757  9.369   1.00 57.51  ? 255 PHE   C C      1 
ATOM   8734  O  O      . PHE   C 1  255 ? -14.254 -34.778  10.122  1.00 51.56  ? 255 PHE   C O      1 
ATOM   8735  C  CB     . PHE   C 1  255 ? -12.318 -36.561  8.190   1.00 53.83  ? 255 PHE   C CB     1 
ATOM   8736  C  CG     . PHE   C 1  255 ? -11.056 -37.358  8.293   1.00 58.19  ? 255 PHE   C CG     1 
ATOM   8737  C  CD1    . PHE   C 1  255 ? -10.143 -37.120  9.315   1.00 50.14  ? 255 PHE   C CD1    1 
ATOM   8738  C  CD2    . PHE   C 1  255 ? -10.768 -38.343  7.358   1.00 57.14  ? 255 PHE   C CD2    1 
ATOM   8739  C  CE1    . PHE   C 1  255 ? -8.976  -37.856  9.395   1.00 45.06  ? 255 PHE   C CE1    1 
ATOM   8740  C  CE2    . PHE   C 1  255 ? -9.593  -39.084  7.439   1.00 49.16  ? 255 PHE   C CE2    1 
ATOM   8741  C  CZ     . PHE   C 1  255 ? -8.707  -38.843  8.451   1.00 45.56  ? 255 PHE   C CZ     1 
ATOM   8742  N  N      . GLN   C 1  256 ? -15.472 -35.911  8.577   1.00 53.07  ? 256 GLN   C N      1 
ATOM   8743  C  CA     . GLN   C 1  256 ? -16.509 -34.880  8.602   1.00 50.09  ? 256 GLN   C CA     1 
ATOM   8744  C  C      . GLN   C 1  256 ? -17.226 -34.834  9.936   1.00 45.65  ? 256 GLN   C C      1 
ATOM   8745  O  O      . GLN   C 1  256 ? -17.800 -33.800  10.286  1.00 45.00  ? 256 GLN   C O      1 
ATOM   8746  C  CB     . GLN   C 1  256 ? -17.575 -35.066  7.537   1.00 50.19  ? 256 GLN   C CB     1 
ATOM   8747  C  CG     . GLN   C 1  256 ? -17.132 -35.428  6.172   1.00 52.72  ? 256 GLN   C CG     1 
ATOM   8748  C  CD     . GLN   C 1  256 ? -18.343 -35.842  5.360   1.00 65.79  ? 256 GLN   C CD     1 
ATOM   8749  O  OE1    . GLN   C 1  256 ? -19.456 -35.336  5.587   1.00 66.59  ? 256 GLN   C OE1    1 
ATOM   8750  N  NE2    . GLN   C 1  256 ? -18.161 -36.815  4.466   1.00 65.99  ? 256 GLN   C NE2    1 
ATOM   8751  N  N      . THR   C 1  257 ? -17.238 -35.942  10.668  1.00 48.08  ? 257 THR   C N      1 
ATOM   8752  C  CA     . THR   C 1  257 ? -17.761 -35.905  12.022  1.00 46.44  ? 257 THR   C CA     1 
ATOM   8753  C  C      . THR   C 1  257 ? -16.997 -34.896  12.849  1.00 42.97  ? 257 THR   C C      1 
ATOM   8754  O  O      . THR   C 1  257 ? -17.584 -34.130  13.623  1.00 39.17  ? 257 THR   C O      1 
ATOM   8755  C  CB     . THR   C 1  257 ? -17.622 -37.267  12.666  1.00 50.73  ? 257 THR   C CB     1 
ATOM   8756  O  OG1    . THR   C 1  257 ? -18.293 -38.246  11.860  1.00 55.98  ? 257 THR   C OG1    1 
ATOM   8757  C  CG2    . THR   C 1  257 ? -18.246 -37.203  14.075  1.00 39.01  ? 257 THR   C CG2    1 
ATOM   8758  N  N      . ASN   C 1  258 ? -15.671 -34.907  12.707  1.00 41.52  ? 258 ASN   C N      1 
ATOM   8759  C  CA     . ASN   C 1  258 ? -14.798 -34.035  13.473  1.00 43.12  ? 258 ASN   C CA     1 
ATOM   8760  C  C      . ASN   C 1  258 ? -14.733 -32.627  12.907  1.00 46.27  ? 258 ASN   C C      1 
ATOM   8761  O  O      . ASN   C 1  258 ? -14.383 -31.693  13.651  1.00 45.71  ? 258 ASN   C O      1 
ATOM   8762  C  CB     . ASN   C 1  258 ? -13.371 -34.599  13.520  1.00 49.28  ? 258 ASN   C CB     1 
ATOM   8763  C  CG     . ASN   C 1  258 ? -13.217 -35.821  14.457  1.00 52.48  ? 258 ASN   C CG     1 
ATOM   8764  O  OD1    . ASN   C 1  258 ? -14.170 -36.287  15.083  1.00 50.70  ? 258 ASN   C OD1    1 
ATOM   8765  N  ND2    . ASN   C 1  258 ? -11.981 -36.326  14.555  1.00 53.50  ? 258 ASN   C ND2    1 
ATOM   8766  N  N      . LEU   C 1  259 ? -15.054 -32.452  11.615  1.00 36.28  ? 259 LEU   C N      1 
ATOM   8767  C  CA     . LEU   C 1  259 ? -14.866 -31.164  10.979  1.00 29.57  ? 259 LEU   C CA     1 
ATOM   8768  C  C      . LEU   C 1  259 ? -16.064 -30.240  11.102  1.00 33.72  ? 259 LEU   C C      1 
ATOM   8769  O  O      . LEU   C 1  259 ? -15.903 -29.017  10.977  1.00 37.93  ? 259 LEU   C O      1 
ATOM   8770  C  CB     . LEU   C 1  259 ? -14.532 -31.351  9.513   1.00 33.61  ? 259 LEU   C CB     1 
ATOM   8771  C  CG     . LEU   C 1  259 ? -13.199 -32.009  9.201   1.00 36.20  ? 259 LEU   C CG     1 
ATOM   8772  C  CD1    . LEU   C 1  259 ? -13.209 -32.398  7.749   1.00 32.35  ? 259 LEU   C CD1    1 
ATOM   8773  C  CD2    . LEU   C 1  259 ? -12.023 -31.096  9.543   1.00 32.75  ? 259 LEU   C CD2    1 
ATOM   8774  N  N      . VAL   C 1  260 ? -17.253 -30.766  11.352  1.00 30.92  ? 260 VAL   C N      1 
ATOM   8775  C  CA     . VAL   C 1  260 ? -18.416 -29.891  11.410  1.00 28.95  ? 260 VAL   C CA     1 
ATOM   8776  C  C      . VAL   C 1  260 ? -18.936 -29.786  12.841  1.00 29.25  ? 260 VAL   C C      1 
ATOM   8777  O  O      . VAL   C 1  260 ? -19.743 -30.608  13.268  1.00 31.22  ? 260 VAL   C O      1 
ATOM   8778  C  CB     . VAL   C 1  260 ? -19.507 -30.390  10.460  1.00 30.89  ? 260 VAL   C CB     1 
ATOM   8779  C  CG1    . VAL   C 1  260 ? -20.672 -29.434  10.486  1.00 30.29  ? 260 VAL   C CG1    1 
ATOM   8780  C  CG2    . VAL   C 1  260 ? -18.946 -30.584  9.043   1.00 27.92  ? 260 VAL   C CG2    1 
ATOM   8781  N  N      . PRO   C 1  261 ? -18.537 -28.778  13.606  1.00 29.72  ? 261 PRO   C N      1 
ATOM   8782  C  CA     . PRO   C 1  261 ? -19.047 -28.679  14.975  1.00 25.93  ? 261 PRO   C CA     1 
ATOM   8783  C  C      . PRO   C 1  261 ? -20.500 -28.297  15.028  1.00 28.89  ? 261 PRO   C C      1 
ATOM   8784  O  O      . PRO   C 1  261 ? -21.224 -28.743  15.921  1.00 34.49  ? 261 PRO   C O      1 
ATOM   8785  C  CB     . PRO   C 1  261 ? -18.166 -27.592  15.581  1.00 31.40  ? 261 PRO   C CB     1 
ATOM   8786  C  CG     . PRO   C 1  261 ? -17.835 -26.710  14.431  1.00 30.39  ? 261 PRO   C CG     1 
ATOM   8787  C  CD     . PRO   C 1  261 ? -17.770 -27.590  13.206  1.00 30.49  ? 261 PRO   C CD     1 
ATOM   8788  N  N      . TYR   C 1  262 ? -20.940 -27.437  14.129  1.00 27.99  ? 262 TYR   C N      1 
ATOM   8789  C  CA     . TYR   C 1  262 ? -22.339 -27.094  13.935  1.00 26.34  ? 262 TYR   C CA     1 
ATOM   8790  C  C      . TYR   C 1  262 ? -22.618 -27.085  12.447  1.00 32.05  ? 262 TYR   C C      1 
ATOM   8791  O  O      . TYR   C 1  262 ? -21.698 -27.074  11.621  1.00 33.33  ? 262 TYR   C O      1 
ATOM   8792  C  CB     . TYR   C 1  262 ? -22.667 -25.726  14.533  1.00 23.38  ? 262 TYR   C CB     1 
ATOM   8793  C  CG     . TYR   C 1  262 ? -22.167 -25.586  15.923  1.00 24.99  ? 262 TYR   C CG     1 
ATOM   8794  C  CD1    . TYR   C 1  262 ? -20.864 -25.203  16.165  1.00 31.79  ? 262 TYR   C CD1    1 
ATOM   8795  C  CD2    . TYR   C 1  262 ? -22.988 -25.799  17.002  1.00 27.47  ? 262 TYR   C CD2    1 
ATOM   8796  C  CE1    . TYR   C 1  262 ? -20.387 -25.077  17.456  1.00 29.33  ? 262 TYR   C CE1    1 
ATOM   8797  C  CE2    . TYR   C 1  262 ? -22.513 -25.673  18.288  1.00 25.77  ? 262 TYR   C CE2    1 
ATOM   8798  C  CZ     . TYR   C 1  262 ? -21.227 -25.304  18.502  1.00 23.85  ? 262 TYR   C CZ     1 
ATOM   8799  O  OH     . TYR   C 1  262 ? -20.778 -25.158  19.782  1.00 28.80  ? 262 TYR   C OH     1 
ATOM   8800  N  N      . PRO   C 1  263 ? -23.886 -27.070  12.059  1.00 32.64  ? 263 PRO   C N      1 
ATOM   8801  C  CA     . PRO   C 1  263 ? -24.190 -27.191  10.625  1.00 26.91  ? 263 PRO   C CA     1 
ATOM   8802  C  C      . PRO   C 1  263 ? -23.621 -26.081  9.761   1.00 26.12  ? 263 PRO   C C      1 
ATOM   8803  O  O      . PRO   C 1  263 ? -23.151 -26.373  8.662   1.00 32.77  ? 263 PRO   C O      1 
ATOM   8804  C  CB     . PRO   C 1  263 ? -25.716 -27.252  10.608  1.00 23.02  ? 263 PRO   C CB     1 
ATOM   8805  C  CG     . PRO   C 1  263 ? -26.064 -27.864  11.966  1.00 27.18  ? 263 PRO   C CG     1 
ATOM   8806  C  CD     . PRO   C 1  263 ? -25.059 -27.295  12.916  1.00 27.01  ? 263 PRO   C CD     1 
ATOM   8807  N  N      . ARG   C 1  264 ? -23.595 -24.833  10.215  1.00 29.29  ? 264 ARG   C N      1 
ATOM   8808  C  CA     . ARG   C 1  264 ? -23.051 -23.753  9.380   1.00 31.92  ? 264 ARG   C CA     1 
ATOM   8809  C  C      . ARG   C 1  264 ? -21.513 -23.696  9.387   1.00 32.80  ? 264 ARG   C C      1 
ATOM   8810  O  O      . ARG   C 1  264 ? -20.908 -23.263  8.397   1.00 34.26  ? 264 ARG   C O      1 
ATOM   8811  C  CB     . ARG   C 1  264 ? -23.629 -22.399  9.825   1.00 27.09  ? 264 ARG   C CB     1 
ATOM   8812  C  CG     . ARG   C 1  264 ? -25.024 -22.179  9.381   1.00 22.49  ? 264 ARG   C CG     1 
ATOM   8813  C  CD     . ARG   C 1  264 ? -25.699 -21.104  10.168  1.00 23.95  ? 264 ARG   C CD     1 
ATOM   8814  N  NE     . ARG   C 1  264 ? -25.108 -19.795  9.941   1.00 33.28  ? 264 ARG   C NE     1 
ATOM   8815  C  CZ     . ARG   C 1  264 ? -25.456 -19.007  8.934   1.00 33.40  ? 264 ARG   C CZ     1 
ATOM   8816  N  NH1    . ARG   C 1  264 ? -26.372 -19.386  8.048   1.00 30.11  ? 264 ARG   C NH1    1 
ATOM   8817  N  NH2    . ARG   C 1  264 ? -24.863 -17.821  8.801   1.00 27.15  ? 264 ARG   C NH2    1 
ATOM   8818  N  N      . ILE   C 1  265 ? -20.856 -24.094  10.475  1.00 27.43  ? 265 ILE   C N      1 
ATOM   8819  C  CA     . ILE   C 1  265 ? -19.409 -24.199  10.436  1.00 29.20  ? 265 ILE   C CA     1 
ATOM   8820  C  C      . ILE   C 1  265 ? -19.003 -25.474  9.711   1.00 30.37  ? 265 ILE   C C      1 
ATOM   8821  O  O      . ILE   C 1  265 ? -18.680 -26.492  10.325  1.00 31.97  ? 265 ILE   C O      1 
ATOM   8822  C  CB     . ILE   C 1  265 ? -18.835 -24.078  11.855  1.00 32.20  ? 265 ILE   C CB     1 
ATOM   8823  C  CG1    . ILE   C 1  265 ? -18.914 -22.609  12.258  1.00 38.42  ? 265 ILE   C CG1    1 
ATOM   8824  C  CG2    . ILE   C 1  265 ? -17.379 -24.515  11.902  1.00 31.84  ? 265 ILE   C CG2    1 
ATOM   8825  C  CD1    . ILE   C 1  265 ? -20.284 -22.072  12.383  1.00 34.51  ? 265 ILE   C CD1    1 
ATOM   8826  N  N      . HIS   C 1  266 ? -19.015 -25.428  8.390   1.00 27.94  ? 266 HIS   C N      1 
ATOM   8827  C  CA     . HIS   C 1  266 ? -18.692 -26.618  7.635   1.00 28.19  ? 266 HIS   C CA     1 
ATOM   8828  C  C      . HIS   C 1  266 ? -17.713 -26.294  6.518   1.00 37.40  ? 266 HIS   C C      1 
ATOM   8829  O  O      . HIS   C 1  266 ? -17.764 -26.891  5.435   1.00 34.44  ? 266 HIS   C O      1 
ATOM   8830  C  CB     . HIS   C 1  266 ? -19.954 -27.296  7.115   1.00 30.87  ? 266 HIS   C CB     1 
ATOM   8831  C  CG     . HIS   C 1  266 ? -20.728 -26.504  6.094   1.00 33.64  ? 266 HIS   C CG     1 
ATOM   8832  N  ND1    . HIS   C 1  266 ? -21.941 -25.908  6.376   1.00 34.70  ? 266 HIS   C ND1    1 
ATOM   8833  C  CD2    . HIS   C 1  266 ? -20.526 -26.317  4.769   1.00 31.63  ? 266 HIS   C CD2    1 
ATOM   8834  C  CE1    . HIS   C 1  266 ? -22.424 -25.346  5.281   1.00 29.53  ? 266 HIS   C CE1    1 
ATOM   8835  N  NE2    . HIS   C 1  266 ? -21.589 -25.588  4.291   1.00 32.62  ? 266 HIS   C NE2    1 
ATOM   8836  N  N      . PHE   C 1  267 ? -16.764 -25.374  6.798   1.00 39.71  ? 267 PHE   C N      1 
ATOM   8837  C  CA     . PHE   C 1  267 ? -15.760 -24.908  5.840   1.00 32.56  ? 267 PHE   C CA     1 
ATOM   8838  C  C      . PHE   C 1  267 ? -14.351 -25.275  6.290   1.00 32.59  ? 267 PHE   C C      1 
ATOM   8839  O  O      . PHE   C 1  267 ? -13.626 -24.450  6.865   1.00 33.84  ? 267 PHE   C O      1 
ATOM   8840  C  CB     . PHE   C 1  267 ? -15.894 -23.406  5.620   1.00 34.08  ? 267 PHE   C CB     1 
ATOM   8841  C  CG     . PHE   C 1  267 ? -17.201 -23.026  5.042   1.00 33.95  ? 267 PHE   C CG     1 
ATOM   8842  C  CD1    . PHE   C 1  267 ? -18.286 -22.745  5.854   1.00 33.80  ? 267 PHE   C CD1    1 
ATOM   8843  C  CD2    . PHE   C 1  267 ? -17.370 -23.037  3.671   1.00 28.71  ? 267 PHE   C CD2    1 
ATOM   8844  C  CE1    . PHE   C 1  267 ? -19.508 -22.433  5.302   1.00 31.21  ? 267 PHE   C CE1    1 
ATOM   8845  C  CE2    . PHE   C 1  267 ? -18.563 -22.728  3.135   1.00 26.03  ? 267 PHE   C CE2    1 
ATOM   8846  C  CZ     . PHE   C 1  267 ? -19.643 -22.423  3.947   1.00 27.83  ? 267 PHE   C CZ     1 
ATOM   8847  N  N      . PRO   C 1  268 ? -13.917 -26.493  6.006   1.00 32.11  ? 268 PRO   C N      1 
ATOM   8848  C  CA     . PRO   C 1  268 ? -12.599 -26.916  6.456   1.00 32.68  ? 268 PRO   C CA     1 
ATOM   8849  C  C      . PRO   C 1  268 ? -11.533 -26.186  5.673   1.00 36.32  ? 268 PRO   C C      1 
ATOM   8850  O  O      . PRO   C 1  268 ? -11.732 -25.789  4.522   1.00 42.81  ? 268 PRO   C O      1 
ATOM   8851  C  CB     . PRO   C 1  268 ? -12.570 -28.418  6.139   1.00 33.11  ? 268 PRO   C CB     1 
ATOM   8852  C  CG     . PRO   C 1  268 ? -13.952 -28.805  5.903   1.00 34.92  ? 268 PRO   C CG     1 
ATOM   8853  C  CD     . PRO   C 1  268 ? -14.601 -27.579  5.294   1.00 34.84  ? 268 PRO   C CD     1 
ATOM   8854  N  N      . LEU   C 1  269 ? -10.384 -26.030  6.310   1.00 36.21  ? 269 LEU   C N      1 
ATOM   8855  C  CA     . LEU   C 1  269 ? -9.208  -25.465  5.686   1.00 32.93  ? 269 LEU   C CA     1 
ATOM   8856  C  C      . LEU   C 1  269 ? -8.285  -26.590  5.263   1.00 31.80  ? 269 LEU   C C      1 
ATOM   8857  O  O      . LEU   C 1  269 ? -7.825  -27.354  6.106   1.00 37.55  ? 269 LEU   C O      1 
ATOM   8858  C  CB     . LEU   C 1  269 ? -8.504  -24.521  6.658   1.00 31.26  ? 269 LEU   C CB     1 
ATOM   8859  C  CG     . LEU   C 1  269 ? -7.200  -23.957  6.104   1.00 35.47  ? 269 LEU   C CG     1 
ATOM   8860  C  CD1    . LEU   C 1  269 ? -7.434  -23.264  4.780   1.00 36.47  ? 269 LEU   C CD1    1 
ATOM   8861  C  CD2    . LEU   C 1  269 ? -6.596  -23.008  7.103   1.00 32.32  ? 269 LEU   C CD2    1 
ATOM   8862  N  N      . ALA   C 1  270 ? -7.978  -26.660  3.977   1.00 33.10  ? 270 ALA   C N      1 
ATOM   8863  C  CA     . ALA   C 1  270 ? -7.008  -27.626  3.467   1.00 35.22  ? 270 ALA   C CA     1 
ATOM   8864  C  C      . ALA   C 1  270 ? -5.622  -27.011  3.348   1.00 34.81  ? 270 ALA   C C      1 
ATOM   8865  O  O      . ALA   C 1  270 ? -5.459  -25.800  3.174   1.00 29.15  ? 270 ALA   C O      1 
ATOM   8866  C  CB     . ALA   C 1  270 ? -7.412  -28.173  2.095   1.00 35.53  ? 270 ALA   C CB     1 
ATOM   8867  N  N      . THR   C 1  271 ? -4.623  -27.887  3.433   1.00 35.13  ? 271 THR   C N      1 
ATOM   8868  C  CA     . THR   C 1  271 ? -3.205  -27.548  3.416   1.00 33.14  ? 271 THR   C CA     1 
ATOM   8869  C  C      . THR   C 1  271 ? -2.491  -28.807  2.975   1.00 34.49  ? 271 THR   C C      1 
ATOM   8870  O  O      . THR   C 1  271 ? -2.691  -29.861  3.584   1.00 33.74  ? 271 THR   C O      1 
ATOM   8871  C  CB     . THR   C 1  271 ? -2.669  -27.126  4.797   1.00 37.59  ? 271 THR   C CB     1 
ATOM   8872  O  OG1    . THR   C 1  271 ? -3.566  -26.212  5.443   1.00 46.26  ? 271 THR   C OG1    1 
ATOM   8873  C  CG2    . THR   C 1  271 ? -1.323  -26.467  4.659   1.00 37.95  ? 271 THR   C CG2    1 
ATOM   8874  N  N      . TYR   C 1  272 ? -1.653  -28.693  1.941   1.00 38.27  ? 272 TYR   C N      1 
ATOM   8875  C  CA     . TYR   C 1  272 ? -1.051  -29.839  1.270   1.00 35.98  ? 272 TYR   C CA     1 
ATOM   8876  C  C      . TYR   C 1  272 ? 0.449   -29.631  1.151   1.00 36.48  ? 272 TYR   C C      1 
ATOM   8877  O  O      . TYR   C 1  272 ? 0.907   -28.501  0.997   1.00 43.70  ? 272 TYR   C O      1 
ATOM   8878  C  CB     . TYR   C 1  272 ? -1.644  -30.013  -0.107  1.00 31.00  ? 272 TYR   C CB     1 
ATOM   8879  C  CG     . TYR   C 1  272 ? -1.119  -31.160  -0.893  1.00 34.06  ? 272 TYR   C CG     1 
ATOM   8880  C  CD1    . TYR   C 1  272 ? -1.687  -32.408  -0.761  1.00 37.03  ? 272 TYR   C CD1    1 
ATOM   8881  C  CD2    . TYR   C 1  272 ? -0.074  -31.002  -1.788  1.00 39.64  ? 272 TYR   C CD2    1 
ATOM   8882  C  CE1    . TYR   C 1  272 ? -1.230  -33.476  -1.496  1.00 42.36  ? 272 TYR   C CE1    1 
ATOM   8883  C  CE2    . TYR   C 1  272 ? 0.396   -32.075  -2.545  1.00 41.12  ? 272 TYR   C CE2    1 
ATOM   8884  C  CZ     . TYR   C 1  272 ? -0.191  -33.313  -2.393  1.00 44.20  ? 272 TYR   C CZ     1 
ATOM   8885  O  OH     . TYR   C 1  272 ? 0.242   -34.407  -3.117  1.00 51.32  ? 272 TYR   C OH     1 
ATOM   8886  N  N      . ALA   C 1  273 ? 1.209   -30.726  1.230   1.00 33.87  ? 273 ALA   C N      1 
ATOM   8887  C  CA     . ALA   C 1  273 ? 2.663   -30.689  1.136   1.00 31.27  ? 273 ALA   C CA     1 
ATOM   8888  C  C      . ALA   C 1  273 ? 3.149   -32.094  0.824   1.00 34.95  ? 273 ALA   C C      1 
ATOM   8889  O  O      . ALA   C 1  273 ? 2.492   -33.059  1.212   1.00 40.20  ? 273 ALA   C O      1 
ATOM   8890  C  CB     . ALA   C 1  273 ? 3.287   -30.178  2.432   1.00 26.58  ? 273 ALA   C CB     1 
ATOM   8891  N  N      . PRO   C 1  274 ? 4.253   -32.250  0.088   1.00 33.36  ? 274 PRO   C N      1 
ATOM   8892  C  CA     . PRO   C 1  274 ? 5.110   -31.240  -0.499  1.00 34.66  ? 274 PRO   C CA     1 
ATOM   8893  C  C      . PRO   C 1  274 ? 4.649   -30.846  -1.888  1.00 36.03  ? 274 PRO   C C      1 
ATOM   8894  O  O      . PRO   C 1  274 ? 4.371   -31.709  -2.716  1.00 35.52  ? 274 PRO   C O      1 
ATOM   8895  C  CB     . PRO   C 1  274 ? 6.455   -31.956  -0.574  1.00 34.15  ? 274 PRO   C CB     1 
ATOM   8896  C  CG     . PRO   C 1  274 ? 6.054   -33.321  -0.959  1.00 31.94  ? 274 PRO   C CG     1 
ATOM   8897  C  CD     . PRO   C 1  274 ? 4.787   -33.590  -0.183  1.00 32.43  ? 274 PRO   C CD     1 
ATOM   8898  N  N      . VAL   C 1  275 ? 4.604   -29.548  -2.165  1.00 37.95  ? 275 VAL   C N      1 
ATOM   8899  C  CA     . VAL   C 1  275 ? 4.519   -29.032  -3.524  1.00 41.71  ? 275 VAL   C CA     1 
ATOM   8900  C  C      . VAL   C 1  275 ? 5.931   -28.610  -3.915  1.00 42.97  ? 275 VAL   C C      1 
ATOM   8901  O  O      . VAL   C 1  275 ? 6.423   -27.552  -3.519  1.00 40.61  ? 275 VAL   C O      1 
ATOM   8902  C  CB     . VAL   C 1  275 ? 3.538   -27.870  -3.638  1.00 39.37  ? 275 VAL   C CB     1 
ATOM   8903  C  CG1    . VAL   C 1  275 ? 3.587   -27.301  -5.031  1.00 39.45  ? 275 VAL   C CG1    1 
ATOM   8904  C  CG2    . VAL   C 1  275 ? 2.157   -28.336  -3.284  1.00 44.04  ? 275 VAL   C CG2    1 
ATOM   8905  N  N      . ILE   C 1  276 ? 6.584   -29.435  -4.708  1.00 41.85  ? 276 ILE   C N      1 
ATOM   8906  C  CA     . ILE   C 1  276 ? 7.995   -29.271  -4.982  1.00 40.67  ? 276 ILE   C CA     1 
ATOM   8907  C  C      . ILE   C 1  276 ? 8.229   -29.645  -6.429  1.00 43.14  ? 276 ILE   C C      1 
ATOM   8908  O  O      . ILE   C 1  276 ? 7.564   -30.532  -6.969  1.00 46.99  ? 276 ILE   C O      1 
ATOM   8909  C  CB     . ILE   C 1  276 ? 8.828   -30.142  -4.025  1.00 42.95  ? 276 ILE   C CB     1 
ATOM   8910  C  CG1    . ILE   C 1  276 ? 10.303  -29.992  -4.302  1.00 43.93  ? 276 ILE   C CG1    1 
ATOM   8911  C  CG2    . ILE   C 1  276 ? 8.437   -31.598  -4.114  1.00 44.19  ? 276 ILE   C CG2    1 
ATOM   8912  C  CD1    . ILE   C 1  276 ? 11.107  -30.725  -3.280  1.00 50.65  ? 276 ILE   C CD1    1 
ATOM   8913  N  N      . SER   C 1  277 ? 9.173   -28.964  -7.057  1.00 44.49  ? 277 SER   C N      1 
ATOM   8914  C  CA     . SER   C 1  277 ? 9.498   -29.245  -8.447  1.00 45.09  ? 277 SER   C CA     1 
ATOM   8915  C  C      . SER   C 1  277 ? 10.551  -30.349  -8.568  1.00 47.92  ? 277 SER   C C      1 
ATOM   8916  O  O      . SER   C 1  277 ? 11.320  -30.619  -7.643  1.00 46.94  ? 277 SER   C O      1 
ATOM   8917  C  CB     . SER   C 1  277 ? 9.987   -27.978  -9.136  1.00 51.50  ? 277 SER   C CB     1 
ATOM   8918  O  OG     . SER   C 1  277 ? 11.340  -27.718  -8.826  1.00 53.93  ? 277 SER   C OG     1 
ATOM   8919  N  N      . ALA   C 1  278 ? 10.579  -30.986  -9.745  1.00 47.76  ? 278 ALA   C N      1 
ATOM   8920  C  CA     . ALA   C 1  278 ? 11.483  -32.115  -9.968  1.00 43.04  ? 278 ALA   C CA     1 
ATOM   8921  C  C      . ALA   C 1  278 ? 12.923  -31.772  -9.602  1.00 47.86  ? 278 ALA   C C      1 
ATOM   8922  O  O      . ALA   C 1  278 ? 13.587  -32.509  -8.870  1.00 46.11  ? 278 ALA   C O      1 
ATOM   8923  C  CB     . ALA   C 1  278 ? 11.402  -32.562  -11.420 1.00 33.22  ? 278 ALA   C CB     1 
ATOM   8924  N  N      . GLU   C 1  279 ? 13.430  -30.665  -10.135 1.00 50.84  ? 279 GLU   C N      1 
ATOM   8925  C  CA     . GLU   C 1  279 ? 14.782  -30.225  -9.819  1.00 46.54  ? 279 GLU   C CA     1 
ATOM   8926  C  C      . GLU   C 1  279 ? 15.019  -30.191  -8.322  1.00 46.72  ? 279 GLU   C C      1 
ATOM   8927  O  O      . GLU   C 1  279 ? 15.973  -30.796  -7.820  1.00 49.05  ? 279 GLU   C O      1 
ATOM   8928  C  CB     . GLU   C 1  279 ? 15.009  -28.842  -10.427 1.00 52.86  ? 279 GLU   C CB     1 
ATOM   8929  C  CG     . GLU   C 1  279 ? 14.892  -28.804  -11.946 1.00 58.13  ? 279 GLU   C CG     1 
ATOM   8930  C  CD     . GLU   C 1  279 ? 13.644  -28.094  -12.417 1.00 68.68  ? 279 GLU   C CD     1 
ATOM   8931  O  OE1    . GLU   C 1  279 ? 12.536  -28.685  -12.258 1.00 59.98  ? 279 GLU   C OE1    1 
ATOM   8932  O  OE2    . GLU   C 1  279 ? 13.775  -26.953  -12.928 1.00 76.32  ? 279 GLU   C OE2    1 
ATOM   8933  N  N      . LYS   C 1  280 ? 14.156  -29.473  -7.589  1.00 47.81  ? 280 LYS   C N      1 
ATOM   8934  C  CA     . LYS   C 1  280 ? 14.347  -29.275  -6.157  1.00 46.82  ? 280 LYS   C CA     1 
ATOM   8935  C  C      . LYS   C 1  280 ? 13.988  -30.518  -5.329  1.00 50.31  ? 280 LYS   C C      1 
ATOM   8936  O  O      . LYS   C 1  280 ? 14.382  -30.613  -4.164  1.00 52.80  ? 280 LYS   C O      1 
ATOM   8937  C  CB     . LYS   C 1  280 ? 13.548  -28.049  -5.705  1.00 35.67  ? 280 LYS   C CB     1 
ATOM   8938  N  N      . ALA   C 1  281 ? 13.280  -31.489  -5.904  1.00 53.94  ? 281 ALA   C N      1 
ATOM   8939  C  CA     . ALA   C 1  281 ? 12.973  -32.735  -5.211  1.00 51.21  ? 281 ALA   C CA     1 
ATOM   8940  C  C      . ALA   C 1  281 ? 14.046  -33.780  -5.408  1.00 49.81  ? 281 ALA   C C      1 
ATOM   8941  O  O      . ALA   C 1  281 ? 14.076  -34.769  -4.672  1.00 50.09  ? 281 ALA   C O      1 
ATOM   8942  C  CB     . ALA   C 1  281 ? 11.634  -33.305  -5.697  1.00 52.13  ? 281 ALA   C CB     1 
ATOM   8943  N  N      . TYR   C 1  282 ? 14.904  -33.577  -6.395  1.00 53.17  ? 282 TYR   C N      1 
ATOM   8944  C  CA     . TYR   C 1  282 ? 15.969  -34.514  -6.712  1.00 54.92  ? 282 TYR   C CA     1 
ATOM   8945  C  C      . TYR   C 1  282 ? 17.047  -34.435  -5.649  1.00 59.61  ? 282 TYR   C C      1 
ATOM   8946  O  O      . TYR   C 1  282 ? 17.501  -33.342  -5.293  1.00 67.38  ? 282 TYR   C O      1 
ATOM   8947  C  CB     . TYR   C 1  282 ? 16.530  -34.174  -8.085  1.00 56.00  ? 282 TYR   C CB     1 
ATOM   8948  C  CG     . TYR   C 1  282 ? 17.721  -34.960  -8.569  1.00 57.37  ? 282 TYR   C CG     1 
ATOM   8949  C  CD1    . TYR   C 1  282 ? 17.592  -36.258  -9.068  1.00 50.39  ? 282 TYR   C CD1    1 
ATOM   8950  C  CD2    . TYR   C 1  282 ? 18.990  -34.385  -8.539  1.00 60.27  ? 282 TYR   C CD2    1 
ATOM   8951  C  CE1    . TYR   C 1  282 ? 18.704  -36.955  -9.537  1.00 51.04  ? 282 TYR   C CE1    1 
ATOM   8952  C  CE2    . TYR   C 1  282 ? 20.096  -35.067  -8.992  1.00 58.77  ? 282 TYR   C CE2    1 
ATOM   8953  C  CZ     . TYR   C 1  282 ? 19.957  -36.349  -9.492  1.00 56.46  ? 282 TYR   C CZ     1 
ATOM   8954  O  OH     . TYR   C 1  282 ? 21.094  -36.998  -9.934  1.00 64.33  ? 282 TYR   C OH     1 
ATOM   8955  N  N      . HIS   C 1  283 ? 17.425  -35.598  -5.120  1.00 60.34  ? 283 HIS   C N      1 
ATOM   8956  C  CA     . HIS   C 1  283 ? 18.420  -35.728  -4.058  1.00 67.44  ? 283 HIS   C CA     1 
ATOM   8957  C  C      . HIS   C 1  283 ? 17.961  -35.207  -2.694  1.00 66.84  ? 283 HIS   C C      1 
ATOM   8958  O  O      . HIS   C 1  283 ? 18.619  -35.491  -1.687  1.00 65.50  ? 283 HIS   C O      1 
ATOM   8959  C  CB     . HIS   C 1  283 ? 19.729  -35.040  -4.452  1.00 72.21  ? 283 HIS   C CB     1 
ATOM   8960  C  CG     . HIS   C 1  283 ? 20.656  -35.923  -5.234  1.00 71.05  ? 283 HIS   C CG     1 
ATOM   8961  N  ND1    . HIS   C 1  283 ? 21.908  -35.514  -5.647  1.00 69.01  ? 283 HIS   C ND1    1 
ATOM   8962  C  CD2    . HIS   C 1  283 ? 20.493  -37.182  -5.713  1.00 63.53  ? 283 HIS   C CD2    1 
ATOM   8963  C  CE1    . HIS   C 1  283 ? 22.482  -36.489  -6.332  1.00 70.32  ? 283 HIS   C CE1    1 
ATOM   8964  N  NE2    . HIS   C 1  283 ? 21.643  -37.510  -6.390  1.00 68.28  ? 283 HIS   C NE2    1 
ATOM   8965  N  N      . GLU   C 1  284 ? 16.853  -34.464  -2.611  1.00 65.28  ? 284 GLU   C N      1 
ATOM   8966  C  CA     . GLU   C 1  284 ? 16.233  -34.202  -1.311  1.00 71.92  ? 284 GLU   C CA     1 
ATOM   8967  C  C      . GLU   C 1  284 ? 14.919  -34.962  -1.204  1.00 71.21  ? 284 GLU   C C      1 
ATOM   8968  O  O      . GLU   C 1  284 ? 13.933  -34.590  -1.844  1.00 79.10  ? 284 GLU   C O      1 
ATOM   8969  C  CB     . GLU   C 1  284 ? 15.991  -32.721  -1.050  1.00 67.33  ? 284 GLU   C CB     1 
ATOM   8970  C  CG     . GLU   C 1  284 ? 17.227  -31.888  -1.124  1.00 78.48  ? 284 GLU   C CG     1 
ATOM   8971  C  CD     . GLU   C 1  284 ? 17.024  -30.527  -0.481  1.00 92.34  ? 284 GLU   C CD     1 
ATOM   8972  O  OE1    . GLU   C 1  284 ? 15.925  -29.947  -0.622  1.00 85.55  ? 284 GLU   C OE1    1 
ATOM   8973  O  OE2    . GLU   C 1  284 ? 17.973  -30.035  0.172   1.00 106.23 ? 284 GLU   C OE2    1 
ATOM   8974  N  N      . GLN   C 1  285 ? 14.909  -36.010  -0.384  1.00 65.06  ? 285 GLN   C N      1 
ATOM   8975  C  CA     . GLN   C 1  285 ? 13.687  -36.676  0.039   1.00 62.66  ? 285 GLN   C CA     1 
ATOM   8976  C  C      . GLN   C 1  285 ? 13.147  -35.989  1.284   1.00 64.11  ? 285 GLN   C C      1 
ATOM   8977  O  O      . GLN   C 1  285 ? 13.880  -35.820  2.268   1.00 59.31  ? 285 GLN   C O      1 
ATOM   8978  C  CB     . GLN   C 1  285 ? 13.961  -38.144  0.346   1.00 63.60  ? 285 GLN   C CB     1 
ATOM   8979  C  CG     . GLN   C 1  285 ? 14.265  -38.988  -0.868  1.00 73.13  ? 285 GLN   C CG     1 
ATOM   8980  C  CD     . GLN   C 1  285 ? 13.037  -39.289  -1.713  1.00 82.35  ? 285 GLN   C CD     1 
ATOM   8981  O  OE1    . GLN   C 1  285 ? 11.891  -39.019  -1.319  1.00 88.42  ? 285 GLN   C OE1    1 
ATOM   8982  N  NE2    . GLN   C 1  285 ? 13.273  -39.870  -2.882  1.00 76.78  ? 285 GLN   C NE2    1 
ATOM   8983  N  N      . LEU   C 1  286 ? 11.871  -35.602  1.252   1.00 57.09  ? 286 LEU   C N      1 
ATOM   8984  C  CA     . LEU   C 1  286 ? 11.263  -34.974  2.417   1.00 53.75  ? 286 LEU   C CA     1 
ATOM   8985  C  C      . LEU   C 1  286 ? 10.577  -36.001  3.307   1.00 51.71  ? 286 LEU   C C      1 
ATOM   8986  O  O      . LEU   C 1  286 ? 9.853   -36.883  2.839   1.00 57.38  ? 286 LEU   C O      1 
ATOM   8987  C  CB     . LEU   C 1  286 ? 10.253  -33.898  2.038   1.00 56.68  ? 286 LEU   C CB     1 
ATOM   8988  C  CG     . LEU   C 1  286 ? 10.766  -32.632  1.366   1.00 58.26  ? 286 LEU   C CG     1 
ATOM   8989  C  CD1    . LEU   C 1  286 ? 10.239  -32.575  -0.087  1.00 58.12  ? 286 LEU   C CD1    1 
ATOM   8990  C  CD2    . LEU   C 1  286 ? 10.470  -31.364  2.194   1.00 50.14  ? 286 LEU   C CD2    1 
ATOM   8991  N  N      . SER   C 1  287 ? 10.786  -35.847  4.599   1.00 45.81  ? 287 SER   C N      1 
ATOM   8992  C  CA     . SER   C 1  287 ? 10.430  -36.836  5.589   1.00 45.29  ? 287 SER   C CA     1 
ATOM   8993  C  C      . SER   C 1  287 ? 9.038   -36.564  6.127   1.00 47.61  ? 287 SER   C C      1 
ATOM   8994  O  O      . SER   C 1  287 ? 8.479   -35.481  5.961   1.00 44.35  ? 287 SER   C O      1 
ATOM   8995  C  CB     . SER   C 1  287 ? 11.425  -36.788  6.724   1.00 40.64  ? 287 SER   C CB     1 
ATOM   8996  O  OG     . SER   C 1  287 ? 11.320  -35.525  7.335   1.00 37.25  ? 287 SER   C OG     1 
ATOM   8997  N  N      . VAL   C 1  288 ? 8.491   -37.562  6.820   1.00 44.43  ? 288 VAL   C N      1 
ATOM   8998  C  CA     . VAL   C 1  288 ? 7.183   -37.385  7.426   1.00 40.21  ? 288 VAL   C CA     1 
ATOM   8999  C  C      . VAL   C 1  288 ? 7.170   -36.202  8.393   1.00 45.44  ? 288 VAL   C C      1 
ATOM   9000  O  O      . VAL   C 1  288 ? 6.123   -35.572  8.597   1.00 45.87  ? 288 VAL   C O      1 
ATOM   9001  C  CB     . VAL   C 1  288 ? 6.735   -38.684  8.108   1.00 36.83  ? 288 VAL   C CB     1 
ATOM   9002  C  CG1    . VAL   C 1  288 ? 5.595   -38.398  9.031   1.00 37.35  ? 288 VAL   C CG1    1 
ATOM   9003  C  CG2    . VAL   C 1  288 ? 6.301   -39.672  7.070   1.00 43.04  ? 288 VAL   C CG2    1 
ATOM   9004  N  N      . ALA   C 1  289 ? 8.309   -35.858  8.997   1.00 43.44  ? 289 ALA   C N      1 
ATOM   9005  C  CA     . ALA   C 1  289 ? 8.278   -34.657  9.831   1.00 47.36  ? 289 ALA   C CA     1 
ATOM   9006  C  C      . ALA   C 1  289 ? 8.359   -33.377  9.011   1.00 48.52  ? 289 ALA   C C      1 
ATOM   9007  O  O      . ALA   C 1  289 ? 7.872   -32.324  9.446   1.00 47.37  ? 289 ALA   C O      1 
ATOM   9008  C  CB     . ALA   C 1  289 ? 9.409   -34.673  10.854  1.00 47.75  ? 289 ALA   C CB     1 
ATOM   9009  N  N      . GLU   C 1  290 ? 8.944   -33.447  7.823   1.00 46.41  ? 290 GLU   C N      1 
ATOM   9010  C  CA     . GLU   C 1  290 ? 9.089   -32.235  7.034   1.00 45.70  ? 290 GLU   C CA     1 
ATOM   9011  C  C      . GLU   C 1  290 ? 7.762   -31.843  6.403   1.00 44.60  ? 290 GLU   C C      1 
ATOM   9012  O  O      . GLU   C 1  290 ? 7.346   -30.672  6.470   1.00 40.38  ? 290 GLU   C O      1 
ATOM   9013  C  CB     . GLU   C 1  290 ? 10.203  -32.438  5.994   1.00 46.72  ? 290 GLU   C CB     1 
ATOM   9014  C  CG     . GLU   C 1  290 ? 11.505  -32.817  6.729   1.00 49.14  ? 290 GLU   C CG     1 
ATOM   9015  C  CD     . GLU   C 1  290 ? 12.751  -32.859  5.877   1.00 49.89  ? 290 GLU   C CD     1 
ATOM   9016  O  OE1    . GLU   C 1  290 ? 12.888  -33.740  5.001   1.00 53.49  ? 290 GLU   C OE1    1 
ATOM   9017  O  OE2    . GLU   C 1  290 ? 13.638  -32.011  6.140   1.00 56.19  ? 290 GLU   C OE2    1 
ATOM   9018  N  N      . ILE   C 1  291 ? 7.073   -32.831  5.828   1.00 44.56  ? 291 ILE   C N      1 
ATOM   9019  C  CA     . ILE   C 1  291 ? 5.795   -32.576  5.197   1.00 38.65  ? 291 ILE   C CA     1 
ATOM   9020  C  C      . ILE   C 1  291 ? 4.719   -32.294  6.238   1.00 43.39  ? 291 ILE   C C      1 
ATOM   9021  O  O      . ILE   C 1  291 ? 3.799   -31.506  5.977   1.00 42.67  ? 291 ILE   C O      1 
ATOM   9022  C  CB     . ILE   C 1  291 ? 5.424   -33.754  4.291   1.00 39.02  ? 291 ILE   C CB     1 
ATOM   9023  C  CG1    . ILE   C 1  291 ? 5.075   -34.989  5.116   1.00 32.96  ? 291 ILE   C CG1    1 
ATOM   9024  C  CG2    . ILE   C 1  291 ? 6.557   -34.059  3.324   1.00 41.81  ? 291 ILE   C CG2    1 
ATOM   9025  C  CD1    . ILE   C 1  291 ? 4.678   -36.131  4.244   1.00 37.78  ? 291 ILE   C CD1    1 
ATOM   9026  N  N      . THR   C 1  292 ? 4.800   -32.920  7.422   1.00 41.92  ? 292 THR   C N      1 
ATOM   9027  C  CA     . THR   C 1  292 ? 3.872   -32.570  8.493   1.00 43.11  ? 292 THR   C CA     1 
ATOM   9028  C  C      . THR   C 1  292 ? 4.036   -31.115  8.891   1.00 45.83  ? 292 THR   C C      1 
ATOM   9029  O  O      . THR   C 1  292 ? 3.050   -30.372  8.988   1.00 45.25  ? 292 THR   C O      1 
ATOM   9030  C  CB     . THR   C 1  292 ? 4.065   -33.489  9.701   1.00 43.97  ? 292 THR   C CB     1 
ATOM   9031  O  OG1    . THR   C 1  292 ? 3.932   -34.855  9.286   1.00 44.39  ? 292 THR   C OG1    1 
ATOM   9032  C  CG2    . THR   C 1  292 ? 3.065   -33.167  10.821  1.00 35.09  ? 292 THR   C CG2    1 
ATOM   9033  N  N      . ASN   C 1  293 ? 5.281   -30.687  9.114   1.00 44.27  ? 293 ASN   C N      1 
ATOM   9034  C  CA     . ASN   C 1  293 ? 5.536   -29.285  9.416   1.00 48.14  ? 293 ASN   C CA     1 
ATOM   9035  C  C      . ASN   C 1  293 ? 4.929   -28.362  8.372   1.00 51.32  ? 293 ASN   C C      1 
ATOM   9036  O  O      . ASN   C 1  293 ? 4.316   -27.341  8.712   1.00 50.91  ? 293 ASN   C O      1 
ATOM   9037  C  CB     . ASN   C 1  293 ? 7.032   -29.052  9.515   1.00 51.04  ? 293 ASN   C CB     1 
ATOM   9038  C  CG     . ASN   C 1  293 ? 7.498   -29.012  10.922  1.00 62.55  ? 293 ASN   C CG     1 
ATOM   9039  O  OD1    . ASN   C 1  293 ? 6.846   -28.404  11.786  1.00 67.42  ? 293 ASN   C OD1    1 
ATOM   9040  N  ND2    . ASN   C 1  293 ? 8.612   -29.694  11.195  1.00 62.26  ? 293 ASN   C ND2    1 
ATOM   9041  N  N      . ALA   C 1  294 ? 5.106   -28.702  7.093   1.00 49.60  ? 294 ALA   C N      1 
ATOM   9042  C  CA     . ALA   C 1  294 ? 4.577   -27.884  6.014   1.00 38.93  ? 294 ALA   C CA     1 
ATOM   9043  C  C      . ALA   C 1  294 ? 3.139   -27.477  6.275   1.00 42.00  ? 294 ALA   C C      1 
ATOM   9044  O  O      . ALA   C 1  294 ? 2.748   -26.340  5.995   1.00 46.02  ? 294 ALA   C O      1 
ATOM   9045  C  CB     . ALA   C 1  294 ? 4.691   -28.650  4.704   1.00 34.34  ? 294 ALA   C CB     1 
ATOM   9046  N  N      . CYS   C 1  295 ? 2.339   -28.390  6.825   1.00 41.31  ? 295 CYS   C N      1 
ATOM   9047  C  CA     . CYS   C 1  295 ? 0.914   -28.135  6.966   1.00 42.71  ? 295 CYS   C CA     1 
ATOM   9048  C  C      . CYS   C 1  295 ? 0.636   -26.934  7.839   1.00 45.45  ? 295 CYS   C C      1 
ATOM   9049  O  O      . CYS   C 1  295 ? -0.365  -26.241  7.641   1.00 52.08  ? 295 CYS   C O      1 
ATOM   9050  C  CB     . CYS   C 1  295 ? 0.228   -29.351  7.554   1.00 44.28  ? 295 CYS   C CB     1 
ATOM   9051  S  SG     . CYS   C 1  295 ? 0.376   -30.728  6.502   1.00 49.89  ? 295 CYS   C SG     1 
ATOM   9052  N  N      . PHE   C 1  296 ? 1.477   -26.687  8.828   1.00 44.27  ? 296 PHE   C N      1 
ATOM   9053  C  CA     . PHE   C 1  296 ? 1.279   -25.557  9.713   1.00 43.95  ? 296 PHE   C CA     1 
ATOM   9054  C  C      . PHE   C 1  296 ? 1.995   -24.319  9.233   1.00 43.39  ? 296 PHE   C C      1 
ATOM   9055  O  O      . PHE   C 1  296 ? 2.033   -23.334  9.963   1.00 51.19  ? 296 PHE   C O      1 
ATOM   9056  C  CB     . PHE   C 1  296 ? 1.692   -25.946  11.134  1.00 50.15  ? 296 PHE   C CB     1 
ATOM   9057  C  CG     . PHE   C 1  296 ? 0.885   -27.091  11.683  1.00 43.94  ? 296 PHE   C CG     1 
ATOM   9058  C  CD1    . PHE   C 1  296 ? 1.207   -28.406  11.376  1.00 40.26  ? 296 PHE   C CD1    1 
ATOM   9059  C  CD2    . PHE   C 1  296 ? -0.228  -26.839  12.476  1.00 41.74  ? 296 PHE   C CD2    1 
ATOM   9060  C  CE1    . PHE   C 1  296 ? 0.435   -29.449  11.850  1.00 36.65  ? 296 PHE   C CE1    1 
ATOM   9061  C  CE2    . PHE   C 1  296 ? -1.000  -27.865  12.950  1.00 39.95  ? 296 PHE   C CE2    1 
ATOM   9062  C  CZ     . PHE   C 1  296 ? -0.663  -29.185  12.636  1.00 39.74  ? 296 PHE   C CZ     1 
ATOM   9063  N  N      . GLU   C 1  297 ? 2.545   -24.340  8.018   1.00 44.57  ? 297 GLU   C N      1 
ATOM   9064  C  CA     . GLU   C 1  297 ? 3.043   -23.125  7.388   1.00 50.21  ? 297 GLU   C CA     1 
ATOM   9065  C  C      . GLU   C 1  297 ? 1.964   -22.467  6.547   1.00 48.51  ? 297 GLU   C C      1 
ATOM   9066  O  O      . GLU   C 1  297 ? 1.676   -22.953  5.436   1.00 42.42  ? 297 GLU   C O      1 
ATOM   9067  C  CB     . GLU   C 1  297 ? 4.272   -23.397  6.532   1.00 52.24  ? 297 GLU   C CB     1 
ATOM   9068  C  CG     . GLU   C 1  297 ? 5.484   -22.831  7.228   1.00 63.89  ? 297 GLU   C CG     1 
ATOM   9069  C  CD     . GLU   C 1  297 ? 5.408   -21.287  7.311   1.00 76.41  ? 297 GLU   C CD     1 
ATOM   9070  O  OE1    . GLU   C 1  297 ? 4.530   -20.653  6.634   1.00 63.86  ? 297 GLU   C OE1    1 
ATOM   9071  O  OE2    . GLU   C 1  297 ? 6.182   -20.721  8.126   1.00 76.83  ? 297 GLU   C OE2    1 
ATOM   9072  N  N      . PRO   C 1  298 ? 1.414   -21.309  6.980   1.00 47.45  ? 298 PRO   C N      1 
ATOM   9073  C  CA     . PRO   C 1  298 ? 0.269   -20.704  6.289   1.00 42.73  ? 298 PRO   C CA     1 
ATOM   9074  C  C      . PRO   C 1  298 ? 0.470   -20.544  4.798   1.00 39.26  ? 298 PRO   C C      1 
ATOM   9075  O  O      . PRO   C 1  298 ? -0.505  -20.460  4.056   1.00 42.60  ? 298 PRO   C O      1 
ATOM   9076  C  CB     . PRO   C 1  298 ? 0.144   -19.337  6.965   1.00 42.99  ? 298 PRO   C CB     1 
ATOM   9077  C  CG     . PRO   C 1  298 ? 0.671   -19.557  8.318   1.00 52.80  ? 298 PRO   C CG     1 
ATOM   9078  C  CD     . PRO   C 1  298 ? 1.855   -20.482  8.113   1.00 48.80  ? 298 PRO   C CD     1 
ATOM   9079  N  N      . ALA   C 1  299 ? 1.711   -20.502  4.340   1.00 41.17  ? 299 ALA   C N      1 
ATOM   9080  C  CA     . ALA   C 1  299 ? 1.989   -20.348  2.922   1.00 39.24  ? 299 ALA   C CA     1 
ATOM   9081  C  C      . ALA   C 1  299 ? 1.712   -21.605  2.105   1.00 45.05  ? 299 ALA   C C      1 
ATOM   9082  O  O      . ALA   C 1  299 ? 1.930   -21.576  0.889   1.00 50.69  ? 299 ALA   C O      1 
ATOM   9083  C  CB     . ALA   C 1  299 ? 3.444   -19.930  2.727   1.00 52.76  ? 299 ALA   C CB     1 
ATOM   9084  N  N      . ASN   C 1  300 ? 1.274   -22.706  2.728   1.00 42.09  ? 300 ASN   C N      1 
ATOM   9085  C  CA     . ASN   C 1  300 ? 0.902   -23.936  2.030   1.00 37.93  ? 300 ASN   C CA     1 
ATOM   9086  C  C      . ASN   C 1  300 ? -0.587  -24.207  2.084   1.00 40.21  ? 300 ASN   C C      1 
ATOM   9087  O  O      . ASN   C 1  300 ? -1.014  -25.321  1.759   1.00 42.51  ? 300 ASN   C O      1 
ATOM   9088  C  CB     . ASN   C 1  300 ? 1.635   -25.137  2.619   1.00 44.93  ? 300 ASN   C CB     1 
ATOM   9089  C  CG     . ASN   C 1  300 ? 3.120   -25.017  2.526   1.00 45.92  ? 300 ASN   C CG     1 
ATOM   9090  O  OD1    . ASN   C 1  300 ? 3.649   -24.559  1.510   1.00 46.05  ? 300 ASN   C OD1    1 
ATOM   9091  N  ND2    . ASN   C 1  300 ? 3.812   -25.363  3.615   1.00 43.63  ? 300 ASN   C ND2    1 
ATOM   9092  N  N      . GLN   C 1  301 ? -1.378  -23.232  2.522   1.00 40.41  ? 301 GLN   C N      1 
ATOM   9093  C  CA     . GLN   C 1  301 ? -2.817  -23.356  2.678   1.00 37.09  ? 301 GLN   C CA     1 
ATOM   9094  C  C      . GLN   C 1  301 ? -3.543  -23.063  1.377   1.00 34.51  ? 301 GLN   C C      1 
ATOM   9095  O  O      . GLN   C 1  301 ? -2.990  -22.596  0.391   1.00 35.41  ? 301 GLN   C O      1 
ATOM   9096  C  CB     . GLN   C 1  301 ? -3.326  -22.419  3.771   1.00 33.31  ? 301 GLN   C CB     1 
ATOM   9097  C  CG     . GLN   C 1  301 ? -2.492  -22.469  4.991   1.00 37.93  ? 301 GLN   C CG     1 
ATOM   9098  C  CD     . GLN   C 1  301 ? -3.022  -21.602  6.089   1.00 43.41  ? 301 GLN   C CD     1 
ATOM   9099  O  OE1    . GLN   C 1  301 ? -2.741  -21.829  7.268   1.00 55.21  ? 301 GLN   C OE1    1 
ATOM   9100  N  NE2    . GLN   C 1  301 ? -3.750  -20.562  5.713   1.00 40.01  ? 301 GLN   C NE2    1 
ATOM   9101  N  N      . MET   C 1  302 ? -4.819  -23.318  1.399   1.00 35.39  ? 302 MET   C N      1 
ATOM   9102  C  CA     . MET   C 1  302 ? -5.578  -23.255  0.186   1.00 34.20  ? 302 MET   C CA     1 
ATOM   9103  C  C      . MET   C 1  302 ? -6.500  -22.080  0.190   1.00 36.02  ? 302 MET   C C      1 
ATOM   9104  O  O      . MET   C 1  302 ? -6.916  -21.629  -0.877  1.00 43.40  ? 302 MET   C O      1 
ATOM   9105  C  CB     . MET   C 1  302 ? -6.393  -24.524  0.057   1.00 39.89  ? 302 MET   C CB     1 
ATOM   9106  C  CG     . MET   C 1  302 ? -5.482  -25.704  0.038   1.00 47.56  ? 302 MET   C CG     1 
ATOM   9107  S  SD     . MET   C 1  302 ? -5.796  -26.184  -1.604  1.00 73.38  ? 302 MET   C SD     1 
ATOM   9108  C  CE     . MET   C 1  302 ? -7.550  -26.528  -1.284  1.00 45.51  ? 302 MET   C CE     1 
ATOM   9109  N  N      . VAL   C 1  303 ? -6.858  -21.614  1.370   1.00 32.95  ? 303 VAL   C N      1 
ATOM   9110  C  CA     . VAL   C 1  303 ? -7.453  -20.312  1.552   1.00 35.42  ? 303 VAL   C CA     1 
ATOM   9111  C  C      . VAL   C 1  303 ? -6.415  -19.484  2.302   1.00 42.31  ? 303 VAL   C C      1 
ATOM   9112  O  O      . VAL   C 1  303 ? -5.790  -19.974  3.257   1.00 39.52  ? 303 VAL   C O      1 
ATOM   9113  C  CB     . VAL   C 1  303 ? -8.774  -20.427  2.320   1.00 30.86  ? 303 VAL   C CB     1 
ATOM   9114  C  CG1    . VAL   C 1  303 ? -9.380  -19.039  2.570   1.00 30.28  ? 303 VAL   C CG1    1 
ATOM   9115  C  CG2    . VAL   C 1  303 ? -9.699  -21.339  1.585   1.00 33.19  ? 303 VAL   C CG2    1 
ATOM   9116  N  N      . LYS   C 1  304 ? -6.175  -18.263  1.837   1.00 36.53  ? 304 LYS   C N      1 
ATOM   9117  C  CA     . LYS   C 1  304 ? -5.301  -17.363  2.575   1.00 34.99  ? 304 LYS   C CA     1 
ATOM   9118  C  C      . LYS   C 1  304 ? -6.016  -16.859  3.837   1.00 40.70  ? 304 LYS   C C      1 
ATOM   9119  O  O      . LYS   C 1  304 ? -6.954  -16.057  3.750   1.00 39.31  ? 304 LYS   C O      1 
ATOM   9120  C  CB     . LYS   C 1  304 ? -4.878  -16.228  1.655   1.00 28.29  ? 304 LYS   C CB     1 
ATOM   9121  C  CG     . LYS   C 1  304 ? -4.208  -16.749  0.426   1.00 31.03  ? 304 LYS   C CG     1 
ATOM   9122  C  CD     . LYS   C 1  304 ? -3.515  -15.699  -0.423  1.00 33.14  ? 304 LYS   C CD     1 
ATOM   9123  C  CE     . LYS   C 1  304 ? -2.252  -15.207  0.177   1.00 37.91  ? 304 LYS   C CE     1 
ATOM   9124  N  NZ     . LYS   C 1  304 ? -1.605  -14.204  -0.711  1.00 51.38  ? 304 LYS   C NZ     1 
ATOM   9125  N  N      . CYS   C 1  305 ? -5.588  -17.339  5.010   1.00 33.87  ? 305 CYS   C N      1 
ATOM   9126  C  CA     . CYS   C 1  305 ? -6.054  -16.829  6.299   1.00 40.69  ? 305 CYS   C CA     1 
ATOM   9127  C  C      . CYS   C 1  305 ? -4.935  -17.022  7.318   1.00 40.48  ? 305 CYS   C C      1 
ATOM   9128  O  O      . CYS   C 1  305 ? -3.907  -17.631  7.024   1.00 37.33  ? 305 CYS   C O      1 
ATOM   9129  C  CB     . CYS   C 1  305 ? -7.338  -17.543  6.736   1.00 42.25  ? 305 CYS   C CB     1 
ATOM   9130  S  SG     . CYS   C 1  305 ? -7.187  -19.383  6.683   1.00 39.51  ? 305 CYS   C SG     1 
ATOM   9131  N  N      . ASP   C 1  306 ? -5.129  -16.539  8.538   1.00 41.70  ? 306 ASP   C N      1 
ATOM   9132  C  CA     . ASP   C 1  306 ? -4.060  -16.821  9.488   1.00 45.71  ? 306 ASP   C CA     1 
ATOM   9133  C  C      . ASP   C 1  306 ? -4.544  -17.742  10.604  1.00 46.99  ? 306 ASP   C C      1 
ATOM   9134  O  O      . ASP   C 1  306 ? -5.165  -17.271  11.579  1.00 42.56  ? 306 ASP   C O      1 
ATOM   9135  C  CB     . ASP   C 1  306 ? -3.485  -15.541  10.084  1.00 49.20  ? 306 ASP   C CB     1 
ATOM   9136  C  CG     . ASP   C 1  306 ? -2.036  -15.722  10.443  1.00 56.81  ? 306 ASP   C CG     1 
ATOM   9137  O  OD1    . ASP   C 1  306 ? -1.663  -16.890  10.704  1.00 57.05  ? 306 ASP   C OD1    1 
ATOM   9138  O  OD2    . ASP   C 1  306 ? -1.281  -14.722  10.477  1.00 68.74  ? 306 ASP   C OD2    1 
ATOM   9139  N  N      . PRO   C 1  307 ? -4.265  -19.051  10.532  1.00 42.68  ? 307 PRO   C N      1 
ATOM   9140  C  CA     . PRO   C 1  307 ? -4.693  -19.916  11.630  1.00 43.17  ? 307 PRO   C CA     1 
ATOM   9141  C  C      . PRO   C 1  307 ? -4.110  -19.472  12.949  1.00 49.20  ? 307 PRO   C C      1 
ATOM   9142  O  O      . PRO   C 1  307 ? -4.834  -19.451  13.950  1.00 53.48  ? 307 PRO   C O      1 
ATOM   9143  C  CB     . PRO   C 1  307 ? -4.210  -21.305  11.189  1.00 37.26  ? 307 PRO   C CB     1 
ATOM   9144  C  CG     . PRO   C 1  307 ? -4.049  -21.217  9.754   1.00 33.60  ? 307 PRO   C CG     1 
ATOM   9145  C  CD     . PRO   C 1  307 ? -3.542  -19.824  9.513   1.00 40.96  ? 307 PRO   C CD     1 
ATOM   9146  N  N      . ARG   C 1  308 ? -2.837  -19.065  12.967  1.00 47.96  ? 308 ARG   C N      1 
ATOM   9147  C  CA     . ARG   C 1  308 ? -2.218  -18.588  14.197  1.00 50.71  ? 308 ARG   C CA     1 
ATOM   9148  C  C      . ARG   C 1  308 ? -3.046  -17.541  14.919  1.00 52.84  ? 308 ARG   C C      1 
ATOM   9149  O  O      . ARG   C 1  308 ? -3.028  -17.499  16.149  1.00 66.12  ? 308 ARG   C O      1 
ATOM   9150  C  CB     . ARG   C 1  308 ? -0.809  -18.058  13.914  1.00 53.80  ? 308 ARG   C CB     1 
ATOM   9151  C  CG     . ARG   C 1  308 ? 0.061   -19.148  13.362  1.00 64.73  ? 308 ARG   C CG     1 
ATOM   9152  C  CD     . ARG   C 1  308 ? 1.438   -18.733  12.907  1.00 69.72  ? 308 ARG   C CD     1 
ATOM   9153  N  NE     . ARG   C 1  308 ? 1.390   -17.912  11.706  1.00 74.19  ? 308 ARG   C NE     1 
ATOM   9154  C  CZ     . ARG   C 1  308 ? 2.440   -17.676  10.933  1.00 72.49  ? 308 ARG   C CZ     1 
ATOM   9155  N  NH1    . ARG   C 1  308 ? 3.603   -18.275  11.147  1.00 66.03  ? 308 ARG   C NH1    1 
ATOM   9156  N  NH2    . ARG   C 1  308 ? 2.311   -16.853  9.897   1.00 69.42  ? 308 ARG   C NH2    1 
ATOM   9157  N  N      . HIS   C 1  309 ? -3.787  -16.701  14.212  1.00 50.24  ? 309 HIS   C N      1 
ATOM   9158  C  CA     . HIS   C 1  309 ? -4.556  -15.680  14.913  1.00 58.37  ? 309 HIS   C CA     1 
ATOM   9159  C  C      . HIS   C 1  309 ? -6.037  -16.052  14.995  1.00 57.93  ? 309 HIS   C C      1 
ATOM   9160  O  O      . HIS   C 1  309 ? -6.903  -15.180  15.105  1.00 63.42  ? 309 HIS   C O      1 
ATOM   9161  C  CB     . HIS   C 1  309 ? -4.328  -14.286  14.301  1.00 57.47  ? 309 HIS   C CB     1 
ATOM   9162  C  CG     . HIS   C 1  309 ? -2.886  -13.838  14.336  1.00 63.29  ? 309 HIS   C CG     1 
ATOM   9163  N  ND1    . HIS   C 1  309 ? -2.114  -13.692  13.201  1.00 69.46  ? 309 HIS   C ND1    1 
ATOM   9164  C  CD2    . HIS   C 1  309 ? -2.054  -13.585  15.378  1.00 67.81  ? 309 HIS   C CD2    1 
ATOM   9165  C  CE1    . HIS   C 1  309 ? -0.885  -13.333  13.540  1.00 66.69  ? 309 HIS   C CE1    1 
ATOM   9166  N  NE2    . HIS   C 1  309 ? -0.821  -13.268  14.858  1.00 66.02  ? 309 HIS   C NE2    1 
ATOM   9167  N  N      . GLY   C 1  310 ? -6.331  -17.354  14.996  1.00 52.34  ? 310 GLY   C N      1 
ATOM   9168  C  CA     . GLY   C 1  310 ? -7.673  -17.895  15.189  1.00 49.30  ? 310 GLY   C CA     1 
ATOM   9169  C  C      . GLY   C 1  310 ? -7.613  -19.165  16.019  1.00 50.77  ? 310 GLY   C C      1 
ATOM   9170  O  O      . GLY   C 1  310 ? -6.558  -19.445  16.590  1.00 55.90  ? 310 GLY   C O      1 
ATOM   9171  N  N      . LYS   C 1  311 ? -8.682  -19.955  16.102  1.00 45.41  ? 311 LYS   C N      1 
ATOM   9172  C  CA     . LYS   C 1  311 ? -8.706  -21.132  16.967  1.00 40.16  ? 311 LYS   C CA     1 
ATOM   9173  C  C      . LYS   C 1  311 ? -9.121  -22.386  16.208  1.00 38.52  ? 311 LYS   C C      1 
ATOM   9174  O  O      . LYS   C 1  311 ? -10.018 -22.343  15.370  1.00 39.82  ? 311 LYS   C O      1 
ATOM   9175  C  CB     . LYS   C 1  311 ? -9.657  -20.940  18.140  1.00 36.08  ? 311 LYS   C CB     1 
ATOM   9176  C  CG     . LYS   C 1  311 ? -9.173  -19.976  19.154  1.00 43.99  ? 311 LYS   C CG     1 
ATOM   9177  C  CD     . LYS   C 1  311 ? -10.127 -19.937  20.312  1.00 47.00  ? 311 LYS   C CD     1 
ATOM   9178  C  CE     . LYS   C 1  311 ? -9.590  -19.076  21.433  1.00 51.33  ? 311 LYS   C CE     1 
ATOM   9179  N  NZ     . LYS   C 1  311 ? -10.675 -18.779  22.397  1.00 53.88  ? 311 LYS   C NZ     1 
ATOM   9180  N  N      . TYR   C 1  312 ? -8.523  -23.516  16.557  1.00 36.77  ? 312 TYR   C N      1 
ATOM   9181  C  CA     . TYR   C 1  312 ? -8.879  -24.771  15.926  1.00 36.81  ? 312 TYR   C CA     1 
ATOM   9182  C  C      . TYR   C 1  312 ? -10.064 -25.411  16.624  1.00 38.47  ? 312 TYR   C C      1 
ATOM   9183  O  O      . TYR   C 1  312 ? -10.150 -25.423  17.852  1.00 36.23  ? 312 TYR   C O      1 
ATOM   9184  C  CB     . TYR   C 1  312 ? -7.720  -25.744  15.959  1.00 36.57  ? 312 TYR   C CB     1 
ATOM   9185  C  CG     . TYR   C 1  312 ? -6.570  -25.370  15.070  1.00 38.24  ? 312 TYR   C CG     1 
ATOM   9186  C  CD1    . TYR   C 1  312 ? -5.617  -24.478  15.517  1.00 42.87  ? 312 TYR   C CD1    1 
ATOM   9187  C  CD2    . TYR   C 1  312 ? -6.396  -25.952  13.820  1.00 36.08  ? 312 TYR   C CD2    1 
ATOM   9188  C  CE1    . TYR   C 1  312 ? -4.545  -24.154  14.749  1.00 46.45  ? 312 TYR   C CE1    1 
ATOM   9189  C  CE2    . TYR   C 1  312 ? -5.322  -25.619  13.041  1.00 36.53  ? 312 TYR   C CE2    1 
ATOM   9190  C  CZ     . TYR   C 1  312 ? -4.399  -24.722  13.517  1.00 38.54  ? 312 TYR   C CZ     1 
ATOM   9191  O  OH     . TYR   C 1  312 ? -3.307  -24.359  12.786  1.00 46.95  ? 312 TYR   C OH     1 
ATOM   9192  N  N      . MET   C 1  313 ? -10.971 -25.955  15.825  1.00 41.77  ? 313 MET   C N      1 
ATOM   9193  C  CA     . MET   C 1  313 ? -12.044 -26.794  16.324  1.00 39.52  ? 313 MET   C CA     1 
ATOM   9194  C  C      . MET   C 1  313 ? -11.915 -28.213  15.823  1.00 37.47  ? 313 MET   C C      1 
ATOM   9195  O  O      . MET   C 1  313 ? -12.863 -28.990  15.953  1.00 39.56  ? 313 MET   C O      1 
ATOM   9196  C  CB     . MET   C 1  313 ? -13.412 -26.234  15.930  1.00 36.86  ? 313 MET   C CB     1 
ATOM   9197  C  CG     . MET   C 1  313 ? -13.574 -24.785  16.269  1.00 39.76  ? 313 MET   C CG     1 
ATOM   9198  S  SD     . MET   C 1  313 ? -15.123 -24.120  15.678  1.00 45.82  ? 313 MET   C SD     1 
ATOM   9199  C  CE     . MET   C 1  313 ? -14.541 -23.340  14.182  1.00 34.25  ? 313 MET   C CE     1 
ATOM   9200  N  N      . ALA   C 1  314 ? -10.772 -28.556  15.231  1.00 35.97  ? 314 ALA   C N      1 
ATOM   9201  C  CA     . ALA   C 1  314 ? -10.617 -29.822  14.521  1.00 38.28  ? 314 ALA   C CA     1 
ATOM   9202  C  C      . ALA   C 1  314 ? -9.374  -29.766  13.661  1.00 38.71  ? 314 ALA   C C      1 
ATOM   9203  O  O      . ALA   C 1  314 ? -9.024  -28.709  13.128  1.00 43.49  ? 314 ALA   C O      1 
ATOM   9204  C  CB     . ALA   C 1  314 ? -11.827 -30.147  13.635  1.00 35.48  ? 314 ALA   C CB     1 
ATOM   9205  N  N      . CYS   C 1  315 ? -8.721  -30.912  13.502  1.00 41.06  ? 315 CYS   C N      1 
ATOM   9206  C  CA     . CYS   C 1  315 ? -7.413  -31.000  12.854  1.00 35.27  ? 315 CYS   C CA     1 
ATOM   9207  C  C      . CYS   C 1  315 ? -7.155  -32.438  12.442  1.00 38.15  ? 315 CYS   C C      1 
ATOM   9208  O  O      . CYS   C 1  315 ? -7.054  -33.318  13.298  1.00 42.74  ? 315 CYS   C O      1 
ATOM   9209  C  CB     . CYS   C 1  315 ? -6.341  -30.500  13.790  1.00 40.65  ? 315 CYS   C CB     1 
ATOM   9210  S  SG     . CYS   C 1  315 ? -4.836  -30.212  12.966  1.00 51.14  ? 315 CYS   C SG     1 
ATOM   9211  N  N      . CYS   C 1  316 ? -7.058  -32.678  11.143  1.00 36.87  ? 316 CYS   C N      1 
ATOM   9212  C  CA     . CYS   C 1  316 ? -6.957  -34.021  10.598  1.00 37.48  ? 316 CYS   C CA     1 
ATOM   9213  C  C      . CYS   C 1  316 ? -5.746  -34.080  9.685   1.00 38.29  ? 316 CYS   C C      1 
ATOM   9214  O  O      . CYS   C 1  316 ? -5.481  -33.144  8.930   1.00 35.78  ? 316 CYS   C O      1 
ATOM   9215  C  CB     . CYS   C 1  316 ? -8.203  -34.369  9.803   1.00 37.55  ? 316 CYS   C CB     1 
ATOM   9216  S  SG     . CYS   C 1  316 ? -9.695  -34.143  10.771  1.00 53.55  ? 316 CYS   C SG     1 
ATOM   9217  N  N      . LEU   C 1  317 ? -5.007  -35.170  9.748   1.00 36.54  ? 317 LEU   C N      1 
ATOM   9218  C  CA     . LEU   C 1  317 ? -3.927  -35.375  8.804   1.00 34.80  ? 317 LEU   C CA     1 
ATOM   9219  C  C      . LEU   C 1  317 ? -4.248  -36.610  7.984   1.00 33.84  ? 317 LEU   C C      1 
ATOM   9220  O  O      . LEU   C 1  317 ? -4.523  -37.680  8.535   1.00 31.45  ? 317 LEU   C O      1 
ATOM   9221  C  CB     . LEU   C 1  317 ? -2.569  -35.480  9.514   1.00 37.53  ? 317 LEU   C CB     1 
ATOM   9222  C  CG     . LEU   C 1  317 ? -2.198  -34.178  10.245  1.00 39.76  ? 317 LEU   C CG     1 
ATOM   9223  C  CD1    . LEU   C 1  317 ? -1.049  -34.352  11.212  1.00 29.53  ? 317 LEU   C CD1    1 
ATOM   9224  C  CD2    . LEU   C 1  317 ? -1.918  -33.037  9.260   1.00 40.53  ? 317 LEU   C CD2    1 
ATOM   9225  N  N      . LEU   C 1  318 ? -4.240  -36.438  6.676   1.00 31.61  ? 318 LEU   C N      1 
ATOM   9226  C  CA     . LEU   C 1  318 ? -4.471  -37.510  5.716   1.00 36.69  ? 318 LEU   C CA     1 
ATOM   9227  C  C      . LEU   C 1  318 ? -3.157  -37.764  4.970   1.00 37.09  ? 318 LEU   C C      1 
ATOM   9228  O  O      . LEU   C 1  318 ? -2.828  -37.040  4.027   1.00 37.80  ? 318 LEU   C O      1 
ATOM   9229  C  CB     . LEU   C 1  318 ? -5.597  -37.129  4.753   1.00 32.02  ? 318 LEU   C CB     1 
ATOM   9230  C  CG     . LEU   C 1  318 ? -7.026  -36.970  5.260   1.00 27.30  ? 318 LEU   C CG     1 
ATOM   9231  C  CD1    . LEU   C 1  318 ? -7.106  -35.981  6.354   1.00 32.57  ? 318 LEU   C CD1    1 
ATOM   9232  C  CD2    . LEU   C 1  318 ? -7.854  -36.485  4.125   1.00 34.02  ? 318 LEU   C CD2    1 
ATOM   9233  N  N      . TYR   C 1  319 ? -2.404  -38.783  5.395   1.00 35.09  ? 319 TYR   C N      1 
ATOM   9234  C  CA     . TYR   C 1  319 ? -1.127  -39.129  4.781   1.00 34.17  ? 319 TYR   C CA     1 
ATOM   9235  C  C      . TYR   C 1  319 ? -1.364  -40.153  3.693   1.00 32.40  ? 319 TYR   C C      1 
ATOM   9236  O  O      . TYR   C 1  319 ? -2.216  -41.026  3.833   1.00 36.24  ? 319 TYR   C O      1 
ATOM   9237  C  CB     . TYR   C 1  319 ? -0.151  -39.711  5.806   1.00 36.85  ? 319 TYR   C CB     1 
ATOM   9238  C  CG     . TYR   C 1  319 ? 0.298   -38.745  6.888   1.00 33.91  ? 319 TYR   C CG     1 
ATOM   9239  C  CD1    . TYR   C 1  319 ? 1.396   -37.933  6.710   1.00 32.66  ? 319 TYR   C CD1    1 
ATOM   9240  C  CD2    . TYR   C 1  319 ? -0.396  -38.652  8.094   1.00 33.33  ? 319 TYR   C CD2    1 
ATOM   9241  C  CE1    . TYR   C 1  319 ? 1.807   -37.046  7.718   1.00 40.43  ? 319 TYR   C CE1    1 
ATOM   9242  C  CE2    . TYR   C 1  319 ? -0.010  -37.770  9.103   1.00 33.68  ? 319 TYR   C CE2    1 
ATOM   9243  C  CZ     . TYR   C 1  319 ? 1.094   -36.972  8.917   1.00 40.57  ? 319 TYR   C CZ     1 
ATOM   9244  O  OH     . TYR   C 1  319 ? 1.492   -36.102  9.915   1.00 33.57  ? 319 TYR   C OH     1 
ATOM   9245  N  N      . ARG   C 1  320 ? -0.624  -40.037  2.599   1.00 35.24  ? 320 ARG   C N      1 
ATOM   9246  C  CA     . ARG   C 1  320 ? -0.603  -41.101  1.614   1.00 39.62  ? 320 ARG   C CA     1 
ATOM   9247  C  C      . ARG   C 1  320 ? 0.828   -41.407  1.222   1.00 42.75  ? 320 ARG   C C      1 
ATOM   9248  O  O      . ARG   C 1  320 ? 1.714   -40.556  1.306   1.00 40.80  ? 320 ARG   C O      1 
ATOM   9249  C  CB     . ARG   C 1  320 ? -1.389  -40.796  0.352   1.00 39.22  ? 320 ARG   C CB     1 
ATOM   9250  C  CG     . ARG   C 1  320 ? -0.797  -39.786  -0.581  1.00 43.54  ? 320 ARG   C CG     1 
ATOM   9251  C  CD     . ARG   C 1  320 ? -1.930  -39.337  -1.468  1.00 44.83  ? 320 ARG   C CD     1 
ATOM   9252  N  NE     . ARG   C 1  320 ? -2.429  -40.478  -2.221  1.00 48.63  ? 320 ARG   C NE     1 
ATOM   9253  C  CZ     . ARG   C 1  320 ? -3.354  -40.396  -3.165  1.00 49.51  ? 320 ARG   C CZ     1 
ATOM   9254  N  NH1    . ARG   C 1  320 ? -3.956  -39.251  -3.436  1.00 45.61  ? 320 ARG   C NH1    1 
ATOM   9255  N  NH2    . ARG   C 1  320 ? -3.708  -41.495  -3.831  1.00 48.80  ? 320 ARG   C NH2    1 
ATOM   9256  N  N      . GLY   C 1  321 ? 1.031   -42.647  0.805   1.00 41.87  ? 321 GLY   C N      1 
ATOM   9257  C  CA     . GLY   C 1  321 ? 2.330   -43.146  0.459   1.00 41.08  ? 321 GLY   C CA     1 
ATOM   9258  C  C      . GLY   C 1  321 ? 3.077   -43.726  1.632   1.00 42.91  ? 321 GLY   C C      1 
ATOM   9259  O  O      . GLY   C 1  321 ? 2.505   -44.405  2.488   1.00 44.79  ? 321 GLY   C O      1 
ATOM   9260  N  N      . ASP   C 1  322 ? 4.376   -43.434  1.675   1.00 47.31  ? 322 ASP   C N      1 
ATOM   9261  C  CA     . ASP   C 1  322 ? 5.322   -44.128  2.541   1.00 43.16  ? 322 ASP   C CA     1 
ATOM   9262  C  C      . ASP   C 1  322 ? 5.325   -43.465  3.920   1.00 45.26  ? 322 ASP   C C      1 
ATOM   9263  O  O      . ASP   C 1  322 ? 6.162   -42.611  4.236   1.00 46.56  ? 322 ASP   C O      1 
ATOM   9264  C  CB     . ASP   C 1  322 ? 6.691   -44.125  1.881   1.00 40.88  ? 322 ASP   C CB     1 
ATOM   9265  C  CG     . ASP   C 1  322 ? 7.727   -44.815  2.706   1.00 48.93  ? 322 ASP   C CG     1 
ATOM   9266  O  OD1    . ASP   C 1  322 ? 7.379   -45.884  3.262   1.00 46.12  ? 322 ASP   C OD1    1 
ATOM   9267  O  OD2    . ASP   C 1  322 ? 8.881   -44.319  2.758   1.00 47.47  ? 322 ASP   C OD2    1 
ATOM   9268  N  N      . VAL   C 1  323 ? 4.362   -43.867  4.755   1.00 37.33  ? 323 VAL   C N      1 
ATOM   9269  C  CA     . VAL   C 1  323 ? 4.203   -43.308  6.095   1.00 42.45  ? 323 VAL   C CA     1 
ATOM   9270  C  C      . VAL   C 1  323 ? 3.758   -44.408  7.046   1.00 49.54  ? 323 VAL   C C      1 
ATOM   9271  O  O      . VAL   C 1  323 ? 2.985   -45.296  6.663   1.00 49.72  ? 323 VAL   C O      1 
ATOM   9272  C  CB     . VAL   C 1  323 ? 3.188   -42.150  6.123   1.00 38.87  ? 323 VAL   C CB     1 
ATOM   9273  C  CG1    . VAL   C 1  323 ? 2.897   -41.746  7.566   1.00 37.26  ? 323 VAL   C CG1    1 
ATOM   9274  C  CG2    . VAL   C 1  323 ? 3.695   -40.991  5.322   1.00 34.15  ? 323 VAL   C CG2    1 
ATOM   9275  N  N      . VAL   C 1  324 ? 4.241   -44.345  8.289   1.00 44.44  ? 324 VAL   C N      1 
ATOM   9276  C  CA     . VAL   C 1  324 ? 3.912   -45.339  9.306   1.00 37.76  ? 324 VAL   C CA     1 
ATOM   9277  C  C      . VAL   C 1  324 ? 3.509   -44.565  10.541  1.00 41.55  ? 324 VAL   C C      1 
ATOM   9278  O  O      . VAL   C 1  324 ? 4.088   -43.504  10.796  1.00 41.83  ? 324 VAL   C O      1 
ATOM   9279  C  CB     . VAL   C 1  324 ? 5.103   -46.225  9.652   1.00 34.91  ? 324 VAL   C CB     1 
ATOM   9280  C  CG1    . VAL   C 1  324 ? 5.608   -46.953  8.425   1.00 30.77  ? 324 VAL   C CG1    1 
ATOM   9281  C  CG2    . VAL   C 1  324 ? 6.152   -45.376  10.313  1.00 39.73  ? 324 VAL   C CG2    1 
ATOM   9282  N  N      . PRO   C 1  325 ? 2.578   -45.061  11.351  1.00 45.84  ? 325 PRO   C N      1 
ATOM   9283  C  CA     . PRO   C 1  325 ? 2.117   -44.254  12.495  1.00 40.73  ? 325 PRO   C CA     1 
ATOM   9284  C  C      . PRO   C 1  325 ? 3.220   -43.776  13.431  1.00 44.07  ? 325 PRO   C C      1 
ATOM   9285  O  O      . PRO   C 1  325 ? 3.122   -42.635  13.900  1.00 42.68  ? 325 PRO   C O      1 
ATOM   9286  C  CB     . PRO   C 1  325 ? 1.096   -45.175  13.175  1.00 36.55  ? 325 PRO   C CB     1 
ATOM   9287  C  CG     . PRO   C 1  325 ? 0.534   -45.965  12.038  1.00 47.16  ? 325 PRO   C CG     1 
ATOM   9288  C  CD     . PRO   C 1  325 ? 1.724   -46.238  11.126  1.00 45.95  ? 325 PRO   C CD     1 
ATOM   9289  N  N      . LYS   C 1  326 ? 4.264   -44.573  13.704  1.00 46.60  ? 326 LYS   C N      1 
ATOM   9290  C  CA     . LYS   C 1  326 ? 5.353   -44.106  14.575  1.00 47.33  ? 326 LYS   C CA     1 
ATOM   9291  C  C      . LYS   C 1  326 ? 5.855   -42.723  14.173  1.00 43.16  ? 326 LYS   C C      1 
ATOM   9292  O  O      . LYS   C 1  326 ? 5.927   -41.810  15.007  1.00 41.59  ? 326 LYS   C O      1 
ATOM   9293  C  CB     . LYS   C 1  326 ? 6.535   -45.082  14.563  1.00 51.66  ? 326 LYS   C CB     1 
ATOM   9294  C  CG     . LYS   C 1  326 ? 7.710   -44.562  15.405  1.00 58.02  ? 326 LYS   C CG     1 
ATOM   9295  C  CD     . LYS   C 1  326 ? 8.932   -45.488  15.486  1.00 65.62  ? 326 LYS   C CD     1 
ATOM   9296  C  CE     . LYS   C 1  326 ? 9.682   -45.575  14.159  1.00 68.90  ? 326 LYS   C CE     1 
ATOM   9297  N  NZ     . LYS   C 1  326 ? 10.776  -46.594  14.183  1.00 88.25  ? 326 LYS   C NZ     1 
ATOM   9298  N  N      . ASP   C 1  327 ? 6.253   -42.570  12.905  1.00 39.29  ? 327 ASP   C N      1 
ATOM   9299  C  CA     . ASP   C 1  327 ? 6.754   -41.290  12.404  1.00 41.67  ? 327 ASP   C CA     1 
ATOM   9300  C  C      . ASP   C 1  327 ? 5.749   -40.177  12.660  1.00 43.80  ? 327 ASP   C C      1 
ATOM   9301  O  O      . ASP   C 1  327 ? 6.025   -39.217  13.386  1.00 45.49  ? 327 ASP   C O      1 
ATOM   9302  C  CB     . ASP   C 1  327 ? 7.032   -41.400  10.909  1.00 45.01  ? 327 ASP   C CB     1 
ATOM   9303  C  CG     . ASP   C 1  327 ? 8.036   -42.484  10.586  1.00 52.98  ? 327 ASP   C CG     1 
ATOM   9304  O  OD1    . ASP   C 1  327 ? 8.910   -42.734  11.457  1.00 43.32  ? 327 ASP   C OD1    1 
ATOM   9305  O  OD2    . ASP   C 1  327 ? 7.898   -43.108  9.488   1.00 54.26  ? 327 ASP   C OD2    1 
ATOM   9306  N  N      . VAL   C 1  328 ? 4.577   -40.294  12.049  1.00 42.45  ? 328 VAL   C N      1 
ATOM   9307  C  CA     . VAL   C 1  328 ? 3.445   -39.407  12.259  1.00 37.35  ? 328 VAL   C CA     1 
ATOM   9308  C  C      . VAL   C 1  328 ? 3.334   -38.957  13.704  1.00 43.08  ? 328 VAL   C C      1 
ATOM   9309  O  O      . VAL   C 1  328 ? 3.229   -37.758  13.993  1.00 46.43  ? 328 VAL   C O      1 
ATOM   9310  C  CB     . VAL   C 1  328 ? 2.156   -40.106  11.831  1.00 35.39  ? 328 VAL   C CB     1 
ATOM   9311  C  CG1    . VAL   C 1  328 ? 0.963   -39.264  12.250  1.00 36.78  ? 328 VAL   C CG1    1 
ATOM   9312  C  CG2    . VAL   C 1  328 ? 2.210   -40.353  10.333  1.00 37.02  ? 328 VAL   C CG2    1 
ATOM   9313  N  N      . ASN   C 1  329 ? 3.315   -39.912  14.628  1.00 41.34  ? 329 ASN   C N      1 
ATOM   9314  C  CA     . ASN   C 1  329 ? 3.222   -39.539  16.032  1.00 42.20  ? 329 ASN   C CA     1 
ATOM   9315  C  C      . ASN   C 1  329 ? 4.425   -38.713  16.458  1.00 45.05  ? 329 ASN   C C      1 
ATOM   9316  O  O      . ASN   C 1  329 ? 4.272   -37.642  17.052  1.00 47.15  ? 329 ASN   C O      1 
ATOM   9317  C  CB     . ASN   C 1  329 ? 3.065   -40.791  16.882  1.00 51.61  ? 329 ASN   C CB     1 
ATOM   9318  C  CG     . ASN   C 1  329 ? 1.761   -41.526  16.596  1.00 55.24  ? 329 ASN   C CG     1 
ATOM   9319  O  OD1    . ASN   C 1  329 ? 0.749   -40.895  16.244  1.00 54.61  ? 329 ASN   C OD1    1 
ATOM   9320  N  ND2    . ASN   C 1  329 ? 1.776   -42.866  16.740  1.00 47.95  ? 329 ASN   C ND2    1 
ATOM   9321  N  N      . ALA   C 1  330 ? 5.635   -39.179  16.141  1.00 44.89  ? 330 ALA   C N      1 
ATOM   9322  C  CA     . ALA   C 1  330 ? 6.825   -38.390  16.437  1.00 41.04  ? 330 ALA   C CA     1 
ATOM   9323  C  C      . ALA   C 1  330 ? 6.646   -36.944  15.994  1.00 46.69  ? 330 ALA   C C      1 
ATOM   9324  O  O      . ALA   C 1  330 ? 6.688   -36.013  16.808  1.00 45.85  ? 330 ALA   C O      1 
ATOM   9325  C  CB     . ALA   C 1  330 ? 8.025   -39.010  15.744  1.00 36.70  ? 330 ALA   C CB     1 
ATOM   9326  N  N      . ALA   C 1  331 ? 6.420   -36.759  14.689  1.00 47.11  ? 331 ALA   C N      1 
ATOM   9327  C  CA     . ALA   C 1  331 ? 6.288   -35.440  14.082  1.00 41.86  ? 331 ALA   C CA     1 
ATOM   9328  C  C      . ALA   C 1  331 ? 5.261   -34.584  14.798  1.00 45.84  ? 331 ALA   C C      1 
ATOM   9329  O  O      . ALA   C 1  331 ? 5.516   -33.420  15.113  1.00 49.72  ? 331 ALA   C O      1 
ATOM   9330  C  CB     . ALA   C 1  331 ? 5.909   -35.601  12.618  1.00 39.73  ? 331 ALA   C CB     1 
ATOM   9331  N  N      . ILE   C 1  332 ? 4.073   -35.135  15.040  1.00 48.95  ? 332 ILE   C N      1 
ATOM   9332  C  CA     . ILE   C 1  332 ? 3.023   -34.352  15.687  1.00 49.24  ? 332 ILE   C CA     1 
ATOM   9333  C  C      . ILE   C 1  332 ? 3.488   -33.863  17.050  1.00 52.74  ? 332 ILE   C C      1 
ATOM   9334  O  O      . ILE   C 1  332 ? 3.171   -32.738  17.467  1.00 51.55  ? 332 ILE   C O      1 
ATOM   9335  C  CB     . ILE   C 1  332 ? 1.735   -35.189  15.776  1.00 39.20  ? 332 ILE   C CB     1 
ATOM   9336  C  CG1    . ILE   C 1  332 ? 1.233   -35.475  14.367  1.00 36.33  ? 332 ILE   C CG1    1 
ATOM   9337  C  CG2    . ILE   C 1  332 ? 0.701   -34.470  16.595  1.00 43.51  ? 332 ILE   C CG2    1 
ATOM   9338  C  CD1    . ILE   C 1  332 ? -0.089  -36.123  14.291  1.00 42.42  ? 332 ILE   C CD1    1 
ATOM   9339  N  N      . ALA   C 1  333 ? 4.266   -34.691  17.752  1.00 54.46  ? 333 ALA   C N      1 
ATOM   9340  C  CA     . ALA   C 1  333 ? 4.776   -34.322  19.064  1.00 55.21  ? 333 ALA   C CA     1 
ATOM   9341  C  C      . ALA   C 1  333 ? 5.624   -33.066  18.980  1.00 62.10  ? 333 ALA   C C      1 
ATOM   9342  O  O      . ALA   C 1  333 ? 5.418   -32.106  19.734  1.00 70.51  ? 333 ALA   C O      1 
ATOM   9343  C  CB     . ALA   C 1  333 ? 5.586   -35.475  19.636  1.00 51.22  ? 333 ALA   C CB     1 
ATOM   9344  N  N      . THR   C 1  334 ? 6.589   -33.053  18.061  1.00 52.92  ? 334 THR   C N      1 
ATOM   9345  C  CA     . THR   C 1  334 ? 7.432   -31.877  17.926  1.00 58.31  ? 334 THR   C CA     1 
ATOM   9346  C  C      . THR   C 1  334 ? 6.600   -30.647  17.585  1.00 62.42  ? 334 THR   C C      1 
ATOM   9347  O  O      . THR   C 1  334 ? 6.773   -29.584  18.192  1.00 68.18  ? 334 THR   C O      1 
ATOM   9348  C  CB     . THR   C 1  334 ? 8.516   -32.125  16.880  1.00 61.03  ? 334 THR   C CB     1 
ATOM   9349  O  OG1    . THR   C 1  334 ? 7.911   -32.566  15.663  1.00 68.61  ? 334 THR   C OG1    1 
ATOM   9350  C  CG2    . THR   C 1  334 ? 9.494   -33.190  17.367  1.00 65.37  ? 334 THR   C CG2    1 
ATOM   9351  N  N      . ILE   C 1  335 ? 5.657   -30.782  16.653  1.00 58.80  ? 335 ILE   C N      1 
ATOM   9352  C  CA     . ILE   C 1  335 ? 4.872   -29.619  16.256  1.00 63.83  ? 335 ILE   C CA     1 
ATOM   9353  C  C      . ILE   C 1  335 ? 4.087   -29.060  17.435  1.00 67.99  ? 335 ILE   C C      1 
ATOM   9354  O  O      . ILE   C 1  335 ? 3.970   -27.836  17.590  1.00 65.54  ? 335 ILE   C O      1 
ATOM   9355  C  CB     . ILE   C 1  335 ? 3.951   -29.961  15.077  1.00 53.51  ? 335 ILE   C CB     1 
ATOM   9356  C  CG1    . ILE   C 1  335 ? 4.794   -30.159  13.818  1.00 53.89  ? 335 ILE   C CG1    1 
ATOM   9357  C  CG2    . ILE   C 1  335 ? 2.922   -28.868  14.913  1.00 51.13  ? 335 ILE   C CG2    1 
ATOM   9358  C  CD1    . ILE   C 1  335 ? 4.012   -30.631  12.608  1.00 53.39  ? 335 ILE   C CD1    1 
ATOM   9359  N  N      . LYS   C 1  336 ? 3.528   -29.934  18.282  1.00 65.43  ? 336 LYS   C N      1 
ATOM   9360  C  CA     . LYS   C 1  336 ? 2.686   -29.410  19.350  1.00 68.48  ? 336 LYS   C CA     1 
ATOM   9361  C  C      . LYS   C 1  336 ? 3.495   -28.594  20.353  1.00 76.39  ? 336 LYS   C C      1 
ATOM   9362  O  O      . LYS   C 1  336 ? 2.947   -27.672  20.972  1.00 80.51  ? 336 LYS   C O      1 
ATOM   9363  C  CB     . LYS   C 1  336 ? 1.906   -30.531  20.046  1.00 65.49  ? 336 LYS   C CB     1 
ATOM   9364  C  CG     . LYS   C 1  336 ? 0.676   -31.032  19.252  1.00 66.18  ? 336 LYS   C CG     1 
ATOM   9365  C  CD     . LYS   C 1  336 ? -0.065  -32.159  19.981  1.00 66.11  ? 336 LYS   C CD     1 
ATOM   9366  C  CE     . LYS   C 1  336 ? 0.921   -33.257  20.434  1.00 76.26  ? 336 LYS   C CE     1 
ATOM   9367  N  NZ     . LYS   C 1  336 ? 0.331   -34.634  20.600  1.00 77.99  ? 336 LYS   C NZ     1 
ATOM   9368  N  N      . THR   C 1  337 ? 4.797   -28.878  20.503  1.00 69.64  ? 337 THR   C N      1 
ATOM   9369  C  CA     . THR   C 1  337 ? 5.613   -27.999  21.338  1.00 74.85  ? 337 THR   C CA     1 
ATOM   9370  C  C      . THR   C 1  337 ? 6.013   -26.741  20.578  1.00 75.05  ? 337 THR   C C      1 
ATOM   9371  O  O      . THR   C 1  337 ? 5.935   -25.631  21.113  1.00 81.05  ? 337 THR   C O      1 
ATOM   9372  C  CB     . THR   C 1  337 ? 6.875   -28.711  21.830  1.00 77.05  ? 337 THR   C CB     1 
ATOM   9373  O  OG1    . THR   C 1  337 ? 7.771   -28.891  20.731  1.00 69.68  ? 337 THR   C OG1    1 
ATOM   9374  C  CG2    . THR   C 1  337 ? 6.537   -30.080  22.435  1.00 75.70  ? 337 THR   C CG2    1 
ATOM   9375  N  N      . LYS   C 1  338 ? 6.404   -26.893  19.320  1.00 73.27  ? 338 LYS   C N      1 
ATOM   9376  C  CA     . LYS   C 1  338 ? 7.067   -25.830  18.580  1.00 75.19  ? 338 LYS   C CA     1 
ATOM   9377  C  C      . LYS   C 1  338 ? 6.134   -24.964  17.735  1.00 79.21  ? 338 LYS   C C      1 
ATOM   9378  O  O      . LYS   C 1  338 ? 6.628   -24.047  17.061  1.00 82.24  ? 338 LYS   C O      1 
ATOM   9379  C  CB     . LYS   C 1  338 ? 8.159   -26.424  17.677  1.00 70.64  ? 338 LYS   C CB     1 
ATOM   9380  C  CG     . LYS   C 1  338 ? 9.338   -26.967  18.442  1.00 65.46  ? 338 LYS   C CG     1 
ATOM   9381  C  CD     . LYS   C 1  338 ? 10.304  -27.685  17.546  1.00 67.25  ? 338 LYS   C CD     1 
ATOM   9382  C  CE     . LYS   C 1  338 ? 11.564  -28.006  18.316  1.00 71.99  ? 338 LYS   C CE     1 
ATOM   9383  N  NZ     . LYS   C 1  338 ? 12.488  -26.813  18.286  1.00 84.19  ? 338 LYS   C NZ     1 
ATOM   9384  N  N      . ARG   C 1  339 ? 4.817   -25.209  17.723  1.00 77.86  ? 339 ARG   C N      1 
ATOM   9385  C  CA     . ARG   C 1  339 ? 3.935   -24.351  16.938  1.00 77.62  ? 339 ARG   C CA     1 
ATOM   9386  C  C      . ARG   C 1  339 ? 2.755   -23.844  17.756  1.00 76.94  ? 339 ARG   C C      1 
ATOM   9387  O  O      . ARG   C 1  339 ? 2.371   -24.406  18.797  1.00 71.48  ? 339 ARG   C O      1 
ATOM   9388  C  CB     . ARG   C 1  339 ? 3.399   -25.032  15.681  1.00 66.44  ? 339 ARG   C CB     1 
ATOM   9389  C  CG     . ARG   C 1  339 ? 4.445   -25.276  14.628  1.00 68.18  ? 339 ARG   C CG     1 
ATOM   9390  C  CD     . ARG   C 1  339 ? 3.863   -25.152  13.238  1.00 68.23  ? 339 ARG   C CD     1 
ATOM   9391  N  NE     . ARG   C 1  339 ? 4.824   -25.529  12.202  1.00 69.83  ? 339 ARG   C NE     1 
ATOM   9392  C  CZ     . ARG   C 1  339 ? 5.453   -24.688  11.391  1.00 73.94  ? 339 ARG   C CZ     1 
ATOM   9393  N  NH1    . ARG   C 1  339 ? 5.209   -23.383  11.419  1.00 75.27  ? 339 ARG   C NH1    1 
ATOM   9394  N  NH2    . ARG   C 1  339 ? 6.335   -25.171  10.517  1.00 69.65  ? 339 ARG   C NH2    1 
ATOM   9395  N  N      . SER   C 1  340 ? 2.202   -22.750  17.230  1.00 76.72  ? 340 SER   C N      1 
ATOM   9396  C  CA     . SER   C 1  340 ? 1.026   -22.054  17.746  1.00 84.60  ? 340 SER   C CA     1 
ATOM   9397  C  C      . SER   C 1  340 ? -0.228  -22.802  17.291  1.00 77.82  ? 340 SER   C C      1 
ATOM   9398  O  O      . SER   C 1  340 ? -0.712  -22.592  16.172  1.00 79.82  ? 340 SER   C O      1 
ATOM   9399  C  CB     . SER   C 1  340 ? 1.038   -20.610  17.234  1.00 80.35  ? 340 SER   C CB     1 
ATOM   9400  O  OG     . SER   C 1  340 ? -0.023  -19.816  17.771  1.00 83.15  ? 340 SER   C OG     1 
ATOM   9401  N  N      . ILE   C 1  341 ? -0.776  -23.680  18.137  1.00 56.99  ? 341 ILE   C N      1 
ATOM   9402  C  CA     . ILE   C 1  341 ? -1.951  -24.475  17.772  1.00 56.20  ? 341 ILE   C CA     1 
ATOM   9403  C  C      . ILE   C 1  341 ? -2.945  -24.379  18.924  1.00 56.21  ? 341 ILE   C C      1 
ATOM   9404  O  O      . ILE   C 1  341 ? -2.953  -25.225  19.819  1.00 56.29  ? 341 ILE   C O      1 
ATOM   9405  C  CB     . ILE   C 1  341 ? -1.615  -25.936  17.481  1.00 55.43  ? 341 ILE   C CB     1 
ATOM   9406  C  CG1    . ILE   C 1  341 ? -0.693  -26.054  16.276  1.00 56.89  ? 341 ILE   C CG1    1 
ATOM   9407  C  CG2    . ILE   C 1  341 ? -2.912  -26.690  17.199  1.00 51.64  ? 341 ILE   C CG2    1 
ATOM   9408  C  CD1    . ILE   C 1  341 ? 0.084   -27.376  16.230  1.00 53.32  ? 341 ILE   C CD1    1 
ATOM   9409  N  N      . GLN   C 1  342 ? -3.830  -23.394  18.880  1.00 50.65  ? 342 GLN   C N      1 
ATOM   9410  C  CA     . GLN   C 1  342 ? -4.732  -23.161  19.989  1.00 45.52  ? 342 GLN   C CA     1 
ATOM   9411  C  C      . GLN   C 1  342 ? -6.107  -23.719  19.647  1.00 42.93  ? 342 GLN   C C      1 
ATOM   9412  O  O      . GLN   C 1  342 ? -6.712  -23.298  18.659  1.00 44.13  ? 342 GLN   C O      1 
ATOM   9413  C  CB     . GLN   C 1  342 ? -4.824  -21.677  20.292  1.00 51.54  ? 342 GLN   C CB     1 
ATOM   9414  C  CG     . GLN   C 1  342 ? -5.308  -21.433  21.661  1.00 64.71  ? 342 GLN   C CG     1 
ATOM   9415  C  CD     . GLN   C 1  342 ? -4.159  -21.579  22.642  1.00 86.47  ? 342 GLN   C CD     1 
ATOM   9416  O  OE1    . GLN   C 1  342 ? -3.157  -20.858  22.546  1.00 87.32  ? 342 GLN   C OE1    1 
ATOM   9417  N  NE2    . GLN   C 1  342 ? -4.287  -22.521  23.587  1.00 83.06  ? 342 GLN   C NE2    1 
ATOM   9418  N  N      . PHE   C 1  343 ? -6.610  -24.651  20.464  1.00 39.06  ? 343 PHE   C N      1 
ATOM   9419  C  CA     . PHE   C 1  343 ? -7.958  -25.177  20.273  1.00 35.81  ? 343 PHE   C CA     1 
ATOM   9420  C  C      . PHE   C 1  343 ? -8.979  -24.384  21.078  1.00 36.62  ? 343 PHE   C C      1 
ATOM   9421  O  O      . PHE   C 1  343 ? -8.678  -23.867  22.154  1.00 38.31  ? 343 PHE   C O      1 
ATOM   9422  C  CB     . PHE   C 1  343 ? -8.063  -26.636  20.692  1.00 36.24  ? 343 PHE   C CB     1 
ATOM   9423  C  CG     . PHE   C 1  343 ? -7.576  -27.604  19.673  1.00 35.32  ? 343 PHE   C CG     1 
ATOM   9424  C  CD1    . PHE   C 1  343 ? -6.221  -27.830  19.503  1.00 40.78  ? 343 PHE   C CD1    1 
ATOM   9425  C  CD2    . PHE   C 1  343 ? -8.466  -28.268  18.859  1.00 35.12  ? 343 PHE   C CD2    1 
ATOM   9426  C  CE1    . PHE   C 1  343 ? -5.751  -28.729  18.546  1.00 42.16  ? 343 PHE   C CE1    1 
ATOM   9427  C  CE2    . PHE   C 1  343 ? -8.010  -29.167  17.892  1.00 41.27  ? 343 PHE   C CE2    1 
ATOM   9428  C  CZ     . PHE   C 1  343 ? -6.652  -29.401  17.735  1.00 40.95  ? 343 PHE   C CZ     1 
ATOM   9429  N  N      . VAL   C 1  344 ? -10.204 -24.306  20.566  1.00 37.78  ? 344 VAL   C N      1 
ATOM   9430  C  CA     . VAL   C 1  344 ? -11.292 -23.764  21.369  1.00 40.56  ? 344 VAL   C CA     1 
ATOM   9431  C  C      . VAL   C 1  344 ? -11.391 -24.614  22.632  1.00 41.84  ? 344 VAL   C C      1 
ATOM   9432  O  O      . VAL   C 1  344 ? -10.922 -25.762  22.668  1.00 35.47  ? 344 VAL   C O      1 
ATOM   9433  C  CB     . VAL   C 1  344 ? -12.628 -23.722  20.597  1.00 38.37  ? 344 VAL   C CB     1 
ATOM   9434  C  CG1    . VAL   C 1  344 ? -12.408 -23.034  19.286  1.00 44.78  ? 344 VAL   C CG1    1 
ATOM   9435  C  CG2    . VAL   C 1  344 ? -13.213 -25.106  20.381  1.00 32.65  ? 344 VAL   C CG2    1 
ATOM   9436  N  N      . ASP   C 1  345 ? -11.975 -24.055  23.688  1.00 39.56  ? 345 ASP   C N      1 
ATOM   9437  C  CA     . ASP   C 1  345 ? -11.991 -24.824  24.919  1.00 37.78  ? 345 ASP   C CA     1 
ATOM   9438  C  C      . ASP   C 1  345 ? -13.056 -25.897  24.932  1.00 40.97  ? 345 ASP   C C      1 
ATOM   9439  O  O      . ASP   C 1  345 ? -13.147 -26.632  25.914  1.00 49.16  ? 345 ASP   C O      1 
ATOM   9440  C  CB     . ASP   C 1  345 ? -12.201 -23.927  26.137  1.00 46.73  ? 345 ASP   C CB     1 
ATOM   9441  C  CG     . ASP   C 1  345 ? -13.561 -23.297  26.174  1.00 47.39  ? 345 ASP   C CG     1 
ATOM   9442  O  OD1    . ASP   C 1  345 ? -14.509 -23.870  25.577  1.00 43.82  ? 345 ASP   C OD1    1 
ATOM   9443  O  OD2    . ASP   C 1  345 ? -13.669 -22.217  26.810  1.00 50.12  ? 345 ASP   C OD2    1 
ATOM   9444  N  N      . TRP   C 1  346 ? -13.886 -25.998  23.909  1.00 39.38  ? 346 TRP   C N      1 
ATOM   9445  C  CA     . TRP   C 1  346 ? -14.963 -26.957  23.976  1.00 34.63  ? 346 TRP   C CA     1 
ATOM   9446  C  C      . TRP   C 1  346 ? -14.692 -28.203  23.162  1.00 37.36  ? 346 TRP   C C      1 
ATOM   9447  O  O      . TRP   C 1  346 ? -15.618 -28.988  22.951  1.00 45.78  ? 346 TRP   C O      1 
ATOM   9448  C  CB     . TRP   C 1  346 ? -16.297 -26.333  23.546  1.00 32.21  ? 346 TRP   C CB     1 
ATOM   9449  C  CG     . TRP   C 1  346 ? -16.280 -25.490  22.321  1.00 37.48  ? 346 TRP   C CG     1 
ATOM   9450  C  CD1    . TRP   C 1  346 ? -16.129 -24.133  22.260  1.00 37.31  ? 346 TRP   C CD1    1 
ATOM   9451  C  CD2    . TRP   C 1  346 ? -16.409 -25.940  20.960  1.00 38.23  ? 346 TRP   C CD2    1 
ATOM   9452  N  NE1    . TRP   C 1  346 ? -16.177 -23.704  20.957  1.00 33.68  ? 346 TRP   C NE1    1 
ATOM   9453  C  CE2    . TRP   C 1  346 ? -16.340 -24.789  20.135  1.00 36.77  ? 346 TRP   C CE2    1 
ATOM   9454  C  CE3    . TRP   C 1  346 ? -16.582 -27.200  20.358  1.00 34.26  ? 346 TRP   C CE3    1 
ATOM   9455  C  CZ2    . TRP   C 1  346 ? -16.435 -24.859  18.738  1.00 34.48  ? 346 TRP   C CZ2    1 
ATOM   9456  C  CZ3    . TRP   C 1  346 ? -16.674 -27.267  18.977  1.00 38.69  ? 346 TRP   C CZ3    1 
ATOM   9457  C  CH2    . TRP   C 1  346 ? -16.607 -26.093  18.178  1.00 35.05  ? 346 TRP   C CH2    1 
ATOM   9458  N  N      . CYS   C 1  347 ? -13.472 -28.430  22.691  1.00 33.53  ? 347 CYS   C N      1 
ATOM   9459  C  CA     . CYS   C 1  347 ? -13.292 -29.659  21.928  1.00 38.54  ? 347 CYS   C CA     1 
ATOM   9460  C  C      . CYS   C 1  347 ? -11.871 -30.167  22.099  1.00 39.18  ? 347 CYS   C C      1 
ATOM   9461  O  O      . CYS   C 1  347 ? -10.934 -29.373  22.242  1.00 42.21  ? 347 CYS   C O      1 
ATOM   9462  C  CB     . CYS   C 1  347 ? -13.596 -29.470  20.437  1.00 41.99  ? 347 CYS   C CB     1 
ATOM   9463  S  SG     . CYS   C 1  347 ? -12.250 -28.796  19.502  1.00 58.52  ? 347 CYS   C SG     1 
ATOM   9464  N  N      . PRO   C 1  348 ? -11.672 -31.482  22.021  1.00 40.22  ? 348 PRO   C N      1 
ATOM   9465  C  CA     . PRO   C 1  348 ? -10.363 -32.067  22.327  1.00 38.05  ? 348 PRO   C CA     1 
ATOM   9466  C  C      . PRO   C 1  348 ? -9.324  -31.590  21.330  1.00 44.98  ? 348 PRO   C C      1 
ATOM   9467  O  O      . PRO   C 1  348 ? -9.653  -31.101  20.240  1.00 46.86  ? 348 PRO   C O      1 
ATOM   9468  C  CB     . PRO   C 1  348 ? -10.595 -33.570  22.163  1.00 32.11  ? 348 PRO   C CB     1 
ATOM   9469  C  CG     . PRO   C 1  348 ? -12.082 -33.726  21.849  1.00 39.11  ? 348 PRO   C CG     1 
ATOM   9470  C  CD     . PRO   C 1  348 ? -12.533 -32.429  21.298  1.00 38.59  ? 348 PRO   C CD     1 
ATOM   9471  N  N      . THR   C 1  349 ? -8.048  -31.777  21.684  1.00 35.64  ? 349 THR   C N      1 
ATOM   9472  C  CA     . THR   C 1  349 ? -6.983  -31.279  20.831  1.00 38.51  ? 349 THR   C CA     1 
ATOM   9473  C  C      . THR   C 1  349 ? -6.229  -32.382  20.092  1.00 36.33  ? 349 THR   C C      1 
ATOM   9474  O  O      . THR   C 1  349 ? -5.277  -32.092  19.373  1.00 45.46  ? 349 THR   C O      1 
ATOM   9475  C  CB     . THR   C 1  349 ? -6.027  -30.393  21.641  1.00 36.71  ? 349 THR   C CB     1 
ATOM   9476  O  OG1    . THR   C 1  349 ? -5.348  -31.168  22.617  1.00 34.46  ? 349 THR   C OG1    1 
ATOM   9477  C  CG2    . THR   C 1  349 ? -6.808  -29.342  22.359  1.00 33.36  ? 349 THR   C CG2    1 
ATOM   9478  N  N      . GLY   C 1  350 ? -6.668  -33.623  20.174  1.00 31.56  ? 350 GLY   C N      1 
ATOM   9479  C  CA     . GLY   C 1  350 ? -5.970  -34.677  19.456  1.00 41.63  ? 350 GLY   C CA     1 
ATOM   9480  C  C      . GLY   C 1  350 ? -6.192  -34.619  17.953  1.00 38.74  ? 350 GLY   C C      1 
ATOM   9481  O  O      . GLY   C 1  350 ? -7.284  -34.312  17.476  1.00 45.94  ? 350 GLY   C O      1 
ATOM   9482  N  N      . PHE   C 1  351 ? -5.149  -34.959  17.202  1.00 34.64  ? 351 PHE   C N      1 
ATOM   9483  C  CA     . PHE   C 1  351 ? -5.178  -34.885  15.748  1.00 36.03  ? 351 PHE   C CA     1 
ATOM   9484  C  C      . PHE   C 1  351 ? -5.628  -36.203  15.136  1.00 37.78  ? 351 PHE   C C      1 
ATOM   9485  O  O      . PHE   C 1  351 ? -5.016  -37.249  15.379  1.00 46.27  ? 351 PHE   C O      1 
ATOM   9486  C  CB     . PHE   C 1  351 ? -3.801  -34.556  15.186  1.00 44.29  ? 351 PHE   C CB     1 
ATOM   9487  C  CG     . PHE   C 1  351 ? -3.328  -33.198  15.503  1.00 47.71  ? 351 PHE   C CG     1 
ATOM   9488  C  CD1    . PHE   C 1  351 ? -4.069  -32.366  16.309  1.00 49.19  ? 351 PHE   C CD1    1 
ATOM   9489  C  CD2    . PHE   C 1  351 ? -2.147  -32.732  14.956  1.00 46.79  ? 351 PHE   C CD2    1 
ATOM   9490  C  CE1    . PHE   C 1  351 ? -3.618  -31.091  16.607  1.00 55.41  ? 351 PHE   C CE1    1 
ATOM   9491  C  CE2    . PHE   C 1  351 ? -1.700  -31.458  15.232  1.00 49.71  ? 351 PHE   C CE2    1 
ATOM   9492  C  CZ     . PHE   C 1  351 ? -2.430  -30.633  16.064  1.00 51.83  ? 351 PHE   C CZ     1 
ATOM   9493  N  N      . LYS   C 1  352 ? -6.641  -36.140  14.278  1.00 35.07  ? 352 LYS   C N      1 
ATOM   9494  C  CA     . LYS   C 1  352 ? -7.138  -37.333  13.619  1.00 31.92  ? 352 LYS   C CA     1 
ATOM   9495  C  C      . LYS   C 1  352 ? -6.303  -37.623  12.389  1.00 37.58  ? 352 LYS   C C      1 
ATOM   9496  O  O      . LYS   C 1  352 ? -6.026  -36.728  11.582  1.00 41.62  ? 352 LYS   C O      1 
ATOM   9497  C  CB     . LYS   C 1  352 ? -8.619  -37.172  13.278  1.00 36.69  ? 352 LYS   C CB     1 
ATOM   9498  C  CG     . LYS   C 1  352 ? -9.316  -38.508  13.227  1.00 36.97  ? 352 LYS   C CG     1 
ATOM   9499  C  CD     . LYS   C 1  352 ? -10.644 -38.496  12.519  1.00 44.35  ? 352 LYS   C CD     1 
ATOM   9500  C  CE     . LYS   C 1  352 ? -11.222 -39.915  12.389  1.00 46.10  ? 352 LYS   C CE     1 
ATOM   9501  N  NZ     . LYS   C 1  352 ? -10.132 -40.937  12.276  1.00 43.55  ? 352 LYS   C NZ     1 
ATOM   9502  N  N      . VAL   C 1  353 ? -5.892  -38.876  12.257  1.00 40.01  ? 353 VAL   C N      1 
ATOM   9503  C  CA     . VAL   C 1  353 ? -4.850  -39.282  11.320  1.00 35.34  ? 353 VAL   C CA     1 
ATOM   9504  C  C      . VAL   C 1  353 ? -5.307  -40.460  10.477  1.00 37.54  ? 353 VAL   C C      1 
ATOM   9505  O  O      . VAL   C 1  353 ? -5.935  -41.402  10.969  1.00 43.89  ? 353 VAL   C O      1 
ATOM   9506  C  CB     . VAL   C 1  353 ? -3.552  -39.652  12.053  1.00 31.45  ? 353 VAL   C CB     1 
ATOM   9507  C  CG1    . VAL   C 1  353 ? -2.556  -40.246  11.071  1.00 29.74  ? 353 VAL   C CG1    1 
ATOM   9508  C  CG2    . VAL   C 1  353 ? -2.989  -38.428  12.799  1.00 29.25  ? 353 VAL   C CG2    1 
ATOM   9509  N  N      . GLY   C 1  354 ? -4.976  -40.412  9.203   1.00 36.67  ? 354 GLY   C N      1 
ATOM   9510  C  CA     . GLY   C 1  354 ? -5.241  -41.525  8.332   1.00 36.55  ? 354 GLY   C CA     1 
ATOM   9511  C  C      . GLY   C 1  354 ? -4.054  -41.676  7.416   1.00 40.56  ? 354 GLY   C C      1 
ATOM   9512  O  O      . GLY   C 1  354 ? -3.292  -40.729  7.202   1.00 41.02  ? 354 GLY   C O      1 
ATOM   9513  N  N      . ILE   C 1  355 ? -3.895  -42.890  6.896   1.00 39.36  ? 355 ILE   C N      1 
ATOM   9514  C  CA     . ILE   C 1  355 ? -2.779  -43.218  6.029   1.00 35.36  ? 355 ILE   C CA     1 
ATOM   9515  C  C      . ILE   C 1  355 ? -3.303  -44.089  4.910   1.00 42.11  ? 355 ILE   C C      1 
ATOM   9516  O  O      . ILE   C 1  355 ? -3.940  -45.111  5.167   1.00 51.53  ? 355 ILE   C O      1 
ATOM   9517  C  CB     . ILE   C 1  355 ? -1.631  -43.910  6.790   1.00 40.73  ? 355 ILE   C CB     1 
ATOM   9518  C  CG1    . ILE   C 1  355 ? -1.135  -43.031  7.956   1.00 33.05  ? 355 ILE   C CG1    1 
ATOM   9519  C  CG2    . ILE   C 1  355 ? -0.541  -44.326  5.845   1.00 44.40  ? 355 ILE   C CG2    1 
ATOM   9520  C  CD1    . ILE   C 1  355 ? 0.070   -43.535  8.655   1.00 31.72  ? 355 ILE   C CD1    1 
ATOM   9521  N  N      . ASN   C 1  356 ? -3.105  -43.647  3.673   1.00 47.94  ? 356 ASN   C N      1 
ATOM   9522  C  CA     . ASN   C 1  356 ? -3.215  -44.497  2.496   1.00 52.32  ? 356 ASN   C CA     1 
ATOM   9523  C  C      . ASN   C 1  356 ? -1.829  -44.803  1.983   1.00 47.73  ? 356 ASN   C C      1 
ATOM   9524  O  O      . ASN   C 1  356 ? -0.958  -43.943  2.000   1.00 48.79  ? 356 ASN   C O      1 
ATOM   9525  C  CB     . ASN   C 1  356 ? -4.044  -43.859  1.392   1.00 49.86  ? 356 ASN   C CB     1 
ATOM   9526  C  CG     . ASN   C 1  356 ? -5.512  -44.010  1.648   1.00 56.75  ? 356 ASN   C CG     1 
ATOM   9527  O  OD1    . ASN   C 1  356 ? -6.131  -44.950  1.149   1.00 63.75  ? 356 ASN   C OD1    1 
ATOM   9528  N  ND2    . ASN   C 1  356 ? -6.070  -43.139  2.483   1.00 58.43  ? 356 ASN   C ND2    1 
ATOM   9529  N  N      . TYR   C 1  357 ? -1.608  -46.034  1.581   1.00 49.07  ? 357 TYR   C N      1 
ATOM   9530  C  CA     . TYR   C 1  357 ? -0.240  -46.366  1.262   1.00 47.26  ? 357 TYR   C CA     1 
ATOM   9531  C  C      . TYR   C 1  357 ? 0.063   -46.069  -0.178  1.00 50.65  ? 357 TYR   C C      1 
ATOM   9532  O  O      . TYR   C 1  357 ? 1.194   -45.699  -0.505  1.00 53.45  ? 357 TYR   C O      1 
ATOM   9533  C  CB     . TYR   C 1  357 ? 0.033   -47.820  1.629   1.00 54.58  ? 357 TYR   C CB     1 
ATOM   9534  C  CG     . TYR   C 1  357 ? 0.120   -47.988  3.142   1.00 63.65  ? 357 TYR   C CG     1 
ATOM   9535  C  CD1    . TYR   C 1  357 ? 0.813   -47.056  3.923   1.00 62.84  ? 357 TYR   C CD1    1 
ATOM   9536  C  CD2    . TYR   C 1  357 ? -0.536  -49.029  3.797   1.00 68.23  ? 357 TYR   C CD2    1 
ATOM   9537  C  CE1    . TYR   C 1  357 ? 0.887   -47.183  5.310   1.00 64.77  ? 357 TYR   C CE1    1 
ATOM   9538  C  CE2    . TYR   C 1  357 ? -0.472  -49.161  5.185   1.00 67.36  ? 357 TYR   C CE2    1 
ATOM   9539  C  CZ     . TYR   C 1  357 ? 0.235   -48.232  5.932   1.00 66.41  ? 357 TYR   C CZ     1 
ATOM   9540  O  OH     . TYR   C 1  357 ? 0.302   -48.356  7.299   1.00 64.34  ? 357 TYR   C OH     1 
ATOM   9541  N  N      . GLN   C 1  358 ? -0.942  -46.155  -1.020  1.00 56.43  ? 358 GLN   C N      1 
ATOM   9542  C  CA     . GLN   C 1  358 ? -0.823  -45.850  -2.434  1.00 56.86  ? 358 GLN   C CA     1 
ATOM   9543  C  C      . GLN   C 1  358 ? -0.160  -44.483  -2.531  1.00 59.60  ? 358 GLN   C C      1 
ATOM   9544  O  O      . GLN   C 1  358 ? -0.771  -43.479  -2.123  1.00 58.25  ? 358 GLN   C O      1 
ATOM   9545  C  CB     . GLN   C 1  358 ? -2.204  -45.855  -3.101  1.00 53.09  ? 358 GLN   C CB     1 
ATOM   9546  C  CG     . GLN   C 1  358 ? -2.799  -47.265  -3.295  1.00 60.61  ? 358 GLN   C CG     1 
ATOM   9547  C  CD     . GLN   C 1  358 ? -3.460  -47.883  -2.017  1.00 68.06  ? 358 GLN   C CD     1 
ATOM   9548  O  OE1    . GLN   C 1  358 ? -3.545  -47.256  -0.936  1.00 67.55  ? 358 GLN   C OE1    1 
ATOM   9549  N  NE2    . GLN   C 1  358 ? -3.917  -49.131  -2.156  1.00 65.58  ? 358 GLN   C NE2    1 
ATOM   9550  N  N      . PRO   C 1  359 ? 1.078   -44.395  -3.029  1.00 62.50  ? 359 PRO   C N      1 
ATOM   9551  C  CA     . PRO   C 1  359 ? 1.781   -43.092  -3.052  1.00 56.75  ? 359 PRO   C CA     1 
ATOM   9552  C  C      . PRO   C 1  359 ? 1.141   -42.161  -4.061  1.00 50.64  ? 359 PRO   C C      1 
ATOM   9553  O  O      . PRO   C 1  359 ? 0.434   -42.596  -4.983  1.00 50.71  ? 359 PRO   C O      1 
ATOM   9554  C  CB     . PRO   C 1  359 ? 3.215   -43.452  -3.455  1.00 55.84  ? 359 PRO   C CB     1 
ATOM   9555  C  CG     . PRO   C 1  359 ? 3.061   -44.738  -4.237  1.00 65.75  ? 359 PRO   C CG     1 
ATOM   9556  C  CD     . PRO   C 1  359 ? 1.866   -45.470  -3.659  1.00 56.55  ? 359 PRO   C CD     1 
ATOM   9557  N  N      . PRO   C 1  360 ? 1.344   -40.871  -3.906  1.00 47.64  ? 360 PRO   C N      1 
ATOM   9558  C  CA     . PRO   C 1  360 ? 0.714   -39.921  -4.826  1.00 53.58  ? 360 PRO   C CA     1 
ATOM   9559  C  C      . PRO   C 1  360 ? 1.251   -40.092  -6.240  1.00 52.10  ? 360 PRO   C C      1 
ATOM   9560  O  O      . PRO   C 1  360 ? 2.399   -40.497  -6.450  1.00 53.98  ? 360 PRO   C O      1 
ATOM   9561  C  CB     . PRO   C 1  360 ? 1.078   -38.552  -4.231  1.00 52.76  ? 360 PRO   C CB     1 
ATOM   9562  C  CG     . PRO   C 1  360 ? 2.309   -38.814  -3.390  1.00 54.91  ? 360 PRO   C CG     1 
ATOM   9563  C  CD     . PRO   C 1  360 ? 2.182   -40.230  -2.883  1.00 50.59  ? 360 PRO   C CD     1 
ATOM   9564  N  N      . THR   C 1  361 ? 0.399   -39.817  -7.220  1.00 43.81  ? 361 THR   C N      1 
ATOM   9565  C  CA     . THR   C 1  361 ? 0.874   -39.826  -8.591  1.00 47.24  ? 361 THR   C CA     1 
ATOM   9566  C  C      . THR   C 1  361 ? 1.046   -38.406  -9.100  1.00 50.38  ? 361 THR   C C      1 
ATOM   9567  O  O      . THR   C 1  361 ? 0.584   -37.428  -8.506  1.00 46.51  ? 361 THR   C O      1 
ATOM   9568  C  CB     . THR   C 1  361 ? -0.065  -40.573  -9.541  1.00 51.84  ? 361 THR   C CB     1 
ATOM   9569  O  OG1    . THR   C 1  361 ? -0.527  -41.780  -8.934  1.00 50.73  ? 361 THR   C OG1    1 
ATOM   9570  C  CG2    . THR   C 1  361 ? 0.690   -40.927  -10.823 1.00 54.05  ? 361 THR   C CG2    1 
ATOM   9571  N  N      . VAL   C 1  362 ? 1.713   -38.311  -10.241 1.00 51.65  ? 362 VAL   C N      1 
ATOM   9572  C  CA     . VAL   C 1  362 ? 1.839   -37.062  -10.959 1.00 44.32  ? 362 VAL   C CA     1 
ATOM   9573  C  C      . VAL   C 1  362 ? 1.387   -37.336  -12.368 1.00 48.23  ? 362 VAL   C C      1 
ATOM   9574  O  O      . VAL   C 1  362 ? 1.481   -38.464  -12.854 1.00 45.42  ? 362 VAL   C O      1 
ATOM   9575  C  CB     . VAL   C 1  362 ? 3.271   -36.531  -10.964 1.00 43.08  ? 362 VAL   C CB     1 
ATOM   9576  C  CG1    . VAL   C 1  362 ? 3.596   -35.917  -9.641  1.00 45.05  ? 362 VAL   C CG1    1 
ATOM   9577  C  CG2    . VAL   C 1  362 ? 4.224   -37.675  -11.293 1.00 41.00  ? 362 VAL   C CG2    1 
ATOM   9578  N  N      . VAL   C 1  363 ? 0.874   -36.296  -13.001 1.00 49.23  ? 363 VAL   C N      1 
ATOM   9579  C  CA     . VAL   C 1  363 ? 0.540   -36.329  -14.419 1.00 47.33  ? 363 VAL   C CA     1 
ATOM   9580  C  C      . VAL   C 1  363 ? 1.802   -36.077  -15.237 1.00 54.64  ? 363 VAL   C C      1 
ATOM   9581  O  O      . VAL   C 1  363 ? 2.586   -35.186  -14.887 1.00 56.20  ? 363 VAL   C O      1 
ATOM   9582  C  CB     . VAL   C 1  363 ? -0.528  -35.306  -14.733 1.00 48.31  ? 363 VAL   C CB     1 
ATOM   9583  C  CG1    . VAL   C 1  363 ? -0.798  -35.307  -16.206 1.00 57.42  ? 363 VAL   C CG1    1 
ATOM   9584  C  CG2    . VAL   C 1  363 ? -1.799  -35.715  -14.021 1.00 45.13  ? 363 VAL   C CG2    1 
ATOM   9585  N  N      . PRO   C 1  364 ? 2.020   -36.860  -16.315 1.00 59.27  ? 364 PRO   C N      1 
ATOM   9586  C  CA     . PRO   C 1  364 ? 3.098   -36.590  -17.274 1.00 57.03  ? 364 PRO   C CA     1 
ATOM   9587  C  C      . PRO   C 1  364 ? 3.351   -35.122  -17.551 1.00 54.36  ? 364 PRO   C C      1 
ATOM   9588  O  O      . PRO   C 1  364 ? 2.420   -34.359  -17.822 1.00 54.01  ? 364 PRO   C O      1 
ATOM   9589  C  CB     . PRO   C 1  364 ? 2.597   -37.290  -18.546 1.00 56.66  ? 364 PRO   C CB     1 
ATOM   9590  C  CG     . PRO   C 1  364 ? 1.718   -38.366  -18.053 1.00 58.43  ? 364 PRO   C CG     1 
ATOM   9591  C  CD     . PRO   C 1  364 ? 1.037   -37.812  -16.859 1.00 60.01  ? 364 PRO   C CD     1 
ATOM   9592  N  N      . GLY   C 1  365 ? 4.621   -34.723  -17.515 1.00 58.65  ? 365 GLY   C N      1 
ATOM   9593  C  CA     . GLY   C 1  365 ? 4.948   -33.364  -17.879 1.00 61.27  ? 365 GLY   C CA     1 
ATOM   9594  C  C      . GLY   C 1  365 ? 4.349   -32.323  -16.969 1.00 63.98  ? 365 GLY   C C      1 
ATOM   9595  O  O      . GLY   C 1  365 ? 4.347   -31.140  -17.320 1.00 62.74  ? 365 GLY   C O      1 
ATOM   9596  N  N      . GLY   C 1  366 ? 3.811   -32.724  -15.822 1.00 65.20  ? 366 GLY   C N      1 
ATOM   9597  C  CA     . GLY   C 1  366 ? 3.396   -31.759  -14.835 1.00 61.98  ? 366 GLY   C CA     1 
ATOM   9598  C  C      . GLY   C 1  366 ? 4.601   -31.194  -14.123 1.00 57.66  ? 366 GLY   C C      1 
ATOM   9599  O  O      . GLY   C 1  366 ? 5.734   -31.647  -14.268 1.00 59.15  ? 366 GLY   C O      1 
ATOM   9600  N  N      . ASP   C 1  367 ? 4.351   -30.191  -13.311 1.00 48.21  ? 367 ASP   C N      1 
ATOM   9601  C  CA     . ASP   C 1  367 ? 5.456   -29.578  -12.617 1.00 51.39  ? 367 ASP   C CA     1 
ATOM   9602  C  C      . ASP   C 1  367 ? 5.680   -30.145  -11.215 1.00 56.80  ? 367 ASP   C C      1 
ATOM   9603  O  O      . ASP   C 1  367 ? 6.758   -29.926  -10.638 1.00 58.94  ? 367 ASP   C O      1 
ATOM   9604  C  CB     . ASP   C 1  367 ? 5.229   -28.073  -12.604 1.00 58.50  ? 367 ASP   C CB     1 
ATOM   9605  C  CG     . ASP   C 1  367 ? 4.956   -27.542  -13.992 1.00 66.95  ? 367 ASP   C CG     1 
ATOM   9606  O  OD1    . ASP   C 1  367 ? 3.785   -27.637  -14.423 1.00 70.51  ? 367 ASP   C OD1    1 
ATOM   9607  O  OD2    . ASP   C 1  367 ? 5.915   -27.080  -14.663 1.00 66.00  ? 367 ASP   C OD2    1 
ATOM   9608  N  N      . LEU   C 1  368 ? 4.724   -30.898  -10.671 1.00 46.81  ? 368 LEU   C N      1 
ATOM   9609  C  CA     . LEU   C 1  368 ? 4.931   -31.518  -9.373  1.00 42.67  ? 368 LEU   C CA     1 
ATOM   9610  C  C      . LEU   C 1  368 ? 5.933   -32.648  -9.464  1.00 42.47  ? 368 LEU   C C      1 
ATOM   9611  O  O      . LEU   C 1  368 ? 5.899   -33.464  -10.387 1.00 40.93  ? 368 LEU   C O      1 
ATOM   9612  C  CB     . LEU   C 1  368 ? 3.630   -32.062  -8.802  1.00 40.88  ? 368 LEU   C CB     1 
ATOM   9613  C  CG     . LEU   C 1  368 ? 2.838   -31.121  -7.927  1.00 41.16  ? 368 LEU   C CG     1 
ATOM   9614  C  CD1    . LEU   C 1  368 ? 1.511   -31.748  -7.555  1.00 37.34  ? 368 LEU   C CD1    1 
ATOM   9615  C  CD2    . LEU   C 1  368 ? 3.690   -30.870  -6.683  1.00 48.07  ? 368 LEU   C CD2    1 
ATOM   9616  N  N      . ALA   C 1  369 ? 6.842   -32.672  -8.503  1.00 39.41  ? 369 ALA   C N      1 
ATOM   9617  C  CA     . ALA   C 1  369 ? 7.734   -33.799  -8.367  1.00 38.81  ? 369 ALA   C CA     1 
ATOM   9618  C  C      . ALA   C 1  369 ? 6.927   -34.985  -7.895  1.00 41.42  ? 369 ALA   C C      1 
ATOM   9619  O  O      . ALA   C 1  369 ? 5.996   -34.846  -7.103  1.00 47.35  ? 369 ALA   C O      1 
ATOM   9620  C  CB     . ALA   C 1  369 ? 8.854   -33.489  -7.374  1.00 39.28  ? 369 ALA   C CB     1 
ATOM   9621  N  N      . LYS   C 1  370 ? 7.258   -36.159  -8.393  1.00 46.55  ? 370 LYS   C N      1 
ATOM   9622  C  CA     . LYS   C 1  370 ? 6.687   -37.356  -7.798  1.00 48.72  ? 370 LYS   C CA     1 
ATOM   9623  C  C      . LYS   C 1  370 ? 7.391   -37.570  -6.459  1.00 46.03  ? 370 LYS   C C      1 
ATOM   9624  O  O      . LYS   C 1  370 ? 8.604   -37.796  -6.416  1.00 47.61  ? 370 LYS   C O      1 
ATOM   9625  C  CB     . LYS   C 1  370 ? 6.834   -38.561  -8.730  1.00 42.47  ? 370 LYS   C CB     1 
ATOM   9626  C  CG     . LYS   C 1  370 ? 5.875   -39.684  -8.404  1.00 44.58  ? 370 LYS   C CG     1 
ATOM   9627  C  CD     . LYS   C 1  370 ? 5.989   -40.867  -9.341  1.00 51.78  ? 370 LYS   C CD     1 
ATOM   9628  C  CE     . LYS   C 1  370 ? 5.154   -42.027  -8.798  1.00 60.80  ? 370 LYS   C CE     1 
ATOM   9629  N  NZ     . LYS   C 1  370 ? 5.526   -43.366  -9.348  1.00 56.38  ? 370 LYS   C NZ     1 
ATOM   9630  N  N      . VAL   C 1  371 ? 6.660   -37.449  -5.376  1.00 44.56  ? 371 VAL   C N      1 
ATOM   9631  C  CA     . VAL   C 1  371 ? 7.234   -37.667  -4.055  1.00 49.00  ? 371 VAL   C CA     1 
ATOM   9632  C  C      . VAL   C 1  371 ? 6.846   -39.056  -3.565  1.00 49.77  ? 371 VAL   C C      1 
ATOM   9633  O  O      . VAL   C 1  371 ? 5.813   -39.615  -3.967  1.00 47.57  ? 371 VAL   C O      1 
ATOM   9634  C  CB     . VAL   C 1  371 ? 6.756   -36.581  -3.080  1.00 48.76  ? 371 VAL   C CB     1 
ATOM   9635  C  CG1    . VAL   C 1  371 ? 7.334   -35.240  -3.478  1.00 45.82  ? 371 VAL   C CG1    1 
ATOM   9636  C  CG2    . VAL   C 1  371 ? 5.244   -36.534  -3.089  1.00 53.30  ? 371 VAL   C CG2    1 
ATOM   9637  N  N      . GLN   C 1  372 ? 7.687   -39.630  -2.693  1.00 52.13  ? 372 GLN   C N      1 
ATOM   9638  C  CA     . GLN   C 1  372 ? 7.354   -40.921  -2.083  1.00 57.49  ? 372 GLN   C CA     1 
ATOM   9639  C  C      . GLN   C 1  372 ? 6.222   -40.822  -1.057  1.00 54.54  ? 372 GLN   C C      1 
ATOM   9640  O  O      . GLN   C 1  372 ? 5.461   -41.784  -0.896  1.00 51.68  ? 372 GLN   C O      1 
ATOM   9641  C  CB     . GLN   C 1  372 ? 8.573   -41.546  -1.406  1.00 53.77  ? 372 GLN   C CB     1 
ATOM   9642  C  CG     . GLN   C 1  372 ? 9.545   -42.313  -2.255  1.00 49.48  ? 372 GLN   C CG     1 
ATOM   9643  C  CD     . GLN   C 1  372 ? 10.757  -42.776  -1.412  1.00 62.11  ? 372 GLN   C CD     1 
ATOM   9644  O  OE1    . GLN   C 1  372 ? 11.312  -42.000  -0.606  1.00 58.05  ? 372 GLN   C OE1    1 
ATOM   9645  N  NE2    . GLN   C 1  372 ? 11.133  -44.059  -1.557  1.00 54.85  ? 372 GLN   C NE2    1 
ATOM   9646  N  N      . ARG   C 1  373 ? 6.116   -39.704  -0.336  1.00 50.34  ? 373 ARG   C N      1 
ATOM   9647  C  CA     . ARG   C 1  373 ? 5.058   -39.515  0.648   1.00 48.18  ? 373 ARG   C CA     1 
ATOM   9648  C  C      . ARG   C 1  373 ? 4.496   -38.097  0.585   1.00 45.87  ? 373 ARG   C C      1 
ATOM   9649  O  O      . ARG   C 1  373 ? 5.159   -37.159  0.147   1.00 50.08  ? 373 ARG   C O      1 
ATOM   9650  C  CB     . ARG   C 1  373 ? 5.549   -39.825  2.056   1.00 42.87  ? 373 ARG   C CB     1 
ATOM   9651  C  CG     . ARG   C 1  373 ? 6.608   -38.909  2.574   1.00 42.98  ? 373 ARG   C CG     1 
ATOM   9652  C  CD     . ARG   C 1  373 ? 7.306   -39.630  3.701   1.00 47.36  ? 373 ARG   C CD     1 
ATOM   9653  N  NE     . ARG   C 1  373 ? 7.927   -40.852  3.206   1.00 51.53  ? 373 ARG   C NE     1 
ATOM   9654  C  CZ     . ARG   C 1  373 ? 9.127   -40.910  2.650   1.00 52.26  ? 373 ARG   C CZ     1 
ATOM   9655  N  NH1    . ARG   C 1  373 ? 9.917   -39.848  2.595   1.00 47.53  ? 373 ARG   C NH1    1 
ATOM   9656  N  NH2    . ARG   C 1  373 ? 9.558   -42.069  2.163   1.00 51.10  ? 373 ARG   C NH2    1 
ATOM   9657  N  N      . ALA   C 1  374 ? 3.259   -37.950  1.047   1.00 40.89  ? 374 ALA   C N      1 
ATOM   9658  C  CA     . ALA   C 1  374 ? 2.537   -36.690  0.941   1.00 41.29  ? 374 ALA   C CA     1 
ATOM   9659  C  C      . ALA   C 1  374 ? 1.526   -36.606  2.079   1.00 37.90  ? 374 ALA   C C      1 
ATOM   9660  O  O      . ALA   C 1  374 ? 1.272   -37.589  2.772   1.00 40.11  ? 374 ALA   C O      1 
ATOM   9661  C  CB     . ALA   C 1  374 ? 1.849   -36.569  -0.416  1.00 39.33  ? 374 ALA   C CB     1 
ATOM   9662  N  N      . VAL   C 1  375 ? 0.945   -35.420  2.275   1.00 33.41  ? 375 VAL   C N      1 
ATOM   9663  C  CA     . VAL   C 1  375 ? -0.012  -35.203  3.359   1.00 33.89  ? 375 VAL   C CA     1 
ATOM   9664  C  C      . VAL   C 1  375 ? -0.945  -34.045  3.010   1.00 36.17  ? 375 VAL   C C      1 
ATOM   9665  O  O      . VAL   C 1  375 ? -0.540  -33.042  2.417   1.00 37.93  ? 375 VAL   C O      1 
ATOM   9666  C  CB     . VAL   C 1  375 ? 0.682   -34.930  4.716   1.00 34.82  ? 375 VAL   C CB     1 
ATOM   9667  C  CG1    . VAL   C 1  375 ? 1.561   -33.669  4.650   1.00 31.09  ? 375 VAL   C CG1    1 
ATOM   9668  C  CG2    . VAL   C 1  375 ? -0.357  -34.855  5.857   1.00 30.74  ? 375 VAL   C CG2    1 
ATOM   9669  N  N      . CYS   C 1  376 ? -2.203  -34.185  3.400   1.00 31.55  ? 376 CYS   C N      1 
ATOM   9670  C  CA     . CYS   C 1  376 ? -3.164  -33.104  3.334   1.00 30.49  ? 376 CYS   C CA     1 
ATOM   9671  C  C      . CYS   C 1  376 ? -3.802  -33.011  4.704   1.00 31.25  ? 376 CYS   C C      1 
ATOM   9672  O  O      . CYS   C 1  376 ? -4.272  -34.018  5.237   1.00 31.98  ? 376 CYS   C O      1 
ATOM   9673  C  CB     . CYS   C 1  376 ? -4.215  -33.351  2.254   1.00 34.22  ? 376 CYS   C CB     1 
ATOM   9674  S  SG     . CYS   C 1  376 ? -5.498  -32.116  2.155   1.00 38.00  ? 376 CYS   C SG     1 
ATOM   9675  N  N      . MET   C 1  377 ? -3.746  -31.827  5.292   1.00 28.51  ? 377 MET   C N      1 
ATOM   9676  C  CA     . MET   C 1  377 ? -4.357  -31.556  6.574   1.00 28.66  ? 377 MET   C CA     1 
ATOM   9677  C  C      . MET   C 1  377 ? -5.695  -30.870  6.328   1.00 34.35  ? 377 MET   C C      1 
ATOM   9678  O  O      . MET   C 1  377 ? -5.799  -29.970  5.481   1.00 37.86  ? 377 MET   C O      1 
ATOM   9679  C  CB     . MET   C 1  377 ? -3.452  -30.677  7.437   1.00 33.73  ? 377 MET   C CB     1 
ATOM   9680  C  CG     . MET   C 1  377 ? -4.048  -30.337  8.791   1.00 39.29  ? 377 MET   C CG     1 
ATOM   9681  S  SD     . MET   C 1  377 ? -2.932  -29.540  9.962   1.00 44.13  ? 377 MET   C SD     1 
ATOM   9682  C  CE     . MET   C 1  377 ? -2.919  -27.856  9.390   1.00 43.07  ? 377 MET   C CE     1 
ATOM   9683  N  N      . LEU   C 1  378 ? -6.726  -31.319  7.037   1.00 31.33  ? 378 LEU   C N      1 
ATOM   9684  C  CA     . LEU   C 1  378 ? -8.025  -30.672  7.021   1.00 27.30  ? 378 LEU   C CA     1 
ATOM   9685  C  C      . LEU   C 1  378 ? -8.289  -30.189  8.432   1.00 32.13  ? 378 LEU   C C      1 
ATOM   9686  O  O      . LEU   C 1  378 ? -8.278  -30.992  9.368   1.00 34.55  ? 378 LEU   C O      1 
ATOM   9687  C  CB     . LEU   C 1  378 ? -9.116  -31.634  6.576   1.00 30.08  ? 378 LEU   C CB     1 
ATOM   9688  C  CG     . LEU   C 1  378 ? -9.113  -32.256  5.204   1.00 28.56  ? 378 LEU   C CG     1 
ATOM   9689  C  CD1    . LEU   C 1  378 ? -10.275 -33.199  5.133   1.00 25.30  ? 378 LEU   C CD1    1 
ATOM   9690  C  CD2    . LEU   C 1  378 ? -9.258  -31.139  4.208   1.00 30.28  ? 378 LEU   C CD2    1 
ATOM   9691  N  N      . SER   C 1  379 ? -8.505  -28.887  8.590   1.00 32.56  ? 379 SER   C N      1 
ATOM   9692  C  CA     . SER   C 1  379 ? -8.755  -28.303  9.905   1.00 34.79  ? 379 SER   C CA     1 
ATOM   9693  C  C      . SER   C 1  379 ? -9.908  -27.317  9.832   1.00 37.21  ? 379 SER   C C      1 
ATOM   9694  O  O      . SER   C 1  379 ? -10.046 -26.575  8.854   1.00 40.04  ? 379 SER   C O      1 
ATOM   9695  C  CB     . SER   C 1  379 ? -7.496  -27.626  10.500  1.00 35.21  ? 379 SER   C CB     1 
ATOM   9696  O  OG     . SER   C 1  379 ? -6.748  -26.894  9.552   1.00 42.15  ? 379 SER   C OG     1 
ATOM   9697  N  N      . ASN   C 1  380 ? -10.760 -27.349  10.854  1.00 33.11  ? 380 ASN   C N      1 
ATOM   9698  C  CA     . ASN   C 1  380 ? -11.781 -26.331  11.045  1.00 32.09  ? 380 ASN   C CA     1 
ATOM   9699  C  C      . ASN   C 1  380 ? -11.193 -25.253  11.947  1.00 37.38  ? 380 ASN   C C      1 
ATOM   9700  O  O      . ASN   C 1  380 ? -11.075 -25.437  13.158  1.00 36.56  ? 380 ASN   C O      1 
ATOM   9701  C  CB     . ASN   C 1  380 ? -13.034 -26.905  11.676  1.00 34.18  ? 380 ASN   C CB     1 
ATOM   9702  C  CG     . ASN   C 1  380 ? -14.135 -25.882  11.785  1.00 39.59  ? 380 ASN   C CG     1 
ATOM   9703  O  OD1    . ASN   C 1  380 ? -14.696 -25.708  12.857  1.00 48.02  ? 380 ASN   C OD1    1 
ATOM   9704  N  ND2    . ASN   C 1  380 ? -14.516 -25.267  10.668  1.00 41.29  ? 380 ASN   C ND2    1 
ATOM   9705  N  N      . THR   C 1  381 ? -10.808 -24.134  11.363  1.00 38.12  ? 381 THR   C N      1 
ATOM   9706  C  CA     . THR   C 1  381 ? -10.227 -23.034  12.105  1.00 29.60  ? 381 THR   C CA     1 
ATOM   9707  C  C      . THR   C 1  381 ? -11.098 -21.813  11.890  1.00 33.02  ? 381 THR   C C      1 
ATOM   9708  O  O      . THR   C 1  381 ? -11.629 -21.611  10.794  1.00 37.59  ? 381 THR   C O      1 
ATOM   9709  C  CB     . THR   C 1  381 ? -8.830  -22.742  11.633  1.00 33.25  ? 381 THR   C CB     1 
ATOM   9710  O  OG1    . THR   C 1  381 ? -8.377  -21.540  12.256  1.00 46.08  ? 381 THR   C OG1    1 
ATOM   9711  C  CG2    . THR   C 1  381 ? -8.820  -22.499  10.157  1.00 31.85  ? 381 THR   C CG2    1 
ATOM   9712  N  N      . THR   C 1  382 ? -11.257 -21.005  12.930  1.00 30.91  ? 382 THR   C N      1 
ATOM   9713  C  CA     . THR   C 1  382 ? -12.004 -19.774  12.751  1.00 31.51  ? 382 THR   C CA     1 
ATOM   9714  C  C      . THR   C 1  382 ? -11.332 -18.868  11.744  1.00 34.71  ? 382 THR   C C      1 
ATOM   9715  O  O      . THR   C 1  382 ? -12.006 -18.073  11.084  1.00 34.08  ? 382 THR   C O      1 
ATOM   9716  C  CB     . THR   C 1  382 ? -12.161 -19.070  14.085  1.00 32.86  ? 382 THR   C CB     1 
ATOM   9717  O  OG1    . THR   C 1  382 ? -10.858 -18.718  14.585  1.00 36.87  ? 382 THR   C OG1    1 
ATOM   9718  C  CG2    . THR   C 1  382 ? -12.891 -19.977  15.070  1.00 30.52  ? 382 THR   C CG2    1 
ATOM   9719  N  N      . ALA   C 1  383 ? -10.017 -18.998  11.592  1.00 35.75  ? 383 ALA   C N      1 
ATOM   9720  C  CA     . ALA   C 1  383 ? -9.293  -18.182  10.628  1.00 38.45  ? 383 ALA   C CA     1 
ATOM   9721  C  C      . ALA   C 1  383 ? -9.962  -18.157  9.251   1.00 37.85  ? 383 ALA   C C      1 
ATOM   9722  O  O      . ALA   C 1  383 ? -9.853  -17.155  8.542   1.00 39.37  ? 383 ALA   C O      1 
ATOM   9723  C  CB     . ALA   C 1  383 ? -7.850  -18.680  10.517  1.00 38.70  ? 383 ALA   C CB     1 
ATOM   9724  N  N      . ILE   C 1  384 ? -10.625 -19.246  8.839   1.00 34.08  ? 384 ILE   C N      1 
ATOM   9725  C  CA     . ILE   C 1  384 ? -11.270 -19.277  7.527   1.00 31.58  ? 384 ILE   C CA     1 
ATOM   9726  C  C      . ILE   C 1  384 ? -12.223 -18.097  7.356   1.00 33.94  ? 384 ILE   C C      1 
ATOM   9727  O  O      . ILE   C 1  384 ? -12.453 -17.621  6.239   1.00 30.94  ? 384 ILE   C O      1 
ATOM   9728  C  CB     . ILE   C 1  384 ? -12.007 -20.618  7.343   1.00 37.68  ? 384 ILE   C CB     1 
ATOM   9729  C  CG1    . ILE   C 1  384 ? -12.321 -20.905  5.866   1.00 34.71  ? 384 ILE   C CG1    1 
ATOM   9730  C  CG2    . ILE   C 1  384 ? -13.279 -20.648  8.205   1.00 36.55  ? 384 ILE   C CG2    1 
ATOM   9731  C  CD1    . ILE   C 1  384 ? -11.143 -21.356  5.045   1.00 32.36  ? 384 ILE   C CD1    1 
ATOM   9732  N  N      . ALA   C 1  385 ? -12.797 -17.604  8.448   1.00 31.07  ? 385 ALA   C N      1 
ATOM   9733  C  CA     . ALA   C 1  385 ? -13.774 -16.541  8.305   1.00 31.61  ? 385 ALA   C CA     1 
ATOM   9734  C  C      . ALA   C 1  385 ? -13.145 -15.327  7.656   1.00 32.49  ? 385 ALA   C C      1 
ATOM   9735  O  O      . ALA   C 1  385 ? -13.830 -14.551  6.983   1.00 35.55  ? 385 ALA   C O      1 
ATOM   9736  C  CB     . ALA   C 1  385 ? -14.389 -16.189  9.673   1.00 30.47  ? 385 ALA   C CB     1 
ATOM   9737  N  N      . GLU   C 1  386 ? -11.843 -15.141  7.845   1.00 32.13  ? 386 GLU   C N      1 
ATOM   9738  C  CA     . GLU   C 1  386 ? -11.159 -14.048  7.164   1.00 36.94  ? 386 GLU   C CA     1 
ATOM   9739  C  C      . GLU   C 1  386 ? -11.556 -14.004  5.693   1.00 32.52  ? 386 GLU   C C      1 
ATOM   9740  O  O      . GLU   C 1  386 ? -11.911 -12.950  5.161   1.00 32.37  ? 386 GLU   C O      1 
ATOM   9741  C  CB     . GLU   C 1  386 ? -9.641  -14.181  7.293   1.00 35.60  ? 386 GLU   C CB     1 
ATOM   9742  C  CG     . GLU   C 1  386 ? -9.063  -13.685  8.600   1.00 35.09  ? 386 GLU   C CG     1 
ATOM   9743  C  CD     . GLU   C 1  386 ? -7.600  -14.077  8.733   1.00 48.41  ? 386 GLU   C CD     1 
ATOM   9744  O  OE1    . GLU   C 1  386 ? -6.856  -13.852  7.740   1.00 53.21  ? 386 GLU   C OE1    1 
ATOM   9745  O  OE2    . GLU   C 1  386 ? -7.187  -14.586  9.799   1.00 47.75  ? 386 GLU   C OE2    1 
ATOM   9746  N  N      . ALA   C 1  387 ? -11.527 -15.155  5.027   1.00 32.25  ? 387 ALA   C N      1 
ATOM   9747  C  CA     . ALA   C 1  387 ? -11.954 -15.208  3.635   1.00 35.87  ? 387 ALA   C CA     1 
ATOM   9748  C  C      . ALA   C 1  387 ? -13.368 -14.671  3.457   1.00 35.28  ? 387 ALA   C C      1 
ATOM   9749  O  O      . ALA   C 1  387 ? -13.651 -14.003  2.457   1.00 36.56  ? 387 ALA   C O      1 
ATOM   9750  C  CB     . ALA   C 1  387 ? -11.860 -16.639  3.115   1.00 36.10  ? 387 ALA   C CB     1 
ATOM   9751  N  N      . TRP   C 1  388 ? -14.263 -14.934  4.411   1.00 33.67  ? 388 TRP   C N      1 
ATOM   9752  C  CA     . TRP   C 1  388 ? -15.611 -14.382  4.313   1.00 36.11  ? 388 TRP   C CA     1 
ATOM   9753  C  C      . TRP   C 1  388 ? -15.598 -12.861  4.399   1.00 39.69  ? 388 TRP   C C      1 
ATOM   9754  O  O      . TRP   C 1  388 ? -16.316 -12.193  3.643   1.00 39.82  ? 388 TRP   C O      1 
ATOM   9755  C  CB     . TRP   C 1  388 ? -16.534 -14.974  5.389   1.00 37.63  ? 388 TRP   C CB     1 
ATOM   9756  C  CG     . TRP   C 1  388 ? -16.742 -16.480  5.275   1.00 41.10  ? 388 TRP   C CG     1 
ATOM   9757  C  CD1    . TRP   C 1  388 ? -16.654 -17.424  6.280   1.00 40.13  ? 388 TRP   C CD1    1 
ATOM   9758  C  CD2    . TRP   C 1  388 ? -17.095 -17.197  4.090   1.00 35.48  ? 388 TRP   C CD2    1 
ATOM   9759  N  NE1    . TRP   C 1  388 ? -16.931 -18.676  5.777   1.00 38.95  ? 388 TRP   C NE1    1 
ATOM   9760  C  CE2    . TRP   C 1  388 ? -17.196 -18.560  4.436   1.00 36.54  ? 388 TRP   C CE2    1 
ATOM   9761  C  CE3    . TRP   C 1  388 ? -17.344 -16.814  2.768   1.00 37.55  ? 388 TRP   C CE3    1 
ATOM   9762  C  CZ2    . TRP   C 1  388 ? -17.526 -19.540  3.500   1.00 45.50  ? 388 TRP   C CZ2    1 
ATOM   9763  C  CZ3    . TRP   C 1  388 ? -17.683 -17.785  1.841   1.00 39.43  ? 388 TRP   C CZ3    1 
ATOM   9764  C  CH2    . TRP   C 1  388 ? -17.770 -19.132  2.208   1.00 41.23  ? 388 TRP   C CH2    1 
ATOM   9765  N  N      . ALA   C 1  389 ? -14.792 -12.292  5.308   1.00 36.90  ? 389 ALA   C N      1 
ATOM   9766  C  CA     . ALA   C 1  389 ? -14.735 -10.836  5.441   1.00 33.52  ? 389 ALA   C CA     1 
ATOM   9767  C  C      . ALA   C 1  389 ? -14.150 -10.178  4.189   1.00 38.94  ? 389 ALA   C C      1 
ATOM   9768  O  O      . ALA   C 1  389 ? -14.752 -9.258   3.614   1.00 36.09  ? 389 ALA   C O      1 
ATOM   9769  C  CB     . ALA   C 1  389 ? -13.926 -10.460  6.667   1.00 28.88  ? 389 ALA   C CB     1 
ATOM   9770  N  N      . ARG   C 1  390 ? -12.976 -10.621  3.748   1.00 32.57  ? 390 ARG   C N      1 
ATOM   9771  C  CA     . ARG   C 1  390 ? -12.482 -10.127  2.480   1.00 29.19  ? 390 ARG   C CA     1 
ATOM   9772  C  C      . ARG   C 1  390 ? -13.593 -10.045  1.446   1.00 37.52  ? 390 ARG   C C      1 
ATOM   9773  O  O      . ARG   C 1  390 ? -13.859 -8.962   0.915   1.00 44.42  ? 390 ARG   C O      1 
ATOM   9774  C  CB     . ARG   C 1  390 ? -11.329 -10.974  1.970   1.00 31.56  ? 390 ARG   C CB     1 
ATOM   9775  C  CG     . ARG   C 1  390 ? -10.133 -10.847  2.813   1.00 30.83  ? 390 ARG   C CG     1 
ATOM   9776  C  CD     . ARG   C 1  390 ? -8.912  -11.378  2.121   1.00 29.62  ? 390 ARG   C CD     1 
ATOM   9777  N  NE     . ARG   C 1  390 ? -8.951  -12.773  1.714   1.00 39.63  ? 390 ARG   C NE     1 
ATOM   9778  C  CZ     . ARG   C 1  390 ? -8.540  -13.779  2.478   1.00 35.02  ? 390 ARG   C CZ     1 
ATOM   9779  N  NH1    . ARG   C 1  390 ? -8.248  -13.607  3.757   1.00 35.37  ? 390 ARG   C NH1    1 
ATOM   9780  N  NH2    . ARG   C 1  390 ? -8.381  -14.978  1.935   1.00 37.45  ? 390 ARG   C NH2    1 
ATOM   9781  N  N      . LEU   C 1  391 ? -14.258 -11.175  1.142   1.00 36.20  ? 391 LEU   C N      1 
ATOM   9782  C  CA     . LEU   C 1  391 ? -15.357 -11.138  0.172   1.00 32.80  ? 391 LEU   C CA     1 
ATOM   9783  C  C      . LEU   C 1  391 ? -16.477 -10.218  0.624   1.00 35.99  ? 391 LEU   C C      1 
ATOM   9784  O  O      . LEU   C 1  391 ? -16.959 -9.393   -0.158  1.00 35.83  ? 391 LEU   C O      1 
ATOM   9785  C  CB     . LEU   C 1  391 ? -15.939 -12.520  -0.100  1.00 29.97  ? 391 LEU   C CB     1 
ATOM   9786  C  CG     . LEU   C 1  391 ? -15.565 -13.283  -1.353  1.00 32.08  ? 391 LEU   C CG     1 
ATOM   9787  C  CD1    . LEU   C 1  391 ? -16.450 -14.519  -1.502  1.00 29.97  ? 391 LEU   C CD1    1 
ATOM   9788  C  CD2    . LEU   C 1  391 ? -15.737 -12.353  -2.546  1.00 33.48  ? 391 LEU   C CD2    1 
ATOM   9789  N  N      . ASP   C 1  392 ? -16.939 -10.371  1.870   1.00 34.49  ? 392 ASP   C N      1 
ATOM   9790  C  CA     . ASP   C 1  392 ? -18.030 -9.527   2.333   1.00 36.41  ? 392 ASP   C CA     1 
ATOM   9791  C  C      . ASP   C 1  392 ? -17.715 -8.041   2.164   1.00 40.49  ? 392 ASP   C C      1 
ATOM   9792  O  O      . ASP   C 1  392 ? -18.615 -7.246   1.868   1.00 38.73  ? 392 ASP   C O      1 
ATOM   9793  C  CB     . ASP   C 1  392 ? -18.379 -9.877   3.775   1.00 36.62  ? 392 ASP   C CB     1 
ATOM   9794  C  CG     . ASP   C 1  392 ? -19.150 -11.186  3.870   1.00 43.44  ? 392 ASP   C CG     1 
ATOM   9795  O  OD1    . ASP   C 1  392 ? -19.646 -11.619  2.810   1.00 40.05  ? 392 ASP   C OD1    1 
ATOM   9796  O  OD2    . ASP   C 1  392 ? -19.323 -11.757  4.983   1.00 47.49  ? 392 ASP   C OD2    1 
ATOM   9797  N  N      . HIS   C 1  393 ? -16.442 -7.650   2.289   1.00 39.71  ? 393 HIS   C N      1 
ATOM   9798  C  CA     . HIS   C 1  393 ? -16.068 -6.255   2.050   1.00 38.29  ? 393 HIS   C CA     1 
ATOM   9799  C  C      . HIS   C 1  393 ? -16.198 -5.852   0.584   1.00 38.08  ? 393 HIS   C C      1 
ATOM   9800  O  O      . HIS   C 1  393 ? -16.797 -4.813   0.270   1.00 36.96  ? 393 HIS   C O      1 
ATOM   9801  C  CB     . HIS   C 1  393 ? -14.647 -5.996   2.525   1.00 35.22  ? 393 HIS   C CB     1 
ATOM   9802  C  CG     . HIS   C 1  393 ? -14.231 -4.566   2.394   1.00 38.91  ? 393 HIS   C CG     1 
ATOM   9803  N  ND1    . HIS   C 1  393 ? -14.878 -3.538   3.052   1.00 42.40  ? 393 HIS   C ND1    1 
ATOM   9804  C  CD2    . HIS   C 1  393 ? -13.212 -3.996   1.712   1.00 38.43  ? 393 HIS   C CD2    1 
ATOM   9805  C  CE1    . HIS   C 1  393 ? -14.281 -2.396   2.769   1.00 38.44  ? 393 HIS   C CE1    1 
ATOM   9806  N  NE2    . HIS   C 1  393 ? -13.265 -2.646   1.958   1.00 43.49  ? 393 HIS   C NE2    1 
ATOM   9807  N  N      . LYS   C 1  394 ? -15.585 -6.617   -0.329  1.00 34.23  ? 394 LYS   C N      1 
ATOM   9808  C  CA     . LYS   C 1  394 ? -15.695 -6.248   -1.733  1.00 33.54  ? 394 LYS   C CA     1 
ATOM   9809  C  C      . LYS   C 1  394 ? -17.155 -6.170   -2.139  1.00 35.85  ? 394 LYS   C C      1 
ATOM   9810  O  O      . LYS   C 1  394 ? -17.584 -5.196   -2.768  1.00 33.63  ? 394 LYS   C O      1 
ATOM   9811  C  CB     . LYS   C 1  394 ? -14.940 -7.227   -2.626  1.00 29.77  ? 394 LYS   C CB     1 
ATOM   9812  C  CG     . LYS   C 1  394 ? -13.466 -7.347   -2.308  1.00 32.23  ? 394 LYS   C CG     1 
ATOM   9813  C  CD     . LYS   C 1  394 ? -12.844 -8.450   -3.138  1.00 34.73  ? 394 LYS   C CD     1 
ATOM   9814  C  CE     . LYS   C 1  394 ? -11.437 -8.126   -3.605  1.00 28.29  ? 394 LYS   C CE     1 
ATOM   9815  N  NZ     . LYS   C 1  394 ? -10.787 -7.263   -2.621  1.00 50.90  ? 394 LYS   C NZ     1 
ATOM   9816  N  N      . PHE   C 1  395 ? -17.948 -7.165   -1.732  1.00 35.20  ? 395 PHE   C N      1 
ATOM   9817  C  CA     . PHE   C 1  395 ? -19.390 -7.091   -1.930  1.00 33.47  ? 395 PHE   C CA     1 
ATOM   9818  C  C      . PHE   C 1  395 ? -19.937 -5.750   -1.477  1.00 37.23  ? 395 PHE   C C      1 
ATOM   9819  O  O      . PHE   C 1  395 ? -20.663 -5.076   -2.218  1.00 39.37  ? 395 PHE   C O      1 
ATOM   9820  C  CB     . PHE   C 1  395 ? -20.093 -8.205   -1.178  1.00 31.09  ? 395 PHE   C CB     1 
ATOM   9821  C  CG     . PHE   C 1  395 ? -21.587 -8.142   -1.280  1.00 35.25  ? 395 PHE   C CG     1 
ATOM   9822  C  CD1    . PHE   C 1  395 ? -22.331 -7.260   -0.494  1.00 30.54  ? 395 PHE   C CD1    1 
ATOM   9823  C  CD2    . PHE   C 1  395 ? -22.257 -8.966   -2.206  1.00 35.13  ? 395 PHE   C CD2    1 
ATOM   9824  C  CE1    . PHE   C 1  395 ? -23.713 -7.221   -0.605  1.00 30.25  ? 395 PHE   C CE1    1 
ATOM   9825  C  CE2    . PHE   C 1  395 ? -23.638 -8.936   -2.316  1.00 30.43  ? 395 PHE   C CE2    1 
ATOM   9826  C  CZ     . PHE   C 1  395 ? -24.368 -8.047   -1.509  1.00 30.00  ? 395 PHE   C CZ     1 
ATOM   9827  N  N      . ASP   C 1  396 ? -19.578 -5.330   -0.265  1.00 39.89  ? 396 ASP   C N      1 
ATOM   9828  C  CA     . ASP   C 1  396 ? -20.158 -4.108   0.296   1.00 38.39  ? 396 ASP   C CA     1 
ATOM   9829  C  C      . ASP   C 1  396 ? -19.777 -2.857   -0.494  1.00 33.83  ? 396 ASP   C C      1 
ATOM   9830  O  O      . ASP   C 1  396 ? -20.612 -1.971   -0.694  1.00 32.54  ? 396 ASP   C O      1 
ATOM   9831  C  CB     . ASP   C 1  396 ? -19.755 -3.983   1.757   1.00 36.51  ? 396 ASP   C CB     1 
ATOM   9832  C  CG     . ASP   C 1  396 ? -20.540 -4.903   2.643   1.00 39.71  ? 396 ASP   C CG     1 
ATOM   9833  O  OD1    . ASP   C 1  396 ? -21.615 -5.386   2.199   1.00 40.21  ? 396 ASP   C OD1    1 
ATOM   9834  O  OD2    . ASP   C 1  396 ? -20.055 -5.178   3.758   1.00 44.50  ? 396 ASP   C OD2    1 
ATOM   9835  N  N      . LEU   C 1  397 ? -18.530 -2.759   -0.948  1.00 30.26  ? 397 LEU   C N      1 
ATOM   9836  C  CA     . LEU   C 1  397 ? -18.127 -1.557   -1.671  1.00 34.68  ? 397 LEU   C CA     1 
ATOM   9837  C  C      . LEU   C 1  397 ? -19.052 -1.262   -2.838  1.00 36.85  ? 397 LEU   C C      1 
ATOM   9838  O  O      . LEU   C 1  397 ? -19.407 -0.102   -3.086  1.00 38.97  ? 397 LEU   C O      1 
ATOM   9839  C  CB     . LEU   C 1  397 ? -16.706 -1.707   -2.174  1.00 34.82  ? 397 LEU   C CB     1 
ATOM   9840  C  CG     . LEU   C 1  397 ? -15.677 -1.570   -1.085  1.00 34.73  ? 397 LEU   C CG     1 
ATOM   9841  C  CD1    . LEU   C 1  397 ? -14.386 -2.074   -1.640  1.00 36.18  ? 397 LEU   C CD1    1 
ATOM   9842  C  CD2    . LEU   C 1  397 ? -15.575 -0.116   -0.743  1.00 24.36  ? 397 LEU   C CD2    1 
ATOM   9843  N  N      . MET   C 1  398 ? -19.432 -2.294   -3.585  1.00 36.69  ? 398 MET   C N      1 
ATOM   9844  C  CA     . MET   C 1  398 ? -20.214 -2.066   -4.786  1.00 33.13  ? 398 MET   C CA     1 
ATOM   9845  C  C      . MET   C 1  398 ? -21.697 -1.946   -4.453  1.00 36.18  ? 398 MET   C C      1 
ATOM   9846  O  O      . MET   C 1  398 ? -22.417 -1.133   -5.041  1.00 34.67  ? 398 MET   C O      1 
ATOM   9847  C  CB     . MET   C 1  398 ? -19.976 -3.201   -5.776  1.00 28.86  ? 398 MET   C CB     1 
ATOM   9848  C  CG     . MET   C 1  398 ? -18.603 -3.204   -6.422  1.00 28.96  ? 398 MET   C CG     1 
ATOM   9849  S  SD     . MET   C 1  398 ? -18.464 -4.587   -7.590  1.00 37.33  ? 398 MET   C SD     1 
ATOM   9850  C  CE     . MET   C 1  398 ? -18.770 -6.023   -6.592  1.00 31.67  ? 398 MET   C CE     1 
ATOM   9851  N  N      . TYR   C 1  399 ? -22.172 -2.742   -3.505  1.00 34.62  ? 399 TYR   C N      1 
ATOM   9852  C  CA     . TYR   C 1  399 ? -23.596 -2.726   -3.237  1.00 35.75  ? 399 TYR   C CA     1 
ATOM   9853  C  C      . TYR   C 1  399 ? -24.049 -1.379   -2.674  1.00 36.57  ? 399 TYR   C C      1 
ATOM   9854  O  O      . TYR   C 1  399 ? -25.207 -0.982   -2.867  1.00 35.53  ? 399 TYR   C O      1 
ATOM   9855  C  CB     . TYR   C 1  399 ? -23.955 -3.879   -2.296  1.00 33.20  ? 399 TYR   C CB     1 
ATOM   9856  C  CG     . TYR   C 1  399 ? -25.436 -4.113   -2.243  1.00 34.66  ? 399 TYR   C CG     1 
ATOM   9857  C  CD1    . TYR   C 1  399 ? -26.098 -4.755   -3.270  1.00 35.39  ? 399 TYR   C CD1    1 
ATOM   9858  C  CD2    . TYR   C 1  399 ? -26.189 -3.574   -1.210  1.00 30.45  ? 399 TYR   C CD2    1 
ATOM   9859  C  CE1    . TYR   C 1  399 ? -27.474 -4.916   -3.220  1.00 37.38  ? 399 TYR   C CE1    1 
ATOM   9860  C  CE2    . TYR   C 1  399 ? -27.525 -3.733   -1.146  1.00 30.04  ? 399 TYR   C CE2    1 
ATOM   9861  C  CZ     . TYR   C 1  399 ? -28.176 -4.398   -2.143  1.00 38.58  ? 399 TYR   C CZ     1 
ATOM   9862  O  OH     . TYR   C 1  399 ? -29.541 -4.526   -2.039  1.00 42.96  ? 399 TYR   C OH     1 
ATOM   9863  N  N      . ALA   C 1  400 ? -23.160 -0.665   -1.980  1.00 36.14  ? 400 ALA   C N      1 
ATOM   9864  C  CA     . ALA   C 1  400 ? -23.528 0.627    -1.415  1.00 31.59  ? 400 ALA   C CA     1 
ATOM   9865  C  C      . ALA   C 1  400 ? -23.888 1.627    -2.505  1.00 38.54  ? 400 ALA   C C      1 
ATOM   9866  O  O      . ALA   C 1  400 ? -24.815 2.425    -2.339  1.00 45.14  ? 400 ALA   C O      1 
ATOM   9867  C  CB     . ALA   C 1  400 ? -22.397 1.163    -0.561  1.00 33.45  ? 400 ALA   C CB     1 
ATOM   9868  N  N      . LYS   C 1  401 ? -23.172 1.609    -3.625  1.00 39.92  ? 401 LYS   C N      1 
ATOM   9869  C  CA     . LYS   C 1  401 ? -23.567 2.388    -4.794  1.00 40.07  ? 401 LYS   C CA     1 
ATOM   9870  C  C      . LYS   C 1  401 ? -24.481 1.606    -5.730  1.00 36.73  ? 401 LYS   C C      1 
ATOM   9871  O  O      . LYS   C 1  401 ? -24.747 2.062    -6.838  1.00 37.17  ? 401 LYS   C O      1 
ATOM   9872  C  CB     . LYS   C 1  401 ? -22.335 2.875    -5.554  1.00 39.04  ? 401 LYS   C CB     1 
ATOM   9873  C  CG     . LYS   C 1  401 ? -21.188 3.316    -4.647  1.00 43.22  ? 401 LYS   C CG     1 
ATOM   9874  C  CD     . LYS   C 1  401 ? -21.446 4.651    -3.968  1.00 44.54  ? 401 LYS   C CD     1 
ATOM   9875  C  CE     . LYS   C 1  401 ? -20.263 5.085    -3.104  1.00 50.20  ? 401 LYS   C CE     1 
ATOM   9876  N  NZ     . LYS   C 1  401 ? -19.981 4.122    -2.005  1.00 51.21  ? 401 LYS   C NZ     1 
ATOM   9877  N  N      . ARG   C 1  402 ? -24.959 0.443    -5.300  1.00 40.07  ? 402 ARG   C N      1 
ATOM   9878  C  CA     . ARG   C 1  402 ? -25.765 -0.464   -6.122  1.00 40.19  ? 402 ARG   C CA     1 
ATOM   9879  C  C      . ARG   C 1  402 ? -25.143 -0.774   -7.490  1.00 36.54  ? 402 ARG   C C      1 
ATOM   9880  O  O      . ARG   C 1  402 ? -25.854 -1.128   -8.433  1.00 33.34  ? 402 ARG   C O      1 
ATOM   9881  C  CB     . ARG   C 1  402 ? -27.165 0.081    -6.306  1.00 34.23  ? 402 ARG   C CB     1 
ATOM   9882  C  CG     . ARG   C 1  402 ? -27.971 0.116    -5.043  1.00 39.60  ? 402 ARG   C CG     1 
ATOM   9883  C  CD     . ARG   C 1  402 ? -28.055 -1.246   -4.391  1.00 44.13  ? 402 ARG   C CD     1 
ATOM   9884  N  NE     . ARG   C 1  402 ? -29.120 -1.309   -3.396  1.00 46.75  ? 402 ARG   C NE     1 
ATOM   9885  C  CZ     . ARG   C 1  402 ? -29.017 -0.932   -2.128  1.00 43.30  ? 402 ARG   C CZ     1 
ATOM   9886  N  NH1    . ARG   C 1  402 ? -27.888 -0.435   -1.643  1.00 35.32  ? 402 ARG   C NH1    1 
ATOM   9887  N  NH2    . ARG   C 1  402 ? -30.073 -1.077   -1.324  1.00 39.77  ? 402 ARG   C NH2    1 
ATOM   9888  N  N      . ALA   C 1  403 ? -23.815 -0.693   -7.597  1.00 33.92  ? 403 ALA   C N      1 
ATOM   9889  C  CA     . ALA   C 1  403 ? -23.143 -0.968   -8.863  1.00 34.76  ? 403 ALA   C CA     1 
ATOM   9890  C  C      . ALA   C 1  403 ? -23.494 -2.350   -9.392  1.00 30.88  ? 403 ALA   C C      1 
ATOM   9891  O  O      . ALA   C 1  403 ? -23.446 -3.334   -8.661  1.00 36.51  ? 403 ALA   C O      1 
ATOM   9892  C  CB     . ALA   C 1  403 ? -21.625 -0.841   -8.700  1.00 33.24  ? 403 ALA   C CB     1 
ATOM   9893  N  N      . PHE   C 1  404 ? -23.824 -2.421   -10.679 1.00 32.73  ? 404 PHE   C N      1 
ATOM   9894  C  CA     . PHE   C 1  404 ? -24.142 -3.633   -11.424 1.00 33.24  ? 404 PHE   C CA     1 
ATOM   9895  C  C      . PHE   C 1  404 ? -25.409 -4.304   -10.951 1.00 35.10  ? 404 PHE   C C      1 
ATOM   9896  O  O      . PHE   C 1  404 ? -25.769 -5.343   -11.509 1.00 34.28  ? 404 PHE   C O      1 
ATOM   9897  C  CB     . PHE   C 1  404 ? -23.012 -4.669   -11.375 1.00 34.45  ? 404 PHE   C CB     1 
ATOM   9898  C  CG     . PHE   C 1  404 ? -21.700 -4.131   -11.807 1.00 36.10  ? 404 PHE   C CG     1 
ATOM   9899  C  CD1    . PHE   C 1  404 ? -21.326 -4.177   -13.122 1.00 37.20  ? 404 PHE   C CD1    1 
ATOM   9900  C  CD2    . PHE   C 1  404 ? -20.871 -3.502   -10.905 1.00 40.35  ? 404 PHE   C CD2    1 
ATOM   9901  C  CE1    . PHE   C 1  404 ? -20.129 -3.661   -13.513 1.00 40.31  ? 404 PHE   C CE1    1 
ATOM   9902  C  CE2    . PHE   C 1  404 ? -19.662 -2.975   -11.302 1.00 38.92  ? 404 PHE   C CE2    1 
ATOM   9903  C  CZ     . PHE   C 1  404 ? -19.296 -3.048   -12.598 1.00 37.33  ? 404 PHE   C CZ     1 
ATOM   9904  N  N      . VAL   C 1  405 ? -26.117 -3.748   -9.966  1.00 33.23  ? 405 VAL   C N      1 
ATOM   9905  C  CA     . VAL   C 1  405 ? -27.244 -4.487   -9.436  1.00 36.56  ? 405 VAL   C CA     1 
ATOM   9906  C  C      . VAL   C 1  405 ? -28.336 -4.607   -10.484 1.00 39.47  ? 405 VAL   C C      1 
ATOM   9907  O  O      . VAL   C 1  405 ? -29.126 -5.565   -10.455 1.00 40.46  ? 405 VAL   C O      1 
ATOM   9908  C  CB     . VAL   C 1  405 ? -27.773 -3.849   -8.141  1.00 37.72  ? 405 VAL   C CB     1 
ATOM   9909  C  CG1    . VAL   C 1  405 ? -29.126 -4.492   -7.721  1.00 32.89  ? 405 VAL   C CG1    1 
ATOM   9910  C  CG2    . VAL   C 1  405 ? -26.714 -3.964   -7.051  1.00 36.53  ? 405 VAL   C CG2    1 
ATOM   9911  N  N      . HIS   C 1  406 ? -28.357 -3.691   -11.455 1.00 39.48  ? 406 HIS   C N      1 
ATOM   9912  C  CA     . HIS   C 1  406 ? -29.374 -3.740   -12.506 1.00 41.44  ? 406 HIS   C CA     1 
ATOM   9913  C  C      . HIS   C 1  406 ? -29.244 -4.962   -13.404 1.00 36.31  ? 406 HIS   C C      1 
ATOM   9914  O  O      . HIS   C 1  406 ? -30.258 -5.441   -13.908 1.00 40.50  ? 406 HIS   C O      1 
ATOM   9915  C  CB     . HIS   C 1  406 ? -29.358 -2.457   -13.346 1.00 36.65  ? 406 HIS   C CB     1 
ATOM   9916  C  CG     . HIS   C 1  406 ? -28.239 -2.379   -14.328 1.00 34.12  ? 406 HIS   C CG     1 
ATOM   9917  N  ND1    . HIS   C 1  406 ? -26.996 -1.884   -13.996 1.00 37.19  ? 406 HIS   C ND1    1 
ATOM   9918  C  CD2    . HIS   C 1  406 ? -28.173 -2.719   -15.634 1.00 40.08  ? 406 HIS   C CD2    1 
ATOM   9919  C  CE1    . HIS   C 1  406 ? -26.207 -1.934   -15.049 1.00 38.89  ? 406 HIS   C CE1    1 
ATOM   9920  N  NE2    . HIS   C 1  406 ? -26.898 -2.436   -16.057 1.00 44.95  ? 406 HIS   C NE2    1 
ATOM   9921  N  N      . TRP   C 1  407 ? -28.036 -5.476   -13.641 1.00 35.44  ? 407 TRP   C N      1 
ATOM   9922  C  CA     . TRP   C 1  407 ? -27.949 -6.670   -14.476 1.00 37.36  ? 407 TRP   C CA     1 
ATOM   9923  C  C      . TRP   C 1  407 ? -28.591 -7.864   -13.793 1.00 41.88  ? 407 TRP   C C      1 
ATOM   9924  O  O      . TRP   C 1  407 ? -28.931 -8.843   -14.461 1.00 40.88  ? 407 TRP   C O      1 
ATOM   9925  C  CB     . TRP   C 1  407 ? -26.499 -7.001   -14.818 1.00 36.24  ? 407 TRP   C CB     1 
ATOM   9926  C  CG     . TRP   C 1  407 ? -25.829 -6.008   -15.698 1.00 43.98  ? 407 TRP   C CG     1 
ATOM   9927  C  CD1    . TRP   C 1  407 ? -24.770 -5.210   -15.366 1.00 43.57  ? 407 TRP   C CD1    1 
ATOM   9928  C  CD2    . TRP   C 1  407 ? -26.124 -5.725   -17.067 1.00 43.08  ? 407 TRP   C CD2    1 
ATOM   9929  N  NE1    . TRP   C 1  407 ? -24.411 -4.427   -16.429 1.00 39.82  ? 407 TRP   C NE1    1 
ATOM   9930  C  CE2    . TRP   C 1  407 ? -25.222 -4.730   -17.490 1.00 45.11  ? 407 TRP   C CE2    1 
ATOM   9931  C  CE3    . TRP   C 1  407 ? -27.059 -6.211   -17.975 1.00 41.74  ? 407 TRP   C CE3    1 
ATOM   9932  C  CZ2    . TRP   C 1  407 ? -25.235 -4.214   -18.783 1.00 48.98  ? 407 TRP   C CZ2    1 
ATOM   9933  C  CZ3    . TRP   C 1  407 ? -27.065 -5.701   -19.256 1.00 47.75  ? 407 TRP   C CZ3    1 
ATOM   9934  C  CH2    . TRP   C 1  407 ? -26.167 -4.711   -19.647 1.00 52.86  ? 407 TRP   C CH2    1 
ATOM   9935  N  N      . TYR   C 1  408 ? -28.744 -7.814   -12.473 1.00 39.99  ? 408 TYR   C N      1 
ATOM   9936  C  CA     . TYR   C 1  408 ? -29.409 -8.884   -11.763 1.00 36.34  ? 408 TYR   C CA     1 
ATOM   9937  C  C      . TYR   C 1  408 ? -30.911 -8.621   -11.637 1.00 43.21  ? 408 TYR   C C      1 
ATOM   9938  O  O      . TYR   C 1  408 ? -31.720 -9.539   -11.789 1.00 42.58  ? 408 TYR   C O      1 
ATOM   9939  C  CB     . TYR   C 1  408 ? -28.777 -9.059   -10.387 1.00 36.25  ? 408 TYR   C CB     1 
ATOM   9940  C  CG     . TYR   C 1  408 ? -27.320 -9.480   -10.373 1.00 40.11  ? 408 TYR   C CG     1 
ATOM   9941  C  CD1    . TYR   C 1  408 ? -26.313 -8.554   -10.626 1.00 39.69  ? 408 TYR   C CD1    1 
ATOM   9942  C  CD2    . TYR   C 1  408 ? -26.941 -10.793  -10.054 1.00 39.20  ? 408 TYR   C CD2    1 
ATOM   9943  C  CE1    . TYR   C 1  408 ? -24.962 -8.914   -10.589 1.00 33.47  ? 408 TYR   C CE1    1 
ATOM   9944  C  CE2    . TYR   C 1  408 ? -25.578 -11.172  -10.013 1.00 36.86  ? 408 TYR   C CE2    1 
ATOM   9945  C  CZ     . TYR   C 1  408 ? -24.593 -10.214  -10.288 1.00 36.14  ? 408 TYR   C CZ     1 
ATOM   9946  O  OH     . TYR   C 1  408 ? -23.236 -10.518  -10.276 1.00 33.21  ? 408 TYR   C OH     1 
ATOM   9947  N  N      . VAL   C 1  409 ? -31.312 -7.372   -11.394 1.00 45.08  ? 409 VAL   C N      1 
ATOM   9948  C  CA     . VAL   C 1  409 ? -32.737 -7.042   -11.323 1.00 44.88  ? 409 VAL   C CA     1 
ATOM   9949  C  C      . VAL   C 1  409 ? -33.454 -7.267   -12.657 1.00 47.80  ? 409 VAL   C C      1 
ATOM   9950  O  O      . VAL   C 1  409 ? -34.619 -7.691   -12.680 1.00 51.70  ? 409 VAL   C O      1 
ATOM   9951  C  CB     . VAL   C 1  409 ? -32.914 -5.599   -10.830 1.00 38.85  ? 409 VAL   C CB     1 
ATOM   9952  C  CG1    . VAL   C 1  409 ? -34.316 -5.200   -11.007 1.00 38.43  ? 409 VAL   C CG1    1 
ATOM   9953  C  CG2    . VAL   C 1  409 ? -32.563 -5.529   -9.355  1.00 44.23  ? 409 VAL   C CG2    1 
ATOM   9954  N  N      . GLY   C 1  410 ? -32.792 -6.988   -13.780 1.00 44.96  ? 410 GLY   C N      1 
ATOM   9955  C  CA     . GLY   C 1  410 ? -33.373 -7.210   -15.096 1.00 42.96  ? 410 GLY   C CA     1 
ATOM   9956  C  C      . GLY   C 1  410 ? -33.546 -8.663   -15.474 1.00 45.16  ? 410 GLY   C C      1 
ATOM   9957  O  O      . GLY   C 1  410 ? -34.258 -8.948   -16.441 1.00 50.07  ? 410 GLY   C O      1 
ATOM   9958  N  N      . GLU   C 1  411 ? -32.905 -9.581   -14.755 1.00 45.01  ? 411 GLU   C N      1 
ATOM   9959  C  CA     . GLU   C 1  411 ? -33.114 -11.008  -14.926 1.00 44.95  ? 411 GLU   C CA     1 
ATOM   9960  C  C      . GLU   C 1  411 ? -34.089 -11.571  -13.885 1.00 48.37  ? 411 GLU   C C      1 
ATOM   9961  O  O      . GLU   C 1  411 ? -34.205 -12.793  -13.751 1.00 48.04  ? 411 GLU   C O      1 
ATOM   9962  C  CB     . GLU   C 1  411 ? -31.774 -11.739  -14.855 1.00 40.78  ? 411 GLU   C CB     1 
ATOM   9963  C  CG     . GLU   C 1  411 ? -30.777 -11.364  -15.922 1.00 42.14  ? 411 GLU   C CG     1 
ATOM   9964  C  CD     . GLU   C 1  411 ? -31.138 -11.907  -17.285 1.00 49.47  ? 411 GLU   C CD     1 
ATOM   9965  O  OE1    . GLU   C 1  411 ? -32.071 -12.724  -17.361 1.00 52.63  ? 411 GLU   C OE1    1 
ATOM   9966  O  OE2    . GLU   C 1  411 ? -30.472 -11.539  -18.275 1.00 50.10  ? 411 GLU   C OE2    1 
ATOM   9967  N  N      . GLY   C 1  412 ? -34.758 -10.708  -13.122 1.00 45.16  ? 412 GLY   C N      1 
ATOM   9968  C  CA     . GLY   C 1  412 ? -35.833 -11.121  -12.243 1.00 49.06  ? 412 GLY   C CA     1 
ATOM   9969  C  C      . GLY   C 1  412 ? -35.516 -11.193  -10.763 1.00 51.02  ? 412 GLY   C C      1 
ATOM   9970  O  O      . GLY   C 1  412 ? -36.354 -11.669  -9.997  1.00 56.30  ? 412 GLY   C O      1 
ATOM   9971  N  N      . MET   C 1  413 ? -34.342 -10.750  -10.333 1.00 49.64  ? 413 MET   C N      1 
ATOM   9972  C  CA     . MET   C 1  413 ? -34.013 -10.725  -8.915  1.00 49.24  ? 413 MET   C CA     1 
ATOM   9973  C  C      . MET   C 1  413 ? -34.398 -9.389   -8.291  1.00 47.01  ? 413 MET   C C      1 
ATOM   9974  O  O      . MET   C 1  413 ? -34.503 -8.366   -8.973  1.00 52.34  ? 413 MET   C O      1 
ATOM   9975  C  CB     . MET   C 1  413 ? -32.520 -10.980  -8.681  1.00 48.10  ? 413 MET   C CB     1 
ATOM   9976  C  CG     . MET   C 1  413 ? -32.053 -12.352  -9.093  1.00 43.72  ? 413 MET   C CG     1 
ATOM   9977  S  SD     . MET   C 1  413 ? -30.352 -12.601  -8.618  1.00 47.76  ? 413 MET   C SD     1 
ATOM   9978  C  CE     . MET   C 1  413 ? -30.377 -12.683  -6.837  1.00 34.89  ? 413 MET   C CE     1 
ATOM   9979  N  N      . GLU   C 1  414 ? -34.597 -9.410   -6.974  1.00 37.93  ? 414 GLU   C N      1 
ATOM   9980  C  CA     . GLU   C 1  414 ? -34.956 -8.238   -6.194  1.00 34.80  ? 414 GLU   C CA     1 
ATOM   9981  C  C      . GLU   C 1  414 ? -33.781 -7.828   -5.338  1.00 40.59  ? 414 GLU   C C      1 
ATOM   9982  O  O      . GLU   C 1  414 ? -33.012 -8.674   -4.876  1.00 44.44  ? 414 GLU   C O      1 
ATOM   9983  C  CB     . GLU   C 1  414 ? -36.168 -8.516   -5.302  1.00 35.56  ? 414 GLU   C CB     1 
ATOM   9984  C  CG     . GLU   C 1  414 ? -37.357 -9.013   -6.085  1.00 43.64  ? 414 GLU   C CG     1 
ATOM   9985  C  CD     . GLU   C 1  414 ? -38.562 -9.232   -5.224  1.00 51.65  ? 414 GLU   C CD     1 
ATOM   9986  O  OE1    . GLU   C 1  414 ? -38.920 -8.291   -4.495  1.00 64.06  ? 414 GLU   C OE1    1 
ATOM   9987  O  OE2    . GLU   C 1  414 ? -39.211 -10.298  -5.349  1.00 55.02  ? 414 GLU   C OE2    1 
ATOM   9988  N  N      . GLU   C 1  415 ? -33.628 -6.514   -5.152  1.00 44.95  ? 415 GLU   C N      1 
ATOM   9989  C  CA     . GLU   C 1  415 ? -32.628 -6.034   -4.206  1.00 39.81  ? 415 GLU   C CA     1 
ATOM   9990  C  C      . GLU   C 1  415 ? -32.688 -6.804   -2.893  1.00 45.05  ? 415 GLU   C C      1 
ATOM   9991  O  O      . GLU   C 1  415 ? -31.652 -6.995   -2.241  1.00 48.29  ? 415 GLU   C O      1 
ATOM   9992  C  CB     . GLU   C 1  415 ? -32.810 -4.529   -3.945  1.00 47.23  ? 415 GLU   C CB     1 
ATOM   9993  C  CG     . GLU   C 1  415 ? -32.030 -3.560   -4.851  1.00 45.70  ? 415 GLU   C CG     1 
ATOM   9994  C  CD     . GLU   C 1  415 ? -32.080 -2.119   -4.330  1.00 52.87  ? 415 GLU   C CD     1 
ATOM   9995  O  OE1    . GLU   C 1  415 ? -32.786 -1.852   -3.317  1.00 52.28  ? 415 GLU   C OE1    1 
ATOM   9996  O  OE2    . GLU   C 1  415 ? -31.380 -1.262   -4.918  1.00 54.76  ? 415 GLU   C OE2    1 
ATOM   9997  N  N      . GLY   C 1  416 ? -33.881 -7.261   -2.496  1.00 42.11  ? 416 GLY   C N      1 
ATOM   9998  C  CA     . GLY   C 1  416 ? -34.014 -7.942   -1.220  1.00 40.11  ? 416 GLY   C CA     1 
ATOM   9999  C  C      . GLY   C 1  416 ? -33.072 -9.117   -1.088  1.00 40.24  ? 416 GLY   C C      1 
ATOM   10000 O  O      . GLY   C 1  416 ? -32.316 -9.219   -0.116  1.00 39.17  ? 416 GLY   C O      1 
ATOM   10001 N  N      . GLU   C 1  417 ? -33.100 -10.015  -2.074  1.00 38.69  ? 417 GLU   C N      1 
ATOM   10002 C  CA     . GLU   C 1  417 ? -32.168 -11.138  -2.106  1.00 43.66  ? 417 GLU   C CA     1 
ATOM   10003 C  C      . GLU   C 1  417 ? -30.747 -10.715  -1.787  1.00 39.93  ? 417 GLU   C C      1 
ATOM   10004 O  O      . GLU   C 1  417 ? -30.017 -11.434  -1.097  1.00 40.09  ? 417 GLU   C O      1 
ATOM   10005 C  CB     . GLU   C 1  417 ? -32.193 -11.791  -3.478  1.00 41.42  ? 417 GLU   C CB     1 
ATOM   10006 C  CG     . GLU   C 1  417 ? -33.414 -12.572  -3.697  1.00 45.75  ? 417 GLU   C CG     1 
ATOM   10007 C  CD     . GLU   C 1  417 ? -33.648 -12.855  -5.132  1.00 49.46  ? 417 GLU   C CD     1 
ATOM   10008 O  OE1    . GLU   C 1  417 ? -34.267 -11.987  -5.793  1.00 40.59  ? 417 GLU   C OE1    1 
ATOM   10009 O  OE2    . GLU   C 1  417 ? -33.195 -13.951  -5.571  1.00 53.71  ? 417 GLU   C OE2    1 
ATOM   10010 N  N      . PHE   C 1  418 ? -30.324 -9.576   -2.324  1.00 36.25  ? 418 PHE   C N      1 
ATOM   10011 C  CA     . PHE   C 1  418 ? -28.987 -9.080   -2.050  1.00 37.34  ? 418 PHE   C CA     1 
ATOM   10012 C  C      . PHE   C 1  418 ? -28.784 -8.880   -0.557  1.00 37.26  ? 418 PHE   C C      1 
ATOM   10013 O  O      . PHE   C 1  418 ? -27.896 -9.481   0.056   1.00 38.26  ? 418 PHE   C O      1 
ATOM   10014 C  CB     . PHE   C 1  418 ? -28.755 -7.791   -2.841  1.00 36.60  ? 418 PHE   C CB     1 
ATOM   10015 C  CG     . PHE   C 1  418 ? -28.290 -8.056   -4.229  1.00 34.61  ? 418 PHE   C CG     1 
ATOM   10016 C  CD1    . PHE   C 1  418 ? -29.171 -8.522   -5.182  1.00 33.30  ? 418 PHE   C CD1    1 
ATOM   10017 C  CD2    . PHE   C 1  418 ? -26.958 -7.927   -4.565  1.00 31.10  ? 418 PHE   C CD2    1 
ATOM   10018 C  CE1    . PHE   C 1  418 ? -28.729 -8.831   -6.453  1.00 34.71  ? 418 PHE   C CE1    1 
ATOM   10019 C  CE2    . PHE   C 1  418 ? -26.505 -8.223   -5.835  1.00 31.10  ? 418 PHE   C CE2    1 
ATOM   10020 C  CZ     . PHE   C 1  418 ? -27.389 -8.681   -6.784  1.00 32.37  ? 418 PHE   C CZ     1 
ATOM   10021 N  N      . SER   C 1  419 ? -29.620 -8.059   0.057   1.00 37.31  ? 419 SER   C N      1 
ATOM   10022 C  CA     . SER   C 1  419 ? -29.475 -7.833   1.487   1.00 36.45  ? 419 SER   C CA     1 
ATOM   10023 C  C      . SER   C 1  419 ? -29.764 -9.097   2.280   1.00 43.76  ? 419 SER   C C      1 
ATOM   10024 O  O      . SER   C 1  419 ? -29.155 -9.319   3.338   1.00 46.69  ? 419 SER   C O      1 
ATOM   10025 C  CB     . SER   C 1  419 ? -30.391 -6.692   1.893   1.00 34.26  ? 419 SER   C CB     1 
ATOM   10026 O  OG     . SER   C 1  419 ? -31.637 -6.905   1.246   1.00 46.53  ? 419 SER   C OG     1 
ATOM   10027 N  N      . GLU   C 1  420 ? -30.672 -9.945   1.782   1.00 39.06  ? 420 GLU   C N      1 
ATOM   10028 C  CA     . GLU   C 1  420 ? -30.948 -11.194  2.470   1.00 33.44  ? 420 GLU   C CA     1 
ATOM   10029 C  C      . GLU   C 1  420 ? -29.726 -12.097  2.451   1.00 35.58  ? 420 GLU   C C      1 
ATOM   10030 O  O      . GLU   C 1  420 ? -29.443 -12.789  3.429   1.00 36.80  ? 420 GLU   C O      1 
ATOM   10031 C  CB     . GLU   C 1  420 ? -32.158 -11.876  1.844   1.00 38.05  ? 420 GLU   C CB     1 
ATOM   10032 C  CG     . GLU   C 1  420 ? -32.320 -13.324  2.282   1.00 48.95  ? 420 GLU   C CG     1 
ATOM   10033 C  CD     . GLU   C 1  420 ? -33.385 -14.061  1.499   1.00 61.68  ? 420 GLU   C CD     1 
ATOM   10034 O  OE1    . GLU   C 1  420 ? -34.508 -13.510  1.364   1.00 70.89  ? 420 GLU   C OE1    1 
ATOM   10035 O  OE2    . GLU   C 1  420 ? -33.094 -15.181  1.016   1.00 53.40  ? 420 GLU   C OE2    1 
ATOM   10036 N  N      . ALA   C 1  421 ? -28.988 -12.110  1.344   1.00 40.28  ? 421 ALA   C N      1 
ATOM   10037 C  CA     . ALA   C 1  421 ? -27.746 -12.869  1.312   1.00 34.70  ? 421 ALA   C CA     1 
ATOM   10038 C  C      . ALA   C 1  421 ? -26.709 -12.224  2.211   1.00 36.74  ? 421 ALA   C C      1 
ATOM   10039 O  O      . ALA   C 1  421 ? -26.109 -12.884  3.063   1.00 38.86  ? 421 ALA   C O      1 
ATOM   10040 C  CB     . ALA   C 1  421 ? -27.222 -12.976  -0.119  1.00 30.42  ? 421 ALA   C CB     1 
ATOM   10041 N  N      . ARG   C 1  422 ? -26.493 -10.924  2.053   1.00 37.47  ? 422 ARG   C N      1 
ATOM   10042 C  CA     . ARG   C 1  422 ? -25.403 -10.318  2.796   1.00 35.76  ? 422 ARG   C CA     1 
ATOM   10043 C  C      . ARG   C 1  422 ? -25.625 -10.447  4.300   1.00 34.88  ? 422 ARG   C C      1 
ATOM   10044 O  O      . ARG   C 1  422 ? -24.669 -10.630  5.052   1.00 34.10  ? 422 ARG   C O      1 
ATOM   10045 C  CB     . ARG   C 1  422 ? -25.222 -8.864   2.382   1.00 33.26  ? 422 ARG   C CB     1 
ATOM   10046 C  CG     . ARG   C 1  422 ? -24.286 -8.157   3.304   1.00 36.00  ? 422 ARG   C CG     1 
ATOM   10047 C  CD     . ARG   C 1  422 ? -22.903 -8.639   2.990   1.00 34.40  ? 422 ARG   C CD     1 
ATOM   10048 N  NE     . ARG   C 1  422 ? -21.860 -7.881   3.647   1.00 31.38  ? 422 ARG   C NE     1 
ATOM   10049 C  CZ     . ARG   C 1  422 ? -21.350 -8.197   4.825   1.00 39.38  ? 422 ARG   C CZ     1 
ATOM   10050 N  NH1    . ARG   C 1  422 ? -21.914 -9.111   5.600   1.00 35.79  ? 422 ARG   C NH1    1 
ATOM   10051 N  NH2    . ARG   C 1  422 ? -20.242 -7.584   5.239   1.00 42.39  ? 422 ARG   C NH2    1 
ATOM   10052 N  N      . GLU   C 1  423 ? -26.875 -10.394  4.758   1.00 36.42  ? 423 GLU   C N      1 
ATOM   10053 C  CA     . GLU   C 1  423 ? -27.127 -10.584  6.181   1.00 38.22  ? 423 GLU   C CA     1 
ATOM   10054 C  C      . GLU   C 1  423 ? -26.775 -11.997  6.618   1.00 35.47  ? 423 GLU   C C      1 
ATOM   10055 O  O      . GLU   C 1  423 ? -26.281 -12.207  7.726   1.00 41.34  ? 423 GLU   C O      1 
ATOM   10056 C  CB     . GLU   C 1  423 ? -28.578 -10.281  6.486   1.00 37.06  ? 423 GLU   C CB     1 
ATOM   10057 C  CG     . GLU   C 1  423 ? -28.799 -8.844   6.751   1.00 50.11  ? 423 GLU   C CG     1 
ATOM   10058 C  CD     . GLU   C 1  423 ? -30.254 -8.484   6.702   1.00 62.43  ? 423 GLU   C CD     1 
ATOM   10059 O  OE1    . GLU   C 1  423 ? -31.063 -9.213   7.325   1.00 63.47  ? 423 GLU   C OE1    1 
ATOM   10060 O  OE2    . GLU   C 1  423 ? -30.585 -7.495   5.999   1.00 62.97  ? 423 GLU   C OE2    1 
ATOM   10061 N  N      . ASP   C 1  424 ? -27.049 -12.984  5.779   1.00 30.61  ? 424 ASP   C N      1 
ATOM   10062 C  CA     . ASP   C 1  424 ? -26.626 -14.329  6.103   1.00 24.64  ? 424 ASP   C CA     1 
ATOM   10063 C  C      . ASP   C 1  424 ? -25.123 -14.356  6.302   1.00 31.60  ? 424 ASP   C C      1 
ATOM   10064 O  O      . ASP   C 1  424 ? -24.633 -14.801  7.340   1.00 34.26  ? 424 ASP   C O      1 
ATOM   10065 C  CB     . ASP   C 1  424 ? -27.068 -15.285  5.001   1.00 26.37  ? 424 ASP   C CB     1 
ATOM   10066 C  CG     . ASP   C 1  424 ? -27.077 -16.694  5.456   1.00 28.42  ? 424 ASP   C CG     1 
ATOM   10067 O  OD1    . ASP   C 1  424 ? -26.753 -16.830  6.648   1.00 31.84  ? 424 ASP   C OD1    1 
ATOM   10068 O  OD2    . ASP   C 1  424 ? -27.411 -17.640  4.682   1.00 24.94  ? 424 ASP   C OD2    1 
ATOM   10069 N  N      . MET   C 1  425 ? -24.369 -13.838  5.324   1.00 35.49  ? 425 MET   C N      1 
ATOM   10070 C  CA     . MET   C 1  425 ? -22.910 -13.799  5.435   1.00 34.94  ? 425 MET   C CA     1 
ATOM   10071 C  C      . MET   C 1  425 ? -22.484 -13.040  6.683   1.00 35.47  ? 425 MET   C C      1 
ATOM   10072 O  O      . MET   C 1  425 ? -21.544 -13.430  7.376   1.00 34.16  ? 425 MET   C O      1 
ATOM   10073 C  CB     . MET   C 1  425 ? -22.302 -13.121  4.207   1.00 34.97  ? 425 MET   C CB     1 
ATOM   10074 C  CG     . MET   C 1  425 ? -22.528 -13.850  2.918   1.00 34.05  ? 425 MET   C CG     1 
ATOM   10075 S  SD     . MET   C 1  425 ? -22.026 -15.534  3.064   1.00 42.88  ? 425 MET   C SD     1 
ATOM   10076 C  CE     . MET   C 1  425 ? -20.308 -15.358  3.452   1.00 38.84  ? 425 MET   C CE     1 
ATOM   10077 N  N      . ALA   C 1  426 ? -23.142 -11.918  6.954   1.00 36.25  ? 426 ALA   C N      1 
ATOM   10078 C  CA     . ALA   C 1  426 ? -22.878 -11.168  8.169   1.00 30.49  ? 426 ALA   C CA     1 
ATOM   10079 C  C      . ALA   C 1  426 ? -23.003 -12.054  9.402   1.00 37.66  ? 426 ALA   C C      1 
ATOM   10080 O  O      . ALA   C 1  426 ? -22.206 -11.940  10.345  1.00 39.84  ? 426 ALA   C O      1 
ATOM   10081 C  CB     . ALA   C 1  426 ? -23.851 -10.005  8.242   1.00 27.39  ? 426 ALA   C CB     1 
ATOM   10082 N  N      . ALA   C 1  427 ? -24.021 -12.923  9.419   1.00 36.36  ? 427 ALA   C N      1 
ATOM   10083 C  CA     . ALA   C 1  427 ? -24.258 -13.806  10.552  1.00 32.19  ? 427 ALA   C CA     1 
ATOM   10084 C  C      . ALA   C 1  427 ? -23.257 -14.958  10.570  1.00 36.24  ? 427 ALA   C C      1 
ATOM   10085 O  O      . ALA   C 1  427 ? -22.686 -15.279  11.615  1.00 35.41  ? 427 ALA   C O      1 
ATOM   10086 C  CB     . ALA   C 1  427 ? -25.691 -14.312  10.498  1.00 25.51  ? 427 ALA   C CB     1 
ATOM   10087 N  N      . LEU   C 1  428 ? -23.029 -15.587  9.416   1.00 36.15  ? 428 LEU   C N      1 
ATOM   10088 C  CA     . LEU   C 1  428 ? -21.976 -16.581  9.292   1.00 31.05  ? 428 LEU   C CA     1 
ATOM   10089 C  C      . LEU   C 1  428 ? -20.676 -16.086  9.911   1.00 35.58  ? 428 LEU   C C      1 
ATOM   10090 O  O      . LEU   C 1  428 ? -19.953 -16.851  10.550  1.00 39.23  ? 428 LEU   C O      1 
ATOM   10091 C  CB     . LEU   C 1  428 ? -21.748 -16.894  7.824   1.00 29.78  ? 428 LEU   C CB     1 
ATOM   10092 C  CG     . LEU   C 1  428 ? -20.882 -18.121  7.625   1.00 30.34  ? 428 LEU   C CG     1 
ATOM   10093 C  CD1    . LEU   C 1  428 ? -21.600 -19.295  8.254   1.00 27.72  ? 428 LEU   C CD1    1 
ATOM   10094 C  CD2    . LEU   C 1  428 ? -20.510 -18.351  6.159   1.00 31.93  ? 428 LEU   C CD2    1 
ATOM   10095 N  N      . GLU   C 1  429 ? -20.335 -14.817  9.685   1.00 35.31  ? 429 GLU   C N      1 
ATOM   10096 C  CA     . GLU   C 1  429 ? -19.098 -14.268  10.229  1.00 33.66  ? 429 GLU   C CA     1 
ATOM   10097 C  C      . GLU   C 1  429 ? -19.165 -14.136  11.736  1.00 37.42  ? 429 GLU   C C      1 
ATOM   10098 O  O      . GLU   C 1  429 ? -18.130 -14.216  12.405  1.00 42.40  ? 429 GLU   C O      1 
ATOM   10099 C  CB     . GLU   C 1  429 ? -18.814 -12.902  9.600   1.00 37.29  ? 429 GLU   C CB     1 
ATOM   10100 C  CG     . GLU   C 1  429 ? -18.169 -12.913  8.216   1.00 44.24  ? 429 GLU   C CG     1 
ATOM   10101 C  CD     . GLU   C 1  429 ? -17.648 -11.535  7.838   1.00 49.64  ? 429 GLU   C CD     1 
ATOM   10102 O  OE1    . GLU   C 1  429 ? -16.784 -11.011  8.580   1.00 52.52  ? 429 GLU   C OE1    1 
ATOM   10103 O  OE2    . GLU   C 1  429 ? -18.075 -10.991  6.791   1.00 43.41  ? 429 GLU   C OE2    1 
ATOM   10104 N  N      . LYS   C 1  430 ? -20.357 -13.887  12.279  1.00 35.93  ? 430 LYS   C N      1 
ATOM   10105 C  CA     . LYS   C 1  430 ? -20.525 -13.785  13.723  1.00 41.85  ? 430 LYS   C CA     1 
ATOM   10106 C  C      . LYS   C 1  430 ? -20.550 -15.160  14.389  1.00 42.61  ? 430 LYS   C C      1 
ATOM   10107 O  O      . LYS   C 1  430 ? -19.960 -15.340  15.461  1.00 42.02  ? 430 LYS   C O      1 
ATOM   10108 C  CB     . LYS   C 1  430 ? -21.789 -12.985  14.061  1.00 39.15  ? 430 LYS   C CB     1 
ATOM   10109 C  CG     . LYS   C 1  430 ? -21.891 -12.695  15.546  1.00 54.19  ? 430 LYS   C CG     1 
ATOM   10110 C  CD     . LYS   C 1  430 ? -22.662 -11.460  15.927  1.00 68.93  ? 430 LYS   C CD     1 
ATOM   10111 C  CE     . LYS   C 1  430 ? -22.390 -11.146  17.412  1.00 81.48  ? 430 LYS   C CE     1 
ATOM   10112 N  NZ     . LYS   C 1  430 ? -20.920 -11.016  17.713  1.00 75.60  ? 430 LYS   C NZ     1 
ATOM   10113 N  N      . ASP   C 1  431 ? -21.223 -16.133  13.770  1.00 38.11  ? 431 ASP   C N      1 
ATOM   10114 C  CA     . ASP   C 1  431 ? -21.077 -17.517  14.186  1.00 35.88  ? 431 ASP   C CA     1 
ATOM   10115 C  C      . ASP   C 1  431 ? -19.606 -17.869  14.296  1.00 36.29  ? 431 ASP   C C      1 
ATOM   10116 O  O      . ASP   C 1  431 ? -19.153 -18.498  15.264  1.00 34.05  ? 431 ASP   C O      1 
ATOM   10117 C  CB     . ASP   C 1  431 ? -21.769 -18.420  13.180  1.00 30.14  ? 431 ASP   C CB     1 
ATOM   10118 C  CG     . ASP   C 1  431 ? -23.236 -18.132  13.087  1.00 41.89  ? 431 ASP   C CG     1 
ATOM   10119 O  OD1    . ASP   C 1  431 ? -23.791 -17.536  14.036  1.00 54.74  ? 431 ASP   C OD1    1 
ATOM   10120 O  OD2    . ASP   C 1  431 ? -23.841 -18.499  12.064  1.00 42.46  ? 431 ASP   C OD2    1 
ATOM   10121 N  N      . TYR   C 1  432 ? -18.832 -17.449  13.316  1.00 33.77  ? 432 TYR   C N      1 
ATOM   10122 C  CA     . TYR   C 1  432 ? -17.432 -17.787  13.387  1.00 32.74  ? 432 TYR   C CA     1 
ATOM   10123 C  C      . TYR   C 1  432 ? -16.780 -17.096  14.569  1.00 34.58  ? 432 TYR   C C      1 
ATOM   10124 O  O      . TYR   C 1  432 ? -15.953 -17.721  15.234  1.00 40.91  ? 432 TYR   C O      1 
ATOM   10125 C  CB     . TYR   C 1  432 ? -16.738 -17.538  12.029  1.00 31.70  ? 432 TYR   C CB     1 
ATOM   10126 C  CG     . TYR   C 1  432 ? -16.707 -18.829  11.199  1.00 30.09  ? 432 TYR   C CG     1 
ATOM   10127 C  CD1    . TYR   C 1  432 ? -15.771 -19.803  11.493  1.00 29.99  ? 432 TYR   C CD1    1 
ATOM   10128 C  CD2    . TYR   C 1  432 ? -17.592 -19.072  10.136  1.00 30.18  ? 432 TYR   C CD2    1 
ATOM   10129 C  CE1    . TYR   C 1  432 ? -15.696 -20.989  10.808  1.00 31.34  ? 432 TYR   C CE1    1 
ATOM   10130 C  CE2    . TYR   C 1  432 ? -17.523 -20.284  9.406   1.00 34.49  ? 432 TYR   C CE2    1 
ATOM   10131 C  CZ     . TYR   C 1  432 ? -16.553 -21.257  9.760   1.00 39.53  ? 432 TYR   C CZ     1 
ATOM   10132 O  OH     . TYR   C 1  432 ? -16.384 -22.509  9.118   1.00 35.20  ? 432 TYR   C OH     1 
ATOM   10133 N  N      . GLU   C 1  433 ? -17.191 -15.869  14.930  1.00 33.89  ? 433 GLU   C N      1 
ATOM   10134 C  CA     . GLU   C 1  433 ? -16.670 -15.309  16.180  1.00 37.07  ? 433 GLU   C CA     1 
ATOM   10135 C  C      . GLU   C 1  433 ? -17.146 -16.098  17.392  1.00 42.34  ? 433 GLU   C C      1 
ATOM   10136 O  O      . GLU   C 1  433 ? -16.357 -16.400  18.301  1.00 43.26  ? 433 GLU   C O      1 
ATOM   10137 C  CB     . GLU   C 1  433 ? -17.040 -13.840  16.364  1.00 43.32  ? 433 GLU   C CB     1 
ATOM   10138 C  CG     . GLU   C 1  433 ? -16.090 -12.839  15.697  1.00 63.06  ? 433 GLU   C CG     1 
ATOM   10139 C  CD     . GLU   C 1  433 ? -16.608 -11.406  15.762  1.00 77.20  ? 433 GLU   C CD     1 
ATOM   10140 O  OE1    . GLU   C 1  433 ? -17.188 -11.046  16.816  1.00 71.26  ? 433 GLU   C OE1    1 
ATOM   10141 O  OE2    . GLU   C 1  433 ? -16.427 -10.648  14.775  1.00 86.54  ? 433 GLU   C OE2    1 
ATOM   10142 N  N      . GLU   C 1  434 ? -18.435 -16.424  17.424  1.00 37.75  ? 434 GLU   C N      1 
ATOM   10143 C  CA     . GLU   C 1  434 ? -19.028 -17.026  18.604  1.00 35.16  ? 434 GLU   C CA     1 
ATOM   10144 C  C      . GLU   C 1  434 ? -18.383 -18.374  18.932  1.00 40.60  ? 434 GLU   C C      1 
ATOM   10145 O  O      . GLU   C 1  434 ? -18.087 -18.664  20.099  1.00 41.27  ? 434 GLU   C O      1 
ATOM   10146 C  CB     . GLU   C 1  434 ? -20.533 -17.155  18.381  1.00 38.81  ? 434 GLU   C CB     1 
ATOM   10147 C  CG     . GLU   C 1  434 ? -21.333 -15.881  18.690  1.00 44.31  ? 434 GLU   C CG     1 
ATOM   10148 C  CD     . GLU   C 1  434 ? -22.771 -15.907  18.154  1.00 59.37  ? 434 GLU   C CD     1 
ATOM   10149 O  OE1    . GLU   C 1  434 ? -23.279 -16.998  17.796  1.00 62.24  ? 434 GLU   C OE1    1 
ATOM   10150 O  OE2    . GLU   C 1  434 ? -23.398 -14.824  18.101  1.00 57.87  ? 434 GLU   C OE2    1 
ATOM   10151 N  N      . VAL   C 1  435 ? -18.159 -19.222  17.930  1.00 37.14  ? 435 VAL   C N      1 
ATOM   10152 C  CA     . VAL   C 1  435 ? -17.556 -20.507  18.255  1.00 33.32  ? 435 VAL   C CA     1 
ATOM   10153 C  C      . VAL   C 1  435 ? -16.230 -20.306  18.965  1.00 35.31  ? 435 VAL   C C      1 
ATOM   10154 O  O      . VAL   C 1  435 ? -15.814 -21.142  19.767  1.00 40.39  ? 435 VAL   C O      1 
ATOM   10155 C  CB     . VAL   C 1  435 ? -17.376 -21.362  16.990  1.00 33.52  ? 435 VAL   C CB     1 
ATOM   10156 C  CG1    . VAL   C 1  435 ? -18.700 -21.882  16.521  1.00 26.25  ? 435 VAL   C CG1    1 
ATOM   10157 C  CG2    . VAL   C 1  435 ? -16.663 -20.565  15.912  1.00 34.60  ? 435 VAL   C CG2    1 
ATOM   10158 N  N      . GLY   C 1  436 ? -15.541 -19.216  18.690  1.00 36.46  ? 436 GLY   C N      1 
ATOM   10159 C  CA     . GLY   C 1  436 ? -14.194 -19.106  19.215  1.00 39.92  ? 436 GLY   C CA     1 
ATOM   10160 C  C      . GLY   C 1  436 ? -14.083 -18.544  20.608  1.00 41.43  ? 436 GLY   C C      1 
ATOM   10161 O  O      . GLY   C 1  436 ? -13.027 -18.639  21.229  1.00 41.99  ? 436 GLY   C O      1 
ATOM   10162 N  N      . VAL   C 1  437 ? -15.151 -17.946  21.119  1.00 39.15  ? 437 VAL   C N      1 
ATOM   10163 C  CA     . VAL   C 1  437 ? -15.128 -17.392  22.457  1.00 35.99  ? 437 VAL   C CA     1 
ATOM   10164 C  C      . VAL   C 1  437 ? -15.111 -18.512  23.489  1.00 45.77  ? 437 VAL   C C      1 
ATOM   10165 O  O      . VAL   C 1  437 ? -15.735 -19.574  23.305  1.00 41.51  ? 437 VAL   C O      1 
ATOM   10166 C  CB     . VAL   C 1  437 ? -16.362 -16.509  22.645  1.00 38.36  ? 437 VAL   C CB     1 
ATOM   10167 C  CG1    . VAL   C 1  437 ? -16.519 -16.142  24.090  1.00 43.76  ? 437 VAL   C CG1    1 
ATOM   10168 C  CG2    . VAL   C 1  437 ? -16.279 -15.316  21.748  1.00 46.36  ? 437 VAL   C CG2    1 
ATOM   10169 N  N      . ASP   C 1  438 ? -14.416 -18.277  24.599  1.00 51.12  ? 438 ASP   C N      1 
ATOM   10170 C  CA     . ASP   C 1  438 ? -14.398 -19.264  25.669  1.00 47.07  ? 438 ASP   C CA     1 
ATOM   10171 C  C      . ASP   C 1  438 ? -15.788 -19.443  26.273  1.00 47.72  ? 438 ASP   C C      1 
ATOM   10172 O  O      . ASP   C 1  438 ? -16.714 -18.663  26.029  1.00 43.18  ? 438 ASP   C O      1 
ATOM   10173 C  CB     . ASP   C 1  438 ? -13.407 -18.866  26.755  1.00 44.28  ? 438 ASP   C CB     1 
ATOM   10174 C  CG     . ASP   C 1  438 ? -11.989 -19.100  26.354  1.00 49.11  ? 438 ASP   C CG     1 
ATOM   10175 O  OD1    . ASP   C 1  438 ? -11.739 -19.946  25.466  1.00 53.22  ? 438 ASP   C OD1    1 
ATOM   10176 O  OD2    . ASP   C 1  438 ? -11.122 -18.421  26.923  1.00 57.90  ? 438 ASP   C OD2    1 
ATOM   10177 N  N      . SER   C 1  439 ? -15.910 -20.498  27.088  1.00 49.97  ? 439 SER   C N      1 
ATOM   10178 C  CA     . SER   C 1  439 ? -17.142 -20.902  27.742  1.00 45.04  ? 439 SER   C CA     1 
ATOM   10179 C  C      . SER   C 1  439 ? -17.206 -20.290  29.139  1.00 54.82  ? 439 SER   C C      1 
ATOM   10180 O  O      . SER   C 1  439 ? -16.262 -19.636  29.593  1.00 55.04  ? 439 SER   C O      1 
ATOM   10181 C  CB     . SER   C 1  439 ? -17.229 -22.422  27.790  1.00 40.17  ? 439 SER   C CB     1 
ATOM   10182 O  OG     . SER   C 1  439 ? -16.779 -23.010  26.587  1.00 39.39  ? 439 SER   C OG     1 
ATOM   10183 N  N      . VAL   C 1  440 ? -18.324 -20.531  29.843  1.00 62.60  ? 440 VAL   C N      1 
ATOM   10184 C  CA     . VAL   C 1  440 ? -18.646 -19.831  31.093  1.00 60.27  ? 440 VAL   C CA     1 
ATOM   10185 C  C      . VAL   C 1  440 ? -19.079 -20.757  32.243  1.00 66.96  ? 440 VAL   C C      1 
ATOM   10186 O  O      . VAL   C 1  440 ? -18.712 -20.555  33.416  1.00 73.04  ? 440 VAL   C O      1 
ATOM   10187 C  CB     . VAL   C 1  440 ? -19.736 -18.800  30.821  1.00 64.14  ? 440 VAL   C CB     1 
ATOM   10188 C  CG1    . VAL   C 1  440 ? -19.156 -17.628  30.034  1.00 51.80  ? 440 VAL   C CG1    1 
ATOM   10189 C  CG2    . VAL   C 1  440 ? -20.915 -19.440  30.095  1.00 69.52  ? 440 VAL   C CG2    1 
ATOM   10190 N  N      . MET   D 2  1   ? -21.560 -21.362  -31.643 1.00 87.07  ? 1   MET   D N      1 
ATOM   10191 C  CA     . MET   D 2  1   ? -21.632 -20.125  -32.419 1.00 89.44  ? 1   MET   D CA     1 
ATOM   10192 C  C      . MET   D 2  1   ? -22.394 -19.028  -31.670 1.00 84.57  ? 1   MET   D C      1 
ATOM   10193 O  O      . MET   D 2  1   ? -23.487 -19.259  -31.153 1.00 86.99  ? 1   MET   D O      1 
ATOM   10194 C  CB     . MET   D 2  1   ? -22.328 -20.363  -33.751 1.00 96.58  ? 1   MET   D CB     1 
ATOM   10195 C  CG     . MET   D 2  1   ? -23.270 -21.546  -33.734 1.00 102.50 ? 1   MET   D CG     1 
ATOM   10196 S  SD     . MET   D 2  1   ? -23.902 -21.906  -35.382 1.00 125.33 ? 1   MET   D SD     1 
ATOM   10197 C  CE     . MET   D 2  1   ? -24.798 -23.442  -35.113 1.00 105.00 ? 1   MET   D CE     1 
ATOM   10198 N  N      . ARG   D 2  2   ? -21.818 -17.828  -31.633 1.00 72.18  ? 2   ARG   D N      1 
ATOM   10199 C  CA     . ARG   D 2  2   ? -22.422 -16.647  -31.017 1.00 62.29  ? 2   ARG   D CA     1 
ATOM   10200 C  C      . ARG   D 2  2   ? -22.359 -15.594  -32.109 1.00 64.77  ? 2   ARG   D C      1 
ATOM   10201 O  O      . ARG   D 2  2   ? -21.332 -14.949  -32.316 1.00 71.08  ? 2   ARG   D O      1 
ATOM   10202 C  CB     . ARG   D 2  2   ? -21.682 -16.240  -29.734 1.00 63.97  ? 2   ARG   D CB     1 
ATOM   10203 C  CG     . ARG   D 2  2   ? -21.748 -17.263  -28.611 1.00 58.84  ? 2   ARG   D CG     1 
ATOM   10204 C  CD     . ARG   D 2  2   ? -23.108 -17.223  -27.903 1.00 55.40  ? 2   ARG   D CD     1 
ATOM   10205 N  NE     . ARG   D 2  2   ? -23.284 -15.884  -27.331 1.00 64.14  ? 2   ARG   D NE     1 
ATOM   10206 C  CZ     . ARG   D 2  2   ? -24.396 -15.390  -26.788 1.00 63.25  ? 2   ARG   D CZ     1 
ATOM   10207 N  NH1    . ARG   D 2  2   ? -25.524 -16.077  -26.770 1.00 60.89  ? 2   ARG   D NH1    1 
ATOM   10208 N  NH2    . ARG   D 2  2   ? -24.368 -14.177  -26.229 1.00 57.57  ? 2   ARG   D NH2    1 
ATOM   10209 N  N      . GLU   D 2  3   ? -23.442 -15.452  -32.851 1.00 65.75  ? 3   GLU   D N      1 
ATOM   10210 C  CA     . GLU   D 2  3   ? -23.412 -14.567  -33.993 1.00 62.14  ? 3   GLU   D CA     1 
ATOM   10211 C  C      . GLU   D 2  3   ? -23.715 -13.150  -33.562 1.00 56.81  ? 3   GLU   D C      1 
ATOM   10212 O  O      . GLU   D 2  3   ? -24.591 -12.902  -32.736 1.00 60.46  ? 3   GLU   D O      1 
ATOM   10213 C  CB     . GLU   D 2  3   ? -24.391 -15.027  -35.074 1.00 66.62  ? 3   GLU   D CB     1 
ATOM   10214 C  CG     . GLU   D 2  3   ? -24.100 -16.433  -35.611 1.00 72.23  ? 3   GLU   D CG     1 
ATOM   10215 C  CD     . GLU   D 2  3   ? -24.783 -17.535  -34.824 1.00 71.78  ? 3   GLU   D CD     1 
ATOM   10216 O  OE1    . GLU   D 2  3   ? -25.354 -17.213  -33.764 1.00 70.62  ? 3   GLU   D OE1    1 
ATOM   10217 O  OE2    . GLU   D 2  3   ? -24.714 -18.716  -35.248 1.00 69.09  ? 3   GLU   D OE2    1 
ATOM   10218 N  N      . ILE   D 2  4   ? -22.956 -12.239  -34.089 1.00 58.70  ? 4   ILE   D N      1 
ATOM   10219 C  CA     . ILE   D 2  4   ? -23.255 -10.826  -34.004 1.00 57.90  ? 4   ILE   D CA     1 
ATOM   10220 C  C      . ILE   D 2  4   ? -23.753 -10.419  -35.380 1.00 62.51  ? 4   ILE   D C      1 
ATOM   10221 O  O      . ILE   D 2  4   ? -23.196 -10.840  -36.399 1.00 59.70  ? 4   ILE   D O      1 
ATOM   10222 C  CB     . ILE   D 2  4   ? -22.006 -10.027  -33.584 1.00 56.77  ? 4   ILE   D CB     1 
ATOM   10223 C  CG1    . ILE   D 2  4   ? -21.567 -10.476  -32.199 1.00 56.02  ? 4   ILE   D CG1    1 
ATOM   10224 C  CG2    . ILE   D 2  4   ? -22.309 -8.556   -33.526 1.00 54.95  ? 4   ILE   D CG2    1 
ATOM   10225 C  CD1    . ILE   D 2  4   ? -20.385 -9.771   -31.686 1.00 49.98  ? 4   ILE   D CD1    1 
ATOM   10226 N  N      . VAL   D 2  5   ? -24.841 -9.663   -35.414 1.00 63.22  ? 5   VAL   D N      1 
ATOM   10227 C  CA     . VAL   D 2  5   ? -25.329 -9.022   -36.626 1.00 52.91  ? 5   VAL   D CA     1 
ATOM   10228 C  C      . VAL   D 2  5   ? -24.812 -7.596   -36.663 1.00 62.75  ? 5   VAL   D C      1 
ATOM   10229 O  O      . VAL   D 2  5   ? -24.844 -6.892   -35.646 1.00 62.03  ? 5   VAL   D O      1 
ATOM   10230 C  CB     . VAL   D 2  5   ? -26.861 -9.079   -36.702 1.00 56.46  ? 5   VAL   D CB     1 
ATOM   10231 C  CG1    . VAL   D 2  5   ? -27.346 -8.339   -37.896 1.00 66.65  ? 5   VAL   D CG1    1 
ATOM   10232 C  CG2    . VAL   D 2  5   ? -27.283 -10.510  -36.899 1.00 59.32  ? 5   VAL   D CG2    1 
ATOM   10233 N  N      . HIS   D 2  6   ? -24.327 -7.182   -37.837 1.00 68.65  ? 6   HIS   D N      1 
ATOM   10234 C  CA     . HIS   D 2  6   ? -23.699 -5.892   -38.096 1.00 67.86  ? 6   HIS   D CA     1 
ATOM   10235 C  C      . HIS   D 2  6   ? -24.623 -4.976   -38.897 1.00 68.57  ? 6   HIS   D C      1 
ATOM   10236 O  O      . HIS   D 2  6   ? -25.421 -5.434   -39.718 1.00 67.74  ? 6   HIS   D O      1 
ATOM   10237 C  CB     . HIS   D 2  6   ? -22.389 -6.109   -38.853 1.00 68.99  ? 6   HIS   D CB     1 
ATOM   10238 C  CG     . HIS   D 2  6   ? -21.663 -4.850   -39.210 1.00 76.01  ? 6   HIS   D CG     1 
ATOM   10239 N  ND1    . HIS   D 2  6   ? -20.756 -4.247   -38.364 1.00 77.23  ? 6   HIS   D ND1    1 
ATOM   10240 C  CD2    . HIS   D 2  6   ? -21.661 -4.115   -40.349 1.00 75.99  ? 6   HIS   D CD2    1 
ATOM   10241 C  CE1    . HIS   D 2  6   ? -20.253 -3.175   -38.954 1.00 77.48  ? 6   HIS   D CE1    1 
ATOM   10242 N  NE2    . HIS   D 2  6   ? -20.786 -3.073   -40.160 1.00 77.78  ? 6   HIS   D NE2    1 
ATOM   10243 N  N      . ILE   D 2  7   ? -24.502 -3.672   -38.660 1.00 63.70  ? 7   ILE   D N      1 
ATOM   10244 C  CA     . ILE   D 2  7   ? -25.374 -2.695   -39.302 1.00 60.53  ? 7   ILE   D CA     1 
ATOM   10245 C  C      . ILE   D 2  7   ? -24.675 -1.352   -39.496 1.00 67.09  ? 7   ILE   D C      1 
ATOM   10246 O  O      . ILE   D 2  7   ? -24.476 -0.596   -38.532 1.00 60.06  ? 7   ILE   D O      1 
ATOM   10247 C  CB     . ILE   D 2  7   ? -26.696 -2.540   -38.514 1.00 56.61  ? 7   ILE   D CB     1 
ATOM   10248 C  CG1    . ILE   D 2  7   ? -27.463 -3.860   -38.477 1.00 58.17  ? 7   ILE   D CG1    1 
ATOM   10249 C  CG2    . ILE   D 2  7   ? -27.554 -1.383   -39.003 1.00 46.92  ? 7   ILE   D CG2    1 
ATOM   10250 C  CD1    . ILE   D 2  7   ? -28.883 -3.691   -37.974 1.00 57.95  ? 7   ILE   D CD1    1 
ATOM   10251 N  N      . GLN   D 2  8   ? -24.322 -1.057   -40.765 1.00 67.37  ? 8   GLN   D N      1 
ATOM   10252 C  CA     . GLN   D 2  8   ? -23.861 0.252    -41.232 1.00 59.70  ? 8   GLN   D CA     1 
ATOM   10253 C  C      . GLN   D 2  8   ? -25.030 1.120    -41.668 1.00 58.55  ? 8   GLN   D C      1 
ATOM   10254 O  O      . GLN   D 2  8   ? -25.974 0.628    -42.289 1.00 62.17  ? 8   GLN   D O      1 
ATOM   10255 C  CB     . GLN   D 2  8   ? -22.944 0.089    -42.424 1.00 59.36  ? 8   GLN   D CB     1 
ATOM   10256 C  CG     . GLN   D 2  8   ? -22.120 -1.132   -42.386 1.00 66.75  ? 8   GLN   D CG     1 
ATOM   10257 C  CD     . GLN   D 2  8   ? -21.268 -1.236   -43.619 1.00 72.33  ? 8   GLN   D CD     1 
ATOM   10258 O  OE1    . GLN   D 2  8   ? -21.509 -0.530   -44.613 1.00 71.64  ? 8   GLN   D OE1    1 
ATOM   10259 N  NE2    . GLN   D 2  8   ? -20.252 -2.100   -43.569 1.00 69.86  ? 8   GLN   D NE2    1 
ATOM   10260 N  N      . ALA   D 2  9   ? -24.939 2.419    -41.390 1.00 56.02  ? 9   ALA   D N      1 
ATOM   10261 C  CA     . ALA   D 2  9   ? -26.028 3.327    -41.708 1.00 62.50  ? 9   ALA   D CA     1 
ATOM   10262 C  C      . ALA   D 2  9   ? -25.481 4.726    -41.959 1.00 77.66  ? 9   ALA   D C      1 
ATOM   10263 O  O      . ALA   D 2  9   ? -24.511 5.164    -41.326 1.00 74.18  ? 9   ALA   D O      1 
ATOM   10264 C  CB     . ALA   D 2  9   ? -27.076 3.371    -40.599 1.00 58.50  ? 9   ALA   D CB     1 
ATOM   10265 N  N      . GLY   D 2  10  ? -26.136 5.433    -42.878 1.00 83.81  ? 10  GLY   D N      1 
ATOM   10266 C  CA     . GLY   D 2  10  ? -25.762 6.796    -43.204 1.00 86.37  ? 10  GLY   D CA     1 
ATOM   10267 C  C      . GLY   D 2  10  ? -24.470 6.882    -43.993 1.00 86.16  ? 10  GLY   D C      1 
ATOM   10268 O  O      . GLY   D 2  10  ? -23.873 5.870    -44.421 1.00 72.54  ? 10  GLY   D O      1 
ATOM   10269 N  N      . GLN   D 2  11  ? -24.017 8.124    -44.177 1.00 90.72  ? 11  GLN   D N      1 
ATOM   10270 C  CA     . GLN   D 2  11  ? -22.785 8.298    -44.937 1.00 95.94  ? 11  GLN   D CA     1 
ATOM   10271 C  C      . GLN   D 2  11  ? -21.584 7.780    -44.141 1.00 87.08  ? 11  GLN   D C      1 
ATOM   10272 O  O      . GLN   D 2  11  ? -20.899 6.841    -44.566 1.00 70.32  ? 11  GLN   D O      1 
ATOM   10273 C  CB     . GLN   D 2  11  ? -22.600 9.777    -45.308 1.00 101.93 ? 11  GLN   D CB     1 
ATOM   10274 C  CG     . GLN   D 2  11  ? -21.390 10.033   -46.203 1.00 98.11  ? 11  GLN   D CG     1 
ATOM   10275 C  CD     . GLN   D 2  11  ? -21.156 11.507   -46.549 1.00 94.36  ? 11  GLN   D CD     1 
ATOM   10276 O  OE1    . GLN   D 2  11  ? -21.832 12.440   -46.078 1.00 75.33  ? 11  GLN   D OE1    1 
ATOM   10277 N  NE2    . GLN   D 2  11  ? -20.167 11.711   -47.405 1.00 100.09 ? 11  GLN   D NE2    1 
ATOM   10278 N  N      . CYS   D 2  12  ? -21.328 8.386    -42.964 1.00 85.35  ? 12  CYS   D N      1 
ATOM   10279 C  CA     . CYS   D 2  12  ? -20.242 7.948    -42.078 1.00 82.16  ? 12  CYS   D CA     1 
ATOM   10280 C  C      . CYS   D 2  12  ? -20.311 6.463    -41.760 1.00 76.39  ? 12  CYS   D C      1 
ATOM   10281 O  O      . CYS   D 2  12  ? -19.301 5.752    -41.843 1.00 69.85  ? 12  CYS   D O      1 
ATOM   10282 C  CB     . CYS   D 2  12  ? -20.254 8.734    -40.772 1.00 84.28  ? 12  CYS   D CB     1 
ATOM   10283 S  SG     . CYS   D 2  12  ? -18.986 8.115    -39.585 1.00 69.37  ? 12  CYS   D SG     1 
ATOM   10284 N  N      . GLY   D 2  13  ? -21.484 5.991    -41.341 1.00 70.45  ? 13  GLY   D N      1 
ATOM   10285 C  CA     . GLY   D 2  13  ? -21.591 4.607    -40.917 1.00 70.01  ? 13  GLY   D CA     1 
ATOM   10286 C  C      . GLY   D 2  13  ? -21.011 3.628    -41.922 1.00 70.35  ? 13  GLY   D C      1 
ATOM   10287 O  O      . GLY   D 2  13  ? -20.204 2.756    -41.579 1.00 64.35  ? 13  GLY   D O      1 
ATOM   10288 N  N      . ASN   D 2  14  ? -21.416 3.751    -43.183 1.00 72.03  ? 14  ASN   D N      1 
ATOM   10289 C  CA     . ASN   D 2  14  ? -21.022 2.735    -44.148 1.00 70.62  ? 14  ASN   D CA     1 
ATOM   10290 C  C      . ASN   D 2  14  ? -19.511 2.721    -44.349 1.00 76.86  ? 14  ASN   D C      1 
ATOM   10291 O  O      . ASN   D 2  14  ? -18.898 1.648    -44.433 1.00 71.84  ? 14  ASN   D O      1 
ATOM   10292 C  CB     . ASN   D 2  14  ? -21.765 2.973    -45.449 1.00 65.08  ? 14  ASN   D CB     1 
ATOM   10293 C  CG     . ASN   D 2  14  ? -23.218 2.634    -45.326 1.00 71.37  ? 14  ASN   D CG     1 
ATOM   10294 O  OD1    . ASN   D 2  14  ? -23.612 1.470    -45.485 1.00 60.89  ? 14  ASN   D OD1    1 
ATOM   10295 N  ND2    . ASN   D 2  14  ? -24.035 3.644    -44.978 1.00 74.55  ? 14  ASN   D ND2    1 
ATOM   10296 N  N      . GLN   D 2  15  ? -18.882 3.901    -44.388 1.00 79.41  ? 15  GLN   D N      1 
ATOM   10297 C  CA     . GLN   D 2  15  ? -17.460 3.955    -44.706 1.00 74.19  ? 15  GLN   D CA     1 
ATOM   10298 C  C      . GLN   D 2  15  ? -16.630 3.263    -43.624 1.00 74.82  ? 15  GLN   D C      1 
ATOM   10299 O  O      . GLN   D 2  15  ? -15.872 2.324    -43.919 1.00 69.25  ? 15  GLN   D O      1 
ATOM   10300 C  CB     . GLN   D 2  15  ? -17.029 5.408    -44.914 1.00 78.01  ? 15  GLN   D CB     1 
ATOM   10301 C  CG     . GLN   D 2  15  ? -16.724 5.746    -46.399 1.00 85.01  ? 15  GLN   D CG     1 
ATOM   10302 C  CD     . GLN   D 2  15  ? -16.681 7.256    -46.677 1.00 89.65  ? 15  GLN   D CD     1 
ATOM   10303 O  OE1    . GLN   D 2  15  ? -17.728 7.916    -46.746 1.00 87.94  ? 15  GLN   D OE1    1 
ATOM   10304 N  NE2    . GLN   D 2  15  ? -15.474 7.793    -46.897 1.00 86.23  ? 15  GLN   D NE2    1 
ATOM   10305 N  N      . ILE   D 2  16  ? -16.785 3.683    -42.354 1.00 75.27  ? 16  ILE   D N      1 
ATOM   10306 C  CA     . ILE   D 2  16  ? -16.016 3.053    -41.275 1.00 70.46  ? 16  ILE   D CA     1 
ATOM   10307 C  C      . ILE   D 2  16  ? -16.416 1.591    -41.134 1.00 64.89  ? 16  ILE   D C      1 
ATOM   10308 O  O      . ILE   D 2  16  ? -15.588 0.742    -40.782 1.00 55.64  ? 16  ILE   D O      1 
ATOM   10309 C  CB     . ILE   D 2  16  ? -16.186 3.797    -39.937 1.00 65.34  ? 16  ILE   D CB     1 
ATOM   10310 C  CG1    . ILE   D 2  16  ? -17.447 3.349    -39.211 1.00 62.97  ? 16  ILE   D CG1    1 
ATOM   10311 C  CG2    . ILE   D 2  16  ? -16.310 5.282    -40.165 1.00 69.44  ? 16  ILE   D CG2    1 
ATOM   10312 C  CD1    . ILE   D 2  16  ? -17.618 4.009    -37.861 1.00 51.50  ? 16  ILE   D CD1    1 
ATOM   10313 N  N      . GLY   D 2  17  ? -17.685 1.275    -41.411 1.00 62.86  ? 17  GLY   D N      1 
ATOM   10314 C  CA     . GLY   D 2  17  ? -18.083 -0.119   -41.525 1.00 66.65  ? 17  GLY   D CA     1 
ATOM   10315 C  C      . GLY   D 2  17  ? -17.292 -0.876   -42.577 1.00 68.12  ? 17  GLY   D C      1 
ATOM   10316 O  O      . GLY   D 2  17  ? -16.899 -2.029   -42.367 1.00 66.87  ? 17  GLY   D O      1 
ATOM   10317 N  N      . ALA   D 2  18  ? -17.044 -0.240   -43.723 1.00 67.37  ? 18  ALA   D N      1 
ATOM   10318 C  CA     . ALA   D 2  18  ? -16.314 -0.923   -44.783 1.00 70.96  ? 18  ALA   D CA     1 
ATOM   10319 C  C      . ALA   D 2  18  ? -14.905 -1.298   -44.330 1.00 74.88  ? 18  ALA   D C      1 
ATOM   10320 O  O      . ALA   D 2  18  ? -14.502 -2.473   -44.391 1.00 62.19  ? 18  ALA   D O      1 
ATOM   10321 C  CB     . ALA   D 2  18  ? -16.269 -0.047   -46.028 1.00 67.83  ? 18  ALA   D CB     1 
ATOM   10322 N  N      . LYS   D 2  19  ? -14.140 -0.310   -43.854 1.00 74.04  ? 19  LYS   D N      1 
ATOM   10323 C  CA     . LYS   D 2  19  ? -12.735 -0.586   -43.583 1.00 72.75  ? 19  LYS   D CA     1 
ATOM   10324 C  C      . LYS   D 2  19  ? -12.604 -1.562   -42.424 1.00 70.60  ? 19  LYS   D C      1 
ATOM   10325 O  O      . LYS   D 2  19  ? -11.630 -2.323   -42.357 1.00 66.68  ? 19  LYS   D O      1 
ATOM   10326 C  CB     . LYS   D 2  19  ? -11.985 0.714    -43.310 1.00 75.86  ? 19  LYS   D CB     1 
ATOM   10327 C  CG     . LYS   D 2  19  ? -12.094 1.692    -44.489 1.00 85.64  ? 19  LYS   D CG     1 
ATOM   10328 C  CD     . LYS   D 2  19  ? -11.498 1.186    -45.813 1.00 85.67  ? 19  LYS   D CD     1 
ATOM   10329 C  CE     . LYS   D 2  19  ? -11.892 2.141    -46.951 1.00 85.62  ? 19  LYS   D CE     1 
ATOM   10330 N  NZ     . LYS   D 2  19  ? -11.616 1.589    -48.310 1.00 100.99 ? 19  LYS   D NZ     1 
ATOM   10331 N  N      . PHE   D 2  20  ? -13.600 -1.579   -41.526 1.00 73.03  ? 20  PHE   D N      1 
ATOM   10332 C  CA     . PHE   D 2  20  ? -13.648 -2.602   -40.485 1.00 68.69  ? 20  PHE   D CA     1 
ATOM   10333 C  C      . PHE   D 2  20  ? -13.620 -3.996   -41.100 1.00 69.54  ? 20  PHE   D C      1 
ATOM   10334 O  O      . PHE   D 2  20  ? -12.747 -4.814   -40.779 1.00 65.92  ? 20  PHE   D O      1 
ATOM   10335 C  CB     . PHE   D 2  20  ? -14.893 -2.421   -39.596 1.00 69.22  ? 20  PHE   D CB     1 
ATOM   10336 C  CG     . PHE   D 2  20  ? -15.189 -3.624   -38.712 1.00 71.76  ? 20  PHE   D CG     1 
ATOM   10337 C  CD1    . PHE   D 2  20  ? -14.418 -3.877   -37.586 1.00 66.20  ? 20  PHE   D CD1    1 
ATOM   10338 C  CD2    . PHE   D 2  20  ? -16.233 -4.485   -38.993 1.00 71.90  ? 20  PHE   D CD2    1 
ATOM   10339 C  CE1    . PHE   D 2  20  ? -14.649 -4.975   -36.796 1.00 61.44  ? 20  PHE   D CE1    1 
ATOM   10340 C  CE2    . PHE   D 2  20  ? -16.474 -5.583   -38.188 1.00 68.16  ? 20  PHE   D CE2    1 
ATOM   10341 C  CZ     . PHE   D 2  20  ? -15.682 -5.820   -37.089 1.00 64.75  ? 20  PHE   D CZ     1 
ATOM   10342 N  N      . TRP   D 2  21  ? -14.560 -4.275   -42.009 1.00 68.19  ? 21  TRP   D N      1 
ATOM   10343 C  CA     . TRP   D 2  21  ? -14.616 -5.588   -42.644 1.00 69.62  ? 21  TRP   D CA     1 
ATOM   10344 C  C      . TRP   D 2  21  ? -13.334 -5.909   -43.401 1.00 68.84  ? 21  TRP   D C      1 
ATOM   10345 O  O      . TRP   D 2  21  ? -12.876 -7.058   -43.402 1.00 66.28  ? 21  TRP   D O      1 
ATOM   10346 C  CB     . TRP   D 2  21  ? -15.834 -5.658   -43.551 1.00 68.62  ? 21  TRP   D CB     1 
ATOM   10347 C  CG     . TRP   D 2  21  ? -17.078 -5.741   -42.765 1.00 65.77  ? 21  TRP   D CG     1 
ATOM   10348 C  CD1    . TRP   D 2  21  ? -17.990 -4.750   -42.552 1.00 65.70  ? 21  TRP   D CD1    1 
ATOM   10349 C  CD2    . TRP   D 2  21  ? -17.573 -6.899   -42.090 1.00 63.21  ? 21  TRP   D CD2    1 
ATOM   10350 N  NE1    . TRP   D 2  21  ? -19.017 -5.217   -41.762 1.00 66.99  ? 21  TRP   D NE1    1 
ATOM   10351 C  CE2    . TRP   D 2  21  ? -18.785 -6.536   -41.470 1.00 66.37  ? 21  TRP   D CE2    1 
ATOM   10352 C  CE3    . TRP   D 2  21  ? -17.107 -8.208   -41.947 1.00 61.67  ? 21  TRP   D CE3    1 
ATOM   10353 C  CZ2    . TRP   D 2  21  ? -19.536 -7.433   -40.718 1.00 64.06  ? 21  TRP   D CZ2    1 
ATOM   10354 C  CZ3    . TRP   D 2  21  ? -17.854 -9.095   -41.199 1.00 67.99  ? 21  TRP   D CZ3    1 
ATOM   10355 C  CH2    . TRP   D 2  21  ? -19.054 -8.704   -40.592 1.00 65.24  ? 21  TRP   D CH2    1 
ATOM   10356 N  N      . GLU   D 2  22  ? -12.731 -4.912   -44.044 1.00 69.86  ? 22  GLU   D N      1 
ATOM   10357 C  CA     . GLU   D 2  22  ? -11.448 -5.159   -44.690 1.00 71.42  ? 22  GLU   D CA     1 
ATOM   10358 C  C      . GLU   D 2  22  ? -10.424 -5.646   -43.670 1.00 73.05  ? 22  GLU   D C      1 
ATOM   10359 O  O      . GLU   D 2  22  ? -9.749  -6.661   -43.883 1.00 69.73  ? 22  GLU   D O      1 
ATOM   10360 C  CB     . GLU   D 2  22  ? -10.964 -3.891   -45.393 1.00 75.18  ? 22  GLU   D CB     1 
ATOM   10361 C  CG     . GLU   D 2  22  ? -11.592 -3.651   -46.772 1.00 84.71  ? 22  GLU   D CG     1 
ATOM   10362 C  CD     . GLU   D 2  22  ? -11.338 -2.243   -47.285 1.00 88.95  ? 22  GLU   D CD     1 
ATOM   10363 O  OE1    . GLU   D 2  22  ? -10.215 -1.737   -47.062 1.00 92.44  ? 22  GLU   D OE1    1 
ATOM   10364 O  OE2    . GLU   D 2  22  ? -12.266 -1.630   -47.867 1.00 81.34  ? 22  GLU   D OE2    1 
ATOM   10365 N  N      . VAL   D 2  23  ? -10.336 -4.958   -42.526 1.00 72.59  ? 23  VAL   D N      1 
ATOM   10366 C  CA     . VAL   D 2  23  ? -9.235  -5.180   -41.591 1.00 64.67  ? 23  VAL   D CA     1 
ATOM   10367 C  C      . VAL   D 2  23  ? -9.366  -6.538   -40.921 1.00 70.50  ? 23  VAL   D C      1 
ATOM   10368 O  O      . VAL   D 2  23  ? -8.417  -7.332   -40.898 1.00 71.15  ? 23  VAL   D O      1 
ATOM   10369 C  CB     . VAL   D 2  23  ? -9.184  -4.060   -40.540 1.00 64.84  ? 23  VAL   D CB     1 
ATOM   10370 C  CG1    . VAL   D 2  23  ? -8.047  -4.311   -39.572 1.00 62.24  ? 23  VAL   D CG1    1 
ATOM   10371 C  CG2    . VAL   D 2  23  ? -9.079  -2.695   -41.183 1.00 67.60  ? 23  VAL   D CG2    1 
ATOM   10372 N  N      . ILE   D 2  24  ? -10.533 -6.812   -40.331 1.00 71.30  ? 24  ILE   D N      1 
ATOM   10373 C  CA     . ILE   D 2  24  ? -10.709 -8.078   -39.629 1.00 73.43  ? 24  ILE   D CA     1 
ATOM   10374 C  C      . ILE   D 2  24  ? -10.787 -9.238   -40.612 1.00 73.12  ? 24  ILE   D C      1 
ATOM   10375 O  O      . ILE   D 2  24  ? -10.535 -10.390  -40.232 1.00 67.37  ? 24  ILE   D O      1 
ATOM   10376 C  CB     . ILE   D 2  24  ? -11.943 -8.011   -38.703 1.00 70.46  ? 24  ILE   D CB     1 
ATOM   10377 C  CG1    . ILE   D 2  24  ? -13.239 -8.080   -39.495 1.00 69.28  ? 24  ILE   D CG1    1 
ATOM   10378 C  CG2    . ILE   D 2  24  ? -11.938 -6.741   -37.876 1.00 68.99  ? 24  ILE   D CG2    1 
ATOM   10379 C  CD1    . ILE   D 2  24  ? -14.435 -8.231   -38.611 1.00 65.79  ? 24  ILE   D CD1    1 
ATOM   10380 N  N      . SER   D 2  25  ? -11.110 -8.950   -41.879 1.00 72.41  ? 25  SER   D N      1 
ATOM   10381 C  CA     . SER   D 2  25  ? -11.020 -9.961   -42.929 1.00 73.81  ? 25  SER   D CA     1 
ATOM   10382 C  C      . SER   D 2  25  ? -9.575  -10.388  -43.140 1.00 77.62  ? 25  SER   D C      1 
ATOM   10383 O  O      . SER   D 2  25  ? -9.256  -11.582  -43.148 1.00 73.26  ? 25  SER   D O      1 
ATOM   10384 C  CB     . SER   D 2  25  ? -11.593 -9.406   -44.226 1.00 69.82  ? 25  SER   D CB     1 
ATOM   10385 O  OG     . SER   D 2  25  ? -12.898 -8.935   -44.013 1.00 70.98  ? 25  SER   D OG     1 
ATOM   10386 N  N      . ASP   D 2  26  ? -8.687  -9.411   -43.335 1.00 76.29  ? 26  ASP   D N      1 
ATOM   10387 C  CA     . ASP   D 2  26  ? -7.262  -9.693   -43.429 1.00 72.85  ? 26  ASP   D CA     1 
ATOM   10388 C  C      . ASP   D 2  26  ? -6.740  -10.452  -42.219 1.00 77.42  ? 26  ASP   D C      1 
ATOM   10389 O  O      . ASP   D 2  26  ? -5.945  -11.389  -42.370 1.00 79.25  ? 26  ASP   D O      1 
ATOM   10390 C  CB     . ASP   D 2  26  ? -6.491  -8.399   -43.602 1.00 71.55  ? 26  ASP   D CB     1 
ATOM   10391 C  CG     . ASP   D 2  26  ? -5.023  -8.582   -43.347 1.00 80.60  ? 26  ASP   D CG     1 
ATOM   10392 O  OD1    . ASP   D 2  26  ? -4.344  -9.196   -44.194 1.00 93.35  ? 26  ASP   D OD1    1 
ATOM   10393 O  OD2    . ASP   D 2  26  ? -4.548  -8.089   -42.302 1.00 76.33  ? 26  ASP   D OD2    1 
ATOM   10394 N  N      . GLU   D 2  27  ? -7.136  -10.038  -41.009 1.00 77.23  ? 27  GLU   D N      1 
ATOM   10395 C  CA     . GLU   D 2  27  ? -6.658  -10.711  -39.805 1.00 72.14  ? 27  GLU   D CA     1 
ATOM   10396 C  C      . GLU   D 2  27  ? -7.068  -12.177  -39.789 1.00 76.63  ? 27  GLU   D C      1 
ATOM   10397 O  O      . GLU   D 2  27  ? -6.285  -13.043  -39.383 1.00 74.29  ? 27  GLU   D O      1 
ATOM   10398 C  CB     . GLU   D 2  27  ? -7.182  -10.005  -38.562 1.00 72.39  ? 27  GLU   D CB     1 
ATOM   10399 C  CG     . GLU   D 2  27  ? -6.944  -8.511   -38.531 1.00 73.96  ? 27  GLU   D CG     1 
ATOM   10400 C  CD     . GLU   D 2  27  ? -7.148  -7.919   -37.135 1.00 72.56  ? 27  GLU   D CD     1 
ATOM   10401 O  OE1    . GLU   D 2  27  ? -7.678  -8.627   -36.253 1.00 67.89  ? 27  GLU   D OE1    1 
ATOM   10402 O  OE2    . GLU   D 2  27  ? -6.778  -6.743   -36.922 1.00 75.39  ? 27  GLU   D OE2    1 
ATOM   10403 N  N      . HIS   D 2  28  ? -8.292  -12.474  -40.235 1.00 83.08  ? 28  HIS   D N      1 
ATOM   10404 C  CA     . HIS   D 2  28  ? -8.820  -13.833  -40.315 1.00 84.78  ? 28  HIS   D CA     1 
ATOM   10405 C  C      . HIS   D 2  28  ? -8.446  -14.558  -41.610 1.00 86.30  ? 28  HIS   D C      1 
ATOM   10406 O  O      . HIS   D 2  28  ? -8.798  -15.732  -41.771 1.00 89.95  ? 28  HIS   D O      1 
ATOM   10407 C  CB     . HIS   D 2  28  ? -10.355 -13.822  -40.179 1.00 85.20  ? 28  HIS   D CB     1 
ATOM   10408 C  CG     . HIS   D 2  28  ? -10.862 -13.464  -38.810 1.00 83.46  ? 28  HIS   D CG     1 
ATOM   10409 N  ND1    . HIS   D 2  28  ? -10.858 -14.355  -37.756 1.00 76.43  ? 28  HIS   D ND1    1 
ATOM   10410 C  CD2    . HIS   D 2  28  ? -11.462 -12.341  -38.349 1.00 73.75  ? 28  HIS   D CD2    1 
ATOM   10411 C  CE1    . HIS   D 2  28  ? -11.385 -13.777  -36.692 1.00 70.26  ? 28  HIS   D CE1    1 
ATOM   10412 N  NE2    . HIS   D 2  28  ? -11.766 -12.558  -37.027 1.00 70.75  ? 28  HIS   D NE2    1 
ATOM   10413 N  N      . GLY   D 2  29  ? -7.769  -13.895  -42.543 1.00 86.89  ? 29  GLY   D N      1 
ATOM   10414 C  CA     . GLY   D 2  29  ? -7.404  -14.533  -43.796 1.00 93.25  ? 29  GLY   D CA     1 
ATOM   10415 C  C      . GLY   D 2  29  ? -8.583  -14.814  -44.707 1.00 94.96  ? 29  GLY   D C      1 
ATOM   10416 O  O      . GLY   D 2  29  ? -8.919  -15.978  -44.954 1.00 95.68  ? 29  GLY   D O      1 
ATOM   10417 N  N      . ILE   D 2  30  ? -9.219  -13.752  -45.208 1.00 89.07  ? 30  ILE   D N      1 
ATOM   10418 C  CA     . ILE   D 2  30  ? -10.345 -13.846  -46.131 1.00 85.11  ? 30  ILE   D CA     1 
ATOM   10419 C  C      . ILE   D 2  30  ? -10.207 -12.764  -47.189 1.00 94.21  ? 30  ILE   D C      1 
ATOM   10420 O  O      . ILE   D 2  30  ? -10.180 -11.571  -46.868 1.00 93.99  ? 30  ILE   D O      1 
ATOM   10421 C  CB     . ILE   D 2  30  ? -11.704 -13.722  -45.426 1.00 84.08  ? 30  ILE   D CB     1 
ATOM   10422 C  CG1    . ILE   D 2  30  ? -12.022 -15.000  -44.645 1.00 86.19  ? 30  ILE   D CG1    1 
ATOM   10423 C  CG2    . ILE   D 2  30  ? -12.793 -13.365  -46.421 1.00 89.60  ? 30  ILE   D CG2    1 
ATOM   10424 C  CD1    . ILE   D 2  30  ? -13.427 -15.046  -44.126 1.00 78.41  ? 30  ILE   D CD1    1 
ATOM   10425 N  N      . ASP   D 2  31  ? -10.139 -13.175  -48.441 1.00 98.31  ? 31  ASP   D N      1 
ATOM   10426 C  CA     . ASP   D 2  31  ? -10.019 -12.279  -49.581 1.00 97.15  ? 31  ASP   D CA     1 
ATOM   10427 C  C      . ASP   D 2  31  ? -11.387 -11.809  -50.036 1.00 96.43  ? 31  ASP   D C      1 
ATOM   10428 O  O      . ASP   D 2  31  ? -12.423 -12.336  -49.628 1.00 100.27 ? 31  ASP   D O      1 
ATOM   10429 C  CB     . ASP   D 2  31  ? -9.299  -13.005  -50.700 1.00 91.89  ? 31  ASP   D CB     1 
ATOM   10430 C  CG     . ASP   D 2  31  ? -9.892  -14.355  -50.945 1.00 96.49  ? 31  ASP   D CG     1 
ATOM   10431 O  OD1    . ASP   D 2  31  ? -11.062 -14.548  -50.556 1.00 97.36  ? 31  ASP   D OD1    1 
ATOM   10432 O  OD2    . ASP   D 2  31  ? -9.179  -15.235  -51.473 1.00 103.34 ? 31  ASP   D OD2    1 
ATOM   10433 N  N      . PRO   D 2  32  ? -11.433 -10.807  -50.912 1.00 90.43  ? 32  PRO   D N      1 
ATOM   10434 C  CA     . PRO   D 2  32  ? -12.733 -10.238  -51.298 1.00 95.48  ? 32  PRO   D CA     1 
ATOM   10435 C  C      . PRO   D 2  32  ? -13.700 -11.256  -51.888 1.00 91.46  ? 32  PRO   D C      1 
ATOM   10436 O  O      . PRO   D 2  32  ? -14.888 -10.946  -52.037 1.00 93.07  ? 32  PRO   D O      1 
ATOM   10437 C  CB     . PRO   D 2  32  ? -12.353 -9.146   -52.310 1.00 97.20  ? 32  PRO   D CB     1 
ATOM   10438 C  CG     . PRO   D 2  32  ? -10.941 -8.772   -51.917 1.00 96.53  ? 32  PRO   D CG     1 
ATOM   10439 C  CD     . PRO   D 2  32  ? -10.302 -10.068  -51.494 1.00 87.12  ? 32  PRO   D CD     1 
ATOM   10440 N  N      . THR   D 2  33  ? -13.252 -12.466  -52.201 1.00 89.69  ? 33  THR   D N      1 
ATOM   10441 C  CA     . THR   D 2  33  ? -14.194 -13.454  -52.698 1.00 99.26  ? 33  THR   D CA     1 
ATOM   10442 C  C      . THR   D 2  33  ? -14.933 -14.165  -51.571 1.00 105.45 ? 33  THR   D C      1 
ATOM   10443 O  O      . THR   D 2  33  ? -16.046 -14.654  -51.790 1.00 109.64 ? 33  THR   D O      1 
ATOM   10444 C  CB     . THR   D 2  33  ? -13.489 -14.496  -53.576 1.00 100.54 ? 33  THR   D CB     1 
ATOM   10445 O  OG1    . THR   D 2  33  ? -14.437 -15.485  -53.992 1.00 107.89 ? 33  THR   D OG1    1 
ATOM   10446 C  CG2    . THR   D 2  33  ? -12.409 -15.201  -52.798 1.00 99.16  ? 33  THR   D CG2    1 
ATOM   10447 N  N      . GLY   D 2  34  ? -14.350 -14.232  -50.379 1.00 99.95  ? 34  GLY   D N      1 
ATOM   10448 C  CA     . GLY   D 2  34  ? -14.977 -14.908  -49.267 1.00 94.61  ? 34  GLY   D CA     1 
ATOM   10449 C  C      . GLY   D 2  34  ? -14.361 -16.233  -48.896 1.00 96.92  ? 34  GLY   D C      1 
ATOM   10450 O  O      . GLY   D 2  34  ? -14.910 -16.934  -48.039 1.00 96.31  ? 34  GLY   D O      1 
ATOM   10451 N  N      . SER   D 2  35  ? -13.249 -16.604  -49.510 1.00 101.11 ? 35  SER   D N      1 
ATOM   10452 C  CA     . SER   D 2  35  ? -12.568 -17.847  -49.188 1.00 100.81 ? 35  SER   D CA     1 
ATOM   10453 C  C      . SER   D 2  35  ? -11.372 -17.574  -48.278 1.00 94.73  ? 35  SER   D C      1 
ATOM   10454 O  O      . SER   D 2  35  ? -10.931 -16.436  -48.098 1.00 92.70  ? 35  SER   D O      1 
ATOM   10455 C  CB     . SER   D 2  35  ? -12.156 -18.571  -50.477 1.00 103.49 ? 35  SER   D CB     1 
ATOM   10456 O  OG     . SER   D 2  35  ? -11.646 -17.662  -51.441 1.00 103.03 ? 35  SER   D OG     1 
ATOM   10457 N  N      . TYR   D 2  36  ? -10.855 -18.641  -47.690 1.00 90.93  ? 36  TYR   D N      1 
ATOM   10458 C  CA     . TYR   D 2  36  ? -9.909  -18.542  -46.586 1.00 94.79  ? 36  TYR   D CA     1 
ATOM   10459 C  C      . TYR   D 2  36  ? -8.519  -18.960  -47.045 1.00 98.57  ? 36  TYR   D C      1 
ATOM   10460 O  O      . TYR   D 2  36  ? -8.207  -20.151  -47.119 1.00 93.99  ? 36  TYR   D O      1 
ATOM   10461 C  CB     . TYR   D 2  36  ? -10.363 -19.396  -45.412 1.00 95.73  ? 36  TYR   D CB     1 
ATOM   10462 C  CG     . TYR   D 2  36  ? -9.294  -19.574  -44.368 1.00 97.29  ? 36  TYR   D CG     1 
ATOM   10463 C  CD1    . TYR   D 2  36  ? -8.838  -18.494  -43.618 1.00 96.89  ? 36  TYR   D CD1    1 
ATOM   10464 C  CD2    . TYR   D 2  36  ? -8.721  -20.817  -44.147 1.00 97.11  ? 36  TYR   D CD2    1 
ATOM   10465 C  CE1    . TYR   D 2  36  ? -7.852  -18.654  -42.663 1.00 97.91  ? 36  TYR   D CE1    1 
ATOM   10466 C  CE2    . TYR   D 2  36  ? -7.734  -20.988  -43.197 1.00 100.54 ? 36  TYR   D CE2    1 
ATOM   10467 C  CZ     . TYR   D 2  36  ? -7.303  -19.906  -42.455 1.00 100.15 ? 36  TYR   D CZ     1 
ATOM   10468 O  OH     . TYR   D 2  36  ? -6.319  -20.086  -41.508 1.00 97.62  ? 36  TYR   D OH     1 
ATOM   10469 N  N      . HIS   D 2  37  ? -7.678  -17.975  -47.325 1.00 103.52 ? 37  HIS   D N      1 
ATOM   10470 C  CA     . HIS   D 2  37  ? -6.262  -18.202  -47.570 1.00 105.29 ? 37  HIS   D CA     1 
ATOM   10471 C  C      . HIS   D 2  37  ? -5.528  -17.702  -46.336 1.00 106.22 ? 37  HIS   D C      1 
ATOM   10472 O  O      . HIS   D 2  37  ? -4.996  -16.594  -46.304 1.00 111.70 ? 37  HIS   D O      1 
ATOM   10473 C  CB     . HIS   D 2  37  ? -5.817  -17.512  -48.817 1.00 111.33 ? 37  HIS   D CB     1 
ATOM   10474 C  CG     . HIS   D 2  37  ? -6.298  -18.183  -50.063 1.00 120.75 ? 37  HIS   D CG     1 
ATOM   10475 N  ND1    . HIS   D 2  37  ? -7.573  -18.008  -50.555 1.00 116.60 ? 37  HIS   D ND1    1 
ATOM   10476 C  CD2    . HIS   D 2  37  ? -5.686  -19.056  -50.899 1.00 119.39 ? 37  HIS   D CD2    1 
ATOM   10477 C  CE1    . HIS   D 2  37  ? -7.721  -18.733  -51.650 1.00 121.81 ? 37  HIS   D CE1    1 
ATOM   10478 N  NE2    . HIS   D 2  37  ? -6.592  -19.378  -51.881 1.00 119.62 ? 37  HIS   D NE2    1 
ATOM   10479 N  N      . GLY   D 2  38  ? -5.521  -18.539  -45.301 1.00 101.08 ? 38  GLY   D N      1 
ATOM   10480 C  CA     . GLY   D 2  38  ? -4.958  -18.159  -44.029 1.00 110.10 ? 38  GLY   D CA     1 
ATOM   10481 C  C      . GLY   D 2  38  ? -3.979  -19.199  -43.520 1.00 115.58 ? 38  GLY   D C      1 
ATOM   10482 O  O      . GLY   D 2  38  ? -4.062  -20.385  -43.839 1.00 112.27 ? 38  GLY   D O      1 
ATOM   10483 N  N      . ASP   D 2  39  ? -3.048  -18.723  -42.696 1.00 118.42 ? 39  ASP   D N      1 
ATOM   10484 C  CA     . ASP   D 2  39  ? -1.996  -19.588  -42.181 1.00 120.26 ? 39  ASP   D CA     1 
ATOM   10485 C  C      . ASP   D 2  39  ? -2.461  -20.393  -40.975 1.00 116.04 ? 39  ASP   D C      1 
ATOM   10486 O  O      . ASP   D 2  39  ? -2.385  -21.624  -40.971 1.00 121.55 ? 39  ASP   D O      1 
ATOM   10487 C  CB     . ASP   D 2  39  ? -0.771  -18.756  -41.812 1.00 127.15 ? 39  ASP   D CB     1 
ATOM   10488 C  CG     . ASP   D 2  39  ? 0.488   -19.569  -41.846 1.00 136.08 ? 39  ASP   D CG     1 
ATOM   10489 O  OD1    . ASP   D 2  39  ? 0.366   -20.809  -41.951 1.00 140.81 ? 39  ASP   D OD1    1 
ATOM   10490 O  OD2    . ASP   D 2  39  ? 1.587   -18.988  -41.760 1.00 138.31 ? 39  ASP   D OD2    1 
ATOM   10491 N  N      . SER   D 2  40  ? -2.924  -19.709  -39.934 1.00 114.16 ? 40  SER   D N      1 
ATOM   10492 C  CA     . SER   D 2  40  ? -3.320  -20.343  -38.686 1.00 101.90 ? 40  SER   D CA     1 
ATOM   10493 C  C      . SER   D 2  40  ? -4.830  -20.527  -38.638 1.00 98.34  ? 40  SER   D C      1 
ATOM   10494 O  O      . SER   D 2  40  ? -5.589  -19.662  -39.086 1.00 98.45  ? 40  SER   D O      1 
ATOM   10495 C  CB     . SER   D 2  40  ? -2.858  -19.504  -37.496 1.00 98.06  ? 40  SER   D CB     1 
ATOM   10496 O  OG     . SER   D 2  40  ? -3.235  -20.101  -36.275 1.00 93.16  ? 40  SER   D OG     1 
ATOM   10497 N  N      . ASP   D 2  41  ? -5.263  -21.664  -38.095 1.00 95.81  ? 41  ASP   D N      1 
ATOM   10498 C  CA     . ASP   D 2  41  ? -6.690  -21.900  -37.923 1.00 95.47  ? 41  ASP   D CA     1 
ATOM   10499 C  C      . ASP   D 2  41  ? -7.281  -21.079  -36.788 1.00 99.52  ? 41  ASP   D C      1 
ATOM   10500 O  O      . ASP   D 2  41  ? -8.509  -21.007  -36.666 1.00 100.03 ? 41  ASP   D O      1 
ATOM   10501 C  CB     . ASP   D 2  41  ? -6.966  -23.379  -37.662 1.00 99.40  ? 41  ASP   D CB     1 
ATOM   10502 C  CG     . ASP   D 2  41  ? -5.979  -23.995  -36.703 1.00 103.75 ? 41  ASP   D CG     1 
ATOM   10503 O  OD1    . ASP   D 2  41  ? -4.881  -23.421  -36.525 1.00 106.14 ? 41  ASP   D OD1    1 
ATOM   10504 O  OD2    . ASP   D 2  41  ? -6.301  -25.062  -36.138 1.00 100.61 ? 41  ASP   D OD2    1 
ATOM   10505 N  N      . LEU   D 2  42  ? -6.443  -20.474  -35.948 1.00 99.28  ? 42  LEU   D N      1 
ATOM   10506 C  CA     . LEU   D 2  42  ? -6.950  -19.549  -34.947 1.00 92.96  ? 42  LEU   D CA     1 
ATOM   10507 C  C      . LEU   D 2  42  ? -7.864  -18.516  -35.580 1.00 94.17  ? 42  LEU   D C      1 
ATOM   10508 O  O      . LEU   D 2  42  ? -8.729  -17.949  -34.901 1.00 96.49  ? 42  LEU   D O      1 
ATOM   10509 C  CB     . LEU   D 2  42  ? -5.787  -18.859  -34.252 1.00 89.79  ? 42  LEU   D CB     1 
ATOM   10510 C  CG     . LEU   D 2  42  ? -5.002  -19.806  -33.359 1.00 93.15  ? 42  LEU   D CG     1 
ATOM   10511 C  CD1    . LEU   D 2  42  ? -3.926  -19.047  -32.620 1.00 99.81  ? 42  LEU   D CD1    1 
ATOM   10512 C  CD2    . LEU   D 2  42  ? -5.930  -20.505  -32.403 1.00 88.80  ? 42  LEU   D CD2    1 
ATOM   10513 N  N      . GLN   D 2  43  ? -7.684  -18.260  -36.878 1.00 86.95  ? 43  GLN   D N      1 
ATOM   10514 C  CA     . GLN   D 2  43  ? -8.456  -17.266  -37.608 1.00 88.87  ? 43  GLN   D CA     1 
ATOM   10515 C  C      . GLN   D 2  43  ? -9.856  -17.736  -37.954 1.00 85.02  ? 43  GLN   D C      1 
ATOM   10516 O  O      . GLN   D 2  43  ? -10.691 -16.912  -38.345 1.00 80.93  ? 43  GLN   D O      1 
ATOM   10517 C  CB     . GLN   D 2  43  ? -7.724  -16.887  -38.889 1.00 91.33  ? 43  GLN   D CB     1 
ATOM   10518 C  CG     . GLN   D 2  43  ? -6.339  -16.357  -38.656 1.00 89.28  ? 43  GLN   D CG     1 
ATOM   10519 C  CD     . GLN   D 2  43  ? -5.513  -16.404  -39.906 1.00 96.98  ? 43  GLN   D CD     1 
ATOM   10520 O  OE1    . GLN   D 2  43  ? -5.043  -15.374  -40.381 1.00 106.31 ? 43  GLN   D OE1    1 
ATOM   10521 N  NE2    . GLN   D 2  43  ? -5.316  -17.606  -40.448 1.00 98.88  ? 43  GLN   D NE2    1 
ATOM   10522 N  N      . LEU   D 2  44  ? -10.127 -19.029  -37.832 1.00 82.15  ? 44  LEU   D N      1 
ATOM   10523 C  CA     . LEU   D 2  44  ? -11.433 -19.570  -38.163 1.00 82.46  ? 44  LEU   D CA     1 
ATOM   10524 C  C      . LEU   D 2  44  ? -12.233 -20.003  -36.949 1.00 85.86  ? 44  LEU   D C      1 
ATOM   10525 O  O      . LEU   D 2  44  ? -13.457 -19.860  -36.959 1.00 88.49  ? 44  LEU   D O      1 
ATOM   10526 C  CB     . LEU   D 2  44  ? -11.286 -20.756  -39.122 1.00 82.26  ? 44  LEU   D CB     1 
ATOM   10527 C  CG     . LEU   D 2  44  ? -10.689 -20.431  -40.491 1.00 87.58  ? 44  LEU   D CG     1 
ATOM   10528 C  CD1    . LEU   D 2  44  ? -10.655 -21.694  -41.319 1.00 85.09  ? 44  LEU   D CD1    1 
ATOM   10529 C  CD2    . LEU   D 2  44  ? -11.490 -19.322  -41.204 1.00 82.97  ? 44  LEU   D CD2    1 
ATOM   10530 N  N      . GLU   D 2  45  ? -11.565 -20.477  -35.893 1.00 88.42  ? 45  GLU   D N      1 
ATOM   10531 C  CA     . GLU   D 2  45  ? -12.205 -21.033  -34.701 1.00 81.56  ? 45  GLU   D CA     1 
ATOM   10532 C  C      . GLU   D 2  45  ? -13.453 -20.303  -34.217 1.00 77.61  ? 45  GLU   D C      1 
ATOM   10533 O  O      . GLU   D 2  45  ? -14.405 -20.933  -33.750 1.00 80.38  ? 45  GLU   D O      1 
ATOM   10534 C  CB     . GLU   D 2  45  ? -11.222 -21.062  -33.552 1.00 78.77  ? 45  GLU   D CB     1 
ATOM   10535 C  CG     . GLU   D 2  45  ? -11.591 -22.100  -32.562 1.00 83.91  ? 45  GLU   D CG     1 
ATOM   10536 C  CD     . GLU   D 2  45  ? -10.558 -22.237  -31.498 1.00 92.79  ? 45  GLU   D CD     1 
ATOM   10537 O  OE1    . GLU   D 2  45  ? -10.321 -21.232  -30.797 1.00 93.83  ? 45  GLU   D OE1    1 
ATOM   10538 O  OE2    . GLU   D 2  45  ? -9.988  -23.339  -31.363 1.00 97.08  ? 45  GLU   D OE2    1 
ATOM   10539 N  N      . ARG   D 2  46  ? -13.451 -18.980  -34.292 1.00 75.20  ? 46  ARG   D N      1 
ATOM   10540 C  CA     . ARG   D 2  46  ? -14.609 -18.180  -33.928 1.00 74.79  ? 46  ARG   D CA     1 
ATOM   10541 C  C      . ARG   D 2  46  ? -15.026 -17.298  -35.100 1.00 74.37  ? 46  ARG   D C      1 
ATOM   10542 O  O      . ARG   D 2  46  ? -15.570 -16.204  -34.918 1.00 66.08  ? 46  ARG   D O      1 
ATOM   10543 C  CB     . ARG   D 2  46  ? -14.309 -17.349  -32.681 1.00 77.89  ? 46  ARG   D CB     1 
ATOM   10544 C  CG     . ARG   D 2  46  ? -14.303 -18.164  -31.382 1.00 81.97  ? 46  ARG   D CG     1 
ATOM   10545 C  CD     . ARG   D 2  46  ? -14.076 -17.293  -30.145 1.00 80.03  ? 46  ARG   D CD     1 
ATOM   10546 N  NE     . ARG   D 2  46  ? -15.305 -16.572  -29.832 1.00 89.51  ? 46  ARG   D NE     1 
ATOM   10547 C  CZ     . ARG   D 2  46  ? -15.486 -15.793  -28.775 1.00 81.24  ? 46  ARG   D CZ     1 
ATOM   10548 N  NH1    . ARG   D 2  46  ? -14.554 -15.663  -27.848 1.00 77.39  ? 46  ARG   D NH1    1 
ATOM   10549 N  NH2    . ARG   D 2  46  ? -16.635 -15.126  -28.650 1.00 77.24  ? 46  ARG   D NH2    1 
ATOM   10550 N  N      . ILE   D 2  47  ? -14.768 -17.773  -36.320 1.00 76.14  ? 47  ILE   D N      1 
ATOM   10551 C  CA     . ILE   D 2  47  ? -14.969 -16.933  -37.492 1.00 78.02  ? 47  ILE   D CA     1 
ATOM   10552 C  C      . ILE   D 2  47  ? -16.441 -16.685  -37.762 1.00 75.65  ? 47  ILE   D C      1 
ATOM   10553 O  O      . ILE   D 2  47  ? -16.794 -15.683  -38.397 1.00 71.00  ? 47  ILE   D O      1 
ATOM   10554 C  CB     . ILE   D 2  47  ? -14.296 -17.549  -38.728 1.00 75.58  ? 47  ILE   D CB     1 
ATOM   10555 C  CG1    . ILE   D 2  47  ? -14.319 -16.534  -39.866 1.00 77.97  ? 47  ILE   D CG1    1 
ATOM   10556 C  CG2    . ILE   D 2  47  ? -15.002 -18.821  -39.144 1.00 73.67  ? 47  ILE   D CG2    1 
ATOM   10557 C  CD1    . ILE   D 2  47  ? -13.469 -15.325  -39.601 1.00 75.76  ? 47  ILE   D CD1    1 
ATOM   10558 N  N      . ASN   D 2  48  ? -17.306 -17.583  -37.299 1.00 74.59  ? 48  ASN   D N      1 
ATOM   10559 C  CA     . ASN   D 2  48  ? -18.750 -17.474  -37.449 1.00 76.60  ? 48  ASN   D CA     1 
ATOM   10560 C  C      . ASN   D 2  48  ? -19.374 -16.357  -36.612 1.00 74.92  ? 48  ASN   D C      1 
ATOM   10561 O  O      . ASN   D 2  48  ? -20.560 -16.043  -36.793 1.00 66.20  ? 48  ASN   D O      1 
ATOM   10562 C  CB     . ASN   D 2  48  ? -19.350 -18.827  -37.104 1.00 71.84  ? 48  ASN   D CB     1 
ATOM   10563 C  CG     . ASN   D 2  48  ? -18.730 -19.410  -35.861 1.00 84.66  ? 48  ASN   D CG     1 
ATOM   10564 O  OD1    . ASN   D 2  48  ? -17.545 -19.771  -35.876 1.00 83.73  ? 48  ASN   D OD1    1 
ATOM   10565 N  ND2    . ASN   D 2  48  ? -19.499 -19.486  -34.772 1.00 84.99  ? 48  ASN   D ND2    1 
ATOM   10566 N  N      . VAL   D 2  49  ? -18.614 -15.741  -35.709 1.00 72.50  ? 49  VAL   D N      1 
ATOM   10567 C  CA     . VAL   D 2  49  ? -19.133 -14.585  -34.990 1.00 69.48  ? 49  VAL   D CA     1 
ATOM   10568 C  C      . VAL   D 2  49  ? -19.563 -13.504  -35.978 1.00 69.87  ? 49  VAL   D C      1 
ATOM   10569 O  O      . VAL   D 2  49  ? -20.673 -12.958  -35.894 1.00 64.20  ? 49  VAL   D O      1 
ATOM   10570 C  CB     . VAL   D 2  49  ? -18.079 -14.061  -34.001 1.00 62.34  ? 49  VAL   D CB     1 
ATOM   10571 C  CG1    . VAL   D 2  49  ? -18.386 -12.615  -33.620 1.00 61.77  ? 49  VAL   D CG1    1 
ATOM   10572 C  CG2    . VAL   D 2  49  ? -18.010 -14.958  -32.792 1.00 64.94  ? 49  VAL   D CG2    1 
ATOM   10573 N  N      . TYR   D 2  50  ? -18.694 -13.191  -36.940 1.00 67.25  ? 50  TYR   D N      1 
ATOM   10574 C  CA     . TYR   D 2  50  ? -18.931 -12.114  -37.886 1.00 66.96  ? 50  TYR   D CA     1 
ATOM   10575 C  C      . TYR   D 2  50  ? -19.165 -12.600  -39.308 1.00 71.55  ? 50  TYR   D C      1 
ATOM   10576 O  O      . TYR   D 2  50  ? -19.387 -11.775  -40.199 1.00 71.21  ? 50  TYR   D O      1 
ATOM   10577 C  CB     . TYR   D 2  50  ? -17.750 -11.146  -37.863 1.00 65.56  ? 50  TYR   D CB     1 
ATOM   10578 C  CG     . TYR   D 2  50  ? -17.759 -10.168  -36.710 1.00 63.87  ? 50  TYR   D CG     1 
ATOM   10579 C  CD1    . TYR   D 2  50  ? -18.565 -9.044   -36.748 1.00 64.99  ? 50  TYR   D CD1    1 
ATOM   10580 C  CD2    . TYR   D 2  50  ? -16.969 -10.369  -35.586 1.00 58.62  ? 50  TYR   D CD2    1 
ATOM   10581 C  CE1    . TYR   D 2  50  ? -18.584 -8.141   -35.709 1.00 62.73  ? 50  TYR   D CE1    1 
ATOM   10582 C  CE2    . TYR   D 2  50  ? -16.977 -9.472   -34.539 1.00 58.85  ? 50  TYR   D CE2    1 
ATOM   10583 C  CZ     . TYR   D 2  50  ? -17.787 -8.351   -34.605 1.00 63.13  ? 50  TYR   D CZ     1 
ATOM   10584 O  OH     . TYR   D 2  50  ? -17.814 -7.426   -33.574 1.00 55.97  ? 50  TYR   D OH     1 
ATOM   10585 N  N      . TYR   D 2  51  ? -19.143 -13.907  -39.545 1.00 68.94  ? 51  TYR   D N      1 
ATOM   10586 C  CA     . TYR   D 2  51  ? -19.137 -14.430  -40.899 1.00 69.77  ? 51  TYR   D CA     1 
ATOM   10587 C  C      . TYR   D 2  51  ? -20.120 -15.581  -41.039 1.00 74.36  ? 51  TYR   D C      1 
ATOM   10588 O  O      . TYR   D 2  51  ? -20.102 -16.525  -40.239 1.00 69.11  ? 51  TYR   D O      1 
ATOM   10589 C  CB     . TYR   D 2  51  ? -17.730 -14.896  -41.296 1.00 79.43  ? 51  TYR   D CB     1 
ATOM   10590 C  CG     . TYR   D 2  51  ? -16.759 -13.764  -41.493 1.00 78.68  ? 51  TYR   D CG     1 
ATOM   10591 C  CD1    . TYR   D 2  51  ? -16.735 -13.053  -42.681 1.00 82.15  ? 51  TYR   D CD1    1 
ATOM   10592 C  CD2    . TYR   D 2  51  ? -15.855 -13.415  -40.501 1.00 76.32  ? 51  TYR   D CD2    1 
ATOM   10593 C  CE1    . TYR   D 2  51  ? -15.851 -12.014  -42.869 1.00 82.63  ? 51  TYR   D CE1    1 
ATOM   10594 C  CE2    . TYR   D 2  51  ? -14.964 -12.379  -40.680 1.00 74.03  ? 51  TYR   D CE2    1 
ATOM   10595 C  CZ     . TYR   D 2  51  ? -14.969 -11.685  -41.865 1.00 79.35  ? 51  TYR   D CZ     1 
ATOM   10596 O  OH     . TYR   D 2  51  ? -14.095 -10.651  -42.069 1.00 81.90  ? 51  TYR   D OH     1 
ATOM   10597 N  N      . ASN   D 2  52  ? -20.958 -15.501  -42.076 1.00 80.10  ? 52  ASN   D N      1 
ATOM   10598 C  CA     . ASN   D 2  52  ? -21.857 -16.577  -42.475 1.00 76.72  ? 52  ASN   D CA     1 
ATOM   10599 C  C      . ASN   D 2  52  ? -21.102 -17.574  -43.345 1.00 77.66  ? 52  ASN   D C      1 
ATOM   10600 O  O      . ASN   D 2  52  ? -20.322 -17.187  -44.215 1.00 80.91  ? 52  ASN   D O      1 
ATOM   10601 C  CB     . ASN   D 2  52  ? -23.011 -16.001  -43.279 1.00 74.01  ? 52  ASN   D CB     1 
ATOM   10602 C  CG     . ASN   D 2  52  ? -24.078 -15.408  -42.414 1.00 71.68  ? 52  ASN   D CG     1 
ATOM   10603 O  OD1    . ASN   D 2  52  ? -24.362 -15.907  -41.326 1.00 70.15  ? 52  ASN   D OD1    1 
ATOM   10604 N  ND2    . ASN   D 2  52  ? -24.646 -14.287  -42.873 1.00 65.26  ? 52  ASN   D ND2    1 
ATOM   10605 N  N      . GLU   D 2  53  ? -21.340 -18.858  -43.139 1.00 86.59  ? 53  GLU   D N      1 
ATOM   10606 C  CA     . GLU   D 2  53  ? -20.600 -19.867  -43.884 1.00 88.64  ? 53  GLU   D CA     1 
ATOM   10607 C  C      . GLU   D 2  53  ? -21.431 -20.296  -45.087 1.00 95.97  ? 53  GLU   D C      1 
ATOM   10608 O  O      . GLU   D 2  53  ? -22.532 -20.833  -44.935 1.00 103.39 ? 53  GLU   D O      1 
ATOM   10609 C  CB     . GLU   D 2  53  ? -20.250 -21.058  -42.993 1.00 92.55  ? 53  GLU   D CB     1 
ATOM   10610 C  CG     . GLU   D 2  53  ? -19.167 -21.955  -43.567 1.00 98.23  ? 53  GLU   D CG     1 
ATOM   10611 C  CD     . GLU   D 2  53  ? -18.884 -23.167  -42.697 1.00 106.26 ? 53  GLU   D CD     1 
ATOM   10612 O  OE1    . GLU   D 2  53  ? -19.451 -23.262  -41.585 1.00 102.47 ? 53  GLU   D OE1    1 
ATOM   10613 O  OE2    . GLU   D 2  53  ? -18.063 -24.010  -43.116 1.00 113.12 ? 53  GLU   D OE2    1 
ATOM   10614 N  N      . ALA   D 2  54  ? -20.917 -20.031  -46.280 1.00 100.59 ? 54  ALA   D N      1 
ATOM   10615 C  CA     . ALA   D 2  54  ? -21.543 -20.458  -47.523 1.00 104.77 ? 54  ALA   D CA     1 
ATOM   10616 C  C      . ALA   D 2  54  ? -20.724 -21.599  -48.113 1.00 117.25 ? 54  ALA   D C      1 
ATOM   10617 O  O      . ALA   D 2  54  ? -19.491 -21.514  -48.186 1.00 116.60 ? 54  ALA   D O      1 
ATOM   10618 C  CB     . ALA   D 2  54  ? -21.650 -19.299  -48.520 1.00 94.94  ? 54  ALA   D CB     1 
ATOM   10619 N  N      . THR   D 2  55  ? -21.407 -22.668  -48.514 1.00 121.62 ? 55  THR   D N      1 
ATOM   10620 C  CA     . THR   D 2  55  ? -20.724 -23.787  -49.143 1.00 118.89 ? 55  THR   D CA     1 
ATOM   10621 C  C      . THR   D 2  55  ? -19.945 -23.314  -50.374 1.00 116.49 ? 55  THR   D C      1 
ATOM   10622 O  O      . THR   D 2  55  ? -20.167 -22.224  -50.917 1.00 109.39 ? 55  THR   D O      1 
ATOM   10623 C  CB     . THR   D 2  55  ? -21.719 -24.891  -49.504 1.00 120.68 ? 55  THR   D CB     1 
ATOM   10624 O  OG1    . THR   D 2  55  ? -22.825 -24.328  -50.222 1.00 127.22 ? 55  THR   D OG1    1 
ATOM   10625 C  CG2    . THR   D 2  55  ? -22.223 -25.587  -48.245 1.00 115.58 ? 55  THR   D CG2    1 
ATOM   10626 N  N      . GLY   D 2  56  ? -19.025 -24.165  -50.818 1.00 117.88 ? 56  GLY   D N      1 
ATOM   10627 C  CA     . GLY   D 2  56  ? -17.876 -23.668  -51.533 1.00 112.44 ? 56  GLY   D CA     1 
ATOM   10628 C  C      . GLY   D 2  56  ? -16.898 -22.979  -50.612 1.00 112.32 ? 56  GLY   D C      1 
ATOM   10629 O  O      . GLY   D 2  56  ? -16.138 -22.121  -51.066 1.00 116.66 ? 56  GLY   D O      1 
ATOM   10630 N  N      . ASN   D 2  57  ? -16.898 -23.349  -49.323 1.00 105.92 ? 57  ASN   D N      1 
ATOM   10631 C  CA     . ASN   D 2  57  ? -16.235 -22.628  -48.236 1.00 105.90 ? 57  ASN   D CA     1 
ATOM   10632 C  C      . ASN   D 2  57  ? -16.000 -21.157  -48.527 1.00 108.24 ? 57  ASN   D C      1 
ATOM   10633 O  O      . ASN   D 2  57  ? -14.854 -20.706  -48.641 1.00 108.62 ? 57  ASN   D O      1 
ATOM   10634 C  CB     . ASN   D 2  57  ? -14.908 -23.284  -47.840 1.00 106.99 ? 57  ASN   D CB     1 
ATOM   10635 C  CG     . ASN   D 2  57  ? -15.096 -24.469  -46.910 1.00 113.93 ? 57  ASN   D CG     1 
ATOM   10636 O  OD1    . ASN   D 2  57  ? -14.968 -25.622  -47.315 1.00 122.27 ? 57  ASN   D OD1    1 
ATOM   10637 N  ND2    . ASN   D 2  57  ? -15.372 -24.181  -45.638 1.00 99.93  ? 57  ASN   D ND2    1 
ATOM   10638 N  N      . LYS   D 2  58  ? -17.080 -20.398  -48.618 1.00 104.61 ? 58  LYS   D N      1 
ATOM   10639 C  CA     . LYS   D 2  58  ? -17.009 -18.954  -48.714 1.00 101.20 ? 58  LYS   D CA     1 
ATOM   10640 C  C      . LYS   D 2  58  ? -17.675 -18.355  -47.486 1.00 92.65  ? 58  LYS   D C      1 
ATOM   10641 O  O      . LYS   D 2  58  ? -18.726 -18.829  -47.053 1.00 96.14  ? 58  LYS   D O      1 
ATOM   10642 C  CB     . LYS   D 2  58  ? -17.668 -18.465  -50.006 1.00 102.78 ? 58  LYS   D CB     1 
ATOM   10643 C  CG     . LYS   D 2  58  ? -16.857 -18.806  -51.252 1.00 102.37 ? 58  LYS   D CG     1 
ATOM   10644 C  CD     . LYS   D 2  58  ? -15.960 -17.636  -51.649 1.00 102.99 ? 58  LYS   D CD     1 
ATOM   10645 C  CE     . LYS   D 2  58  ? -15.287 -17.853  -52.991 1.00 99.91  ? 58  LYS   D CE     1 
ATOM   10646 N  NZ     . LYS   D 2  58  ? -14.440 -19.062  -52.990 1.00 108.12 ? 58  LYS   D NZ     1 
ATOM   10647 N  N      . TYR   D 2  59  ? -17.042 -17.341  -46.901 1.00 90.43  ? 59  TYR   D N      1 
ATOM   10648 C  CA     . TYR   D 2  59  ? -17.508 -16.729  -45.662 1.00 82.94  ? 59  TYR   D CA     1 
ATOM   10649 C  C      . TYR   D 2  59  ? -18.075 -15.355  -45.977 1.00 80.64  ? 59  TYR   D C      1 
ATOM   10650 O  O      . TYR   D 2  59  ? -17.404 -14.536  -46.614 1.00 83.59  ? 59  TYR   D O      1 
ATOM   10651 C  CB     . TYR   D 2  59  ? -16.375 -16.587  -44.658 1.00 84.57  ? 59  TYR   D CB     1 
ATOM   10652 C  CG     . TYR   D 2  59  ? -15.759 -17.897  -44.265 1.00 82.48  ? 59  TYR   D CG     1 
ATOM   10653 C  CD1    . TYR   D 2  59  ? -16.405 -18.762  -43.416 1.00 82.21  ? 59  TYR   D CD1    1 
ATOM   10654 C  CD2    . TYR   D 2  59  ? -14.505 -18.249  -44.729 1.00 82.38  ? 59  TYR   D CD2    1 
ATOM   10655 C  CE1    . TYR   D 2  59  ? -15.832 -19.950  -43.060 1.00 88.65  ? 59  TYR   D CE1    1 
ATOM   10656 C  CE2    . TYR   D 2  59  ? -13.922 -19.424  -44.373 1.00 77.77  ? 59  TYR   D CE2    1 
ATOM   10657 C  CZ     . TYR   D 2  59  ? -14.587 -20.275  -43.539 1.00 85.62  ? 59  TYR   D CZ     1 
ATOM   10658 O  OH     . TYR   D 2  59  ? -14.002 -21.465  -43.183 1.00 90.57  ? 59  TYR   D OH     1 
ATOM   10659 N  N      . VAL   D 2  60  ? -19.293 -15.099  -45.526 1.00 79.52  ? 60  VAL   D N      1 
ATOM   10660 C  CA     . VAL   D 2  60  ? -20.032 -13.888  -45.870 1.00 75.02  ? 60  VAL   D CA     1 
ATOM   10661 C  C      . VAL   D 2  60  ? -20.148 -13.024  -44.623 1.00 74.00  ? 60  VAL   D C      1 
ATOM   10662 O  O      . VAL   D 2  60  ? -20.601 -13.513  -43.584 1.00 74.92  ? 60  VAL   D O      1 
ATOM   10663 C  CB     . VAL   D 2  60  ? -21.431 -14.205  -46.423 1.00 70.89  ? 60  VAL   D CB     1 
ATOM   10664 C  CG1    . VAL   D 2  60  ? -22.020 -12.959  -47.098 1.00 74.63  ? 60  VAL   D CG1    1 
ATOM   10665 C  CG2    . VAL   D 2  60  ? -21.391 -15.416  -47.325 1.00 65.26  ? 60  VAL   D CG2    1 
ATOM   10666 N  N      . PRO   D 2  61  ? -19.775 -11.758  -44.683 1.00 74.86  ? 61  PRO   D N      1 
ATOM   10667 C  CA     . PRO   D 2  61  ? -20.066 -10.859  -43.566 1.00 74.37  ? 61  PRO   D CA     1 
ATOM   10668 C  C      . PRO   D 2  61  ? -21.545 -10.918  -43.222 1.00 75.02  ? 61  PRO   D C      1 
ATOM   10669 O  O      . PRO   D 2  61  ? -22.405 -10.825  -44.099 1.00 78.99  ? 61  PRO   D O      1 
ATOM   10670 C  CB     . PRO   D 2  61  ? -19.679 -9.485   -44.116 1.00 74.92  ? 61  PRO   D CB     1 
ATOM   10671 C  CG     . PRO   D 2  61  ? -18.673 -9.789   -45.188 1.00 81.65  ? 61  PRO   D CG     1 
ATOM   10672 C  CD     . PRO   D 2  61  ? -19.152 -11.059  -45.817 1.00 80.74  ? 61  PRO   D CD     1 
ATOM   10673 N  N      . ARG   D 2  62  ? -21.850 -11.085  -41.936 1.00 70.94  ? 62  ARG   D N      1 
ATOM   10674 C  CA     . ARG   D 2  62  ? -23.228 -10.932  -41.481 1.00 66.71  ? 62  ARG   D CA     1 
ATOM   10675 C  C      . ARG   D 2  62  ? -23.519 -9.440   -41.324 1.00 68.14  ? 62  ARG   D C      1 
ATOM   10676 O  O      . ARG   D 2  62  ? -23.660 -8.904   -40.222 1.00 65.82  ? 62  ARG   D O      1 
ATOM   10677 C  CB     . ARG   D 2  62  ? -23.467 -11.677  -40.181 1.00 63.72  ? 62  ARG   D CB     1 
ATOM   10678 C  CG     . ARG   D 2  62  ? -24.933 -11.987  -39.974 1.00 66.32  ? 62  ARG   D CG     1 
ATOM   10679 C  CD     . ARG   D 2  62  ? -25.146 -12.718  -38.694 1.00 69.43  ? 62  ARG   D CD     1 
ATOM   10680 N  NE     . ARG   D 2  62  ? -24.483 -14.009  -38.725 1.00 63.01  ? 62  ARG   D NE     1 
ATOM   10681 C  CZ     . ARG   D 2  62  ? -23.285 -14.215  -38.206 1.00 64.55  ? 62  ARG   D CZ     1 
ATOM   10682 N  NH1    . ARG   D 2  62  ? -22.610 -13.236  -37.629 1.00 68.52  ? 62  ARG   D NH1    1 
ATOM   10683 N  NH2    . ARG   D 2  62  ? -22.756 -15.431  -38.258 1.00 65.47  ? 62  ARG   D NH2    1 
ATOM   10684 N  N      . ALA   D 2  63  ? -23.604 -8.760   -42.468 1.00 67.43  ? 63  ALA   D N      1 
ATOM   10685 C  CA     . ALA   D 2  63  ? -23.639 -7.308   -42.504 1.00 67.15  ? 63  ALA   D CA     1 
ATOM   10686 C  C      . ALA   D 2  63  ? -24.884 -6.808   -43.223 1.00 65.24  ? 63  ALA   D C      1 
ATOM   10687 O  O      . ALA   D 2  63  ? -25.419 -7.472   -44.110 1.00 71.66  ? 63  ALA   D O      1 
ATOM   10688 C  CB     . ALA   D 2  63  ? -22.378 -6.764   -43.177 1.00 62.96  ? 63  ALA   D CB     1 
ATOM   10689 N  N      . ILE   D 2  64  ? -25.346 -5.633   -42.819 1.00 59.84  ? 64  ILE   D N      1 
ATOM   10690 C  CA     . ILE   D 2  64  ? -26.482 -4.960   -43.432 1.00 63.72  ? 64  ILE   D CA     1 
ATOM   10691 C  C      . ILE   D 2  64  ? -26.009 -3.565   -43.797 1.00 72.36  ? 64  ILE   D C      1 
ATOM   10692 O  O      . ILE   D 2  64  ? -25.653 -2.780   -42.910 1.00 73.70  ? 64  ILE   D O      1 
ATOM   10693 C  CB     . ILE   D 2  64  ? -27.695 -4.867   -42.487 1.00 63.92  ? 64  ILE   D CB     1 
ATOM   10694 C  CG1    . ILE   D 2  64  ? -28.074 -6.237   -41.942 1.00 60.37  ? 64  ILE   D CG1    1 
ATOM   10695 C  CG2    . ILE   D 2  64  ? -28.877 -4.209   -43.184 1.00 64.45  ? 64  ILE   D CG2    1 
ATOM   10696 C  CD1    . ILE   D 2  64  ? -27.957 -7.315   -42.937 1.00 69.78  ? 64  ILE   D CD1    1 
ATOM   10697 N  N      . LEU   D 2  65  ? -26.008 -3.248   -45.086 1.00 76.30  ? 65  LEU   D N      1 
ATOM   10698 C  CA     . LEU   D 2  65  ? -25.615 -1.927   -45.557 1.00 68.25  ? 65  LEU   D CA     1 
ATOM   10699 C  C      . LEU   D 2  65  ? -26.877 -1.108   -45.778 1.00 66.63  ? 65  LEU   D C      1 
ATOM   10700 O  O      . LEU   D 2  65  ? -27.844 -1.618   -46.348 1.00 69.99  ? 65  LEU   D O      1 
ATOM   10701 C  CB     . LEU   D 2  65  ? -24.799 -2.052   -46.835 1.00 63.14  ? 65  LEU   D CB     1 
ATOM   10702 C  CG     . LEU   D 2  65  ? -23.522 -2.843   -46.566 1.00 68.44  ? 65  LEU   D CG     1 
ATOM   10703 C  CD1    . LEU   D 2  65  ? -23.686 -4.327   -46.883 1.00 66.42  ? 65  LEU   D CD1    1 
ATOM   10704 C  CD2    . LEU   D 2  65  ? -22.372 -2.271   -47.340 1.00 82.48  ? 65  LEU   D CD2    1 
ATOM   10705 N  N      . VAL   D 2  66  ? -26.882 0.140    -45.303 1.00 63.00  ? 66  VAL   D N      1 
ATOM   10706 C  CA     . VAL   D 2  66  ? -28.087 0.970    -45.279 1.00 70.33  ? 66  VAL   D CA     1 
ATOM   10707 C  C      . VAL   D 2  66  ? -27.718 2.422    -45.545 1.00 78.04  ? 66  VAL   D C      1 
ATOM   10708 O  O      . VAL   D 2  66  ? -26.670 2.898    -45.097 1.00 77.14  ? 66  VAL   D O      1 
ATOM   10709 C  CB     . VAL   D 2  66  ? -28.839 0.840    -43.933 1.00 68.24  ? 66  VAL   D CB     1 
ATOM   10710 C  CG1    . VAL   D 2  66  ? -29.997 1.838    -43.834 1.00 62.32  ? 66  VAL   D CG1    1 
ATOM   10711 C  CG2    . VAL   D 2  66  ? -29.347 -0.585   -43.756 1.00 67.43  ? 66  VAL   D CG2    1 
ATOM   10712 N  N      . ASP   D 2  67  ? -28.590 3.125    -46.268 1.00 82.16  ? 67  ASP   D N      1 
ATOM   10713 C  CA     . ASP   D 2  67  ? -28.455 4.561    -46.477 1.00 81.71  ? 67  ASP   D CA     1 
ATOM   10714 C  C      . ASP   D 2  67  ? -29.742 5.092    -47.085 1.00 84.43  ? 67  ASP   D C      1 
ATOM   10715 O  O      . ASP   D 2  67  ? -30.532 4.340    -47.657 1.00 86.80  ? 67  ASP   D O      1 
ATOM   10716 C  CB     . ASP   D 2  67  ? -27.253 4.891    -47.363 1.00 80.33  ? 67  ASP   D CB     1 
ATOM   10717 C  CG     . ASP   D 2  67  ? -26.790 6.309    -47.186 1.00 86.09  ? 67  ASP   D CG     1 
ATOM   10718 O  OD1    . ASP   D 2  67  ? -27.470 7.062    -46.455 1.00 85.88  ? 67  ASP   D OD1    1 
ATOM   10719 O  OD2    . ASP   D 2  67  ? -25.738 6.664    -47.751 1.00 89.24  ? 67  ASP   D OD2    1 
ATOM   10720 N  N      . LEU   D 2  68  ? -29.957 6.391    -46.936 1.00 85.22  ? 68  LEU   D N      1 
ATOM   10721 C  CA     . LEU   D 2  68  ? -31.112 7.030    -47.547 1.00 92.30  ? 68  LEU   D CA     1 
ATOM   10722 C  C      . LEU   D 2  68  ? -30.794 7.639    -48.916 1.00 99.00  ? 68  LEU   D C      1 
ATOM   10723 O  O      . LEU   D 2  68  ? -31.616 8.385    -49.460 1.00 98.36  ? 68  LEU   D O      1 
ATOM   10724 C  CB     . LEU   D 2  68  ? -31.668 8.092    -46.606 1.00 87.83  ? 68  LEU   D CB     1 
ATOM   10725 C  CG     . LEU   D 2  68  ? -32.495 7.497    -45.468 1.00 80.85  ? 68  LEU   D CG     1 
ATOM   10726 C  CD1    . LEU   D 2  68  ? -33.152 8.595    -44.636 1.00 82.95  ? 68  LEU   D CD1    1 
ATOM   10727 C  CD2    . LEU   D 2  68  ? -33.506 6.478    -45.967 1.00 81.27  ? 68  LEU   D CD2    1 
ATOM   10728 N  N      . GLU   D 2  69  ? -29.627 7.322    -49.482 1.00 99.79  ? 69  GLU   D N      1 
ATOM   10729 C  CA     . GLU   D 2  69  ? -29.130 7.869    -50.737 1.00 101.19 ? 69  GLU   D CA     1 
ATOM   10730 C  C      . GLU   D 2  69  ? -28.225 6.876    -51.450 1.00 100.29 ? 69  GLU   D C      1 
ATOM   10731 O  O      . GLU   D 2  69  ? -27.114 6.606    -50.986 1.00 95.26  ? 69  GLU   D O      1 
ATOM   10732 C  CB     . GLU   D 2  69  ? -28.365 9.162    -50.492 1.00 105.18 ? 69  GLU   D CB     1 
ATOM   10733 C  CG     . GLU   D 2  69  ? -27.857 9.792    -51.764 1.00 118.69 ? 69  GLU   D CG     1 
ATOM   10734 C  CD     . GLU   D 2  69  ? -27.713 11.292   -51.651 1.00 125.53 ? 69  GLU   D CD     1 
ATOM   10735 O  OE1    . GLU   D 2  69  ? -28.060 11.850   -50.582 1.00 121.00 ? 69  GLU   D OE1    1 
ATOM   10736 O  OE2    . GLU   D 2  69  ? -27.270 11.913   -52.642 1.00 135.15 ? 69  GLU   D OE2    1 
ATOM   10737 N  N      . PRO   D 2  70  ? -28.634 6.365    -52.614 1.00 108.37 ? 70  PRO   D N      1 
ATOM   10738 C  CA     . PRO   D 2  70  ? -27.883 5.268    -53.250 1.00 111.28 ? 70  PRO   D CA     1 
ATOM   10739 C  C      . PRO   D 2  70  ? -26.444 5.604    -53.530 1.00 111.85 ? 70  PRO   D C      1 
ATOM   10740 O  O      . PRO   D 2  70  ? -25.705 4.718    -53.979 1.00 110.08 ? 70  PRO   D O      1 
ATOM   10741 C  CB     . PRO   D 2  70  ? -28.643 5.021    -54.560 1.00 111.36 ? 70  PRO   D CB     1 
ATOM   10742 C  CG     . PRO   D 2  70  ? -29.953 5.745    -54.394 1.00 120.11 ? 70  PRO   D CG     1 
ATOM   10743 C  CD     . PRO   D 2  70  ? -29.668 6.911    -53.502 1.00 111.89 ? 70  PRO   D CD     1 
ATOM   10744 N  N      . GLY   D 2  71  ? -26.029 6.847    -53.305 1.00 109.13 ? 71  GLY   D N      1 
ATOM   10745 C  CA     . GLY   D 2  71  ? -24.650 7.232    -53.510 1.00 110.75 ? 71  GLY   D CA     1 
ATOM   10746 C  C      . GLY   D 2  71  ? -23.690 6.363    -52.727 1.00 111.73 ? 71  GLY   D C      1 
ATOM   10747 O  O      . GLY   D 2  71  ? -22.897 5.614    -53.304 1.00 110.02 ? 71  GLY   D O      1 
ATOM   10748 N  N      . THR   D 2  72  ? -23.767 6.446    -51.397 1.00 121.39 ? 72  THR   D N      1 
ATOM   10749 C  CA     . THR   D 2  72  ? -22.850 5.683    -50.558 1.00 118.64 ? 72  THR   D CA     1 
ATOM   10750 C  C      . THR   D 2  72  ? -22.916 4.192    -50.880 1.00 115.48 ? 72  THR   D C      1 
ATOM   10751 O  O      . THR   D 2  72  ? -21.882 3.513    -50.910 1.00 115.04 ? 72  THR   D O      1 
ATOM   10752 C  CB     . THR   D 2  72  ? -23.149 5.939    -49.074 1.00 109.89 ? 72  THR   D CB     1 
ATOM   10753 O  OG1    . THR   D 2  72  ? -24.518 5.623    -48.783 1.00 111.19 ? 72  THR   D OG1    1 
ATOM   10754 C  CG2    . THR   D 2  72  ? -22.895 7.406    -48.721 1.00 110.81 ? 72  THR   D CG2    1 
ATOM   10755 N  N      . MET   D 2  73  ? -24.116 3.663    -51.147 1.00 115.58 ? 73  MET   D N      1 
ATOM   10756 C  CA     . MET   D 2  73  ? -24.232 2.225    -51.377 1.00 118.72 ? 73  MET   D CA     1 
ATOM   10757 C  C      . MET   D 2  73  ? -23.363 1.796    -52.556 1.00 118.84 ? 73  MET   D C      1 
ATOM   10758 O  O      . MET   D 2  73  ? -22.681 0.765    -52.495 1.00 114.11 ? 73  MET   D O      1 
ATOM   10759 C  CB     . MET   D 2  73  ? -25.708 1.835    -51.589 1.00 126.00 ? 73  MET   D CB     1 
ATOM   10760 C  CG     . MET   D 2  73  ? -25.979 0.441    -52.219 1.00 120.66 ? 73  MET   D CG     1 
ATOM   10761 S  SD     . MET   D 2  73  ? -26.064 0.333    -54.029 1.00 141.34 ? 73  MET   D SD     1 
ATOM   10762 C  CE     . MET   D 2  73  ? -25.520 -1.351   -54.350 1.00 108.11 ? 73  MET   D CE     1 
ATOM   10763 N  N      . ASP   D 2  74  ? -23.335 2.602    -53.621 1.00 123.21 ? 74  ASP   D N      1 
ATOM   10764 C  CA     . ASP   D 2  74  ? -22.575 2.243    -54.815 1.00 120.55 ? 74  ASP   D CA     1 
ATOM   10765 C  C      . ASP   D 2  74  ? -21.087 2.145    -54.509 1.00 116.54 ? 74  ASP   D C      1 
ATOM   10766 O  O      . ASP   D 2  74  ? -20.455 1.107    -54.741 1.00 107.51 ? 74  ASP   D O      1 
ATOM   10767 C  CB     . ASP   D 2  74  ? -22.836 3.273    -55.908 1.00 119.12 ? 74  ASP   D CB     1 
ATOM   10768 C  CG     . ASP   D 2  74  ? -24.093 2.983    -56.672 1.00 122.38 ? 74  ASP   D CG     1 
ATOM   10769 O  OD1    . ASP   D 2  74  ? -24.021 2.222    -57.658 1.00 125.50 ? 74  ASP   D OD1    1 
ATOM   10770 O  OD2    . ASP   D 2  74  ? -25.159 3.485    -56.256 1.00 121.83 ? 74  ASP   D OD2    1 
ATOM   10771 N  N      . SER   D 2  75  ? -20.512 3.229    -53.977 1.00 116.97 ? 75  SER   D N      1 
ATOM   10772 C  CA     . SER   D 2  75  ? -19.095 3.247    -53.629 1.00 114.18 ? 75  SER   D CA     1 
ATOM   10773 C  C      . SER   D 2  75  ? -18.693 2.035    -52.803 1.00 111.47 ? 75  SER   D C      1 
ATOM   10774 O  O      . SER   D 2  75  ? -17.517 1.659    -52.776 1.00 110.44 ? 75  SER   D O      1 
ATOM   10775 C  CB     . SER   D 2  75  ? -18.775 4.526    -52.859 1.00 117.17 ? 75  SER   D CB     1 
ATOM   10776 O  OG     . SER   D 2  75  ? -19.712 4.712    -51.808 1.00 120.49 ? 75  SER   D OG     1 
ATOM   10777 N  N      . VAL   D 2  76  ? -19.647 1.415    -52.114 1.00 114.27 ? 76  VAL   D N      1 
ATOM   10778 C  CA     . VAL   D 2  76  ? -19.322 0.288    -51.246 1.00 111.92 ? 76  VAL   D CA     1 
ATOM   10779 C  C      . VAL   D 2  76  ? -18.988 -0.942   -52.073 1.00 110.73 ? 76  VAL   D C      1 
ATOM   10780 O  O      . VAL   D 2  76  ? -17.876 -1.477   -52.005 1.00 108.20 ? 76  VAL   D O      1 
ATOM   10781 C  CB     . VAL   D 2  76  ? -20.479 -0.002   -50.281 1.00 106.79 ? 76  VAL   D CB     1 
ATOM   10782 C  CG1    . VAL   D 2  76  ? -20.194 -1.277   -49.505 1.00 101.66 ? 76  VAL   D CG1    1 
ATOM   10783 C  CG2    . VAL   D 2  76  ? -20.681 1.168    -49.353 1.00 105.27 ? 76  VAL   D CG2    1 
ATOM   10784 N  N      . ARG   D 2  77  ? -19.967 -1.432   -52.837 1.00 113.21 ? 77  ARG   D N      1 
ATOM   10785 C  CA     . ARG   D 2  77  ? -19.730 -2.588   -53.691 1.00 110.66 ? 77  ARG   D CA     1 
ATOM   10786 C  C      . ARG   D 2  77  ? -18.526 -2.348   -54.584 1.00 112.01 ? 77  ARG   D C      1 
ATOM   10787 O  O      . ARG   D 2  77  ? -17.646 -3.206   -54.713 1.00 106.97 ? 77  ARG   D O      1 
ATOM   10788 C  CB     . ARG   D 2  77  ? -20.972 -2.884   -54.526 1.00 108.80 ? 77  ARG   D CB     1 
ATOM   10789 C  CG     . ARG   D 2  77  ? -21.004 -4.295   -55.025 1.00 112.49 ? 77  ARG   D CG     1 
ATOM   10790 C  CD     . ARG   D 2  77  ? -22.308 -4.631   -55.728 1.00 124.62 ? 77  ARG   D CD     1 
ATOM   10791 N  NE     . ARG   D 2  77  ? -22.585 -3.732   -56.844 1.00 139.64 ? 77  ARG   D NE     1 
ATOM   10792 C  CZ     . ARG   D 2  77  ? -23.642 -3.822   -57.643 1.00 144.04 ? 77  ARG   D CZ     1 
ATOM   10793 N  NH1    . ARG   D 2  77  ? -24.505 -4.821   -57.542 1.00 136.01 ? 77  ARG   D NH1    1 
ATOM   10794 N  NH2    . ARG   D 2  77  ? -23.817 -2.907   -58.595 1.00 148.43 ? 77  ARG   D NH2    1 
ATOM   10795 N  N      . SER   D 2  78  ? -18.471 -1.164   -55.198 1.00 116.29 ? 78  SER   D N      1 
ATOM   10796 C  CA     . SER   D 2  78  ? -17.290 -0.767   -55.953 1.00 114.17 ? 78  SER   D CA     1 
ATOM   10797 C  C      . SER   D 2  78  ? -16.041 -0.840   -55.090 1.00 110.64 ? 78  SER   D C      1 
ATOM   10798 O  O      . SER   D 2  78  ? -15.008 -1.365   -55.522 1.00 104.10 ? 78  SER   D O      1 
ATOM   10799 C  CB     . SER   D 2  78  ? -17.480 0.647    -56.504 1.00 116.96 ? 78  SER   D CB     1 
ATOM   10800 O  OG     . SER   D 2  78  ? -17.672 1.583    -55.455 1.00 122.91 ? 78  SER   D OG     1 
ATOM   10801 N  N      . GLY   D 2  79  ? -16.125 -0.333   -53.862 1.00 115.37 ? 79  GLY   D N      1 
ATOM   10802 C  CA     . GLY   D 2  79  ? -15.000 -0.285   -52.963 1.00 117.97 ? 79  GLY   D CA     1 
ATOM   10803 C  C      . GLY   D 2  79  ? -14.224 -1.586   -52.872 1.00 117.02 ? 79  GLY   D C      1 
ATOM   10804 O  O      . GLY   D 2  79  ? -14.581 -2.614   -53.465 1.00 112.32 ? 79  GLY   D O      1 
ATOM   10805 N  N      . PRO   D 2  80  ? -13.123 -1.550   -52.126 1.00 115.57 ? 80  PRO   D N      1 
ATOM   10806 C  CA     . PRO   D 2  80  ? -12.338 -2.775   -51.901 1.00 111.00 ? 80  PRO   D CA     1 
ATOM   10807 C  C      . PRO   D 2  80  ? -13.161 -3.796   -51.125 1.00 111.25 ? 80  PRO   D C      1 
ATOM   10808 O  O      . PRO   D 2  80  ? -13.811 -3.458   -50.134 1.00 117.10 ? 80  PRO   D O      1 
ATOM   10809 C  CB     . PRO   D 2  80  ? -11.134 -2.277   -51.087 1.00 109.02 ? 80  PRO   D CB     1 
ATOM   10810 C  CG     . PRO   D 2  80  ? -11.094 -0.753   -51.322 1.00 111.14 ? 80  PRO   D CG     1 
ATOM   10811 C  CD     . PRO   D 2  80  ? -12.526 -0.355   -51.496 1.00 110.42 ? 80  PRO   D CD     1 
ATOM   10812 N  N      . PHE   D 2  81  ? -13.143 -5.052   -51.577 1.00 105.00 ? 81  PHE   D N      1 
ATOM   10813 C  CA     . PHE   D 2  81  ? -13.915 -6.147   -50.971 1.00 100.78 ? 81  PHE   D CA     1 
ATOM   10814 C  C      . PHE   D 2  81  ? -15.407 -6.104   -51.275 1.00 100.89 ? 81  PHE   D C      1 
ATOM   10815 O  O      . PHE   D 2  81  ? -16.120 -6.994   -50.806 1.00 97.63  ? 81  PHE   D O      1 
ATOM   10816 C  CB     . PHE   D 2  81  ? -13.840 -6.189   -49.438 1.00 96.65  ? 81  PHE   D CB     1 
ATOM   10817 C  CG     . PHE   D 2  81  ? -12.687 -6.953   -48.886 1.00 93.53  ? 81  PHE   D CG     1 
ATOM   10818 C  CD1    . PHE   D 2  81  ? -11.445 -6.363   -48.745 1.00 98.28  ? 81  PHE   D CD1    1 
ATOM   10819 C  CD2    . PHE   D 2  81  ? -12.852 -8.267   -48.481 1.00 93.96  ? 81  PHE   D CD2    1 
ATOM   10820 C  CE1    . PHE   D 2  81  ? -10.380 -7.073   -48.208 1.00 94.43  ? 81  PHE   D CE1    1 
ATOM   10821 C  CE2    . PHE   D 2  81  ? -11.792 -8.990   -47.950 1.00 93.35  ? 81  PHE   D CE2    1 
ATOM   10822 C  CZ     . PHE   D 2  81  ? -10.553 -8.391   -47.815 1.00 92.79  ? 81  PHE   D CZ     1 
ATOM   10823 N  N      . GLY   D 2  82  ? -15.917 -5.091   -51.970 1.00 103.79 ? 82  GLY   D N      1 
ATOM   10824 C  CA     . GLY   D 2  82  ? -17.351 -4.945   -52.146 1.00 102.21 ? 82  GLY   D CA     1 
ATOM   10825 C  C      . GLY   D 2  82  ? -18.085 -6.207   -52.565 1.00 105.75 ? 82  GLY   D C      1 
ATOM   10826 O  O      . GLY   D 2  82  ? -19.299 -6.312   -52.372 1.00 102.23 ? 82  GLY   D O      1 
ATOM   10827 N  N      . GLN   D 2  83  ? -17.362 -7.177   -53.132 1.00 109.40 ? 83  GLN   D N      1 
ATOM   10828 C  CA     . GLN   D 2  83  ? -17.944 -8.398   -53.683 1.00 106.07 ? 83  GLN   D CA     1 
ATOM   10829 C  C      . GLN   D 2  83  ? -17.952 -9.563   -52.696 1.00 101.46 ? 83  GLN   D C      1 
ATOM   10830 O  O      . GLN   D 2  83  ? -18.177 -10.709  -53.107 1.00 99.59  ? 83  GLN   D O      1 
ATOM   10831 C  CB     . GLN   D 2  83  ? -17.195 -8.810   -54.959 1.00 110.85 ? 83  GLN   D CB     1 
ATOM   10832 C  CG     . GLN   D 2  83  ? -17.105 -7.735   -56.060 1.00 115.40 ? 83  GLN   D CG     1 
ATOM   10833 C  CD     . GLN   D 2  83  ? -18.466 -7.256   -56.578 1.00 118.92 ? 83  GLN   D CD     1 
ATOM   10834 O  OE1    . GLN   D 2  83  ? -18.784 -6.061   -56.535 1.00 115.53 ? 83  GLN   D OE1    1 
ATOM   10835 N  NE2    . GLN   D 2  83  ? -19.260 -8.191   -57.095 1.00 119.42 ? 83  GLN   D NE2    1 
ATOM   10836 N  N      . ILE   D 2  84  ? -17.693 -9.305   -51.415 1.00 102.25 ? 84  ILE   D N      1 
ATOM   10837 C  CA     . ILE   D 2  84  ? -17.855 -10.327  -50.384 1.00 100.42 ? 84  ILE   D CA     1 
ATOM   10838 C  C      . ILE   D 2  84  ? -19.171 -10.174  -49.632 1.00 87.89  ? 84  ILE   D C      1 
ATOM   10839 O  O      . ILE   D 2  84  ? -19.648 -11.150  -49.033 1.00 83.46  ? 84  ILE   D O      1 
ATOM   10840 C  CB     . ILE   D 2  84  ? -16.680 -10.315  -49.382 1.00 95.64  ? 84  ILE   D CB     1 
ATOM   10841 C  CG1    . ILE   D 2  84  ? -16.678 -11.600  -48.550 1.00 84.89  ? 84  ILE   D CG1    1 
ATOM   10842 C  CG2    . ILE   D 2  84  ? -16.752 -9.073   -48.495 1.00 94.19  ? 84  ILE   D CG2    1 
ATOM   10843 C  CD1    . ILE   D 2  84  ? -15.390 -11.834  -47.818 1.00 85.36  ? 84  ILE   D CD1    1 
ATOM   10844 N  N      . PHE   D 2  85  ? -19.762 -8.991   -49.637 1.00 80.54  ? 85  PHE   D N      1 
ATOM   10845 C  CA     . PHE   D 2  85  ? -21.023 -8.800   -48.955 1.00 87.10  ? 85  PHE   D CA     1 
ATOM   10846 C  C      . PHE   D 2  85  ? -22.124 -9.599   -49.646 1.00 88.08  ? 85  PHE   D C      1 
ATOM   10847 O  O      . PHE   D 2  85  ? -21.975 -10.071  -50.776 1.00 92.32  ? 85  PHE   D O      1 
ATOM   10848 C  CB     . PHE   D 2  85  ? -21.341 -7.306   -48.881 1.00 90.96  ? 85  PHE   D CB     1 
ATOM   10849 C  CG     . PHE   D 2  85  ? -20.301 -6.518   -48.127 1.00 93.39  ? 85  PHE   D CG     1 
ATOM   10850 C  CD1    . PHE   D 2  85  ? -20.317 -6.468   -46.740 1.00 90.78  ? 85  PHE   D CD1    1 
ATOM   10851 C  CD2    . PHE   D 2  85  ? -19.251 -5.923   -48.794 1.00 100.00 ? 85  PHE   D CD2    1 
ATOM   10852 C  CE1    . PHE   D 2  85  ? -19.348 -5.774   -46.042 1.00 80.95  ? 85  PHE   D CE1    1 
ATOM   10853 C  CE2    . PHE   D 2  85  ? -18.274 -5.232   -48.098 1.00 98.64  ? 85  PHE   D CE2    1 
ATOM   10854 C  CZ     . PHE   D 2  85  ? -18.324 -5.159   -46.722 1.00 87.11  ? 85  PHE   D CZ     1 
ATOM   10855 N  N      . ARG   D 2  86  ? -23.228 -9.794   -48.924 1.00 88.42  ? 86  ARG   D N      1 
ATOM   10856 C  CA     . ARG   D 2  86  ? -24.386 -10.422  -49.542 1.00 80.92  ? 86  ARG   D CA     1 
ATOM   10857 C  C      . ARG   D 2  86  ? -25.184 -9.359   -50.290 1.00 81.28  ? 86  ARG   D C      1 
ATOM   10858 O  O      . ARG   D 2  86  ? -25.513 -8.313   -49.709 1.00 75.35  ? 86  ARG   D O      1 
ATOM   10859 C  CB     . ARG   D 2  86  ? -25.253 -11.126  -48.498 1.00 82.04  ? 86  ARG   D CB     1 
ATOM   10860 C  CG     . ARG   D 2  86  ? -26.683 -11.395  -48.936 1.00 92.24  ? 86  ARG   D CG     1 
ATOM   10861 C  CD     . ARG   D 2  86  ? -27.454 -12.286  -47.948 1.00 93.60  ? 86  ARG   D CD     1 
ATOM   10862 N  NE     . ARG   D 2  86  ? -28.850 -12.446  -48.363 1.00 102.83 ? 86  ARG   D NE     1 
ATOM   10863 C  CZ     . ARG   D 2  86  ? -29.349 -13.511  -48.984 1.00 102.76 ? 86  ARG   D CZ     1 
ATOM   10864 N  NH1    . ARG   D 2  86  ? -28.616 -14.589  -49.212 1.00 105.91 ? 86  ARG   D NH1    1 
ATOM   10865 N  NH2    . ARG   D 2  86  ? -30.620 -13.496  -49.384 1.00 90.38  ? 86  ARG   D NH2    1 
ATOM   10866 N  N      . PRO   D 2  87  ? -25.472 -9.571   -51.579 1.00 87.45  ? 87  PRO   D N      1 
ATOM   10867 C  CA     . PRO   D 2  87  ? -26.095 -8.496   -52.365 1.00 80.60  ? 87  PRO   D CA     1 
ATOM   10868 C  C      . PRO   D 2  87  ? -27.479 -8.137   -51.879 1.00 78.52  ? 87  PRO   D C      1 
ATOM   10869 O  O      . PRO   D 2  87  ? -27.870 -6.969   -51.973 1.00 78.01  ? 87  PRO   D O      1 
ATOM   10870 C  CB     . PRO   D 2  87  ? -26.112 -9.066   -53.789 1.00 73.01  ? 87  PRO   D CB     1 
ATOM   10871 C  CG     . PRO   D 2  87  ? -25.047 -10.126  -53.794 1.00 72.61  ? 87  PRO   D CG     1 
ATOM   10872 C  CD     . PRO   D 2  87  ? -25.113 -10.727  -52.419 1.00 83.41  ? 87  PRO   D CD     1 
ATOM   10873 N  N      . ASP   D 2  88  ? -28.228 -9.099   -51.348 1.00 78.34  ? 88  ASP   D N      1 
ATOM   10874 C  CA     . ASP   D 2  88  ? -29.525 -8.777   -50.775 1.00 83.00  ? 88  ASP   D CA     1 
ATOM   10875 C  C      . ASP   D 2  88  ? -29.430 -7.805   -49.607 1.00 85.40  ? 88  ASP   D C      1 
ATOM   10876 O  O      . ASP   D 2  88  ? -30.426 -7.144   -49.289 1.00 84.69  ? 88  ASP   D O      1 
ATOM   10877 C  CB     . ASP   D 2  88  ? -30.206 -10.054  -50.324 1.00 89.96  ? 88  ASP   D CB     1 
ATOM   10878 C  CG     . ASP   D 2  88  ? -30.625 -10.910  -51.485 1.00 102.42 ? 88  ASP   D CG     1 
ATOM   10879 O  OD1    . ASP   D 2  88  ? -31.491 -10.462  -52.272 1.00 105.67 ? 88  ASP   D OD1    1 
ATOM   10880 O  OD2    . ASP   D 2  88  ? -30.064 -12.016  -51.625 1.00 106.33 ? 88  ASP   D OD2    1 
ATOM   10881 N  N      . ASN   D 2  89  ? -28.264 -7.695   -48.969 1.00 83.82  ? 89  ASN   D N      1 
ATOM   10882 C  CA     . ASN   D 2  89  ? -28.129 -6.948   -47.726 1.00 77.86  ? 89  ASN   D CA     1 
ATOM   10883 C  C      . ASN   D 2  89  ? -27.832 -5.477   -47.933 1.00 79.12  ? 89  ASN   D C      1 
ATOM   10884 O  O      . ASN   D 2  89  ? -27.416 -4.805   -46.984 1.00 80.11  ? 89  ASN   D O      1 
ATOM   10885 C  CB     . ASN   D 2  89  ? -27.048 -7.572   -46.849 1.00 76.48  ? 89  ASN   D CB     1 
ATOM   10886 C  CG     . ASN   D 2  89  ? -27.406 -8.975   -46.420 1.00 83.63  ? 89  ASN   D CG     1 
ATOM   10887 O  OD1    . ASN   D 2  89  ? -28.330 -9.572   -46.972 1.00 89.37  ? 89  ASN   D OD1    1 
ATOM   10888 N  ND2    . ASN   D 2  89  ? -26.685 -9.512   -45.431 1.00 75.91  ? 89  ASN   D ND2    1 
ATOM   10889 N  N      . PHE   D 2  90  ? -28.039 -4.955   -49.132 1.00 82.46  ? 90  PHE   D N      1 
ATOM   10890 C  CA     . PHE   D 2  90  ? -27.963 -3.523   -49.371 1.00 78.94  ? 90  PHE   D CA     1 
ATOM   10891 C  C      . PHE   D 2  90  ? -29.386 -2.982   -49.387 1.00 78.52  ? 90  PHE   D C      1 
ATOM   10892 O  O      . PHE   D 2  90  ? -30.211 -3.428   -50.192 1.00 84.00  ? 90  PHE   D O      1 
ATOM   10893 C  CB     . PHE   D 2  90  ? -27.266 -3.215   -50.693 1.00 76.16  ? 90  PHE   D CB     1 
ATOM   10894 C  CG     . PHE   D 2  90  ? -25.807 -3.551   -50.712 1.00 70.72  ? 90  PHE   D CG     1 
ATOM   10895 C  CD1    . PHE   D 2  90  ? -25.392 -4.868   -50.802 1.00 70.53  ? 90  PHE   D CD1    1 
ATOM   10896 C  CD2    . PHE   D 2  90  ? -24.848 -2.556   -50.674 1.00 78.05  ? 90  PHE   D CD2    1 
ATOM   10897 C  CE1    . PHE   D 2  90  ? -24.039 -5.191   -50.850 1.00 75.77  ? 90  PHE   D CE1    1 
ATOM   10898 C  CE2    . PHE   D 2  90  ? -23.495 -2.874   -50.719 1.00 78.59  ? 90  PHE   D CE2    1 
ATOM   10899 C  CZ     . PHE   D 2  90  ? -23.091 -4.191   -50.805 1.00 75.36  ? 90  PHE   D CZ     1 
ATOM   10900 N  N      . VAL   D 2  91  ? -29.678 -2.047   -48.490 1.00 77.08  ? 91  VAL   D N      1 
ATOM   10901 C  CA     . VAL   D 2  91  ? -30.955 -1.341   -48.462 1.00 80.54  ? 91  VAL   D CA     1 
ATOM   10902 C  C      . VAL   D 2  91  ? -30.671 0.143    -48.587 1.00 85.24  ? 91  VAL   D C      1 
ATOM   10903 O  O      . VAL   D 2  91  ? -30.017 0.739    -47.722 1.00 81.96  ? 91  VAL   D O      1 
ATOM   10904 C  CB     . VAL   D 2  91  ? -31.763 -1.635   -47.191 1.00 75.03  ? 91  VAL   D CB     1 
ATOM   10905 C  CG1    . VAL   D 2  91  ? -33.111 -0.908   -47.249 1.00 71.96  ? 91  VAL   D CG1    1 
ATOM   10906 C  CG2    . VAL   D 2  91  ? -31.944 -3.137   -47.028 1.00 69.83  ? 91  VAL   D CG2    1 
ATOM   10907 N  N      . PHE   D 2  92  ? -31.195 0.738    -49.638 1.00 90.75  ? 92  PHE   D N      1 
ATOM   10908 C  CA     . PHE   D 2  92  ? -30.855 2.079    -50.064 1.00 92.10  ? 92  PHE   D CA     1 
ATOM   10909 C  C      . PHE   D 2  92  ? -32.147 2.833    -50.317 1.00 95.47  ? 92  PHE   D C      1 
ATOM   10910 O  O      . PHE   D 2  92  ? -33.082 2.293    -50.915 1.00 95.17  ? 92  PHE   D O      1 
ATOM   10911 C  CB     . PHE   D 2  92  ? -30.035 1.991    -51.325 1.00 99.08  ? 92  PHE   D CB     1 
ATOM   10912 C  CG     . PHE   D 2  92  ? -30.713 1.167    -52.355 1.00 107.16 ? 92  PHE   D CG     1 
ATOM   10913 C  CD1    . PHE   D 2  92  ? -30.550 -0.208   -52.358 1.00 107.95 ? 92  PHE   D CD1    1 
ATOM   10914 C  CD2    . PHE   D 2  92  ? -31.592 1.738    -53.259 1.00 112.18 ? 92  PHE   D CD2    1 
ATOM   10915 C  CE1    . PHE   D 2  92  ? -31.218 -0.998   -53.272 1.00 110.73 ? 92  PHE   D CE1    1 
ATOM   10916 C  CE2    . PHE   D 2  92  ? -32.262 0.955    -54.181 1.00 114.33 ? 92  PHE   D CE2    1 
ATOM   10917 C  CZ     . PHE   D 2  92  ? -32.073 -0.416   -54.188 1.00 115.97 ? 92  PHE   D CZ     1 
ATOM   10918 N  N      . GLY   D 2  93  ? -32.214 4.056    -49.833 1.00 101.46 ? 93  GLY   D N      1 
ATOM   10919 C  CA     . GLY   D 2  93  ? -33.273 4.969    -50.199 1.00 104.60 ? 93  GLY   D CA     1 
ATOM   10920 C  C      . GLY   D 2  93  ? -32.943 5.688    -51.486 1.00 111.55 ? 93  GLY   D C      1 
ATOM   10921 O  O      . GLY   D 2  93  ? -32.224 5.178    -52.352 1.00 106.93 ? 93  GLY   D O      1 
ATOM   10922 N  N      . GLN   D 2  94  ? -33.467 6.899    -51.612 1.00 113.93 ? 94  GLN   D N      1 
ATOM   10923 C  CA     . GLN   D 2  94  ? -33.147 7.731    -52.759 1.00 109.36 ? 94  GLN   D CA     1 
ATOM   10924 C  C      . GLN   D 2  94  ? -33.180 9.173    -52.308 1.00 107.09 ? 94  GLN   D C      1 
ATOM   10925 O  O      . GLN   D 2  94  ? -32.190 9.897    -52.439 1.00 103.60 ? 94  GLN   D O      1 
ATOM   10926 C  CB     . GLN   D 2  94  ? -34.139 7.505    -53.898 1.00 109.00 ? 94  GLN   D CB     1 
ATOM   10927 C  CG     . GLN   D 2  94  ? -34.137 6.102    -54.448 1.00 110.39 ? 94  GLN   D CG     1 
ATOM   10928 C  CD     . GLN   D 2  94  ? -32.937 5.836    -55.324 1.00 112.09 ? 94  GLN   D CD     1 
ATOM   10929 O  OE1    . GLN   D 2  94  ? -32.396 6.747    -55.949 1.00 108.88 ? 94  GLN   D OE1    1 
ATOM   10930 N  NE2    . GLN   D 2  94  ? -32.514 4.580    -55.380 1.00 112.24 ? 94  GLN   D NE2    1 
ATOM   10931 N  N      . SER   D 2  95  ? -34.323 9.571    -51.740 1.00 108.74 ? 95  SER   D N      1 
ATOM   10932 C  CA     . SER   D 2  95  ? -34.549 10.959   -51.356 1.00 113.98 ? 95  SER   D CA     1 
ATOM   10933 C  C      . SER   D 2  95  ? -33.344 11.562   -50.637 1.00 115.94 ? 95  SER   D C      1 
ATOM   10934 O  O      . SER   D 2  95  ? -33.123 12.780   -50.708 1.00 110.93 ? 95  SER   D O      1 
ATOM   10935 C  CB     . SER   D 2  95  ? -35.801 11.047   -50.475 1.00 111.71 ? 95  SER   D CB     1 
ATOM   10936 O  OG     . SER   D 2  95  ? -36.978 10.768   -51.215 1.00 105.61 ? 95  SER   D OG     1 
ATOM   10937 N  N      . GLY   D 2  96  ? -32.549 10.736   -49.964 1.00 114.65 ? 96  GLY   D N      1 
ATOM   10938 C  CA     . GLY   D 2  96  ? -31.479 11.224   -49.122 1.00 105.66 ? 96  GLY   D CA     1 
ATOM   10939 C  C      . GLY   D 2  96  ? -32.013 11.865   -47.852 1.00 107.00 ? 96  GLY   D C      1 
ATOM   10940 O  O      . GLY   D 2  96  ? -33.200 12.163   -47.715 1.00 104.40 ? 96  GLY   D O      1 
ATOM   10941 N  N      . ALA   D 2  97  ? -31.101 12.081   -46.903 1.00 106.33 ? 97  ALA   D N      1 
ATOM   10942 C  CA     . ALA   D 2  97  ? -31.457 12.616   -45.592 1.00 97.01  ? 97  ALA   D CA     1 
ATOM   10943 C  C      . ALA   D 2  97  ? -31.169 14.098   -45.443 1.00 94.15  ? 97  ALA   D C      1 
ATOM   10944 O  O      . ALA   D 2  97  ? -31.839 14.769   -44.648 1.00 94.01  ? 97  ALA   D O      1 
ATOM   10945 C  CB     . ALA   D 2  97  ? -30.715 11.860   -44.486 1.00 92.31  ? 97  ALA   D CB     1 
ATOM   10946 N  N      . GLY   D 2  98  ? -30.187 14.616   -46.174 1.00 95.19  ? 98  GLY   D N      1 
ATOM   10947 C  CA     . GLY   D 2  98  ? -29.873 16.033   -46.111 1.00 91.14  ? 98  GLY   D CA     1 
ATOM   10948 C  C      . GLY   D 2  98  ? -29.581 16.525   -44.712 1.00 89.27  ? 98  GLY   D C      1 
ATOM   10949 O  O      . GLY   D 2  98  ? -30.084 17.582   -44.313 1.00 90.19  ? 98  GLY   D O      1 
ATOM   10950 N  N      . ASN   D 2  99  ? -28.782 15.774   -43.950 1.00 90.53  ? 99  ASN   D N      1 
ATOM   10951 C  CA     . ASN   D 2  99  ? -28.333 16.161   -42.608 1.00 82.46  ? 99  ASN   D CA     1 
ATOM   10952 C  C      . ASN   D 2  99  ? -29.480 16.541   -41.678 1.00 82.41  ? 99  ASN   D C      1 
ATOM   10953 O  O      . ASN   D 2  99  ? -29.268 17.265   -40.707 1.00 78.74  ? 99  ASN   D O      1 
ATOM   10954 C  CB     . ASN   D 2  99  ? -27.328 17.316   -42.654 1.00 70.65  ? 99  ASN   D CB     1 
ATOM   10955 C  CG     . ASN   D 2  99  ? -25.968 16.893   -43.158 1.00 78.50  ? 99  ASN   D CG     1 
ATOM   10956 O  OD1    . ASN   D 2  99  ? -25.832 15.925   -43.910 1.00 75.32  ? 99  ASN   D OD1    1 
ATOM   10957 N  ND2    . ASN   D 2  99  ? -24.941 17.618   -42.732 1.00 86.81  ? 99  ASN   D ND2    1 
ATOM   10958 N  N      . ASN   D 2  100 ? -30.704 16.094   -41.931 1.00 85.47  ? 100 ASN   D N      1 
ATOM   10959 C  CA     . ASN   D 2  100 ? -31.803 16.364   -41.016 1.00 87.63  ? 100 ASN   D CA     1 
ATOM   10960 C  C      . ASN   D 2  100 ? -32.137 15.082   -40.270 1.00 91.50  ? 100 ASN   D C      1 
ATOM   10961 O  O      . ASN   D 2  100 ? -32.321 14.025   -40.886 1.00 88.49  ? 100 ASN   D O      1 
ATOM   10962 C  CB     . ASN   D 2  100 ? -33.037 16.908   -41.743 1.00 87.75  ? 100 ASN   D CB     1 
ATOM   10963 C  CG     . ASN   D 2  100 ? -34.078 17.485   -40.784 1.00 88.56  ? 100 ASN   D CG     1 
ATOM   10964 O  OD1    . ASN   D 2  100 ? -34.339 16.932   -39.716 1.00 87.81  ? 100 ASN   D OD1    1 
ATOM   10965 N  ND2    . ASN   D 2  100 ? -34.659 18.614   -41.160 1.00 94.66  ? 100 ASN   D ND2    1 
ATOM   10966 N  N      . TRP   D 2  101 ? -32.192 15.179   -38.941 1.00 92.34  ? 101 TRP   D N      1 
ATOM   10967 C  CA     . TRP   D 2  101 ? -32.492 14.015   -38.111 1.00 90.20  ? 101 TRP   D CA     1 
ATOM   10968 C  C      . TRP   D 2  101 ? -33.961 13.616   -38.223 1.00 89.88  ? 101 TRP   D C      1 
ATOM   10969 O  O      . TRP   D 2  101 ? -34.274 12.444   -38.480 1.00 90.68  ? 101 TRP   D O      1 
ATOM   10970 C  CB     . TRP   D 2  101 ? -32.086 14.302   -36.656 1.00 90.41  ? 101 TRP   D CB     1 
ATOM   10971 C  CG     . TRP   D 2  101 ? -32.124 13.107   -35.716 1.00 88.52  ? 101 TRP   D CG     1 
ATOM   10972 C  CD1    . TRP   D 2  101 ? -31.162 12.143   -35.543 1.00 80.80  ? 101 TRP   D CD1    1 
ATOM   10973 C  CD2    . TRP   D 2  101 ? -33.172 12.796   -34.785 1.00 86.53  ? 101 TRP   D CD2    1 
ATOM   10974 N  NE1    . TRP   D 2  101 ? -31.570 11.237   -34.589 1.00 74.35  ? 101 TRP   D NE1    1 
ATOM   10975 C  CE2    . TRP   D 2  101 ? -32.795 11.620   -34.107 1.00 78.23  ? 101 TRP   D CE2    1 
ATOM   10976 C  CE3    . TRP   D 2  101 ? -34.405 13.392   -34.474 1.00 85.33  ? 101 TRP   D CE3    1 
ATOM   10977 C  CZ2    . TRP   D 2  101 ? -33.601 11.032   -33.136 1.00 80.06  ? 101 TRP   D CZ2    1 
ATOM   10978 C  CZ3    . TRP   D 2  101 ? -35.206 12.805   -33.513 1.00 81.67  ? 101 TRP   D CZ3    1 
ATOM   10979 C  CH2    . TRP   D 2  101 ? -34.802 11.639   -32.854 1.00 82.04  ? 101 TRP   D CH2    1 
ATOM   10980 N  N      . ALA   D 2  102 ? -34.883 14.573   -38.052 1.00 86.39  ? 102 ALA   D N      1 
ATOM   10981 C  CA     . ALA   D 2  102 ? -36.298 14.236   -38.183 1.00 86.76  ? 102 ALA   D CA     1 
ATOM   10982 C  C      . ALA   D 2  102 ? -36.576 13.509   -39.497 1.00 85.29  ? 102 ALA   D C      1 
ATOM   10983 O  O      . ALA   D 2  102 ? -37.430 12.617   -39.544 1.00 84.32  ? 102 ALA   D O      1 
ATOM   10984 C  CB     . ALA   D 2  102 ? -37.158 15.494   -38.056 1.00 82.11  ? 102 ALA   D CB     1 
ATOM   10985 N  N      . LYS   D 2  103 ? -35.839 13.848   -40.559 1.00 85.83  ? 103 LYS   D N      1 
ATOM   10986 C  CA     . LYS   D 2  103 ? -36.001 13.163   -41.840 1.00 90.81  ? 103 LYS   D CA     1 
ATOM   10987 C  C      . LYS   D 2  103 ? -35.557 11.708   -41.767 1.00 88.43  ? 103 LYS   D C      1 
ATOM   10988 O  O      . LYS   D 2  103 ? -36.131 10.848   -42.449 1.00 91.05  ? 103 LYS   D O      1 
ATOM   10989 C  CB     . LYS   D 2  103 ? -35.205 13.876   -42.943 1.00 94.92  ? 103 LYS   D CB     1 
ATOM   10990 C  CG     . LYS   D 2  103 ? -35.952 14.926   -43.758 1.00 91.13  ? 103 LYS   D CG     1 
ATOM   10991 C  CD     . LYS   D 2  103 ? -35.010 15.512   -44.803 1.00 90.92  ? 103 LYS   D CD     1 
ATOM   10992 C  CE     . LYS   D 2  103 ? -35.750 16.389   -45.810 1.00 100.28 ? 103 LYS   D CE     1 
ATOM   10993 N  NZ     . LYS   D 2  103 ? -35.022 16.527   -47.112 1.00 95.93  ? 103 LYS   D NZ     1 
ATOM   10994 N  N      . GLY   D 2  104 ? -34.518 11.420   -40.991 1.00 85.94  ? 104 GLY   D N      1 
ATOM   10995 C  CA     . GLY   D 2  104 ? -34.016 10.067   -40.896 1.00 81.95  ? 104 GLY   D CA     1 
ATOM   10996 C  C      . GLY   D 2  104 ? -34.821 9.269    -39.899 1.00 79.82  ? 104 GLY   D C      1 
ATOM   10997 O  O      . GLY   D 2  104 ? -35.123 8.091    -40.127 1.00 74.54  ? 104 GLY   D O      1 
ATOM   10998 N  N      . HIS   D 2  105 ? -35.187 9.923    -38.791 1.00 79.26  ? 105 HIS   D N      1 
ATOM   10999 C  CA     . HIS   D 2  105 ? -35.898 9.252    -37.706 1.00 80.14  ? 105 HIS   D CA     1 
ATOM   11000 C  C      . HIS   D 2  105 ? -37.377 9.078    -38.014 1.00 81.52  ? 105 HIS   D C      1 
ATOM   11001 O  O      . HIS   D 2  105 ? -37.880 7.949    -38.073 1.00 80.20  ? 105 HIS   D O      1 
ATOM   11002 C  CB     . HIS   D 2  105 ? -35.702 10.010   -36.385 1.00 80.47  ? 105 HIS   D CB     1 
ATOM   11003 C  CG     . HIS   D 2  105 ? -35.965 9.174    -35.166 1.00 78.68  ? 105 HIS   D CG     1 
ATOM   11004 N  ND1    . HIS   D 2  105 ? -35.117 8.177    -34.738 1.00 67.64  ? 105 HIS   D ND1    1 
ATOM   11005 C  CD2    . HIS   D 2  105 ? -36.971 9.223    -34.258 1.00 82.21  ? 105 HIS   D CD2    1 
ATOM   11006 C  CE1    . HIS   D 2  105 ? -35.612 7.620    -33.648 1.00 70.62  ? 105 HIS   D CE1    1 
ATOM   11007 N  NE2    . HIS   D 2  105 ? -36.732 8.244    -33.328 1.00 73.77  ? 105 HIS   D NE2    1 
ATOM   11008 N  N      . TYR   D 2  106 ? -38.086 10.183   -38.220 1.00 82.03  ? 106 TYR   D N      1 
ATOM   11009 C  CA     . TYR   D 2  106 ? -39.539 10.117   -38.217 1.00 84.88  ? 106 TYR   D CA     1 
ATOM   11010 C  C      . TYR   D 2  106 ? -40.163 9.931    -39.599 1.00 89.83  ? 106 TYR   D C      1 
ATOM   11011 O  O      . TYR   D 2  106 ? -41.165 9.215    -39.726 1.00 95.30  ? 106 TYR   D O      1 
ATOM   11012 C  CB     . TYR   D 2  106 ? -40.107 11.370   -37.562 1.00 84.31  ? 106 TYR   D CB     1 
ATOM   11013 C  CG     . TYR   D 2  106 ? -39.901 11.416   -36.080 1.00 83.98  ? 106 TYR   D CG     1 
ATOM   11014 C  CD1    . TYR   D 2  106 ? -40.507 10.478   -35.251 1.00 87.99  ? 106 TYR   D CD1    1 
ATOM   11015 C  CD2    . TYR   D 2  106 ? -39.148 12.421   -35.499 1.00 83.81  ? 106 TYR   D CD2    1 
ATOM   11016 C  CE1    . TYR   D 2  106 ? -40.342 10.526   -33.877 1.00 89.64  ? 106 TYR   D CE1    1 
ATOM   11017 C  CE2    . TYR   D 2  106 ? -38.976 12.482   -34.132 1.00 87.12  ? 106 TYR   D CE2    1 
ATOM   11018 C  CZ     . TYR   D 2  106 ? -39.575 11.535   -33.324 1.00 87.63  ? 106 TYR   D CZ     1 
ATOM   11019 O  OH     . TYR   D 2  106 ? -39.401 11.600   -31.963 1.00 88.62  ? 106 TYR   D OH     1 
ATOM   11020 N  N      . THR   D 2  107 ? -39.621 10.560   -40.646 1.00 85.31  ? 107 THR   D N      1 
ATOM   11021 C  CA     . THR   D 2  107 ? -40.325 10.606   -41.913 1.00 84.02  ? 107 THR   D CA     1 
ATOM   11022 C  C      . THR   D 2  107 ? -39.621 9.663    -42.880 1.00 82.57  ? 107 THR   D C      1 
ATOM   11023 O  O      . THR   D 2  107 ? -39.961 8.467    -42.927 1.00 85.93  ? 107 THR   D O      1 
ATOM   11024 C  CB     . THR   D 2  107 ? -40.414 12.043   -42.438 1.00 85.39  ? 107 THR   D CB     1 
ATOM   11025 O  OG1    . THR   D 2  107 ? -39.112 12.486   -42.824 1.00 86.48  ? 107 THR   D OG1    1 
ATOM   11026 C  CG2    . THR   D 2  107 ? -40.959 12.990   -41.344 1.00 84.50  ? 107 THR   D CG2    1 
ATOM   11027 N  N      . GLU   D 2  108 ? -38.636 10.129   -43.641 1.00 84.66  ? 108 GLU   D N      1 
ATOM   11028 C  CA     . GLU   D 2  108 ? -38.144 9.368    -44.790 1.00 91.69  ? 108 GLU   D CA     1 
ATOM   11029 C  C      . GLU   D 2  108 ? -37.472 8.067    -44.371 1.00 91.37  ? 108 GLU   D C      1 
ATOM   11030 O  O      . GLU   D 2  108 ? -37.698 7.018    -44.988 1.00 92.19  ? 108 GLU   D O      1 
ATOM   11031 C  CB     . GLU   D 2  108 ? -37.204 10.252   -45.600 1.00 88.03  ? 108 GLU   D CB     1 
ATOM   11032 C  CG     . GLU   D 2  108 ? -37.890 11.552   -45.961 1.00 95.88  ? 108 GLU   D CG     1 
ATOM   11033 C  CD     . GLU   D 2  108 ? -37.057 12.455   -46.819 1.00 103.63 ? 108 GLU   D CD     1 
ATOM   11034 O  OE1    . GLU   D 2  108 ? -36.576 11.993   -47.874 1.00 110.05 ? 108 GLU   D OE1    1 
ATOM   11035 O  OE2    . GLU   D 2  108 ? -36.911 13.639   -46.441 1.00 105.88 ? 108 GLU   D OE2    1 
ATOM   11036 N  N      . GLY   D 2  109 ? -36.642 8.109    -43.329 1.00 91.16  ? 109 GLY   D N      1 
ATOM   11037 C  CA     . GLY   D 2  109 ? -36.128 6.870    -42.767 1.00 88.55  ? 109 GLY   D CA     1 
ATOM   11038 C  C      . GLY   D 2  109 ? -37.236 5.945    -42.301 1.00 86.43  ? 109 GLY   D C      1 
ATOM   11039 O  O      . GLY   D 2  109 ? -37.191 4.737    -42.546 1.00 82.73  ? 109 GLY   D O      1 
ATOM   11040 N  N      . ALA   D 2  110 ? -38.252 6.503    -41.628 1.00 86.19  ? 110 ALA   D N      1 
ATOM   11041 C  CA     . ALA   D 2  110 ? -39.402 5.714    -41.197 1.00 80.09  ? 110 ALA   D CA     1 
ATOM   11042 C  C      . ALA   D 2  110 ? -39.944 4.849    -42.328 1.00 84.81  ? 110 ALA   D C      1 
ATOM   11043 O  O      . ALA   D 2  110 ? -40.366 3.709    -42.103 1.00 83.81  ? 110 ALA   D O      1 
ATOM   11044 C  CB     . ALA   D 2  110 ? -40.496 6.638    -40.667 1.00 78.23  ? 110 ALA   D CB     1 
ATOM   11045 N  N      . GLU   D 2  111 ? -39.942 5.374    -43.554 1.00 87.45  ? 111 GLU   D N      1 
ATOM   11046 C  CA     . GLU   D 2  111 ? -40.489 4.638    -44.685 1.00 85.70  ? 111 GLU   D CA     1 
ATOM   11047 C  C      . GLU   D 2  111 ? -39.564 3.517    -45.136 1.00 89.20  ? 111 GLU   D C      1 
ATOM   11048 O  O      . GLU   D 2  111 ? -40.017 2.399    -45.413 1.00 92.14  ? 111 GLU   D O      1 
ATOM   11049 C  CB     . GLU   D 2  111 ? -40.756 5.605    -45.821 1.00 85.26  ? 111 GLU   D CB     1 
ATOM   11050 C  CG     . GLU   D 2  111 ? -41.804 6.594    -45.437 1.00 93.25  ? 111 GLU   D CG     1 
ATOM   11051 C  CD     . GLU   D 2  111 ? -41.846 7.760    -46.373 1.00 102.85 ? 111 GLU   D CD     1 
ATOM   11052 O  OE1    . GLU   D 2  111 ? -41.713 7.539    -47.594 1.00 113.84 ? 111 GLU   D OE1    1 
ATOM   11053 O  OE2    . GLU   D 2  111 ? -42.017 8.895    -45.887 1.00 101.30 ? 111 GLU   D OE2    1 
ATOM   11054 N  N      . LEU   D 2  112 ? -38.270 3.788    -45.217 1.00 86.56  ? 112 LEU   D N      1 
ATOM   11055 C  CA     . LEU   D 2  112 ? -37.342 2.723    -45.551 1.00 82.07  ? 112 LEU   D CA     1 
ATOM   11056 C  C      . LEU   D 2  112 ? -37.101 1.746    -44.397 1.00 83.15  ? 112 LEU   D C      1 
ATOM   11057 O  O      . LEU   D 2  112 ? -36.582 0.655    -44.647 1.00 81.32  ? 112 LEU   D O      1 
ATOM   11058 C  CB     . LEU   D 2  112 ? -36.027 3.339    -46.035 1.00 73.68  ? 112 LEU   D CB     1 
ATOM   11059 C  CG     . LEU   D 2  112 ? -34.935 2.400    -46.551 1.00 79.70  ? 112 LEU   D CG     1 
ATOM   11060 C  CD1    . LEU   D 2  112 ? -35.275 1.780    -47.889 1.00 81.50  ? 112 LEU   D CD1    1 
ATOM   11061 C  CD2    . LEU   D 2  112 ? -33.630 3.173    -46.653 1.00 83.11  ? 112 LEU   D CD2    1 
ATOM   11062 N  N      . VAL   D 2  113 ? -37.498 2.080    -43.159 1.00 83.26  ? 113 VAL   D N      1 
ATOM   11063 C  CA     . VAL   D 2  113 ? -37.066 1.299    -41.992 1.00 81.05  ? 113 VAL   D CA     1 
ATOM   11064 C  C      . VAL   D 2  113 ? -37.586 -0.134   -42.070 1.00 79.33  ? 113 VAL   D C      1 
ATOM   11065 O  O      . VAL   D 2  113 ? -36.822 -1.096   -41.923 1.00 69.45  ? 113 VAL   D O      1 
ATOM   11066 C  CB     . VAL   D 2  113 ? -37.494 1.984    -40.675 1.00 77.60  ? 113 VAL   D CB     1 
ATOM   11067 C  CG1    . VAL   D 2  113 ? -38.998 1.945    -40.486 1.00 81.92  ? 113 VAL   D CG1    1 
ATOM   11068 C  CG2    . VAL   D 2  113 ? -36.806 1.348    -39.477 1.00 63.18  ? 113 VAL   D CG2    1 
ATOM   11069 N  N      . ASP   D 2  114 ? -38.897 -0.298   -42.288 1.00 84.05  ? 114 ASP   D N      1 
ATOM   11070 C  CA     . ASP   D 2  114 ? -39.481 -1.635   -42.314 1.00 78.05  ? 114 ASP   D CA     1 
ATOM   11071 C  C      . ASP   D 2  114 ? -38.839 -2.476   -43.404 1.00 76.91  ? 114 ASP   D C      1 
ATOM   11072 O  O      . ASP   D 2  114 ? -38.824 -3.705   -43.305 1.00 75.96  ? 114 ASP   D O      1 
ATOM   11073 C  CB     . ASP   D 2  114 ? -41.001 -1.552   -42.510 1.00 78.17  ? 114 ASP   D CB     1 
ATOM   11074 C  CG     . ASP   D 2  114 ? -41.723 -0.910   -41.310 1.00 87.96  ? 114 ASP   D CG     1 
ATOM   11075 O  OD1    . ASP   D 2  114 ? -41.132 -0.819   -40.217 1.00 88.10  ? 114 ASP   D OD1    1 
ATOM   11076 O  OD2    . ASP   D 2  114 ? -42.882 -0.464   -41.456 1.00 95.81  ? 114 ASP   D OD2    1 
ATOM   11077 N  N      . SER   D 2  115 ? -38.270 -1.822   -44.417 1.00 82.43  ? 115 SER   D N      1 
ATOM   11078 C  CA     . SER   D 2  115 ? -37.538 -2.466   -45.505 1.00 85.99  ? 115 SER   D CA     1 
ATOM   11079 C  C      . SER   D 2  115 ? -36.169 -2.979   -45.066 1.00 79.26  ? 115 SER   D C      1 
ATOM   11080 O  O      . SER   D 2  115 ? -35.630 -3.899   -45.699 1.00 68.52  ? 115 SER   D O      1 
ATOM   11081 C  CB     . SER   D 2  115 ? -37.374 -1.462   -46.650 1.00 90.01  ? 115 SER   D CB     1 
ATOM   11082 O  OG     . SER   D 2  115 ? -38.525 -0.618   -46.752 1.00 95.66  ? 115 SER   D OG     1 
ATOM   11083 N  N      . VAL   D 2  116 ? -35.601 -2.374   -44.011 1.00 82.06  ? 116 VAL   D N      1 
ATOM   11084 C  CA     . VAL   D 2  116 ? -34.350 -2.827   -43.404 1.00 77.25  ? 116 VAL   D CA     1 
ATOM   11085 C  C      . VAL   D 2  116 ? -34.621 -3.927   -42.388 1.00 74.99  ? 116 VAL   D C      1 
ATOM   11086 O  O      . VAL   D 2  116 ? -33.966 -4.977   -42.382 1.00 69.76  ? 116 VAL   D O      1 
ATOM   11087 C  CB     . VAL   D 2  116 ? -33.633 -1.642   -42.730 1.00 74.01  ? 116 VAL   D CB     1 
ATOM   11088 C  CG1    . VAL   D 2  116 ? -32.272 -2.073   -42.146 1.00 62.70  ? 116 VAL   D CG1    1 
ATOM   11089 C  CG2    . VAL   D 2  116 ? -33.546 -0.427   -43.659 1.00 73.79  ? 116 VAL   D CG2    1 
ATOM   11090 N  N      . LEU   D 2  117 ? -35.590 -3.682   -41.503 1.00 73.00  ? 117 LEU   D N      1 
ATOM   11091 C  CA     . LEU   D 2  117 ? -35.924 -4.655   -40.477 1.00 71.96  ? 117 LEU   D CA     1 
ATOM   11092 C  C      . LEU   D 2  117 ? -36.099 -6.036   -41.082 1.00 71.57  ? 117 LEU   D C      1 
ATOM   11093 O  O      . LEU   D 2  117 ? -35.606 -7.028   -40.538 1.00 72.31  ? 117 LEU   D O      1 
ATOM   11094 C  CB     . LEU   D 2  117 ? -37.183 -4.218   -39.736 1.00 64.67  ? 117 LEU   D CB     1 
ATOM   11095 C  CG     . LEU   D 2  117 ? -36.873 -3.034   -38.835 1.00 62.39  ? 117 LEU   D CG     1 
ATOM   11096 C  CD1    . LEU   D 2  117 ? -38.126 -2.432   -38.233 1.00 63.96  ? 117 LEU   D CD1    1 
ATOM   11097 C  CD2    . LEU   D 2  117 ? -35.863 -3.427   -37.769 1.00 69.22  ? 117 LEU   D CD2    1 
ATOM   11098 N  N      . ASP   D 2  118 ? -36.784 -6.120   -42.220 1.00 72.62  ? 118 ASP   D N      1 
ATOM   11099 C  CA     . ASP   D 2  118 ? -36.872 -7.400   -42.910 1.00 76.50  ? 118 ASP   D CA     1 
ATOM   11100 C  C      . ASP   D 2  118 ? -35.501 -8.057   -43.003 1.00 69.87  ? 118 ASP   D C      1 
ATOM   11101 O  O      . ASP   D 2  118 ? -35.348 -9.250   -42.718 1.00 68.30  ? 118 ASP   D O      1 
ATOM   11102 C  CB     . ASP   D 2  118 ? -37.481 -7.214   -44.305 1.00 76.98  ? 118 ASP   D CB     1 
ATOM   11103 C  CG     . ASP   D 2  118 ? -38.976 -6.870   -44.265 1.00 83.87  ? 118 ASP   D CG     1 
ATOM   11104 O  OD1    . ASP   D 2  118 ? -39.579 -6.887   -43.164 1.00 84.04  ? 118 ASP   D OD1    1 
ATOM   11105 O  OD2    . ASP   D 2  118 ? -39.548 -6.573   -45.344 1.00 90.72  ? 118 ASP   D OD2    1 
ATOM   11106 N  N      . VAL   D 2  119 ? -34.479 -7.282   -43.364 1.00 72.63  ? 119 VAL   D N      1 
ATOM   11107 C  CA     . VAL   D 2  119 ? -33.196 -7.905   -43.667 1.00 75.65  ? 119 VAL   D CA     1 
ATOM   11108 C  C      . VAL   D 2  119 ? -32.510 -8.350   -42.372 1.00 74.90  ? 119 VAL   D C      1 
ATOM   11109 O  O      . VAL   D 2  119 ? -31.733 -9.317   -42.367 1.00 72.26  ? 119 VAL   D O      1 
ATOM   11110 C  CB     . VAL   D 2  119 ? -32.318 -6.947   -44.500 1.00 69.36  ? 119 VAL   D CB     1 
ATOM   11111 C  CG1    . VAL   D 2  119 ? -30.976 -7.613   -44.871 1.00 64.61  ? 119 VAL   D CG1    1 
ATOM   11112 C  CG2    . VAL   D 2  119 ? -33.082 -6.446   -45.733 1.00 72.27  ? 119 VAL   D CG2    1 
ATOM   11113 N  N      . VAL   D 2  120 ? -32.795 -7.680   -41.251 1.00 68.70  ? 120 VAL   D N      1 
ATOM   11114 C  CA     . VAL   D 2  120 ? -32.235 -8.115   -39.975 1.00 66.52  ? 120 VAL   D CA     1 
ATOM   11115 C  C      . VAL   D 2  120 ? -32.770 -9.503   -39.616 1.00 69.78  ? 120 VAL   D C      1 
ATOM   11116 O  O      . VAL   D 2  120 ? -32.004 -10.463  -39.461 1.00 68.78  ? 120 VAL   D O      1 
ATOM   11117 C  CB     . VAL   D 2  120 ? -32.539 -7.084   -38.871 1.00 67.48  ? 120 VAL   D CB     1 
ATOM   11118 C  CG1    . VAL   D 2  120 ? -32.075 -7.605   -37.535 1.00 70.92  ? 120 VAL   D CG1    1 
ATOM   11119 C  CG2    . VAL   D 2  120 ? -31.902 -5.726   -39.169 1.00 68.57  ? 120 VAL   D CG2    1 
ATOM   11120 N  N      . ARG   D 2  121 ? -34.100 -9.629   -39.498 1.00 68.11  ? 121 ARG   D N      1 
ATOM   11121 C  CA     . ARG   D 2  121 ? -34.749 -10.919  -39.261 1.00 65.66  ? 121 ARG   D CA     1 
ATOM   11122 C  C      . ARG   D 2  121 ? -34.167 -12.047  -40.087 1.00 66.57  ? 121 ARG   D C      1 
ATOM   11123 O  O      . ARG   D 2  121 ? -33.877 -13.125  -39.564 1.00 72.79  ? 121 ARG   D O      1 
ATOM   11124 C  CB     . ARG   D 2  121 ? -36.246 -10.820  -39.549 1.00 65.12  ? 121 ARG   D CB     1 
ATOM   11125 C  CG     . ARG   D 2  121 ? -36.981 -9.872   -38.681 1.00 67.18  ? 121 ARG   D CG     1 
ATOM   11126 C  CD     . ARG   D 2  121 ? -38.452 -9.916   -38.968 1.00 64.97  ? 121 ARG   D CD     1 
ATOM   11127 N  NE     . ARG   D 2  121 ? -39.068 -8.683   -38.496 1.00 78.63  ? 121 ARG   D NE     1 
ATOM   11128 C  CZ     . ARG   D 2  121 ? -39.425 -7.656   -39.256 1.00 78.62  ? 121 ARG   D CZ     1 
ATOM   11129 N  NH1    . ARG   D 2  121 ? -39.260 -7.677   -40.571 1.00 76.18  ? 121 ARG   D NH1    1 
ATOM   11130 N  NH2    . ARG   D 2  121 ? -39.965 -6.579   -38.679 1.00 68.62  ? 121 ARG   D NH2    1 
ATOM   11131 N  N      . LYS   D 2  122 ? -34.044 -11.842  -41.394 1.00 66.84  ? 122 LYS   D N      1 
ATOM   11132 C  CA     . LYS   D 2  122 ? -33.501 -12.896  -42.237 1.00 65.52  ? 122 LYS   D CA     1 
ATOM   11133 C  C      . LYS   D 2  122 ? -32.151 -13.354  -41.706 1.00 69.97  ? 122 LYS   D C      1 
ATOM   11134 O  O      . LYS   D 2  122 ? -31.896 -14.556  -41.589 1.00 72.27  ? 122 LYS   D O      1 
ATOM   11135 C  CB     . LYS   D 2  122 ? -33.400 -12.400  -43.680 1.00 68.82  ? 122 LYS   D CB     1 
ATOM   11136 C  CG     . LYS   D 2  122 ? -32.751 -13.368  -44.667 1.00 78.12  ? 122 LYS   D CG     1 
ATOM   11137 C  CD     . LYS   D 2  122 ? -33.706 -14.481  -45.081 1.00 83.52  ? 122 LYS   D CD     1 
ATOM   11138 C  CE     . LYS   D 2  122 ? -33.157 -15.296  -46.248 1.00 85.35  ? 122 LYS   D CE     1 
ATOM   11139 N  NZ     . LYS   D 2  122 ? -34.177 -16.252  -46.767 1.00 84.78  ? 122 LYS   D NZ     1 
ATOM   11140 N  N      . GLU   D 2  123 ? -31.277 -12.405  -41.343 1.00 74.99  ? 123 GLU   D N      1 
ATOM   11141 C  CA     . GLU   D 2  123 ? -29.974 -12.782  -40.797 1.00 74.86  ? 123 GLU   D CA     1 
ATOM   11142 C  C      . GLU   D 2  123 ? -30.099 -13.317  -39.381 1.00 66.86  ? 123 GLU   D C      1 
ATOM   11143 O  O      . GLU   D 2  123 ? -29.422 -14.282  -39.013 1.00 66.27  ? 123 GLU   D O      1 
ATOM   11144 C  CB     . GLU   D 2  123 ? -29.001 -11.594  -40.831 1.00 73.74  ? 123 GLU   D CB     1 
ATOM   11145 C  CG     . GLU   D 2  123 ? -28.617 -11.054  -42.215 1.00 68.54  ? 123 GLU   D CG     1 
ATOM   11146 C  CD     . GLU   D 2  123 ? -27.413 -11.794  -42.812 1.00 72.66  ? 123 GLU   D CD     1 
ATOM   11147 O  OE1    . GLU   D 2  123 ? -26.928 -12.749  -42.157 1.00 73.69  ? 123 GLU   D OE1    1 
ATOM   11148 O  OE2    . GLU   D 2  123 ? -26.917 -11.396  -43.898 1.00 69.05  ? 123 GLU   D OE2    1 
ATOM   11149 N  N      . SER   D 2  124 ? -30.953 -12.695  -38.577 1.00 63.96  ? 124 SER   D N      1 
ATOM   11150 C  CA     . SER   D 2  124 ? -31.154 -13.133  -37.203 1.00 67.89  ? 124 SER   D CA     1 
ATOM   11151 C  C      . SER   D 2  124 ? -31.553 -14.604  -37.141 1.00 72.05  ? 124 SER   D C      1 
ATOM   11152 O  O      . SER   D 2  124 ? -30.904 -15.405  -36.459 1.00 71.61  ? 124 SER   D O      1 
ATOM   11153 C  CB     . SER   D 2  124 ? -32.224 -12.268  -36.555 1.00 65.76  ? 124 SER   D CB     1 
ATOM   11154 O  OG     . SER   D 2  124 ? -31.670 -11.023  -36.214 1.00 67.26  ? 124 SER   D OG     1 
ATOM   11155 N  N      . GLU   D 2  125 ? -32.637 -14.980  -37.838 1.00 70.35  ? 125 GLU   D N      1 
ATOM   11156 C  CA     . GLU   D 2  125 ? -33.145 -16.346  -37.726 1.00 73.64  ? 125 GLU   D CA     1 
ATOM   11157 C  C      . GLU   D 2  125 ? -32.112 -17.382  -38.153 1.00 73.63  ? 125 GLU   D C      1 
ATOM   11158 O  O      . GLU   D 2  125 ? -32.165 -18.538  -37.711 1.00 65.26  ? 125 GLU   D O      1 
ATOM   11159 C  CB     . GLU   D 2  125 ? -34.396 -16.531  -38.571 1.00 80.42  ? 125 GLU   D CB     1 
ATOM   11160 C  CG     . GLU   D 2  125 ? -35.612 -15.748  -38.160 1.00 83.86  ? 125 GLU   D CG     1 
ATOM   11161 C  CD     . GLU   D 2  125 ? -36.703 -15.951  -39.194 1.00 96.74  ? 125 GLU   D CD     1 
ATOM   11162 O  OE1    . GLU   D 2  125 ? -36.428 -16.678  -40.176 1.00 94.34  ? 125 GLU   D OE1    1 
ATOM   11163 O  OE2    . GLU   D 2  125 ? -37.808 -15.388  -39.051 1.00 107.13 ? 125 GLU   D OE2    1 
ATOM   11164 N  N      . SER   D 2  126 ? -31.189 -17.000  -39.033 1.00 74.57  ? 126 SER   D N      1 
ATOM   11165 C  CA     . SER   D 2  126 ? -30.121 -17.905  -39.417 1.00 73.88  ? 126 SER   D CA     1 
ATOM   11166 C  C      . SER   D 2  126 ? -29.108 -18.123  -38.293 1.00 79.74  ? 126 SER   D C      1 
ATOM   11167 O  O      . SER   D 2  126 ? -28.206 -18.957  -38.448 1.00 84.11  ? 126 SER   D O      1 
ATOM   11168 C  CB     . SER   D 2  126 ? -29.431 -17.371  -40.678 1.00 74.83  ? 126 SER   D CB     1 
ATOM   11169 O  OG     . SER   D 2  126 ? -28.230 -18.080  -40.951 1.00 85.30  ? 126 SER   D OG     1 
ATOM   11170 N  N      . CYS   D 2  127 ? -29.241 -17.418  -37.166 1.00 75.20  ? 127 CYS   D N      1 
ATOM   11171 C  CA     . CYS   D 2  127 ? -28.289 -17.534  -36.064 1.00 73.42  ? 127 CYS   D CA     1 
ATOM   11172 C  C      . CYS   D 2  127 ? -28.670 -18.634  -35.088 1.00 71.23  ? 127 CYS   D C      1 
ATOM   11173 O  O      . CYS   D 2  127 ? -29.794 -18.672  -34.576 1.00 69.52  ? 127 CYS   D O      1 
ATOM   11174 C  CB     . CYS   D 2  127 ? -28.153 -16.224  -35.288 1.00 69.54  ? 127 CYS   D CB     1 
ATOM   11175 S  SG     . CYS   D 2  127 ? -27.357 -14.931  -36.175 1.00 67.45  ? 127 CYS   D SG     1 
ATOM   11176 N  N      . ASP   D 2  128 ? -27.704 -19.497  -34.802 1.00 66.30  ? 128 ASP   D N      1 
ATOM   11177 C  CA     . ASP   D 2  128 ? -27.875 -20.453  -33.728 1.00 66.31  ? 128 ASP   D CA     1 
ATOM   11178 C  C      . ASP   D 2  128 ? -28.057 -19.737  -32.394 1.00 65.32  ? 128 ASP   D C      1 
ATOM   11179 O  O      . ASP   D 2  128 ? -28.960 -20.063  -31.621 1.00 74.12  ? 128 ASP   D O      1 
ATOM   11180 C  CB     . ASP   D 2  128 ? -26.673 -21.388  -33.702 1.00 75.09  ? 128 ASP   D CB     1 
ATOM   11181 C  CG     . ASP   D 2  128 ? -26.802 -22.473  -32.664 1.00 84.68  ? 128 ASP   D CG     1 
ATOM   11182 O  OD1    . ASP   D 2  128 ? -27.948 -22.745  -32.238 1.00 81.31  ? 128 ASP   D OD1    1 
ATOM   11183 O  OD2    . ASP   D 2  128 ? -25.754 -23.040  -32.269 1.00 86.17  ? 128 ASP   D OD2    1 
ATOM   11184 N  N      . CYS   D 2  129 ? -27.224 -18.738  -32.117 1.00 60.01  ? 129 CYS   D N      1 
ATOM   11185 C  CA     . CYS   D 2  129 ? -27.260 -18.042  -30.831 1.00 60.60  ? 129 CYS   D CA     1 
ATOM   11186 C  C      . CYS   D 2  129 ? -26.952 -16.564  -31.046 1.00 63.13  ? 129 CYS   D C      1 
ATOM   11187 O  O      . CYS   D 2  129 ? -25.827 -16.105  -30.872 1.00 69.29  ? 129 CYS   D O      1 
ATOM   11188 C  CB     . CYS   D 2  129 ? -26.277 -18.630  -29.825 1.00 62.32  ? 129 CYS   D CB     1 
ATOM   11189 S  SG     . CYS   D 2  129 ? -26.671 -18.149  -28.150 1.00 61.10  ? 129 CYS   D SG     1 
ATOM   11190 N  N      . LEU   D 2  130 ? -27.972 -15.803  -31.392 1.00 61.28  ? 130 LEU   D N      1 
ATOM   11191 C  CA     . LEU   D 2  130 ? -27.751 -14.402  -31.698 1.00 61.33  ? 130 LEU   D CA     1 
ATOM   11192 C  C      . LEU   D 2  130 ? -27.291 -13.664  -30.432 1.00 64.44  ? 130 LEU   D C      1 
ATOM   11193 O  O      . LEU   D 2  130 ? -28.037 -13.569  -29.446 1.00 64.47  ? 130 LEU   D O      1 
ATOM   11194 C  CB     . LEU   D 2  130 ? -29.033 -13.822  -32.284 1.00 62.59  ? 130 LEU   D CB     1 
ATOM   11195 C  CG     . LEU   D 2  130 ? -29.082 -12.317  -32.462 1.00 62.51  ? 130 LEU   D CG     1 
ATOM   11196 C  CD1    . LEU   D 2  130 ? -28.236 -11.994  -33.663 1.00 59.91  ? 130 LEU   D CD1    1 
ATOM   11197 C  CD2    . LEU   D 2  130 ? -30.506 -11.855  -32.672 1.00 55.76  ? 130 LEU   D CD2    1 
ATOM   11198 N  N      . GLN   D 2  131 ? -26.041 -13.176  -30.436 1.00 60.63  ? 131 GLN   D N      1 
ATOM   11199 C  CA     . GLN   D 2  131 ? -25.544 -12.288  -29.384 1.00 58.84  ? 131 GLN   D CA     1 
ATOM   11200 C  C      . GLN   D 2  131 ? -26.319 -10.984  -29.401 1.00 56.46  ? 131 GLN   D C      1 
ATOM   11201 O  O      . GLN   D 2  131 ? -27.063 -10.643  -28.477 1.00 57.67  ? 131 GLN   D O      1 
ATOM   11202 C  CB     . GLN   D 2  131 ? -24.054 -11.953  -29.563 1.00 56.43  ? 131 GLN   D CB     1 
ATOM   11203 C  CG     . GLN   D 2  131 ? -23.054 -13.098  -29.443 1.00 57.54  ? 131 GLN   D CG     1 
ATOM   11204 C  CD     . GLN   D 2  131 ? -21.606 -12.591  -29.382 1.00 57.97  ? 131 GLN   D CD     1 
ATOM   11205 O  OE1    . GLN   D 2  131 ? -21.320 -11.579  -28.748 1.00 57.77  ? 131 GLN   D OE1    1 
ATOM   11206 N  NE2    . GLN   D 2  131 ? -20.688 -13.315  -30.005 1.00 60.36  ? 131 GLN   D NE2    1 
ATOM   11207 N  N      . GLY   D 2  132 ? -26.128 -10.248  -30.476 1.00 54.38  ? 132 GLY   D N      1 
ATOM   11208 C  CA     . GLY   D 2  132 ? -26.842 -9.000   -30.652 1.00 55.87  ? 132 GLY   D CA     1 
ATOM   11209 C  C      . GLY   D 2  132 ? -26.314 -8.303   -31.875 1.00 57.78  ? 132 GLY   D C      1 
ATOM   11210 O  O      . GLY   D 2  132 ? -25.825 -8.946   -32.811 1.00 58.56  ? 132 GLY   D O      1 
ATOM   11211 N  N      . PHE   D 2  133 ? -26.349 -6.977   -31.822 1.00 59.44  ? 133 PHE   D N      1 
ATOM   11212 C  CA     . PHE   D 2  133 ? -26.057 -6.128   -32.963 1.00 64.52  ? 133 PHE   D CA     1 
ATOM   11213 C  C      . PHE   D 2  133 ? -25.000 -5.098   -32.591 1.00 63.77  ? 133 PHE   D C      1 
ATOM   11214 O  O      . PHE   D 2  133 ? -24.782 -4.800   -31.412 1.00 62.68  ? 133 PHE   D O      1 
ATOM   11215 C  CB     . PHE   D 2  133 ? -27.348 -5.454   -33.443 1.00 64.09  ? 133 PHE   D CB     1 
ATOM   11216 C  CG     . PHE   D 2  133 ? -28.498 -6.404   -33.532 1.00 61.72  ? 133 PHE   D CG     1 
ATOM   11217 C  CD1    . PHE   D 2  133 ? -29.318 -6.615   -32.443 1.00 57.91  ? 133 PHE   D CD1    1 
ATOM   11218 C  CD2    . PHE   D 2  133 ? -28.712 -7.144   -34.680 1.00 60.70  ? 133 PHE   D CD2    1 
ATOM   11219 C  CE1    . PHE   D 2  133 ? -30.367 -7.510   -32.518 1.00 59.78  ? 133 PHE   D CE1    1 
ATOM   11220 C  CE2    . PHE   D 2  133 ? -29.746 -8.047   -34.755 1.00 59.98  ? 133 PHE   D CE2    1 
ATOM   11221 C  CZ     . PHE   D 2  133 ? -30.578 -8.230   -33.674 1.00 60.66  ? 133 PHE   D CZ     1 
ATOM   11222 N  N      . GLN   D 2  134 ? -24.321 -4.572   -33.614 1.00 62.72  ? 134 GLN   D N      1 
ATOM   11223 C  CA     . GLN   D 2  134 ? -23.373 -3.466   -33.446 1.00 60.64  ? 134 GLN   D CA     1 
ATOM   11224 C  C      . GLN   D 2  134 ? -23.515 -2.530   -34.645 1.00 67.02  ? 134 GLN   D C      1 
ATOM   11225 O  O      . GLN   D 2  134 ? -23.016 -2.820   -35.738 1.00 71.80  ? 134 GLN   D O      1 
ATOM   11226 C  CB     . GLN   D 2  134 ? -21.942 -3.971   -33.273 1.00 55.13  ? 134 GLN   D CB     1 
ATOM   11227 C  CG     . GLN   D 2  134 ? -21.325 -4.614   -34.504 1.00 62.43  ? 134 GLN   D CG     1 
ATOM   11228 C  CD     . GLN   D 2  134 ? -19.857 -5.002   -34.314 1.00 66.58  ? 134 GLN   D CD     1 
ATOM   11229 O  OE1    . GLN   D 2  134 ? -19.432 -5.379   -33.219 1.00 67.34  ? 134 GLN   D OE1    1 
ATOM   11230 N  NE2    . GLN   D 2  134 ? -19.077 -4.902   -35.385 1.00 66.13  ? 134 GLN   D NE2    1 
ATOM   11231 N  N      . LEU   D 2  135 ? -24.216 -1.416   -34.441 1.00 60.79  ? 135 LEU   D N      1 
ATOM   11232 C  CA     . LEU   D 2  135 ? -24.412 -0.424   -35.484 1.00 58.14  ? 135 LEU   D CA     1 
ATOM   11233 C  C      . LEU   D 2  135 ? -23.199 0.491    -35.558 1.00 61.65  ? 135 LEU   D C      1 
ATOM   11234 O  O      . LEU   D 2  135 ? -22.681 0.939    -34.535 1.00 62.75  ? 135 LEU   D O      1 
ATOM   11235 C  CB     . LEU   D 2  135 ? -25.666 0.420    -35.225 1.00 54.91  ? 135 LEU   D CB     1 
ATOM   11236 C  CG     . LEU   D 2  135 ? -25.767 1.618    -36.170 1.00 55.52  ? 135 LEU   D CG     1 
ATOM   11237 C  CD1    . LEU   D 2  135 ? -26.403 1.127    -37.470 1.00 58.78  ? 135 LEU   D CD1    1 
ATOM   11238 C  CD2    . LEU   D 2  135 ? -26.518 2.802    -35.597 1.00 51.86  ? 135 LEU   D CD2    1 
ATOM   11239 N  N      . THR   D 2  136 ? -22.760 0.778    -36.777 1.00 66.32  ? 136 THR   D N      1 
ATOM   11240 C  CA     . THR   D 2  136 ? -21.787 1.826    -37.054 1.00 57.88  ? 136 THR   D CA     1 
ATOM   11241 C  C      . THR   D 2  136 ? -22.491 2.999    -37.708 1.00 55.03  ? 136 THR   D C      1 
ATOM   11242 O  O      . THR   D 2  136 ? -23.373 2.805    -38.542 1.00 57.40  ? 136 THR   D O      1 
ATOM   11243 C  CB     . THR   D 2  136 ? -20.718 1.308    -37.981 1.00 54.43  ? 136 THR   D CB     1 
ATOM   11244 O  OG1    . THR   D 2  136 ? -21.293 1.215    -39.276 1.00 56.39  ? 136 THR   D OG1    1 
ATOM   11245 C  CG2    . THR   D 2  136 ? -20.293 -0.057   -37.545 1.00 62.28  ? 136 THR   D CG2    1 
ATOM   11246 N  N      . HIS   D 2  137 ? -22.119 4.207    -37.339 1.00 56.71  ? 137 HIS   D N      1 
ATOM   11247 C  CA     . HIS   D 2  137 ? -22.823 5.364    -37.871 1.00 59.27  ? 137 HIS   D CA     1 
ATOM   11248 C  C      . HIS   D 2  137 ? -22.131 6.630    -37.382 1.00 63.50  ? 137 HIS   D C      1 
ATOM   11249 O  O      . HIS   D 2  137 ? -21.001 6.594    -36.879 1.00 62.52  ? 137 HIS   D O      1 
ATOM   11250 C  CB     . HIS   D 2  137 ? -24.296 5.320    -37.475 1.00 57.37  ? 137 HIS   D CB     1 
ATOM   11251 C  CG     . HIS   D 2  137 ? -24.540 5.503    -36.006 1.00 64.48  ? 137 HIS   D CG     1 
ATOM   11252 N  ND1    . HIS   D 2  137 ? -25.634 6.182    -35.516 1.00 66.26  ? 137 HIS   D ND1    1 
ATOM   11253 C  CD2    . HIS   D 2  137 ? -23.832 5.105    -34.922 1.00 62.52  ? 137 HIS   D CD2    1 
ATOM   11254 C  CE1    . HIS   D 2  137 ? -25.599 6.185    -34.196 1.00 57.35  ? 137 HIS   D CE1    1 
ATOM   11255 N  NE2    . HIS   D 2  137 ? -24.509 5.548    -33.811 1.00 62.23  ? 137 HIS   D NE2    1 
ATOM   11256 N  N      . SER   D 2  138 ? -22.805 7.756    -37.571 1.00 63.75  ? 138 SER   D N      1 
ATOM   11257 C  CA     . SER   D 2  138 ? -22.369 9.045    -37.086 1.00 64.51  ? 138 SER   D CA     1 
ATOM   11258 C  C      . SER   D 2  138 ? -23.570 9.665    -36.402 1.00 66.77  ? 138 SER   D C      1 
ATOM   11259 O  O      . SER   D 2  138 ? -24.689 9.170    -36.538 1.00 69.32  ? 138 SER   D O      1 
ATOM   11260 C  CB     . SER   D 2  138 ? -21.876 9.918    -38.230 1.00 67.19  ? 138 SER   D CB     1 
ATOM   11261 O  OG     . SER   D 2  138 ? -22.832 9.888    -39.276 1.00 81.23  ? 138 SER   D OG     1 
ATOM   11262 N  N      . LEU   D 2  139 ? -23.348 10.748   -35.665 1.00 63.47  ? 139 LEU   D N      1 
ATOM   11263 C  CA     . LEU   D 2  139 ? -24.438 11.387   -34.943 1.00 65.78  ? 139 LEU   D CA     1 
ATOM   11264 C  C      . LEU   D 2  139 ? -24.712 12.807   -35.434 1.00 75.28  ? 139 LEU   D C      1 
ATOM   11265 O  O      . LEU   D 2  139 ? -25.418 13.571   -34.761 1.00 74.69  ? 139 LEU   D O      1 
ATOM   11266 C  CB     . LEU   D 2  139 ? -24.151 11.356   -33.440 1.00 75.17  ? 139 LEU   D CB     1 
ATOM   11267 C  CG     . LEU   D 2  139 ? -23.834 9.963    -32.869 1.00 68.15  ? 139 LEU   D CG     1 
ATOM   11268 C  CD1    . LEU   D 2  139 ? -23.576 10.012   -31.390 1.00 59.26  ? 139 LEU   D CD1    1 
ATOM   11269 C  CD2    . LEU   D 2  139 ? -24.991 9.032    -33.131 1.00 67.36  ? 139 LEU   D CD2    1 
ATOM   11270 N  N      . GLY   D 2  140 ? -24.170 13.166   -36.602 1.00 82.21  ? 140 GLY   D N      1 
ATOM   11271 C  CA     . GLY   D 2  140 ? -24.492 14.402   -37.301 1.00 81.83  ? 140 GLY   D CA     1 
ATOM   11272 C  C      . GLY   D 2  140 ? -25.146 14.186   -38.660 1.00 78.67  ? 140 GLY   D C      1 
ATOM   11273 O  O      . GLY   D 2  140 ? -25.894 15.043   -39.126 1.00 72.64  ? 140 GLY   D O      1 
ATOM   11274 N  N      . GLY   D 2  141 ? -24.914 13.027   -39.278 1.00 89.22  ? 141 GLY   D N      1 
ATOM   11275 C  CA     . GLY   D 2  141 ? -25.290 12.781   -40.656 1.00 92.95  ? 141 GLY   D CA     1 
ATOM   11276 C  C      . GLY   D 2  141 ? -26.719 12.391   -40.976 1.00 93.71  ? 141 GLY   D C      1 
ATOM   11277 O  O      . GLY   D 2  141 ? -26.955 11.637   -41.931 1.00 101.03 ? 141 GLY   D O      1 
ATOM   11278 N  N      . GLY   D 2  142 ? -27.675 12.903   -40.202 1.00 76.63  ? 142 GLY   D N      1 
ATOM   11279 C  CA     . GLY   D 2  142 ? -29.084 12.725   -40.504 1.00 81.23  ? 142 GLY   D CA     1 
ATOM   11280 C  C      . GLY   D 2  142 ? -29.579 11.305   -40.740 1.00 82.41  ? 142 GLY   D C      1 
ATOM   11281 O  O      . GLY   D 2  142 ? -30.586 10.897   -40.147 1.00 82.06  ? 142 GLY   D O      1 
ATOM   11282 N  N      . THR   D 2  143 ? -28.918 10.549   -41.621 1.00 77.26  ? 143 THR   D N      1 
ATOM   11283 C  CA     . THR   D 2  143 ? -29.329 9.169    -41.850 1.00 75.61  ? 143 THR   D CA     1 
ATOM   11284 C  C      . THR   D 2  143 ? -28.743 8.229    -40.814 1.00 76.51  ? 143 THR   D C      1 
ATOM   11285 O  O      . THR   D 2  143 ? -29.474 7.470    -40.174 1.00 74.92  ? 143 THR   D O      1 
ATOM   11286 C  CB     . THR   D 2  143 ? -28.911 8.716    -43.240 1.00 82.62  ? 143 THR   D CB     1 
ATOM   11287 O  OG1    . THR   D 2  143 ? -29.736 9.361    -44.208 1.00 91.85  ? 143 THR   D OG1    1 
ATOM   11288 C  CG2    . THR   D 2  143 ? -29.051 7.224    -43.377 1.00 76.91  ? 143 THR   D CG2    1 
ATOM   11289 N  N      . GLY   D 2  144 ? -27.422 8.273    -40.646 1.00 81.21  ? 144 GLY   D N      1 
ATOM   11290 C  CA     . GLY   D 2  144 ? -26.785 7.489    -39.603 1.00 74.81  ? 144 GLY   D CA     1 
ATOM   11291 C  C      . GLY   D 2  144 ? -27.250 7.855    -38.202 1.00 74.13  ? 144 GLY   D C      1 
ATOM   11292 O  O      . GLY   D 2  144 ? -27.358 6.988    -37.334 1.00 68.55  ? 144 GLY   D O      1 
ATOM   11293 N  N      . SER   D 2  145 ? -27.522 9.139    -37.953 1.00 74.29  ? 145 SER   D N      1 
ATOM   11294 C  CA     . SER   D 2  145 ? -27.986 9.523    -36.623 1.00 70.77  ? 145 SER   D CA     1 
ATOM   11295 C  C      . SER   D 2  145 ? -29.474 9.253    -36.450 1.00 70.64  ? 145 SER   D C      1 
ATOM   11296 O  O      . SER   D 2  145 ? -29.886 8.614    -35.480 1.00 75.15  ? 145 SER   D O      1 
ATOM   11297 C  CB     . SER   D 2  145 ? -27.681 10.996   -36.337 1.00 72.05  ? 145 SER   D CB     1 
ATOM   11298 O  OG     . SER   D 2  145 ? -28.060 11.829   -37.405 1.00 78.34  ? 145 SER   D OG     1 
ATOM   11299 N  N      . GLY   D 2  146 ? -30.295 9.726    -37.373 1.00 76.87  ? 146 GLY   D N      1 
ATOM   11300 C  CA     . GLY   D 2  146 ? -31.732 9.623    -37.217 1.00 77.67  ? 146 GLY   D CA     1 
ATOM   11301 C  C      . GLY   D 2  146 ? -32.295 8.249    -37.501 1.00 73.36  ? 146 GLY   D C      1 
ATOM   11302 O  O      . GLY   D 2  146 ? -32.908 7.632    -36.630 1.00 72.06  ? 146 GLY   D O      1 
ATOM   11303 N  N      . MET   D 2  147 ? -32.138 7.763    -38.729 1.00 80.59  ? 147 MET   D N      1 
ATOM   11304 C  CA     . MET   D 2  147 ? -32.643 6.429    -39.024 1.00 77.43  ? 147 MET   D CA     1 
ATOM   11305 C  C      . MET   D 2  147 ? -31.943 5.401    -38.150 1.00 75.08  ? 147 MET   D C      1 
ATOM   11306 O  O      . MET   D 2  147 ? -32.575 4.460    -37.648 1.00 73.08  ? 147 MET   D O      1 
ATOM   11307 C  CB     . MET   D 2  147 ? -32.447 6.105    -40.504 1.00 76.23  ? 147 MET   D CB     1 
ATOM   11308 C  CG     . MET   D 2  147 ? -33.224 4.893    -40.960 1.00 77.32  ? 147 MET   D CG     1 
ATOM   11309 S  SD     . MET   D 2  147 ? -32.798 4.426    -42.646 1.00 71.14  ? 147 MET   D SD     1 
ATOM   11310 C  CE     . MET   D 2  147 ? -33.598 2.825    -42.772 1.00 67.70  ? 147 MET   D CE     1 
ATOM   11311 N  N      . GLY   D 2  148 ? -30.641 5.608    -37.910 1.00 77.81  ? 148 GLY   D N      1 
ATOM   11312 C  CA     . GLY   D 2  148 ? -29.861 4.657    -37.127 1.00 72.66  ? 148 GLY   D CA     1 
ATOM   11313 C  C      . GLY   D 2  148 ? -30.347 4.502    -35.698 1.00 66.24  ? 148 GLY   D C      1 
ATOM   11314 O  O      . GLY   D 2  148 ? -30.372 3.394    -35.166 1.00 68.07  ? 148 GLY   D O      1 
ATOM   11315 N  N      . THR   D 2  149 ? -30.727 5.608    -35.053 1.00 61.56  ? 149 THR   D N      1 
ATOM   11316 C  CA     . THR   D 2  149 ? -31.301 5.512    -33.722 1.00 62.69  ? 149 THR   D CA     1 
ATOM   11317 C  C      . THR   D 2  149 ? -32.773 5.117    -33.765 1.00 66.22  ? 149 THR   D C      1 
ATOM   11318 O  O      . THR   D 2  149 ? -33.298 4.610    -32.763 1.00 67.90  ? 149 THR   D O      1 
ATOM   11319 C  CB     . THR   D 2  149 ? -31.118 6.825    -32.946 1.00 65.64  ? 149 THR   D CB     1 
ATOM   11320 O  OG1    . THR   D 2  149 ? -31.749 7.905    -33.631 1.00 71.12  ? 149 THR   D OG1    1 
ATOM   11321 C  CG2    . THR   D 2  149 ? -29.649 7.158    -32.822 1.00 65.04  ? 149 THR   D CG2    1 
ATOM   11322 N  N      . LEU   D 2  150 ? -33.449 5.329    -34.898 1.00 64.67  ? 150 LEU   D N      1 
ATOM   11323 C  CA     . LEU   D 2  150 ? -34.756 4.706    -35.088 1.00 70.98  ? 150 LEU   D CA     1 
ATOM   11324 C  C      . LEU   D 2  150 ? -34.617 3.213    -35.331 1.00 68.03  ? 150 LEU   D C      1 
ATOM   11325 O  O      . LEU   D 2  150 ? -35.414 2.415    -34.817 1.00 61.01  ? 150 LEU   D O      1 
ATOM   11326 C  CB     . LEU   D 2  150 ? -35.508 5.346    -36.250 1.00 74.49  ? 150 LEU   D CB     1 
ATOM   11327 C  CG     . LEU   D 2  150 ? -36.750 4.546    -36.680 1.00 72.52  ? 150 LEU   D CG     1 
ATOM   11328 C  CD1    . LEU   D 2  150 ? -37.952 4.755    -35.760 1.00 70.20  ? 150 LEU   D CD1    1 
ATOM   11329 C  CD2    . LEU   D 2  150 ? -37.108 4.908    -38.103 1.00 70.17  ? 150 LEU   D CD2    1 
ATOM   11330 N  N      . LEU   D 2  151 ? -33.611 2.820    -36.113 1.00 62.84  ? 151 LEU   D N      1 
ATOM   11331 C  CA     . LEU   D 2  151 ? -33.405 1.406    -36.376 1.00 63.32  ? 151 LEU   D CA     1 
ATOM   11332 C  C      . LEU   D 2  151 ? -33.108 0.655    -35.080 1.00 69.65  ? 151 LEU   D C      1 
ATOM   11333 O  O      . LEU   D 2  151 ? -33.607 -0.456   -34.862 1.00 70.63  ? 151 LEU   D O      1 
ATOM   11334 C  CB     . LEU   D 2  151 ? -32.274 1.221    -37.383 1.00 61.08  ? 151 LEU   D CB     1 
ATOM   11335 C  CG     . LEU   D 2  151 ? -32.261 -0.186   -37.966 1.00 63.88  ? 151 LEU   D CG     1 
ATOM   11336 C  CD1    . LEU   D 2  151 ? -33.279 -0.277   -39.092 1.00 68.78  ? 151 LEU   D CD1    1 
ATOM   11337 C  CD2    . LEU   D 2  151 ? -30.894 -0.618   -38.419 1.00 73.59  ? 151 LEU   D CD2    1 
ATOM   11338 N  N      . ILE   D 2  152 ? -32.296 1.244    -34.203 1.00 68.71  ? 152 ILE   D N      1 
ATOM   11339 C  CA     . ILE   D 2  152 ? -32.103 0.718    -32.857 1.00 63.04  ? 152 ILE   D CA     1 
ATOM   11340 C  C      . ILE   D 2  152 ? -33.475 0.480    -32.239 1.00 61.87  ? 152 ILE   D C      1 
ATOM   11341 O  O      . ILE   D 2  152 ? -33.866 -0.671   -32.026 1.00 60.65  ? 152 ILE   D O      1 
ATOM   11342 C  CB     . ILE   D 2  152 ? -31.227 1.661    -32.007 1.00 59.97  ? 152 ILE   D CB     1 
ATOM   11343 C  CG1    . ILE   D 2  152 ? -29.779 1.581    -32.503 1.00 64.57  ? 152 ILE   D CG1    1 
ATOM   11344 C  CG2    . ILE   D 2  152 ? -31.330 1.340    -30.528 1.00 55.24  ? 152 ILE   D CG2    1 
ATOM   11345 C  CD1    . ILE   D 2  152 ? -28.841 2.685    -31.989 1.00 64.36  ? 152 ILE   D CD1    1 
ATOM   11346 N  N      . SER   D 2  153 ? -34.222 1.553    -31.959 1.00 62.02  ? 153 SER   D N      1 
ATOM   11347 C  CA     . SER   D 2  153 ? -35.538 1.396    -31.347 1.00 58.52  ? 153 SER   D CA     1 
ATOM   11348 C  C      . SER   D 2  153 ? -36.297 0.202    -31.913 1.00 62.10  ? 153 SER   D C      1 
ATOM   11349 O  O      . SER   D 2  153 ? -36.849 -0.604   -31.161 1.00 67.55  ? 153 SER   D O      1 
ATOM   11350 C  CB     . SER   D 2  153 ? -36.361 2.672    -31.514 1.00 63.25  ? 153 SER   D CB     1 
ATOM   11351 O  OG     . SER   D 2  153 ? -36.226 3.519    -30.388 1.00 67.82  ? 153 SER   D OG     1 
ATOM   11352 N  N      . LYS   D 2  154 ? -36.323 0.051    -33.236 1.00 61.33  ? 154 LYS   D N      1 
ATOM   11353 C  CA     . LYS   D 2  154 ? -37.154 -1.004   -33.810 1.00 61.88  ? 154 LYS   D CA     1 
ATOM   11354 C  C      . LYS   D 2  154 ? -36.549 -2.372   -33.551 1.00 61.09  ? 154 LYS   D C      1 
ATOM   11355 O  O      . LYS   D 2  154 ? -37.269 -3.343   -33.315 1.00 59.44  ? 154 LYS   D O      1 
ATOM   11356 C  CB     . LYS   D 2  154 ? -37.358 -0.782   -35.312 1.00 65.64  ? 154 LYS   D CB     1 
ATOM   11357 C  CG     . LYS   D 2  154 ? -38.202 0.444    -35.610 1.00 66.78  ? 154 LYS   D CG     1 
ATOM   11358 C  CD     . LYS   D 2  154 ? -39.671 0.204    -35.325 1.00 63.43  ? 154 LYS   D CD     1 
ATOM   11359 C  CE     . LYS   D 2  154 ? -40.436 1.525    -35.299 1.00 64.77  ? 154 LYS   D CE     1 
ATOM   11360 N  NZ     . LYS   D 2  154 ? -41.882 1.318    -34.993 1.00 73.14  ? 154 LYS   D NZ     1 
ATOM   11361 N  N      . ILE   D 2  155 ? -35.226 -2.470   -33.594 1.00 66.72  ? 155 ILE   D N      1 
ATOM   11362 C  CA     . ILE   D 2  155 ? -34.570 -3.746   -33.337 1.00 64.18  ? 155 ILE   D CA     1 
ATOM   11363 C  C      . ILE   D 2  155 ? -34.781 -4.161   -31.889 1.00 62.48  ? 155 ILE   D C      1 
ATOM   11364 O  O      . ILE   D 2  155 ? -35.086 -5.325   -31.598 1.00 57.42  ? 155 ILE   D O      1 
ATOM   11365 C  CB     . ILE   D 2  155 ? -33.078 -3.634   -33.679 1.00 62.23  ? 155 ILE   D CB     1 
ATOM   11366 C  CG1    . ILE   D 2  155 ? -32.945 -3.133   -35.117 1.00 65.73  ? 155 ILE   D CG1    1 
ATOM   11367 C  CG2    . ILE   D 2  155 ? -32.406 -4.986   -33.498 1.00 62.22  ? 155 ILE   D CG2    1 
ATOM   11368 C  CD1    . ILE   D 2  155 ? -31.526 -3.017   -35.627 1.00 74.18  ? 155 ILE   D CD1    1 
ATOM   11369 N  N      . ARG   D 2  156 ? -34.626 -3.201   -30.964 1.00 63.29  ? 156 ARG   D N      1 
ATOM   11370 C  CA     . ARG   D 2  156 ? -34.760 -3.472   -29.538 1.00 62.32  ? 156 ARG   D CA     1 
ATOM   11371 C  C      . ARG   D 2  156 ? -36.196 -3.855   -29.172 1.00 67.89  ? 156 ARG   D C      1 
ATOM   11372 O  O      . ARG   D 2  156 ? -36.419 -4.658   -28.256 1.00 66.02  ? 156 ARG   D O      1 
ATOM   11373 C  CB     . ARG   D 2  156 ? -34.279 -2.249   -28.743 1.00 63.31  ? 156 ARG   D CB     1 
ATOM   11374 C  CG     . ARG   D 2  156 ? -33.931 -2.517   -27.267 1.00 69.72  ? 156 ARG   D CG     1 
ATOM   11375 C  CD     . ARG   D 2  156 ? -33.222 -1.324   -26.606 1.00 63.49  ? 156 ARG   D CD     1 
ATOM   11376 N  NE     . ARG   D 2  156 ? -32.725 -1.637   -25.264 1.00 70.57  ? 156 ARG   D NE     1 
ATOM   11377 C  CZ     . ARG   D 2  156 ? -31.748 -2.504   -24.996 1.00 68.01  ? 156 ARG   D CZ     1 
ATOM   11378 N  NH1    . ARG   D 2  156 ? -31.185 -3.237   -25.947 1.00 62.17  ? 156 ARG   D NH1    1 
ATOM   11379 N  NH2    . ARG   D 2  156 ? -31.329 -2.647   -23.738 1.00 59.59  ? 156 ARG   D NH2    1 
ATOM   11380 N  N      . GLU   D 2  157 ? -37.186 -3.315   -29.884 1.00 69.27  ? 157 GLU   D N      1 
ATOM   11381 C  CA     . GLU   D 2  157 ? -38.566 -3.731   -29.647 1.00 67.83  ? 157 GLU   D CA     1 
ATOM   11382 C  C      . GLU   D 2  157 ? -38.753 -5.209   -29.986 1.00 64.99  ? 157 GLU   D C      1 
ATOM   11383 O  O      . GLU   D 2  157 ? -39.505 -5.919   -29.310 1.00 70.50  ? 157 GLU   D O      1 
ATOM   11384 C  CB     . GLU   D 2  157 ? -39.501 -2.828   -30.460 1.00 66.54  ? 157 GLU   D CB     1 
ATOM   11385 C  CG     . GLU   D 2  157 ? -40.964 -2.811   -30.063 1.00 68.94  ? 157 GLU   D CG     1 
ATOM   11386 C  CD     . GLU   D 2  157 ? -41.779 -1.796   -30.875 1.00 82.27  ? 157 GLU   D CD     1 
ATOM   11387 O  OE1    . GLU   D 2  157 ? -41.286 -1.313   -31.922 1.00 73.11  ? 157 GLU   D OE1    1 
ATOM   11388 O  OE2    . GLU   D 2  157 ? -42.910 -1.467   -30.447 1.00 81.04  ? 157 GLU   D OE2    1 
ATOM   11389 N  N      . GLU   D 2  158 ? -38.039 -5.696   -30.988 1.00 55.25  ? 158 GLU   D N      1 
ATOM   11390 C  CA     . GLU   D 2  158 ? -38.207 -7.053   -31.474 1.00 60.31  ? 158 GLU   D CA     1 
ATOM   11391 C  C      . GLU   D 2  158 ? -37.223 -8.040   -30.876 1.00 66.20  ? 158 GLU   D C      1 
ATOM   11392 O  O      . GLU   D 2  158 ? -37.471 -9.251   -30.931 1.00 64.70  ? 158 GLU   D O      1 
ATOM   11393 C  CB     . GLU   D 2  158 ? -38.072 -7.070   -32.996 1.00 66.45  ? 158 GLU   D CB     1 
ATOM   11394 C  CG     . GLU   D 2  158 ? -38.482 -8.361   -33.646 1.00 71.46  ? 158 GLU   D CG     1 
ATOM   11395 C  CD     . GLU   D 2  158 ? -38.723 -8.216   -35.133 1.00 69.38  ? 158 GLU   D CD     1 
ATOM   11396 O  OE1    . GLU   D 2  158 ? -39.118 -7.104   -35.562 1.00 62.56  ? 158 GLU   D OE1    1 
ATOM   11397 O  OE2    . GLU   D 2  158 ? -38.495 -9.210   -35.864 1.00 70.25  ? 158 GLU   D OE2    1 
ATOM   11398 N  N      . TYR   D 2  159 ? -36.110 -7.560   -30.332 1.00 64.46  ? 159 TYR   D N      1 
ATOM   11399 C  CA     . TYR   D 2  159 ? -35.120 -8.406   -29.672 1.00 56.00  ? 159 TYR   D CA     1 
ATOM   11400 C  C      . TYR   D 2  159 ? -34.759 -7.794   -28.333 1.00 56.06  ? 159 TYR   D C      1 
ATOM   11401 O  O      . TYR   D 2  159 ? -33.587 -7.530   -28.057 1.00 64.26  ? 159 TYR   D O      1 
ATOM   11402 C  CB     . TYR   D 2  159 ? -33.873 -8.566   -30.534 1.00 56.82  ? 159 TYR   D CB     1 
ATOM   11403 C  CG     . TYR   D 2  159 ? -34.107 -9.113   -31.915 1.00 61.42  ? 159 TYR   D CG     1 
ATOM   11404 C  CD1    . TYR   D 2  159 ? -34.467 -8.274   -32.960 1.00 66.13  ? 159 TYR   D CD1    1 
ATOM   11405 C  CD2    . TYR   D 2  159 ? -33.915 -10.462  -32.188 1.00 53.00  ? 159 TYR   D CD2    1 
ATOM   11406 C  CE1    . TYR   D 2  159 ? -34.664 -8.769   -34.241 1.00 65.48  ? 159 TYR   D CE1    1 
ATOM   11407 C  CE2    . TYR   D 2  159 ? -34.108 -10.967  -33.453 1.00 58.84  ? 159 TYR   D CE2    1 
ATOM   11408 C  CZ     . TYR   D 2  159 ? -34.484 -10.113  -34.486 1.00 64.76  ? 159 TYR   D CZ     1 
ATOM   11409 O  OH     . TYR   D 2  159 ? -34.674 -10.590  -35.762 1.00 55.49  ? 159 TYR   D OH     1 
ATOM   11410 N  N      . PRO   D 2  160 ? -35.737 -7.558   -27.472 1.00 53.72  ? 160 PRO   D N      1 
ATOM   11411 C  CA     . PRO   D 2  160 ? -35.482 -6.741   -26.278 1.00 61.45  ? 160 PRO   D CA     1 
ATOM   11412 C  C      . PRO   D 2  160 ? -34.515 -7.393   -25.304 1.00 57.83  ? 160 PRO   D C      1 
ATOM   11413 O  O      . PRO   D 2  160 ? -34.195 -6.823   -24.259 1.00 60.31  ? 160 PRO   D O      1 
ATOM   11414 C  CB     . PRO   D 2  160 ? -36.877 -6.582   -25.661 1.00 54.13  ? 160 PRO   D CB     1 
ATOM   11415 C  CG     . PRO   D 2  160 ? -37.596 -7.761   -26.113 1.00 59.34  ? 160 PRO   D CG     1 
ATOM   11416 C  CD     . PRO   D 2  160 ? -37.122 -8.031   -27.510 1.00 61.67  ? 160 PRO   D CD     1 
ATOM   11417 N  N      . ASP   D 2  161 ? -34.042 -8.587   -25.654 1.00 57.10  ? 161 ASP   D N      1 
ATOM   11418 C  CA     . ASP   D 2  161 ? -33.180 -9.402   -24.811 1.00 56.28  ? 161 ASP   D CA     1 
ATOM   11419 C  C      . ASP   D 2  161 ? -31.905 -9.803   -25.559 1.00 50.93  ? 161 ASP   D C      1 
ATOM   11420 O  O      . ASP   D 2  161 ? -31.367 -10.895  -25.368 1.00 50.45  ? 161 ASP   D O      1 
ATOM   11421 C  CB     . ASP   D 2  161 ? -33.954 -10.619  -24.314 1.00 53.58  ? 161 ASP   D CB     1 
ATOM   11422 C  CG     . ASP   D 2  161 ? -34.410 -11.528  -25.447 1.00 58.99  ? 161 ASP   D CG     1 
ATOM   11423 O  OD1    . ASP   D 2  161 ? -34.606 -11.052  -26.587 1.00 61.74  ? 161 ASP   D OD1    1 
ATOM   11424 O  OD2    . ASP   D 2  161 ? -34.591 -12.733  -25.196 1.00 67.62  ? 161 ASP   D OD2    1 
ATOM   11425 N  N      . ARG   D 2  162 ? -31.432 -8.922   -26.429 1.00 47.90  ? 162 ARG   D N      1 
ATOM   11426 C  CA     . ARG   D 2  162 ? -30.192 -9.075   -27.166 1.00 51.66  ? 162 ARG   D CA     1 
ATOM   11427 C  C      . ARG   D 2  162 ? -29.390 -7.797   -26.967 1.00 54.60  ? 162 ARG   D C      1 
ATOM   11428 O  O      . ARG   D 2  162 ? -29.942 -6.744   -26.640 1.00 58.25  ? 162 ARG   D O      1 
ATOM   11429 C  CB     . ARG   D 2  162 ? -30.450 -9.330   -28.661 1.00 54.72  ? 162 ARG   D CB     1 
ATOM   11430 C  CG     . ARG   D 2  162 ? -31.270 -10.584  -29.019 1.00 55.21  ? 162 ARG   D CG     1 
ATOM   11431 C  CD     . ARG   D 2  162 ? -30.742 -11.833  -28.357 1.00 59.77  ? 162 ARG   D CD     1 
ATOM   11432 N  NE     . ARG   D 2  162 ? -31.281 -13.052  -28.954 1.00 64.20  ? 162 ARG   D NE     1 
ATOM   11433 C  CZ     . ARG   D 2  162 ? -31.137 -14.269  -28.439 1.00 70.81  ? 162 ARG   D CZ     1 
ATOM   11434 N  NH1    . ARG   D 2  162 ? -30.465 -14.473  -27.314 1.00 76.92  ? 162 ARG   D NH1    1 
ATOM   11435 N  NH2    . ARG   D 2  162 ? -31.674 -15.308  -29.070 1.00 66.96  ? 162 ARG   D NH2    1 
ATOM   11436 N  N      . ILE   D 2  163 ? -28.085 -7.881   -27.135 1.00 50.64  ? 163 ILE   D N      1 
ATOM   11437 C  CA     . ILE   D 2  163 ? -27.265 -6.724   -26.796 1.00 52.69  ? 163 ILE   D CA     1 
ATOM   11438 C  C      . ILE   D 2  163 ? -27.260 -5.756   -27.962 1.00 51.04  ? 163 ILE   D C      1 
ATOM   11439 O  O      . ILE   D 2  163 ? -27.149 -6.167   -29.120 1.00 59.73  ? 163 ILE   D O      1 
ATOM   11440 C  CB     . ILE   D 2  163 ? -25.840 -7.149   -26.395 1.00 53.45  ? 163 ILE   D CB     1 
ATOM   11441 C  CG1    . ILE   D 2  163 ? -25.930 -8.051   -25.165 1.00 45.37  ? 163 ILE   D CG1    1 
ATOM   11442 C  CG2    . ILE   D 2  163 ? -24.949 -5.932   -26.158 1.00 49.96  ? 163 ILE   D CG2    1 
ATOM   11443 C  CD1    . ILE   D 2  163 ? -26.200 -7.278   -23.929 1.00 41.82  ? 163 ILE   D CD1    1 
ATOM   11444 N  N      . MET   D 2  164 ? -27.389 -4.466   -27.667 1.00 53.24  ? 164 MET   D N      1 
ATOM   11445 C  CA     . MET   D 2  164 ? -27.351 -3.419   -28.686 1.00 55.96  ? 164 MET   D CA     1 
ATOM   11446 C  C      . MET   D 2  164 ? -26.056 -2.627   -28.507 1.00 52.87  ? 164 MET   D C      1 
ATOM   11447 O  O      . MET   D 2  164 ? -25.945 -1.798   -27.601 1.00 53.31  ? 164 MET   D O      1 
ATOM   11448 C  CB     . MET   D 2  164 ? -28.576 -2.506   -28.596 1.00 57.20  ? 164 MET   D CB     1 
ATOM   11449 C  CG     . MET   D 2  164 ? -28.687 -1.513   -29.739 1.00 56.83  ? 164 MET   D CG     1 
ATOM   11450 S  SD     . MET   D 2  164 ? -28.693 -2.354   -31.319 1.00 69.92  ? 164 MET   D SD     1 
ATOM   11451 C  CE     . MET   D 2  164 ? -30.276 -3.185   -31.222 1.00 63.00  ? 164 MET   D CE     1 
ATOM   11452 N  N      . ASN   D 2  165 ? -25.093 -2.871   -29.384 1.00 53.24  ? 165 ASN   D N      1 
ATOM   11453 C  CA     . ASN   D 2  165 ? -23.782 -2.237   -29.360 1.00 55.93  ? 165 ASN   D CA     1 
ATOM   11454 C  C      . ASN   D 2  165 ? -23.657 -1.260   -30.532 1.00 59.07  ? 165 ASN   D C      1 
ATOM   11455 O  O      . ASN   D 2  165 ? -23.981 -1.612   -31.671 1.00 59.44  ? 165 ASN   D O      1 
ATOM   11456 C  CB     . ASN   D 2  165 ? -22.706 -3.323   -29.435 1.00 54.61  ? 165 ASN   D CB     1 
ATOM   11457 C  CG     . ASN   D 2  165 ? -21.302 -2.768   -29.414 1.00 62.81  ? 165 ASN   D CG     1 
ATOM   11458 O  OD1    . ASN   D 2  165 ? -20.908 -2.069   -28.478 1.00 61.95  ? 165 ASN   D OD1    1 
ATOM   11459 N  ND2    . ASN   D 2  165 ? -20.524 -3.093   -30.445 1.00 65.36  ? 165 ASN   D ND2    1 
ATOM   11460 N  N      . THR   D 2  166 ? -23.205 -0.032   -30.269 1.00 54.03  ? 166 THR   D N      1 
ATOM   11461 C  CA     . THR   D 2  166 ? -23.019 0.927    -31.352 1.00 55.25  ? 166 THR   D CA     1 
ATOM   11462 C  C      . THR   D 2  166 ? -21.630 1.538    -31.289 1.00 59.03  ? 166 THR   D C      1 
ATOM   11463 O  O      . THR   D 2  166 ? -21.047 1.669    -30.214 1.00 62.11  ? 166 THR   D O      1 
ATOM   11464 C  CB     . THR   D 2  166 ? -24.031 2.089    -31.346 1.00 55.61  ? 166 THR   D CB     1 
ATOM   11465 O  OG1    . THR   D 2  166 ? -23.672 3.052    -30.345 1.00 56.98  ? 166 THR   D OG1    1 
ATOM   11466 C  CG2    . THR   D 2  166 ? -25.434 1.573    -31.073 1.00 58.74  ? 166 THR   D CG2    1 
ATOM   11467 N  N      . PHE   D 2  167 ? -21.119 1.914    -32.473 1.00 63.96  ? 167 PHE   D N      1 
ATOM   11468 C  CA     . PHE   D 2  167 ? -19.947 2.775    -32.663 1.00 57.54  ? 167 PHE   D CA     1 
ATOM   11469 C  C      . PHE   D 2  167 ? -20.465 4.104    -33.209 1.00 59.22  ? 167 PHE   D C      1 
ATOM   11470 O  O      . PHE   D 2  167 ? -20.741 4.227    -34.402 1.00 58.90  ? 167 PHE   D O      1 
ATOM   11471 C  CB     . PHE   D 2  167 ? -18.967 2.140    -33.630 1.00 48.92  ? 167 PHE   D CB     1 
ATOM   11472 C  CG     . PHE   D 2  167 ? -18.379 0.864    -33.138 1.00 57.15  ? 167 PHE   D CG     1 
ATOM   11473 C  CD1    . PHE   D 2  167 ? -19.069 -0.331   -33.298 1.00 60.43  ? 167 PHE   D CD1    1 
ATOM   11474 C  CD2    . PHE   D 2  167 ? -17.117 0.836    -32.571 1.00 55.11  ? 167 PHE   D CD2    1 
ATOM   11475 C  CE1    . PHE   D 2  167 ? -18.534 -1.530   -32.870 1.00 56.40  ? 167 PHE   D CE1    1 
ATOM   11476 C  CE2    . PHE   D 2  167 ? -16.571 -0.358   -32.145 1.00 55.66  ? 167 PHE   D CE2    1 
ATOM   11477 C  CZ     . PHE   D 2  167 ? -17.282 -1.544   -32.297 1.00 58.57  ? 167 PHE   D CZ     1 
ATOM   11478 N  N      . SER   D 2  168 ? -20.633 5.087    -32.344 1.00 56.25  ? 168 SER   D N      1 
ATOM   11479 C  CA     . SER   D 2  168 ? -21.180 6.368    -32.751 1.00 59.38  ? 168 SER   D CA     1 
ATOM   11480 C  C      . SER   D 2  168 ? -20.029 7.352    -32.944 1.00 64.86  ? 168 SER   D C      1 
ATOM   11481 O  O      . SER   D 2  168 ? -19.170 7.483    -32.067 1.00 65.93  ? 168 SER   D O      1 
ATOM   11482 C  CB     . SER   D 2  168 ? -22.178 6.884    -31.706 1.00 65.16  ? 168 SER   D CB     1 
ATOM   11483 O  OG     . SER   D 2  168 ? -23.230 5.954    -31.463 1.00 61.56  ? 168 SER   D OG     1 
ATOM   11484 N  N      . VAL   D 2  169 ? -20.014 8.043    -34.088 1.00 67.87  ? 169 VAL   D N      1 
ATOM   11485 C  CA     . VAL   D 2  169 ? -18.996 9.045    -34.405 1.00 65.85  ? 169 VAL   D CA     1 
ATOM   11486 C  C      . VAL   D 2  169 ? -19.561 10.446   -34.182 1.00 67.34  ? 169 VAL   D C      1 
ATOM   11487 O  O      . VAL   D 2  169 ? -20.554 10.827   -34.814 1.00 68.42  ? 169 VAL   D O      1 
ATOM   11488 C  CB     . VAL   D 2  169 ? -18.493 8.885    -35.842 1.00 56.61  ? 169 VAL   D CB     1 
ATOM   11489 C  CG1    . VAL   D 2  169 ? -17.436 9.905    -36.102 1.00 63.24  ? 169 VAL   D CG1    1 
ATOM   11490 C  CG2    . VAL   D 2  169 ? -17.937 7.505    -36.030 1.00 54.93  ? 169 VAL   D CG2    1 
ATOM   11491 N  N      . MET   D 2  170 ? -18.893 11.236   -33.312 1.00 67.24  ? 170 MET   D N      1 
ATOM   11492 C  CA     . MET   D 2  170 ? -19.374 12.516   -32.793 1.00 72.94  ? 170 MET   D CA     1 
ATOM   11493 C  C      . MET   D 2  170 ? -18.909 13.678   -33.663 1.00 83.80  ? 170 MET   D C      1 
ATOM   11494 O  O      . MET   D 2  170 ? -17.760 13.692   -34.125 1.00 81.44  ? 170 MET   D O      1 
ATOM   11495 C  CB     . MET   D 2  170 ? -18.881 12.761   -31.376 1.00 74.41  ? 170 MET   D CB     1 
ATOM   11496 C  CG     . MET   D 2  170 ? -18.698 11.513   -30.557 1.00 79.45  ? 170 MET   D CG     1 
ATOM   11497 S  SD     . MET   D 2  170 ? -20.226 10.607   -30.272 1.00 94.85  ? 170 MET   D SD     1 
ATOM   11498 C  CE     . MET   D 2  170 ? -20.972 11.614   -28.978 1.00 76.16  ? 170 MET   D CE     1 
ATOM   11499 N  N      . PRO   D 2  171 ? -19.802 14.657   -33.810 1.00 85.74  ? 171 PRO   D N      1 
ATOM   11500 C  CA     . PRO   D 2  171 ? -19.499 15.840   -34.630 1.00 85.72  ? 171 PRO   D CA     1 
ATOM   11501 C  C      . PRO   D 2  171 ? -18.506 16.812   -33.991 1.00 88.24  ? 171 PRO   D C      1 
ATOM   11502 O  O      . PRO   D 2  171 ? -18.628 17.192   -32.823 1.00 88.73  ? 171 PRO   D O      1 
ATOM   11503 C  CB     . PRO   D 2  171 ? -20.873 16.494   -34.802 1.00 88.25  ? 171 PRO   D CB     1 
ATOM   11504 C  CG     . PRO   D 2  171 ? -21.641 16.083   -33.578 1.00 84.58  ? 171 PRO   D CG     1 
ATOM   11505 C  CD     . PRO   D 2  171 ? -21.170 14.684   -33.263 1.00 78.53  ? 171 PRO   D CD     1 
ATOM   11506 N  N      . SER   D 2  172 ? -17.548 17.261   -34.806 1.00 93.12  ? 172 SER   D N      1 
ATOM   11507 C  CA     . SER   D 2  172 ? -16.511 18.207   -34.385 1.00 90.82  ? 172 SER   D CA     1 
ATOM   11508 C  C      . SER   D 2  172 ? -16.402 19.364   -35.377 1.00 86.19  ? 172 SER   D C      1 
ATOM   11509 O  O      . SER   D 2  172 ? -16.111 19.130   -36.571 1.00 81.28  ? 172 SER   D O      1 
ATOM   11510 C  CB     . SER   D 2  172 ? -15.176 17.474   -34.250 1.00 79.10  ? 172 SER   D CB     1 
ATOM   11511 O  OG     . SER   D 2  172 ? -14.202 18.324   -33.690 1.00 78.29  ? 172 SER   D OG     1 
ATOM   11512 N  N      . PRO   D 2  173 ? -16.620 20.630   -34.950 1.00 79.83  ? 173 PRO   D N      1 
ATOM   11513 C  CA     . PRO   D 2  173 ? -16.439 21.754   -35.879 1.00 76.68  ? 173 PRO   D CA     1 
ATOM   11514 C  C      . PRO   D 2  173 ? -15.068 21.756   -36.541 1.00 79.05  ? 173 PRO   D C      1 
ATOM   11515 O  O      . PRO   D 2  173 ? -14.859 22.437   -37.552 1.00 85.23  ? 173 PRO   D O      1 
ATOM   11516 C  CB     . PRO   D 2  173 ? -16.663 22.985   -34.990 1.00 65.63  ? 173 PRO   D CB     1 
ATOM   11517 C  CG     . PRO   D 2  173 ? -17.550 22.517   -33.924 1.00 66.80  ? 173 PRO   D CG     1 
ATOM   11518 C  CD     . PRO   D 2  173 ? -17.192 21.072   -33.667 1.00 77.07  ? 173 PRO   D CD     1 
ATOM   11519 N  N      . LYS   D 2  174 ? -14.136 20.982   -36.001 1.00 72.62  ? 174 LYS   D N      1 
ATOM   11520 C  CA     . LYS   D 2  174 ? -12.854 20.764   -36.651 1.00 77.40  ? 174 LYS   D CA     1 
ATOM   11521 C  C      . LYS   D 2  174 ? -12.932 19.783   -37.804 1.00 77.94  ? 174 LYS   D C      1 
ATOM   11522 O  O      . LYS   D 2  174 ? -11.871 19.350   -38.259 1.00 81.58  ? 174 LYS   D O      1 
ATOM   11523 C  CB     . LYS   D 2  174 ? -11.823 20.232   -35.647 1.00 85.54  ? 174 LYS   D CB     1 
ATOM   11524 C  CG     . LYS   D 2  174 ? -11.707 21.032   -34.371 1.00 85.02  ? 174 LYS   D CG     1 
ATOM   11525 C  CD     . LYS   D 2  174 ? -10.512 20.592   -33.524 1.00 81.14  ? 174 LYS   D CD     1 
ATOM   11526 C  CE     . LYS   D 2  174 ? -10.723 21.051   -32.078 1.00 78.07  ? 174 LYS   D CE     1 
ATOM   11527 N  NZ     . LYS   D 2  174 ? -9.532  20.982   -31.196 1.00 74.36  ? 174 LYS   D NZ     1 
ATOM   11528 N  N      . VAL   D 2  175 ? -14.127 19.382   -38.257 1.00 77.98  ? 175 VAL   D N      1 
ATOM   11529 C  CA     . VAL   D 2  175 ? -14.233 18.391   -39.336 1.00 83.48  ? 175 VAL   D CA     1 
ATOM   11530 C  C      . VAL   D 2  175 ? -15.466 18.582   -40.222 1.00 83.68  ? 175 VAL   D C      1 
ATOM   11531 O  O      . VAL   D 2  175 ? -15.456 18.188   -41.396 1.00 84.98  ? 175 VAL   D O      1 
ATOM   11532 C  CB     . VAL   D 2  175 ? -14.187 16.947   -38.789 1.00 75.71  ? 175 VAL   D CB     1 
ATOM   11533 C  CG1    . VAL   D 2  175 ? -14.433 15.967   -39.896 1.00 75.41  ? 175 VAL   D CG1    1 
ATOM   11534 C  CG2    . VAL   D 2  175 ? -12.817 16.640   -38.218 1.00 77.90  ? 175 VAL   D CG2    1 
ATOM   11535 N  N      . SER   D 2  176 ? -16.536 19.171   -39.692 1.00 77.65  ? 176 SER   D N      1 
ATOM   11536 C  CA     . SER   D 2  176 ? -17.662 19.498   -40.552 1.00 81.94  ? 176 SER   D CA     1 
ATOM   11537 C  C      . SER   D 2  176 ? -18.210 20.859   -40.175 1.00 86.91  ? 176 SER   D C      1 
ATOM   11538 O  O      . SER   D 2  176 ? -18.349 21.185   -38.993 1.00 79.92  ? 176 SER   D O      1 
ATOM   11539 C  CB     . SER   D 2  176 ? -18.795 18.469   -40.492 1.00 78.65  ? 176 SER   D CB     1 
ATOM   11540 O  OG     . SER   D 2  176 ? -19.904 18.914   -41.265 1.00 80.28  ? 176 SER   D OG     1 
ATOM   11541 N  N      . ASP   D 2  177 ? -18.521 21.640   -41.201 1.00 90.49  ? 177 ASP   D N      1 
ATOM   11542 C  CA     . ASP   D 2  177 ? -18.995 22.996   -41.023 1.00 89.70  ? 177 ASP   D CA     1 
ATOM   11543 C  C      . ASP   D 2  177 ? -20.505 23.054   -40.860 1.00 93.46  ? 177 ASP   D C      1 
ATOM   11544 O  O      . ASP   D 2  177 ? -21.025 24.060   -40.354 1.00 97.16  ? 177 ASP   D O      1 
ATOM   11545 C  CB     . ASP   D 2  177 ? -18.541 23.834   -42.218 1.00 97.57  ? 177 ASP   D CB     1 
ATOM   11546 C  CG     . ASP   D 2  177 ? -17.042 23.710   -42.469 1.00 109.94 ? 177 ASP   D CG     1 
ATOM   11547 O  OD1    . ASP   D 2  177 ? -16.610 22.633   -42.958 1.00 103.20 ? 177 ASP   D OD1    1 
ATOM   11548 O  OD2    . ASP   D 2  177 ? -16.304 24.683   -42.191 1.00 113.10 ? 177 ASP   D OD2    1 
ATOM   11549 N  N      . THR   D 2  178 ? -21.210 21.981   -41.233 1.00 82.96  ? 178 THR   D N      1 
ATOM   11550 C  CA     . THR   D 2  178 ? -22.667 21.996   -41.308 1.00 87.52  ? 178 THR   D CA     1 
ATOM   11551 C  C      . THR   D 2  178 ? -23.294 22.325   -39.960 1.00 87.01  ? 178 THR   D C      1 
ATOM   11552 O  O      . THR   D 2  178 ? -23.367 21.480   -39.067 1.00 87.88  ? 178 THR   D O      1 
ATOM   11553 C  CB     . THR   D 2  178 ? -23.177 20.664   -41.883 1.00 85.63  ? 178 THR   D CB     1 
ATOM   11554 O  OG1    . THR   D 2  178 ? -22.682 19.570   -41.115 1.00 83.66  ? 178 THR   D OG1    1 
ATOM   11555 C  CG2    . THR   D 2  178 ? -22.732 20.491   -43.322 1.00 91.63  ? 178 THR   D CG2    1 
ATOM   11556 N  N      . VAL   D 2  179 ? -23.762 23.567   -39.827 1.00 90.97  ? 179 VAL   D N      1 
ATOM   11557 C  CA     . VAL   D 2  179 ? -24.131 24.138   -38.533 1.00 93.00  ? 179 VAL   D CA     1 
ATOM   11558 C  C      . VAL   D 2  179 ? -24.966 23.188   -37.681 1.00 90.90  ? 179 VAL   D C      1 
ATOM   11559 O  O      . VAL   D 2  179 ? -24.868 23.210   -36.448 1.00 90.50  ? 179 VAL   D O      1 
ATOM   11560 C  CB     . VAL   D 2  179 ? -24.863 25.479   -38.758 1.00 96.00  ? 179 VAL   D CB     1 
ATOM   11561 C  CG1    . VAL   D 2  179 ? -25.979 25.302   -39.786 1.00 100.53 ? 179 VAL   D CG1    1 
ATOM   11562 C  CG2    . VAL   D 2  179 ? -25.422 26.037   -37.437 1.00 93.63  ? 179 VAL   D CG2    1 
ATOM   11563 N  N      . VAL   D 2  180 ? -25.788 22.339   -38.302 1.00 92.14  ? 180 VAL   D N      1 
ATOM   11564 C  CA     . VAL   D 2  180 ? -26.851 21.648   -37.567 1.00 94.09  ? 180 VAL   D CA     1 
ATOM   11565 C  C      . VAL   D 2  180 ? -26.404 20.322   -36.944 1.00 89.13  ? 180 VAL   D C      1 
ATOM   11566 O  O      . VAL   D 2  180 ? -27.241 19.470   -36.620 1.00 87.96  ? 180 VAL   D O      1 
ATOM   11567 C  CB     . VAL   D 2  180 ? -28.080 21.426   -38.476 1.00 85.25  ? 180 VAL   D CB     1 
ATOM   11568 C  CG1    . VAL   D 2  180 ? -28.802 22.737   -38.722 1.00 92.00  ? 180 VAL   D CG1    1 
ATOM   11569 C  CG2    . VAL   D 2  180 ? -27.654 20.814   -39.784 1.00 80.10  ? 180 VAL   D CG2    1 
ATOM   11570 N  N      . GLU   D 2  181 ? -25.097 20.137   -36.738 1.00 80.21  ? 181 GLU   D N      1 
ATOM   11571 C  CA     . GLU   D 2  181 ? -24.655 18.888   -36.127 1.00 78.44  ? 181 GLU   D CA     1 
ATOM   11572 C  C      . GLU   D 2  181 ? -24.834 18.832   -34.613 1.00 84.13  ? 181 GLU   D C      1 
ATOM   11573 O  O      . GLU   D 2  181 ? -25.219 17.780   -34.088 1.00 83.70  ? 181 GLU   D O      1 
ATOM   11574 C  CB     . GLU   D 2  181 ? -23.213 18.590   -36.523 1.00 75.18  ? 181 GLU   D CB     1 
ATOM   11575 C  CG     . GLU   D 2  181 ? -23.100 18.283   -37.983 1.00 75.15  ? 181 GLU   D CG     1 
ATOM   11576 C  CD     . GLU   D 2  181 ? -21.759 17.709   -38.387 1.00 74.20  ? 181 GLU   D CD     1 
ATOM   11577 O  OE1    . GLU   D 2  181 ? -20.739 17.967   -37.722 1.00 72.12  ? 181 GLU   D OE1    1 
ATOM   11578 O  OE2    . GLU   D 2  181 ? -21.760 16.869   -39.310 1.00 80.62  ? 181 GLU   D OE2    1 
ATOM   11579 N  N      . PRO   D 2  182 ? -24.591 19.908   -33.869 1.00 83.83  ? 182 PRO   D N      1 
ATOM   11580 C  CA     . PRO   D 2  182 ? -24.953 19.881   -32.440 1.00 81.06  ? 182 PRO   D CA     1 
ATOM   11581 C  C      . PRO   D 2  182 ? -26.422 19.537   -32.199 1.00 79.37  ? 182 PRO   D C      1 
ATOM   11582 O  O      . PRO   D 2  182 ? -26.770 19.094   -31.098 1.00 78.06  ? 182 PRO   D O      1 
ATOM   11583 C  CB     . PRO   D 2  182 ? -24.610 21.301   -31.960 1.00 78.91  ? 182 PRO   D CB     1 
ATOM   11584 C  CG     . PRO   D 2  182 ? -23.510 21.724   -32.884 1.00 83.31  ? 182 PRO   D CG     1 
ATOM   11585 C  CD     . PRO   D 2  182 ? -23.867 21.135   -34.230 1.00 81.42  ? 182 PRO   D CD     1 
ATOM   11586 N  N      . TYR   D 2  183 ? -27.294 19.737   -33.189 1.00 80.37  ? 183 TYR   D N      1 
ATOM   11587 C  CA     . TYR   D 2  183 ? -28.680 19.295   -33.068 1.00 79.71  ? 183 TYR   D CA     1 
ATOM   11588 C  C      . TYR   D 2  183 ? -28.803 17.792   -33.264 1.00 76.54  ? 183 TYR   D C      1 
ATOM   11589 O  O      . TYR   D 2  183 ? -29.434 17.098   -32.459 1.00 71.57  ? 183 TYR   D O      1 
ATOM   11590 C  CB     . TYR   D 2  183 ? -29.549 20.041   -34.080 1.00 77.95  ? 183 TYR   D CB     1 
ATOM   11591 C  CG     . TYR   D 2  183 ? -29.979 21.408   -33.634 1.00 78.27  ? 183 TYR   D CG     1 
ATOM   11592 C  CD1    . TYR   D 2  183 ? -30.174 21.690   -32.291 1.00 81.10  ? 183 TYR   D CD1    1 
ATOM   11593 C  CD2    . TYR   D 2  183 ? -30.104 22.445   -34.547 1.00 85.86  ? 183 TYR   D CD2    1 
ATOM   11594 C  CE1    . TYR   D 2  183 ? -30.563 22.953   -31.870 1.00 85.72  ? 183 TYR   D CE1    1 
ATOM   11595 C  CE2    . TYR   D 2  183 ? -30.472 23.718   -34.138 1.00 90.96  ? 183 TYR   D CE2    1 
ATOM   11596 C  CZ     . TYR   D 2  183 ? -30.698 23.964   -32.798 1.00 91.10  ? 183 TYR   D CZ     1 
ATOM   11597 O  OH     . TYR   D 2  183 ? -31.061 25.219   -32.384 1.00 87.79  ? 183 TYR   D OH     1 
ATOM   11598 N  N      . ASN   D 2  184 ? -28.209 17.275   -34.335 1.00 80.82  ? 184 ASN   D N      1 
ATOM   11599 C  CA     . ASN   D 2  184 ? -28.354 15.864   -34.659 1.00 79.08  ? 184 ASN   D CA     1 
ATOM   11600 C  C      . ASN   D 2  184 ? -27.869 14.996   -33.510 1.00 73.06  ? 184 ASN   D C      1 
ATOM   11601 O  O      . ASN   D 2  184 ? -28.643 14.231   -32.922 1.00 71.18  ? 184 ASN   D O      1 
ATOM   11602 C  CB     . ASN   D 2  184 ? -27.588 15.534   -35.944 1.00 85.44  ? 184 ASN   D CB     1 
ATOM   11603 C  CG     . ASN   D 2  184 ? -28.174 16.206   -37.183 1.00 78.98  ? 184 ASN   D CG     1 
ATOM   11604 O  OD1    . ASN   D 2  184 ? -29.236 16.826   -37.135 1.00 76.69  ? 184 ASN   D OD1    1 
ATOM   11605 N  ND2    . ASN   D 2  184 ? -27.492 16.046   -38.306 1.00 75.72  ? 184 ASN   D ND2    1 
ATOM   11606 N  N      . ALA   D 2  185 ? -26.581 15.110   -33.173 1.00 73.40  ? 185 ALA   D N      1 
ATOM   11607 C  CA     . ALA   D 2  185 ? -26.018 14.327   -32.077 1.00 69.26  ? 185 ALA   D CA     1 
ATOM   11608 C  C      . ALA   D 2  185 ? -26.905 14.397   -30.829 1.00 67.05  ? 185 ALA   D C      1 
ATOM   11609 O  O      . ALA   D 2  185 ? -27.459 13.383   -30.397 1.00 71.50  ? 185 ALA   D O      1 
ATOM   11610 C  CB     . ALA   D 2  185 ? -24.588 14.790   -31.784 1.00 57.27  ? 185 ALA   D CB     1 
ATOM   11611 N  N      . THR   D 2  186 ? -27.095 15.592   -30.256 1.00 57.85  ? 186 THR   D N      1 
ATOM   11612 C  CA     . THR   D 2  186 ? -27.885 15.685   -29.027 1.00 61.29  ? 186 THR   D CA     1 
ATOM   11613 C  C      . THR   D 2  186 ? -29.246 15.008   -29.140 1.00 69.20  ? 186 THR   D C      1 
ATOM   11614 O  O      . THR   D 2  186 ? -29.832 14.621   -28.122 1.00 69.84  ? 186 THR   D O      1 
ATOM   11615 C  CB     . THR   D 2  186 ? -28.082 17.139   -28.602 1.00 59.97  ? 186 THR   D CB     1 
ATOM   11616 O  OG1    . THR   D 2  186 ? -26.804 17.752   -28.407 1.00 64.28  ? 186 THR   D OG1    1 
ATOM   11617 C  CG2    . THR   D 2  186 ? -28.900 17.214   -27.304 1.00 55.66  ? 186 THR   D CG2    1 
ATOM   11618 N  N      . LEU   D 2  187 ? -29.786 14.878   -30.351 1.00 74.04  ? 187 LEU   D N      1 
ATOM   11619 C  CA     . LEU   D 2  187 ? -31.009 14.099   -30.494 1.00 75.74  ? 187 LEU   D CA     1 
ATOM   11620 C  C      . LEU   D 2  187 ? -30.693 12.611   -30.571 1.00 68.82  ? 187 LEU   D C      1 
ATOM   11621 O  O      . LEU   D 2  187 ? -31.421 11.792   -29.997 1.00 66.93  ? 187 LEU   D O      1 
ATOM   11622 C  CB     . LEU   D 2  187 ? -31.814 14.561   -31.724 1.00 77.60  ? 187 LEU   D CB     1 
ATOM   11623 C  CG     . LEU   D 2  187 ? -32.383 15.992   -31.793 1.00 68.83  ? 187 LEU   D CG     1 
ATOM   11624 C  CD1    . LEU   D 2  187 ? -32.932 16.269   -33.168 1.00 74.46  ? 187 LEU   D CD1    1 
ATOM   11625 C  CD2    . LEU   D 2  187 ? -33.435 16.280   -30.733 1.00 67.54  ? 187 LEU   D CD2    1 
ATOM   11626 N  N      . SER   D 2  188 ? -29.607 12.256   -31.266 1.00 68.27  ? 188 SER   D N      1 
ATOM   11627 C  CA     . SER   D 2  188 ? -29.139 10.874   -31.280 1.00 70.97  ? 188 SER   D CA     1 
ATOM   11628 C  C      . SER   D 2  188 ? -28.909 10.359   -29.865 1.00 71.66  ? 188 SER   D C      1 
ATOM   11629 O  O      . SER   D 2  188 ? -29.332 9.248    -29.527 1.00 73.11  ? 188 SER   D O      1 
ATOM   11630 C  CB     . SER   D 2  188 ? -27.841 10.767   -32.086 1.00 70.39  ? 188 SER   D CB     1 
ATOM   11631 O  OG     . SER   D 2  188 ? -27.998 11.240   -33.408 1.00 71.84  ? 188 SER   D OG     1 
ATOM   11632 N  N      . VAL   D 2  189 ? -28.238 11.156   -29.024 1.00 70.41  ? 189 VAL   D N      1 
ATOM   11633 C  CA     . VAL   D 2  189 ? -27.825 10.692   -27.702 1.00 63.40  ? 189 VAL   D CA     1 
ATOM   11634 C  C      . VAL   D 2  189 ? -29.042 10.388   -26.838 1.00 64.06  ? 189 VAL   D C      1 
ATOM   11635 O  O      . VAL   D 2  189 ? -29.198 9.268    -26.340 1.00 67.67  ? 189 VAL   D O      1 
ATOM   11636 C  CB     . VAL   D 2  189 ? -26.899 11.724   -27.040 1.00 64.51  ? 189 VAL   D CB     1 
ATOM   11637 C  CG1    . VAL   D 2  189 ? -26.817 11.480   -25.546 1.00 59.07  ? 189 VAL   D CG1    1 
ATOM   11638 C  CG2    . VAL   D 2  189 ? -25.512 11.679   -27.693 1.00 62.97  ? 189 VAL   D CG2    1 
ATOM   11639 N  N      . HIS   D 2  190 ? -29.923 11.374   -26.650 1.00 60.65  ? 190 HIS   D N      1 
ATOM   11640 C  CA     . HIS   D 2  190 ? -31.236 11.152   -26.045 1.00 62.70  ? 190 HIS   D CA     1 
ATOM   11641 C  C      . HIS   D 2  190 ? -31.826 9.778    -26.370 1.00 66.01  ? 190 HIS   D C      1 
ATOM   11642 O  O      . HIS   D 2  190 ? -32.590 9.223    -25.573 1.00 64.89  ? 190 HIS   D O      1 
ATOM   11643 C  CB     . HIS   D 2  190 ? -32.195 12.243   -26.506 1.00 65.66  ? 190 HIS   D CB     1 
ATOM   11644 C  CG     . HIS   D 2  190 ? -33.565 12.148   -25.911 1.00 71.67  ? 190 HIS   D CG     1 
ATOM   11645 N  ND1    . HIS   D 2  190 ? -33.806 12.251   -24.559 1.00 73.41  ? 190 HIS   D ND1    1 
ATOM   11646 C  CD2    . HIS   D 2  190 ? -34.773 11.945   -26.493 1.00 74.91  ? 190 HIS   D CD2    1 
ATOM   11647 C  CE1    . HIS   D 2  190 ? -35.103 12.132   -24.334 1.00 73.84  ? 190 HIS   D CE1    1 
ATOM   11648 N  NE2    . HIS   D 2  190 ? -35.712 11.943   -25.491 1.00 76.78  ? 190 HIS   D NE2    1 
ATOM   11649 N  N      . GLN   D 2  191 ? -31.496 9.233    -27.549 1.00 63.12  ? 191 GLN   D N      1 
ATOM   11650 C  CA     . GLN   D 2  191 ? -31.904 7.879    -27.918 1.00 63.67  ? 191 GLN   D CA     1 
ATOM   11651 C  C      . GLN   D 2  191 ? -30.891 6.839    -27.444 1.00 62.62  ? 191 GLN   D C      1 
ATOM   11652 O  O      . GLN   D 2  191 ? -31.284 5.779    -26.940 1.00 59.99  ? 191 GLN   D O      1 
ATOM   11653 C  CB     . GLN   D 2  191 ? -32.089 7.761    -29.441 1.00 61.00  ? 191 GLN   D CB     1 
ATOM   11654 C  CG     . GLN   D 2  191 ? -33.068 8.732    -30.061 1.00 63.95  ? 191 GLN   D CG     1 
ATOM   11655 C  CD     . GLN   D 2  191 ? -34.520 8.396    -29.770 1.00 70.24  ? 191 GLN   D CD     1 
ATOM   11656 O  OE1    . GLN   D 2  191 ? -34.934 7.232    -29.872 1.00 68.32  ? 191 GLN   D OE1    1 
ATOM   11657 N  NE2    . GLN   D 2  191 ? -35.313 9.419    -29.439 1.00 66.87  ? 191 GLN   D NE2    1 
ATOM   11658 N  N      . LEU   D 2  192 ? -29.587 7.117    -27.603 1.00 61.00  ? 192 LEU   D N      1 
ATOM   11659 C  CA     . LEU   D 2  192 ? -28.567 6.134    -27.240 1.00 59.31  ? 192 LEU   D CA     1 
ATOM   11660 C  C      . LEU   D 2  192 ? -28.512 5.875    -25.738 1.00 60.17  ? 192 LEU   D C      1 
ATOM   11661 O  O      . LEU   D 2  192 ? -28.162 4.765    -25.318 1.00 57.34  ? 192 LEU   D O      1 
ATOM   11662 C  CB     . LEU   D 2  192 ? -27.185 6.562    -27.735 1.00 56.71  ? 192 LEU   D CB     1 
ATOM   11663 C  CG     . LEU   D 2  192 ? -26.925 6.568    -29.231 1.00 57.70  ? 192 LEU   D CG     1 
ATOM   11664 C  CD1    . LEU   D 2  192 ? -25.540 7.099    -29.462 1.00 56.60  ? 192 LEU   D CD1    1 
ATOM   11665 C  CD2    . LEU   D 2  192 ? -27.050 5.156    -29.781 1.00 56.87  ? 192 LEU   D CD2    1 
ATOM   11666 N  N      . VAL   D 2  193 ? -28.840 6.875    -24.918 1.00 58.34  ? 193 VAL   D N      1 
ATOM   11667 C  CA     . VAL   D 2  193 ? -28.869 6.658    -23.479 1.00 56.45  ? 193 VAL   D CA     1 
ATOM   11668 C  C      . VAL   D 2  193 ? -29.938 5.647    -23.079 1.00 57.53  ? 193 VAL   D C      1 
ATOM   11669 O  O      . VAL   D 2  193 ? -29.772 4.938    -22.075 1.00 59.12  ? 193 VAL   D O      1 
ATOM   11670 C  CB     . VAL   D 2  193 ? -29.008 8.010    -22.758 1.00 61.14  ? 193 VAL   D CB     1 
ATOM   11671 C  CG1    . VAL   D 2  193 ? -29.468 7.835    -21.320 1.00 57.59  ? 193 VAL   D CG1    1 
ATOM   11672 C  CG2    . VAL   D 2  193 ? -27.644 8.644    -22.712 1.00 52.86  ? 193 VAL   D CG2    1 
ATOM   11673 N  N      . GLU   D 2  194 ? -31.008 5.506    -23.864 1.00 55.69  ? 194 GLU   D N      1 
ATOM   11674 C  CA     . GLU   D 2  194 ? -32.110 4.646    -23.457 1.00 50.31  ? 194 GLU   D CA     1 
ATOM   11675 C  C      . GLU   D 2  194 ? -32.140 3.295    -24.143 1.00 45.93  ? 194 GLU   D C      1 
ATOM   11676 O  O      . GLU   D 2  194 ? -32.820 2.400    -23.645 1.00 53.73  ? 194 GLU   D O      1 
ATOM   11677 C  CB     . GLU   D 2  194 ? -33.448 5.326    -23.725 1.00 50.66  ? 194 GLU   D CB     1 
ATOM   11678 C  CG     . GLU   D 2  194 ? -33.509 6.701    -23.164 1.00 52.67  ? 194 GLU   D CG     1 
ATOM   11679 C  CD     . GLU   D 2  194 ? -33.919 6.702    -21.736 1.00 59.26  ? 194 GLU   D CD     1 
ATOM   11680 O  OE1    . GLU   D 2  194 ? -34.798 5.871    -21.407 1.00 68.46  ? 194 GLU   D OE1    1 
ATOM   11681 O  OE2    . GLU   D 2  194 ? -33.371 7.525    -20.956 1.00 57.86  ? 194 GLU   D OE2    1 
ATOM   11682 N  N      . ASN   D 2  195 ? -31.455 3.106    -25.265 1.00 45.96  ? 195 ASN   D N      1 
ATOM   11683 C  CA     . ASN   D 2  195 ? -31.687 1.900    -26.059 1.00 55.54  ? 195 ASN   D CA     1 
ATOM   11684 C  C      . ASN   D 2  195 ? -30.427 1.170    -26.511 1.00 55.31  ? 195 ASN   D C      1 
ATOM   11685 O  O      . ASN   D 2  195 ? -30.529 0.262    -27.344 1.00 54.49  ? 195 ASN   D O      1 
ATOM   11686 C  CB     . ASN   D 2  195 ? -32.556 2.223    -27.282 1.00 54.48  ? 195 ASN   D CB     1 
ATOM   11687 C  CG     . ASN   D 2  195 ? -33.920 2.750    -26.889 1.00 62.16  ? 195 ASN   D CG     1 
ATOM   11688 O  OD1    . ASN   D 2  195 ? -34.526 2.260    -25.940 1.00 67.68  ? 195 ASN   D OD1    1 
ATOM   11689 N  ND2    . ASN   D 2  195 ? -34.387 3.780    -27.578 1.00 64.26  ? 195 ASN   D ND2    1 
ATOM   11690 N  N      . THR   D 2  196 ? -29.257 1.515    -25.984 1.00 52.74  ? 196 THR   D N      1 
ATOM   11691 C  CA     . THR   D 2  196 ? -28.055 0.720    -26.185 1.00 56.91  ? 196 THR   D CA     1 
ATOM   11692 C  C      . THR   D 2  196 ? -27.457 0.256    -24.862 1.00 60.40  ? 196 THR   D C      1 
ATOM   11693 O  O      . THR   D 2  196 ? -27.505 0.952    -23.838 1.00 57.08  ? 196 THR   D O      1 
ATOM   11694 C  CB     . THR   D 2  196 ? -26.993 1.483    -26.945 1.00 54.44  ? 196 THR   D CB     1 
ATOM   11695 O  OG1    . THR   D 2  196 ? -26.813 2.747    -26.306 1.00 59.29  ? 196 THR   D OG1    1 
ATOM   11696 C  CG2    . THR   D 2  196 ? -27.381 1.657    -28.368 1.00 54.09  ? 196 THR   D CG2    1 
ATOM   11697 N  N      . ASP   D 2  197 ? -26.868 -0.928   -24.919 1.00 53.93  ? 197 ASP   D N      1 
ATOM   11698 C  CA     . ASP   D 2  197 ? -26.124 -1.485   -23.811 1.00 54.80  ? 197 ASP   D CA     1 
ATOM   11699 C  C      . ASP   D 2  197 ? -24.660 -1.071   -23.821 1.00 55.39  ? 197 ASP   D C      1 
ATOM   11700 O  O      . ASP   D 2  197 ? -24.072 -0.908   -22.753 1.00 56.37  ? 197 ASP   D O      1 
ATOM   11701 C  CB     . ASP   D 2  197 ? -26.285 -3.000   -23.847 1.00 57.97  ? 197 ASP   D CB     1 
ATOM   11702 C  CG     . ASP   D 2  197 ? -27.732 -3.392   -23.838 1.00 59.41  ? 197 ASP   D CG     1 
ATOM   11703 O  OD1    . ASP   D 2  197 ? -28.378 -3.082   -22.814 1.00 65.65  ? 197 ASP   D OD1    1 
ATOM   11704 O  OD2    . ASP   D 2  197 ? -28.239 -3.935   -24.849 1.00 53.23  ? 197 ASP   D OD2    1 
ATOM   11705 N  N      . GLU   D 2  198 ? -24.058 -0.860   -24.990 1.00 61.95  ? 198 GLU   D N      1 
ATOM   11706 C  CA     . GLU   D 2  198 ? -22.695 -0.337   -25.077 1.00 61.06  ? 198 GLU   D CA     1 
ATOM   11707 C  C      . GLU   D 2  198 ? -22.559 0.650    -26.236 1.00 60.43  ? 198 GLU   D C      1 
ATOM   11708 O  O      . GLU   D 2  198 ? -22.926 0.325    -27.370 1.00 61.44  ? 198 GLU   D O      1 
ATOM   11709 C  CB     . GLU   D 2  198 ? -21.675 -1.473   -25.265 1.00 57.13  ? 198 GLU   D CB     1 
ATOM   11710 C  CG     . GLU   D 2  198 ? -21.787 -2.637   -24.307 1.00 59.11  ? 198 GLU   D CG     1 
ATOM   11711 C  CD     . GLU   D 2  198 ? -21.559 -3.975   -24.996 1.00 65.02  ? 198 GLU   D CD     1 
ATOM   11712 O  OE1    . GLU   D 2  198 ? -21.514 -3.996   -26.240 1.00 63.34  ? 198 GLU   D OE1    1 
ATOM   11713 O  OE2    . GLU   D 2  198 ? -21.396 -5.005   -24.295 1.00 63.94  ? 198 GLU   D OE2    1 
ATOM   11714 N  N      . THR   D 2  199 ? -22.010 1.841    -25.971 1.00 57.27  ? 199 THR   D N      1 
ATOM   11715 C  CA     . THR   D 2  199 ? -21.588 2.758    -27.033 1.00 52.86  ? 199 THR   D CA     1 
ATOM   11716 C  C      . THR   D 2  199 ? -20.121 3.122    -26.892 1.00 52.63  ? 199 THR   D C      1 
ATOM   11717 O  O      . THR   D 2  199 ? -19.714 3.710    -25.882 1.00 50.82  ? 199 THR   D O      1 
ATOM   11718 C  CB     . THR   D 2  199 ? -22.405 4.045    -27.066 1.00 53.60  ? 199 THR   D CB     1 
ATOM   11719 O  OG1    . THR   D 2  199 ? -23.685 3.781    -27.639 1.00 54.67  ? 199 THR   D OG1    1 
ATOM   11720 C  CG2    . THR   D 2  199 ? -21.666 5.087    -27.878 1.00 54.89  ? 199 THR   D CG2    1 
ATOM   11721 N  N      . TYR   D 2  200 ? -19.354 2.792    -27.925 1.00 50.01  ? 200 TYR   D N      1 
ATOM   11722 C  CA     . TYR   D 2  200 ? -17.980 3.232    -28.142 1.00 52.33  ? 200 TYR   D CA     1 
ATOM   11723 C  C      . TYR   D 2  200 ? -17.996 4.622    -28.767 1.00 56.03  ? 200 TYR   D C      1 
ATOM   11724 O  O      . TYR   D 2  200 ? -18.190 4.757    -29.974 1.00 58.01  ? 200 TYR   D O      1 
ATOM   11725 C  CB     . TYR   D 2  200 ? -17.285 2.251    -29.079 1.00 50.25  ? 200 TYR   D CB     1 
ATOM   11726 C  CG     . TYR   D 2  200 ? -17.075 0.863    -28.545 1.00 53.49  ? 200 TYR   D CG     1 
ATOM   11727 C  CD1    . TYR   D 2  200 ? -16.022 0.559    -27.701 1.00 51.63  ? 200 TYR   D CD1    1 
ATOM   11728 C  CD2    . TYR   D 2  200 ? -18.019 -0.110   -28.773 1.00 55.31  ? 200 TYR   D CD2    1 
ATOM   11729 C  CE1    . TYR   D 2  200 ? -15.857 -0.724   -27.211 1.00 46.81  ? 200 TYR   D CE1    1 
ATOM   11730 C  CE2    . TYR   D 2  200 ? -17.885 -1.371   -28.270 1.00 56.45  ? 200 TYR   D CE2    1 
ATOM   11731 C  CZ     . TYR   D 2  200 ? -16.804 -1.683   -27.491 1.00 55.50  ? 200 TYR   D CZ     1 
ATOM   11732 O  OH     . TYR   D 2  200 ? -16.699 -2.975   -27.015 1.00 56.55  ? 200 TYR   D OH     1 
ATOM   11733 N  N      . CYS   D 2  201 ? -17.774 5.655    -27.958 1.00 52.04  ? 201 CYS   D N      1 
ATOM   11734 C  CA     . CYS   D 2  201 ? -17.654 7.017    -28.466 1.00 53.65  ? 201 CYS   D CA     1 
ATOM   11735 C  C      . CYS   D 2  201 ? -16.419 7.161    -29.345 1.00 58.23  ? 201 CYS   D C      1 
ATOM   11736 O  O      . CYS   D 2  201 ? -15.294 6.998    -28.867 1.00 56.50  ? 201 CYS   D O      1 
ATOM   11737 C  CB     . CYS   D 2  201 ? -17.573 7.990    -27.304 1.00 58.80  ? 201 CYS   D CB     1 
ATOM   11738 S  SG     . CYS   D 2  201 ? -18.956 7.831    -26.238 1.00 68.04  ? 201 CYS   D SG     1 
ATOM   11739 N  N      . ILE   D 2  202 ? -16.627 7.484    -30.621 1.00 67.05  ? 202 ILE   D N      1 
ATOM   11740 C  CA     . ILE   D 2  202 ? -15.560 7.746    -31.584 1.00 62.91  ? 202 ILE   D CA     1 
ATOM   11741 C  C      . ILE   D 2  202 ? -15.632 9.240    -31.860 1.00 65.93  ? 202 ILE   D C      1 
ATOM   11742 O  O      . ILE   D 2  202 ? -16.514 9.691    -32.595 1.00 72.94  ? 202 ILE   D O      1 
ATOM   11743 C  CB     . ILE   D 2  202 ? -15.733 6.939    -32.877 1.00 63.48  ? 202 ILE   D CB     1 
ATOM   11744 C  CG1    . ILE   D 2  202 ? -15.759 5.421    -32.628 1.00 59.42  ? 202 ILE   D CG1    1 
ATOM   11745 C  CG2    . ILE   D 2  202 ? -14.607 7.253    -33.840 1.00 64.11  ? 202 ILE   D CG2    1 
ATOM   11746 C  CD1    . ILE   D 2  202 ? -14.517 4.858    -32.031 1.00 59.66  ? 202 ILE   D CD1    1 
ATOM   11747 N  N      . ASP   D 2  203 ? -14.746 10.026   -31.252 1.00 67.59  ? 203 ASP   D N      1 
ATOM   11748 C  CA     . ASP   D 2  203 ? -14.848 11.484   -31.316 1.00 71.01  ? 203 ASP   D CA     1 
ATOM   11749 C  C      . ASP   D 2  203 ? -14.028 11.995   -32.510 1.00 76.95  ? 203 ASP   D C      1 
ATOM   11750 O  O      . ASP   D 2  203 ? -12.791 11.911   -32.524 1.00 73.28  ? 203 ASP   D O      1 
ATOM   11751 C  CB     . ASP   D 2  203 ? -14.393 12.099   -29.994 1.00 62.03  ? 203 ASP   D CB     1 
ATOM   11752 C  CG     . ASP   D 2  203 ? -14.727 13.577   -29.878 1.00 71.23  ? 203 ASP   D CG     1 
ATOM   11753 O  OD1    . ASP   D 2  203 ? -15.119 14.205   -30.882 1.00 75.83  ? 203 ASP   D OD1    1 
ATOM   11754 O  OD2    . ASP   D 2  203 ? -14.619 14.117   -28.759 1.00 72.82  ? 203 ASP   D OD2    1 
ATOM   11755 N  N      . ASN   D 2  204 ? -14.718 12.517   -33.528 1.00 78.52  ? 204 ASN   D N      1 
ATOM   11756 C  CA     . ASN   D 2  204 ? -14.006 13.069   -34.677 1.00 80.60  ? 204 ASN   D CA     1 
ATOM   11757 C  C      . ASN   D 2  204 ? -13.070 14.201   -34.261 1.00 76.39  ? 204 ASN   D C      1 
ATOM   11758 O  O      . ASN   D 2  204 ? -11.964 14.327   -34.800 1.00 76.06  ? 204 ASN   D O      1 
ATOM   11759 C  CB     . ASN   D 2  204 ? -15.003 13.539   -35.741 1.00 76.91  ? 204 ASN   D CB     1 
ATOM   11760 C  CG     . ASN   D 2  204 ? -15.245 12.490   -36.816 1.00 74.40  ? 204 ASN   D CG     1 
ATOM   11761 O  OD1    . ASN   D 2  204 ? -14.567 11.457   -36.871 1.00 70.32  ? 204 ASN   D OD1    1 
ATOM   11762 N  ND2    . ASN   D 2  204 ? -16.205 12.761   -37.691 1.00 79.84  ? 204 ASN   D ND2    1 
ATOM   11763 N  N      . GLU   D 2  205 ? -13.494 15.037   -33.306 1.00 74.71  ? 205 GLU   D N      1 
ATOM   11764 C  CA     . GLU   D 2  205 ? -12.568 15.998   -32.720 1.00 78.11  ? 205 GLU   D CA     1 
ATOM   11765 C  C      . GLU   D 2  205 ? -11.325 15.303   -32.191 1.00 74.58  ? 205 GLU   D C      1 
ATOM   11766 O  O      . GLU   D 2  205 ? -10.216 15.837   -32.292 1.00 77.06  ? 205 GLU   D O      1 
ATOM   11767 C  CB     . GLU   D 2  205 ? -13.230 16.787   -31.592 1.00 78.86  ? 205 GLU   D CB     1 
ATOM   11768 C  CG     . GLU   D 2  205 ? -12.220 17.605   -30.800 1.00 74.54  ? 205 GLU   D CG     1 
ATOM   11769 C  CD     . GLU   D 2  205 ? -12.713 18.994   -30.478 1.00 82.35  ? 205 GLU   D CD     1 
ATOM   11770 O  OE1    . GLU   D 2  205 ? -13.794 19.369   -30.981 1.00 83.83  ? 205 GLU   D OE1    1 
ATOM   11771 O  OE2    . GLU   D 2  205 ? -12.016 19.712   -29.726 1.00 87.99  ? 205 GLU   D OE2    1 
ATOM   11772 N  N      . ALA   D 2  206 ? -11.490 14.116   -31.617 1.00 69.39  ? 206 ALA   D N      1 
ATOM   11773 C  CA     . ALA   D 2  206 ? -10.334 13.394   -31.106 1.00 71.16  ? 206 ALA   D CA     1 
ATOM   11774 C  C      . ALA   D 2  206 ? -9.475  12.826   -32.225 1.00 72.77  ? 206 ALA   D C      1 
ATOM   11775 O  O      . ALA   D 2  206 ? -8.247  12.784   -32.097 1.00 70.63  ? 206 ALA   D O      1 
ATOM   11776 C  CB     . ALA   D 2  206 ? -10.781 12.276   -30.168 1.00 67.53  ? 206 ALA   D CB     1 
ATOM   11777 N  N      . LEU   D 2  207 ? -10.099 12.385   -33.317 1.00 77.56  ? 207 LEU   D N      1 
ATOM   11778 C  CA     . LEU   D 2  207 ? -9.354  11.811   -34.436 1.00 75.94  ? 207 LEU   D CA     1 
ATOM   11779 C  C      . LEU   D 2  207 ? -8.571  12.883   -35.177 1.00 77.16  ? 207 LEU   D C      1 
ATOM   11780 O  O      . LEU   D 2  207 ? -7.402  12.689   -35.529 1.00 73.10  ? 207 LEU   D O      1 
ATOM   11781 C  CB     . LEU   D 2  207 ? -10.325 11.113   -35.383 1.00 78.93  ? 207 LEU   D CB     1 
ATOM   11782 C  CG     . LEU   D 2  207 ? -11.193 10.014   -34.784 1.00 73.65  ? 207 LEU   D CG     1 
ATOM   11783 C  CD1    . LEU   D 2  207 ? -12.236 9.624    -35.782 1.00 68.64  ? 207 LEU   D CD1    1 
ATOM   11784 C  CD2    . LEU   D 2  207 ? -10.312 8.831    -34.485 1.00 68.91  ? 207 LEU   D CD2    1 
ATOM   11785 N  N      . TYR   D 2  208 ? -9.221  14.014   -35.451 1.00 82.04  ? 208 TYR   D N      1 
ATOM   11786 C  CA     . TYR   D 2  208 ? -8.525  15.151   -36.042 1.00 87.89  ? 208 TYR   D CA     1 
ATOM   11787 C  C      . TYR   D 2  208 ? -7.339  15.577   -35.190 1.00 90.53  ? 208 TYR   D C      1 
ATOM   11788 O  O      . TYR   D 2  208 ? -6.214  15.681   -35.691 1.00 91.24  ? 208 TYR   D O      1 
ATOM   11789 C  CB     . TYR   D 2  208 ? -9.500  16.307   -36.255 1.00 90.23  ? 208 TYR   D CB     1 
ATOM   11790 C  CG     . TYR   D 2  208 ? -8.857  17.525   -36.861 1.00 102.72 ? 208 TYR   D CG     1 
ATOM   11791 C  CD1    . TYR   D 2  208 ? -8.559  17.576   -38.217 1.00 102.71 ? 208 TYR   D CD1    1 
ATOM   11792 C  CD2    . TYR   D 2  208 ? -8.617  18.661   -36.086 1.00 103.22 ? 208 TYR   D CD2    1 
ATOM   11793 C  CE1    . TYR   D 2  208 ? -7.974  18.699   -38.777 1.00 106.82 ? 208 TYR   D CE1    1 
ATOM   11794 C  CE2    . TYR   D 2  208 ? -8.043  19.799   -36.644 1.00 107.49 ? 208 TYR   D CE2    1 
ATOM   11795 C  CZ     . TYR   D 2  208 ? -7.723  19.810   -37.988 1.00 106.72 ? 208 TYR   D CZ     1 
ATOM   11796 O  OH     . TYR   D 2  208 ? -7.154  20.933   -38.541 1.00 108.05 ? 208 TYR   D OH     1 
ATOM   11797 N  N      . ASP   D 2  209 ? -7.563  15.788   -33.888 1.00 88.18  ? 209 ASP   D N      1 
ATOM   11798 C  CA     . ASP   D 2  209 ? -6.494  16.296   -33.041 1.00 81.85  ? 209 ASP   D CA     1 
ATOM   11799 C  C      . ASP   D 2  209 ? -5.358  15.293   -32.934 1.00 77.42  ? 209 ASP   D C      1 
ATOM   11800 O  O      . ASP   D 2  209 ? -4.208  15.678   -32.736 1.00 84.44  ? 209 ASP   D O      1 
ATOM   11801 C  CB     . ASP   D 2  209 ? -7.035  16.648   -31.664 1.00 70.78  ? 209 ASP   D CB     1 
ATOM   11802 C  CG     . ASP   D 2  209 ? -7.871  17.896   -31.687 1.00 81.31  ? 209 ASP   D CG     1 
ATOM   11803 O  OD1    . ASP   D 2  209 ? -7.987  18.498   -32.774 1.00 87.62  ? 209 ASP   D OD1    1 
ATOM   11804 O  OD2    . ASP   D 2  209 ? -8.388  18.301   -30.629 1.00 82.40  ? 209 ASP   D OD2    1 
ATOM   11805 N  N      . ILE   D 2  210 ? -5.647  14.006   -33.071 1.00 75.49  ? 210 ILE   D N      1 
ATOM   11806 C  CA     . ILE   D 2  210 ? -4.568  13.031   -33.154 1.00 79.97  ? 210 ILE   D CA     1 
ATOM   11807 C  C      . ILE   D 2  210 ? -3.761  13.259   -34.420 1.00 91.09  ? 210 ILE   D C      1 
ATOM   11808 O  O      . ILE   D 2  210 ? -2.574  13.600   -34.365 1.00 96.14  ? 210 ILE   D O      1 
ATOM   11809 C  CB     . ILE   D 2  210 ? -5.110  11.592   -33.103 1.00 79.00  ? 210 ILE   D CB     1 
ATOM   11810 C  CG1    . ILE   D 2  210 ? -5.736  11.285   -31.744 1.00 73.50  ? 210 ILE   D CG1    1 
ATOM   11811 C  CG2    . ILE   D 2  210 ? -4.000  10.596   -33.420 1.00 79.10  ? 210 ILE   D CG2    1 
ATOM   11812 C  CD1    . ILE   D 2  210 ? -6.220  9.867    -31.613 1.00 66.86  ? 210 ILE   D CD1    1 
ATOM   11813 N  N      . CYS   D 2  211 ? -4.404  13.075   -35.578 1.00 94.86  ? 211 CYS   D N      1 
ATOM   11814 C  CA     . CYS   D 2  211 ? -3.705  13.135   -36.861 1.00 98.48  ? 211 CYS   D CA     1 
ATOM   11815 C  C      . CYS   D 2  211 ? -2.903  14.434   -36.999 1.00 99.57  ? 211 CYS   D C      1 
ATOM   11816 O  O      . CYS   D 2  211 ? -1.760  14.426   -37.474 1.00 97.38  ? 211 CYS   D O      1 
ATOM   11817 C  CB     . CYS   D 2  211 ? -4.728  12.984   -38.000 1.00 100.00 ? 211 CYS   D CB     1 
ATOM   11818 S  SG     . CYS   D 2  211 ? -5.452  11.295   -38.287 1.00 83.22  ? 211 CYS   D SG     1 
ATOM   11819 N  N      . PHE   D 2  212 ? -3.481  15.555   -36.560 1.00 98.05  ? 212 PHE   D N      1 
ATOM   11820 C  CA     . PHE   D 2  212 ? -2.840  16.860   -36.698 1.00 99.63  ? 212 PHE   D CA     1 
ATOM   11821 C  C      . PHE   D 2  212 ? -1.591  16.952   -35.826 1.00 99.98  ? 212 PHE   D C      1 
ATOM   11822 O  O      . PHE   D 2  212 ? -0.509  17.292   -36.313 1.00 103.44 ? 212 PHE   D O      1 
ATOM   11823 C  CB     . PHE   D 2  212 ? -3.868  17.942   -36.337 1.00 108.04 ? 212 PHE   D CB     1 
ATOM   11824 C  CG     . PHE   D 2  212 ? -3.368  19.367   -36.412 1.00 117.92 ? 212 PHE   D CG     1 
ATOM   11825 C  CD1    . PHE   D 2  212 ? -2.621  19.814   -37.499 1.00 114.12 ? 212 PHE   D CD1    1 
ATOM   11826 C  CD2    . PHE   D 2  212 ? -3.735  20.285   -35.430 1.00 117.86 ? 212 PHE   D CD2    1 
ATOM   11827 C  CE1    . PHE   D 2  212 ? -2.203  21.132   -37.569 1.00 113.66 ? 212 PHE   D CE1    1 
ATOM   11828 C  CE2    . PHE   D 2  212 ? -3.328  21.606   -35.500 1.00 117.70 ? 212 PHE   D CE2    1 
ATOM   11829 C  CZ     . PHE   D 2  212 ? -2.559  22.031   -36.567 1.00 114.49 ? 212 PHE   D CZ     1 
ATOM   11830 N  N      . ARG   D 2  213 ? -1.715  16.619   -34.537 1.00 97.12  ? 213 ARG   D N      1 
ATOM   11831 C  CA     . ARG   D 2  213 ? -0.601  16.792   -33.609 1.00 93.78  ? 213 ARG   D CA     1 
ATOM   11832 C  C      . ARG   D 2  213 ? 0.352   15.610   -33.661 1.00 93.06  ? 213 ARG   D C      1 
ATOM   11833 O  O      . ARG   D 2  213 ? 1.541   15.762   -33.952 1.00 96.72  ? 213 ARG   D O      1 
ATOM   11834 C  CB     . ARG   D 2  213 ? -1.093  16.955   -32.168 1.00 83.81  ? 213 ARG   D CB     1 
ATOM   11835 C  CG     . ARG   D 2  213 ? -1.692  18.285   -31.792 1.00 84.54  ? 213 ARG   D CG     1 
ATOM   11836 C  CD     . ARG   D 2  213 ? -3.199  18.209   -31.854 1.00 93.29  ? 213 ARG   D CD     1 
ATOM   11837 N  NE     . ARG   D 2  213 ? -3.833  19.329   -31.170 1.00 102.51 ? 213 ARG   D NE     1 
ATOM   11838 C  CZ     . ARG   D 2  213 ? -3.964  19.439   -29.852 1.00 97.48  ? 213 ARG   D CZ     1 
ATOM   11839 N  NH1    . ARG   D 2  213 ? -3.354  18.606   -29.022 1.00 90.12  ? 213 ARG   D NH1    1 
ATOM   11840 N  NH2    . ARG   D 2  213 ? -4.709  20.423   -29.354 1.00 97.59  ? 213 ARG   D NH2    1 
ATOM   11841 N  N      . THR   D 2  214 ? -0.148  14.424   -33.344 1.00 90.90  ? 214 THR   D N      1 
ATOM   11842 C  CA     . THR   D 2  214 ? 0.759   13.303   -33.139 1.00 96.52  ? 214 THR   D CA     1 
ATOM   11843 C  C      . THR   D 2  214 ? 1.271   12.736   -34.457 1.00 99.16  ? 214 THR   D C      1 
ATOM   11844 O  O      . THR   D 2  214 ? 2.438   12.336   -34.548 1.00 96.77  ? 214 THR   D O      1 
ATOM   11845 C  CB     . THR   D 2  214 ? 0.067   12.217   -32.312 1.00 99.21  ? 214 THR   D CB     1 
ATOM   11846 O  OG1    . THR   D 2  214 ? -0.415  12.786   -31.084 1.00 96.01  ? 214 THR   D OG1    1 
ATOM   11847 C  CG2    . THR   D 2  214 ? 1.034   11.063   -32.016 1.00 94.70  ? 214 THR   D CG2    1 
ATOM   11848 N  N      . LEU   D 2  215 ? 0.420   12.700   -35.485 1.00 102.71 ? 215 LEU   D N      1 
ATOM   11849 C  CA     . LEU   D 2  215 ? 0.804   12.212   -36.802 1.00 100.76 ? 215 LEU   D CA     1 
ATOM   11850 C  C      . LEU   D 2  215 ? 1.228   13.327   -37.749 1.00 100.54 ? 215 LEU   D C      1 
ATOM   11851 O  O      . LEU   D 2  215 ? 1.731   13.033   -38.838 1.00 98.07  ? 215 LEU   D O      1 
ATOM   11852 C  CB     . LEU   D 2  215 ? -0.346  11.418   -37.436 1.00 101.19 ? 215 LEU   D CB     1 
ATOM   11853 C  CG     . LEU   D 2  215 ? -0.864  10.259   -36.582 1.00 97.55  ? 215 LEU   D CG     1 
ATOM   11854 C  CD1    . LEU   D 2  215 ? -1.814  10.801   -35.524 1.00 93.19  ? 215 LEU   D CD1    1 
ATOM   11855 C  CD2    . LEU   D 2  215 ? -1.523  9.170    -37.419 1.00 87.95  ? 215 LEU   D CD2    1 
ATOM   11856 N  N      . LYS   D 2  216 ? 1.034   14.592   -37.373 1.00 102.30 ? 216 LYS   D N      1 
ATOM   11857 C  CA     . LYS   D 2  216 ? 1.491   15.720   -38.178 1.00 106.82 ? 216 LYS   D CA     1 
ATOM   11858 C  C      . LYS   D 2  216 ? 0.890   15.671   -39.589 1.00 107.98 ? 216 LYS   D C      1 
ATOM   11859 O  O      . LYS   D 2  216 ? 1.581   15.487   -40.593 1.00 107.37 ? 216 LYS   D O      1 
ATOM   11860 C  CB     . LYS   D 2  216 ? 3.024   15.759   -38.224 1.00 107.79 ? 216 LYS   D CB     1 
ATOM   11861 C  CG     . LYS   D 2  216 ? 3.708   15.962   -36.880 1.00 101.57 ? 216 LYS   D CG     1 
ATOM   11862 C  CD     . LYS   D 2  216 ? 3.327   17.302   -36.271 1.00 107.07 ? 216 LYS   D CD     1 
ATOM   11863 C  CE     . LYS   D 2  216 ? 4.037   17.516   -34.950 1.00 110.53 ? 216 LYS   D CE     1 
ATOM   11864 N  NZ     . LYS   D 2  216 ? 3.654   18.811   -34.335 1.00 115.85 ? 216 LYS   D NZ     1 
ATOM   11865 N  N      . LEU   D 2  217 ? -0.421  15.849   -39.652 1.00 104.31 ? 217 LEU   D N      1 
ATOM   11866 C  CA     . LEU   D 2  217 ? -1.144  15.900   -40.915 1.00 100.32 ? 217 LEU   D CA     1 
ATOM   11867 C  C      . LEU   D 2  217 ? -1.853  17.249   -40.938 1.00 111.03 ? 217 LEU   D C      1 
ATOM   11868 O  O      . LEU   D 2  217 ? -2.866  17.436   -40.261 1.00 116.90 ? 217 LEU   D O      1 
ATOM   11869 C  CB     . LEU   D 2  217 ? -2.107  14.727   -41.014 1.00 97.15  ? 217 LEU   D CB     1 
ATOM   11870 C  CG     . LEU   D 2  217 ? -1.398  13.372   -40.968 1.00 94.92  ? 217 LEU   D CG     1 
ATOM   11871 C  CD1    . LEU   D 2  217 ? -2.321  12.288   -40.446 1.00 96.66  ? 217 LEU   D CD1    1 
ATOM   11872 C  CD2    . LEU   D 2  217 ? -0.848  12.986   -42.320 1.00 96.75  ? 217 LEU   D CD2    1 
ATOM   11873 N  N      . THR   D 2  218 ? -1.302  18.205   -41.686 1.00 113.30 ? 218 THR   D N      1 
ATOM   11874 C  CA     . THR   D 2  218 ? -1.828  19.566   -41.621 1.00 117.97 ? 218 THR   D CA     1 
ATOM   11875 C  C      . THR   D 2  218 ? -3.307  19.591   -41.980 1.00 116.57 ? 218 THR   D C      1 
ATOM   11876 O  O      . THR   D 2  218 ? -4.134  20.114   -41.223 1.00 112.36 ? 218 THR   D O      1 
ATOM   11877 C  CB     . THR   D 2  218 ? -1.024  20.489   -42.535 1.00 120.72 ? 218 THR   D CB     1 
ATOM   11878 O  OG1    . THR   D 2  218 ? -1.569  21.815   -42.483 1.00 118.29 ? 218 THR   D OG1    1 
ATOM   11879 C  CG2    . THR   D 2  218 ? -1.036  19.971   -43.972 1.00 126.48 ? 218 THR   D CG2    1 
ATOM   11880 N  N      . THR   D 2  219 ? -3.656  19.018   -43.126 1.00 117.25 ? 219 THR   D N      1 
ATOM   11881 C  CA     . THR   D 2  219 ? -5.047  18.787   -43.517 1.00 117.25 ? 219 THR   D CA     1 
ATOM   11882 C  C      . THR   D 2  219 ? -5.288  17.286   -43.604 1.00 116.75 ? 219 THR   D C      1 
ATOM   11883 O  O      . THR   D 2  219 ? -4.786  16.633   -44.542 1.00 107.48 ? 219 THR   D O      1 
ATOM   11884 C  CB     . THR   D 2  219 ? -5.384  19.467   -44.846 1.00 114.69 ? 219 THR   D CB     1 
ATOM   11885 O  OG1    . THR   D 2  219 ? -5.478  20.885   -44.653 1.00 109.40 ? 219 THR   D OG1    1 
ATOM   11886 C  CG2    . THR   D 2  219 ? -6.700  18.938   -45.406 1.00 119.71 ? 219 THR   D CG2    1 
ATOM   11887 N  N      . PRO   D 2  220 ? -6.030  16.688   -42.645 1.00 116.71 ? 220 PRO   D N      1 
ATOM   11888 C  CA     . PRO   D 2  220 ? -6.301  15.243   -42.702 1.00 106.83 ? 220 PRO   D CA     1 
ATOM   11889 C  C      . PRO   D 2  220 ? -7.631  14.899   -43.358 1.00 99.52  ? 220 PRO   D C      1 
ATOM   11890 O  O      . PRO   D 2  220 ? -8.659  15.529   -43.097 1.00 98.62  ? 220 PRO   D O      1 
ATOM   11891 C  CB     . PRO   D 2  220 ? -6.281  14.834   -41.224 1.00 101.74 ? 220 PRO   D CB     1 
ATOM   11892 C  CG     . PRO   D 2  220 ? -6.641  16.120   -40.458 1.00 109.09 ? 220 PRO   D CG     1 
ATOM   11893 C  CD     . PRO   D 2  220 ? -6.583  17.291   -41.418 1.00 111.76 ? 220 PRO   D CD     1 
ATOM   11894 N  N      . THR   D 2  221 ? -7.599  13.894   -44.225 1.00 98.15  ? 221 THR   D N      1 
ATOM   11895 C  CA     . THR   D 2  221 ? -8.760  13.405   -44.951 1.00 94.79  ? 221 THR   D CA     1 
ATOM   11896 C  C      . THR   D 2  221 ? -9.673  12.583   -44.036 1.00 91.29  ? 221 THR   D C      1 
ATOM   11897 O  O      . THR   D 2  221 ? -9.246  12.046   -43.012 1.00 89.13  ? 221 THR   D O      1 
ATOM   11898 C  CB     . THR   D 2  221 ? -8.301  12.567   -46.160 1.00 90.20  ? 221 THR   D CB     1 
ATOM   11899 O  OG1    . THR   D 2  221 ? -9.431  12.121   -46.921 1.00 91.72  ? 221 THR   D OG1    1 
ATOM   11900 C  CG2    . THR   D 2  221 ? -7.436  11.363   -45.729 1.00 77.39  ? 221 THR   D CG2    1 
ATOM   11901 N  N      . TYR   D 2  222 ? -10.946 12.463   -44.429 1.00 83.87  ? 222 TYR   D N      1 
ATOM   11902 C  CA     . TYR   D 2  222 ? -11.815 11.495   -43.774 1.00 69.31  ? 222 TYR   D CA     1 
ATOM   11903 C  C      . TYR   D 2  222 ? -11.225 10.099   -43.918 1.00 65.68  ? 222 TYR   D C      1 
ATOM   11904 O  O      . TYR   D 2  222 ? -11.823 9.130    -43.465 1.00 73.55  ? 222 TYR   D O      1 
ATOM   11905 C  CB     . TYR   D 2  222 ? -13.231 11.503   -44.363 1.00 68.82  ? 222 TYR   D CB     1 
ATOM   11906 C  CG     . TYR   D 2  222 ? -14.160 12.567   -43.841 1.00 67.82  ? 222 TYR   D CG     1 
ATOM   11907 C  CD1    . TYR   D 2  222 ? -14.106 12.972   -42.524 1.00 74.15  ? 222 TYR   D CD1    1 
ATOM   11908 C  CD2    . TYR   D 2  222 ? -15.094 13.168   -44.672 1.00 66.02  ? 222 TYR   D CD2    1 
ATOM   11909 C  CE1    . TYR   D 2  222 ? -14.955 13.945   -42.042 1.00 73.10  ? 222 TYR   D CE1    1 
ATOM   11910 C  CE2    . TYR   D 2  222 ? -15.944 14.144   -44.202 1.00 68.52  ? 222 TYR   D CE2    1 
ATOM   11911 C  CZ     . TYR   D 2  222 ? -15.866 14.529   -42.880 1.00 72.68  ? 222 TYR   D CZ     1 
ATOM   11912 O  OH     . TYR   D 2  222 ? -16.698 15.498   -42.376 1.00 78.99  ? 222 TYR   D OH     1 
ATOM   11913 N  N      . GLY   D 2  223 ? -10.085 9.962    -44.568 1.00 70.19  ? 223 GLY   D N      1 
ATOM   11914 C  CA     . GLY   D 2  223 ? -9.505  8.649    -44.744 1.00 74.19  ? 223 GLY   D CA     1 
ATOM   11915 C  C      . GLY   D 2  223 ? -8.334  8.445    -43.813 1.00 77.94  ? 223 GLY   D C      1 
ATOM   11916 O  O      . GLY   D 2  223 ? -7.959  7.309    -43.513 1.00 75.21  ? 223 GLY   D O      1 
ATOM   11917 N  N      . ASP   D 2  224 ? -7.722  9.552    -43.387 1.00 83.75  ? 224 ASP   D N      1 
ATOM   11918 C  CA     . ASP   D 2  224 ? -6.760  9.507    -42.290 1.00 84.98  ? 224 ASP   D CA     1 
ATOM   11919 C  C      . ASP   D 2  224 ? -7.446  9.180    -40.973 1.00 78.91  ? 224 ASP   D C      1 
ATOM   11920 O  O      . ASP   D 2  224 ? -7.020  8.269    -40.257 1.00 73.95  ? 224 ASP   D O      1 
ATOM   11921 C  CB     . ASP   D 2  224 ? -6.022  10.842   -42.182 1.00 92.39  ? 224 ASP   D CB     1 
ATOM   11922 C  CG     . ASP   D 2  224 ? -4.993  11.024   -43.256 1.00 93.42  ? 224 ASP   D CG     1 
ATOM   11923 O  OD1    . ASP   D 2  224 ? -4.258  10.047   -43.519 1.00 91.75  ? 224 ASP   D OD1    1 
ATOM   11924 O  OD2    . ASP   D 2  224 ? -4.927  12.132   -43.834 1.00 101.25 ? 224 ASP   D OD2    1 
ATOM   11925 N  N      . LEU   D 2  225 ? -8.500  9.934    -40.633 1.00 77.04  ? 225 LEU   D N      1 
ATOM   11926 C  CA     . LEU   D 2  225 ? -9.297  9.652    -39.443 1.00 74.29  ? 225 LEU   D CA     1 
ATOM   11927 C  C      . LEU   D 2  225 ? -9.740  8.194    -39.406 1.00 74.46  ? 225 LEU   D C      1 
ATOM   11928 O  O      . LEU   D 2  225 ? -9.418  7.451    -38.473 1.00 73.71  ? 225 LEU   D O      1 
ATOM   11929 C  CB     . LEU   D 2  225 ? -10.520 10.566   -39.397 1.00 63.82  ? 225 LEU   D CB     1 
ATOM   11930 C  CG     . LEU   D 2  225 ? -10.255 12.039   -39.651 1.00 70.30  ? 225 LEU   D CG     1 
ATOM   11931 C  CD1    . LEU   D 2  225 ? -11.488 12.893   -39.285 1.00 72.14  ? 225 LEU   D CD1    1 
ATOM   11932 C  CD2    . LEU   D 2  225 ? -8.999  12.473   -38.909 1.00 78.53  ? 225 LEU   D CD2    1 
ATOM   11933 N  N      . ASN   D 2  226 ? -10.496 7.770    -40.418 1.00 71.39  ? 226 ASN   D N      1 
ATOM   11934 C  CA     . ASN   D 2  226 ? -11.015 6.412    -40.429 1.00 64.60  ? 226 ASN   D CA     1 
ATOM   11935 C  C      . ASN   D 2  226 ? -9.892  5.386    -40.367 1.00 66.77  ? 226 ASN   D C      1 
ATOM   11936 O  O      . ASN   D 2  226 ? -10.137 4.230    -40.010 1.00 67.77  ? 226 ASN   D O      1 
ATOM   11937 C  CB     . ASN   D 2  226 ? -11.920 6.217    -41.652 1.00 60.58  ? 226 ASN   D CB     1 
ATOM   11938 C  CG     . ASN   D 2  226 ? -13.227 7.066    -41.574 1.00 70.07  ? 226 ASN   D CG     1 
ATOM   11939 O  OD1    . ASN   D 2  226 ? -13.572 7.627    -40.524 1.00 66.23  ? 226 ASN   D OD1    1 
ATOM   11940 N  ND2    . ASN   D 2  226 ? -13.941 7.161    -42.694 1.00 64.06  ? 226 ASN   D ND2    1 
ATOM   11941 N  N      . HIS   D 2  227 ? -8.658  5.784    -40.662 1.00 71.90  ? 227 HIS   D N      1 
ATOM   11942 C  CA     . HIS   D 2  227 ? -7.531  4.890    -40.419 1.00 77.06  ? 227 HIS   D CA     1 
ATOM   11943 C  C      . HIS   D 2  227 ? -7.433  4.574    -38.938 1.00 74.81  ? 227 HIS   D C      1 
ATOM   11944 O  O      . HIS   D 2  227 ? -7.282  3.411    -38.538 1.00 70.58  ? 227 HIS   D O      1 
ATOM   11945 C  CB     . HIS   D 2  227 ? -6.234  5.533    -40.917 1.00 83.14  ? 227 HIS   D CB     1 
ATOM   11946 C  CG     . HIS   D 2  227 ? -4.999  4.745    -40.593 1.00 89.36  ? 227 HIS   D CG     1 
ATOM   11947 N  ND1    . HIS   D 2  227 ? -4.668  3.578    -41.252 1.00 85.52  ? 227 HIS   D ND1    1 
ATOM   11948 C  CD2    . HIS   D 2  227 ? -4.029  4.944    -39.666 1.00 88.15  ? 227 HIS   D CD2    1 
ATOM   11949 C  CE1    . HIS   D 2  227 ? -3.540  3.100    -40.754 1.00 95.10  ? 227 HIS   D CE1    1 
ATOM   11950 N  NE2    . HIS   D 2  227 ? -3.134  3.908    -39.788 1.00 102.72 ? 227 HIS   D NE2    1 
ATOM   11951 N  N      . LEU   D 2  228 ? -7.509  5.626    -38.114 1.00 74.49  ? 228 LEU   D N      1 
ATOM   11952 C  CA     . LEU   D 2  228 ? -7.533  5.491    -36.664 1.00 71.12  ? 228 LEU   D CA     1 
ATOM   11953 C  C      . LEU   D 2  228 ? -8.647  4.542    -36.230 1.00 72.70  ? 228 LEU   D C      1 
ATOM   11954 O  O      . LEU   D 2  228 ? -8.439  3.669    -35.376 1.00 69.28  ? 228 LEU   D O      1 
ATOM   11955 C  CB     . LEU   D 2  228 ? -7.736  6.875    -36.035 1.00 68.13  ? 228 LEU   D CB     1 
ATOM   11956 C  CG     . LEU   D 2  228 ? -6.682  7.994    -36.093 1.00 63.48  ? 228 LEU   D CG     1 
ATOM   11957 C  CD1    . LEU   D 2  228 ? -7.186  9.202    -35.310 1.00 70.24  ? 228 LEU   D CD1    1 
ATOM   11958 C  CD2    . LEU   D 2  228 ? -5.295  7.583    -35.634 1.00 62.84  ? 228 LEU   D CD2    1 
ATOM   11959 N  N      . VAL   D 2  229 ? -9.828  4.679    -36.846 1.00 72.35  ? 229 VAL   D N      1 
ATOM   11960 C  CA     . VAL   D 2  229 ? -11.034 3.973    -36.421 1.00 64.84  ? 229 VAL   D CA     1 
ATOM   11961 C  C      . VAL   D 2  229 ? -10.973 2.479    -36.723 1.00 62.60  ? 229 VAL   D C      1 
ATOM   11962 O  O      . VAL   D 2  229 ? -11.517 1.674    -35.967 1.00 62.96  ? 229 VAL   D O      1 
ATOM   11963 C  CB     . VAL   D 2  229 ? -12.271 4.647    -37.048 1.00 60.46  ? 229 VAL   D CB     1 
ATOM   11964 C  CG1    . VAL   D 2  229 ? -13.524 3.948    -36.624 1.00 63.35  ? 229 VAL   D CG1    1 
ATOM   11965 C  CG2    . VAL   D 2  229 ? -12.361 6.093    -36.582 1.00 57.94  ? 229 VAL   D CG2    1 
ATOM   11966 N  N      . SER   D 2  230 ? -10.329 2.065    -37.807 1.00 67.58  ? 230 SER   D N      1 
ATOM   11967 C  CA     . SER   D 2  230 ? -10.242 0.626    -38.034 1.00 67.33  ? 230 SER   D CA     1 
ATOM   11968 C  C      . SER   D 2  230 ? -9.321  -0.051   -37.023 1.00 66.76  ? 230 SER   D C      1 
ATOM   11969 O  O      . SER   D 2  230 ? -9.585  -1.185   -36.610 1.00 63.32  ? 230 SER   D O      1 
ATOM   11970 C  CB     . SER   D 2  230 ? -9.778  0.328    -39.458 1.00 67.55  ? 230 SER   D CB     1 
ATOM   11971 O  OG     . SER   D 2  230 ? -8.382  0.516    -39.568 1.00 81.38  ? 230 SER   D OG     1 
ATOM   11972 N  N      . ALA   D 2  231 ? -8.244  0.616    -36.604 1.00 69.54  ? 231 ALA   D N      1 
ATOM   11973 C  CA     . ALA   D 2  231 ? -7.375  0.027    -35.586 1.00 71.56  ? 231 ALA   D CA     1 
ATOM   11974 C  C      . ALA   D 2  231 ? -8.087  -0.069   -34.240 1.00 71.69  ? 231 ALA   D C      1 
ATOM   11975 O  O      . ALA   D 2  231 ? -8.035  -1.109   -33.575 1.00 69.99  ? 231 ALA   D O      1 
ATOM   11976 C  CB     . ALA   D 2  231 ? -6.088  0.837    -35.454 1.00 75.49  ? 231 ALA   D CB     1 
ATOM   11977 N  N      . THR   D 2  232 ? -8.734  1.022    -33.814 1.00 68.27  ? 232 THR   D N      1 
ATOM   11978 C  CA     . THR   D 2  232 ? -9.611  1.007    -32.646 1.00 60.64  ? 232 THR   D CA     1 
ATOM   11979 C  C      . THR   D 2  232 ? -10.590 -0.159   -32.688 1.00 62.95  ? 232 THR   D C      1 
ATOM   11980 O  O      . THR   D 2  232 ? -10.603 -1.020   -31.801 1.00 62.10  ? 232 THR   D O      1 
ATOM   11981 C  CB     . THR   D 2  232 ? -10.381 2.328    -32.574 1.00 62.29  ? 232 THR   D CB     1 
ATOM   11982 O  OG1    . THR   D 2  232 ? -9.458  3.422    -32.522 1.00 68.55  ? 232 THR   D OG1    1 
ATOM   11983 C  CG2    . THR   D 2  232 ? -11.322 2.355    -31.377 1.00 53.14  ? 232 THR   D CG2    1 
ATOM   11984 N  N      . MET   D 2  233 ? -11.437 -0.183   -33.716 1.00 66.32  ? 233 MET   D N      1 
ATOM   11985 C  CA     . MET   D 2  233 ? -12.489 -1.185   -33.805 1.00 60.23  ? 233 MET   D CA     1 
ATOM   11986 C  C      . MET   D 2  233 ? -11.926 -2.595   -33.890 1.00 61.73  ? 233 MET   D C      1 
ATOM   11987 O  O      . MET   D 2  233 ? -12.450 -3.511   -33.246 1.00 60.39  ? 233 MET   D O      1 
ATOM   11988 C  CB     . MET   D 2  233 ? -13.377 -0.876   -34.996 1.00 58.85  ? 233 MET   D CB     1 
ATOM   11989 C  CG     . MET   D 2  233 ? -14.345 0.230    -34.726 1.00 62.64  ? 233 MET   D CG     1 
ATOM   11990 S  SD     . MET   D 2  233 ? -15.414 0.412    -36.161 1.00 74.55  ? 233 MET   D SD     1 
ATOM   11991 C  CE     . MET   D 2  233 ? -16.157 -1.211   -36.282 1.00 64.82  ? 233 MET   D CE     1 
ATOM   11992 N  N      . SER   D 2  234 ? -10.867 -2.806   -34.672 1.00 65.21  ? 234 SER   D N      1 
ATOM   11993 C  CA     . SER   D 2  234 ? -10.227 -4.119   -34.635 1.00 67.36  ? 234 SER   D CA     1 
ATOM   11994 C  C      . SER   D 2  234 ? -9.743  -4.452   -33.226 1.00 67.12  ? 234 SER   D C      1 
ATOM   11995 O  O      . SER   D 2  234 ? -9.649  -5.630   -32.859 1.00 66.15  ? 234 SER   D O      1 
ATOM   11996 C  CB     . SER   D 2  234 ? -9.060  -4.181   -35.624 1.00 60.52  ? 234 SER   D CB     1 
ATOM   11997 O  OG     . SER   D 2  234 ? -8.392  -5.428   -35.526 1.00 55.96  ? 234 SER   D OG     1 
ATOM   11998 N  N      . GLY   D 2  235 ? -9.429  -3.431   -32.431 1.00 62.35  ? 235 GLY   D N      1 
ATOM   11999 C  CA     . GLY   D 2  235 ? -8.937  -3.640   -31.091 1.00 60.46  ? 235 GLY   D CA     1 
ATOM   12000 C  C      . GLY   D 2  235 ? -10.015 -4.188   -30.182 1.00 67.45  ? 235 GLY   D C      1 
ATOM   12001 O  O      . GLY   D 2  235 ? -9.874  -5.284   -29.622 1.00 64.44  ? 235 GLY   D O      1 
ATOM   12002 N  N      . VAL   D 2  236 ? -11.121 -3.445   -30.063 1.00 63.67  ? 236 VAL   D N      1 
ATOM   12003 C  CA     . VAL   D 2  236 ? -12.130 -3.765   -29.063 1.00 56.39  ? 236 VAL   D CA     1 
ATOM   12004 C  C      . VAL   D 2  236 ? -12.935 -5.015   -29.405 1.00 58.01  ? 236 VAL   D C      1 
ATOM   12005 O  O      . VAL   D 2  236 ? -13.684 -5.510   -28.551 1.00 62.55  ? 236 VAL   D O      1 
ATOM   12006 C  CB     . VAL   D 2  236 ? -13.065 -2.556   -28.841 1.00 53.58  ? 236 VAL   D CB     1 
ATOM   12007 C  CG1    . VAL   D 2  236 ? -12.252 -1.310   -28.492 1.00 52.75  ? 236 VAL   D CG1    1 
ATOM   12008 C  CG2    . VAL   D 2  236 ? -14.035 -2.337   -30.001 1.00 53.51  ? 236 VAL   D CG2    1 
ATOM   12009 N  N      . THR   D 2  237 ? -12.809 -5.550   -30.620 1.00 57.58  ? 237 THR   D N      1 
ATOM   12010 C  CA     . THR   D 2  237 ? -13.486 -6.789   -30.978 1.00 56.72  ? 237 THR   D CA     1 
ATOM   12011 C  C      . THR   D 2  237 ? -12.550 -7.987   -30.922 1.00 57.74  ? 237 THR   D C      1 
ATOM   12012 O  O      . THR   D 2  237 ? -12.975 -9.100   -31.221 1.00 55.18  ? 237 THR   D O      1 
ATOM   12013 C  CB     . THR   D 2  237 ? -14.124 -6.693   -32.377 1.00 55.45  ? 237 THR   D CB     1 
ATOM   12014 O  OG1    . THR   D 2  237 ? -13.185 -6.191   -33.333 1.00 61.25  ? 237 THR   D OG1    1 
ATOM   12015 C  CG2    . THR   D 2  237 ? -15.292 -5.743   -32.349 1.00 56.12  ? 237 THR   D CG2    1 
ATOM   12016 N  N      . THR   D 2  238 ? -11.292 -7.788   -30.520 1.00 60.29  ? 238 THR   D N      1 
ATOM   12017 C  CA     . THR   D 2  238 ? -10.304 -8.862   -30.603 1.00 64.99  ? 238 THR   D CA     1 
ATOM   12018 C  C      . THR   D 2  238 ? -10.712 -10.065  -29.752 1.00 68.41  ? 238 THR   D C      1 
ATOM   12019 O  O      . THR   D 2  238 ? -10.611 -11.221  -30.192 1.00 64.14  ? 238 THR   D O      1 
ATOM   12020 C  CB     . THR   D 2  238 ? -8.938  -8.330   -30.177 1.00 61.68  ? 238 THR   D CB     1 
ATOM   12021 O  OG1    . THR   D 2  238 ? -8.611  -7.195   -30.984 1.00 63.09  ? 238 THR   D OG1    1 
ATOM   12022 C  CG2    . THR   D 2  238 ? -7.869  -9.381   -30.392 1.00 58.24  ? 238 THR   D CG2    1 
ATOM   12023 N  N      . CYS   D 2  239 ? -11.191 -9.816   -28.534 1.00 70.60  ? 239 CYS   D N      1 
ATOM   12024 C  CA     . CYS   D 2  239 ? -11.604 -10.903  -27.659 1.00 68.21  ? 239 CYS   D CA     1 
ATOM   12025 C  C      . CYS   D 2  239 ? -12.938 -11.505  -28.062 1.00 65.22  ? 239 CYS   D C      1 
ATOM   12026 O  O      . CYS   D 2  239 ? -13.337 -12.518  -27.483 1.00 67.69  ? 239 CYS   D O      1 
ATOM   12027 C  CB     . CYS   D 2  239 ? -11.668 -10.411  -26.218 1.00 66.75  ? 239 CYS   D CB     1 
ATOM   12028 S  SG     . CYS   D 2  239 ? -10.100 -9.752   -25.681 1.00 77.16  ? 239 CYS   D SG     1 
ATOM   12029 N  N      . LEU   D 2  240 ? -13.638 -10.904  -29.024 1.00 64.27  ? 240 LEU   D N      1 
ATOM   12030 C  CA     . LEU   D 2  240 ? -14.806 -11.557  -29.608 1.00 66.74  ? 240 LEU   D CA     1 
ATOM   12031 C  C      . LEU   D 2  240 ? -14.390 -12.520  -30.724 1.00 68.28  ? 240 LEU   D C      1 
ATOM   12032 O  O      . LEU   D 2  240 ? -14.823 -13.678  -30.755 1.00 62.55  ? 240 LEU   D O      1 
ATOM   12033 C  CB     . LEU   D 2  240 ? -15.789 -10.502  -30.135 1.00 55.64  ? 240 LEU   D CB     1 
ATOM   12034 C  CG     . LEU   D 2  240 ? -16.118 -9.306   -29.237 1.00 51.65  ? 240 LEU   D CG     1 
ATOM   12035 C  CD1    . LEU   D 2  240 ? -16.958 -8.300   -29.968 1.00 47.52  ? 240 LEU   D CD1    1 
ATOM   12036 C  CD2    . LEU   D 2  240 ? -16.832 -9.750   -27.995 1.00 56.65  ? 240 LEU   D CD2    1 
ATOM   12037 N  N      . ARG   D 2  241 ? -13.521 -12.053  -31.630 1.00 73.26  ? 241 ARG   D N      1 
ATOM   12038 C  CA     . ARG   D 2  241 ? -13.161 -12.790  -32.839 1.00 71.08  ? 241 ARG   D CA     1 
ATOM   12039 C  C      . ARG   D 2  241 ? -12.195 -13.943  -32.556 1.00 75.67  ? 241 ARG   D C      1 
ATOM   12040 O  O      . ARG   D 2  241 ? -12.302 -15.013  -33.172 1.00 73.58  ? 241 ARG   D O      1 
ATOM   12041 C  CB     . ARG   D 2  241 ? -12.562 -11.811  -33.847 1.00 58.12  ? 241 ARG   D CB     1 
ATOM   12042 C  CG     . ARG   D 2  241 ? -13.467 -10.649  -34.175 1.00 58.08  ? 241 ARG   D CG     1 
ATOM   12043 C  CD     . ARG   D 2  241 ? -12.899 -9.849   -35.316 1.00 61.60  ? 241 ARG   D CD     1 
ATOM   12044 N  NE     . ARG   D 2  241 ? -12.031 -8.783   -34.838 1.00 61.43  ? 241 ARG   D NE     1 
ATOM   12045 C  CZ     . ARG   D 2  241 ? -10.707 -8.833   -34.858 1.00 64.41  ? 241 ARG   D CZ     1 
ATOM   12046 N  NH1    . ARG   D 2  241 ? -10.063 -9.922   -35.239 1.00 65.74  ? 241 ARG   D NH1    1 
ATOM   12047 N  NH2    . ARG   D 2  241 ? -10.012 -7.774   -34.456 1.00 65.10  ? 241 ARG   D NH2    1 
ATOM   12048 N  N      . PHE   D 2  242 ? -11.257 -13.759  -31.642 1.00 70.25  ? 242 PHE   D N      1 
ATOM   12049 C  CA     . PHE   D 2  242 ? -10.289 -14.803  -31.393 1.00 69.04  ? 242 PHE   D CA     1 
ATOM   12050 C  C      . PHE   D 2  242 ? -10.571 -15.471  -30.064 1.00 79.53  ? 242 PHE   D C      1 
ATOM   12051 O  O      . PHE   D 2  242 ? -11.215 -14.890  -29.185 1.00 84.91  ? 242 PHE   D O      1 
ATOM   12052 C  CB     . PHE   D 2  242 ? -8.867  -14.244  -31.387 1.00 71.89  ? 242 PHE   D CB     1 
ATOM   12053 C  CG     . PHE   D 2  242 ? -8.431  -13.703  -32.708 1.00 72.65  ? 242 PHE   D CG     1 
ATOM   12054 C  CD1    . PHE   D 2  242 ? -7.974  -14.551  -33.696 1.00 72.58  ? 242 PHE   D CD1    1 
ATOM   12055 C  CD2    . PHE   D 2  242 ? -8.477  -12.338  -32.958 1.00 69.53  ? 242 PHE   D CD2    1 
ATOM   12056 C  CE1    . PHE   D 2  242 ? -7.582  -14.054  -34.904 1.00 73.99  ? 242 PHE   D CE1    1 
ATOM   12057 C  CE2    . PHE   D 2  242 ? -8.088  -11.833  -34.164 1.00 68.82  ? 242 PHE   D CE2    1 
ATOM   12058 C  CZ     . PHE   D 2  242 ? -7.638  -12.689  -35.141 1.00 75.49  ? 242 PHE   D CZ     1 
ATOM   12059 N  N      . PRO   D 2  243 ? -10.104 -16.693  -29.881 1.00 83.07  ? 243 PRO   D N      1 
ATOM   12060 C  CA     . PRO   D 2  243 ? -10.278 -17.368  -28.589 1.00 86.38  ? 243 PRO   D CA     1 
ATOM   12061 C  C      . PRO   D 2  243 ? -9.563  -16.602  -27.481 1.00 89.91  ? 243 PRO   D C      1 
ATOM   12062 O  O      . PRO   D 2  243 ? -9.170  -15.446  -27.685 1.00 93.77  ? 243 PRO   D O      1 
ATOM   12063 C  CB     . PRO   D 2  243 ? -9.653  -18.751  -28.829 1.00 84.65  ? 243 PRO   D CB     1 
ATOM   12064 C  CG     . PRO   D 2  243 ? -9.460  -18.848  -30.326 1.00 79.71  ? 243 PRO   D CG     1 
ATOM   12065 C  CD     . PRO   D 2  243 ? -9.271  -17.467  -30.812 1.00 81.58  ? 243 PRO   D CD     1 
ATOM   12066 N  N      . GLY   D 2  244 ? -9.375  -17.214  -26.318 1.00 80.99  ? 244 GLY   D N      1 
ATOM   12067 C  CA     . GLY   D 2  244 ? -8.616  -16.560  -25.269 1.00 88.93  ? 244 GLY   D CA     1 
ATOM   12068 C  C      . GLY   D 2  244 ? -8.934  -17.176  -23.928 1.00 93.82  ? 244 GLY   D C      1 
ATOM   12069 O  O      . GLY   D 2  244 ? -9.756  -18.095  -23.827 1.00 95.27  ? 244 GLY   D O      1 
ATOM   12070 N  N      . GLN   D 2  245 ? -8.261  -16.657  -22.884 1.00 97.13  ? 245 GLN   D N      1 
ATOM   12071 C  CA     . GLN   D 2  245 ? -8.501  -17.226  -21.558 1.00 86.55  ? 245 GLN   D CA     1 
ATOM   12072 C  C      . GLN   D 2  245 ? -9.949  -16.983  -21.169 1.00 89.72  ? 245 GLN   D C      1 
ATOM   12073 O  O      . GLN   D 2  245 ? -10.601 -17.865  -20.594 1.00 99.47  ? 245 GLN   D O      1 
ATOM   12074 C  CB     . GLN   D 2  245 ? -7.547  -16.668  -20.480 1.00 75.67  ? 245 GLN   D CB     1 
ATOM   12075 C  CG     . GLN   D 2  245 ? -7.355  -17.673  -19.262 1.00 83.59  ? 245 GLN   D CG     1 
ATOM   12076 C  CD     . GLN   D 2  245 ? -6.492  -17.194  -18.023 1.00 81.11  ? 245 GLN   D CD     1 
ATOM   12077 O  OE1    . GLN   D 2  245 ? -6.549  -16.032  -17.597 1.00 81.32  ? 245 GLN   D OE1    1 
ATOM   12078 N  NE2    . GLN   D 2  245 ? -5.653  -18.107  -17.499 1.00 70.45  ? 245 GLN   D NE2    1 
ATOM   12079 N  N      . LEU   D 2  246 ? -10.493 -15.817  -21.538 1.00 76.11  ? 246 LEU   D N      1 
ATOM   12080 C  CA     . LEU   D 2  246 ? -11.880 -15.482  -21.250 1.00 79.96  ? 246 LEU   D CA     1 
ATOM   12081 C  C      . LEU   D 2  246 ? -12.751 -15.626  -22.493 1.00 80.05  ? 246 LEU   D C      1 
ATOM   12082 O  O      . LEU   D 2  246 ? -12.287 -15.475  -23.626 1.00 85.55  ? 246 LEU   D O      1 
ATOM   12083 C  CB     . LEU   D 2  246 ? -12.002 -14.073  -20.649 1.00 76.00  ? 246 LEU   D CB     1 
ATOM   12084 C  CG     . LEU   D 2  246 ? -11.545 -12.763  -21.302 1.00 72.69  ? 246 LEU   D CG     1 
ATOM   12085 C  CD1    . LEU   D 2  246 ? -12.640 -12.131  -22.095 1.00 78.08  ? 246 LEU   D CD1    1 
ATOM   12086 C  CD2    . LEU   D 2  246 ? -11.118 -11.791  -20.214 1.00 60.14  ? 246 LEU   D CD2    1 
ATOM   12087 N  N      . ASN   D 2  247 ? -14.023 -15.948  -22.264 1.00 80.38  ? 247 ASN   D N      1 
ATOM   12088 C  CA     . ASN   D 2  247 ? -14.972 -16.244  -23.342 1.00 84.49  ? 247 ASN   D CA     1 
ATOM   12089 C  C      . ASN   D 2  247 ? -15.729 -14.975  -23.740 1.00 74.77  ? 247 ASN   D C      1 
ATOM   12090 O  O      . ASN   D 2  247 ? -16.939 -14.859  -23.548 1.00 78.96  ? 247 ASN   D O      1 
ATOM   12091 C  CB     . ASN   D 2  247 ? -15.949 -17.341  -22.907 1.00 88.85  ? 247 ASN   D CB     1 
ATOM   12092 C  CG     . ASN   D 2  247 ? -15.439 -18.762  -23.187 1.00 88.47  ? 247 ASN   D CG     1 
ATOM   12093 O  OD1    . ASN   D 2  247 ? -15.128 -19.116  -24.337 1.00 93.89  ? 247 ASN   D OD1    1 
ATOM   12094 N  ND2    . ASN   D 2  247 ? -15.395 -19.595  -22.138 1.00 78.72  ? 247 ASN   D ND2    1 
ATOM   12095 N  N      . ALA   D 2  248 ? -15.001 -14.015  -24.300 1.00 61.87  ? 248 ALA   D N      1 
ATOM   12096 C  CA     . ALA   D 2  248 ? -15.563 -12.684  -24.468 1.00 59.26  ? 248 ALA   D CA     1 
ATOM   12097 C  C      . ALA   D 2  248 ? -16.789 -12.717  -25.363 1.00 56.02  ? 248 ALA   D C      1 
ATOM   12098 O  O      . ALA   D 2  248 ? -16.859 -13.507  -26.303 1.00 61.03  ? 248 ALA   D O      1 
ATOM   12099 C  CB     . ALA   D 2  248 ? -14.521 -11.742  -25.048 1.00 68.53  ? 248 ALA   D CB     1 
ATOM   12100 N  N      . ASP   D 2  249 ? -17.771 -11.872  -25.044 1.00 52.09  ? 249 ASP   D N      1 
ATOM   12101 C  CA     . ASP   D 2  249 ? -18.923 -11.637  -25.911 1.00 48.28  ? 249 ASP   D CA     1 
ATOM   12102 C  C      . ASP   D 2  249 ? -19.632 -10.356  -25.482 1.00 51.25  ? 249 ASP   D C      1 
ATOM   12103 O  O      . ASP   D 2  249 ? -19.323 -9.754   -24.448 1.00 50.75  ? 249 ASP   D O      1 
ATOM   12104 C  CB     . ASP   D 2  249 ? -19.891 -12.822  -25.909 1.00 48.15  ? 249 ASP   D CB     1 
ATOM   12105 C  CG     . ASP   D 2  249 ? -20.457 -13.124  -24.542 1.00 47.56  ? 249 ASP   D CG     1 
ATOM   12106 O  OD1    . ASP   D 2  249 ? -20.909 -12.198  -23.840 1.00 46.90  ? 249 ASP   D OD1    1 
ATOM   12107 O  OD2    . ASP   D 2  249 ? -20.452 -14.310  -24.159 1.00 61.41  ? 249 ASP   D OD2    1 
ATOM   12108 N  N      . LEU   D 2  250 ? -20.617 -9.962   -26.284 1.00 43.20  ? 250 LEU   D N      1 
ATOM   12109 C  CA     . LEU   D 2  250 ? -21.220 -8.649   -26.103 1.00 45.77  ? 250 LEU   D CA     1 
ATOM   12110 C  C      . LEU   D 2  250 ? -21.878 -8.500   -24.737 1.00 47.71  ? 250 LEU   D C      1 
ATOM   12111 O  O      . LEU   D 2  250 ? -21.930 -7.387   -24.191 1.00 49.21  ? 250 LEU   D O      1 
ATOM   12112 C  CB     . LEU   D 2  250 ? -22.224 -8.387   -27.231 1.00 51.22  ? 250 LEU   D CB     1 
ATOM   12113 C  CG     . LEU   D 2  250 ? -21.611 -8.102   -28.612 1.00 48.88  ? 250 LEU   D CG     1 
ATOM   12114 C  CD1    . LEU   D 2  250 ? -22.684 -8.095   -29.625 1.00 50.28  ? 250 LEU   D CD1    1 
ATOM   12115 C  CD2    . LEU   D 2  250 ? -20.873 -6.787   -28.647 1.00 48.10  ? 250 LEU   D CD2    1 
ATOM   12116 N  N      . ARG   D 2  251 ? -22.375 -9.594   -24.156 1.00 44.39  ? 251 ARG   D N      1 
ATOM   12117 C  CA     . ARG   D 2  251 ? -23.126 -9.476   -22.909 1.00 44.74  ? 251 ARG   D CA     1 
ATOM   12118 C  C      . ARG   D 2  251 ? -22.177 -9.362   -21.714 1.00 46.22  ? 251 ARG   D C      1 
ATOM   12119 O  O      . ARG   D 2  251 ? -22.342 -8.502   -20.835 1.00 39.20  ? 251 ARG   D O      1 
ATOM   12120 C  CB     . ARG   D 2  251 ? -24.034 -10.687  -22.756 1.00 38.59  ? 251 ARG   D CB     1 
ATOM   12121 C  CG     . ARG   D 2  251 ? -25.081 -10.625  -21.660 1.00 38.71  ? 251 ARG   D CG     1 
ATOM   12122 C  CD     . ARG   D 2  251 ? -26.045 -11.810  -21.850 1.00 43.69  ? 251 ARG   D CD     1 
ATOM   12123 N  NE     . ARG   D 2  251 ? -27.133 -11.547  -22.786 1.00 40.57  ? 251 ARG   D NE     1 
ATOM   12124 C  CZ     . ARG   D 2  251 ? -27.965 -10.517  -22.716 1.00 48.65  ? 251 ARG   D CZ     1 
ATOM   12125 N  NH1    . ARG   D 2  251 ? -27.850 -9.591   -21.782 1.00 51.84  ? 251 ARG   D NH1    1 
ATOM   12126 N  NH2    . ARG   D 2  251 ? -28.948 -10.420  -23.600 1.00 58.01  ? 251 ARG   D NH2    1 
ATOM   12127 N  N      . LYS   D 2  252 ? -21.163 -10.223  -21.678 1.00 44.05  ? 252 LYS   D N      1 
ATOM   12128 C  CA     . LYS   D 2  252 ? -20.208 -10.188  -20.579 1.00 44.28  ? 252 LYS   D CA     1 
ATOM   12129 C  C      . LYS   D 2  252 ? -19.459 -8.859   -20.549 1.00 46.55  ? 252 LYS   D C      1 
ATOM   12130 O  O      . LYS   D 2  252 ? -19.191 -8.310   -19.477 1.00 45.51  ? 252 LYS   D O      1 
ATOM   12131 C  CB     . LYS   D 2  252 ? -19.250 -11.359  -20.722 1.00 40.94  ? 252 LYS   D CB     1 
ATOM   12132 C  CG     . LYS   D 2  252 ? -19.805 -12.696  -20.290 1.00 41.04  ? 252 LYS   D CG     1 
ATOM   12133 C  CD     . LYS   D 2  252 ? -18.832 -13.770  -20.753 1.00 48.21  ? 252 LYS   D CD     1 
ATOM   12134 C  CE     . LYS   D 2  252 ? -19.127 -15.145  -20.235 1.00 48.35  ? 252 LYS   D CE     1 
ATOM   12135 N  NZ     . LYS   D 2  252 ? -18.015 -16.038  -20.650 1.00 58.29  ? 252 LYS   D NZ     1 
ATOM   12136 N  N      . LEU   D 2  253 ? -19.107 -8.325   -21.715 1.00 47.24  ? 253 LEU   D N      1 
ATOM   12137 C  CA     . LEU   D 2  253 ? -18.506 -6.997   -21.754 1.00 49.60  ? 253 LEU   D CA     1 
ATOM   12138 C  C      . LEU   D 2  253 ? -19.417 -5.968   -21.098 1.00 41.53  ? 253 LEU   D C      1 
ATOM   12139 O  O      . LEU   D 2  253 ? -18.981 -5.192   -20.246 1.00 36.69  ? 253 LEU   D O      1 
ATOM   12140 C  CB     . LEU   D 2  253 ? -18.214 -6.603   -23.199 1.00 55.78  ? 253 LEU   D CB     1 
ATOM   12141 C  CG     . LEU   D 2  253 ? -17.680 -5.190   -23.394 1.00 52.55  ? 253 LEU   D CG     1 
ATOM   12142 C  CD1    . LEU   D 2  253 ? -16.212 -5.105   -22.924 1.00 49.84  ? 253 LEU   D CD1    1 
ATOM   12143 C  CD2    . LEU   D 2  253 ? -17.881 -4.745   -24.843 1.00 51.36  ? 253 LEU   D CD2    1 
ATOM   12144 N  N      . ALA   D 2  254 ? -20.701 -5.969   -21.470 1.00 48.47  ? 254 ALA   D N      1 
ATOM   12145 C  CA     . ALA   D 2  254 ? -21.656 -4.999   -20.925 1.00 49.18  ? 254 ALA   D CA     1 
ATOM   12146 C  C      . ALA   D 2  254 ? -21.888 -5.192   -19.423 1.00 43.55  ? 254 ALA   D C      1 
ATOM   12147 O  O      . ALA   D 2  254 ? -21.967 -4.208   -18.680 1.00 41.21  ? 254 ALA   D O      1 
ATOM   12148 C  CB     . ALA   D 2  254 ? -22.976 -5.087   -21.690 1.00 43.77  ? 254 ALA   D CB     1 
ATOM   12149 N  N      . VAL   D 2  255 ? -21.993 -6.449   -18.958 1.00 44.62  ? 255 VAL   D N      1 
ATOM   12150 C  CA     . VAL   D 2  255 ? -22.126 -6.738   -17.524 1.00 41.44  ? 255 VAL   D CA     1 
ATOM   12151 C  C      . VAL   D 2  255 ? -20.937 -6.195   -16.726 1.00 43.60  ? 255 VAL   D C      1 
ATOM   12152 O  O      . VAL   D 2  255 ? -21.098 -5.479   -15.730 1.00 38.89  ? 255 VAL   D O      1 
ATOM   12153 C  CB     . VAL   D 2  255 ? -22.277 -8.246   -17.295 1.00 37.85  ? 255 VAL   D CB     1 
ATOM   12154 C  CG1    . VAL   D 2  255 ? -22.263 -8.512   -15.825 1.00 44.05  ? 255 VAL   D CG1    1 
ATOM   12155 C  CG2    . VAL   D 2  255 ? -23.550 -8.725   -17.872 1.00 42.95  ? 255 VAL   D CG2    1 
ATOM   12156 N  N      . ASN   D 2  256 ? -19.728 -6.568   -17.121 1.00 42.72  ? 256 ASN   D N      1 
ATOM   12157 C  CA     . ASN   D 2  256 ? -18.552 -6.142   -16.381 1.00 45.13  ? 256 ASN   D CA     1 
ATOM   12158 C  C      . ASN   D 2  256 ? -18.223 -4.658   -16.557 1.00 44.82  ? 256 ASN   D C      1 
ATOM   12159 O  O      . ASN   D 2  256 ? -17.559 -4.085   -15.681 1.00 40.27  ? 256 ASN   D O      1 
ATOM   12160 C  CB     . ASN   D 2  256 ? -17.379 -7.043   -16.784 1.00 41.51  ? 256 ASN   D CB     1 
ATOM   12161 C  CG     . ASN   D 2  256 ? -17.558 -8.461   -16.283 1.00 45.14  ? 256 ASN   D CG     1 
ATOM   12162 O  OD1    . ASN   D 2  256 ? -17.520 -8.712   -15.084 1.00 48.58  ? 256 ASN   D OD1    1 
ATOM   12163 N  ND2    . ASN   D 2  256 ? -17.906 -9.359   -17.179 1.00 43.46  ? 256 ASN   D ND2    1 
ATOM   12164 N  N      . MET   D 2  257 ? -18.695 -4.010   -17.630 1.00 43.07  ? 257 MET   D N      1 
ATOM   12165 C  CA     . MET   D 2  257 ? -18.335 -2.620   -17.891 1.00 39.56  ? 257 MET   D CA     1 
ATOM   12166 C  C      . MET   D 2  257 ? -19.397 -1.633   -17.461 1.00 38.40  ? 257 MET   D C      1 
ATOM   12167 O  O      . MET   D 2  257 ? -19.058 -0.504   -17.120 1.00 42.35  ? 257 MET   D O      1 
ATOM   12168 C  CB     . MET   D 2  257 ? -18.050 -2.369   -19.380 1.00 40.94  ? 257 MET   D CB     1 
ATOM   12169 C  CG     . MET   D 2  257 ? -16.809 -3.052   -19.918 1.00 41.61  ? 257 MET   D CG     1 
ATOM   12170 S  SD     . MET   D 2  257 ? -15.259 -2.461   -19.228 1.00 47.16  ? 257 MET   D SD     1 
ATOM   12171 C  CE     . MET   D 2  257 ? -15.151 -0.809   -19.864 1.00 44.89  ? 257 MET   D CE     1 
ATOM   12172 N  N      . VAL   D 2  258 ? -20.671 -1.994   -17.477 1.00 38.78  ? 258 VAL   D N      1 
ATOM   12173 C  CA     . VAL   D 2  258 ? -21.680 -0.963   -17.249 1.00 39.47  ? 258 VAL   D CA     1 
ATOM   12174 C  C      . VAL   D 2  258 ? -22.217 -1.073   -15.832 1.00 40.45  ? 258 VAL   D C      1 
ATOM   12175 O  O      . VAL   D 2  258 ? -23.141 -1.855   -15.570 1.00 41.12  ? 258 VAL   D O      1 
ATOM   12176 C  CB     . VAL   D 2  258 ? -22.803 -1.034   -18.287 1.00 36.06  ? 258 VAL   D CB     1 
ATOM   12177 C  CG1    . VAL   D 2  258 ? -23.811 0.016    -18.000 1.00 38.18  ? 258 VAL   D CG1    1 
ATOM   12178 C  CG2    . VAL   D 2  258 ? -22.215 -0.809   -19.652 1.00 38.81  ? 258 VAL   D CG2    1 
ATOM   12179 N  N      . PRO   D 2  259 ? -21.675 -0.291   -14.897 1.00 38.14  ? 259 PRO   D N      1 
ATOM   12180 C  CA     . PRO   D 2  259 ? -22.128 -0.386   -13.506 1.00 37.67  ? 259 PRO   D CA     1 
ATOM   12181 C  C      . PRO   D 2  259 ? -23.467 0.263    -13.275 1.00 40.11  ? 259 PRO   D C      1 
ATOM   12182 O  O      . PRO   D 2  259 ? -24.043 0.085    -12.196 1.00 40.39  ? 259 PRO   D O      1 
ATOM   12183 C  CB     . PRO   D 2  259 ? -21.039 0.365    -12.735 1.00 39.49  ? 259 PRO   D CB     1 
ATOM   12184 C  CG     . PRO   D 2  259 ? -20.545 1.363    -13.727 1.00 38.15  ? 259 PRO   D CG     1 
ATOM   12185 C  CD     . PRO   D 2  259 ? -20.591 0.688    -15.063 1.00 36.12  ? 259 PRO   D CD     1 
ATOM   12186 N  N      . PHE   D 2  260 ? -23.950 1.059    -14.223 1.00 42.17  ? 260 PHE   D N      1 
ATOM   12187 C  CA     . PHE   D 2  260 ? -25.248 1.674    -14.145 1.00 40.41  ? 260 PHE   D CA     1 
ATOM   12188 C  C      . PHE   D 2  260 ? -25.714 1.781    -15.579 1.00 43.22  ? 260 PHE   D C      1 
ATOM   12189 O  O      . PHE   D 2  260 ? -24.919 2.171    -16.445 1.00 46.03  ? 260 PHE   D O      1 
ATOM   12190 C  CB     . PHE   D 2  260 ? -25.210 3.034    -13.454 1.00 37.86  ? 260 PHE   D CB     1 
ATOM   12191 C  CG     . PHE   D 2  260 ? -24.552 2.985    -12.110 1.00 43.39  ? 260 PHE   D CG     1 
ATOM   12192 C  CD1    . PHE   D 2  260 ? -25.253 2.526    -11.004 1.00 42.15  ? 260 PHE   D CD1    1 
ATOM   12193 C  CD2    . PHE   D 2  260 ? -23.243 3.389    -11.943 1.00 49.99  ? 260 PHE   D CD2    1 
ATOM   12194 C  CE1    . PHE   D 2  260 ? -24.658 2.448    -9.773  1.00 40.79  ? 260 PHE   D CE1    1 
ATOM   12195 C  CE2    . PHE   D 2  260 ? -22.639 3.331    -10.683 1.00 47.83  ? 260 PHE   D CE2    1 
ATOM   12196 C  CZ     . PHE   D 2  260 ? -23.347 2.857    -9.608  1.00 43.82  ? 260 PHE   D CZ     1 
ATOM   12197 N  N      . PRO   D 2  261 ? -26.966 1.431    -15.870 1.00 46.97  ? 261 PRO   D N      1 
ATOM   12198 C  CA     . PRO   D 2  261 ? -27.337 1.180    -17.277 1.00 47.98  ? 261 PRO   D CA     1 
ATOM   12199 C  C      . PRO   D 2  261 ? -27.122 2.378    -18.194 1.00 47.79  ? 261 PRO   D C      1 
ATOM   12200 O  O      . PRO   D 2  261 ? -26.745 2.182    -19.357 1.00 48.91  ? 261 PRO   D O      1 
ATOM   12201 C  CB     . PRO   D 2  261 ? -28.818 0.778    -17.194 1.00 40.35  ? 261 PRO   D CB     1 
ATOM   12202 C  CG     . PRO   D 2  261 ? -29.212 0.865    -15.772 1.00 37.48  ? 261 PRO   D CG     1 
ATOM   12203 C  CD     . PRO   D 2  261 ? -28.135 1.551    -14.990 1.00 39.94  ? 261 PRO   D CD     1 
ATOM   12204 N  N      . ARG   D 2  262 ? -27.335 3.608    -17.703 1.00 42.68  ? 262 ARG   D N      1 
ATOM   12205 C  CA     . ARG   D 2  262 ? -27.177 4.789    -18.547 1.00 45.71  ? 262 ARG   D CA     1 
ATOM   12206 C  C      . ARG   D 2  262 ? -25.716 5.089    -18.854 1.00 46.93  ? 262 ARG   D C      1 
ATOM   12207 O  O      . ARG   D 2  262 ? -25.393 5.484    -19.976 1.00 49.33  ? 262 ARG   D O      1 
ATOM   12208 C  CB     . ARG   D 2  262 ? -27.836 5.994    -17.888 1.00 46.87  ? 262 ARG   D CB     1 
ATOM   12209 C  CG     . ARG   D 2  262 ? -29.316 5.850    -17.855 1.00 46.11  ? 262 ARG   D CG     1 
ATOM   12210 C  CD     . ARG   D 2  262 ? -29.952 6.830    -16.941 1.00 51.25  ? 262 ARG   D CD     1 
ATOM   12211 N  NE     . ARG   D 2  262 ? -29.414 8.161    -17.140 1.00 58.11  ? 262 ARG   D NE     1 
ATOM   12212 C  CZ     . ARG   D 2  262 ? -29.880 8.999    -18.052 1.00 69.34  ? 262 ARG   D CZ     1 
ATOM   12213 N  NH1    . ARG   D 2  262 ? -30.832 8.633    -18.904 1.00 67.55  ? 262 ARG   D NH1    1 
ATOM   12214 N  NH2    . ARG   D 2  262 ? -29.374 10.229   -18.120 1.00 65.24  ? 262 ARG   D NH2    1 
ATOM   12215 N  N      . LEU   D 2  263 ? -24.822 4.936    -17.872 1.00 49.44  ? 263 LEU   D N      1 
ATOM   12216 C  CA     . LEU   D 2  263 ? -23.395 5.245    -18.030 1.00 46.49  ? 263 LEU   D CA     1 
ATOM   12217 C  C      . LEU   D 2  263 ? -22.699 4.120    -18.794 1.00 48.45  ? 263 LEU   D C      1 
ATOM   12218 O  O      . LEU   D 2  263 ? -21.906 3.345    -18.250 1.00 46.71  ? 263 LEU   D O      1 
ATOM   12219 C  CB     . LEU   D 2  263 ? -22.741 5.459    -16.679 1.00 42.70  ? 263 LEU   D CB     1 
ATOM   12220 C  CG     . LEU   D 2  263 ? -23.485 6.398    -15.746 1.00 44.34  ? 263 LEU   D CG     1 
ATOM   12221 C  CD1    . LEU   D 2  263 ? -22.572 6.743    -14.612 1.00 51.11  ? 263 LEU   D CD1    1 
ATOM   12222 C  CD2    . LEU   D 2  263 ? -23.857 7.641    -16.494 1.00 48.55  ? 263 LEU   D CD2    1 
ATOM   12223 N  N      . HIS   D 2  264 ? -23.004 4.058    -20.095 1.00 46.36  ? 264 HIS   D N      1 
ATOM   12224 C  CA     . HIS   D 2  264 ? -22.507 3.008    -20.966 1.00 46.11  ? 264 HIS   D CA     1 
ATOM   12225 C  C      . HIS   D 2  264 ? -21.762 3.561    -22.176 1.00 53.33  ? 264 HIS   D C      1 
ATOM   12226 O  O      . HIS   D 2  264 ? -21.816 2.964    -23.262 1.00 52.98  ? 264 HIS   D O      1 
ATOM   12227 C  CB     . HIS   D 2  264 ? -23.650 2.098    -21.412 1.00 48.40  ? 264 HIS   D CB     1 
ATOM   12228 C  CG     . HIS   D 2  264 ? -24.714 2.777    -22.211 1.00 52.04  ? 264 HIS   D CG     1 
ATOM   12229 N  ND1    . HIS   D 2  264 ? -25.902 3.211    -21.659 1.00 55.19  ? 264 HIS   D ND1    1 
ATOM   12230 C  CD2    . HIS   D 2  264 ? -24.809 3.015    -23.541 1.00 53.80  ? 264 HIS   D CD2    1 
ATOM   12231 C  CE1    . HIS   D 2  264 ? -26.661 3.732    -22.607 1.00 52.88  ? 264 HIS   D CE1    1 
ATOM   12232 N  NE2    . HIS   D 2  264 ? -26.021 3.625    -23.758 1.00 53.35  ? 264 HIS   D NE2    1 
ATOM   12233 N  N      . PHE   D 2  265 ? -21.055 4.686    -22.012 1.00 48.88  ? 265 PHE   D N      1 
ATOM   12234 C  CA     . PHE   D 2  265 ? -20.346 5.324    -23.118 1.00 48.35  ? 265 PHE   D CA     1 
ATOM   12235 C  C      . PHE   D 2  265 ? -18.845 5.263    -22.854 1.00 52.99  ? 265 PHE   D C      1 
ATOM   12236 O  O      . PHE   D 2  265 ? -18.364 5.781    -21.835 1.00 57.95  ? 265 PHE   D O      1 
ATOM   12237 C  CB     . PHE   D 2  265 ? -20.813 6.765    -23.332 1.00 47.14  ? 265 PHE   D CB     1 
ATOM   12238 C  CG     . PHE   D 2  265 ? -22.269 6.877    -23.624 1.00 51.18  ? 265 PHE   D CG     1 
ATOM   12239 C  CD1    . PHE   D 2  265 ? -22.740 6.673    -24.903 1.00 53.20  ? 265 PHE   D CD1    1 
ATOM   12240 C  CD2    . PHE   D 2  265 ? -23.159 7.260    -22.645 1.00 53.87  ? 265 PHE   D CD2    1 
ATOM   12241 C  CE1    . PHE   D 2  265 ? -24.081 6.759    -25.176 1.00 54.03  ? 265 PHE   D CE1    1 
ATOM   12242 C  CE2    . PHE   D 2  265 ? -24.505 7.371    -22.922 1.00 53.01  ? 265 PHE   D CE2    1 
ATOM   12243 C  CZ     . PHE   D 2  265 ? -24.963 7.121    -24.182 1.00 52.76  ? 265 PHE   D CZ     1 
ATOM   12244 N  N      . PHE   D 2  266 ? -18.100 4.659    -23.778 1.00 42.83  ? 266 PHE   D N      1 
ATOM   12245 C  CA     . PHE   D 2  266 ? -16.722 4.279    -23.514 1.00 44.30  ? 266 PHE   D CA     1 
ATOM   12246 C  C      . PHE   D 2  266 ? -15.735 5.145    -24.285 1.00 47.86  ? 266 PHE   D C      1 
ATOM   12247 O  O      . PHE   D 2  266 ? -15.911 5.391    -25.478 1.00 52.35  ? 266 PHE   D O      1 
ATOM   12248 C  CB     . PHE   D 2  266 ? -16.468 2.817    -23.887 1.00 46.75  ? 266 PHE   D CB     1 
ATOM   12249 C  CG     . PHE   D 2  266 ? -17.432 1.848    -23.265 1.00 45.78  ? 266 PHE   D CG     1 
ATOM   12250 C  CD1    . PHE   D 2  266 ? -18.093 2.162    -22.091 1.00 44.53  ? 266 PHE   D CD1    1 
ATOM   12251 C  CD2    . PHE   D 2  266 ? -17.651 0.605    -23.846 1.00 44.82  ? 266 PHE   D CD2    1 
ATOM   12252 C  CE1    . PHE   D 2  266 ? -18.974 1.268    -21.528 1.00 48.66  ? 266 PHE   D CE1    1 
ATOM   12253 C  CE2    . PHE   D 2  266 ? -18.523 -0.296   -23.286 1.00 42.10  ? 266 PHE   D CE2    1 
ATOM   12254 C  CZ     . PHE   D 2  266 ? -19.186 0.031    -22.125 1.00 46.61  ? 266 PHE   D CZ     1 
ATOM   12255 N  N      . MET   D 2  267 ? -14.673 5.553    -23.603 1.00 46.40  ? 267 MET   D N      1 
ATOM   12256 C  CA     . MET   D 2  267 ? -13.476 6.148    -24.182 1.00 42.20  ? 267 MET   D CA     1 
ATOM   12257 C  C      . MET   D 2  267 ? -12.585 5.037    -24.704 1.00 46.16  ? 267 MET   D C      1 
ATOM   12258 O  O      . MET   D 2  267 ? -12.003 4.289    -23.909 1.00 47.84  ? 267 MET   D O      1 
ATOM   12259 C  CB     . MET   D 2  267 ? -12.697 6.935    -23.137 1.00 40.41  ? 267 MET   D CB     1 
ATOM   12260 C  CG     . MET   D 2  267 ? -12.886 8.424    -23.155 1.00 55.09  ? 267 MET   D CG     1 
ATOM   12261 S  SD     . MET   D 2  267 ? -11.707 9.148    -22.002 1.00 70.81  ? 267 MET   D SD     1 
ATOM   12262 C  CE     . MET   D 2  267 ? -10.323 8.059    -22.294 1.00 53.26  ? 267 MET   D CE     1 
ATOM   12263 N  N      . PRO   D 2  268 ? -12.455 4.875    -26.010 1.00 48.03  ? 268 PRO   D N      1 
ATOM   12264 C  CA     . PRO   D 2  268 ? -11.499 3.901    -26.549 1.00 46.19  ? 268 PRO   D CA     1 
ATOM   12265 C  C      . PRO   D 2  268 ? -10.093 4.480    -26.663 1.00 50.83  ? 268 PRO   D C      1 
ATOM   12266 O  O      . PRO   D 2  268 ? -9.889  5.690    -26.753 1.00 54.55  ? 268 PRO   D O      1 
ATOM   12267 C  CB     . PRO   D 2  268 ? -12.071 3.574    -27.937 1.00 48.93  ? 268 PRO   D CB     1 
ATOM   12268 C  CG     . PRO   D 2  268 ? -13.456 4.209    -27.962 1.00 55.29  ? 268 PRO   D CG     1 
ATOM   12269 C  CD     . PRO   D 2  268 ? -13.386 5.365    -27.031 1.00 48.86  ? 268 PRO   D CD     1 
ATOM   12270 N  N      . GLY   D 2  269 ? -9.113  3.584    -26.656 1.00 49.36  ? 269 GLY   D N      1 
ATOM   12271 C  CA     . GLY   D 2  269 ? -7.731  4.012    -26.727 1.00 49.07  ? 269 GLY   D CA     1 
ATOM   12272 C  C      . GLY   D 2  269 ? -6.837  3.042    -27.468 1.00 51.40  ? 269 GLY   D C      1 
ATOM   12273 O  O      . GLY   D 2  269 ? -6.962  1.827    -27.299 1.00 49.86  ? 269 GLY   D O      1 
ATOM   12274 N  N      . PHE   D 2  270 ? -5.937  3.562    -28.302 1.00 57.84  ? 270 PHE   D N      1 
ATOM   12275 C  CA     . PHE   D 2  270 ? -5.027  2.734    -29.081 1.00 63.25  ? 270 PHE   D CA     1 
ATOM   12276 C  C      . PHE   D 2  270 ? -3.614  3.272    -28.931 1.00 68.47  ? 270 PHE   D C      1 
ATOM   12277 O  O      . PHE   D 2  270 ? -3.406  4.488    -28.815 1.00 68.29  ? 270 PHE   D O      1 
ATOM   12278 C  CB     . PHE   D 2  270 ? -5.418  2.690    -30.578 1.00 65.99  ? 270 PHE   D CB     1 
ATOM   12279 C  CG     . PHE   D 2  270 ? -4.757  1.571    -31.357 1.00 70.45  ? 270 PHE   D CG     1 
ATOM   12280 C  CD1    . PHE   D 2  270 ? -5.253  0.283    -31.315 1.00 72.66  ? 270 PHE   D CD1    1 
ATOM   12281 C  CD2    . PHE   D 2  270 ? -3.625  1.810    -32.127 1.00 80.10  ? 270 PHE   D CD2    1 
ATOM   12282 C  CE1    . PHE   D 2  270 ? -4.629  -0.757   -32.043 1.00 79.52  ? 270 PHE   D CE1    1 
ATOM   12283 C  CE2    . PHE   D 2  270 ? -2.996  0.774    -32.851 1.00 76.99  ? 270 PHE   D CE2    1 
ATOM   12284 C  CZ     . PHE   D 2  270 ? -3.499  -0.504   -32.804 1.00 73.51  ? 270 PHE   D CZ     1 
ATOM   12285 N  N      . ALA   D 2  271 ? -2.652  2.344    -28.919 1.00 64.78  ? 271 ALA   D N      1 
ATOM   12286 C  CA     . ALA   D 2  271 ? -1.230  2.613    -28.865 1.00 70.47  ? 271 ALA   D CA     1 
ATOM   12287 C  C      . ALA   D 2  271 ? -0.518  1.425    -29.494 1.00 76.53  ? 271 ALA   D C      1 
ATOM   12288 O  O      . ALA   D 2  271 ? -0.908  0.274    -29.238 1.00 74.40  ? 271 ALA   D O      1 
ATOM   12289 C  CB     . ALA   D 2  271 ? -0.720  2.830    -27.440 1.00 74.05  ? 271 ALA   D CB     1 
ATOM   12290 N  N      . PRO   D 2  272 ? 0.524   1.663    -30.311 1.00 79.63  ? 272 PRO   D N      1 
ATOM   12291 C  CA     . PRO   D 2  272 ? 1.116   2.969    -30.654 1.00 73.02  ? 272 PRO   D CA     1 
ATOM   12292 C  C      . PRO   D 2  272 ? 0.431   3.654    -31.829 1.00 66.45  ? 272 PRO   D C      1 
ATOM   12293 O  O      . PRO   D 2  272 ? -0.325  3.032    -32.558 1.00 63.63  ? 272 PRO   D O      1 
ATOM   12294 C  CB     . PRO   D 2  272 ? 2.560   2.588    -30.968 1.00 74.00  ? 272 PRO   D CB     1 
ATOM   12295 C  CG     . PRO   D 2  272 ? 2.420   1.242    -31.626 1.00 74.89  ? 272 PRO   D CG     1 
ATOM   12296 C  CD     . PRO   D 2  272 ? 1.300   0.549    -30.888 1.00 72.47  ? 272 PRO   D CD     1 
ATOM   12297 N  N      . LEU   D 2  273 ? 0.666   4.941    -32.042 1.00 70.55  ? 273 LEU   D N      1 
ATOM   12298 C  CA     . LEU   D 2  273 ? 0.050   5.625    -33.171 1.00 73.31  ? 273 LEU   D CA     1 
ATOM   12299 C  C      . LEU   D 2  273 ? 1.125   6.062    -34.166 1.00 74.01  ? 273 LEU   D C      1 
ATOM   12300 O  O      . LEU   D 2  273 ? 1.180   5.583    -35.302 1.00 79.04  ? 273 LEU   D O      1 
ATOM   12301 C  CB     . LEU   D 2  273 ? -0.749  6.838    -32.702 1.00 79.10  ? 273 LEU   D CB     1 
ATOM   12302 C  CG     . LEU   D 2  273 ? -1.924  6.642    -31.740 1.00 75.32  ? 273 LEU   D CG     1 
ATOM   12303 C  CD1    . LEU   D 2  273 ? -2.437  8.020    -31.310 1.00 79.59  ? 273 LEU   D CD1    1 
ATOM   12304 C  CD2    . LEU   D 2  273 ? -3.036  5.764    -32.294 1.00 71.47  ? 273 LEU   D CD2    1 
ATOM   12305 N  N      . LEU   D 2  284 ? 7.726   -1.354   -29.852 1.00 99.90  ? 284 LEU   D N      1 
ATOM   12306 C  CA     . LEU   D 2  284 ? 7.421   -0.597   -28.636 1.00 93.36  ? 284 LEU   D CA     1 
ATOM   12307 C  C      . LEU   D 2  284 ? 7.613   -1.471   -27.395 1.00 95.00  ? 284 LEU   D C      1 
ATOM   12308 O  O      . LEU   D 2  284 ? 7.526   -2.697   -27.495 1.00 98.66  ? 284 LEU   D O      1 
ATOM   12309 C  CB     . LEU   D 2  284 ? 5.992   -0.051   -28.694 1.00 86.42  ? 284 LEU   D CB     1 
ATOM   12310 C  CG     . LEU   D 2  284 ? 5.785   1.280    -27.974 1.00 89.23  ? 284 LEU   D CG     1 
ATOM   12311 C  CD1    . LEU   D 2  284 ? 6.797   2.329    -28.444 1.00 101.25 ? 284 LEU   D CD1    1 
ATOM   12312 C  CD2    . LEU   D 2  284 ? 4.364   1.780    -28.179 1.00 85.22  ? 284 LEU   D CD2    1 
ATOM   12313 N  N      . THR   D 2  285 ? 7.875   -0.858   -26.236 1.00 93.78  ? 285 THR   D N      1 
ATOM   12314 C  CA     . THR   D 2  285 ? 8.084   -1.619   -25.006 1.00 88.71  ? 285 THR   D CA     1 
ATOM   12315 C  C      . THR   D 2  285 ? 6.775   -1.782   -24.226 1.00 86.37  ? 285 THR   D C      1 
ATOM   12316 O  O      . THR   D 2  285 ? 5.838   -0.983   -24.341 1.00 79.43  ? 285 THR   D O      1 
ATOM   12317 C  CB     . THR   D 2  285 ? 9.133   -0.965   -24.099 1.00 89.68  ? 285 THR   D CB     1 
ATOM   12318 O  OG1    . THR   D 2  285 ? 9.574   -1.915   -23.120 1.00 92.99  ? 285 THR   D OG1    1 
ATOM   12319 C  CG2    . THR   D 2  285 ? 8.539   0.200    -23.345 1.00 84.92  ? 285 THR   D CG2    1 
ATOM   12320 N  N      . VAL   D 2  286 ? 6.736   -2.841   -23.408 1.00 86.97  ? 286 VAL   D N      1 
ATOM   12321 C  CA     . VAL   D 2  286 ? 5.500   -3.170   -22.691 1.00 80.77  ? 286 VAL   D CA     1 
ATOM   12322 C  C      . VAL   D 2  286 ? 5.118   -2.076   -21.717 1.00 79.84  ? 286 VAL   D C      1 
ATOM   12323 O  O      . VAL   D 2  286 ? 3.917   -1.799   -21.562 1.00 76.10  ? 286 VAL   D O      1 
ATOM   12324 C  CB     . VAL   D 2  286 ? 5.646   -4.546   -22.015 1.00 76.45  ? 286 VAL   D CB     1 
ATOM   12325 C  CG1    . VAL   D 2  286 ? 4.366   -4.894   -21.289 1.00 75.36  ? 286 VAL   D CG1    1 
ATOM   12326 C  CG2    . VAL   D 2  286 ? 6.040   -5.593   -23.035 1.00 82.67  ? 286 VAL   D CG2    1 
ATOM   12327 N  N      . PRO   D 2  287 ? 6.043   -1.435   -20.998 1.00 74.62  ? 287 PRO   D N      1 
ATOM   12328 C  CA     . PRO   D 2  287 ? 5.667   -0.270   -20.198 1.00 71.44  ? 287 PRO   D CA     1 
ATOM   12329 C  C      . PRO   D 2  287 ? 5.326   0.934    -21.036 1.00 73.45  ? 287 PRO   D C      1 
ATOM   12330 O  O      . PRO   D 2  287 ? 4.555   1.783    -20.585 1.00 76.12  ? 287 PRO   D O      1 
ATOM   12331 C  CB     . PRO   D 2  287 ? 6.914   -0.018   -19.351 1.00 79.78  ? 287 PRO   D CB     1 
ATOM   12332 C  CG     . PRO   D 2  287 ? 7.560   -1.355   -19.247 1.00 74.06  ? 287 PRO   D CG     1 
ATOM   12333 C  CD     . PRO   D 2  287 ? 7.336   -2.000   -20.575 1.00 75.66  ? 287 PRO   D CD     1 
ATOM   12334 N  N      . GLU   D 2  288 ? 5.885   1.051    -22.237 1.00 78.65  ? 288 GLU   D N      1 
ATOM   12335 C  CA     . GLU   D 2  288 ? 5.512   2.162    -23.102 1.00 83.83  ? 288 GLU   D CA     1 
ATOM   12336 C  C      . GLU   D 2  288 ? 4.116   1.966    -23.682 1.00 82.07  ? 288 GLU   D C      1 
ATOM   12337 O  O      . GLU   D 2  288 ? 3.346   2.931    -23.799 1.00 81.06  ? 288 GLU   D O      1 
ATOM   12338 C  CB     . GLU   D 2  288 ? 6.543   2.338    -24.215 1.00 90.38  ? 288 GLU   D CB     1 
ATOM   12339 C  CG     . GLU   D 2  288 ? 7.773   3.143    -23.808 1.00 94.46  ? 288 GLU   D CG     1 
ATOM   12340 C  CD     . GLU   D 2  288 ? 8.969   2.904    -24.720 1.00 93.53  ? 288 GLU   D CD     1 
ATOM   12341 O  OE1    . GLU   D 2  288 ? 9.001   1.868    -25.426 1.00 84.11  ? 288 GLU   D OE1    1 
ATOM   12342 O  OE2    . GLU   D 2  288 ? 9.873   3.766    -24.731 1.00 96.95  ? 288 GLU   D OE2    1 
ATOM   12343 N  N      . LEU   D 2  289 ? 3.768   0.736    -24.067 1.00 77.58  ? 289 LEU   D N      1 
ATOM   12344 C  CA     . LEU   D 2  289 ? 2.381   0.472    -24.425 1.00 75.35  ? 289 LEU   D CA     1 
ATOM   12345 C  C      . LEU   D 2  289 ? 1.445   0.963    -23.327 1.00 77.12  ? 289 LEU   D C      1 
ATOM   12346 O  O      . LEU   D 2  289 ? 0.586   1.823    -23.554 1.00 75.66  ? 289 LEU   D O      1 
ATOM   12347 C  CB     . LEU   D 2  289 ? 2.177   -1.019   -24.709 1.00 71.05  ? 289 LEU   D CB     1 
ATOM   12348 C  CG     . LEU   D 2  289 ? 2.520   -1.472   -26.127 1.00 70.47  ? 289 LEU   D CG     1 
ATOM   12349 C  CD1    . LEU   D 2  289 ? 2.462   -2.972   -26.301 1.00 68.97  ? 289 LEU   D CD1    1 
ATOM   12350 C  CD2    . LEU   D 2  289 ? 1.510   -0.831   -27.047 1.00 69.60  ? 289 LEU   D CD2    1 
ATOM   12351 N  N      . THR   D 2  290 ? 1.641   0.454    -22.112 1.00 78.55  ? 290 THR   D N      1 
ATOM   12352 C  CA     . THR   D 2  290 ? 0.786   0.823    -20.987 1.00 76.15  ? 290 THR   D CA     1 
ATOM   12353 C  C      . THR   D 2  290 ? 0.829   2.326    -20.722 1.00 77.77  ? 290 THR   D C      1 
ATOM   12354 O  O      . THR   D 2  290 ? -0.215  2.977    -20.572 1.00 73.12  ? 290 THR   D O      1 
ATOM   12355 C  CB     . THR   D 2  290 ? 1.225   0.046    -19.749 1.00 73.27  ? 290 THR   D CB     1 
ATOM   12356 O  OG1    . THR   D 2  290 ? 1.180   -1.360   -20.027 1.00 66.15  ? 290 THR   D OG1    1 
ATOM   12357 C  CG2    . THR   D 2  290 ? 0.337   0.380    -18.568 1.00 75.93  ? 290 THR   D CG2    1 
ATOM   12358 N  N      . GLN   D 2  291 ? 2.038   2.887    -20.625 1.00 78.43  ? 291 GLN   D N      1 
ATOM   12359 C  CA     . GLN   D 2  291 ? 2.180   4.323    -20.435 1.00 77.72  ? 291 GLN   D CA     1 
ATOM   12360 C  C      . GLN   D 2  291 ? 1.293   5.073    -21.414 1.00 77.66  ? 291 GLN   D C      1 
ATOM   12361 O  O      . GLN   D 2  291 ? 0.382   5.807    -21.017 1.00 74.22  ? 291 GLN   D O      1 
ATOM   12362 C  CB     . GLN   D 2  291 ? 3.643   4.728    -20.613 1.00 84.06  ? 291 GLN   D CB     1 
ATOM   12363 C  CG     . GLN   D 2  291 ? 3.923   6.193    -20.301 1.00 96.96  ? 291 GLN   D CG     1 
ATOM   12364 C  CD     . GLN   D 2  291 ? 4.111   6.477    -18.821 1.00 97.74  ? 291 GLN   D CD     1 
ATOM   12365 O  OE1    . GLN   D 2  291 ? 4.536   5.608    -18.059 1.00 106.30 ? 291 GLN   D OE1    1 
ATOM   12366 N  NE2    . GLN   D 2  291 ? 3.777   7.694    -18.406 1.00 95.18  ? 291 GLN   D NE2    1 
ATOM   12367 N  N      . GLN   D 2  292 ? 1.536   4.853    -22.710 1.00 81.57  ? 292 GLN   D N      1 
ATOM   12368 C  CA     . GLN   D 2  292 ? 0.794   5.537    -23.764 1.00 83.13  ? 292 GLN   D CA     1 
ATOM   12369 C  C      . GLN   D 2  292 ? -0.697  5.240    -23.665 1.00 81.45  ? 292 GLN   D C      1 
ATOM   12370 O  O      . GLN   D 2  292 ? -1.534  6.151    -23.729 1.00 78.48  ? 292 GLN   D O      1 
ATOM   12371 C  CB     . GLN   D 2  292 ? 1.326   5.101    -25.128 1.00 79.84  ? 292 GLN   D CB     1 
ATOM   12372 C  CG     . GLN   D 2  292 ? 2.821   5.278    -25.309 1.00 84.67  ? 292 GLN   D CG     1 
ATOM   12373 C  CD     . GLN   D 2  292 ? 3.223   5.389    -26.766 1.00 90.02  ? 292 GLN   D CD     1 
ATOM   12374 O  OE1    . GLN   D 2  292 ? 3.834   4.478    -27.325 1.00 83.89  ? 292 GLN   D OE1    1 
ATOM   12375 N  NE2    . GLN   D 2  292 ? 2.904   6.522    -27.382 1.00 100.41 ? 292 GLN   D NE2    1 
ATOM   12376 N  N      . MET   D 2  293 ? -1.044  3.958    -23.492 1.00 80.78  ? 293 MET   D N      1 
ATOM   12377 C  CA     . MET   D 2  293 ? -2.437  3.519    -23.534 1.00 78.66  ? 293 MET   D CA     1 
ATOM   12378 C  C      . MET   D 2  293 ? -3.316  4.200    -22.482 1.00 80.37  ? 293 MET   D C      1 
ATOM   12379 O  O      . MET   D 2  293 ? -4.538  4.277    -22.669 1.00 78.63  ? 293 MET   D O      1 
ATOM   12380 C  CB     . MET   D 2  293 ? -2.504  1.998    -23.370 1.00 69.66  ? 293 MET   D CB     1 
ATOM   12381 C  CG     . MET   D 2  293 ? -3.921  1.451    -23.308 1.00 67.12  ? 293 MET   D CG     1 
ATOM   12382 S  SD     . MET   D 2  293 ? -4.001  -0.341   -23.077 1.00 74.32  ? 293 MET   D SD     1 
ATOM   12383 C  CE     . MET   D 2  293 ? -2.836  -0.614   -21.742 1.00 67.41  ? 293 MET   D CE     1 
ATOM   12384 N  N      . PHE   D 2  294 ? -2.741  4.680    -21.379 1.00 69.75  ? 294 PHE   D N      1 
ATOM   12385 C  CA     . PHE   D 2  294 ? -3.482  5.494    -20.429 1.00 72.57  ? 294 PHE   D CA     1 
ATOM   12386 C  C      . PHE   D 2  294 ? -3.222  6.975    -20.617 1.00 83.28  ? 294 PHE   D C      1 
ATOM   12387 O  O      . PHE   D 2  294 ? -3.542  7.771    -19.724 1.00 81.92  ? 294 PHE   D O      1 
ATOM   12388 C  CB     . PHE   D 2  294 ? -3.141  5.099    -18.999 1.00 83.89  ? 294 PHE   D CB     1 
ATOM   12389 C  CG     . PHE   D 2  294 ? -3.838  3.861    -18.530 1.00 82.85  ? 294 PHE   D CG     1 
ATOM   12390 C  CD1    . PHE   D 2  294 ? -3.365  2.611    -18.884 1.00 79.17  ? 294 PHE   D CD1    1 
ATOM   12391 C  CD2    . PHE   D 2  294 ? -4.941  3.946    -17.700 1.00 71.37  ? 294 PHE   D CD2    1 
ATOM   12392 C  CE1    . PHE   D 2  294 ? -3.995  1.469    -18.451 1.00 70.45  ? 294 PHE   D CE1    1 
ATOM   12393 C  CE2    . PHE   D 2  294 ? -5.568  2.807    -17.261 1.00 65.52  ? 294 PHE   D CE2    1 
ATOM   12394 C  CZ     . PHE   D 2  294 ? -5.094  1.567    -17.635 1.00 65.14  ? 294 PHE   D CZ     1 
ATOM   12395 N  N      . ASP   D 2  295 ? -2.632  7.354    -21.750 1.00 81.73  ? 295 ASP   D N      1 
ATOM   12396 C  CA     . ASP   D 2  295 ? -2.277  8.738    -22.025 1.00 78.12  ? 295 ASP   D CA     1 
ATOM   12397 C  C      . ASP   D 2  295 ? -3.430  9.407    -22.744 1.00 72.58  ? 295 ASP   D C      1 
ATOM   12398 O  O      . ASP   D 2  295 ? -3.936  8.867    -23.729 1.00 73.99  ? 295 ASP   D O      1 
ATOM   12399 C  CB     . ASP   D 2  295 ? -1.000  8.802    -22.866 1.00 79.15  ? 295 ASP   D CB     1 
ATOM   12400 C  CG     . ASP   D 2  295 ? -0.544  10.222   -23.145 1.00 85.55  ? 295 ASP   D CG     1 
ATOM   12401 O  OD1    . ASP   D 2  295 ? -1.144  11.174   -22.594 1.00 87.08  ? 295 ASP   D OD1    1 
ATOM   12402 O  OD2    . ASP   D 2  295 ? 0.452   10.376   -23.886 1.00 90.56  ? 295 ASP   D OD2    1 
ATOM   12403 N  N      . SER   D 2  296 ? -3.851  10.571   -22.243 1.00 65.43  ? 296 SER   D N      1 
ATOM   12404 C  CA     . SER   D 2  296 ? -4.911  11.317   -22.906 1.00 69.23  ? 296 SER   D CA     1 
ATOM   12405 C  C      . SER   D 2  296 ? -4.644  11.527   -24.397 1.00 75.16  ? 296 SER   D C      1 
ATOM   12406 O  O      . SER   D 2  296 ? -5.584  11.773   -25.162 1.00 73.58  ? 296 SER   D O      1 
ATOM   12407 C  CB     . SER   D 2  296 ? -5.093  12.664   -22.221 1.00 75.67  ? 296 SER   D CB     1 
ATOM   12408 O  OG     . SER   D 2  296 ? -5.547  13.639   -23.147 1.00 87.31  ? 296 SER   D OG     1 
ATOM   12409 N  N      . LYS   D 2  297 ? -3.387  11.436   -24.831 1.00 81.44  ? 297 LYS   D N      1 
ATOM   12410 C  CA     . LYS   D 2  297 ? -3.062  11.566   -26.244 1.00 78.93  ? 297 LYS   D CA     1 
ATOM   12411 C  C      . LYS   D 2  297 ? -3.436  10.333   -27.061 1.00 76.40  ? 297 LYS   D C      1 
ATOM   12412 O  O      . LYS   D 2  297 ? -3.488  10.422   -28.298 1.00 78.35  ? 297 LYS   D O      1 
ATOM   12413 C  CB     . LYS   D 2  297 ? -1.567  11.885   -26.413 1.00 75.60  ? 297 LYS   D CB     1 
ATOM   12414 C  CG     . LYS   D 2  297 ? -1.171  13.273   -25.906 1.00 84.66  ? 297 LYS   D CG     1 
ATOM   12415 C  CD     . LYS   D 2  297 ? 0.243   13.658   -26.328 1.00 99.98  ? 297 LYS   D CD     1 
ATOM   12416 C  CE     . LYS   D 2  297 ? 1.059   14.182   -25.150 1.00 103.59 ? 297 LYS   D CE     1 
ATOM   12417 N  NZ     . LYS   D 2  297 ? 1.410   13.108   -24.169 1.00 101.08 ? 297 LYS   D NZ     1 
ATOM   12418 N  N      . ASN   D 2  298 ? -3.704  9.196    -26.419 1.00 69.25  ? 298 ASN   D N      1 
ATOM   12419 C  CA     . ASN   D 2  298 ? -4.068  7.986    -27.138 1.00 68.82  ? 298 ASN   D CA     1 
ATOM   12420 C  C      . ASN   D 2  298 ? -5.554  7.659    -27.011 1.00 69.34  ? 298 ASN   D C      1 
ATOM   12421 O  O      . ASN   D 2  298 ? -5.966  6.554    -27.381 1.00 65.17  ? 298 ASN   D O      1 
ATOM   12422 C  CB     . ASN   D 2  298 ? -3.238  6.810    -26.637 1.00 72.99  ? 298 ASN   D CB     1 
ATOM   12423 C  CG     . ASN   D 2  298 ? -1.791  6.943    -26.988 1.00 74.07  ? 298 ASN   D CG     1 
ATOM   12424 O  OD1    . ASN   D 2  298 ? -1.304  8.058    -27.147 1.00 72.49  ? 298 ASN   D OD1    1 
ATOM   12425 N  ND2    . ASN   D 2  298 ? -1.090  5.818    -27.127 1.00 73.02  ? 298 ASN   D ND2    1 
ATOM   12426 N  N      . MET   D 2  299 ? -6.371  8.589    -26.504 1.00 66.39  ? 299 MET   D N      1 
ATOM   12427 C  CA     . MET   D 2  299 ? -7.804  8.366    -26.335 1.00 60.46  ? 299 MET   D CA     1 
ATOM   12428 C  C      . MET   D 2  299 ? -8.540  8.839    -27.577 1.00 61.10  ? 299 MET   D C      1 
ATOM   12429 O  O      . MET   D 2  299 ? -8.426  10.011   -27.959 1.00 62.28  ? 299 MET   D O      1 
ATOM   12430 C  CB     . MET   D 2  299 ? -8.358  9.097    -25.109 1.00 60.24  ? 299 MET   D CB     1 
ATOM   12431 C  CG     . MET   D 2  299 ? -7.815  8.624    -23.770 1.00 64.26  ? 299 MET   D CG     1 
ATOM   12432 S  SD     . MET   D 2  299 ? -7.721  6.827    -23.623 1.00 64.15  ? 299 MET   D SD     1 
ATOM   12433 C  CE     . MET   D 2  299 ? -6.912  6.657    -22.042 1.00 67.42  ? 299 MET   D CE     1 
ATOM   12434 N  N      . MET   D 2  300 ? -9.312  7.931    -28.182 1.00 56.75  ? 300 MET   D N      1 
ATOM   12435 C  CA     . MET   D 2  300 ? -10.199 8.232    -29.290 1.00 47.41  ? 300 MET   D CA     1 
ATOM   12436 C  C      . MET   D 2  300 ? -11.457 8.958    -28.867 1.00 48.24  ? 300 MET   D C      1 
ATOM   12437 O  O      . MET   D 2  300 ? -12.437 8.907    -29.601 1.00 48.70  ? 300 MET   D O      1 
ATOM   12438 C  CB     . MET   D 2  300 ? -10.577 6.956    -30.013 1.00 43.88  ? 300 MET   D CB     1 
ATOM   12439 C  CG     . MET   D 2  300 ? -9.388  6.131    -30.443 1.00 50.98  ? 300 MET   D CG     1 
ATOM   12440 S  SD     . MET   D 2  300 ? -8.437  6.845    -31.803 1.00 62.02  ? 300 MET   D SD     1 
ATOM   12441 C  CE     . MET   D 2  300 ? -7.046  5.718    -31.808 1.00 57.56  ? 300 MET   D CE     1 
ATOM   12442 N  N      . ALA   D 2  301 ? -11.464 9.605    -27.701 1.00 51.54  ? 301 ALA   D N      1 
ATOM   12443 C  CA     . ALA   D 2  301 ? -12.476 10.588   -27.337 1.00 57.07  ? 301 ALA   D CA     1 
ATOM   12444 C  C      . ALA   D 2  301 ? -11.748 11.841   -26.914 1.00 59.36  ? 301 ALA   D C      1 
ATOM   12445 O  O      . ALA   D 2  301 ? -10.664 11.761   -26.338 1.00 65.45  ? 301 ALA   D O      1 
ATOM   12446 C  CB     . ALA   D 2  301 ? -13.395 10.129   -26.199 1.00 52.59  ? 301 ALA   D CB     1 
ATOM   12447 N  N      . ALA   D 2  302 ? -12.325 12.996   -27.220 1.00 62.37  ? 302 ALA   D N      1 
ATOM   12448 C  CA     . ALA   D 2  302 ? -11.681 14.247   -26.852 1.00 63.76  ? 302 ALA   D CA     1 
ATOM   12449 C  C      . ALA   D 2  302 ? -11.850 14.489   -25.363 1.00 62.52  ? 302 ALA   D C      1 
ATOM   12450 O  O      . ALA   D 2  302 ? -12.480 15.482   -24.981 1.00 67.69  ? 302 ALA   D O      1 
ATOM   12451 C  CB     . ALA   D 2  302 ? -12.259 15.425   -27.642 1.00 71.89  ? 302 ALA   D CB     1 
ATOM   12452 N  N      . CYS   D 2  303 ? -11.302 13.591   -24.528 1.00 60.16  ? 303 CYS   D N      1 
ATOM   12453 C  CA     . CYS   D 2  303 ? -11.434 13.644   -23.073 1.00 61.95  ? 303 CYS   D CA     1 
ATOM   12454 C  C      . CYS   D 2  303 ? -10.104 13.335   -22.396 1.00 66.69  ? 303 CYS   D C      1 
ATOM   12455 O  O      . CYS   D 2  303 ? -9.275  12.591   -22.933 1.00 64.36  ? 303 CYS   D O      1 
ATOM   12456 C  CB     . CYS   D 2  303 ? -12.501 12.668   -22.560 1.00 60.16  ? 303 CYS   D CB     1 
ATOM   12457 S  SG     . CYS   D 2  303 ? -14.104 12.852   -23.354 1.00 73.70  ? 303 CYS   D SG     1 
ATOM   12458 N  N      . ASP   D 2  304 ? -9.915  13.915   -21.198 1.00 66.54  ? 304 ASP   D N      1 
ATOM   12459 C  CA     . ASP   D 2  304 ? -8.715  13.715   -20.379 1.00 67.90  ? 304 ASP   D CA     1 
ATOM   12460 C  C      . ASP   D 2  304 ? -9.074  12.773   -19.233 1.00 64.71  ? 304 ASP   D C      1 
ATOM   12461 O  O      . ASP   D 2  304 ? -9.904  13.141   -18.382 1.00 63.90  ? 304 ASP   D O      1 
ATOM   12462 C  CB     . ASP   D 2  304 ? -8.207  15.052   -19.814 1.00 73.71  ? 304 ASP   D CB     1 
ATOM   12463 C  CG     . ASP   D 2  304 ? -6.761  14.983   -19.250 1.00 74.63  ? 304 ASP   D CG     1 
ATOM   12464 O  OD1    . ASP   D 2  304 ? -6.300  13.900   -18.826 1.00 67.05  ? 304 ASP   D OD1    1 
ATOM   12465 O  OD2    . ASP   D 2  304 ? -6.110  16.053   -19.160 1.00 81.75  ? 304 ASP   D OD2    1 
ATOM   12466 N  N      . PRO   D 2  305 ? -8.491  11.573   -19.143 1.00 59.33  ? 305 PRO   D N      1 
ATOM   12467 C  CA     . PRO   D 2  305 ? -8.834  10.695   -18.013 1.00 57.69  ? 305 PRO   D CA     1 
ATOM   12468 C  C      . PRO   D 2  305 ? -8.625  11.345   -16.656 1.00 62.39  ? 305 PRO   D C      1 
ATOM   12469 O  O      . PRO   D 2  305 ? -9.464  11.188   -15.757 1.00 63.57  ? 305 PRO   D O      1 
ATOM   12470 C  CB     . PRO   D 2  305 ? -7.914  9.487    -18.223 1.00 52.64  ? 305 PRO   D CB     1 
ATOM   12471 C  CG     . PRO   D 2  305 ? -7.513  9.542    -19.647 1.00 60.56  ? 305 PRO   D CG     1 
ATOM   12472 C  CD     . PRO   D 2  305 ? -7.447  10.989   -19.995 1.00 65.07  ? 305 PRO   D CD     1 
ATOM   12473 N  N      . ARG   D 2  306 ? -7.540  12.077   -16.487 1.00 53.12  ? 306 ARG   D N      1 
ATOM   12474 C  CA     . ARG   D 2  306 ? -7.152  12.706   -15.238 1.00 52.88  ? 306 ARG   D CA     1 
ATOM   12475 C  C      . ARG   D 2  306 ? -8.061  13.850   -14.831 1.00 59.62  ? 306 ARG   D C      1 
ATOM   12476 O  O      . ARG   D 2  306 ? -7.804  14.580   -13.849 1.00 60.87  ? 306 ARG   D O      1 
ATOM   12477 C  CB     . ARG   D 2  306 ? -5.711  13.167   -15.375 1.00 56.26  ? 306 ARG   D CB     1 
ATOM   12478 C  CG     . ARG   D 2  306 ? -4.784  11.995   -15.517 1.00 52.48  ? 306 ARG   D CG     1 
ATOM   12479 C  CD     . ARG   D 2  306 ? -3.373  12.415   -15.675 1.00 57.43  ? 306 ARG   D CD     1 
ATOM   12480 N  NE     . ARG   D 2  306 ? -2.504  11.248   -15.724 1.00 64.73  ? 306 ARG   D NE     1 
ATOM   12481 C  CZ     . ARG   D 2  306 ? -1.649  10.919   -14.759 1.00 74.43  ? 306 ARG   D CZ     1 
ATOM   12482 N  NH1    . ARG   D 2  306 ? -1.594  11.593   -13.611 1.00 64.95  ? 306 ARG   D NH1    1 
ATOM   12483 N  NH2    . ARG   D 2  306 ? -0.842  9.878    -14.938 1.00 75.72  ? 306 ARG   D NH2    1 
ATOM   12484 N  N      . HIS   D 2  307 ? -9.160  14.050   -15.550 1.00 58.86  ? 307 HIS   D N      1 
ATOM   12485 C  CA     . HIS   D 2  307 ? -10.164 15.020   -15.155 1.00 55.14  ? 307 HIS   D CA     1 
ATOM   12486 C  C      . HIS   D 2  307 ? -11.391 14.357   -14.545 1.00 62.74  ? 307 HIS   D C      1 
ATOM   12487 O  O      . HIS   D 2  307 ? -12.171 15.026   -13.850 1.00 61.47  ? 307 HIS   D O      1 
ATOM   12488 C  CB     . HIS   D 2  307 ? -10.516 15.880   -16.371 1.00 62.03  ? 307 HIS   D CB     1 
ATOM   12489 C  CG     . HIS   D 2  307 ? -9.380  16.751   -16.833 1.00 71.50  ? 307 HIS   D CG     1 
ATOM   12490 N  ND1    . HIS   D 2  307 ? -9.442  17.516   -17.978 1.00 70.13  ? 307 HIS   D ND1    1 
ATOM   12491 C  CD2    . HIS   D 2  307 ? -8.194  17.052   -16.247 1.00 71.15  ? 307 HIS   D CD2    1 
ATOM   12492 C  CE1    . HIS   D 2  307 ? -8.315  18.192   -18.116 1.00 72.17  ? 307 HIS   D CE1    1 
ATOM   12493 N  NE2    . HIS   D 2  307 ? -7.546  17.937   -17.072 1.00 70.24  ? 307 HIS   D NE2    1 
ATOM   12494 N  N      . GLY   D 2  308 ? -11.537 13.049   -14.732 1.00 63.21  ? 308 GLY   D N      1 
ATOM   12495 C  CA     . GLY   D 2  308 ? -12.488 12.270   -13.966 1.00 60.76  ? 308 GLY   D CA     1 
ATOM   12496 C  C      . GLY   D 2  308 ? -11.872 11.041   -13.322 1.00 59.32  ? 308 GLY   D C      1 
ATOM   12497 O  O      . GLY   D 2  308 ? -10.651 10.961   -13.144 1.00 55.99  ? 308 GLY   D O      1 
ATOM   12498 N  N      . ARG   D 2  309 ? -12.718 10.077   -12.965 1.00 58.13  ? 309 ARG   D N      1 
ATOM   12499 C  CA     . ARG   D 2  309 ? -12.300 8.799    -12.412 1.00 51.55  ? 309 ARG   D CA     1 
ATOM   12500 C  C      . ARG   D 2  309 ? -12.801 7.675    -13.308 1.00 46.25  ? 309 ARG   D C      1 
ATOM   12501 O  O      . ARG   D 2  309 ? -13.901 7.760    -13.858 1.00 44.50  ? 309 ARG   D O      1 
ATOM   12502 C  CB     . ARG   D 2  309 ? -12.841 8.615    -10.983 1.00 55.35  ? 309 ARG   D CB     1 
ATOM   12503 C  CG     . ARG   D 2  309 ? -12.175 9.438    -9.904  1.00 55.11  ? 309 ARG   D CG     1 
ATOM   12504 C  CD     . ARG   D 2  309 ? -12.816 9.128    -8.570  1.00 52.78  ? 309 ARG   D CD     1 
ATOM   12505 N  NE     . ARG   D 2  309 ? -12.853 10.297   -7.713  1.00 62.81  ? 309 ARG   D NE     1 
ATOM   12506 C  CZ     . ARG   D 2  309 ? -11.843 10.649   -6.929  1.00 67.49  ? 309 ARG   D CZ     1 
ATOM   12507 N  NH1    . ARG   D 2  309 ? -10.738 9.927    -6.870  1.00 65.22  ? 309 ARG   D NH1    1 
ATOM   12508 N  NH2    . ARG   D 2  309 ? -11.934 11.763   -6.201  1.00 67.17  ? 309 ARG   D NH2    1 
ATOM   12509 N  N      . TYR   D 2  310 ? -11.994 6.621    -13.449 1.00 49.77  ? 310 TYR   D N      1 
ATOM   12510 C  CA     . TYR   D 2  310 ? -12.412 5.406    -14.150 1.00 47.07  ? 310 TYR   D CA     1 
ATOM   12511 C  C      . TYR   D 2  310 ? -13.393 4.605    -13.310 1.00 47.97  ? 310 TYR   D C      1 
ATOM   12512 O  O      . TYR   D 2  310 ? -13.097 4.253    -12.163 1.00 48.89  ? 310 TYR   D O      1 
ATOM   12513 C  CB     . TYR   D 2  310 ? -11.216 4.520    -14.476 1.00 46.60  ? 310 TYR   D CB     1 
ATOM   12514 C  CG     . TYR   D 2  310 ? -10.394 4.998    -15.634 1.00 55.17  ? 310 TYR   D CG     1 
ATOM   12515 C  CD1    . TYR   D 2  310 ? -10.845 4.857    -16.949 1.00 54.07  ? 310 TYR   D CD1    1 
ATOM   12516 C  CD2    . TYR   D 2  310 ? -9.182  5.607    -15.425 1.00 52.14  ? 310 TYR   D CD2    1 
ATOM   12517 C  CE1    . TYR   D 2  310 ? -10.090 5.299    -18.018 1.00 47.15  ? 310 TYR   D CE1    1 
ATOM   12518 C  CE2    . TYR   D 2  310 ? -8.430  6.050    -16.481 1.00 56.73  ? 310 TYR   D CE2    1 
ATOM   12519 C  CZ     . TYR   D 2  310 ? -8.884  5.902    -17.771 1.00 51.52  ? 310 TYR   D CZ     1 
ATOM   12520 O  OH     . TYR   D 2  310 ? -8.099  6.365    -18.800 1.00 53.59  ? 310 TYR   D OH     1 
ATOM   12521 N  N      . LEU   D 2  311 ? -14.550 4.297    -13.889 1.00 50.90  ? 311 LEU   D N      1 
ATOM   12522 C  CA     . LEU   D 2  311 ? -15.422 3.289    -13.302 1.00 46.66  ? 311 LEU   D CA     1 
ATOM   12523 C  C      . LEU   D 2  311 ? -14.911 1.887    -13.625 1.00 48.34  ? 311 LEU   D C      1 
ATOM   12524 O  O      . LEU   D 2  311 ? -14.602 1.101    -12.721 1.00 45.16  ? 311 LEU   D O      1 
ATOM   12525 C  CB     . LEU   D 2  311 ? -16.853 3.477    -13.803 1.00 45.46  ? 311 LEU   D CB     1 
ATOM   12526 C  CG     . LEU   D 2  311 ? -17.558 4.795    -13.510 1.00 43.78  ? 311 LEU   D CG     1 
ATOM   12527 C  CD1    . LEU   D 2  311 ? -18.917 4.814    -14.193 1.00 44.91  ? 311 LEU   D CD1    1 
ATOM   12528 C  CD2    . LEU   D 2  311 ? -17.696 4.995    -12.021 1.00 38.56  ? 311 LEU   D CD2    1 
ATOM   12529 N  N      . THR   D 2  312 ? -14.807 1.551    -14.916 1.00 48.95  ? 312 THR   D N      1 
ATOM   12530 C  CA     . THR   D 2  312 ? -14.231 0.265    -15.299 1.00 49.35  ? 312 THR   D CA     1 
ATOM   12531 C  C      . THR   D 2  312 ? -13.344 0.441    -16.517 1.00 44.78  ? 312 THR   D C      1 
ATOM   12532 O  O      . THR   D 2  312 ? -13.444 1.429    -17.238 1.00 45.90  ? 312 THR   D O      1 
ATOM   12533 C  CB     . THR   D 2  312 ? -15.280 -0.770   -15.652 1.00 49.00  ? 312 THR   D CB     1 
ATOM   12534 O  OG1    . THR   D 2  312 ? -16.081 -0.247   -16.717 1.00 44.84  ? 312 THR   D OG1    1 
ATOM   12535 C  CG2    . THR   D 2  312 ? -16.159 -1.057   -14.421 1.00 43.77  ? 312 THR   D CG2    1 
ATOM   12536 N  N      . VAL   D 2  313 ? -12.502 -0.559   -16.761 1.00 45.26  ? 313 VAL   D N      1 
ATOM   12537 C  CA     . VAL   D 2  313 ? -11.495 -0.511   -17.815 1.00 44.11  ? 313 VAL   D CA     1 
ATOM   12538 C  C      . VAL   D 2  313 ? -11.187 -1.927   -18.283 1.00 48.80  ? 313 VAL   D C      1 
ATOM   12539 O  O      . VAL   D 2  313 ? -10.835 -2.795   -17.476 1.00 42.39  ? 313 VAL   D O      1 
ATOM   12540 C  CB     . VAL   D 2  313 ? -10.198 0.161    -17.334 1.00 41.81  ? 313 VAL   D CB     1 
ATOM   12541 C  CG1    . VAL   D 2  313 ? -9.146  0.068    -18.419 1.00 46.82  ? 313 VAL   D CG1    1 
ATOM   12542 C  CG2    . VAL   D 2  313 ? -10.456 1.598    -16.941 1.00 47.41  ? 313 VAL   D CG2    1 
ATOM   12543 N  N      . ALA   D 2  314 ? -11.309 -2.152   -19.593 1.00 45.10  ? 314 ALA   D N      1 
ATOM   12544 C  CA     . ALA   D 2  314 ? -10.756 -3.322   -20.251 1.00 44.99  ? 314 ALA   D CA     1 
ATOM   12545 C  C      . ALA   D 2  314 ? -9.551  -2.905   -21.087 1.00 52.52  ? 314 ALA   D C      1 
ATOM   12546 O  O      . ALA   D 2  314 ? -9.443  -1.750   -21.500 1.00 49.68  ? 314 ALA   D O      1 
ATOM   12547 C  CB     . ALA   D 2  314 ? -11.795 -3.996   -21.139 1.00 48.57  ? 314 ALA   D CB     1 
ATOM   12548 N  N      . ALA   D 2  315 ? -8.647  -3.853   -21.337 1.00 57.18  ? 315 ALA   D N      1 
ATOM   12549 C  CA     . ALA   D 2  315 ? -7.378  -3.587   -22.009 1.00 51.02  ? 315 ALA   D CA     1 
ATOM   12550 C  C      . ALA   D 2  315 ? -7.009  -4.808   -22.832 1.00 55.99  ? 315 ALA   D C      1 
ATOM   12551 O  O      . ALA   D 2  315 ? -6.900  -5.901   -22.265 1.00 55.79  ? 315 ALA   D O      1 
ATOM   12552 C  CB     . ALA   D 2  315 ? -6.281  -3.294   -20.983 1.00 48.47  ? 315 ALA   D CB     1 
ATOM   12553 N  N      . ILE   D 2  316 ? -6.809  -4.648   -24.148 1.00 52.39  ? 316 ILE   D N      1 
ATOM   12554 C  CA     . ILE   D 2  316 ? -6.376  -5.763   -25.002 1.00 56.80  ? 316 ILE   D CA     1 
ATOM   12555 C  C      . ILE   D 2  316 ? -4.921  -5.544   -25.390 1.00 62.04  ? 316 ILE   D C      1 
ATOM   12556 O  O      . ILE   D 2  316 ? -4.603  -4.579   -26.101 1.00 62.37  ? 316 ILE   D O      1 
ATOM   12557 C  CB     . ILE   D 2  316 ? -7.202  -5.923   -26.289 1.00 54.56  ? 316 ILE   D CB     1 
ATOM   12558 C  CG1    . ILE   D 2  316 ? -8.696  -5.834   -26.055 1.00 61.74  ? 316 ILE   D CG1    1 
ATOM   12559 C  CG2    . ILE   D 2  316 ? -6.927  -7.287   -26.892 1.00 52.92  ? 316 ILE   D CG2    1 
ATOM   12560 C  CD1    . ILE   D 2  316 ? -9.226  -4.426   -26.155 1.00 60.51  ? 316 ILE   D CD1    1 
ATOM   12561 N  N      . PHE   D 2  317 ? -4.043  -6.461   -24.969 1.00 56.96  ? 317 PHE   D N      1 
ATOM   12562 C  CA     . PHE   D 2  317 ? -2.671  -6.507   -25.466 1.00 61.81  ? 317 PHE   D CA     1 
ATOM   12563 C  C      . PHE   D 2  317 ? -2.583  -7.517   -26.597 1.00 68.61  ? 317 PHE   D C      1 
ATOM   12564 O  O      . PHE   D 2  317 ? -2.685  -8.727   -26.372 1.00 69.05  ? 317 PHE   D O      1 
ATOM   12565 C  CB     . PHE   D 2  317 ? -1.681  -6.838   -24.356 1.00 59.44  ? 317 PHE   D CB     1 
ATOM   12566 C  CG     . PHE   D 2  317 ? -1.523  -5.736   -23.390 1.00 58.51  ? 317 PHE   D CG     1 
ATOM   12567 C  CD1    . PHE   D 2  317 ? -2.403  -5.593   -22.342 1.00 56.75  ? 317 PHE   D CD1    1 
ATOM   12568 C  CD2    . PHE   D 2  317 ? -0.540  -4.796   -23.572 1.00 57.95  ? 317 PHE   D CD2    1 
ATOM   12569 C  CE1    . PHE   D 2  317 ? -2.287  -4.564   -21.476 1.00 57.13  ? 317 PHE   D CE1    1 
ATOM   12570 C  CE2    . PHE   D 2  317 ? -0.419  -3.763   -22.709 1.00 58.43  ? 317 PHE   D CE2    1 
ATOM   12571 C  CZ     . PHE   D 2  317 ? -1.299  -3.642   -21.655 1.00 61.78  ? 317 PHE   D CZ     1 
ATOM   12572 N  N      . ARG   D 2  318 ? -2.396  -7.013   -27.811 1.00 72.86  ? 318 ARG   D N      1 
ATOM   12573 C  CA     . ARG   D 2  318 ? -2.205  -7.837   -28.994 1.00 75.15  ? 318 ARG   D CA     1 
ATOM   12574 C  C      . ARG   D 2  318 ? -0.718  -7.883   -29.305 1.00 74.26  ? 318 ARG   D C      1 
ATOM   12575 O  O      . ARG   D 2  318 ? -0.041  -6.848   -29.284 1.00 74.04  ? 318 ARG   D O      1 
ATOM   12576 C  CB     . ARG   D 2  318 ? -2.979  -7.262   -30.176 1.00 71.60  ? 318 ARG   D CB     1 
ATOM   12577 C  CG     . ARG   D 2  318 ? -4.469  -7.218   -29.971 1.00 66.18  ? 318 ARG   D CG     1 
ATOM   12578 C  CD     . ARG   D 2  318 ? -5.127  -6.882   -31.268 1.00 71.89  ? 318 ARG   D CD     1 
ATOM   12579 N  NE     . ARG   D 2  318 ? -5.072  -8.020   -32.174 1.00 77.10  ? 318 ARG   D NE     1 
ATOM   12580 C  CZ     . ARG   D 2  318 ? -5.831  -8.152   -33.251 1.00 75.79  ? 318 ARG   D CZ     1 
ATOM   12581 N  NH1    . ARG   D 2  318 ? -6.710  -7.219   -33.593 1.00 72.47  ? 318 ARG   D NH1    1 
ATOM   12582 N  NH2    . ARG   D 2  318 ? -5.697  -9.240   -34.011 1.00 70.80  ? 318 ARG   D NH2    1 
ATOM   12583 N  N      . GLY   D 2  319 ? -0.214  -9.075   -29.580 1.00 67.89  ? 319 GLY   D N      1 
ATOM   12584 C  CA     . GLY   D 2  319 ? 1.179   -9.256   -29.891 1.00 68.71  ? 319 GLY   D CA     1 
ATOM   12585 C  C      . GLY   D 2  319 ? 1.778   -10.375  -29.081 1.00 73.07  ? 319 GLY   D C      1 
ATOM   12586 O  O      . GLY   D 2  319 ? 1.125   -11.006  -28.255 1.00 75.95  ? 319 GLY   D O      1 
ATOM   12587 N  N      . ARG   D 2  320 ? 3.044   -10.634  -29.353 1.00 84.07  ? 320 ARG   D N      1 
ATOM   12588 C  CA     . ARG   D 2  320 ? 3.856   -11.567  -28.588 1.00 84.63  ? 320 ARG   D CA     1 
ATOM   12589 C  C      . ARG   D 2  320 ? 4.640   -10.783  -27.546 1.00 82.08  ? 320 ARG   D C      1 
ATOM   12590 O  O      . ARG   D 2  320 ? 5.377   -9.859   -27.893 1.00 88.50  ? 320 ARG   D O      1 
ATOM   12591 C  CB     . ARG   D 2  320 ? 4.805   -12.308  -29.515 1.00 86.89  ? 320 ARG   D CB     1 
ATOM   12592 C  CG     . ARG   D 2  320 ? 5.292   -13.604  -28.999 1.00 96.01  ? 320 ARG   D CG     1 
ATOM   12593 C  CD     . ARG   D 2  320 ? 5.672   -14.459  -30.175 1.00 108.82 ? 320 ARG   D CD     1 
ATOM   12594 N  NE     . ARG   D 2  320 ? 6.412   -15.640  -29.756 1.00 112.97 ? 320 ARG   D NE     1 
ATOM   12595 C  CZ     . ARG   D 2  320 ? 5.848   -16.745  -29.294 1.00 113.21 ? 320 ARG   D CZ     1 
ATOM   12596 N  NH1    . ARG   D 2  320 ? 4.533   -16.848  -29.170 1.00 112.18 ? 320 ARG   D NH1    1 
ATOM   12597 N  NH2    . ARG   D 2  320 ? 6.621   -17.773  -28.953 1.00 93.82  ? 320 ARG   D NH2    1 
ATOM   12598 N  N      . MET   D 2  321 ? 4.482   -11.139  -26.279 1.00 81.33  ? 321 MET   D N      1 
ATOM   12599 C  CA     . MET   D 2  321 ? 5.059   -10.345  -25.199 1.00 84.25  ? 321 MET   D CA     1 
ATOM   12600 C  C      . MET   D 2  321 ? 4.949   -11.144  -23.913 1.00 85.18  ? 321 MET   D C      1 
ATOM   12601 O  O      . MET   D 2  321 ? 4.124   -12.056  -23.805 1.00 84.05  ? 321 MET   D O      1 
ATOM   12602 C  CB     . MET   D 2  321 ? 4.358   -8.989   -25.047 1.00 82.14  ? 321 MET   D CB     1 
ATOM   12603 C  CG     . MET   D 2  321 ? 2.947   -9.096   -24.471 1.00 81.13  ? 321 MET   D CG     1 
ATOM   12604 S  SD     . MET   D 2  321 ? 1.866   -7.721   -24.937 1.00 83.27  ? 321 MET   D SD     1 
ATOM   12605 C  CE     . MET   D 2  321 ? 1.911   -7.795   -26.732 1.00 84.66  ? 321 MET   D CE     1 
ATOM   12606 N  N      . SER   D 2  322 ? 5.790   -10.798  -22.938 1.00 88.19  ? 322 SER   D N      1 
ATOM   12607 C  CA     . SER   D 2  322 ? 5.854   -11.572  -21.698 1.00 88.51  ? 322 SER   D CA     1 
ATOM   12608 C  C      . SER   D 2  322 ? 4.722   -11.121  -20.787 1.00 81.60  ? 322 SER   D C      1 
ATOM   12609 O  O      . SER   D 2  322 ? 4.797   -10.066  -20.153 1.00 85.29  ? 322 SER   D O      1 
ATOM   12610 C  CB     . SER   D 2  322 ? 7.207   -11.414  -21.020 1.00 86.70  ? 322 SER   D CB     1 
ATOM   12611 O  OG     . SER   D 2  322 ? 7.174   -12.007  -19.734 1.00 75.21  ? 322 SER   D OG     1 
ATOM   12612 N  N      . MET   D 2  323 ? 3.673   -11.936  -20.709 1.00 79.00  ? 323 MET   D N      1 
ATOM   12613 C  CA     . MET   D 2  323 ? 2.449   -11.527  -20.035 1.00 85.42  ? 323 MET   D CA     1 
ATOM   12614 C  C      . MET   D 2  323 ? 2.643   -11.360  -18.530 1.00 85.67  ? 323 MET   D C      1 
ATOM   12615 O  O      . MET   D 2  323 ? 1.849   -10.663  -17.888 1.00 81.56  ? 323 MET   D O      1 
ATOM   12616 C  CB     . MET   D 2  323 ? 1.350   -12.536  -20.366 1.00 84.84  ? 323 MET   D CB     1 
ATOM   12617 C  CG     . MET   D 2  323 ? 0.894   -12.426  -21.828 1.00 88.16  ? 323 MET   D CG     1 
ATOM   12618 S  SD     . MET   D 2  323 ? 0.438   -14.000  -22.614 1.00 120.79 ? 323 MET   D SD     1 
ATOM   12619 C  CE     . MET   D 2  323 ? 2.028   -14.613  -23.214 1.00 93.08  ? 323 MET   D CE     1 
ATOM   12620 N  N      . LYS   D 2  324 ? 3.683   -11.972  -17.960 1.00 87.37  ? 324 LYS   D N      1 
ATOM   12621 C  CA     . LYS   D 2  324 ? 4.132   -11.594  -16.623 1.00 79.94  ? 324 LYS   D CA     1 
ATOM   12622 C  C      . LYS   D 2  324 ? 4.512   -10.120  -16.572 1.00 76.69  ? 324 LYS   D C      1 
ATOM   12623 O  O      . LYS   D 2  324 ? 4.132   -9.396   -15.647 1.00 80.22  ? 324 LYS   D O      1 
ATOM   12624 C  CB     . LYS   D 2  324 ? 5.318   -12.459  -16.208 1.00 76.47  ? 324 LYS   D CB     1 
ATOM   12625 C  CG     . LYS   D 2  324 ? 5.841   -12.142  -14.839 1.00 77.77  ? 324 LYS   D CG     1 
ATOM   12626 C  CD     . LYS   D 2  324 ? 7.303   -12.494  -14.768 1.00 85.14  ? 324 LYS   D CD     1 
ATOM   12627 C  CE     . LYS   D 2  324 ? 7.921   -11.975  -13.488 1.00 90.06  ? 324 LYS   D CE     1 
ATOM   12628 N  NZ     . LYS   D 2  324 ? 9.316   -12.461  -13.323 1.00 89.98  ? 324 LYS   D NZ     1 
ATOM   12629 N  N      . GLU   D 2  325 ? 5.301   -9.665   -17.539 1.00 76.53  ? 325 GLU   D N      1 
ATOM   12630 C  CA     . GLU   D 2  325 ? 5.592   -8.243   -17.633 1.00 76.65  ? 325 GLU   D CA     1 
ATOM   12631 C  C      . GLU   D 2  325 ? 4.307   -7.426   -17.703 1.00 74.94  ? 325 GLU   D C      1 
ATOM   12632 O  O      . GLU   D 2  325 ? 4.175   -6.401   -17.022 1.00 65.42  ? 325 GLU   D O      1 
ATOM   12633 C  CB     . GLU   D 2  325 ? 6.497   -8.003   -18.843 1.00 79.15  ? 325 GLU   D CB     1 
ATOM   12634 C  CG     . GLU   D 2  325 ? 7.301   -6.723   -18.831 1.00 83.48  ? 325 GLU   D CG     1 
ATOM   12635 C  CD     . GLU   D 2  325 ? 8.241   -6.652   -20.016 1.00 86.06  ? 325 GLU   D CD     1 
ATOM   12636 O  OE1    . GLU   D 2  325 ? 8.517   -7.727   -20.596 1.00 81.03  ? 325 GLU   D OE1    1 
ATOM   12637 O  OE2    . GLU   D 2  325 ? 8.657   -5.536   -20.397 1.00 89.04  ? 325 GLU   D OE2    1 
ATOM   12638 N  N      . VAL   D 2  326 ? 3.333   -7.886   -18.497 1.00 76.66  ? 326 VAL   D N      1 
ATOM   12639 C  CA     . VAL   D 2  326 ? 2.088   -7.136   -18.654 1.00 74.23  ? 326 VAL   D CA     1 
ATOM   12640 C  C      . VAL   D 2  326 ? 1.299   -7.140   -17.358 1.00 71.30  ? 326 VAL   D C      1 
ATOM   12641 O  O      . VAL   D 2  326 ? 0.639   -6.149   -17.015 1.00 65.83  ? 326 VAL   D O      1 
ATOM   12642 C  CB     . VAL   D 2  326 ? 1.246   -7.695   -19.813 1.00 70.64  ? 326 VAL   D CB     1 
ATOM   12643 C  CG1    . VAL   D 2  326 ? -0.050  -6.942   -19.910 1.00 65.42  ? 326 VAL   D CG1    1 
ATOM   12644 C  CG2    . VAL   D 2  326 ? 1.991   -7.555   -21.109 1.00 70.50  ? 326 VAL   D CG2    1 
ATOM   12645 N  N      . ASP   D 2  327 ? 1.336   -8.260   -16.630 1.00 75.60  ? 327 ASP   D N      1 
ATOM   12646 C  CA     . ASP   D 2  327 ? 0.688   -8.325   -15.327 1.00 67.08  ? 327 ASP   D CA     1 
ATOM   12647 C  C      . ASP   D 2  327 ? 1.210   -7.222   -14.423 1.00 65.33  ? 327 ASP   D C      1 
ATOM   12648 O  O      . ASP   D 2  327 ? 0.443   -6.385   -13.941 1.00 61.76  ? 327 ASP   D O      1 
ATOM   12649 C  CB     . ASP   D 2  327 ? 0.927   -9.684   -14.687 1.00 64.23  ? 327 ASP   D CB     1 
ATOM   12650 C  CG     . ASP   D 2  327 ? 0.065   -10.755  -15.282 1.00 70.01  ? 327 ASP   D CG     1 
ATOM   12651 O  OD1    . ASP   D 2  327 ? -0.935  -10.413  -15.943 1.00 66.03  ? 327 ASP   D OD1    1 
ATOM   12652 O  OD2    . ASP   D 2  327 ? 0.354   -11.944  -15.040 1.00 79.05  ? 327 ASP   D OD2    1 
ATOM   12653 N  N      . GLU   D 2  328 ? 2.531   -7.194   -14.217 1.00 69.75  ? 328 GLU   D N      1 
ATOM   12654 C  CA     . GLU   D 2  328 ? 3.160   -6.162   -13.400 1.00 66.95  ? 328 GLU   D CA     1 
ATOM   12655 C  C      . GLU   D 2  328 ? 2.922   -4.771   -13.969 1.00 68.50  ? 328 GLU   D C      1 
ATOM   12656 O  O      . GLU   D 2  328 ? 2.739   -3.809   -13.215 1.00 68.16  ? 328 GLU   D O      1 
ATOM   12657 C  CB     . GLU   D 2  328 ? 4.661   -6.422   -13.286 1.00 70.80  ? 328 GLU   D CB     1 
ATOM   12658 C  CG     . GLU   D 2  328 ? 5.074   -7.884   -13.425 1.00 79.73  ? 328 GLU   D CG     1 
ATOM   12659 C  CD     . GLU   D 2  328 ? 6.571   -8.038   -13.651 1.00 90.27  ? 328 GLU   D CD     1 
ATOM   12660 O  OE1    . GLU   D 2  328 ? 7.147   -7.221   -14.416 1.00 91.18  ? 328 GLU   D OE1    1 
ATOM   12661 O  OE2    . GLU   D 2  328 ? 7.169   -8.970   -13.064 1.00 94.73  ? 328 GLU   D OE2    1 
ATOM   12662 N  N      . GLN   D 2  329 ? 2.934   -4.628   -15.295 1.00 65.84  ? 329 GLN   D N      1 
ATOM   12663 C  CA     . GLN   D 2  329 ? 2.777   -3.289   -15.848 1.00 66.23  ? 329 GLN   D CA     1 
ATOM   12664 C  C      . GLN   D 2  329 ? 1.365   -2.759   -15.651 1.00 69.72  ? 329 GLN   D C      1 
ATOM   12665 O  O      . GLN   D 2  329 ? 1.179   -1.590   -15.281 1.00 66.79  ? 329 GLN   D O      1 
ATOM   12666 C  CB     . GLN   D 2  329 ? 3.170   -3.275   -17.314 1.00 65.63  ? 329 GLN   D CB     1 
ATOM   12667 C  CG     . GLN   D 2  329 ? 4.633   -3.066   -17.419 1.00 72.48  ? 329 GLN   D CG     1 
ATOM   12668 C  CD     . GLN   D 2  329 ? 5.065   -1.924   -16.531 1.00 74.46  ? 329 GLN   D CD     1 
ATOM   12669 O  OE1    . GLN   D 2  329 ? 4.338   -0.928   -16.374 1.00 77.59  ? 329 GLN   D OE1    1 
ATOM   12670 N  NE2    . GLN   D 2  329 ? 6.220   -2.082   -15.890 1.00 67.93  ? 329 GLN   D NE2    1 
ATOM   12671 N  N      . MET   D 2  330 ? 0.359   -3.604   -15.889 1.00 66.43  ? 330 MET   D N      1 
ATOM   12672 C  CA     . MET   D 2  330 ? -1.011  -3.174   -15.653 1.00 63.04  ? 330 MET   D CA     1 
ATOM   12673 C  C      . MET   D 2  330 ? -1.259  -2.925   -14.171 1.00 65.01  ? 330 MET   D C      1 
ATOM   12674 O  O      . MET   D 2  330 ? -2.116  -2.105   -13.817 1.00 63.96  ? 330 MET   D O      1 
ATOM   12675 C  CB     . MET   D 2  330 ? -1.999  -4.202   -16.196 1.00 62.80  ? 330 MET   D CB     1 
ATOM   12676 C  CG     . MET   D 2  330 ? -2.230  -4.147   -17.695 1.00 56.75  ? 330 MET   D CG     1 
ATOM   12677 S  SD     . MET   D 2  330 ? -2.744  -2.503   -18.199 1.00 62.58  ? 330 MET   D SD     1 
ATOM   12678 C  CE     . MET   D 2  330 ? -4.194  -2.261   -17.195 1.00 64.96  ? 330 MET   D CE     1 
ATOM   12679 N  N      . LEU   D 2  331 ? -0.515  -3.622   -13.299 1.00 65.97  ? 331 LEU   D N      1 
ATOM   12680 C  CA     . LEU   D 2  331 ? -0.568  -3.368   -11.861 1.00 61.54  ? 331 LEU   D CA     1 
ATOM   12681 C  C      . LEU   D 2  331 ? 0.205   -2.109   -11.491 1.00 61.26  ? 331 LEU   D C      1 
ATOM   12682 O  O      . LEU   D 2  331 ? -0.238  -1.318   -10.652 1.00 56.56  ? 331 LEU   D O      1 
ATOM   12683 C  CB     . LEU   D 2  331 ? -0.023  -4.582   -11.101 1.00 64.00  ? 331 LEU   D CB     1 
ATOM   12684 C  CG     . LEU   D 2  331 ? -0.929  -5.758   -10.698 1.00 71.25  ? 331 LEU   D CG     1 
ATOM   12685 C  CD1    . LEU   D 2  331 ? -1.116  -6.783   -11.804 1.00 78.71  ? 331 LEU   D CD1    1 
ATOM   12686 C  CD2    . LEU   D 2  331 ? -0.317  -6.452   -9.513  1.00 68.31  ? 331 LEU   D CD2    1 
ATOM   12687 N  N      . ASN   D 2  332 ? 1.365   -1.900   -12.095 1.00 65.35  ? 332 ASN   D N      1 
ATOM   12688 C  CA     . ASN   D 2  332 ? 2.108   -0.707   -11.738 1.00 65.78  ? 332 ASN   D CA     1 
ATOM   12689 C  C      . ASN   D 2  332 ? 1.241   0.518    -11.963 1.00 63.32  ? 332 ASN   D C      1 
ATOM   12690 O  O      . ASN   D 2  332 ? 1.126   1.367    -11.073 1.00 63.00  ? 332 ASN   D O      1 
ATOM   12691 C  CB     . ASN   D 2  332 ? 3.435   -0.662   -12.518 1.00 73.08  ? 332 ASN   D CB     1 
ATOM   12692 C  CG     . ASN   D 2  332 ? 4.156   0.687    -12.430 1.00 81.68  ? 332 ASN   D CG     1 
ATOM   12693 O  OD1    . ASN   D 2  332 ? 3.965   1.562    -13.279 1.00 87.28  ? 332 ASN   D OD1    1 
ATOM   12694 N  ND2    . ASN   D 2  332 ? 4.980   0.863    -11.391 1.00 84.66  ? 332 ASN   D ND2    1 
ATOM   12695 N  N      . VAL   D 2  333 ? 0.518   0.556    -13.093 1.00 61.71  ? 333 VAL   D N      1 
ATOM   12696 C  CA     . VAL   D 2  333 ? -0.166  1.779    -13.522 1.00 59.93  ? 333 VAL   D CA     1 
ATOM   12697 C  C      . VAL   D 2  333 ? -1.343  2.109    -12.610 1.00 55.07  ? 333 VAL   D C      1 
ATOM   12698 O  O      . VAL   D 2  333 ? -1.702  3.284    -12.445 1.00 51.61  ? 333 VAL   D O      1 
ATOM   12699 C  CB     . VAL   D 2  333 ? -0.617  1.652    -14.989 1.00 62.24  ? 333 VAL   D CB     1 
ATOM   12700 C  CG1    . VAL   D 2  333 ? -1.682  0.582    -15.109 1.00 67.24  ? 333 VAL   D CG1    1 
ATOM   12701 C  CG2    . VAL   D 2  333 ? -1.140  2.973    -15.512 1.00 59.15  ? 333 VAL   D CG2    1 
ATOM   12702 N  N      . GLN   D 2  334 ? -1.967  1.094    -12.012 1.00 53.81  ? 334 GLN   D N      1 
ATOM   12703 C  CA     . GLN   D 2  334 ? -3.074  1.348    -11.097 1.00 49.73  ? 334 GLN   D CA     1 
ATOM   12704 C  C      . GLN   D 2  334 ? -2.566  1.841    -9.747  1.00 55.48  ? 334 GLN   D C      1 
ATOM   12705 O  O      . GLN   D 2  334 ? -3.190  2.711    -9.131  1.00 59.09  ? 334 GLN   D O      1 
ATOM   12706 C  CB     . GLN   D 2  334 ? -3.902  0.086    -10.917 1.00 48.80  ? 334 GLN   D CB     1 
ATOM   12707 C  CG     . GLN   D 2  334 ? -4.245  -0.636   -12.200 1.00 53.09  ? 334 GLN   D CG     1 
ATOM   12708 C  CD     . GLN   D 2  334 ? -5.082  -1.886   -11.965 1.00 47.58  ? 334 GLN   D CD     1 
ATOM   12709 O  OE1    . GLN   D 2  334 ? -6.143  -1.837   -11.330 1.00 45.28  ? 334 GLN   D OE1    1 
ATOM   12710 N  NE2    . GLN   D 2  334 ? -4.579  -3.022   -12.433 1.00 48.41  ? 334 GLN   D NE2    1 
ATOM   12711 N  N      . ASN   D 2  335 ? -1.454  1.279    -9.257  1.00 54.97  ? 335 ASN   D N      1 
ATOM   12712 C  CA     . ASN   D 2  335 ? -0.717  1.844    -8.129  1.00 50.60  ? 335 ASN   D CA     1 
ATOM   12713 C  C      . ASN   D 2  335 ? -0.382  3.299    -8.347  1.00 51.85  ? 335 ASN   D C      1 
ATOM   12714 O  O      . ASN   D 2  335 ? -0.902  4.180    -7.657  1.00 52.73  ? 335 ASN   D O      1 
ATOM   12715 C  CB     . ASN   D 2  335 ? 0.594   1.102    -7.909  1.00 56.57  ? 335 ASN   D CB     1 
ATOM   12716 C  CG     . ASN   D 2  335 ? 0.391   -0.306   -7.417  1.00 73.23  ? 335 ASN   D CG     1 
ATOM   12717 O  OD1    . ASN   D 2  335 ? -0.621  -0.608   -6.769  1.00 81.11  ? 335 ASN   D OD1    1 
ATOM   12718 N  ND2    . ASN   D 2  335 ? 1.328   -1.197   -7.755  1.00 74.66  ? 335 ASN   D ND2    1 
ATOM   12719 N  N      . LYS   D 2  336 ? 0.519   3.531    -9.300  1.00 56.43  ? 336 LYS   D N      1 
ATOM   12720 C  CA     . LYS   D 2  336 ? 1.016   4.862    -9.593  1.00 51.91  ? 336 LYS   D CA     1 
ATOM   12721 C  C      . LYS   D 2  336 ? -0.117  5.838    -9.920  1.00 51.37  ? 336 LYS   D C      1 
ATOM   12722 O  O      . LYS   D 2  336 ? 0.056   7.046    -9.734  1.00 53.74  ? 336 LYS   D O      1 
ATOM   12723 C  CB     . LYS   D 2  336 ? 2.043   4.741    -10.727 1.00 55.35  ? 336 LYS   D CB     1 
ATOM   12724 C  CG     . LYS   D 2  336 ? 3.350   4.016    -10.303 1.00 63.23  ? 336 LYS   D CG     1 
ATOM   12725 C  CD     . LYS   D 2  336 ? 4.525   4.289    -11.250 1.00 76.97  ? 336 LYS   D CD     1 
ATOM   12726 C  CE     . LYS   D 2  336 ? 4.038   4.336    -12.706 1.00 85.39  ? 336 LYS   D CE     1 
ATOM   12727 N  NZ     . LYS   D 2  336 ? 5.088   4.695    -13.698 1.00 92.09  ? 336 LYS   D NZ     1 
ATOM   12728 N  N      . ASN   D 2  337 ? -1.290  5.351    -10.344 1.00 52.97  ? 337 ASN   D N      1 
ATOM   12729 C  CA     . ASN   D 2  337 ? -2.418  6.220    -10.689 1.00 53.73  ? 337 ASN   D CA     1 
ATOM   12730 C  C      . ASN   D 2  337 ? -3.691  5.860    -9.926  1.00 55.74  ? 337 ASN   D C      1 
ATOM   12731 O  O      . ASN   D 2  337 ? -4.805  6.014    -10.443 1.00 53.46  ? 337 ASN   D O      1 
ATOM   12732 C  CB     . ASN   D 2  337 ? -2.713  6.206    -12.187 1.00 52.29  ? 337 ASN   D CB     1 
ATOM   12733 C  CG     . ASN   D 2  337 ? -1.537  6.592    -13.003 1.00 54.45  ? 337 ASN   D CG     1 
ATOM   12734 O  OD1    . ASN   D 2  337 ? -1.376  7.770    -13.308 1.00 61.80  ? 337 ASN   D OD1    1 
ATOM   12735 N  ND2    . ASN   D 2  337 ? -0.755  5.615    -13.447 1.00 51.34  ? 337 ASN   D ND2    1 
ATOM   12736 N  N      . SER   D 2  338 ? -3.561  5.429    -8.668  1.00 57.34  ? 338 SER   D N      1 
ATOM   12737 C  CA     . SER   D 2  338 ? -4.711  4.878    -7.955  1.00 49.11  ? 338 SER   D CA     1 
ATOM   12738 C  C      . SER   D 2  338 ? -5.843  5.881    -7.795  1.00 50.50  ? 338 SER   D C      1 
ATOM   12739 O  O      . SER   D 2  338 ? -7.009  5.486    -7.766  1.00 55.75  ? 338 SER   D O      1 
ATOM   12740 C  CB     . SER   D 2  338 ? -4.277  4.384    -6.589  1.00 53.72  ? 338 SER   D CB     1 
ATOM   12741 O  OG     . SER   D 2  338 ? -3.905  5.488    -5.794  1.00 60.83  ? 338 SER   D OG     1 
ATOM   12742 N  N      . SER   D 2  339 ? -5.540  7.170    -7.678  1.00 50.35  ? 339 SER   D N      1 
ATOM   12743 C  CA     . SER   D 2  339 ? -6.620  8.112    -7.403  1.00 51.63  ? 339 SER   D CA     1 
ATOM   12744 C  C      . SER   D 2  339 ? -7.505  8.369    -8.609  1.00 51.56  ? 339 SER   D C      1 
ATOM   12745 O  O      . SER   D 2  339 ? -8.458  9.150    -8.499  1.00 55.80  ? 339 SER   D O      1 
ATOM   12746 C  CB     . SER   D 2  339 ? -6.062  9.432    -6.841  1.00 57.24  ? 339 SER   D CB     1 
ATOM   12747 O  OG     . SER   D 2  339 ? -4.912  9.898    -7.525  1.00 58.57  ? 339 SER   D OG     1 
ATOM   12748 N  N      . TYR   D 2  340 ? -7.250  7.700    -9.731  1.00 53.47  ? 340 TYR   D N      1 
ATOM   12749 C  CA     . TYR   D 2  340 ? -8.047  7.855    -10.941 1.00 53.11  ? 340 TYR   D CA     1 
ATOM   12750 C  C      . TYR   D 2  340 ? -8.918  6.637    -11.248 1.00 53.98  ? 340 TYR   D C      1 
ATOM   12751 O  O      . TYR   D 2  340 ? -9.424  6.525    -12.373 1.00 53.40  ? 340 TYR   D O      1 
ATOM   12752 C  CB     . TYR   D 2  340 ? -7.131  8.178    -12.127 1.00 45.51  ? 340 TYR   D CB     1 
ATOM   12753 C  CG     . TYR   D 2  340 ? -6.352  9.482    -11.998 1.00 46.67  ? 340 TYR   D CG     1 
ATOM   12754 C  CD1    . TYR   D 2  340 ? -6.994  10.701   -12.080 1.00 44.48  ? 340 TYR   D CD1    1 
ATOM   12755 C  CD2    . TYR   D 2  340 ? -4.973  9.483    -11.796 1.00 48.80  ? 340 TYR   D CD2    1 
ATOM   12756 C  CE1    . TYR   D 2  340 ? -6.292  11.880   -11.970 1.00 50.18  ? 340 TYR   D CE1    1 
ATOM   12757 C  CE2    . TYR   D 2  340 ? -4.263  10.651   -11.688 1.00 45.92  ? 340 TYR   D CE2    1 
ATOM   12758 C  CZ     . TYR   D 2  340 ? -4.926  11.856   -11.777 1.00 52.16  ? 340 TYR   D CZ     1 
ATOM   12759 O  OH     . TYR   D 2  340 ? -4.222  13.046   -11.680 1.00 54.56  ? 340 TYR   D OH     1 
ATOM   12760 N  N      . PHE   D 2  341 ? -9.111  5.729    -10.279 1.00 51.61  ? 341 PHE   D N      1 
ATOM   12761 C  CA     . PHE   D 2  341 ? -9.993  4.567    -10.410 1.00 45.55  ? 341 PHE   D CA     1 
ATOM   12762 C  C      . PHE   D 2  341 ? -10.958 4.562    -9.233  1.00 46.75  ? 341 PHE   D C      1 
ATOM   12763 O  O      . PHE   D 2  341 ? -10.513 4.645    -8.083  1.00 50.75  ? 341 PHE   D O      1 
ATOM   12764 C  CB     . PHE   D 2  341 ? -9.201  3.262    -10.404 1.00 39.66  ? 341 PHE   D CB     1 
ATOM   12765 C  CG     . PHE   D 2  341 ? -8.187  3.159    -11.480 1.00 43.01  ? 341 PHE   D CG     1 
ATOM   12766 C  CD1    . PHE   D 2  341 ? -6.915  3.683    -11.298 1.00 43.30  ? 341 PHE   D CD1    1 
ATOM   12767 C  CD2    . PHE   D 2  341 ? -8.502  2.541    -12.689 1.00 45.80  ? 341 PHE   D CD2    1 
ATOM   12768 C  CE1    . PHE   D 2  341 ? -5.961  3.589    -12.299 1.00 44.73  ? 341 PHE   D CE1    1 
ATOM   12769 C  CE2    . PHE   D 2  341 ? -7.562  2.447    -13.704 1.00 48.08  ? 341 PHE   D CE2    1 
ATOM   12770 C  CZ     . PHE   D 2  341 ? -6.285  2.976    -13.506 1.00 48.56  ? 341 PHE   D CZ     1 
ATOM   12771 N  N      . VAL   D 2  342 ? -12.267 4.468    -9.479  1.00 38.27  ? 342 VAL   D N      1 
ATOM   12772 C  CA     . VAL   D 2  342 ? -13.152 4.527    -8.325  1.00 39.88  ? 342 VAL   D CA     1 
ATOM   12773 C  C      . VAL   D 2  342 ? -12.831 3.384    -7.374  1.00 45.34  ? 342 VAL   D C      1 
ATOM   12774 O  O      . VAL   D 2  342 ? -12.631 2.231    -7.782  1.00 46.35  ? 342 VAL   D O      1 
ATOM   12775 C  CB     . VAL   D 2  342 ? -14.641 4.525    -8.702  1.00 41.55  ? 342 VAL   D CB     1 
ATOM   12776 C  CG1    . VAL   D 2  342 ? -14.956 5.701    -9.558  1.00 45.24  ? 342 VAL   D CG1    1 
ATOM   12777 C  CG2    . VAL   D 2  342 ? -15.024 3.221    -9.356  1.00 45.77  ? 342 VAL   D CG2    1 
ATOM   12778 N  N      . GLU   D 2  343 ? -12.798 3.714    -6.082  1.00 44.06  ? 343 GLU   D N      1 
ATOM   12779 C  CA     . GLU   D 2  343 ? -12.428 2.785    -5.029  1.00 42.84  ? 343 GLU   D CA     1 
ATOM   12780 C  C      . GLU   D 2  343 ? -13.532 1.805    -4.636  1.00 43.24  ? 343 GLU   D C      1 
ATOM   12781 O  O      . GLU   D 2  343 ? -13.205 0.746    -4.091  1.00 44.31  ? 343 GLU   D O      1 
ATOM   12782 C  CB     . GLU   D 2  343 ? -11.967 3.575    -3.803  1.00 50.46  ? 343 GLU   D CB     1 
ATOM   12783 C  CG     . GLU   D 2  343 ? -13.003 4.544    -3.251  1.00 56.95  ? 343 GLU   D CG     1 
ATOM   12784 C  CD     . GLU   D 2  343 ? -12.553 5.183    -1.963  1.00 64.59  ? 343 GLU   D CD     1 
ATOM   12785 O  OE1    . GLU   D 2  343 ? -11.358 5.021    -1.601  1.00 68.23  ? 343 GLU   D OE1    1 
ATOM   12786 O  OE2    . GLU   D 2  343 ? -13.406 5.819    -1.302  1.00 73.03  ? 343 GLU   D OE2    1 
ATOM   12787 N  N      . TRP   D 2  344 ? -14.809 2.116    -4.898  1.00 37.92  ? 344 TRP   D N      1 
ATOM   12788 C  CA     . TRP   D 2  344 ? -15.945 1.264    -4.539  1.00 38.05  ? 344 TRP   D CA     1 
ATOM   12789 C  C      . TRP   D 2  344 ? -16.275 0.176    -5.588  1.00 42.61  ? 344 TRP   D C      1 
ATOM   12790 O  O      . TRP   D 2  344 ? -17.299 -0.505   -5.457  1.00 42.76  ? 344 TRP   D O      1 
ATOM   12791 C  CB     . TRP   D 2  344 ? -17.197 2.126    -4.264  1.00 42.88  ? 344 TRP   D CB     1 
ATOM   12792 C  CG     . TRP   D 2  344 ? -17.369 3.359    -5.191  1.00 47.36  ? 344 TRP   D CG     1 
ATOM   12793 C  CD1    . TRP   D 2  344 ? -16.867 4.629    -4.997  1.00 47.42  ? 344 TRP   D CD1    1 
ATOM   12794 C  CD2    . TRP   D 2  344 ? -18.051 3.398    -6.445  1.00 45.02  ? 344 TRP   D CD2    1 
ATOM   12795 N  NE1    . TRP   D 2  344 ? -17.205 5.440    -6.044  1.00 45.42  ? 344 TRP   D NE1    1 
ATOM   12796 C  CE2    . TRP   D 2  344 ? -17.922 4.705    -6.953  1.00 49.16  ? 344 TRP   D CE2    1 
ATOM   12797 C  CE3    . TRP   D 2  344 ? -18.747 2.448    -7.198  1.00 42.98  ? 344 TRP   D CE3    1 
ATOM   12798 C  CZ2    . TRP   D 2  344 ? -18.478 5.083    -8.175  1.00 49.86  ? 344 TRP   D CZ2    1 
ATOM   12799 C  CZ3    . TRP   D 2  344 ? -19.295 2.827    -8.407  1.00 42.21  ? 344 TRP   D CZ3    1 
ATOM   12800 C  CH2    . TRP   D 2  344 ? -19.162 4.130    -8.881  1.00 43.61  ? 344 TRP   D CH2    1 
ATOM   12801 N  N      . ILE   D 2  345 ? -15.448 -0.005   -6.617  1.00 41.50  ? 345 ILE   D N      1 
ATOM   12802 C  CA     . ILE   D 2  345 ? -15.597 -1.135   -7.541  1.00 38.76  ? 345 ILE   D CA     1 
ATOM   12803 C  C      . ILE   D 2  345 ? -14.259 -1.859   -7.592  1.00 35.96  ? 345 ILE   D C      1 
ATOM   12804 O  O      . ILE   D 2  345 ? -13.414 -1.532   -8.430  1.00 34.43  ? 345 ILE   D O      1 
ATOM   12805 C  CB     . ILE   D 2  345 ? -16.007 -0.694   -8.956  1.00 41.71  ? 345 ILE   D CB     1 
ATOM   12806 C  CG1    . ILE   D 2  345 ? -17.330 0.061    -8.966  1.00 40.76  ? 345 ILE   D CG1    1 
ATOM   12807 C  CG2    . ILE   D 2  345 ? -16.131 -1.879   -9.874  1.00 32.81  ? 345 ILE   D CG2    1 
ATOM   12808 C  CD1    . ILE   D 2  345 ? -17.663 0.524    -10.366 1.00 38.22  ? 345 ILE   D CD1    1 
ATOM   12809 N  N      . PRO   D 2  346 ? -14.026 -2.835   -6.727  1.00 34.75  ? 346 PRO   D N      1 
ATOM   12810 C  CA     . PRO   D 2  346 ? -12.704 -3.465   -6.660  1.00 34.88  ? 346 PRO   D CA     1 
ATOM   12811 C  C      . PRO   D 2  346 ? -12.344 -4.119   -7.976  1.00 36.11  ? 346 PRO   D C      1 
ATOM   12812 O  O      . PRO   D 2  346 ? -13.212 -4.611   -8.694  1.00 39.76  ? 346 PRO   D O      1 
ATOM   12813 C  CB     . PRO   D 2  346 ? -12.872 -4.518   -5.568  1.00 31.65  ? 346 PRO   D CB     1 
ATOM   12814 C  CG     . PRO   D 2  346 ? -14.103 -4.054   -4.803  1.00 33.07  ? 346 PRO   D CG     1 
ATOM   12815 C  CD     . PRO   D 2  346 ? -14.988 -3.453   -5.811  1.00 31.28  ? 346 PRO   D CD     1 
ATOM   12816 N  N      . ASN   D 2  347 ? -11.051 -4.154   -8.278  1.00 34.48  ? 347 ASN   D N      1 
ATOM   12817 C  CA     . ASN   D 2  347 ? -10.554 -4.976   -9.384  1.00 35.97  ? 347 ASN   D CA     1 
ATOM   12818 C  C      . ASN   D 2  347 ? -11.336 -4.658   -10.649 1.00 40.35  ? 347 ASN   D C      1 
ATOM   12819 O  O      . ASN   D 2  347 ? -11.809 -5.545   -11.368 1.00 46.28  ? 347 ASN   D O      1 
ATOM   12820 C  CB     . ASN   D 2  347 ? -10.642 -6.458   -9.025  1.00 36.34  ? 347 ASN   D CB     1 
ATOM   12821 C  CG     . ASN   D 2  347 ? -10.095 -6.745   -7.621  1.00 43.45  ? 347 ASN   D CG     1 
ATOM   12822 O  OD1    . ASN   D 2  347 ? -10.828 -7.185   -6.720  1.00 42.83  ? 347 ASN   D OD1    1 
ATOM   12823 N  ND2    . ASN   D 2  347 ? -8.793  -6.527   -7.442  1.00 42.56  ? 347 ASN   D ND2    1 
ATOM   12824 N  N      . ASN   D 2  348 ? -11.492 -3.357   -10.892 1.00 38.49  ? 348 ASN   D N      1 
ATOM   12825 C  CA     . ASN   D 2  348 ? -12.235 -2.834   -12.016 1.00 37.10  ? 348 ASN   D CA     1 
ATOM   12826 C  C      . ASN   D 2  348 ? -11.373 -2.620   -13.238 1.00 40.86  ? 348 ASN   D C      1 
ATOM   12827 O  O      . ASN   D 2  348 ? -11.844 -1.991   -14.187 1.00 50.31  ? 348 ASN   D O      1 
ATOM   12828 C  CB     . ASN   D 2  348 ? -12.935 -1.512   -11.647 1.00 38.34  ? 348 ASN   D CB     1 
ATOM   12829 C  CG     . ASN   D 2  348 ? -11.977 -0.413   -11.205 1.00 39.70  ? 348 ASN   D CG     1 
ATOM   12830 O  OD1    . ASN   D 2  348 ? -10.839 -0.656   -10.809 1.00 41.42  ? 348 ASN   D OD1    1 
ATOM   12831 N  ND2    . ASN   D 2  348 ? -12.468 0.814    -11.231 1.00 44.03  ? 348 ASN   D ND2    1 
ATOM   12832 N  N      . VAL   D 2  349 ? -10.146 -3.138   -13.266 1.00 37.33  ? 349 VAL   D N      1 
ATOM   12833 C  CA     . VAL   D 2  349 ? -9.281  -2.993   -14.439 1.00 45.81  ? 349 VAL   D CA     1 
ATOM   12834 C  C      . VAL   D 2  349 ? -8.857  -4.384   -14.910 1.00 49.61  ? 349 VAL   D C      1 
ATOM   12835 O  O      . VAL   D 2  349 ? -7.928  -4.984   -14.358 1.00 55.76  ? 349 VAL   D O      1 
ATOM   12836 C  CB     . VAL   D 2  349 ? -8.066  -2.111   -14.150 1.00 42.75  ? 349 VAL   D CB     1 
ATOM   12837 C  CG1    . VAL   D 2  349 ? -7.277  -1.884   -15.427 1.00 43.89  ? 349 VAL   D CG1    1 
ATOM   12838 C  CG2    . VAL   D 2  349 ? -8.499  -0.803   -13.508 1.00 42.31  ? 349 VAL   D CG2    1 
ATOM   12839 N  N      . LYS   D 2  350 ? -9.495  -4.891   -15.958 1.00 48.05  ? 350 LYS   D N      1 
ATOM   12840 C  CA     . LYS   D 2  350 ? -9.257  -6.236   -16.458 1.00 46.54  ? 350 LYS   D CA     1 
ATOM   12841 C  C      . LYS   D 2  350 ? -8.503  -6.178   -17.781 1.00 48.88  ? 350 LYS   D C      1 
ATOM   12842 O  O      . LYS   D 2  350 ? -8.636  -5.219   -18.544 1.00 50.05  ? 350 LYS   D O      1 
ATOM   12843 C  CB     . LYS   D 2  350 ? -10.587 -6.970   -16.622 1.00 43.64  ? 350 LYS   D CB     1 
ATOM   12844 C  CG     . LYS   D 2  350 ? -10.502 -8.476   -16.557 1.00 55.91  ? 350 LYS   D CG     1 
ATOM   12845 C  CD     . LYS   D 2  350 ? -10.471 -8.867   -15.077 1.00 63.00  ? 350 LYS   D CD     1 
ATOM   12846 C  CE     . LYS   D 2  350 ? -11.602 -8.195   -14.299 1.00 55.40  ? 350 LYS   D CE     1 
ATOM   12847 N  NZ     . LYS   D 2  350 ? -11.642 -8.712   -12.933 1.00 57.23  ? 350 LYS   D NZ     1 
ATOM   12848 N  N      . THR   D 2  351 ? -7.714  -7.215   -18.068 1.00 52.74  ? 351 THR   D N      1 
ATOM   12849 C  CA     . THR   D 2  351 ? -6.938  -7.247   -19.306 1.00 59.38  ? 351 THR   D CA     1 
ATOM   12850 C  C      . THR   D 2  351 ? -6.910  -8.631   -19.956 1.00 53.77  ? 351 THR   D C      1 
ATOM   12851 O  O      . THR   D 2  351 ? -6.852  -9.660   -19.280 1.00 45.96  ? 351 THR   D O      1 
ATOM   12852 C  CB     . THR   D 2  351 ? -5.511  -6.790   -19.048 1.00 60.08  ? 351 THR   D CB     1 
ATOM   12853 O  OG1    . THR   D 2  351 ? -4.874  -7.762   -18.216 1.00 64.93  ? 351 THR   D OG1    1 
ATOM   12854 C  CG2    . THR   D 2  351 ? -5.502  -5.431   -18.361 1.00 61.79  ? 351 THR   D CG2    1 
ATOM   12855 N  N      . ALA   D 2  352 ? -6.916  -8.630   -21.294 1.00 55.56  ? 352 ALA   D N      1 
ATOM   12856 C  CA     . ALA   D 2  352 ? -6.721  -9.819   -22.117 1.00 57.94  ? 352 ALA   D CA     1 
ATOM   12857 C  C      . ALA   D 2  352 ? -5.502  -9.655   -23.022 1.00 58.56  ? 352 ALA   D C      1 
ATOM   12858 O  O      . ALA   D 2  352 ? -5.058  -8.537   -23.313 1.00 54.86  ? 352 ALA   D O      1 
ATOM   12859 C  CB     . ALA   D 2  352 ? -7.950  -10.116  -22.983 1.00 57.38  ? 352 ALA   D CB     1 
ATOM   12860 N  N      . VAL   D 2  353 ? -4.965  -10.790  -23.480 1.00 59.04  ? 353 VAL   D N      1 
ATOM   12861 C  CA     . VAL   D 2  353 ? -3.837  -10.798  -24.406 1.00 66.45  ? 353 VAL   D CA     1 
ATOM   12862 C  C      . VAL   D 2  353 ? -4.125  -11.755  -25.555 1.00 62.95  ? 353 VAL   D C      1 
ATOM   12863 O  O      . VAL   D 2  353 ? -4.664  -12.844  -25.341 1.00 64.52  ? 353 VAL   D O      1 
ATOM   12864 C  CB     . VAL   D 2  353 ? -2.526  -11.190  -23.705 1.00 62.69  ? 353 VAL   D CB     1 
ATOM   12865 C  CG1    . VAL   D 2  353 ? -2.425  -12.693  -23.610 1.00 64.96  ? 353 VAL   D CG1    1 
ATOM   12866 C  CG2    . VAL   D 2  353 ? -1.350  -10.621  -24.468 1.00 70.92  ? 353 VAL   D CG2    1 
ATOM   12867 N  N      . CYS   D 2  354 ? -3.741  -11.353  -26.772 1.00 62.77  ? 354 CYS   D N      1 
ATOM   12868 C  CA     . CYS   D 2  354 ? -3.915  -12.142  -27.990 1.00 66.08  ? 354 CYS   D CA     1 
ATOM   12869 C  C      . CYS   D 2  354 ? -2.584  -12.262  -28.731 1.00 65.45  ? 354 CYS   D C      1 
ATOM   12870 O  O      . CYS   D 2  354 ? -1.738  -11.366  -28.661 1.00 68.17  ? 354 CYS   D O      1 
ATOM   12871 C  CB     . CYS   D 2  354 ? -4.985  -11.493  -28.904 1.00 70.67  ? 354 CYS   D CB     1 
ATOM   12872 S  SG     . CYS   D 2  354 ? -5.470  -12.401  -30.402 1.00 64.70  ? 354 CYS   D SG     1 
ATOM   12873 N  N      . ASP   D 2  355 ? -2.410  -13.364  -29.476 1.00 67.32  ? 355 ASP   D N      1 
ATOM   12874 C  CA     . ASP   D 2  355 ? -1.143  -13.594  -30.183 1.00 71.22  ? 355 ASP   D CA     1 
ATOM   12875 C  C      . ASP   D 2  355 ? -1.057  -12.918  -31.558 1.00 69.11  ? 355 ASP   D C      1 
ATOM   12876 O  O      . ASP   D 2  355 ? 0.047   -12.593  -32.005 1.00 66.99  ? 355 ASP   D O      1 
ATOM   12877 C  CB     . ASP   D 2  355 ? -0.888  -15.094  -30.327 1.00 72.71  ? 355 ASP   D CB     1 
ATOM   12878 C  CG     . ASP   D 2  355 ? -0.364  -15.712  -29.058 1.00 73.37  ? 355 ASP   D CG     1 
ATOM   12879 O  OD1    . ASP   D 2  355 ? 0.491   -15.073  -28.422 1.00 76.39  ? 355 ASP   D OD1    1 
ATOM   12880 O  OD2    . ASP   D 2  355 ? -0.809  -16.821  -28.693 1.00 71.52  ? 355 ASP   D OD2    1 
ATOM   12881 N  N      . ILE   D 2  356 ? -2.161  -12.679  -32.253 1.00 60.81  ? 356 ILE   D N      1 
ATOM   12882 C  CA     . ILE   D 2  356 ? -2.129  -11.972  -33.527 1.00 73.11  ? 356 ILE   D CA     1 
ATOM   12883 C  C      . ILE   D 2  356 ? -2.210  -10.468  -33.258 1.00 77.85  ? 356 ILE   D C      1 
ATOM   12884 O  O      . ILE   D 2  356 ? -3.259  -9.995   -32.793 1.00 83.03  ? 356 ILE   D O      1 
ATOM   12885 C  CB     . ILE   D 2  356 ? -3.252  -12.409  -34.472 1.00 80.44  ? 356 ILE   D CB     1 
ATOM   12886 C  CG1    . ILE   D 2  356 ? -3.216  -11.504  -35.722 1.00 79.91  ? 356 ILE   D CG1    1 
ATOM   12887 C  CG2    . ILE   D 2  356 ? -4.591  -12.451  -33.743 1.00 77.17  ? 356 ILE   D CG2    1 
ATOM   12888 C  CD1    . ILE   D 2  356 ? -4.183  -11.890  -36.824 1.00 83.30  ? 356 ILE   D CD1    1 
ATOM   12889 N  N      . PRO   D 2  357 ? -1.176  -9.694   -33.577 1.00 75.09  ? 357 PRO   D N      1 
ATOM   12890 C  CA     . PRO   D 2  357 ? -1.340  -8.233   -33.657 1.00 75.21  ? 357 PRO   D CA     1 
ATOM   12891 C  C      . PRO   D 2  357 ? -1.879  -7.829   -35.013 1.00 77.78  ? 357 PRO   D C      1 
ATOM   12892 O  O      . PRO   D 2  357 ? -1.785  -8.605   -35.973 1.00 83.80  ? 357 PRO   D O      1 
ATOM   12893 C  CB     . PRO   D 2  357 ? 0.080   -7.694   -33.434 1.00 75.19  ? 357 PRO   D CB     1 
ATOM   12894 C  CG     . PRO   D 2  357 ? 1.008   -8.877   -33.659 1.00 75.09  ? 357 PRO   D CG     1 
ATOM   12895 C  CD     . PRO   D 2  357 ? 0.194   -10.122  -33.892 1.00 69.80  ? 357 PRO   D CD     1 
ATOM   12896 N  N      . PRO   D 2  358 ? -2.464  -6.640   -35.131 1.00 77.74  ? 358 PRO   D N      1 
ATOM   12897 C  CA     . PRO   D 2  358 ? -2.958  -6.195   -36.442 1.00 90.01  ? 358 PRO   D CA     1 
ATOM   12898 C  C      . PRO   D 2  358 ? -1.834  -6.134   -37.469 1.00 91.93  ? 358 PRO   D C      1 
ATOM   12899 O  O      . PRO   D 2  358 ? -0.656  -5.999   -37.131 1.00 89.61  ? 358 PRO   D O      1 
ATOM   12900 C  CB     . PRO   D 2  358 ? -3.537  -4.802   -36.154 1.00 88.11  ? 358 PRO   D CB     1 
ATOM   12901 C  CG     . PRO   D 2  358 ? -2.782  -4.332   -34.939 1.00 82.65  ? 358 PRO   D CG     1 
ATOM   12902 C  CD     . PRO   D 2  358 ? -2.528  -5.575   -34.117 1.00 74.65  ? 358 PRO   D CD     1 
ATOM   12903 N  N      . ARG   D 2  359 ? -2.207  -6.253   -38.740 1.00 91.14  ? 359 ARG   D N      1 
ATOM   12904 C  CA     . ARG   D 2  359 ? -1.225  -6.066   -39.798 1.00 91.75  ? 359 ARG   D CA     1 
ATOM   12905 C  C      . ARG   D 2  359 ? -0.505  -4.746   -39.587 1.00 93.99  ? 359 ARG   D C      1 
ATOM   12906 O  O      . ARG   D 2  359 ? -1.135  -3.681   -39.553 1.00 88.13  ? 359 ARG   D O      1 
ATOM   12907 C  CB     . ARG   D 2  359 ? -1.893  -6.094   -41.176 1.00 84.01  ? 359 ARG   D CB     1 
ATOM   12908 N  N      . GLY   D 2  360 ? 0.811   -4.826   -39.388 1.00 91.18  ? 360 GLY   D N      1 
ATOM   12909 C  CA     . GLY   D 2  360 ? 1.676   -3.663   -39.428 1.00 99.40  ? 360 GLY   D CA     1 
ATOM   12910 C  C      . GLY   D 2  360 ? 2.228   -3.220   -38.094 1.00 96.92  ? 360 GLY   D C      1 
ATOM   12911 O  O      . GLY   D 2  360 ? 3.050   -2.290   -38.064 1.00 94.31  ? 360 GLY   D O      1 
ATOM   12912 N  N      . LEU   D 2  361 ? 1.799   -3.832   -36.994 1.00 87.25  ? 361 LEU   D N      1 
ATOM   12913 C  CA     . LEU   D 2  361 ? 2.346   -3.535   -35.682 1.00 79.55  ? 361 LEU   D CA     1 
ATOM   12914 C  C      . LEU   D 2  361 ? 2.736   -4.847   -35.022 1.00 83.01  ? 361 LEU   D C      1 
ATOM   12915 O  O      . LEU   D 2  361 ? 1.960   -5.808   -35.039 1.00 85.63  ? 361 LEU   D O      1 
ATOM   12916 C  CB     . LEU   D 2  361 ? 1.345   -2.765   -34.826 1.00 77.94  ? 361 LEU   D CB     1 
ATOM   12917 C  CG     . LEU   D 2  361 ? 0.969   -1.409   -35.423 1.00 81.01  ? 361 LEU   D CG     1 
ATOM   12918 C  CD1    . LEU   D 2  361 ? 0.032   -0.626   -34.506 1.00 87.20  ? 361 LEU   D CD1    1 
ATOM   12919 C  CD2    . LEU   D 2  361 ? 2.195   -0.598   -35.803 1.00 85.65  ? 361 LEU   D CD2    1 
ATOM   12920 N  N      . LYS   D 2  362 ? 3.951   -4.887   -34.465 1.00 88.83  ? 362 LYS   D N      1 
ATOM   12921 C  CA     . LYS   D 2  362 ? 4.485   -6.078   -33.804 1.00 91.23  ? 362 LYS   D CA     1 
ATOM   12922 C  C      . LYS   D 2  362 ? 3.847   -6.301   -32.437 1.00 92.13  ? 362 LYS   D C      1 
ATOM   12923 O  O      . LYS   D 2  362 ? 3.827   -7.434   -31.930 1.00 82.56  ? 362 LYS   D O      1 
ATOM   12924 C  CB     . LYS   D 2  362 ? 6.001   -5.943   -33.666 1.00 88.09  ? 362 LYS   D CB     1 
ATOM   12925 C  CG     . LYS   D 2  362 ? 6.751   -6.347   -34.905 1.00 93.67  ? 362 LYS   D CG     1 
ATOM   12926 C  CD     . LYS   D 2  362 ? 8.260   -6.286   -34.721 1.00 104.66 ? 362 LYS   D CD     1 
ATOM   12927 C  CE     . LYS   D 2  362 ? 8.752   -7.164   -33.602 1.00 101.42 ? 362 LYS   D CE     1 
ATOM   12928 N  NZ     . LYS   D 2  362 ? 10.201  -6.909   -33.385 1.00 106.24 ? 362 LYS   D NZ     1 
ATOM   12929 N  N      . MET   D 2  363 ? 3.347   -5.233   -31.822 1.00 88.19  ? 363 MET   D N      1 
ATOM   12930 C  CA     . MET   D 2  363 ? 2.464   -5.364   -30.680 1.00 80.51  ? 363 MET   D CA     1 
ATOM   12931 C  C      . MET   D 2  363 ? 1.740   -4.043   -30.494 1.00 77.01  ? 363 MET   D C      1 
ATOM   12932 O  O      . MET   D 2  363 ? 2.370   -2.979   -30.486 1.00 71.01  ? 363 MET   D O      1 
ATOM   12933 C  CB     . MET   D 2  363 ? 3.235   -5.746   -29.427 1.00 84.31  ? 363 MET   D CB     1 
ATOM   12934 C  CG     . MET   D 2  363 ? 4.446   -4.901   -29.146 1.00 90.40  ? 363 MET   D CG     1 
ATOM   12935 S  SD     . MET   D 2  363 ? 5.353   -5.753   -27.855 1.00 97.32  ? 363 MET   D SD     1 
ATOM   12936 C  CE     . MET   D 2  363 ? 5.548   -7.312   -28.692 1.00 85.90  ? 363 MET   D CE     1 
ATOM   12937 N  N      . SER   D 2  364 ? 0.423   -4.120   -30.385 1.00 73.40  ? 364 SER   D N      1 
ATOM   12938 C  CA     . SER   D 2  364 ? -0.401  -2.980   -30.041 1.00 73.06  ? 364 SER   D CA     1 
ATOM   12939 C  C      . SER   D 2  364 ? -1.082  -3.259   -28.715 1.00 72.29  ? 364 SER   D C      1 
ATOM   12940 O  O      . SER   D 2  364 ? -0.891  -4.311   -28.096 1.00 72.19  ? 364 SER   D O      1 
ATOM   12941 C  CB     . SER   D 2  364 ? -1.454  -2.697   -31.112 1.00 77.62  ? 364 SER   D CB     1 
ATOM   12942 O  OG     . SER   D 2  364 ? -2.269  -3.842   -31.311 1.00 79.26  ? 364 SER   D OG     1 
ATOM   12943 N  N      . ALA   D 2  365 ? -1.886  -2.290   -28.292 1.00 67.28  ? 365 ALA   D N      1 
ATOM   12944 C  CA     . ALA   D 2  365 ? -2.798  -2.446   -27.177 1.00 60.68  ? 365 ALA   D CA     1 
ATOM   12945 C  C      . ALA   D 2  365 ? -4.061  -1.677   -27.515 1.00 64.38  ? 365 ALA   D C      1 
ATOM   12946 O  O      . ALA   D 2  365 ? -3.982  -0.596   -28.106 1.00 66.22  ? 365 ALA   D O      1 
ATOM   12947 C  CB     . ALA   D 2  365 ? -2.186  -1.920   -25.884 1.00 53.88  ? 365 ALA   D CB     1 
ATOM   12948 N  N      . THR   D 2  366 ? -5.223  -2.233   -27.172 1.00 57.09  ? 366 THR   D N      1 
ATOM   12949 C  CA     . THR   D 2  366 ? -6.462  -1.471   -27.213 1.00 53.88  ? 366 THR   D CA     1 
ATOM   12950 C  C      . THR   D 2  366 ? -7.063  -1.332   -25.819 1.00 55.98  ? 366 THR   D C      1 
ATOM   12951 O  O      . THR   D 2  366 ? -6.964  -2.236   -24.980 1.00 55.53  ? 366 THR   D O      1 
ATOM   12952 C  CB     . THR   D 2  366 ? -7.479  -2.087   -28.146 1.00 56.22  ? 366 THR   D CB     1 
ATOM   12953 O  OG1    . THR   D 2  366 ? -6.927  -2.150   -29.462 1.00 59.89  ? 366 THR   D OG1    1 
ATOM   12954 C  CG2    . THR   D 2  366 ? -8.730  -1.238   -28.174 1.00 58.80  ? 366 THR   D CG2    1 
ATOM   12955 N  N      . PHE   D 2  367 ? -7.706  -0.186   -25.597 1.00 50.10  ? 367 PHE   D N      1 
ATOM   12956 C  CA     . PHE   D 2  367 ? -8.080  0.280    -24.269 1.00 47.02  ? 367 PHE   D CA     1 
ATOM   12957 C  C      . PHE   D 2  367 ? -9.518  0.757    -24.313 1.00 48.63  ? 367 PHE   D C      1 
ATOM   12958 O  O      . PHE   D 2  367 ? -9.817  1.737    -24.996 1.00 54.98  ? 367 PHE   D O      1 
ATOM   12959 C  CB     . PHE   D 2  367 ? -7.172  1.427    -23.806 1.00 47.13  ? 367 PHE   D CB     1 
ATOM   12960 C  CG     . PHE   D 2  367 ? -7.764  2.243    -22.700 1.00 49.79  ? 367 PHE   D CG     1 
ATOM   12961 C  CD1    . PHE   D 2  367 ? -8.636  3.270    -22.969 1.00 52.82  ? 367 PHE   D CD1    1 
ATOM   12962 C  CD2    . PHE   D 2  367 ? -7.462  1.974    -21.381 1.00 60.06  ? 367 PHE   D CD2    1 
ATOM   12963 C  CE1    . PHE   D 2  367 ? -9.203  3.997    -21.941 1.00 57.92  ? 367 PHE   D CE1    1 
ATOM   12964 C  CE2    . PHE   D 2  367 ? -8.022  2.711    -20.353 1.00 58.58  ? 367 PHE   D CE2    1 
ATOM   12965 C  CZ     . PHE   D 2  367 ? -8.888  3.715    -20.630 1.00 60.88  ? 367 PHE   D CZ     1 
ATOM   12966 N  N      . ILE   D 2  368 ? -10.394 0.102    -23.554 1.00 48.04  ? 368 ILE   D N      1 
ATOM   12967 C  CA     . ILE   D 2  368 ? -11.788 0.507    -23.416 1.00 41.67  ? 368 ILE   D CA     1 
ATOM   12968 C  C      . ILE   D 2  368 ? -11.979 1.038    -22.012 1.00 47.37  ? 368 ILE   D C      1 
ATOM   12969 O  O      . ILE   D 2  368 ? -11.621 0.360    -21.042 1.00 48.68  ? 368 ILE   D O      1 
ATOM   12970 C  CB     . ILE   D 2  368 ? -12.741 -0.664   -23.664 1.00 38.90  ? 368 ILE   D CB     1 
ATOM   12971 C  CG1    . ILE   D 2  368 ? -12.336 -1.377   -24.955 1.00 47.22  ? 368 ILE   D CG1    1 
ATOM   12972 C  CG2    . ILE   D 2  368 ? -14.151 -0.125   -23.732 1.00 34.97  ? 368 ILE   D CG2    1 
ATOM   12973 C  CD1    . ILE   D 2  368 ? -12.931 -2.755   -25.131 1.00 51.74  ? 368 ILE   D CD1    1 
ATOM   12974 N  N      . GLY   D 2  369 ? -12.564 2.218    -21.896 1.00 45.62  ? 369 GLY   D N      1 
ATOM   12975 C  CA     . GLY   D 2  369 ? -12.677 2.885    -20.611 1.00 39.21  ? 369 GLY   D CA     1 
ATOM   12976 C  C      . GLY   D 2  369 ? -14.053 3.459    -20.390 1.00 36.36  ? 369 GLY   D C      1 
ATOM   12977 O  O      . GLY   D 2  369 ? -14.644 4.040    -21.281 1.00 47.17  ? 369 GLY   D O      1 
ATOM   12978 N  N      . ASN   D 2  370 ? -14.542 3.300    -19.191 1.00 37.25  ? 370 ASN   D N      1 
ATOM   12979 C  CA     . ASN   D 2  370 ? -15.796 3.882    -18.752 1.00 39.53  ? 370 ASN   D CA     1 
ATOM   12980 C  C      . ASN   D 2  370 ? -15.384 4.890    -17.699 1.00 48.42  ? 370 ASN   D C      1 
ATOM   12981 O  O      . ASN   D 2  370 ? -15.337 4.571    -16.509 1.00 50.98  ? 370 ASN   D O      1 
ATOM   12982 C  CB     . ASN   D 2  370 ? -16.750 2.826    -18.206 1.00 40.85  ? 370 ASN   D CB     1 
ATOM   12983 C  CG     . ASN   D 2  370 ? -18.172 3.323    -18.080 1.00 42.12  ? 370 ASN   D CG     1 
ATOM   12984 O  OD1    . ASN   D 2  370 ? -18.455 4.516    -18.205 1.00 47.47  ? 370 ASN   D OD1    1 
ATOM   12985 N  ND2    . ASN   D 2  370 ? -19.085 2.401    -17.840 1.00 41.45  ? 370 ASN   D ND2    1 
ATOM   12986 N  N      . SER   D 2  371 ? -15.059 6.102    -18.159 1.00 50.25  ? 371 SER   D N      1 
ATOM   12987 C  CA     . SER   D 2  371 ? -14.568 7.194    -17.326 1.00 45.30  ? 371 SER   D CA     1 
ATOM   12988 C  C      . SER   D 2  371 ? -15.625 8.269    -17.145 1.00 44.55  ? 371 SER   D C      1 
ATOM   12989 O  O      . SER   D 2  371 ? -16.280 8.658    -18.107 1.00 52.28  ? 371 SER   D O      1 
ATOM   12990 C  CB     . SER   D 2  371 ? -13.340 7.829    -17.950 1.00 43.08  ? 371 SER   D CB     1 
ATOM   12991 O  OG     . SER   D 2  371 ? -13.054 9.041    -17.294 1.00 51.33  ? 371 SER   D OG     1 
ATOM   12992 N  N      . THR   D 2  372 ? -15.782 8.758    -15.912 1.00 48.48  ? 372 THR   D N      1 
ATOM   12993 C  CA     . THR   D 2  372 ? -16.653 9.907    -15.688 1.00 51.27  ? 372 THR   D CA     1 
ATOM   12994 C  C      . THR   D 2  372 ? -16.205 11.117   -16.494 1.00 54.19  ? 372 THR   D C      1 
ATOM   12995 O  O      . THR   D 2  372 ? -16.982 12.069   -16.637 1.00 58.63  ? 372 THR   D O      1 
ATOM   12996 C  CB     . THR   D 2  372 ? -16.720 10.278   -14.191 1.00 47.44  ? 372 THR   D CB     1 
ATOM   12997 O  OG1    . THR   D 2  372 ? -15.412 10.572   -13.700 1.00 45.64  ? 372 THR   D OG1    1 
ATOM   12998 C  CG2    . THR   D 2  372 ? -17.276 9.153    -13.382 1.00 47.09  ? 372 THR   D CG2    1 
ATOM   12999 N  N      . ALA   D 2  373 ? -14.982 11.097   -17.031 1.00 50.09  ? 373 ALA   D N      1 
ATOM   13000 C  CA     . ALA   D 2  373 ? -14.465 12.222   -17.805 1.00 56.47  ? 373 ALA   D CA     1 
ATOM   13001 C  C      . ALA   D 2  373 ? -15.162 12.388   -19.151 1.00 60.20  ? 373 ALA   D C      1 
ATOM   13002 O  O      . ALA   D 2  373 ? -14.989 13.434   -19.796 1.00 59.37  ? 373 ALA   D O      1 
ATOM   13003 C  CB     . ALA   D 2  373 ? -12.958 12.066   -18.021 1.00 56.08  ? 373 ALA   D CB     1 
ATOM   13004 N  N      . ILE   D 2  374 ? -15.936 11.386   -19.590 1.00 61.41  ? 374 ILE   D N      1 
ATOM   13005 C  CA     . ILE   D 2  374 ? -16.667 11.488   -20.844 1.00 54.95  ? 374 ILE   D CA     1 
ATOM   13006 C  C      . ILE   D 2  374 ? -17.605 12.672   -20.796 1.00 55.61  ? 374 ILE   D C      1 
ATOM   13007 O  O      . ILE   D 2  374 ? -17.946 13.223   -21.839 1.00 60.58  ? 374 ILE   D O      1 
ATOM   13008 C  CB     . ILE   D 2  374 ? -17.444 10.190   -21.155 1.00 53.25  ? 374 ILE   D CB     1 
ATOM   13009 C  CG1    . ILE   D 2  374 ? -17.830 10.133   -22.639 1.00 53.43  ? 374 ILE   D CG1    1 
ATOM   13010 C  CG2    . ILE   D 2  374 ? -18.696 10.084   -20.275 1.00 52.13  ? 374 ILE   D CG2    1 
ATOM   13011 C  CD1    . ILE   D 2  374 ? -16.786 9.464    -23.527 1.00 54.52  ? 374 ILE   D CD1    1 
ATOM   13012 N  N      . GLN   D 2  375 ? -18.029 13.096   -19.604 1.00 55.57  ? 375 GLN   D N      1 
ATOM   13013 C  CA     . GLN   D 2  375 ? -18.820 14.316   -19.521 1.00 58.42  ? 375 GLN   D CA     1 
ATOM   13014 C  C      . GLN   D 2  375 ? -18.122 15.462   -20.236 1.00 59.23  ? 375 GLN   D C      1 
ATOM   13015 O  O      . GLN   D 2  375 ? -18.796 16.396   -20.678 1.00 61.36  ? 375 GLN   D O      1 
ATOM   13016 C  CB     . GLN   D 2  375 ? -19.105 14.681   -18.053 1.00 57.38  ? 375 GLN   D CB     1 
ATOM   13017 C  CG     . GLN   D 2  375 ? -17.864 15.056   -17.266 1.00 55.41  ? 375 GLN   D CG     1 
ATOM   13018 C  CD     . GLN   D 2  375 ? -18.175 15.540   -15.880 1.00 60.06  ? 375 GLN   D CD     1 
ATOM   13019 O  OE1    . GLN   D 2  375 ? -18.901 16.518   -15.673 1.00 70.14  ? 375 GLN   D OE1    1 
ATOM   13020 N  NE2    . GLN   D 2  375 ? -17.609 14.865   -14.910 1.00 56.69  ? 375 GLN   D NE2    1 
ATOM   13021 N  N      . GLU   D 2  376 ? -16.789 15.410   -20.388 1.00 58.45  ? 376 GLU   D N      1 
ATOM   13022 C  CA     . GLU   D 2  376 ? -16.119 16.408   -21.219 1.00 60.16  ? 376 GLU   D CA     1 
ATOM   13023 C  C      . GLU   D 2  376 ? -16.717 16.422   -22.622 1.00 59.36  ? 376 GLU   D C      1 
ATOM   13024 O  O      . GLU   D 2  376 ? -17.178 17.465   -23.101 1.00 57.63  ? 376 GLU   D O      1 
ATOM   13025 C  CB     . GLU   D 2  376 ? -14.600 16.166   -21.270 1.00 60.39  ? 376 GLU   D CB     1 
ATOM   13026 C  CG     . GLU   D 2  376 ? -13.856 16.453   -19.962 1.00 60.43  ? 376 GLU   D CG     1 
ATOM   13027 C  CD     . GLU   D 2  376 ? -12.319 16.428   -20.088 1.00 61.23  ? 376 GLU   D CD     1 
ATOM   13028 O  OE1    . GLU   D 2  376 ? -11.765 15.993   -21.126 1.00 54.45  ? 376 GLU   D OE1    1 
ATOM   13029 O  OE2    . GLU   D 2  376 ? -11.660 16.878   -19.124 1.00 57.81  ? 376 GLU   D OE2    1 
ATOM   13030 N  N      . LEU   D 2  377 ? -16.739 15.251   -23.272 1.00 59.75  ? 377 LEU   D N      1 
ATOM   13031 C  CA     . LEU   D 2  377 ? -17.352 15.041   -24.587 1.00 56.44  ? 377 LEU   D CA     1 
ATOM   13032 C  C      . LEU   D 2  377 ? -18.811 15.495   -24.664 1.00 55.36  ? 377 LEU   D C      1 
ATOM   13033 O  O      . LEU   D 2  377 ? -19.187 16.235   -25.571 1.00 63.21  ? 377 LEU   D O      1 
ATOM   13034 C  CB     . LEU   D 2  377 ? -17.250 13.560   -24.932 1.00 61.83  ? 377 LEU   D CB     1 
ATOM   13035 C  CG     . LEU   D 2  377 ? -17.650 13.066   -26.306 1.00 64.00  ? 377 LEU   D CG     1 
ATOM   13036 C  CD1    . LEU   D 2  377 ? -19.162 12.823   -26.313 1.00 62.67  ? 377 LEU   D CD1    1 
ATOM   13037 C  CD2    . LEU   D 2  377 ? -17.227 14.076   -27.335 1.00 73.53  ? 377 LEU   D CD2    1 
ATOM   13038 N  N      . PHE   D 2  378 ? -19.665 15.013   -23.766 1.00 54.85  ? 378 PHE   D N      1 
ATOM   13039 C  CA     . PHE   D 2  378 ? -21.052 15.456   -23.786 1.00 55.94  ? 378 PHE   D CA     1 
ATOM   13040 C  C      . PHE   D 2  378 ? -21.221 16.913   -23.394 1.00 60.26  ? 378 PHE   D C      1 
ATOM   13041 O  O      . PHE   D 2  378 ? -22.253 17.504   -23.722 1.00 66.34  ? 378 PHE   D O      1 
ATOM   13042 C  CB     . PHE   D 2  378 ? -21.907 14.583   -22.875 1.00 58.22  ? 378 PHE   D CB     1 
ATOM   13043 C  CG     . PHE   D 2  378 ? -21.928 13.152   -23.281 1.00 58.39  ? 378 PHE   D CG     1 
ATOM   13044 C  CD1    . PHE   D 2  378 ? -22.415 12.790   -24.521 1.00 61.54  ? 378 PHE   D CD1    1 
ATOM   13045 C  CD2    . PHE   D 2  378 ? -21.433 12.170   -22.448 1.00 60.29  ? 378 PHE   D CD2    1 
ATOM   13046 C  CE1    . PHE   D 2  378 ? -22.439 11.465   -24.920 1.00 66.48  ? 378 PHE   D CE1    1 
ATOM   13047 C  CE2    . PHE   D 2  378 ? -21.442 10.832   -22.837 1.00 65.06  ? 378 PHE   D CE2    1 
ATOM   13048 C  CZ     . PHE   D 2  378 ? -21.949 10.477   -24.078 1.00 66.70  ? 378 PHE   D CZ     1 
ATOM   13049 N  N      . LYS   D 2  379 ? -20.259 17.507   -22.686 1.00 64.35  ? 379 LYS   D N      1 
ATOM   13050 C  CA     . LYS   D 2  379 ? -20.370 18.927   -22.360 1.00 64.62  ? 379 LYS   D CA     1 
ATOM   13051 C  C      . LYS   D 2  379 ? -20.073 19.808   -23.572 1.00 65.98  ? 379 LYS   D C      1 
ATOM   13052 O  O      . LYS   D 2  379 ? -20.667 20.882   -23.717 1.00 69.87  ? 379 LYS   D O      1 
ATOM   13053 C  CB     . LYS   D 2  379 ? -19.437 19.267   -21.204 1.00 60.78  ? 379 LYS   D CB     1 
ATOM   13054 C  CG     . LYS   D 2  379 ? -19.971 18.936   -19.822 1.00 60.30  ? 379 LYS   D CG     1 
ATOM   13055 C  CD     . LYS   D 2  379 ? -19.066 19.592   -18.790 1.00 64.51  ? 379 LYS   D CD     1 
ATOM   13056 C  CE     . LYS   D 2  379 ? -19.622 19.536   -17.396 1.00 67.33  ? 379 LYS   D CE     1 
ATOM   13057 N  NZ     . LYS   D 2  379 ? -18.978 20.604   -16.578 1.00 72.87  ? 379 LYS   D NZ     1 
ATOM   13058 N  N      . ARG   D 2  380 ? -19.171 19.360   -24.447 1.00 62.28  ? 380 ARG   D N      1 
ATOM   13059 C  CA     . ARG   D 2  380 ? -18.879 20.054   -25.701 1.00 67.51  ? 380 ARG   D CA     1 
ATOM   13060 C  C      . ARG   D 2  380 ? -20.084 20.089   -26.637 1.00 71.89  ? 380 ARG   D C      1 
ATOM   13061 O  O      . ARG   D 2  380 ? -20.367 21.119   -27.266 1.00 73.50  ? 380 ARG   D O      1 
ATOM   13062 C  CB     . ARG   D 2  380 ? -17.693 19.371   -26.383 1.00 62.50  ? 380 ARG   D CB     1 
ATOM   13063 C  CG     . ARG   D 2  380 ? -17.370 19.893   -27.729 1.00 60.68  ? 380 ARG   D CG     1 
ATOM   13064 C  CD     . ARG   D 2  380 ? -16.302 19.079   -28.403 1.00 64.59  ? 380 ARG   D CD     1 
ATOM   13065 N  NE     . ARG   D 2  380 ? -16.816 17.982   -29.215 1.00 76.03  ? 380 ARG   D NE     1 
ATOM   13066 C  CZ     . ARG   D 2  380 ? -16.211 16.808   -29.364 1.00 75.16  ? 380 ARG   D CZ     1 
ATOM   13067 N  NH1    . ARG   D 2  380 ? -15.039 16.556   -28.805 1.00 70.35  ? 380 ARG   D NH1    1 
ATOM   13068 N  NH2    . ARG   D 2  380 ? -16.783 15.871   -30.115 1.00 74.60  ? 380 ARG   D NH2    1 
ATOM   13069 N  N      . ILE   D 2  381 ? -20.778 18.962   -26.775 1.00 68.15  ? 381 ILE   D N      1 
ATOM   13070 C  CA     . ILE   D 2  381 ? -21.974 18.921   -27.601 1.00 62.24  ? 381 ILE   D CA     1 
ATOM   13071 C  C      . ILE   D 2  381 ? -23.124 19.661   -26.928 1.00 70.96  ? 381 ILE   D C      1 
ATOM   13072 O  O      . ILE   D 2  381 ? -24.025 20.168   -27.607 1.00 74.04  ? 381 ILE   D O      1 
ATOM   13073 C  CB     . ILE   D 2  381 ? -22.325 17.458   -27.907 1.00 47.68  ? 381 ILE   D CB     1 
ATOM   13074 C  CG1    . ILE   D 2  381 ? -21.228 16.872   -28.788 1.00 56.00  ? 381 ILE   D CG1    1 
ATOM   13075 C  CG2    . ILE   D 2  381 ? -23.687 17.359   -28.545 1.00 48.24  ? 381 ILE   D CG2    1 
ATOM   13076 C  CD1    . ILE   D 2  381 ? -21.489 15.481   -29.266 1.00 62.66  ? 381 ILE   D CD1    1 
ATOM   13077 N  N      . SER   D 2  382 ? -23.125 19.749   -25.596 1.00 67.88  ? 382 SER   D N      1 
ATOM   13078 C  CA     . SER   D 2  382 ? -24.223 20.451   -24.949 1.00 69.36  ? 382 SER   D CA     1 
ATOM   13079 C  C      . SER   D 2  382 ? -24.094 21.952   -25.142 1.00 76.90  ? 382 SER   D C      1 
ATOM   13080 O  O      . SER   D 2  382 ? -25.103 22.666   -25.116 1.00 79.05  ? 382 SER   D O      1 
ATOM   13081 C  CB     . SER   D 2  382 ? -24.290 20.104   -23.465 1.00 70.03  ? 382 SER   D CB     1 
ATOM   13082 O  OG     . SER   D 2  382 ? -25.578 20.392   -22.935 1.00 69.57  ? 382 SER   D OG     1 
ATOM   13083 N  N      . GLU   D 2  383 ? -22.869 22.444   -25.345 1.00 75.35  ? 383 GLU   D N      1 
ATOM   13084 C  CA     . GLU   D 2  383 ? -22.663 23.877   -25.530 1.00 79.72  ? 383 GLU   D CA     1 
ATOM   13085 C  C      . GLU   D 2  383 ? -23.015 24.293   -26.947 1.00 82.84  ? 383 GLU   D C      1 
ATOM   13086 O  O      . GLU   D 2  383 ? -23.814 25.216   -27.150 1.00 88.75  ? 383 GLU   D O      1 
ATOM   13087 C  CB     . GLU   D 2  383 ? -21.218 24.250   -25.198 1.00 79.24  ? 383 GLU   D CB     1 
ATOM   13088 C  CG     . GLU   D 2  383 ? -21.046 25.654   -24.646 1.00 82.58  ? 383 GLU   D CG     1 
ATOM   13089 C  CD     . GLU   D 2  383 ? -19.583 26.079   -24.585 1.00 92.90  ? 383 GLU   D CD     1 
ATOM   13090 O  OE1    . GLU   D 2  383 ? -18.789 25.630   -25.445 1.00 91.30  ? 383 GLU   D OE1    1 
ATOM   13091 O  OE2    . GLU   D 2  383 ? -19.228 26.861   -23.667 1.00 97.53  ? 383 GLU   D OE2    1 
ATOM   13092 N  N      . GLN   D 2  384 ? -22.441 23.600   -27.933 1.00 79.11  ? 384 GLN   D N      1 
ATOM   13093 C  CA     . GLN   D 2  384 ? -22.790 23.845   -29.326 1.00 73.86  ? 384 GLN   D CA     1 
ATOM   13094 C  C      . GLN   D 2  384 ? -24.294 23.748   -29.553 1.00 76.05  ? 384 GLN   D C      1 
ATOM   13095 O  O      . GLN   D 2  384 ? -24.884 24.607   -30.216 1.00 85.36  ? 384 GLN   D O      1 
ATOM   13096 C  CB     . GLN   D 2  384 ? -22.036 22.862   -30.198 1.00 67.95  ? 384 GLN   D CB     1 
ATOM   13097 C  CG     . GLN   D 2  384 ? -20.596 22.780   -29.799 1.00 65.68  ? 384 GLN   D CG     1 
ATOM   13098 C  CD     . GLN   D 2  384 ? -19.834 21.814   -30.663 1.00 81.01  ? 384 GLN   D CD     1 
ATOM   13099 O  OE1    . GLN   D 2  384 ? -20.429 21.014   -31.387 1.00 78.37  ? 384 GLN   D OE1    1 
ATOM   13100 N  NE2    . GLN   D 2  384 ? -18.506 21.903   -30.627 1.00 89.78  ? 384 GLN   D NE2    1 
ATOM   13101 N  N      . PHE   D 2  385 ? -24.936 22.718   -29.009 1.00 74.35  ? 385 PHE   D N      1 
ATOM   13102 C  CA     . PHE   D 2  385 ? -26.390 22.659   -29.048 1.00 75.67  ? 385 PHE   D CA     1 
ATOM   13103 C  C      . PHE   D 2  385 ? -26.994 23.980   -28.576 1.00 80.93  ? 385 PHE   D C      1 
ATOM   13104 O  O      . PHE   D 2  385 ? -27.609 24.710   -29.361 1.00 89.14  ? 385 PHE   D O      1 
ATOM   13105 C  CB     . PHE   D 2  385 ? -26.877 21.469   -28.212 1.00 72.78  ? 385 PHE   D CB     1 
ATOM   13106 C  CG     . PHE   D 2  385 ? -28.385 21.311   -28.148 1.00 69.36  ? 385 PHE   D CG     1 
ATOM   13107 C  CD1    . PHE   D 2  385 ? -29.137 21.944   -27.156 1.00 69.99  ? 385 PHE   D CD1    1 
ATOM   13108 C  CD2    . PHE   D 2  385 ? -29.046 20.518   -29.078 1.00 63.69  ? 385 PHE   D CD2    1 
ATOM   13109 C  CE1    . PHE   D 2  385 ? -30.515 21.779   -27.088 1.00 70.22  ? 385 PHE   D CE1    1 
ATOM   13110 C  CE2    . PHE   D 2  385 ? -30.425 20.358   -29.021 1.00 69.97  ? 385 PHE   D CE2    1 
ATOM   13111 C  CZ     . PHE   D 2  385 ? -31.159 20.990   -28.024 1.00 71.54  ? 385 PHE   D CZ     1 
ATOM   13112 N  N      . THR   D 2  386 ? -26.782 24.331   -27.307 1.00 76.25  ? 386 THR   D N      1 
ATOM   13113 C  CA     . THR   D 2  386 ? -27.513 25.453   -26.722 1.00 81.02  ? 386 THR   D CA     1 
ATOM   13114 C  C      . THR   D 2  386 ? -27.204 26.782   -27.394 1.00 90.33  ? 386 THR   D C      1 
ATOM   13115 O  O      . THR   D 2  386 ? -28.030 27.705   -27.338 1.00 91.89  ? 386 THR   D O      1 
ATOM   13116 C  CB     . THR   D 2  386 ? -27.206 25.544   -25.246 1.00 78.49  ? 386 THR   D CB     1 
ATOM   13117 O  OG1    . THR   D 2  386 ? -25.824 25.896   -25.102 1.00 77.69  ? 386 THR   D OG1    1 
ATOM   13118 C  CG2    . THR   D 2  386 ? -27.505 24.215   -24.588 1.00 81.46  ? 386 THR   D CG2    1 
ATOM   13119 N  N      . ALA   D 2  387 ? -26.020 26.916   -28.002 1.00 88.38  ? 387 ALA   D N      1 
ATOM   13120 C  CA     . ALA   D 2  387 ? -25.756 28.078   -28.844 1.00 87.24  ? 387 ALA   D CA     1 
ATOM   13121 C  C      . ALA   D 2  387 ? -26.884 28.271   -29.840 1.00 90.89  ? 387 ALA   D C      1 
ATOM   13122 O  O      . ALA   D 2  387 ? -27.451 29.363   -29.961 1.00 97.41  ? 387 ALA   D O      1 
ATOM   13123 C  CB     . ALA   D 2  387 ? -24.429 27.912   -29.582 1.00 80.68  ? 387 ALA   D CB     1 
ATOM   13124 N  N      . MET   D 2  388 ? -27.240 27.202   -30.546 1.00 82.21  ? 388 MET   D N      1 
ATOM   13125 C  CA     . MET   D 2  388 ? -28.304 27.291   -31.530 1.00 86.22  ? 388 MET   D CA     1 
ATOM   13126 C  C      . MET   D 2  388 ? -29.689 27.314   -30.890 1.00 88.08  ? 388 MET   D C      1 
ATOM   13127 O  O      . MET   D 2  388 ? -30.540 28.112   -31.292 1.00 90.21  ? 388 MET   D O      1 
ATOM   13128 C  CB     . MET   D 2  388 ? -28.160 26.147   -32.523 1.00 80.30  ? 388 MET   D CB     1 
ATOM   13129 C  CG     . MET   D 2  388 ? -26.858 26.297   -33.256 1.00 88.72  ? 388 MET   D CG     1 
ATOM   13130 S  SD     . MET   D 2  388 ? -26.421 25.019   -34.435 1.00 91.85  ? 388 MET   D SD     1 
ATOM   13131 C  CE     . MET   D 2  388 ? -24.631 25.168   -34.360 1.00 86.56  ? 388 MET   D CE     1 
ATOM   13132 N  N      . PHE   D 2  389 ? -29.939 26.480   -29.882 1.00 88.78  ? 389 PHE   D N      1 
ATOM   13133 C  CA     . PHE   D 2  389 ? -31.302 26.348   -29.368 1.00 89.15  ? 389 PHE   D CA     1 
ATOM   13134 C  C      . PHE   D 2  389 ? -31.780 27.608   -28.652 1.00 89.57  ? 389 PHE   D C      1 
ATOM   13135 O  O      . PHE   D 2  389 ? -32.972 27.924   -28.706 1.00 84.70  ? 389 PHE   D O      1 
ATOM   13136 C  CB     . PHE   D 2  389 ? -31.389 25.134   -28.447 1.00 87.73  ? 389 PHE   D CB     1 
ATOM   13137 C  CG     . PHE   D 2  389 ? -32.789 24.651   -28.192 1.00 83.20  ? 389 PHE   D CG     1 
ATOM   13138 C  CD1    . PHE   D 2  389 ? -33.534 24.078   -29.202 1.00 79.91  ? 389 PHE   D CD1    1 
ATOM   13139 C  CD2    . PHE   D 2  389 ? -33.341 24.731   -26.920 1.00 83.84  ? 389 PHE   D CD2    1 
ATOM   13140 C  CE1    . PHE   D 2  389 ? -34.813 23.619   -28.959 1.00 77.57  ? 389 PHE   D CE1    1 
ATOM   13141 C  CE2    . PHE   D 2  389 ? -34.619 24.271   -26.672 1.00 85.00  ? 389 PHE   D CE2    1 
ATOM   13142 C  CZ     . PHE   D 2  389 ? -35.357 23.713   -27.697 1.00 80.69  ? 389 PHE   D CZ     1 
ATOM   13143 N  N      . ARG   D 2  390 ? -30.889 28.339   -27.971 1.00 94.61  ? 390 ARG   D N      1 
ATOM   13144 C  CA     . ARG   D 2  390 ? -31.327 29.609   -27.398 1.00 98.91  ? 390 ARG   D CA     1 
ATOM   13145 C  C      . ARG   D 2  390 ? -31.628 30.640   -28.481 1.00 98.70  ? 390 ARG   D C      1 
ATOM   13146 O  O      . ARG   D 2  390 ? -32.347 31.609   -28.209 1.00 98.18  ? 390 ARG   D O      1 
ATOM   13147 C  CB     . ARG   D 2  390 ? -30.291 30.179   -26.417 1.00 106.87 ? 390 ARG   D CB     1 
ATOM   13148 C  CG     . ARG   D 2  390 ? -28.950 30.599   -27.025 1.00 104.76 ? 390 ARG   D CG     1 
ATOM   13149 C  CD     . ARG   D 2  390 ? -27.952 31.015   -25.936 1.00 111.48 ? 390 ARG   D CD     1 
ATOM   13150 N  NE     . ARG   D 2  390 ? -26.580 31.090   -26.430 1.00 117.36 ? 390 ARG   D NE     1 
ATOM   13151 C  CZ     . ARG   D 2  390 ? -25.508 31.276   -25.666 1.00 116.93 ? 390 ARG   D CZ     1 
ATOM   13152 N  NH1    . ARG   D 2  390 ? -25.607 31.420   -24.352 1.00 109.82 ? 390 ARG   D NH1    1 
ATOM   13153 N  NH2    . ARG   D 2  390 ? -24.305 31.309   -26.234 1.00 114.73 ? 390 ARG   D NH2    1 
ATOM   13154 N  N      . ARG   D 2  391 ? -31.088 30.453   -29.695 1.00 100.80 ? 391 ARG   D N      1 
ATOM   13155 C  CA     . ARG   D 2  391 ? -31.433 31.253   -30.870 1.00 98.10  ? 391 ARG   D CA     1 
ATOM   13156 C  C      . ARG   D 2  391 ? -32.623 30.704   -31.647 1.00 90.50  ? 391 ARG   D C      1 
ATOM   13157 O  O      . ARG   D 2  391 ? -33.096 31.372   -32.567 1.00 94.58  ? 391 ARG   D O      1 
ATOM   13158 C  CB     . ARG   D 2  391 ? -30.265 31.343   -31.869 1.00 98.40  ? 391 ARG   D CB     1 
ATOM   13159 C  CG     . ARG   D 2  391 ? -29.096 32.253   -31.527 1.00 100.53 ? 391 ARG   D CG     1 
ATOM   13160 C  CD     . ARG   D 2  391 ? -28.139 32.307   -32.719 1.00 100.94 ? 391 ARG   D CD     1 
ATOM   13161 N  NE     . ARG   D 2  391 ? -27.676 30.988   -33.134 1.00 103.05 ? 391 ARG   D NE     1 
ATOM   13162 C  CZ     . ARG   D 2  391 ? -26.926 30.761   -34.205 1.00 107.84 ? 391 ARG   D CZ     1 
ATOM   13163 N  NH1    . ARG   D 2  391 ? -26.470 31.751   -34.954 1.00 115.65 ? 391 ARG   D NH1    1 
ATOM   13164 N  NH2    . ARG   D 2  391 ? -26.625 29.508   -34.535 1.00 105.06 ? 391 ARG   D NH2    1 
ATOM   13165 N  N      . LYS   D 2  392 ? -33.077 29.492   -31.345 1.00 94.18  ? 392 LYS   D N      1 
ATOM   13166 C  CA     . LYS   D 2  392 ? -34.127 28.791   -32.076 1.00 87.24  ? 392 LYS   D CA     1 
ATOM   13167 C  C      . LYS   D 2  392 ? -33.695 28.457   -33.504 1.00 81.98  ? 392 LYS   D C      1 
ATOM   13168 O  O      . LYS   D 2  392 ? -34.490 27.912   -34.275 1.00 79.78  ? 392 LYS   D O      1 
ATOM   13169 C  CB     . LYS   D 2  392 ? -35.424 29.604   -32.077 1.00 89.32  ? 392 LYS   D CB     1 
ATOM   13170 C  CG     . LYS   D 2  392 ? -36.688 28.787   -31.921 1.00 92.50  ? 392 LYS   D CG     1 
ATOM   13171 C  CD     . LYS   D 2  392 ? -36.811 28.296   -30.478 1.00 95.30  ? 392 LYS   D CD     1 
ATOM   13172 C  CE     . LYS   D 2  392 ? -37.101 29.432   -29.488 1.00 95.22  ? 392 LYS   D CE     1 
ATOM   13173 N  NZ     . LYS   D 2  392 ? -38.356 30.173   -29.773 1.00 99.15  ? 392 LYS   D NZ     1 
ATOM   13174 N  N      . ALA   D 2  393 ? -32.433 28.738   -33.853 1.00 87.20  ? 393 ALA   D N      1 
ATOM   13175 C  CA     . ALA   D 2  393 ? -31.906 28.566   -35.209 1.00 86.58  ? 393 ALA   D CA     1 
ATOM   13176 C  C      . ALA   D 2  393 ? -32.191 27.186   -35.784 1.00 82.83  ? 393 ALA   D C      1 
ATOM   13177 O  O      . ALA   D 2  393 ? -31.947 26.165   -35.142 1.00 90.60  ? 393 ALA   D O      1 
ATOM   13178 C  CB     . ALA   D 2  393 ? -30.394 28.814   -35.216 1.00 85.43  ? 393 ALA   D CB     1 
ATOM   13179 N  N      . PHE   D 2  394 ? -32.675 27.165   -37.021 1.00 87.10  ? 394 PHE   D N      1 
ATOM   13180 C  CA     . PHE   D 2  394 ? -32.838 25.980   -37.860 1.00 88.13  ? 394 PHE   D CA     1 
ATOM   13181 C  C      . PHE   D 2  394 ? -33.960 25.068   -37.406 1.00 89.44  ? 394 PHE   D C      1 
ATOM   13182 O  O      . PHE   D 2  394 ? -34.164 24.015   -38.025 1.00 92.63  ? 394 PHE   D O      1 
ATOM   13183 C  CB     . PHE   D 2  394 ? -31.525 25.204   -37.982 1.00 85.36  ? 394 PHE   D CB     1 
ATOM   13184 C  CG     . PHE   D 2  394 ? -30.404 26.049   -38.494 1.00 93.11  ? 394 PHE   D CG     1 
ATOM   13185 C  CD1    . PHE   D 2  394 ? -29.646 26.825   -37.626 1.00 95.95  ? 394 PHE   D CD1    1 
ATOM   13186 C  CD2    . PHE   D 2  394 ? -30.121 26.088   -39.850 1.00 95.80  ? 394 PHE   D CD2    1 
ATOM   13187 C  CE1    . PHE   D 2  394 ? -28.628 27.618   -38.097 1.00 98.31  ? 394 PHE   D CE1    1 
ATOM   13188 C  CE2    . PHE   D 2  394 ? -29.101 26.881   -40.330 1.00 97.44  ? 394 PHE   D CE2    1 
ATOM   13189 C  CZ     . PHE   D 2  394 ? -28.353 27.646   -39.453 1.00 99.10  ? 394 PHE   D CZ     1 
ATOM   13190 N  N      . LEU   D 2  395 ? -34.728 25.465   -36.384 1.00 91.02  ? 395 LEU   D N      1 
ATOM   13191 C  CA     . LEU   D 2  395 ? -35.828 24.629   -35.901 1.00 97.69  ? 395 LEU   D CA     1 
ATOM   13192 C  C      . LEU   D 2  395 ? -36.822 24.271   -37.003 1.00 100.72 ? 395 LEU   D C      1 
ATOM   13193 O  O      . LEU   D 2  395 ? -37.514 23.250   -36.895 1.00 98.45  ? 395 LEU   D O      1 
ATOM   13194 C  CB     . LEU   D 2  395 ? -36.566 25.319   -34.748 1.00 91.70  ? 395 LEU   D CB     1 
ATOM   13195 C  CG     . LEU   D 2  395 ? -35.943 25.201   -33.353 1.00 94.71  ? 395 LEU   D CG     1 
ATOM   13196 C  CD1    . LEU   D 2  395 ? -36.958 25.542   -32.255 1.00 98.30  ? 395 LEU   D CD1    1 
ATOM   13197 C  CD2    . LEU   D 2  395 ? -35.360 23.810   -33.141 1.00 89.44  ? 395 LEU   D CD2    1 
ATOM   13198 N  N      . HIS   D 2  396 ? -36.913 25.087   -38.055 1.00 100.86 ? 396 HIS   D N      1 
ATOM   13199 C  CA     . HIS   D 2  396 ? -37.849 24.777   -39.125 1.00 97.88  ? 396 HIS   D CA     1 
ATOM   13200 C  C      . HIS   D 2  396 ? -37.448 23.494   -39.845 1.00 96.23  ? 396 HIS   D C      1 
ATOM   13201 O  O      . HIS   D 2  396 ? -38.314 22.696   -40.221 1.00 99.52  ? 396 HIS   D O      1 
ATOM   13202 C  CB     . HIS   D 2  396 ? -37.966 25.960   -40.098 1.00 102.85 ? 396 HIS   D CB     1 
ATOM   13203 C  CG     . HIS   D 2  396 ? -36.688 26.330   -40.796 1.00 103.08 ? 396 HIS   D CG     1 
ATOM   13204 N  ND1    . HIS   D 2  396 ? -36.328 25.803   -42.019 1.00 103.97 ? 396 HIS   D ND1    1 
ATOM   13205 C  CD2    . HIS   D 2  396 ? -35.704 27.199   -40.458 1.00 97.18  ? 396 HIS   D CD2    1 
ATOM   13206 C  CE1    . HIS   D 2  396 ? -35.170 26.317   -42.395 1.00 100.86 ? 396 HIS   D CE1    1 
ATOM   13207 N  NE2    . HIS   D 2  396 ? -34.770 27.166   -41.466 1.00 96.79  ? 396 HIS   D NE2    1 
ATOM   13208 N  N      . TRP   D 2  397 ? -36.146 23.255   -40.023 1.00 92.37  ? 397 TRP   D N      1 
ATOM   13209 C  CA     . TRP   D 2  397 ? -35.742 21.997   -40.639 1.00 96.79  ? 397 TRP   D CA     1 
ATOM   13210 C  C      . TRP   D 2  397 ? -36.278 20.795   -39.862 1.00 99.53  ? 397 TRP   D C      1 
ATOM   13211 O  O      . TRP   D 2  397 ? -36.369 19.695   -40.422 1.00 96.40  ? 397 TRP   D O      1 
ATOM   13212 C  CB     . TRP   D 2  397 ? -34.217 21.896   -40.750 1.00 96.87  ? 397 TRP   D CB     1 
ATOM   13213 C  CG     . TRP   D 2  397 ? -33.517 22.910   -41.658 1.00 105.28 ? 397 TRP   D CG     1 
ATOM   13214 C  CD1    . TRP   D 2  397 ? -32.618 23.865   -41.261 1.00 104.67 ? 397 TRP   D CD1    1 
ATOM   13215 C  CD2    . TRP   D 2  397 ? -33.642 23.051   -43.090 1.00 111.87 ? 397 TRP   D CD2    1 
ATOM   13216 N  NE1    . TRP   D 2  397 ? -32.180 24.590   -42.347 1.00 107.24 ? 397 TRP   D NE1    1 
ATOM   13217 C  CE2    . TRP   D 2  397 ? -32.795 24.117   -43.480 1.00 113.96 ? 397 TRP   D CE2    1 
ATOM   13218 C  CE3    . TRP   D 2  397 ? -34.388 22.388   -44.076 1.00 115.61 ? 397 TRP   D CE3    1 
ATOM   13219 C  CZ2    . TRP   D 2  397 ? -32.674 24.535   -44.818 1.00 111.93 ? 397 TRP   D CZ2    1 
ATOM   13220 C  CZ3    . TRP   D 2  397 ? -34.268 22.807   -45.406 1.00 111.98 ? 397 TRP   D CZ3    1 
ATOM   13221 C  CH2    . TRP   D 2  397 ? -33.415 23.870   -45.760 1.00 107.50 ? 397 TRP   D CH2    1 
ATOM   13222 N  N      . TYR   D 2  398 ? -36.642 20.975   -38.585 1.00 99.84  ? 398 TYR   D N      1 
ATOM   13223 C  CA     . TYR   D 2  398 ? -37.164 19.885   -37.760 1.00 97.53  ? 398 TYR   D CA     1 
ATOM   13224 C  C      . TYR   D 2  398 ? -38.650 20.047   -37.461 1.00 98.50  ? 398 TYR   D C      1 
ATOM   13225 O  O      . TYR   D 2  398 ? -39.449 19.170   -37.817 1.00 99.11  ? 398 TYR   D O      1 
ATOM   13226 C  CB     . TYR   D 2  398 ? -36.368 19.749   -36.442 1.00 98.36  ? 398 TYR   D CB     1 
ATOM   13227 C  CG     . TYR   D 2  398 ? -34.888 19.566   -36.668 1.00 89.31  ? 398 TYR   D CG     1 
ATOM   13228 C  CD1    . TYR   D 2  398 ? -34.362 18.310   -36.920 1.00 88.98  ? 398 TYR   D CD1    1 
ATOM   13229 C  CD2    . TYR   D 2  398 ? -34.014 20.632   -36.572 1.00 84.19  ? 398 TYR   D CD2    1 
ATOM   13230 C  CE1    . TYR   D 2  398 ? -33.022 18.129   -37.144 1.00 86.14  ? 398 TYR   D CE1    1 
ATOM   13231 C  CE2    . TYR   D 2  398 ? -32.665 20.457   -36.779 1.00 83.80  ? 398 TYR   D CE2    1 
ATOM   13232 C  CZ     . TYR   D 2  398 ? -32.171 19.201   -37.064 1.00 80.76  ? 398 TYR   D CZ     1 
ATOM   13233 O  OH     . TYR   D 2  398 ? -30.824 19.002   -37.273 1.00 76.06  ? 398 TYR   D OH     1 
ATOM   13234 N  N      . THR   D 2  399 ? -39.042 21.145   -36.799 1.00 94.81  ? 399 THR   D N      1 
ATOM   13235 C  CA     . THR   D 2  399 ? -40.455 21.399   -36.547 1.00 93.58  ? 399 THR   D CA     1 
ATOM   13236 C  C      . THR   D 2  399 ? -41.280 21.309   -37.832 1.00 97.27  ? 399 THR   D C      1 
ATOM   13237 O  O      . THR   D 2  399 ? -42.494 21.075   -37.765 1.00 95.24  ? 399 THR   D O      1 
ATOM   13238 C  CB     . THR   D 2  399 ? -40.614 22.765   -35.850 1.00 90.76  ? 399 THR   D CB     1 
ATOM   13239 O  OG1    . THR   D 2  399 ? -41.936 22.885   -35.308 1.00 96.38  ? 399 THR   D OG1    1 
ATOM   13240 C  CG2    . THR   D 2  399 ? -40.330 23.935   -36.800 1.00 89.20  ? 399 THR   D CG2    1 
ATOM   13241 N  N      . GLY   D 2  400 ? -40.638 21.453   -38.999 1.00 95.06  ? 400 GLY   D N      1 
ATOM   13242 C  CA     . GLY   D 2  400 ? -41.325 21.266   -40.264 1.00 89.18  ? 400 GLY   D CA     1 
ATOM   13243 C  C      . GLY   D 2  400 ? -41.589 19.812   -40.597 1.00 95.26  ? 400 GLY   D C      1 
ATOM   13244 O  O      . GLY   D 2  400 ? -42.587 19.497   -41.254 1.00 98.14  ? 400 GLY   D O      1 
ATOM   13245 N  N      . GLU   D 2  401 ? -40.707 18.906   -40.160 1.00 96.25  ? 401 GLU   D N      1 
ATOM   13246 C  CA     . GLU   D 2  401 ? -40.951 17.470   -40.283 1.00 91.88  ? 401 GLU   D CA     1 
ATOM   13247 C  C      . GLU   D 2  401 ? -41.869 16.917   -39.207 1.00 85.87  ? 401 GLU   D C      1 
ATOM   13248 O  O      . GLU   D 2  401 ? -41.985 15.695   -39.097 1.00 82.93  ? 401 GLU   D O      1 
ATOM   13249 C  CB     . GLU   D 2  401 ? -39.641 16.691   -40.262 1.00 89.70  ? 401 GLU   D CB     1 
ATOM   13250 C  CG     . GLU   D 2  401 ? -38.602 17.154   -41.261 1.00 94.59  ? 401 GLU   D CG     1 
ATOM   13251 C  CD     . GLU   D 2  401 ? -38.808 16.528   -42.628 1.00 91.96  ? 401 GLU   D CD     1 
ATOM   13252 O  OE1    . GLU   D 2  401 ? -39.578 15.549   -42.716 1.00 94.08  ? 401 GLU   D OE1    1 
ATOM   13253 O  OE2    . GLU   D 2  401 ? -38.161 16.973   -43.598 1.00 86.98  ? 401 GLU   D OE2    1 
ATOM   13254 N  N      . GLY   D 2  402 ? -42.518 17.775   -38.427 1.00 85.63  ? 402 GLY   D N      1 
ATOM   13255 C  CA     . GLY   D 2  402 ? -43.563 17.367   -37.516 1.00 92.72  ? 402 GLY   D CA     1 
ATOM   13256 C  C      . GLY   D 2  402 ? -43.193 17.398   -36.054 1.00 99.74  ? 402 GLY   D C      1 
ATOM   13257 O  O      . GLY   D 2  402 ? -43.955 16.869   -35.228 1.00 100.16 ? 402 GLY   D O      1 
ATOM   13258 N  N      . MET   D 2  403 ? -42.071 18.018   -35.703 1.00 94.85  ? 403 MET   D N      1 
ATOM   13259 C  CA     . MET   D 2  403 ? -41.476 17.865   -34.386 1.00 96.15  ? 403 MET   D CA     1 
ATOM   13260 C  C      . MET   D 2  403 ? -41.913 18.974   -33.438 1.00 92.03  ? 403 MET   D C      1 
ATOM   13261 O  O      . MET   D 2  403 ? -42.424 20.015   -33.850 1.00 95.66  ? 403 MET   D O      1 
ATOM   13262 C  CB     . MET   D 2  403 ? -39.955 17.821   -34.502 1.00 95.74  ? 403 MET   D CB     1 
ATOM   13263 C  CG     . MET   D 2  403 ? -39.423 16.445   -34.881 1.00 90.65  ? 403 MET   D CG     1 
ATOM   13264 S  SD     . MET   D 2  403 ? -37.626 16.411   -34.825 1.00 92.52  ? 403 MET   D SD     1 
ATOM   13265 C  CE     . MET   D 2  403 ? -37.356 16.505   -33.054 1.00 89.61  ? 403 MET   D CE     1 
ATOM   13266 N  N      . ASP   D 2  404 ? -41.725 18.720   -32.148 1.00 89.20  ? 404 ASP   D N      1 
ATOM   13267 C  CA     . ASP   D 2  404 ? -42.100 19.648   -31.097 1.00 96.43  ? 404 ASP   D CA     1 
ATOM   13268 C  C      . ASP   D 2  404 ? -40.837 20.288   -30.536 1.00 91.34  ? 404 ASP   D C      1 
ATOM   13269 O  O      . ASP   D 2  404 ? -39.751 19.712   -30.611 1.00 86.94  ? 404 ASP   D O      1 
ATOM   13270 C  CB     . ASP   D 2  404 ? -42.882 18.921   -29.992 1.00 99.06  ? 404 ASP   D CB     1 
ATOM   13271 C  CG     . ASP   D 2  404 ? -43.652 19.868   -29.084 1.00 100.22 ? 404 ASP   D CG     1 
ATOM   13272 O  OD1    . ASP   D 2  404 ? -43.252 21.044   -28.933 1.00 95.81  ? 404 ASP   D OD1    1 
ATOM   13273 O  OD2    . ASP   D 2  404 ? -44.677 19.426   -28.530 1.00 102.81 ? 404 ASP   D OD2    1 
ATOM   13274 N  N      . GLU   D 2  405 ? -40.968 21.505   -30.006 1.00 92.18  ? 405 GLU   D N      1 
ATOM   13275 C  CA     . GLU   D 2  405 ? -39.836 22.087   -29.297 1.00 93.07  ? 405 GLU   D CA     1 
ATOM   13276 C  C      . GLU   D 2  405 ? -39.496 21.266   -28.064 1.00 96.11  ? 405 GLU   D C      1 
ATOM   13277 O  O      . GLU   D 2  405 ? -38.329 20.930   -27.839 1.00 95.72  ? 405 GLU   D O      1 
ATOM   13278 C  CB     . GLU   D 2  405 ? -40.102 23.541   -28.902 1.00 101.87 ? 405 GLU   D CB     1 
ATOM   13279 C  CG     . GLU   D 2  405 ? -39.697 24.581   -29.932 1.00 99.01  ? 405 GLU   D CG     1 
ATOM   13280 C  CD     . GLU   D 2  405 ? -39.679 25.999   -29.346 1.00 107.31 ? 405 GLU   D CD     1 
ATOM   13281 O  OE1    . GLU   D 2  405 ? -39.414 26.151   -28.129 1.00 101.46 ? 405 GLU   D OE1    1 
ATOM   13282 O  OE2    . GLU   D 2  405 ? -39.907 26.966   -30.102 1.00 115.84 ? 405 GLU   D OE2    1 
ATOM   13283 N  N      . MET   D 2  406 ? -40.503 20.936   -27.246 1.00 94.82  ? 406 MET   D N      1 
ATOM   13284 C  CA     . MET   D 2  406 ? -40.213 20.186   -26.033 1.00 90.51  ? 406 MET   D CA     1 
ATOM   13285 C  C      . MET   D 2  406 ? -39.490 18.881   -26.324 1.00 88.10  ? 406 MET   D C      1 
ATOM   13286 O  O      . MET   D 2  406 ? -38.843 18.341   -25.424 1.00 91.87  ? 406 MET   D O      1 
ATOM   13287 C  CB     . MET   D 2  406 ? -41.484 19.936   -25.220 1.00 100.76 ? 406 MET   D CB     1 
ATOM   13288 C  CG     . MET   D 2  406 ? -42.743 19.629   -25.999 1.00 109.77 ? 406 MET   D CG     1 
ATOM   13289 S  SD     . MET   D 2  406 ? -44.114 20.328   -25.046 1.00 128.49 ? 406 MET   D SD     1 
ATOM   13290 C  CE     . MET   D 2  406 ? -45.496 20.303   -26.188 1.00 117.34 ? 406 MET   D CE     1 
ATOM   13291 N  N      . GLU   D 2  407 ? -39.551 18.381   -27.563 1.00 87.85  ? 407 GLU   D N      1 
ATOM   13292 C  CA     . GLU   D 2  407 ? -38.712 17.250   -27.957 1.00 83.75  ? 407 GLU   D CA     1 
ATOM   13293 C  C      . GLU   D 2  407 ? -37.232 17.616   -28.011 1.00 82.74  ? 407 GLU   D C      1 
ATOM   13294 O  O      . GLU   D 2  407 ? -36.379 16.760   -27.767 1.00 81.62  ? 407 GLU   D O      1 
ATOM   13295 C  CB     . GLU   D 2  407 ? -39.161 16.701   -29.309 1.00 85.74  ? 407 GLU   D CB     1 
ATOM   13296 C  CG     . GLU   D 2  407 ? -38.386 15.473   -29.767 1.00 84.12  ? 407 GLU   D CG     1 
ATOM   13297 C  CD     . GLU   D 2  407 ? -39.195 14.586   -30.704 1.00 87.45  ? 407 GLU   D CD     1 
ATOM   13298 O  OE1    . GLU   D 2  407 ? -40.399 14.862   -30.895 1.00 88.70  ? 407 GLU   D OE1    1 
ATOM   13299 O  OE2    . GLU   D 2  407 ? -38.623 13.622   -31.255 1.00 83.39  ? 407 GLU   D OE2    1 
ATOM   13300 N  N      . PHE   D 2  408 ? -36.899 18.858   -28.360 1.00 87.81  ? 408 PHE   D N      1 
ATOM   13301 C  CA     . PHE   D 2  408 ? -35.517 19.304   -28.212 1.00 83.43  ? 408 PHE   D CA     1 
ATOM   13302 C  C      . PHE   D 2  408 ? -35.163 19.517   -26.747 1.00 81.46  ? 408 PHE   D C      1 
ATOM   13303 O  O      . PHE   D 2  408 ? -34.077 19.131   -26.305 1.00 83.65  ? 408 PHE   D O      1 
ATOM   13304 C  CB     . PHE   D 2  408 ? -35.271 20.600   -28.998 1.00 84.60  ? 408 PHE   D CB     1 
ATOM   13305 C  CG     . PHE   D 2  408 ? -34.877 20.386   -30.432 1.00 78.35  ? 408 PHE   D CG     1 
ATOM   13306 C  CD1    . PHE   D 2  408 ? -35.813 20.038   -31.387 1.00 85.85  ? 408 PHE   D CD1    1 
ATOM   13307 C  CD2    . PHE   D 2  408 ? -33.559 20.529   -30.820 1.00 76.32  ? 408 PHE   D CD2    1 
ATOM   13308 C  CE1    . PHE   D 2  408 ? -35.441 19.832   -32.708 1.00 83.55  ? 408 PHE   D CE1    1 
ATOM   13309 C  CE2    . PHE   D 2  408 ? -33.183 20.327   -32.130 1.00 79.24  ? 408 PHE   D CE2    1 
ATOM   13310 C  CZ     . PHE   D 2  408 ? -34.126 19.977   -33.077 1.00 82.28  ? 408 PHE   D CZ     1 
ATOM   13311 N  N      . THR   D 2  409 ? -36.065 20.144   -25.988 1.00 80.59  ? 409 THR   D N      1 
ATOM   13312 C  CA     . THR   D 2  409 ? -35.802 20.399   -24.577 1.00 82.11  ? 409 THR   D CA     1 
ATOM   13313 C  C      . THR   D 2  409 ? -35.540 19.102   -23.827 1.00 84.52  ? 409 THR   D C      1 
ATOM   13314 O  O      . THR   D 2  409 ? -34.649 19.039   -22.970 1.00 79.65  ? 409 THR   D O      1 
ATOM   13315 C  CB     . THR   D 2  409 ? -36.984 21.129   -23.954 1.00 80.05  ? 409 THR   D CB     1 
ATOM   13316 O  OG1    . THR   D 2  409 ? -37.082 22.437   -24.520 1.00 78.83  ? 409 THR   D OG1    1 
ATOM   13317 C  CG2    . THR   D 2  409 ? -36.786 21.242   -22.449 1.00 78.14  ? 409 THR   D CG2    1 
ATOM   13318 N  N      . GLU   D 2  410 ? -36.317 18.059   -24.135 1.00 86.49  ? 410 GLU   D N      1 
ATOM   13319 C  CA     . GLU   D 2  410 ? -36.179 16.783   -23.445 1.00 80.29  ? 410 GLU   D CA     1 
ATOM   13320 C  C      . GLU   D 2  410 ? -34.841 16.140   -23.768 1.00 74.99  ? 410 GLU   D C      1 
ATOM   13321 O  O      . GLU   D 2  410 ? -34.106 15.722   -22.867 1.00 76.68  ? 410 GLU   D O      1 
ATOM   13322 C  CB     . GLU   D 2  410 ? -37.332 15.856   -23.822 1.00 77.28  ? 410 GLU   D CB     1 
ATOM   13323 C  CG     . GLU   D 2  410 ? -38.675 16.324   -23.283 1.00 83.89  ? 410 GLU   D CG     1 
ATOM   13324 C  CD     . GLU   D 2  410 ? -39.848 15.564   -23.873 1.00 89.30  ? 410 GLU   D CD     1 
ATOM   13325 O  OE1    . GLU   D 2  410 ? -39.614 14.617   -24.657 1.00 90.76  ? 410 GLU   D OE1    1 
ATOM   13326 O  OE2    . GLU   D 2  410 ? -41.005 15.942   -23.583 1.00 95.25  ? 410 GLU   D OE2    1 
ATOM   13327 N  N      . ALA   D 2  411 ? -34.504 16.051   -25.050 1.00 71.85  ? 411 ALA   D N      1 
ATOM   13328 C  CA     . ALA   D 2  411 ? -33.170 15.592   -25.416 1.00 75.91  ? 411 ALA   D CA     1 
ATOM   13329 C  C      . ALA   D 2  411 ? -32.089 16.423   -24.738 1.00 75.34  ? 411 ALA   D C      1 
ATOM   13330 O  O      . ALA   D 2  411 ? -31.045 15.889   -24.351 1.00 70.40  ? 411 ALA   D O      1 
ATOM   13331 C  CB     . ALA   D 2  411 ? -32.995 15.632   -26.934 1.00 73.01  ? 411 ALA   D CB     1 
ATOM   13332 N  N      . GLU   D 2  412 ? -32.314 17.729   -24.590 1.00 76.10  ? 412 GLU   D N      1 
ATOM   13333 C  CA     . GLU   D 2  412 ? -31.342 18.571   -23.904 1.00 77.95  ? 412 GLU   D CA     1 
ATOM   13334 C  C      . GLU   D 2  412 ? -31.225 18.171   -22.438 1.00 77.41  ? 412 GLU   D C      1 
ATOM   13335 O  O      . GLU   D 2  412 ? -30.128 17.901   -21.938 1.00 67.99  ? 412 GLU   D O      1 
ATOM   13336 C  CB     . GLU   D 2  412 ? -31.745 20.043   -24.023 1.00 81.31  ? 412 GLU   D CB     1 
ATOM   13337 C  CG     . GLU   D 2  412 ? -30.710 21.037   -23.501 1.00 77.80  ? 412 GLU   D CG     1 
ATOM   13338 C  CD     . GLU   D 2  412 ? -31.304 22.414   -23.279 1.00 80.29  ? 412 GLU   D CD     1 
ATOM   13339 O  OE1    . GLU   D 2  412 ? -32.332 22.503   -22.569 1.00 78.11  ? 412 GLU   D OE1    1 
ATOM   13340 O  OE2    . GLU   D 2  412 ? -30.761 23.397   -23.822 1.00 84.17  ? 412 GLU   D OE2    1 
ATOM   13341 N  N      . SER   D 2  413 ? -32.360 18.122   -21.733 1.00 79.07  ? 413 SER   D N      1 
ATOM   13342 C  CA     . SER   D 2  413 ? -32.340 17.825   -20.307 1.00 72.60  ? 413 SER   D CA     1 
ATOM   13343 C  C      . SER   D 2  413 ? -31.852 16.398   -20.040 1.00 74.97  ? 413 SER   D C      1 
ATOM   13344 O  O      . SER   D 2  413 ? -31.101 16.166   -19.083 1.00 74.12  ? 413 SER   D O      1 
ATOM   13345 C  CB     . SER   D 2  413 ? -33.731 18.071   -19.724 1.00 69.86  ? 413 SER   D CB     1 
ATOM   13346 O  OG     . SER   D 2  413 ? -34.017 17.179   -18.660 1.00 83.62  ? 413 SER   D OG     1 
ATOM   13347 N  N      . ASN   D 2  414 ? -32.246 15.428   -20.879 1.00 74.88  ? 414 ASN   D N      1 
ATOM   13348 C  CA     . ASN   D 2  414 ? -31.768 14.053   -20.701 1.00 70.49  ? 414 ASN   D CA     1 
ATOM   13349 C  C      . ASN   D 2  414 ? -30.242 13.991   -20.753 1.00 65.20  ? 414 ASN   D C      1 
ATOM   13350 O  O      . ASN   D 2  414 ? -29.603 13.434   -19.860 1.00 65.03  ? 414 ASN   D O      1 
ATOM   13351 C  CB     . ASN   D 2  414 ? -32.375 13.130   -21.767 1.00 71.61  ? 414 ASN   D CB     1 
ATOM   13352 C  CG     . ASN   D 2  414 ? -32.055 11.635   -21.531 1.00 67.66  ? 414 ASN   D CG     1 
ATOM   13353 O  OD1    . ASN   D 2  414 ? -31.247 11.288   -20.679 1.00 73.42  ? 414 ASN   D OD1    1 
ATOM   13354 N  ND2    . ASN   D 2  414 ? -32.651 10.764   -22.338 1.00 65.56  ? 414 ASN   D ND2    1 
ATOM   13355 N  N      . MET   D 2  415 ? -29.635 14.554   -21.800 1.00 69.94  ? 415 MET   D N      1 
ATOM   13356 C  CA     . MET   D 2  415 ? -28.177 14.536   -21.885 1.00 65.47  ? 415 MET   D CA     1 
ATOM   13357 C  C      . MET   D 2  415 ? -27.551 15.327   -20.750 1.00 67.99  ? 415 MET   D C      1 
ATOM   13358 O  O      . MET   D 2  415 ? -26.503 14.945   -20.226 1.00 63.96  ? 415 MET   D O      1 
ATOM   13359 C  CB     . MET   D 2  415 ? -27.703 15.087   -23.224 1.00 60.50  ? 415 MET   D CB     1 
ATOM   13360 C  CG     . MET   D 2  415 ? -26.295 14.662   -23.557 1.00 67.77  ? 415 MET   D CG     1 
ATOM   13361 S  SD     . MET   D 2  415 ? -25.655 15.330   -25.113 1.00 76.88  ? 415 MET   D SD     1 
ATOM   13362 C  CE     . MET   D 2  415 ? -25.857 17.090   -24.826 1.00 67.43  ? 415 MET   D CE     1 
ATOM   13363 N  N      . ASN   D 2  416 ? -28.165 16.447   -20.366 1.00 74.99  ? 416 ASN   D N      1 
ATOM   13364 C  CA     . ASN   D 2  416 ? -27.660 17.196   -19.218 1.00 70.77  ? 416 ASN   D CA     1 
ATOM   13365 C  C      . ASN   D 2  416 ? -27.673 16.338   -17.969 1.00 66.58  ? 416 ASN   D C      1 
ATOM   13366 O  O      . ASN   D 2  416 ? -26.742 16.401   -17.162 1.00 66.65  ? 416 ASN   D O      1 
ATOM   13367 C  CB     . ASN   D 2  416 ? -28.487 18.461   -18.995 1.00 77.40  ? 416 ASN   D CB     1 
ATOM   13368 C  CG     . ASN   D 2  416 ? -28.169 19.555   -20.004 1.00 82.44  ? 416 ASN   D CG     1 
ATOM   13369 O  OD1    . ASN   D 2  416 ? -27.139 19.520   -20.697 1.00 72.50  ? 416 ASN   D OD1    1 
ATOM   13370 N  ND2    . ASN   D 2  416 ? -29.067 20.532   -20.103 1.00 88.59  ? 416 ASN   D ND2    1 
ATOM   13371 N  N      . ASP   D 2  417 ? -28.730 15.535   -17.789 1.00 70.23  ? 417 ASP   D N      1 
ATOM   13372 C  CA     . ASP   D 2  417 ? -28.803 14.602   -16.663 1.00 65.93  ? 417 ASP   D CA     1 
ATOM   13373 C  C      . ASP   D 2  417 ? -27.656 13.588   -16.704 1.00 64.28  ? 417 ASP   D C      1 
ATOM   13374 O  O      . ASP   D 2  417 ? -26.974 13.357   -15.699 1.00 59.61  ? 417 ASP   D O      1 
ATOM   13375 C  CB     . ASP   D 2  417 ? -30.159 13.898   -16.679 1.00 61.49  ? 417 ASP   D CB     1 
ATOM   13376 C  CG     . ASP   D 2  417 ? -31.307 14.834   -16.344 1.00 73.24  ? 417 ASP   D CG     1 
ATOM   13377 O  OD1    . ASP   D 2  417 ? -31.043 16.009   -16.001 1.00 75.10  ? 417 ASP   D OD1    1 
ATOM   13378 O  OD2    . ASP   D 2  417 ? -32.476 14.397   -16.431 1.00 79.34  ? 417 ASP   D OD2    1 
ATOM   13379 N  N      . LEU   D 2  418 ? -27.410 13.000   -17.879 1.00 66.47  ? 418 LEU   D N      1 
ATOM   13380 C  CA     . LEU   D 2  418 ? -26.341 12.019   -18.058 1.00 60.27  ? 418 LEU   D CA     1 
ATOM   13381 C  C      . LEU   D 2  418 ? -25.013 12.487   -17.464 1.00 61.07  ? 418 LEU   D C      1 
ATOM   13382 O  O      . LEU   D 2  418 ? -24.259 11.681   -16.907 1.00 61.87  ? 418 LEU   D O      1 
ATOM   13383 C  CB     . LEU   D 2  418 ? -26.150 11.740   -19.544 1.00 54.44  ? 418 LEU   D CB     1 
ATOM   13384 C  CG     . LEU   D 2  418 ? -25.181 10.609   -19.800 1.00 51.58  ? 418 LEU   D CG     1 
ATOM   13385 C  CD1    . LEU   D 2  418 ? -25.869 9.347    -19.303 1.00 62.37  ? 418 LEU   D CD1    1 
ATOM   13386 C  CD2    . LEU   D 2  418 ? -24.756 10.501   -21.243 1.00 48.83  ? 418 LEU   D CD2    1 
ATOM   13387 N  N      . VAL   D 2  419 ? -24.678 13.775   -17.632 1.00 62.62  ? 419 VAL   D N      1 
ATOM   13388 C  CA     . VAL   D 2  419 ? -23.451 14.317   -17.045 1.00 62.68  ? 419 VAL   D CA     1 
ATOM   13389 C  C      . VAL   D 2  419 ? -23.617 14.564   -15.553 1.00 57.90  ? 419 VAL   D C      1 
ATOM   13390 O  O      . VAL   D 2  419 ? -22.695 14.301   -14.775 1.00 60.95  ? 419 VAL   D O      1 
ATOM   13391 C  CB     . VAL   D 2  419 ? -23.000 15.596   -17.777 1.00 55.99  ? 419 VAL   D CB     1 
ATOM   13392 C  CG1    . VAL   D 2  419 ? -22.429 15.278   -19.108 1.00 51.54  ? 419 VAL   D CG1    1 
ATOM   13393 C  CG2    . VAL   D 2  419 ? -24.185 16.479   -17.973 1.00 63.01  ? 419 VAL   D CG2    1 
ATOM   13394 N  N      . SER   D 2  420 ? -24.765 15.097   -15.127 1.00 55.83  ? 420 SER   D N      1 
ATOM   13395 C  CA     . SER   D 2  420 ? -25.052 15.138   -13.695 1.00 61.32  ? 420 SER   D CA     1 
ATOM   13396 C  C      . SER   D 2  420 ? -24.641 13.809   -13.081 1.00 62.80  ? 420 SER   D C      1 
ATOM   13397 O  O      . SER   D 2  420 ? -23.946 13.749   -12.059 1.00 56.12  ? 420 SER   D O      1 
ATOM   13398 C  CB     . SER   D 2  420 ? -26.547 15.387   -13.437 1.00 64.40  ? 420 SER   D CB     1 
ATOM   13399 O  OG     . SER   D 2  420 ? -27.048 16.506   -14.143 1.00 71.17  ? 420 SER   D OG     1 
ATOM   13400 N  N      . GLU   D 2  421 ? -25.034 12.729   -13.759 1.00 63.21  ? 421 GLU   D N      1 
ATOM   13401 C  CA     . GLU   D 2  421 ? -24.884 11.381   -13.249 1.00 55.61  ? 421 GLU   D CA     1 
ATOM   13402 C  C      . GLU   D 2  421 ? -23.446 10.903   -13.329 1.00 55.60  ? 421 GLU   D C      1 
ATOM   13403 O  O      . GLU   D 2  421 ? -22.984 10.204   -12.422 1.00 55.42  ? 421 GLU   D O      1 
ATOM   13404 C  CB     . GLU   D 2  421 ? -25.859 10.460   -13.988 1.00 47.76  ? 421 GLU   D CB     1 
ATOM   13405 C  CG     . GLU   D 2  421 ? -27.298 10.766   -13.543 1.00 58.29  ? 421 GLU   D CG     1 
ATOM   13406 C  CD     . GLU   D 2  421 ? -28.385 10.442   -14.552 1.00 63.39  ? 421 GLU   D CD     1 
ATOM   13407 O  OE1    . GLU   D 2  421 ? -28.119 9.683    -15.508 1.00 65.18  ? 421 GLU   D OE1    1 
ATOM   13408 O  OE2    . GLU   D 2  421 ? -29.527 10.932   -14.356 1.00 62.83  ? 421 GLU   D OE2    1 
ATOM   13409 N  N      . TYR   D 2  422 ? -22.717 11.283   -14.381 1.00 56.43  ? 422 TYR   D N      1 
ATOM   13410 C  CA     . TYR   D 2  422 ? -21.284 11.005   -14.420 1.00 54.12  ? 422 TYR   D CA     1 
ATOM   13411 C  C      . TYR   D 2  422 ? -20.564 11.748   -13.301 1.00 56.40  ? 422 TYR   D C      1 
ATOM   13412 O  O      . TYR   D 2  422 ? -19.750 11.167   -12.575 1.00 53.89  ? 422 TYR   D O      1 
ATOM   13413 C  CB     . TYR   D 2  422 ? -20.716 11.375   -15.789 1.00 50.59  ? 422 TYR   D CB     1 
ATOM   13414 C  CG     . TYR   D 2  422 ? -20.689 10.217   -16.761 1.00 58.01  ? 422 TYR   D CG     1 
ATOM   13415 C  CD1    . TYR   D 2  422 ? -19.901 9.100    -16.514 1.00 52.77  ? 422 TYR   D CD1    1 
ATOM   13416 C  CD2    . TYR   D 2  422 ? -21.496 10.216   -17.915 1.00 63.02  ? 422 TYR   D CD2    1 
ATOM   13417 C  CE1    . TYR   D 2  422 ? -19.882 8.017    -17.414 1.00 56.46  ? 422 TYR   D CE1    1 
ATOM   13418 C  CE2    . TYR   D 2  422 ? -21.487 9.135    -18.825 1.00 54.97  ? 422 TYR   D CE2    1 
ATOM   13419 C  CZ     . TYR   D 2  422 ? -20.679 8.033    -18.563 1.00 57.34  ? 422 TYR   D CZ     1 
ATOM   13420 O  OH     . TYR   D 2  422 ? -20.647 6.943    -19.425 1.00 53.91  ? 422 TYR   D OH     1 
ATOM   13421 N  N      . GLN   D 2  423 ? -20.879 13.029   -13.116 1.00 55.12  ? 423 GLN   D N      1 
ATOM   13422 C  CA     . GLN   D 2  423 ? -20.270 13.745   -12.009 1.00 54.14  ? 423 GLN   D CA     1 
ATOM   13423 C  C      . GLN   D 2  423 ? -20.625 13.101   -10.670 1.00 55.21  ? 423 GLN   D C      1 
ATOM   13424 O  O      . GLN   D 2  423 ? -19.827 13.152   -9.727  1.00 51.78  ? 423 GLN   D O      1 
ATOM   13425 C  CB     . GLN   D 2  423 ? -20.694 15.211   -12.014 1.00 53.77  ? 423 GLN   D CB     1 
ATOM   13426 C  CG     . GLN   D 2  423 ? -19.898 16.046   -11.009 1.00 51.76  ? 423 GLN   D CG     1 
ATOM   13427 C  CD     . GLN   D 2  423 ? -18.442 16.204   -11.416 1.00 54.64  ? 423 GLN   D CD     1 
ATOM   13428 O  OE1    . GLN   D 2  423 ? -18.143 16.430   -12.596 1.00 62.28  ? 423 GLN   D OE1    1 
ATOM   13429 N  NE2    . GLN   D 2  423 ? -17.532 16.071   -10.458 1.00 51.55  ? 423 GLN   D NE2    1 
ATOM   13430 N  N      . GLN   D 2  424 ? -21.812 12.492   -10.560 1.00 55.33  ? 424 GLN   D N      1 
ATOM   13431 C  CA     . GLN   D 2  424 ? -22.235 11.952   -9.272  1.00 51.23  ? 424 GLN   D CA     1 
ATOM   13432 C  C      . GLN   D 2  424 ? -21.319 10.826   -8.823  1.00 53.63  ? 424 GLN   D C      1 
ATOM   13433 O  O      . GLN   D 2  424 ? -20.935 10.756   -7.647  1.00 56.24  ? 424 GLN   D O      1 
ATOM   13434 C  CB     . GLN   D 2  424 ? -23.687 11.478   -9.332  1.00 54.56  ? 424 GLN   D CB     1 
ATOM   13435 C  CG     . GLN   D 2  424 ? -24.143 10.783   -8.039  1.00 63.97  ? 424 GLN   D CG     1 
ATOM   13436 C  CD     . GLN   D 2  424 ? -25.481 10.039   -8.153  1.00 71.68  ? 424 GLN   D CD     1 
ATOM   13437 O  OE1    . GLN   D 2  424 ? -26.214 10.184   -9.134  1.00 73.23  ? 424 GLN   D OE1    1 
ATOM   13438 N  NE2    . GLN   D 2  424 ? -25.777 9.204    -7.156  1.00 68.09  ? 424 GLN   D NE2    1 
ATOM   13439 N  N      . TYR   D 2  425 ? -20.941 9.948    -9.740  1.00 49.15  ? 425 TYR   D N      1 
ATOM   13440 C  CA     . TYR   D 2  425 ? -20.081 8.844    -9.361  1.00 51.37  ? 425 TYR   D CA     1 
ATOM   13441 C  C      . TYR   D 2  425 ? -18.600 9.188    -9.457  1.00 55.51  ? 425 TYR   D C      1 
ATOM   13442 O  O      . TYR   D 2  425 ? -17.761 8.421    -8.968  1.00 59.09  ? 425 TYR   D O      1 
ATOM   13443 C  CB     . TYR   D 2  425 ? -20.406 7.602    -10.205 1.00 51.12  ? 425 TYR   D CB     1 
ATOM   13444 C  CG     . TYR   D 2  425 ? -21.824 7.116    -9.987  1.00 49.28  ? 425 TYR   D CG     1 
ATOM   13445 C  CD1    . TYR   D 2  425 ? -22.225 6.653    -8.752  1.00 49.97  ? 425 TYR   D CD1    1 
ATOM   13446 C  CD2    . TYR   D 2  425 ? -22.736 7.066    -11.021 1.00 47.79  ? 425 TYR   D CD2    1 
ATOM   13447 C  CE1    . TYR   D 2  425 ? -23.497 6.208    -8.532  1.00 49.77  ? 425 TYR   D CE1    1 
ATOM   13448 C  CE2    . TYR   D 2  425 ? -24.017 6.612    -10.810 1.00 49.18  ? 425 TYR   D CE2    1 
ATOM   13449 C  CZ     . TYR   D 2  425 ? -24.388 6.182    -9.559  1.00 53.10  ? 425 TYR   D CZ     1 
ATOM   13450 O  OH     . TYR   D 2  425 ? -25.656 5.716    -9.318  1.00 56.87  ? 425 TYR   D OH     1 
ATOM   13451 N  N      . GLN   D 2  426 ? -18.249 10.318   -10.061 1.00 52.65  ? 426 GLN   D N      1 
ATOM   13452 C  CA     . GLN   D 2  426 ? -16.876 10.782   -9.944  1.00 52.90  ? 426 GLN   D CA     1 
ATOM   13453 C  C      . GLN   D 2  426 ? -16.613 11.388   -8.570  1.00 54.27  ? 426 GLN   D C      1 
ATOM   13454 O  O      . GLN   D 2  426 ? -15.494 11.294   -8.053  1.00 55.60  ? 426 GLN   D O      1 
ATOM   13455 C  CB     . GLN   D 2  426 ? -16.583 11.786   -11.052 1.00 52.80  ? 426 GLN   D CB     1 
ATOM   13456 C  CG     . GLN   D 2  426 ? -15.141 12.204   -11.117 1.00 57.60  ? 426 GLN   D CG     1 
ATOM   13457 C  CD     . GLN   D 2  426 ? -14.934 13.292   -12.121 1.00 57.38  ? 426 GLN   D CD     1 
ATOM   13458 O  OE1    . GLN   D 2  426 ? -15.297 13.136   -13.279 1.00 55.31  ? 426 GLN   D OE1    1 
ATOM   13459 N  NE2    . GLN   D 2  426 ? -14.353 14.404   -11.693 1.00 60.68  ? 426 GLN   D NE2    1 
ATOM   13460 N  N      . ASP   D 2  427 ? -17.643 11.980   -7.965  1.00 50.34  ? 427 ASP   D N      1 
ATOM   13461 C  CA     . ASP   D 2  427 ? -17.587 12.500   -6.608  1.00 51.45  ? 427 ASP   D CA     1 
ATOM   13462 C  C      . ASP   D 2  427 ? -17.811 11.439   -5.549  1.00 52.56  ? 427 ASP   D C      1 
ATOM   13463 O  O      . ASP   D 2  427 ? -17.401 11.646   -4.401  1.00 48.06  ? 427 ASP   D O      1 
ATOM   13464 C  CB     . ASP   D 2  427 ? -18.636 13.600   -6.420  1.00 57.26  ? 427 ASP   D CB     1 
ATOM   13465 C  CG     . ASP   D 2  427 ? -18.407 14.797   -7.333  1.00 57.40  ? 427 ASP   D CG     1 
ATOM   13466 O  OD1    . ASP   D 2  427 ? -17.365 14.817   -8.045  1.00 60.55  ? 427 ASP   D OD1    1 
ATOM   13467 O  OD2    . ASP   D 2  427 ? -19.278 15.702   -7.345  1.00 48.50  ? 427 ASP   D OD2    1 
ATOM   13468 N  N      . ALA   D 2  428 ? -18.464 10.326   -5.896  1.00 58.76  ? 428 ALA   D N      1 
ATOM   13469 C  CA     . ALA   D 2  428 ? -18.761 9.282    -4.915  1.00 58.31  ? 428 ALA   D CA     1 
ATOM   13470 C  C      . ALA   D 2  428 ? -17.492 8.741    -4.269  1.00 54.01  ? 428 ALA   D C      1 
ATOM   13471 O  O      . ALA   D 2  428 ? -16.454 8.603    -4.921  1.00 51.62  ? 428 ALA   D O      1 
ATOM   13472 C  CB     . ALA   D 2  428 ? -19.521 8.131    -5.567  1.00 51.64  ? 428 ALA   D CB     1 
ATOM   13473 N  N      . THR   D 2  429 ? -17.595 8.415    -2.978  1.00 62.22  ? 429 THR   D N      1 
ATOM   13474 C  CA     . THR   D 2  429 ? -16.513 7.804    -2.213  1.00 63.58  ? 429 THR   D CA     1 
ATOM   13475 C  C      . THR   D 2  429 ? -17.008 6.569    -1.473  1.00 64.30  ? 429 THR   D C      1 
ATOM   13476 O  O      . THR   D 2  429 ? -18.205 6.396    -1.218  1.00 55.94  ? 429 THR   D O      1 
ATOM   13477 C  CB     . THR   D 2  429 ? -15.915 8.754    -1.179  1.00 55.62  ? 429 THR   D CB     1 
ATOM   13478 O  OG1    . THR   D 2  429 ? -16.963 9.220    -0.317  1.00 61.96  ? 429 THR   D OG1    1 
ATOM   13479 C  CG2    . THR   D 2  429 ? -15.232 9.911    -1.863  1.00 57.25  ? 429 THR   D CG2    1 
ATOM   13480 N  N      . ALA   D 2  430 ? -16.041 5.729    -1.104  1.00 60.52  ? 430 ALA   D N      1 
ATOM   13481 C  CA     . ALA   D 2  430 ? -16.346 4.510    -0.374  1.00 58.08  ? 430 ALA   D CA     1 
ATOM   13482 C  C      . ALA   D 2  430 ? -16.748 4.809    1.072   1.00 68.53  ? 430 ALA   D C      1 
ATOM   13483 O  O      . ALA   D 2  430 ? -17.781 4.327    1.554   1.00 66.58  ? 430 ALA   D O      1 
ATOM   13484 C  CB     . ALA   D 2  430 ? -15.139 3.589    -0.436  1.00 50.20  ? 430 ALA   D CB     1 
ATOM   13485 N  N      . ASP   D 2  431 ? -15.958 5.614    1.777   1.00 77.08  ? 431 ASP   D N      1 
ATOM   13486 C  CA     . ASP   D 2  431 ? -16.258 5.935    3.177   1.00 83.12  ? 431 ASP   D CA     1 
ATOM   13487 C  C      . ASP   D 2  431 ? -17.546 6.749    3.314   1.00 85.25  ? 431 ASP   D C      1 
ATOM   13488 O  O      . ASP   D 2  431 ? -18.652 6.230    3.148   1.00 86.14  ? 431 ASP   D O      1 
ATOM   13489 C  CB     . ASP   D 2  431 ? -15.092 6.695    3.815   1.00 88.85  ? 431 ASP   D CB     1 
ATOM   13490 N  N      . MET   E 3  4   ? -20.392 -89.709  93.784  1.00 78.42  ? 6   MET   E N      1 
ATOM   13491 C  CA     . MET   E 3  4   ? -20.538 -89.920  92.336  1.00 74.44  ? 6   MET   E CA     1 
ATOM   13492 C  C      . MET   E 3  4   ? -21.360 -91.180  91.990  1.00 75.68  ? 6   MET   E C      1 
ATOM   13493 O  O      . MET   E 3  4   ? -20.805 -92.232  91.686  1.00 76.39  ? 6   MET   E O      1 
ATOM   13494 C  CB     . MET   E 3  4   ? -19.150 -89.974  91.680  1.00 74.57  ? 6   MET   E CB     1 
ATOM   13495 C  CG     . MET   E 3  4   ? -19.154 -89.867  90.149  1.00 76.43  ? 6   MET   E CG     1 
ATOM   13496 S  SD     . MET   E 3  4   ? -17.519 -89.719  89.350  1.00 73.21  ? 6   MET   E SD     1 
ATOM   13497 C  CE     . MET   E 3  4   ? -16.882 -88.292  90.241  1.00 67.77  ? 6   MET   E CE     1 
ATOM   13498 N  N      . GLU   E 3  5   ? -22.690 -91.034  92.009  1.00 74.72  ? 7   GLU   E N      1 
ATOM   13499 C  CA     . GLU   E 3  5   ? -23.634 -92.142  91.862  1.00 74.64  ? 7   GLU   E CA     1 
ATOM   13500 C  C      . GLU   E 3  5   ? -23.757 -92.629  90.420  1.00 71.61  ? 7   GLU   E C      1 
ATOM   13501 O  O      . GLU   E 3  5   ? -24.056 -91.838  89.522  1.00 71.75  ? 7   GLU   E O      1 
ATOM   13502 C  CB     . GLU   E 3  5   ? -25.006 -91.693  92.378  1.00 78.75  ? 7   GLU   E CB     1 
ATOM   13503 C  CG     . GLU   E 3  5   ? -26.083 -92.776  92.464  1.00 81.82  ? 7   GLU   E CG     1 
ATOM   13504 C  CD     . GLU   E 3  5   ? -27.421 -92.223  92.952  1.00 82.69  ? 7   GLU   E CD     1 
ATOM   13505 O  OE1    . GLU   E 3  5   ? -27.799 -91.103  92.550  1.00 81.88  ? 7   GLU   E OE1    1 
ATOM   13506 O  OE2    . GLU   E 3  5   ? -28.080 -92.903  93.768  1.00 84.15  ? 7   GLU   E OE2    1 
ATOM   13507 N  N      . VAL   E 3  6   ? -23.544 -93.968  90.198  1.00 69.60  ? 8   VAL   E N      1 
ATOM   13508 C  CA     . VAL   E 3  6   ? -23.829 -94.633  88.923  1.00 63.82  ? 8   VAL   E CA     1 
ATOM   13509 C  C      . VAL   E 3  6   ? -25.225 -95.226  88.979  1.00 62.57  ? 8   VAL   E C      1 
ATOM   13510 O  O      . VAL   E 3  6   ? -25.694 -95.631  90.040  1.00 68.28  ? 8   VAL   E O      1 
ATOM   13511 C  CB     . VAL   E 3  6   ? -22.794 -95.722  88.593  1.00 52.30  ? 8   VAL   E CB     1 
ATOM   13512 C  CG1    . VAL   E 3  6   ? -23.349 -96.647  87.529  1.00 51.79  ? 8   VAL   E CG1    1 
ATOM   13513 C  CG2    . VAL   E 3  6   ? -21.504 -95.090  88.145  1.00 48.53  ? 8   VAL   E CG2    1 
ATOM   13514 N  N      . ILE   E 3  7   ? -25.911 -95.276  87.839  1.00 59.36  ? 9   ILE   E N      1 
ATOM   13515 C  CA     . ILE   E 3  7   ? -27.333 -95.589  87.831  1.00 63.20  ? 9   ILE   E CA     1 
ATOM   13516 C  C      . ILE   E 3  7   ? -27.697 -96.248  86.512  1.00 63.78  ? 9   ILE   E C      1 
ATOM   13517 O  O      . ILE   E 3  7   ? -26.867 -96.411  85.619  1.00 63.63  ? 9   ILE   E O      1 
ATOM   13518 C  CB     . ILE   E 3  7   ? -28.228 -94.344  88.035  1.00 64.90  ? 9   ILE   E CB     1 
ATOM   13519 C  CG1    . ILE   E 3  7   ? -28.456 -93.636  86.710  1.00 67.67  ? 9   ILE   E CG1    1 
ATOM   13520 C  CG2    . ILE   E 3  7   ? -27.589 -93.346  88.990  1.00 67.97  ? 9   ILE   E CG2    1 
ATOM   13521 C  CD1    . ILE   E 3  7   ? -29.352 -92.424  86.823  1.00 74.12  ? 9   ILE   E CD1    1 
ATOM   13522 N  N      . GLU   E 3  8   ? -28.974 -96.614  86.409  1.00 67.54  ? 10  GLU   E N      1 
ATOM   13523 C  CA     . GLU   E 3  8   ? -29.633 -97.230  85.259  1.00 69.53  ? 10  GLU   E CA     1 
ATOM   13524 C  C      . GLU   E 3  8   ? -28.677 -97.915  84.275  1.00 65.14  ? 10  GLU   E C      1 
ATOM   13525 O  O      . GLU   E 3  8   ? -28.908 -97.916  83.060  1.00 56.77  ? 10  GLU   E O      1 
ATOM   13526 C  CB     . GLU   E 3  8   ? -30.505 -96.164  84.589  1.00 71.69  ? 10  GLU   E CB     1 
ATOM   13527 C  CG     . GLU   E 3  8   ? -31.359 -95.399  85.620  1.00 74.25  ? 10  GLU   E CG     1 
ATOM   13528 C  CD     . GLU   E 3  8   ? -32.624 -94.757  85.052  1.00 87.15  ? 10  GLU   E CD     1 
ATOM   13529 O  OE1    . GLU   E 3  8   ? -32.674 -94.509  83.829  1.00 91.24  ? 10  GLU   E OE1    1 
ATOM   13530 O  OE2    . GLU   E 3  8   ? -33.568 -94.484  85.837  1.00 85.89  ? 10  GLU   E OE2    1 
ATOM   13531 N  N      . LEU   E 3  9   ? -27.634 -98.559  84.811  1.00 67.42  ? 11  LEU   E N      1 
ATOM   13532 C  CA     . LEU   E 3  9   ? -26.678 -99.345  84.033  1.00 61.23  ? 11  LEU   E CA     1 
ATOM   13533 C  C      . LEU   E 3  9   ? -27.335 -100.505 83.301  1.00 60.15  ? 11  LEU   E C      1 
ATOM   13534 O  O      . LEU   E 3  9   ? -27.559 -101.558 83.901  1.00 62.12  ? 11  LEU   E O      1 
ATOM   13535 C  CB     . LEU   E 3  9   ? -25.577 -99.915  84.931  1.00 54.19  ? 11  LEU   E CB     1 
ATOM   13536 C  CG     . LEU   E 3  9   ? -24.713 -100.962 84.227  1.00 50.73  ? 11  LEU   E CG     1 
ATOM   13537 C  CD1    . LEU   E 3  9   ? -23.946 -100.315 83.112  1.00 52.04  ? 11  LEU   E CD1    1 
ATOM   13538 C  CD2    . LEU   E 3  9   ? -23.751 -101.614 85.184  1.00 55.24  ? 11  LEU   E CD2    1 
ATOM   13539 N  N      . ASN   E 3  10  ? -27.611 -100.339 82.010  1.00 57.68  ? 12  ASN   E N      1 
ATOM   13540 C  CA     . ASN   E 3  10  ? -28.107 -101.413 81.160  1.00 58.59  ? 12  ASN   E CA     1 
ATOM   13541 C  C      . ASN   E 3  10  ? -26.939 -101.992 80.362  1.00 56.95  ? 12  ASN   E C      1 
ATOM   13542 O  O      . ASN   E 3  10  ? -26.094 -101.258 79.849  1.00 55.91  ? 12  ASN   E O      1 
ATOM   13543 C  CB     . ASN   E 3  10  ? -29.216 -100.896 80.228  1.00 61.91  ? 12  ASN   E CB     1 
ATOM   13544 C  CG     . ASN   E 3  10  ? -30.411 -100.284 81.011  1.00 77.31  ? 12  ASN   E CG     1 
ATOM   13545 O  OD1    . ASN   E 3  10  ? -30.803 -99.126  80.791  1.00 70.00  ? 12  ASN   E OD1    1 
ATOM   13546 N  ND2    . ASN   E 3  10  ? -30.957 -101.053 81.954  1.00 77.93  ? 12  ASN   E ND2    1 
ATOM   13547 N  N      . LYS   E 3  11  ? -26.855 -103.313 80.306  1.00 62.95  ? 13  LYS   E N      1 
ATOM   13548 C  CA     . LYS   E 3  11  ? -25.841 -103.982 79.506  1.00 60.15  ? 13  LYS   E CA     1 
ATOM   13549 C  C      . LYS   E 3  11  ? -26.498 -104.683 78.333  1.00 60.47  ? 13  LYS   E C      1 
ATOM   13550 O  O      . LYS   E 3  11  ? -27.723 -104.792 78.234  1.00 71.32  ? 13  LYS   E O      1 
ATOM   13551 C  CB     . LYS   E 3  11  ? -25.033 -104.987 80.335  1.00 56.67  ? 13  LYS   E CB     1 
ATOM   13552 C  CG     . LYS   E 3  11  ? -24.270 -104.361 81.488  1.00 60.11  ? 13  LYS   E CG     1 
ATOM   13553 C  CD     . LYS   E 3  11  ? -23.626 -105.420 82.351  1.00 58.56  ? 13  LYS   E CD     1 
ATOM   13554 C  CE     . LYS   E 3  11  ? -22.454 -106.073 81.625  1.00 63.09  ? 13  LYS   E CE     1 
ATOM   13555 N  NZ     . LYS   E 3  11  ? -21.829 -107.258 82.332  1.00 63.50  ? 13  LYS   E NZ     1 
ATOM   13556 N  N      . CYS   E 3  12  ? -25.668 -105.149 77.436  1.00 53.78  ? 14  CYS   E N      1 
ATOM   13557 C  CA     . CYS   E 3  12  ? -26.148 -105.976 76.344  1.00 63.29  ? 14  CYS   E CA     1 
ATOM   13558 C  C      . CYS   E 3  12  ? -24.911 -106.504 75.659  1.00 65.82  ? 14  CYS   E C      1 
ATOM   13559 O  O      . CYS   E 3  12  ? -23.783 -106.264 76.110  1.00 63.98  ? 14  CYS   E O      1 
ATOM   13560 C  CB     . CYS   E 3  12  ? -27.014 -105.206 75.348  1.00 69.83  ? 14  CYS   E CB     1 
ATOM   13561 S  SG     . CYS   E 3  12  ? -26.034 -104.126 74.287  1.00 59.86  ? 14  CYS   E SG     1 
ATOM   13562 N  N      . THR   E 3  13  ? -25.119 -107.174 74.533  1.00 64.44  ? 15  THR   E N      1 
ATOM   13563 C  CA     . THR   E 3  13  ? -23.986 -107.810 73.881  1.00 67.51  ? 15  THR   E CA     1 
ATOM   13564 C  C      . THR   E 3  13  ? -23.129 -106.800 73.107  1.00 62.26  ? 15  THR   E C      1 
ATOM   13565 O  O      . THR   E 3  13  ? -21.916 -107.002 72.994  1.00 48.17  ? 15  THR   E O      1 
ATOM   13566 C  CB     . THR   E 3  13  ? -24.500 -108.952 73.002  1.00 71.57  ? 15  THR   E CB     1 
ATOM   13567 O  OG1    . THR   E 3  13  ? -23.394 -109.605 72.389  1.00 56.84  ? 15  THR   E OG1    1 
ATOM   13568 C  CG2    . THR   E 3  13  ? -25.476 -108.441 71.919  1.00 74.04  ? 15  THR   E CG2    1 
ATOM   13569 N  N      . SER   E 3  14  ? -23.728 -105.682 72.635  1.00 69.72  ? 16  SER   E N      1 
ATOM   13570 C  CA     . SER   E 3  14  ? -23.044 -104.687 71.792  1.00 63.44  ? 16  SER   E CA     1 
ATOM   13571 C  C      . SER   E 3  14  ? -22.191 -103.703 72.586  1.00 64.01  ? 16  SER   E C      1 
ATOM   13572 O  O      . SER   E 3  14  ? -21.186 -103.201 72.067  1.00 60.41  ? 16  SER   E O      1 
ATOM   13573 C  CB     . SER   E 3  14  ? -24.058 -103.870 70.985  1.00 62.22  ? 16  SER   E CB     1 
ATOM   13574 O  OG     . SER   E 3  14  ? -25.061 -104.687 70.434  1.00 73.10  ? 16  SER   E OG     1 
ATOM   13575 N  N      . GLY   E 3  15  ? -22.609 -103.384 73.811  1.00 66.91  ? 17  GLY   E N      1 
ATOM   13576 C  CA     . GLY   E 3  15  ? -21.886 -102.527 74.742  1.00 60.14  ? 17  GLY   E CA     1 
ATOM   13577 C  C      . GLY   E 3  15  ? -22.695 -102.367 76.017  1.00 61.12  ? 17  GLY   E C      1 
ATOM   13578 O  O      . GLY   E 3  15  ? -23.494 -103.249 76.356  1.00 66.51  ? 17  GLY   E O      1 
ATOM   13579 N  N      . GLN   E 3  16  ? -22.505 -101.267 76.740  1.00 51.17  ? 18  GLN   E N      1 
ATOM   13580 C  CA     . GLN   E 3  16  ? -23.415 -100.933 77.824  1.00 50.62  ? 18  GLN   E CA     1 
ATOM   13581 C  C      . GLN   E 3  16  ? -23.590 -99.424  77.886  1.00 52.72  ? 18  GLN   E C      1 
ATOM   13582 O  O      . GLN   E 3  16  ? -22.866 -98.665  77.235  1.00 55.36  ? 18  GLN   E O      1 
ATOM   13583 C  CB     . GLN   E 3  16  ? -22.931 -101.515 79.158  1.00 57.19  ? 18  GLN   E CB     1 
ATOM   13584 C  CG     . GLN   E 3  16  ? -21.480 -101.195 79.519  1.00 55.62  ? 18  GLN   E CG     1 
ATOM   13585 C  CD     . GLN   E 3  16  ? -20.878 -102.203 80.495  1.00 51.60  ? 18  GLN   E CD     1 
ATOM   13586 O  OE1    . GLN   E 3  16  ? -21.233 -102.255 81.670  1.00 54.54  ? 18  GLN   E OE1    1 
ATOM   13587 N  NE2    . GLN   E 3  16  ? -19.984 -103.016 79.999  1.00 52.02  ? 18  GLN   E NE2    1 
ATOM   13588 N  N      . SER   E 3  17  ? -24.562 -98.997  78.689  1.00 48.72  ? 19  SER   E N      1 
ATOM   13589 C  CA     . SER   E 3  17  ? -24.858 -97.591  78.901  1.00 42.93  ? 19  SER   E CA     1 
ATOM   13590 C  C      . SER   E 3  17  ? -25.173 -97.359  80.374  1.00 47.25  ? 19  SER   E C      1 
ATOM   13591 O  O      . SER   E 3  17  ? -25.460 -98.291  81.119  1.00 51.13  ? 19  SER   E O      1 
ATOM   13592 C  CB     . SER   E 3  17  ? -26.030 -97.174  78.037  1.00 55.77  ? 19  SER   E CB     1 
ATOM   13593 O  OG     . SER   E 3  17  ? -27.212 -97.788  78.519  1.00 61.26  ? 19  SER   E OG     1 
ATOM   13594 N  N      . PHE   E 3  18  ? -25.126 -96.104  80.799  1.00 53.12  ? 20  PHE   E N      1 
ATOM   13595 C  CA     . PHE   E 3  18  ? -25.369 -95.772  82.200  1.00 51.51  ? 20  PHE   E CA     1 
ATOM   13596 C  C      . PHE   E 3  18  ? -25.309 -94.258  82.337  1.00 54.66  ? 20  PHE   E C      1 
ATOM   13597 O  O      . PHE   E 3  18  ? -24.863 -93.549  81.430  1.00 59.11  ? 20  PHE   E O      1 
ATOM   13598 C  CB     . PHE   E 3  18  ? -24.361 -96.440  83.137  1.00 47.81  ? 20  PHE   E CB     1 
ATOM   13599 C  CG     . PHE   E 3  18  ? -22.929 -96.012  82.903  1.00 48.55  ? 20  PHE   E CG     1 
ATOM   13600 C  CD1    . PHE   E 3  18  ? -22.152 -96.630  81.922  1.00 48.01  ? 20  PHE   E CD1    1 
ATOM   13601 C  CD2    . PHE   E 3  18  ? -22.348 -95.016  83.676  1.00 51.65  ? 20  PHE   E CD2    1 
ATOM   13602 C  CE1    . PHE   E 3  18  ? -20.827 -96.248  81.694  1.00 47.36  ? 20  PHE   E CE1    1 
ATOM   13603 C  CE2    . PHE   E 3  18  ? -21.017 -94.620  83.461  1.00 51.66  ? 20  PHE   E CE2    1 
ATOM   13604 C  CZ     . PHE   E 3  18  ? -20.259 -95.233  82.468  1.00 49.14  ? 20  PHE   E CZ     1 
ATOM   13605 N  N      . GLU   E 3  19  ? -25.787 -93.768  83.469  1.00 56.39  ? 21  GLU   E N      1 
ATOM   13606 C  CA     . GLU   E 3  19  ? -25.690 -92.365  83.828  1.00 55.59  ? 21  GLU   E CA     1 
ATOM   13607 C  C      . GLU   E 3  19  ? -24.794 -92.256  85.047  1.00 63.49  ? 21  GLU   E C      1 
ATOM   13608 O  O      . GLU   E 3  19  ? -24.579 -93.235  85.763  1.00 66.31  ? 21  GLU   E O      1 
ATOM   13609 C  CB     . GLU   E 3  19  ? -27.060 -91.769  84.127  1.00 55.33  ? 21  GLU   E CB     1 
ATOM   13610 C  CG     . GLU   E 3  19  ? -27.067 -90.296  84.413  1.00 62.30  ? 21  GLU   E CG     1 
ATOM   13611 C  CD     . GLU   E 3  19  ? -28.484 -89.741  84.415  1.00 74.18  ? 21  GLU   E CD     1 
ATOM   13612 O  OE1    . GLU   E 3  19  ? -29.400 -90.506  84.044  1.00 71.64  ? 21  GLU   E OE1    1 
ATOM   13613 O  OE2    . GLU   E 3  19  ? -28.688 -88.562  84.800  1.00 80.44  ? 21  GLU   E OE2    1 
ATOM   13614 N  N      . VAL   E 3  20  ? -24.255 -91.065  85.279  1.00 64.19  ? 22  VAL   E N      1 
ATOM   13615 C  CA     . VAL   E 3  20  ? -23.362 -90.844  86.407  1.00 61.30  ? 22  VAL   E CA     1 
ATOM   13616 C  C      . VAL   E 3  20  ? -23.604 -89.424  86.891  1.00 62.16  ? 22  VAL   E C      1 
ATOM   13617 O  O      . VAL   E 3  20  ? -23.286 -88.462  86.185  1.00 65.88  ? 22  VAL   E O      1 
ATOM   13618 C  CB     . VAL   E 3  20  ? -21.883 -91.070  86.047  1.00 54.18  ? 22  VAL   E CB     1 
ATOM   13619 C  CG1    . VAL   E 3  20  ? -21.426 -90.081  85.000  1.00 63.26  ? 22  VAL   E CG1    1 
ATOM   13620 C  CG2    . VAL   E 3  20  ? -21.014 -90.953  87.274  1.00 62.28  ? 22  VAL   E CG2    1 
ATOM   13621 N  N      . ILE   E 3  21  ? -24.175 -89.287  88.082  1.00 63.10  ? 23  ILE   E N      1 
ATOM   13622 C  CA     . ILE   E 3  21  ? -24.436 -87.979  88.660  1.00 65.03  ? 23  ILE   E CA     1 
ATOM   13623 C  C      . ILE   E 3  21  ? -23.264 -87.614  89.563  1.00 65.89  ? 23  ILE   E C      1 
ATOM   13624 O  O      . ILE   E 3  21  ? -22.784 -88.449  90.335  1.00 67.02  ? 23  ILE   E O      1 
ATOM   13625 C  CB     . ILE   E 3  21  ? -25.751 -87.973  89.447  1.00 62.30  ? 23  ILE   E CB     1 
ATOM   13626 C  CG1    . ILE   E 3  21  ? -26.848 -88.657  88.640  1.00 69.15  ? 23  ILE   E CG1    1 
ATOM   13627 C  CG2    . ILE   E 3  21  ? -26.173 -86.540  89.666  1.00 66.78  ? 23  ILE   E CG2    1 
ATOM   13628 C  CD1    . ILE   E 3  21  ? -26.900 -88.237  87.207  1.00 77.57  ? 23  ILE   E CD1    1 
ATOM   13629 N  N      . LEU   E 3  22  ? -22.782 -86.379  89.453  1.00 64.81  ? 24  LEU   E N      1 
ATOM   13630 C  CA     . LEU   E 3  22  ? -21.814 -85.839  90.399  1.00 64.28  ? 24  LEU   E CA     1 
ATOM   13631 C  C      . LEU   E 3  22  ? -22.437 -84.869  91.389  1.00 72.22  ? 24  LEU   E C      1 
ATOM   13632 O  O      . LEU   E 3  22  ? -21.705 -84.298  92.201  1.00 78.43  ? 24  LEU   E O      1 
ATOM   13633 C  CB     . LEU   E 3  22  ? -20.667 -85.118  89.683  1.00 61.08  ? 24  LEU   E CB     1 
ATOM   13634 C  CG     . LEU   E 3  22  ? -20.002 -85.710  88.448  1.00 69.20  ? 24  LEU   E CG     1 
ATOM   13635 C  CD1    . LEU   E 3  22  ? -18.736 -84.917  88.050  1.00 60.01  ? 24  LEU   E CD1    1 
ATOM   13636 C  CD2    . LEU   E 3  22  ? -19.691 -87.165  88.714  1.00 75.37  ? 24  LEU   E CD2    1 
ATOM   13637 N  N      . LYS   E 3  23  ? -23.760 -84.653  91.335  1.00 66.54  ? 25  LYS   E N      1 
ATOM   13638 C  CA     . LYS   E 3  23  ? -24.404 -83.641  92.170  1.00 76.41  ? 25  LYS   E CA     1 
ATOM   13639 C  C      . LYS   E 3  23  ? -25.808 -83.304  91.681  1.00 79.59  ? 25  LYS   E C      1 
ATOM   13640 O  O      . LYS   E 3  23  ? -26.014 -83.095  90.480  1.00 79.52  ? 25  LYS   E O      1 
ATOM   13641 C  CB     . LYS   E 3  23  ? -23.554 -82.368  92.234  1.00 72.12  ? 25  LYS   E CB     1 
ATOM   13642 C  CG     . LYS   E 3  23  ? -24.183 -81.251  93.046  1.00 79.15  ? 25  LYS   E CG     1 
ATOM   13643 C  CD     . LYS   E 3  23  ? -23.447 -79.946  92.840  1.00 84.29  ? 25  LYS   E CD     1 
ATOM   13644 C  CE     . LYS   E 3  23  ? -21.936 -80.204  92.828  1.00 95.06  ? 25  LYS   E CE     1 
ATOM   13645 N  NZ     . LYS   E 3  23  ? -21.102 -79.023  92.461  1.00 87.54  ? 25  LYS   E NZ     1 
ATOM   13646 N  N      . PRO   E 3  24  ? -26.792 -83.236  92.575  1.00 86.98  ? 26  PRO   E N      1 
ATOM   13647 C  CA     . PRO   E 3  24  ? -28.168 -82.930  92.150  1.00 84.24  ? 26  PRO   E CA     1 
ATOM   13648 C  C      . PRO   E 3  24  ? -28.320 -81.451  91.854  1.00 84.99  ? 26  PRO   E C      1 
ATOM   13649 O  O      . PRO   E 3  24  ? -27.386 -80.665  92.084  1.00 83.76  ? 26  PRO   E O      1 
ATOM   13650 C  CB     . PRO   E 3  24  ? -29.022 -83.345  93.360  1.00 84.69  ? 26  PRO   E CB     1 
ATOM   13651 C  CG     . PRO   E 3  24  ? -28.074 -84.093  94.292  1.00 87.99  ? 26  PRO   E CG     1 
ATOM   13652 C  CD     . PRO   E 3  24  ? -26.713 -83.547  94.013  1.00 84.37  ? 26  PRO   E CD     1 
ATOM   13653 N  N      . PRO   E 3  25  ? -29.487 -81.034  91.349  1.00 84.51  ? 27  PRO   E N      1 
ATOM   13654 C  CA     . PRO   E 3  25  ? -29.726 -79.603  91.070  1.00 86.68  ? 27  PRO   E CA     1 
ATOM   13655 C  C      . PRO   E 3  25  ? -29.563 -78.675  92.278  1.00 89.01  ? 27  PRO   E C      1 
ATOM   13656 O  O      . PRO   E 3  25  ? -28.779 -78.969  93.186  1.00 86.73  ? 27  PRO   E O      1 
ATOM   13657 C  CB     . PRO   E 3  25  ? -31.172 -79.589  90.538  1.00 87.12  ? 27  PRO   E CB     1 
ATOM   13658 C  CG     . PRO   E 3  25  ? -31.419 -81.004  90.039  1.00 85.74  ? 27  PRO   E CG     1 
ATOM   13659 C  CD     . PRO   E 3  25  ? -30.628 -81.888  90.967  1.00 86.73  ? 27  PRO   E CD     1 
ATOM   13660 N  N      . SER   E 3  26  ? -30.265 -77.533  92.269  1.00 90.31  ? 28  SER   E N      1 
ATOM   13661 C  CA     . SER   E 3  26  ? -30.326 -76.598  93.407  1.00 85.03  ? 28  SER   E CA     1 
ATOM   13662 C  C      . SER   E 3  26  ? -31.695 -75.913  93.458  1.00 86.17  ? 28  SER   E C      1 
ATOM   13663 O  O      . SER   E 3  26  ? -32.597 -76.228  92.675  1.00 85.20  ? 28  SER   E O      1 
ATOM   13664 C  CB     . SER   E 3  26  ? -29.217 -75.534  93.340  1.00 76.14  ? 28  SER   E CB     1 
ATOM   13665 O  OG     . SER   E 3  26  ? -27.918 -76.104  93.273  1.00 65.99  ? 28  SER   E OG     1 
ATOM   13666 N  N      . ASP   E 3  42  ? -47.684 -74.283  65.438  1.00 102.63 ? 44  ASP   E N      1 
ATOM   13667 C  CA     . ASP   E 3  42  ? -47.044 -74.327  64.120  1.00 100.92 ? 44  ASP   E CA     1 
ATOM   13668 C  C      . ASP   E 3  42  ? -48.023 -73.818  63.050  1.00 100.38 ? 44  ASP   E C      1 
ATOM   13669 O  O      . ASP   E 3  42  ? -49.197 -74.185  63.083  1.00 101.32 ? 44  ASP   E O      1 
ATOM   13670 C  CB     . ASP   E 3  42  ? -46.582 -75.756  63.773  1.00 93.11  ? 44  ASP   E CB     1 
ATOM   13671 C  CG     . ASP   E 3  42  ? -45.406 -76.228  64.622  1.00 91.23  ? 44  ASP   E CG     1 
ATOM   13672 O  OD1    . ASP   E 3  42  ? -44.608 -75.382  65.084  1.00 83.35  ? 44  ASP   E OD1    1 
ATOM   13673 O  OD2    . ASP   E 3  42  ? -45.255 -77.459  64.790  1.00 97.60  ? 44  ASP   E OD2    1 
ATOM   13674 N  N      . PRO   E 3  43  ? -47.558 -72.991  62.104  1.00 95.62  ? 45  PRO   E N      1 
ATOM   13675 C  CA     . PRO   E 3  43  ? -48.474 -72.457  61.079  1.00 93.79  ? 45  PRO   E CA     1 
ATOM   13676 C  C      . PRO   E 3  43  ? -49.100 -73.551  60.211  1.00 90.99  ? 45  PRO   E C      1 
ATOM   13677 O  O      . PRO   E 3  43  ? -48.603 -74.678  60.116  1.00 88.58  ? 45  PRO   E O      1 
ATOM   13678 C  CB     . PRO   E 3  43  ? -47.580 -71.520  60.249  1.00 78.58  ? 45  PRO   E CB     1 
ATOM   13679 C  CG     . PRO   E 3  43  ? -46.433 -71.194  61.132  1.00 79.02  ? 45  PRO   E CG     1 
ATOM   13680 C  CD     . PRO   E 3  43  ? -46.208 -72.408  61.996  1.00 83.40  ? 45  PRO   E CD     1 
ATOM   13681 N  N      . SER   E 3  44  ? -50.217 -73.190  59.564  1.00 83.42  ? 46  SER   E N      1 
ATOM   13682 C  CA     . SER   E 3  44  ? -51.035 -74.089  58.755  1.00 78.17  ? 46  SER   E CA     1 
ATOM   13683 C  C      . SER   E 3  44  ? -50.521 -74.202  57.319  1.00 78.69  ? 46  SER   E C      1 
ATOM   13684 O  O      . SER   E 3  44  ? -49.823 -73.320  56.816  1.00 78.50  ? 46  SER   E O      1 
ATOM   13685 C  CB     . SER   E 3  44  ? -52.476 -73.594  58.713  1.00 83.93  ? 46  SER   E CB     1 
ATOM   13686 O  OG     . SER   E 3  44  ? -53.174 -74.223  57.647  1.00 91.40  ? 46  SER   E OG     1 
ATOM   13687 N  N      . LEU   E 3  45  ? -50.916 -75.285  56.632  1.00 72.14  ? 47  LEU   E N      1 
ATOM   13688 C  CA     . LEU   E 3  45  ? -50.527 -75.409  55.229  1.00 66.70  ? 47  LEU   E CA     1 
ATOM   13689 C  C      . LEU   E 3  45  ? -50.973 -74.189  54.430  1.00 74.90  ? 47  LEU   E C      1 
ATOM   13690 O  O      . LEU   E 3  45  ? -50.213 -73.665  53.607  1.00 77.07  ? 47  LEU   E O      1 
ATOM   13691 C  CB     . LEU   E 3  45  ? -51.079 -76.694  54.606  1.00 62.87  ? 47  LEU   E CB     1 
ATOM   13692 C  CG     . LEU   E 3  45  ? -50.982 -76.751  53.070  1.00 64.46  ? 47  LEU   E CG     1 
ATOM   13693 C  CD1    . LEU   E 3  45  ? -49.623 -76.260  52.586  1.00 72.53  ? 47  LEU   E CD1    1 
ATOM   13694 C  CD2    . LEU   E 3  45  ? -51.185 -78.160  52.524  1.00 53.33  ? 47  LEU   E CD2    1 
ATOM   13695 N  N      . GLU   E 3  46  ? -52.193 -73.706  54.683  1.00 81.37  ? 48  GLU   E N      1 
ATOM   13696 C  CA     . GLU   E 3  46  ? -52.701 -72.518  54.000  1.00 79.20  ? 48  GLU   E CA     1 
ATOM   13697 C  C      . GLU   E 3  46  ? -51.955 -71.260  54.422  1.00 82.00  ? 48  GLU   E C      1 
ATOM   13698 O  O      . GLU   E 3  46  ? -51.674 -70.394  53.585  1.00 86.91  ? 48  GLU   E O      1 
ATOM   13699 C  CB     . GLU   E 3  46  ? -54.186 -72.356  54.283  1.00 91.60  ? 48  GLU   E CB     1 
ATOM   13700 C  CG     . GLU   E 3  46  ? -55.031 -73.470  53.734  1.00 107.41 ? 48  GLU   E CG     1 
ATOM   13701 C  CD     . GLU   E 3  46  ? -56.222 -72.943  52.982  1.00 112.25 ? 48  GLU   E CD     1 
ATOM   13702 O  OE1    . GLU   E 3  46  ? -56.547 -71.750  53.170  1.00 109.04 ? 48  GLU   E OE1    1 
ATOM   13703 O  OE2    . GLU   E 3  46  ? -56.823 -73.715  52.202  1.00 120.31 ? 48  GLU   E OE2    1 
ATOM   13704 N  N      . GLU   E 3  47  ? -51.661 -71.120  55.720  1.00 78.27  ? 49  GLU   E N      1 
ATOM   13705 C  CA     . GLU   E 3  47  ? -50.833 -70.008  56.179  1.00 77.40  ? 49  GLU   E CA     1 
ATOM   13706 C  C      . GLU   E 3  47  ? -49.506 -69.961  55.429  1.00 80.05  ? 49  GLU   E C      1 
ATOM   13707 O  O      . GLU   E 3  47  ? -48.977 -68.873  55.159  1.00 77.87  ? 49  GLU   E O      1 
ATOM   13708 C  CB     . GLU   E 3  47  ? -50.592 -70.125  57.681  1.00 76.72  ? 49  GLU   E CB     1 
ATOM   13709 C  CG     . GLU   E 3  47  ? -51.841 -70.037  58.525  1.00 83.49  ? 49  GLU   E CG     1 
ATOM   13710 C  CD     . GLU   E 3  47  ? -51.525 -69.723  59.973  1.00 87.98  ? 49  GLU   E CD     1 
ATOM   13711 O  OE1    . GLU   E 3  47  ? -51.070 -68.591  60.257  1.00 83.87  ? 49  GLU   E OE1    1 
ATOM   13712 O  OE2    . GLU   E 3  47  ? -51.739 -70.611  60.827  1.00 90.90  ? 49  GLU   E OE2    1 
ATOM   13713 N  N      . ILE   E 3  48  ? -48.942 -71.140  55.118  1.00 74.32  ? 50  ILE   E N      1 
ATOM   13714 C  CA     . ILE   E 3  48  ? -47.785 -71.252  54.231  1.00 72.16  ? 50  ILE   E CA     1 
ATOM   13715 C  C      . ILE   E 3  48  ? -48.151 -70.836  52.814  1.00 77.80  ? 50  ILE   E C      1 
ATOM   13716 O  O      . ILE   E 3  48  ? -47.479 -69.999  52.194  1.00 70.82  ? 50  ILE   E O      1 
ATOM   13717 C  CB     . ILE   E 3  48  ? -47.237 -72.691  54.270  1.00 67.47  ? 50  ILE   E CB     1 
ATOM   13718 C  CG1    . ILE   E 3  48  ? -46.802 -73.032  55.689  1.00 63.29  ? 50  ILE   E CG1    1 
ATOM   13719 C  CG2    . ILE   E 3  48  ? -46.172 -72.937  53.215  1.00 67.84  ? 50  ILE   E CG2    1 
ATOM   13720 C  CD1    . ILE   E 3  48  ? -46.033 -71.908  56.348  1.00 61.93  ? 50  ILE   E CD1    1 
ATOM   13721 N  N      . GLN   E 3  49  ? -49.219 -71.426  52.279  1.00 80.17  ? 51  GLN   E N      1 
ATOM   13722 C  CA     . GLN   E 3  49  ? -49.655 -71.099  50.933  1.00 76.96  ? 51  GLN   E CA     1 
ATOM   13723 C  C      . GLN   E 3  49  ? -49.799 -69.596  50.750  1.00 76.29  ? 51  GLN   E C      1 
ATOM   13724 O  O      . GLN   E 3  49  ? -49.356 -69.040  49.737  1.00 70.81  ? 51  GLN   E O      1 
ATOM   13725 C  CB     . GLN   E 3  49  ? -50.971 -71.803  50.650  1.00 75.69  ? 51  GLN   E CB     1 
ATOM   13726 C  CG     . GLN   E 3  49  ? -50.731 -73.202  50.269  1.00 78.19  ? 51  GLN   E CG     1 
ATOM   13727 C  CD     . GLN   E 3  49  ? -49.578 -73.267  49.339  1.00 85.15  ? 51  GLN   E CD     1 
ATOM   13728 O  OE1    . GLN   E 3  49  ? -49.416 -72.390  48.489  1.00 88.40  ? 51  GLN   E OE1    1 
ATOM   13729 N  NE2    . GLN   E 3  49  ? -48.740 -74.289  49.496  1.00 88.79  ? 51  GLN   E NE2    1 
ATOM   13730 N  N      . LYS   E 3  50  ? -50.419 -68.919  51.720  1.00 74.00  ? 52  LYS   E N      1 
ATOM   13731 C  CA     . LYS   E 3  50  ? -50.564 -67.472  51.627  1.00 81.67  ? 52  LYS   E CA     1 
ATOM   13732 C  C      . LYS   E 3  50  ? -49.195 -66.838  51.425  1.00 77.49  ? 52  LYS   E C      1 
ATOM   13733 O  O      . LYS   E 3  50  ? -48.882 -66.382  50.321  1.00 77.04  ? 52  LYS   E O      1 
ATOM   13734 C  CB     . LYS   E 3  50  ? -51.233 -66.867  52.873  1.00 85.64  ? 52  LYS   E CB     1 
ATOM   13735 C  CG     . LYS   E 3  50  ? -51.379 -65.327  52.753  1.00 90.05  ? 52  LYS   E CG     1 
ATOM   13736 C  CD     . LYS   E 3  50  ? -52.160 -64.623  53.873  1.00 86.87  ? 52  LYS   E CD     1 
ATOM   13737 C  CE     . LYS   E 3  50  ? -51.470 -64.744  55.224  1.00 90.86  ? 52  LYS   E CE     1 
ATOM   13738 N  NZ     . LYS   E 3  50  ? -52.268 -64.111  56.320  1.00 82.90  ? 52  LYS   E NZ     1 
ATOM   13739 N  N      . LYS   E 3  51  ? -48.377 -66.830  52.486  1.00 79.09  ? 53  LYS   E N      1 
ATOM   13740 C  CA     . LYS   E 3  51  ? -47.066 -66.181  52.458  1.00 75.71  ? 53  LYS   E CA     1 
ATOM   13741 C  C      . LYS   E 3  51  ? -46.235 -66.576  51.232  1.00 69.26  ? 53  LYS   E C      1 
ATOM   13742 O  O      . LYS   E 3  51  ? -45.636 -65.713  50.585  1.00 56.14  ? 53  LYS   E O      1 
ATOM   13743 C  CB     . LYS   E 3  51  ? -46.316 -66.498  53.748  1.00 72.46  ? 53  LYS   E CB     1 
ATOM   13744 C  CG     . LYS   E 3  51  ? -47.042 -66.031  55.021  1.00 79.09  ? 53  LYS   E CG     1 
ATOM   13745 C  CD     . LYS   E 3  51  ? -46.108 -65.179  55.886  1.00 77.07  ? 53  LYS   E CD     1 
ATOM   13746 C  CE     . LYS   E 3  51  ? -45.925 -65.742  57.291  1.00 80.46  ? 53  LYS   E CE     1 
ATOM   13747 N  NZ     . LYS   E 3  51  ? -45.014 -64.875  58.111  1.00 83.37  ? 53  LYS   E NZ     1 
ATOM   13748 N  N      . LEU   E 3  52  ? -46.170 -67.873  50.900  1.00 68.05  ? 54  LEU   E N      1 
ATOM   13749 C  CA     . LEU   E 3  52  ? -45.533 -68.261  49.640  1.00 67.10  ? 54  LEU   E CA     1 
ATOM   13750 C  C      . LEU   E 3  52  ? -46.101 -67.493  48.454  1.00 69.04  ? 54  LEU   E C      1 
ATOM   13751 O  O      . LEU   E 3  52  ? -45.355 -67.026  47.587  1.00 69.03  ? 54  LEU   E O      1 
ATOM   13752 C  CB     . LEU   E 3  52  ? -45.673 -69.761  49.366  1.00 71.07  ? 54  LEU   E CB     1 
ATOM   13753 C  CG     . LEU   E 3  52  ? -44.582 -70.711  49.856  1.00 71.07  ? 54  LEU   E CG     1 
ATOM   13754 C  CD1    . LEU   E 3  52  ? -44.741 -72.110  49.249  1.00 68.54  ? 54  LEU   E CD1    1 
ATOM   13755 C  CD2    . LEU   E 3  52  ? -43.213 -70.151  49.556  1.00 65.69  ? 54  LEU   E CD2    1 
ATOM   13756 N  N      . GLU   E 3  53  ? -47.428 -67.402  48.363  1.00 74.13  ? 55  GLU   E N      1 
ATOM   13757 C  CA     . GLU   E 3  53  ? -48.022 -66.794  47.178  1.00 73.15  ? 55  GLU   E CA     1 
ATOM   13758 C  C      . GLU   E 3  53  ? -47.913 -65.276  47.201  1.00 64.84  ? 55  GLU   E C      1 
ATOM   13759 O  O      . GLU   E 3  53  ? -47.813 -64.653  46.140  1.00 62.82  ? 55  GLU   E O      1 
ATOM   13760 C  CB     . GLU   E 3  53  ? -49.475 -67.242  47.029  1.00 73.20  ? 55  GLU   E CB     1 
ATOM   13761 C  CG     . GLU   E 3  53  ? -49.581 -68.690  46.567  1.00 80.14  ? 55  GLU   E CG     1 
ATOM   13762 C  CD     . GLU   E 3  53  ? -51.004 -69.138  46.284  1.00 86.96  ? 55  GLU   E CD     1 
ATOM   13763 O  OE1    . GLU   E 3  53  ? -51.962 -68.486  46.782  1.00 84.38  ? 55  GLU   E OE1    1 
ATOM   13764 O  OE2    . GLU   E 3  53  ? -51.151 -70.143  45.542  1.00 76.14  ? 55  GLU   E OE2    1 
ATOM   13765 N  N      . ALA   E 3  54  ? -47.913 -64.666  48.387  1.00 59.54  ? 56  ALA   E N      1 
ATOM   13766 C  CA     . ALA   E 3  54  ? -47.706 -63.226  48.472  1.00 59.87  ? 56  ALA   E CA     1 
ATOM   13767 C  C      . ALA   E 3  54  ? -46.358 -62.821  47.899  1.00 62.57  ? 56  ALA   E C      1 
ATOM   13768 O  O      . ALA   E 3  54  ? -46.206 -61.716  47.378  1.00 65.28  ? 56  ALA   E O      1 
ATOM   13769 C  CB     . ALA   E 3  54  ? -47.817 -62.764  49.918  1.00 51.52  ? 56  ALA   E CB     1 
ATOM   13770 N  N      . ALA   E 3  55  ? -45.364 -63.680  48.001  1.00 59.81  ? 57  ALA   E N      1 
ATOM   13771 C  CA     . ALA   E 3  55  ? -44.079 -63.336  47.435  1.00 54.88  ? 57  ALA   E CA     1 
ATOM   13772 C  C      . ALA   E 3  55  ? -43.997 -63.709  45.961  1.00 63.36  ? 57  ALA   E C      1 
ATOM   13773 O  O      . ALA   E 3  55  ? -43.092 -63.240  45.265  1.00 60.29  ? 57  ALA   E O      1 
ATOM   13774 C  CB     . ALA   E 3  55  ? -42.964 -64.010  48.235  1.00 47.80  ? 57  ALA   E CB     1 
ATOM   13775 N  N      . GLU   E 3  56  ? -44.909 -64.543  45.462  1.00 63.99  ? 58  GLU   E N      1 
ATOM   13776 C  CA     . GLU   E 3  56  ? -44.985 -64.699  44.017  1.00 60.86  ? 58  GLU   E CA     1 
ATOM   13777 C  C      . GLU   E 3  56  ? -45.664 -63.501  43.389  1.00 65.02  ? 58  GLU   E C      1 
ATOM   13778 O  O      . GLU   E 3  56  ? -45.283 -63.064  42.302  1.00 67.56  ? 58  GLU   E O      1 
ATOM   13779 C  CB     . GLU   E 3  56  ? -45.720 -65.970  43.623  1.00 55.95  ? 58  GLU   E CB     1 
ATOM   13780 C  CG     . GLU   E 3  56  ? -45.563 -66.238  42.148  1.00 58.13  ? 58  GLU   E CG     1 
ATOM   13781 C  CD     . GLU   E 3  56  ? -46.370 -67.420  41.679  1.00 78.15  ? 58  GLU   E CD     1 
ATOM   13782 O  OE1    . GLU   E 3  56  ? -47.415 -67.686  42.311  1.00 91.67  ? 58  GLU   E OE1    1 
ATOM   13783 O  OE2    . GLU   E 3  56  ? -45.980 -68.060  40.669  1.00 73.42  ? 58  GLU   E OE2    1 
ATOM   13784 N  N      . GLU   E 3  57  ? -46.678 -62.958  44.049  1.00 69.31  ? 59  GLU   E N      1 
ATOM   13785 C  CA     . GLU   E 3  57  ? -47.253 -61.718  43.562  1.00 67.95  ? 59  GLU   E CA     1 
ATOM   13786 C  C      . GLU   E 3  57  ? -46.183 -60.646  43.506  1.00 65.76  ? 59  GLU   E C      1 
ATOM   13787 O  O      . GLU   E 3  57  ? -45.811 -60.174  42.427  1.00 66.26  ? 59  GLU   E O      1 
ATOM   13788 C  CB     . GLU   E 3  57  ? -48.417 -61.275  44.452  1.00 78.93  ? 59  GLU   E CB     1 
ATOM   13789 C  CG     . GLU   E 3  57  ? -49.732 -61.993  44.165  1.00 95.49  ? 59  GLU   E CG     1 
ATOM   13790 C  CD     . GLU   E 3  57  ? -50.062 -62.026  42.677  1.00 109.86 ? 59  GLU   E CD     1 
ATOM   13791 O  OE1    . GLU   E 3  57  ? -49.444 -61.246  41.914  1.00 112.08 ? 59  GLU   E OE1    1 
ATOM   13792 O  OE2    . GLU   E 3  57  ? -50.946 -62.818  42.269  1.00 123.78 ? 59  GLU   E OE2    1 
ATOM   13793 N  N      . ARG   E 3  58  ? -45.640 -60.277  44.666  1.00 67.08  ? 60  ARG   E N      1 
ATOM   13794 C  CA     . ARG   E 3  58  ? -44.640 -59.222  44.739  1.00 59.93  ? 60  ARG   E CA     1 
ATOM   13795 C  C      . ARG   E 3  58  ? -43.591 -59.382  43.642  1.00 59.63  ? 60  ARG   E C      1 
ATOM   13796 O  O      . ARG   E 3  58  ? -43.042 -58.391  43.158  1.00 64.05  ? 60  ARG   E O      1 
ATOM   13797 C  CB     . ARG   E 3  58  ? -43.992 -59.194  46.126  1.00 55.25  ? 60  ARG   E CB     1 
ATOM   13798 C  CG     . ARG   E 3  58  ? -44.850 -58.560  47.227  1.00 54.38  ? 60  ARG   E CG     1 
ATOM   13799 C  CD     . ARG   E 3  58  ? -44.023 -58.280  48.497  1.00 61.14  ? 60  ARG   E CD     1 
ATOM   13800 N  NE     . ARG   E 3  58  ? -43.555 -59.498  49.149  1.00 59.01  ? 60  ARG   E NE     1 
ATOM   13801 C  CZ     . ARG   E 3  58  ? -44.330 -60.337  49.818  1.00 58.14  ? 60  ARG   E CZ     1 
ATOM   13802 N  NH1    . ARG   E 3  58  ? -45.604 -60.072  50.041  1.00 69.13  ? 60  ARG   E NH1    1 
ATOM   13803 N  NH2    . ARG   E 3  58  ? -43.820 -61.482  50.257  1.00 53.65  ? 60  ARG   E NH2    1 
ATOM   13804 N  N      . ARG   E 3  59  ? -43.324 -60.616  43.214  1.00 58.57  ? 61  ARG   E N      1 
ATOM   13805 C  CA     . ARG   E 3  59  ? -42.422 -60.817  42.085  1.00 51.04  ? 61  ARG   E CA     1 
ATOM   13806 C  C      . ARG   E 3  59  ? -43.078 -60.453  40.771  1.00 55.99  ? 61  ARG   E C      1 
ATOM   13807 O  O      . ARG   E 3  59  ? -42.461 -59.775  39.948  1.00 64.03  ? 61  ARG   E O      1 
ATOM   13808 C  CB     . ARG   E 3  59  ? -41.960 -62.265  41.999  1.00 49.37  ? 61  ARG   E CB     1 
ATOM   13809 C  CG     . ARG   E 3  59  ? -40.648 -62.555  42.660  1.00 42.85  ? 61  ARG   E CG     1 
ATOM   13810 C  CD     . ARG   E 3  59  ? -40.115 -63.846  42.082  1.00 50.02  ? 61  ARG   E CD     1 
ATOM   13811 N  NE     . ARG   E 3  59  ? -41.139 -64.890  42.008  1.00 60.96  ? 61  ARG   E NE     1 
ATOM   13812 C  CZ     . ARG   E 3  59  ? -41.516 -65.669  43.023  1.00 61.79  ? 61  ARG   E CZ     1 
ATOM   13813 N  NH1    . ARG   E 3  59  ? -41.035 -65.508  44.246  1.00 53.88  ? 61  ARG   E NH1    1 
ATOM   13814 N  NH2    . ARG   E 3  59  ? -42.431 -66.609  42.814  1.00 62.56  ? 61  ARG   E NH2    1 
ATOM   13815 N  N      . LYS   E 3  60  ? -44.309 -60.927  40.542  1.00 64.08  ? 62  LYS   E N      1 
ATOM   13816 C  CA     . LYS   E 3  60  ? -44.994 -60.650  39.280  1.00 62.74  ? 62  LYS   E CA     1 
ATOM   13817 C  C      . LYS   E 3  60  ? -45.318 -59.161  39.130  1.00 61.56  ? 62  LYS   E C      1 
ATOM   13818 O  O      . LYS   E 3  60  ? -45.342 -58.645  38.003  1.00 59.06  ? 62  LYS   E O      1 
ATOM   13819 C  CB     . LYS   E 3  60  ? -46.269 -61.502  39.151  1.00 57.70  ? 62  LYS   E CB     1 
ATOM   13820 C  CG     . LYS   E 3  60  ? -47.019 -61.244  37.834  1.00 80.94  ? 62  LYS   E CG     1 
ATOM   13821 C  CD     . LYS   E 3  60  ? -48.532 -61.509  37.896  1.00 96.95  ? 62  LYS   E CD     1 
ATOM   13822 C  CE     . LYS   E 3  60  ? -49.190 -61.286  36.516  1.00 89.52  ? 62  LYS   E CE     1 
ATOM   13823 N  NZ     . LYS   E 3  60  ? -50.645 -61.638  36.444  1.00 89.00  ? 62  LYS   E NZ     1 
ATOM   13824 N  N      . TYR   E 3  61  ? -45.546 -58.448  40.239  1.00 56.51  ? 63  TYR   E N      1 
ATOM   13825 C  CA     . TYR   E 3  61  ? -45.752 -57.009  40.139  1.00 55.17  ? 63  TYR   E CA     1 
ATOM   13826 C  C      . TYR   E 3  61  ? -44.474 -56.337  39.667  1.00 56.71  ? 63  TYR   E C      1 
ATOM   13827 O  O      . TYR   E 3  61  ? -44.454 -55.655  38.635  1.00 56.85  ? 63  TYR   E O      1 
ATOM   13828 C  CB     . TYR   E 3  61  ? -46.193 -56.445  41.491  1.00 52.29  ? 63  TYR   E CB     1 
ATOM   13829 C  CG     . TYR   E 3  61  ? -46.251 -54.928  41.594  1.00 56.52  ? 63  TYR   E CG     1 
ATOM   13830 C  CD1    . TYR   E 3  61  ? -47.301 -54.216  41.028  1.00 60.08  ? 63  TYR   E CD1    1 
ATOM   13831 C  CD2    . TYR   E 3  61  ? -45.269 -54.207  42.260  1.00 60.83  ? 63  TYR   E CD2    1 
ATOM   13832 C  CE1    . TYR   E 3  61  ? -47.375 -52.817  41.132  1.00 65.91  ? 63  TYR   E CE1    1 
ATOM   13833 C  CE2    . TYR   E 3  61  ? -45.334 -52.813  42.365  1.00 66.94  ? 63  TYR   E CE2    1 
ATOM   13834 C  CZ     . TYR   E 3  61  ? -46.388 -52.125  41.796  1.00 67.76  ? 63  TYR   E CZ     1 
ATOM   13835 O  OH     . TYR   E 3  61  ? -46.451 -50.750  41.889  1.00 71.41  ? 63  TYR   E OH     1 
ATOM   13836 N  N      . GLN   E 3  62  ? -43.383 -56.565  40.400  1.00 57.50  ? 64  GLN   E N      1 
ATOM   13837 C  CA     . GLN   E 3  62  ? -42.098 -55.967  40.062  1.00 56.79  ? 64  GLN   E CA     1 
ATOM   13838 C  C      . GLN   E 3  62  ? -41.708 -56.247  38.618  1.00 57.50  ? 64  GLN   E C      1 
ATOM   13839 O  O      . GLN   E 3  62  ? -41.125 -55.388  37.943  1.00 56.55  ? 64  GLN   E O      1 
ATOM   13840 C  CB     . GLN   E 3  62  ? -41.024 -56.486  41.007  1.00 51.37  ? 64  GLN   E CB     1 
ATOM   13841 C  CG     . GLN   E 3  62  ? -41.283 -56.207  42.450  1.00 58.40  ? 64  GLN   E CG     1 
ATOM   13842 C  CD     . GLN   E 3  62  ? -40.376 -57.011  43.350  1.00 64.69  ? 64  GLN   E CD     1 
ATOM   13843 O  OE1    . GLN   E 3  62  ? -39.541 -57.795  42.874  1.00 57.94  ? 64  GLN   E OE1    1 
ATOM   13844 N  NE2    . GLN   E 3  62  ? -40.527 -56.821  44.665  1.00 67.95  ? 64  GLN   E NE2    1 
ATOM   13845 N  N      . GLU   E 3  63  ? -41.994 -57.450  38.131  1.00 49.03  ? 65  GLU   E N      1 
ATOM   13846 C  CA     . GLU   E 3  63  ? -41.703 -57.738  36.739  1.00 51.31  ? 65  GLU   E CA     1 
ATOM   13847 C  C      . GLU   E 3  63  ? -42.591 -56.918  35.818  1.00 61.52  ? 65  GLU   E C      1 
ATOM   13848 O  O      . GLU   E 3  63  ? -42.137 -56.445  34.766  1.00 59.49  ? 65  GLU   E O      1 
ATOM   13849 C  CB     . GLU   E 3  63  ? -41.864 -59.223  36.472  1.00 47.77  ? 65  GLU   E CB     1 
ATOM   13850 C  CG     . GLU   E 3  63  ? -41.397 -59.654  35.115  1.00 48.47  ? 65  GLU   E CG     1 
ATOM   13851 C  CD     . GLU   E 3  63  ? -41.777 -61.080  34.829  1.00 59.91  ? 65  GLU   E CD     1 
ATOM   13852 O  OE1    . GLU   E 3  63  ? -42.765 -61.552  35.417  1.00 68.27  ? 65  GLU   E OE1    1 
ATOM   13853 O  OE2    . GLU   E 3  63  ? -41.065 -61.749  34.053  1.00 63.85  ? 65  GLU   E OE2    1 
ATOM   13854 N  N      . ALA   E 3  64  ? -43.859 -56.737  36.201  1.00 64.40  ? 66  ALA   E N      1 
ATOM   13855 C  CA     . ALA   E 3  64  ? -44.750 -55.912  35.399  1.00 59.52  ? 66  ALA   E CA     1 
ATOM   13856 C  C      . ALA   E 3  64  ? -44.252 -54.471  35.357  1.00 58.76  ? 66  ALA   E C      1 
ATOM   13857 O  O      . ALA   E 3  64  ? -44.189 -53.864  34.281  1.00 58.06  ? 66  ALA   E O      1 
ATOM   13858 C  CB     . ALA   E 3  64  ? -46.178 -56.000  35.933  1.00 56.11  ? 66  ALA   E CB     1 
ATOM   13859 N  N      . GLU   E 3  65  ? -43.849 -53.915  36.502  1.00 56.85  ? 67  GLU   E N      1 
ATOM   13860 C  CA     . GLU   E 3  65  ? -43.283 -52.567  36.470  1.00 60.94  ? 67  GLU   E CA     1 
ATOM   13861 C  C      . GLU   E 3  65  ? -42.059 -52.488  35.570  1.00 57.66  ? 67  GLU   E C      1 
ATOM   13862 O  O      . GLU   E 3  65  ? -41.790 -51.438  34.984  1.00 54.13  ? 67  GLU   E O      1 
ATOM   13863 C  CB     . GLU   E 3  65  ? -42.943 -52.096  37.875  1.00 55.58  ? 67  GLU   E CB     1 
ATOM   13864 C  CG     . GLU   E 3  65  ? -44.176 -52.059  38.685  1.00 61.70  ? 67  GLU   E CG     1 
ATOM   13865 C  CD     . GLU   E 3  65  ? -45.169 -51.139  38.043  1.00 70.22  ? 67  GLU   E CD     1 
ATOM   13866 O  OE1    . GLU   E 3  65  ? -44.862 -49.936  37.951  1.00 78.70  ? 67  GLU   E OE1    1 
ATOM   13867 O  OE2    . GLU   E 3  65  ? -46.229 -51.621  37.581  1.00 70.04  ? 67  GLU   E OE2    1 
ATOM   13868 N  N      . LEU   E 3  66  ? -41.307 -53.578  35.448  1.00 54.99  ? 68  LEU   E N      1 
ATOM   13869 C  CA     . LEU   E 3  66  ? -40.191 -53.598  34.515  1.00 54.24  ? 68  LEU   E CA     1 
ATOM   13870 C  C      . LEU   E 3  66  ? -40.691 -53.600  33.078  1.00 55.04  ? 68  LEU   E C      1 
ATOM   13871 O  O      . LEU   E 3  66  ? -40.257 -52.791  32.249  1.00 52.42  ? 68  LEU   E O      1 
ATOM   13872 C  CB     . LEU   E 3  66  ? -39.315 -54.822  34.778  1.00 53.69  ? 68  LEU   E CB     1 
ATOM   13873 C  CG     . LEU   E 3  66  ? -38.308 -55.174  33.673  1.00 55.51  ? 68  LEU   E CG     1 
ATOM   13874 C  CD1    . LEU   E 3  66  ? -37.352 -54.029  33.322  1.00 52.22  ? 68  LEU   E CD1    1 
ATOM   13875 C  CD2    . LEU   E 3  66  ? -37.540 -56.432  34.013  1.00 53.71  ? 68  LEU   E CD2    1 
ATOM   13876 N  N      . LEU   E 3  67  ? -41.601 -54.515  32.771  1.00 56.59  ? 69  LEU   E N      1 
ATOM   13877 C  CA     . LEU   E 3  67  ? -42.092 -54.673  31.413  1.00 51.42  ? 69  LEU   E CA     1 
ATOM   13878 C  C      . LEU   E 3  67  ? -42.881 -53.448  30.966  1.00 53.64  ? 69  LEU   E C      1 
ATOM   13879 O  O      . LEU   E 3  67  ? -42.919 -53.140  29.769  1.00 50.73  ? 69  LEU   E O      1 
ATOM   13880 C  CB     . LEU   E 3  67  ? -42.924 -55.947  31.361  1.00 46.02  ? 69  LEU   E CB     1 
ATOM   13881 C  CG     . LEU   E 3  67  ? -41.903 -57.077  31.462  1.00 50.89  ? 69  LEU   E CG     1 
ATOM   13882 C  CD1    . LEU   E 3  67  ? -42.547 -58.423  31.364  1.00 59.58  ? 69  LEU   E CD1    1 
ATOM   13883 C  CD2    . LEU   E 3  67  ? -40.835 -56.920  30.370  1.00 50.29  ? 69  LEU   E CD2    1 
ATOM   13884 N  N      . LYS   E 3  68  ? -43.491 -52.731  31.918  1.00 53.71  ? 70  LYS   E N      1 
ATOM   13885 C  CA     . LYS   E 3  68  ? -44.170 -51.473  31.619  1.00 51.96  ? 70  LYS   E CA     1 
ATOM   13886 C  C      . LYS   E 3  68  ? -43.164 -50.388  31.261  1.00 53.85  ? 70  LYS   E C      1 
ATOM   13887 O  O      . LYS   E 3  68  ? -43.272 -49.747  30.212  1.00 53.60  ? 70  LYS   E O      1 
ATOM   13888 C  CB     . LYS   E 3  68  ? -45.024 -51.055  32.824  1.00 59.83  ? 70  LYS   E CB     1 
ATOM   13889 C  CG     . LYS   E 3  68  ? -45.405 -49.572  32.887  1.00 69.74  ? 70  LYS   E CG     1 
ATOM   13890 C  CD     . LYS   E 3  68  ? -46.660 -49.317  33.734  1.00 79.31  ? 70  LYS   E CD     1 
ATOM   13891 C  CE     . LYS   E 3  68  ? -47.945 -49.481  32.934  1.00 95.47  ? 70  LYS   E CE     1 
ATOM   13892 N  NZ     . LYS   E 3  68  ? -49.129 -48.937  33.659  1.00 101.75 ? 70  LYS   E NZ     1 
ATOM   13893 N  N      . HIS   E 3  69  ? -42.169 -50.185  32.124  1.00 55.97  ? 71  HIS   E N      1 
ATOM   13894 C  CA     . HIS   E 3  69  ? -41.111 -49.211  31.877  1.00 54.00  ? 71  HIS   E CA     1 
ATOM   13895 C  C      . HIS   E 3  69  ? -40.372 -49.506  30.563  1.00 56.72  ? 71  HIS   E C      1 
ATOM   13896 O  O      . HIS   E 3  69  ? -40.122 -48.595  29.759  1.00 53.60  ? 71  HIS   E O      1 
ATOM   13897 C  CB     . HIS   E 3  69  ? -40.169 -49.228  33.076  1.00 51.17  ? 71  HIS   E CB     1 
ATOM   13898 C  CG     . HIS   E 3  69  ? -38.968 -48.361  32.934  1.00 56.74  ? 71  HIS   E CG     1 
ATOM   13899 N  ND1    . HIS   E 3  69  ? -37.785 -48.816  32.390  1.00 57.12  ? 71  HIS   E ND1    1 
ATOM   13900 C  CD2    . HIS   E 3  69  ? -38.731 -47.093  33.345  1.00 61.32  ? 71  HIS   E CD2    1 
ATOM   13901 C  CE1    . HIS   E 3  69  ? -36.882 -47.851  32.431  1.00 61.59  ? 71  HIS   E CE1    1 
ATOM   13902 N  NE2    . HIS   E 3  69  ? -37.431 -46.795  33.008  1.00 69.10  ? 71  HIS   E NE2    1 
ATOM   13903 N  N      . LEU   E 3  70  ? -40.024 -50.771  30.310  1.00 49.56  ? 72  LEU   E N      1 
ATOM   13904 C  CA     . LEU   E 3  70  ? -39.472 -51.087  28.999  1.00 46.63  ? 72  LEU   E CA     1 
ATOM   13905 C  C      . LEU   E 3  70  ? -40.437 -50.708  27.885  1.00 50.62  ? 72  LEU   E C      1 
ATOM   13906 O  O      . LEU   E 3  70  ? -40.011 -50.290  26.803  1.00 53.57  ? 72  LEU   E O      1 
ATOM   13907 C  CB     . LEU   E 3  70  ? -39.101 -52.566  28.881  1.00 46.79  ? 72  LEU   E CB     1 
ATOM   13908 C  CG     . LEU   E 3  70  ? -37.879 -53.072  29.643  1.00 47.48  ? 72  LEU   E CG     1 
ATOM   13909 C  CD1    . LEU   E 3  70  ? -37.589 -54.503  29.242  1.00 50.46  ? 72  LEU   E CD1    1 
ATOM   13910 C  CD2    . LEU   E 3  70  ? -36.674 -52.195  29.421  1.00 43.13  ? 72  LEU   E CD2    1 
ATOM   13911 N  N      . ALA   E 3  71  ? -41.740 -50.872  28.109  1.00 50.91  ? 73  ALA   E N      1 
ATOM   13912 C  CA     . ALA   E 3  71  ? -42.697 -50.521  27.062  1.00 47.46  ? 73  ALA   E CA     1 
ATOM   13913 C  C      . ALA   E 3  71  ? -42.626 -49.034  26.729  1.00 50.73  ? 73  ALA   E C      1 
ATOM   13914 O  O      . ALA   E 3  71  ? -42.643 -48.654  25.555  1.00 46.71  ? 73  ALA   E O      1 
ATOM   13915 C  CB     . ALA   E 3  71  ? -44.104 -50.909  27.489  1.00 42.17  ? 73  ALA   E CB     1 
ATOM   13916 N  N      . GLU   E 3  72  ? -42.558 -48.178  27.757  1.00 52.82  ? 74  GLU   E N      1 
ATOM   13917 C  CA     . GLU   E 3  72  ? -42.329 -46.753  27.545  1.00 48.44  ? 74  GLU   E CA     1 
ATOM   13918 C  C      . GLU   E 3  72  ? -41.103 -46.513  26.675  1.00 50.49  ? 74  GLU   E C      1 
ATOM   13919 O  O      . GLU   E 3  72  ? -41.103 -45.619  25.820  1.00 50.12  ? 74  GLU   E O      1 
ATOM   13920 C  CB     . GLU   E 3  72  ? -42.157 -46.044  28.889  1.00 51.89  ? 74  GLU   E CB     1 
ATOM   13921 C  CG     . GLU   E 3  72  ? -43.308 -46.179  29.846  1.00 53.96  ? 74  GLU   E CG     1 
ATOM   13922 C  CD     . GLU   E 3  72  ? -43.171 -45.253  31.052  1.00 79.06  ? 74  GLU   E CD     1 
ATOM   13923 O  OE1    . GLU   E 3  72  ? -42.562 -45.660  32.080  1.00 79.55  ? 74  GLU   E OE1    1 
ATOM   13924 O  OE2    . GLU   E 3  72  ? -43.651 -44.102  30.964  1.00 89.92  ? 74  GLU   E OE2    1 
ATOM   13925 N  N      . LYS   E 3  73  ? -40.035 -47.283  26.888  1.00 50.07  ? 75  LYS   E N      1 
ATOM   13926 C  CA     . LYS   E 3  73  ? -38.846 -47.072  26.072  1.00 52.22  ? 75  LYS   E CA     1 
ATOM   13927 C  C      . LYS   E 3  73  ? -39.156 -47.302  24.590  1.00 50.74  ? 75  LYS   E C      1 
ATOM   13928 O  O      . LYS   E 3  73  ? -38.687 -46.542  23.739  1.00 50.40  ? 75  LYS   E O      1 
ATOM   13929 C  CB     . LYS   E 3  73  ? -37.684 -47.956  26.562  1.00 55.87  ? 75  LYS   E CB     1 
ATOM   13930 C  CG     . LYS   E 3  73  ? -36.559 -48.163  25.504  1.00 63.77  ? 75  LYS   E CG     1 
ATOM   13931 C  CD     . LYS   E 3  73  ? -35.115 -48.026  26.045  1.00 62.46  ? 75  LYS   E CD     1 
ATOM   13932 C  CE     . LYS   E 3  73  ? -34.094 -47.813  24.896  1.00 46.52  ? 75  LYS   E CE     1 
ATOM   13933 N  NZ     . LYS   E 3  73  ? -34.305 -46.531  24.128  1.00 39.67  ? 75  LYS   E NZ     1 
ATOM   13934 N  N      . ARG   E 3  74  ? -39.969 -48.319  24.259  1.00 48.40  ? 76  ARG   E N      1 
ATOM   13935 C  CA     . ARG   E 3  74  ? -40.286 -48.568  22.852  1.00 45.27  ? 76  ARG   E CA     1 
ATOM   13936 C  C      . ARG   E 3  74  ? -41.138 -47.444  22.276  1.00 48.76  ? 76  ARG   E C      1 
ATOM   13937 O  O      . ARG   E 3  74  ? -40.996 -47.069  21.106  1.00 51.63  ? 76  ARG   E O      1 
ATOM   13938 C  CB     . ARG   E 3  74  ? -41.022 -49.897  22.679  1.00 40.69  ? 76  ARG   E CB     1 
ATOM   13939 C  CG     . ARG   E 3  74  ? -40.502 -51.092  23.466  1.00 54.83  ? 76  ARG   E CG     1 
ATOM   13940 C  CD     . ARG   E 3  74  ? -39.419 -51.831  22.721  1.00 58.26  ? 76  ARG   E CD     1 
ATOM   13941 N  NE     . ARG   E 3  74  ? -38.063 -51.385  23.051  1.00 60.68  ? 76  ARG   E NE     1 
ATOM   13942 C  CZ     . ARG   E 3  74  ? -37.238 -52.040  23.858  1.00 55.86  ? 76  ARG   E CZ     1 
ATOM   13943 N  NH1    . ARG   E 3  74  ? -37.567 -53.208  24.384  1.00 56.95  ? 76  ARG   E NH1    1 
ATOM   13944 N  NH2    . ARG   E 3  74  ? -36.045 -51.522  24.124  1.00 56.16  ? 76  ARG   E NH2    1 
ATOM   13945 N  N      . GLU   E 3  75  ? -42.055 -46.919  23.072  1.00 53.32  ? 77  GLU   E N      1 
ATOM   13946 C  CA     . GLU   E 3  75  ? -42.864 -45.802  22.620  1.00 52.47  ? 77  GLU   E CA     1 
ATOM   13947 C  C      . GLU   E 3  75  ? -41.963 -44.637  22.241  1.00 49.59  ? 77  GLU   E C      1 
ATOM   13948 O  O      . GLU   E 3  75  ? -42.217 -43.932  21.262  1.00 54.87  ? 77  GLU   E O      1 
ATOM   13949 C  CB     . GLU   E 3  75  ? -43.829 -45.417  23.740  1.00 59.73  ? 77  GLU   E CB     1 
ATOM   13950 C  CG     . GLU   E 3  75  ? -44.985 -44.522  23.388  1.00 72.20  ? 77  GLU   E CG     1 
ATOM   13951 C  CD     . GLU   E 3  75  ? -45.803 -44.181  24.622  1.00 79.07  ? 77  GLU   E CD     1 
ATOM   13952 O  OE1    . GLU   E 3  75  ? -46.059 -45.087  25.446  1.00 76.13  ? 77  GLU   E OE1    1 
ATOM   13953 O  OE2    . GLU   E 3  75  ? -46.212 -43.007  24.757  1.00 92.91  ? 77  GLU   E OE2    1 
ATOM   13954 N  N      . HIS   E 3  76  ? -40.883 -44.441  23.001  1.00 45.52  ? 78  HIS   E N      1 
ATOM   13955 C  CA     . HIS   E 3  76  ? -39.915 -43.389  22.706  1.00 42.48  ? 78  HIS   E CA     1 
ATOM   13956 C  C      . HIS   E 3  76  ? -39.085 -43.733  21.472  1.00 44.51  ? 78  HIS   E C      1 
ATOM   13957 O  O      . HIS   E 3  76  ? -38.910 -42.915  20.570  1.00 41.32  ? 78  HIS   E O      1 
ATOM   13958 C  CB     . HIS   E 3  76  ? -39.007 -43.216  23.904  1.00 36.82  ? 78  HIS   E CB     1 
ATOM   13959 C  CG     . HIS   E 3  76  ? -37.909 -42.230  23.692  1.00 41.71  ? 78  HIS   E CG     1 
ATOM   13960 N  ND1    . HIS   E 3  76  ? -38.144 -40.892  23.476  1.00 44.80  ? 78  HIS   E ND1    1 
ATOM   13961 C  CD2    . HIS   E 3  76  ? -36.567 -42.400  23.603  1.00 41.91  ? 78  HIS   E CD2    1 
ATOM   13962 C  CE1    . HIS   E 3  76  ? -36.990 -40.271  23.302  1.00 45.28  ? 78  HIS   E CE1    1 
ATOM   13963 N  NE2    . HIS   E 3  76  ? -36.019 -41.165  23.362  1.00 41.96  ? 78  HIS   E NE2    1 
ATOM   13964 N  N      . GLU   E 3  77  ? -38.543 -44.944  21.436  1.00 45.55  ? 79  GLU   E N      1 
ATOM   13965 C  CA     . GLU   E 3  77  ? -37.737 -45.385  20.311  1.00 44.57  ? 79  GLU   E CA     1 
ATOM   13966 C  C      . GLU   E 3  77  ? -38.458 -45.130  19.000  1.00 47.62  ? 79  GLU   E C      1 
ATOM   13967 O  O      . GLU   E 3  77  ? -37.833 -44.809  17.980  1.00 48.43  ? 79  GLU   E O      1 
ATOM   13968 C  CB     . GLU   E 3  77  ? -37.440 -46.874  20.461  1.00 44.52  ? 79  GLU   E CB     1 
ATOM   13969 C  CG     . GLU   E 3  77  ? -36.469 -47.201  21.569  1.00 47.79  ? 79  GLU   E CG     1 
ATOM   13970 C  CD     . GLU   E 3  77  ? -36.429 -48.681  21.885  1.00 51.22  ? 79  GLU   E CD     1 
ATOM   13971 O  OE1    . GLU   E 3  77  ? -37.225 -49.433  21.272  1.00 45.88  ? 79  GLU   E OE1    1 
ATOM   13972 O  OE2    . GLU   E 3  77  ? -35.636 -49.072  22.775  1.00 48.86  ? 79  GLU   E OE2    1 
ATOM   13973 N  N      . ARG   E 3  78  ? -39.772 -45.305  18.990  1.00 46.93  ? 80  ARG   E N      1 
ATOM   13974 C  CA     . ARG   E 3  78  ? -40.458 -45.115  17.733  1.00 48.56  ? 80  ARG   E CA     1 
ATOM   13975 C  C      . ARG   E 3  78  ? -40.887 -43.675  17.546  1.00 47.56  ? 80  ARG   E C      1 
ATOM   13976 O  O      . ARG   E 3  78  ? -41.006 -43.234  16.405  1.00 54.41  ? 80  ARG   E O      1 
ATOM   13977 C  CB     . ARG   E 3  78  ? -41.627 -46.101  17.608  1.00 54.11  ? 80  ARG   E CB     1 
ATOM   13978 C  CG     . ARG   E 3  78  ? -42.834 -45.872  18.450  1.00 58.43  ? 80  ARG   E CG     1 
ATOM   13979 C  CD     . ARG   E 3  78  ? -43.951 -46.872  18.052  1.00 66.33  ? 80  ARG   E CD     1 
ATOM   13980 N  NE     . ARG   E 3  78  ? -45.184 -46.586  18.786  1.00 83.41  ? 80  ARG   E NE     1 
ATOM   13981 C  CZ     . ARG   E 3  78  ? -45.519 -47.094  19.973  1.00 85.33  ? 80  ARG   E CZ     1 
ATOM   13982 N  NH1    . ARG   E 3  78  ? -44.742 -47.970  20.607  1.00 68.96  ? 80  ARG   E NH1    1 
ATOM   13983 N  NH2    . ARG   E 3  78  ? -46.656 -46.697  20.551  1.00 81.01  ? 80  ARG   E NH2    1 
ATOM   13984 N  N      . GLU   E 3  79  ? -41.022 -42.904  18.626  1.00 44.07  ? 81  GLU   E N      1 
ATOM   13985 C  CA     . GLU   E 3  79  ? -41.177 -41.460  18.468  1.00 42.46  ? 81  GLU   E CA     1 
ATOM   13986 C  C      . GLU   E 3  79  ? -39.942 -40.838  17.833  1.00 44.74  ? 81  GLU   E C      1 
ATOM   13987 O  O      . GLU   E 3  79  ? -40.047 -39.901  17.039  1.00 47.17  ? 81  GLU   E O      1 
ATOM   13988 C  CB     . GLU   E 3  79  ? -41.446 -40.783  19.808  1.00 39.96  ? 81  GLU   E CB     1 
ATOM   13989 C  CG     . GLU   E 3  79  ? -42.857 -40.934  20.279  1.00 51.03  ? 81  GLU   E CG     1 
ATOM   13990 C  CD     . GLU   E 3  79  ? -43.096 -40.295  21.630  1.00 65.70  ? 81  GLU   E CD     1 
ATOM   13991 O  OE1    . GLU   E 3  79  ? -42.367 -39.321  21.972  1.00 64.76  ? 81  GLU   E OE1    1 
ATOM   13992 O  OE2    . GLU   E 3  79  ? -44.002 -40.799  22.348  1.00 66.95  ? 81  GLU   E OE2    1 
ATOM   13993 N  N      . VAL   E 3  80  ? -38.754 -41.306  18.203  1.00 49.26  ? 82  VAL   E N      1 
ATOM   13994 C  CA     . VAL   E 3  80  ? -37.558 -40.630  17.724  1.00 41.65  ? 82  VAL   E CA     1 
ATOM   13995 C  C      . VAL   E 3  80  ? -37.421 -40.863  16.234  1.00 40.62  ? 82  VAL   E C      1 
ATOM   13996 O  O      . VAL   E 3  80  ? -37.212 -39.922  15.465  1.00 47.16  ? 82  VAL   E O      1 
ATOM   13997 C  CB     . VAL   E 3  80  ? -36.310 -41.089  18.511  1.00 40.45  ? 82  VAL   E CB     1 
ATOM   13998 C  CG1    . VAL   E 3  80  ? -35.026 -40.605  17.851  1.00 34.98  ? 82  VAL   E CG1    1 
ATOM   13999 C  CG2    . VAL   E 3  80  ? -36.376 -40.613  19.970  1.00 38.54  ? 82  VAL   E CG2    1 
ATOM   14000 N  N      . ILE   E 3  81  ? -37.603 -42.103  15.783  1.00 35.71  ? 83  ILE   E N      1 
ATOM   14001 C  CA     . ILE   E 3  81  ? -37.494 -42.328  14.351  1.00 36.97  ? 83  ILE   E CA     1 
ATOM   14002 C  C      . ILE   E 3  81  ? -38.634 -41.645  13.596  1.00 44.50  ? 83  ILE   E C      1 
ATOM   14003 O  O      . ILE   E 3  81  ? -38.475 -41.300  12.420  1.00 39.81  ? 83  ILE   E O      1 
ATOM   14004 C  CB     . ILE   E 3  81  ? -37.450 -43.833  14.060  1.00 34.08  ? 83  ILE   E CB     1 
ATOM   14005 C  CG1    . ILE   E 3  81  ? -36.920 -44.067  12.654  1.00 36.87  ? 83  ILE   E CG1    1 
ATOM   14006 C  CG2    . ILE   E 3  81  ? -38.823 -44.455  14.269  1.00 34.22  ? 83  ILE   E CG2    1 
ATOM   14007 C  CD1    . ILE   E 3  81  ? -36.963 -45.503  12.229  1.00 40.25  ? 83  ILE   E CD1    1 
ATOM   14008 N  N      . GLN   E 3  82  ? -39.794 -41.441  14.241  1.00 46.85  ? 84  GLN   E N      1 
ATOM   14009 C  CA     . GLN   E 3  82  ? -40.843 -40.638  13.614  1.00 45.44  ? 84  GLN   E CA     1 
ATOM   14010 C  C      . GLN   E 3  82  ? -40.407 -39.170  13.526  1.00 44.18  ? 84  GLN   E C      1 
ATOM   14011 O  O      . GLN   E 3  82  ? -40.548 -38.536  12.476  1.00 46.21  ? 84  GLN   E O      1 
ATOM   14012 C  CB     . GLN   E 3  82  ? -42.181 -40.788  14.369  1.00 43.30  ? 84  GLN   E CB     1 
ATOM   14013 C  CG     . GLN   E 3  82  ? -43.060 -42.020  13.934  1.00 58.61  ? 84  GLN   E CG     1 
ATOM   14014 C  CD     . GLN   E 3  82  ? -44.449 -42.115  14.645  1.00 78.40  ? 84  GLN   E CD     1 
ATOM   14015 O  OE1    . GLN   E 3  82  ? -44.539 -42.024  15.874  1.00 71.43  ? 84  GLN   E OE1    1 
ATOM   14016 N  NE2    . GLN   E 3  82  ? -45.513 -42.405  13.863  1.00 69.75  ? 84  GLN   E NE2    1 
ATOM   14017 N  N      . LYS   E 3  83  ? -39.830 -38.628  14.602  1.00 41.61  ? 85  LYS   E N      1 
ATOM   14018 C  CA     . LYS   E 3  83  ? -39.334 -37.256  14.573  1.00 38.52  ? 85  LYS   E CA     1 
ATOM   14019 C  C      . LYS   E 3  83  ? -38.259 -37.074  13.518  1.00 37.78  ? 85  LYS   E C      1 
ATOM   14020 O  O      . LYS   E 3  83  ? -38.238 -36.066  12.812  1.00 40.92  ? 85  LYS   E O      1 
ATOM   14021 C  CB     . LYS   E 3  83  ? -38.804 -36.852  15.947  1.00 37.46  ? 85  LYS   E CB     1 
ATOM   14022 C  CG     . LYS   E 3  83  ? -38.626 -35.336  16.135  1.00 42.58  ? 85  LYS   E CG     1 
ATOM   14023 C  CD     . LYS   E 3  83  ? -38.086 -34.995  17.532  1.00 47.96  ? 85  LYS   E CD     1 
ATOM   14024 C  CE     . LYS   E 3  83  ? -37.500 -33.572  17.605  1.00 55.15  ? 85  LYS   E CE     1 
ATOM   14025 N  NZ     . LYS   E 3  83  ? -36.887 -33.275  18.948  1.00 53.30  ? 85  LYS   E NZ     1 
ATOM   14026 N  N      . ALA   E 3  84  ? -37.343 -38.022  13.403  1.00 41.13  ? 86  ALA   E N      1 
ATOM   14027 C  CA     . ALA   E 3  84  ? -36.320 -37.896  12.375  1.00 41.16  ? 86  ALA   E CA     1 
ATOM   14028 C  C      . ALA   E 3  84  ? -36.956 -37.824  10.997  1.00 46.30  ? 86  ALA   E C      1 
ATOM   14029 O  O      . ALA   E 3  84  ? -36.709 -36.878  10.240  1.00 55.24  ? 86  ALA   E O      1 
ATOM   14030 C  CB     . ALA   E 3  84  ? -35.333 -39.053  12.458  1.00 37.68  ? 86  ALA   E CB     1 
ATOM   14031 N  N      . ILE   E 3  85  ? -37.804 -38.804  10.661  1.00 43.75  ? 87  ILE   E N      1 
ATOM   14032 C  CA     . ILE   E 3  85  ? -38.511 -38.772  9.382   1.00 39.21  ? 87  ILE   E CA     1 
ATOM   14033 C  C      . ILE   E 3  85  ? -39.218 -37.439  9.198   1.00 43.13  ? 87  ILE   E C      1 
ATOM   14034 O  O      . ILE   E 3  85  ? -39.054 -36.778  8.172   1.00 43.78  ? 87  ILE   E O      1 
ATOM   14035 C  CB     . ILE   E 3  85  ? -39.501 -39.943  9.265   1.00 36.42  ? 87  ILE   E CB     1 
ATOM   14036 C  CG1    . ILE   E 3  85  ? -38.758 -41.263  9.149   1.00 38.57  ? 87  ILE   E CG1    1 
ATOM   14037 C  CG2    . ILE   E 3  85  ? -40.352 -39.756  8.040   1.00 41.20  ? 87  ILE   E CG2    1 
ATOM   14038 C  CD1    . ILE   E 3  85  ? -39.626 -42.443  9.015   1.00 37.26  ? 87  ILE   E CD1    1 
ATOM   14039 N  N      . GLU   E 3  86  ? -40.012 -37.022  10.195  1.00 44.15  ? 88  GLU   E N      1 
ATOM   14040 C  CA     . GLU   E 3  86  ? -40.812 -35.804  10.055  1.00 43.02  ? 88  GLU   E CA     1 
ATOM   14041 C  C      . GLU   E 3  86  ? -39.946 -34.631  9.662   1.00 47.98  ? 88  GLU   E C      1 
ATOM   14042 O  O      . GLU   E 3  86  ? -40.314 -33.833  8.793   1.00 57.43  ? 88  GLU   E O      1 
ATOM   14043 C  CB     . GLU   E 3  86  ? -41.540 -35.461  11.350  1.00 40.19  ? 88  GLU   E CB     1 
ATOM   14044 C  CG     . GLU   E 3  86  ? -42.395 -34.205  11.267  1.00 41.31  ? 88  GLU   E CG     1 
ATOM   14045 C  CD     . GLU   E 3  86  ? -43.601 -34.369  10.352  1.00 62.99  ? 88  GLU   E CD     1 
ATOM   14046 O  OE1    . GLU   E 3  86  ? -44.643 -34.864  10.854  1.00 68.71  ? 88  GLU   E OE1    1 
ATOM   14047 O  OE2    . GLU   E 3  86  ? -43.517 -34.027  9.140   1.00 59.53  ? 88  GLU   E OE2    1 
ATOM   14048 N  N      . GLU   E 3  87  ? -38.795 -34.496  10.298  1.00 48.73  ? 89  GLU   E N      1 
ATOM   14049 C  CA     . GLU   E 3  87  ? -37.960 -33.351  9.995   1.00 54.23  ? 89  GLU   E CA     1 
ATOM   14050 C  C      . GLU   E 3  87  ? -37.350 -33.480  8.608   1.00 46.62  ? 89  GLU   E C      1 
ATOM   14051 O  O      . GLU   E 3  87  ? -37.438 -32.550  7.801   1.00 47.47  ? 89  GLU   E O      1 
ATOM   14052 C  CB     . GLU   E 3  87  ? -36.907 -33.182  11.081  1.00 52.54  ? 89  GLU   E CB     1 
ATOM   14053 C  CG     . GLU   E 3  87  ? -37.532 -32.502  12.275  1.00 57.03  ? 89  GLU   E CG     1 
ATOM   14054 C  CD     . GLU   E 3  87  ? -36.549 -32.245  13.383  1.00 73.85  ? 89  GLU   E CD     1 
ATOM   14055 O  OE1    . GLU   E 3  87  ? -35.325 -32.250  13.100  1.00 68.94  ? 89  GLU   E OE1    1 
ATOM   14056 O  OE2    . GLU   E 3  87  ? -37.013 -32.049  14.537  1.00 74.58  ? 89  GLU   E OE2    1 
ATOM   14057 N  N      . ASN   E 3  88  ? -36.774 -34.642  8.289   1.00 43.64  ? 90  ASN   E N      1 
ATOM   14058 C  CA     . ASN   E 3  88  ? -36.234 -34.825  6.946   1.00 47.20  ? 90  ASN   E CA     1 
ATOM   14059 C  C      . ASN   E 3  88  ? -37.270 -34.482  5.892   1.00 50.43  ? 90  ASN   E C      1 
ATOM   14060 O  O      . ASN   E 3  88  ? -36.926 -33.976  4.822   1.00 50.66  ? 90  ASN   E O      1 
ATOM   14061 C  CB     . ASN   E 3  88  ? -35.759 -36.256  6.721   1.00 48.36  ? 90  ASN   E CB     1 
ATOM   14062 C  CG     . ASN   E 3  88  ? -35.406 -36.523  5.249   1.00 59.73  ? 90  ASN   E CG     1 
ATOM   14063 O  OD1    . ASN   E 3  88  ? -34.414 -35.994  4.727   1.00 56.25  ? 90  ASN   E OD1    1 
ATOM   14064 N  ND2    . ASN   E 3  88  ? -36.229 -37.313  4.571   1.00 68.32  ? 90  ASN   E ND2    1 
ATOM   14065 N  N      . ASN   E 3  89  ? -38.547 -34.745  6.180   1.00 56.83  ? 91  ASN   E N      1 
ATOM   14066 C  CA     . ASN   E 3  89  ? -39.634 -34.416  5.261   1.00 50.61  ? 91  ASN   E CA     1 
ATOM   14067 C  C      . ASN   E 3  89  ? -39.956 -32.933  5.259   1.00 51.50  ? 91  ASN   E C      1 
ATOM   14068 O  O      . ASN   E 3  89  ? -40.016 -32.311  4.190   1.00 54.25  ? 91  ASN   E O      1 
ATOM   14069 C  CB     . ASN   E 3  89  ? -40.876 -35.228  5.602   1.00 46.46  ? 91  ASN   E CB     1 
ATOM   14070 C  CG     . ASN   E 3  89  ? -40.832 -36.573  4.986   1.00 49.35  ? 91  ASN   E CG     1 
ATOM   14071 O  OD1    . ASN   E 3  89  ? -39.875 -36.880  4.285   1.00 52.64  ? 91  ASN   E OD1    1 
ATOM   14072 N  ND2    . ASN   E 3  89  ? -41.837 -37.403  5.250   1.00 50.92  ? 91  ASN   E ND2    1 
ATOM   14073 N  N      . ASN   E 3  90  ? -40.183 -32.342  6.432   1.00 51.85  ? 92  ASN   E N      1 
ATOM   14074 C  CA     . ASN   E 3  90  ? -40.432 -30.912  6.421   1.00 53.52  ? 92  ASN   E CA     1 
ATOM   14075 C  C      . ASN   E 3  90  ? -39.300 -30.202  5.675   1.00 52.35  ? 92  ASN   E C      1 
ATOM   14076 O  O      . ASN   E 3  90  ? -39.533 -29.220  4.965   1.00 54.47  ? 92  ASN   E O      1 
ATOM   14077 C  CB     . ASN   E 3  90  ? -40.580 -30.382  7.848   1.00 50.87  ? 92  ASN   E CB     1 
ATOM   14078 C  CG     . ASN   E 3  90  ? -40.537 -28.858  7.900   1.00 71.51  ? 92  ASN   E CG     1 
ATOM   14079 O  OD1    . ASN   E 3  90  ? -41.527 -28.193  7.562   1.00 78.86  ? 92  ASN   E OD1    1 
ATOM   14080 N  ND2    . ASN   E 3  90  ? -39.374 -28.297  8.239   1.00 68.35  ? 92  ASN   E ND2    1 
ATOM   14081 N  N      . PHE   E 3  91  ? -38.078 -30.723  5.771   1.00 48.45  ? 93  PHE   E N      1 
ATOM   14082 C  CA     . PHE   E 3  91  ? -36.973 -30.142  5.021   1.00 45.17  ? 93  PHE   E CA     1 
ATOM   14083 C  C      . PHE   E 3  91  ? -37.192 -30.292  3.526   1.00 45.94  ? 93  PHE   E C      1 
ATOM   14084 O  O      . PHE   E 3  91  ? -37.178 -29.303  2.793   1.00 52.33  ? 93  PHE   E O      1 
ATOM   14085 C  CB     . PHE   E 3  91  ? -35.652 -30.778  5.437   1.00 47.65  ? 93  PHE   E CB     1 
ATOM   14086 C  CG     . PHE   E 3  91  ? -34.474 -30.328  4.623   1.00 45.46  ? 93  PHE   E CG     1 
ATOM   14087 C  CD1    . PHE   E 3  91  ? -33.934 -29.066  4.813   1.00 39.62  ? 93  PHE   E CD1    1 
ATOM   14088 C  CD2    . PHE   E 3  91  ? -33.896 -31.181  3.675   1.00 45.03  ? 93  PHE   E CD2    1 
ATOM   14089 C  CE1    . PHE   E 3  91  ? -32.850 -28.653  4.071   1.00 43.15  ? 93  PHE   E CE1    1 
ATOM   14090 C  CE2    . PHE   E 3  91  ? -32.801 -30.779  2.920   1.00 44.57  ? 93  PHE   E CE2    1 
ATOM   14091 C  CZ     . PHE   E 3  91  ? -32.275 -29.512  3.118   1.00 46.58  ? 93  PHE   E CZ     1 
ATOM   14092 N  N      . ILE   E 3  92  ? -37.399 -31.513  3.039   1.00 42.44  ? 94  ILE   E N      1 
ATOM   14093 C  CA     . ILE   E 3  92  ? -37.729 -31.625  1.622   1.00 47.04  ? 94  ILE   E CA     1 
ATOM   14094 C  C      . ILE   E 3  92  ? -38.939 -30.753  1.275   1.00 50.34  ? 94  ILE   E C      1 
ATOM   14095 O  O      . ILE   E 3  92  ? -38.957 -30.103  0.223   1.00 44.25  ? 94  ILE   E O      1 
ATOM   14096 C  CB     . ILE   E 3  92  ? -37.932 -33.088  1.193   1.00 43.38  ? 94  ILE   E CB     1 
ATOM   14097 C  CG1    . ILE   E 3  92  ? -36.642 -33.873  1.334   1.00 43.80  ? 94  ILE   E CG1    1 
ATOM   14098 C  CG2    . ILE   E 3  92  ? -38.351 -33.160  -0.256  1.00 45.60  ? 94  ILE   E CG2    1 
ATOM   14099 C  CD1    . ILE   E 3  92  ? -36.802 -35.342  1.014   1.00 47.04  ? 94  ILE   E CD1    1 
ATOM   14100 N  N      . LYS   E 3  93  ? -39.954 -30.696  2.153   1.00 50.79  ? 95  LYS   E N      1 
ATOM   14101 C  CA     . LYS   E 3  93  ? -41.092 -29.807  1.919   1.00 47.30  ? 95  LYS   E CA     1 
ATOM   14102 C  C      . LYS   E 3  93  ? -40.641 -28.370  1.721   1.00 51.61  ? 95  LYS   E C      1 
ATOM   14103 O  O      . LYS   E 3  93  ? -40.844 -27.779  0.658   1.00 52.20  ? 95  LYS   E O      1 
ATOM   14104 C  CB     . LYS   E 3  93  ? -42.077 -29.870  3.082   1.00 55.52  ? 95  LYS   E CB     1 
ATOM   14105 C  CG     . LYS   E 3  93  ? -43.465 -29.350  2.693   1.00 68.17  ? 95  LYS   E CG     1 
ATOM   14106 C  CD     . LYS   E 3  93  ? -44.445 -29.310  3.853   1.00 69.19  ? 95  LYS   E CD     1 
ATOM   14107 C  CE     . LYS   E 3  93  ? -44.411 -27.973  4.579   1.00 77.17  ? 95  LYS   E CE     1 
ATOM   14108 N  NZ     . LYS   E 3  93  ? -45.779 -27.571  5.032   1.00 80.69  ? 95  LYS   E NZ     1 
ATOM   14109 N  N      . MET   E 3  94  ? -40.040 -27.783  2.755   1.00 53.73  ? 96  MET   E N      1 
ATOM   14110 C  CA     . MET   E 3  94  ? -39.823 -26.342  2.777   1.00 51.43  ? 96  MET   E CA     1 
ATOM   14111 C  C      . MET   E 3  94  ? -38.865 -25.923  1.679   1.00 47.59  ? 96  MET   E C      1 
ATOM   14112 O  O      . MET   E 3  94  ? -39.014 -24.852  1.095   1.00 48.66  ? 96  MET   E O      1 
ATOM   14113 C  CB     . MET   E 3  94  ? -39.305 -25.939  4.151   1.00 58.08  ? 96  MET   E CB     1 
ATOM   14114 C  CG     . MET   E 3  94  ? -40.440 -25.608  5.121   1.00 70.70  ? 96  MET   E CG     1 
ATOM   14115 S  SD     . MET   E 3  94  ? -39.854 -25.138  6.754   1.00 93.14  ? 96  MET   E SD     1 
ATOM   14116 C  CE     . MET   E 3  94  ? -38.405 -24.162  6.310   1.00 95.42  ? 96  MET   E CE     1 
ATOM   14117 N  N      . ALA   E 3  95  ? -37.876 -26.757  1.386   1.00 46.95  ? 97  ALA   E N      1 
ATOM   14118 C  CA     . ALA   E 3  95  ? -37.042 -26.564  0.216   1.00 42.42  ? 97  ALA   E CA     1 
ATOM   14119 C  C      . ALA   E 3  95  ? -37.914 -26.423  -1.017  1.00 43.84  ? 97  ALA   E C      1 
ATOM   14120 O  O      . ALA   E 3  95  ? -38.052 -25.330  -1.573  1.00 44.12  ? 97  ALA   E O      1 
ATOM   14121 C  CB     . ALA   E 3  95  ? -36.084 -27.735  0.052   1.00 39.52  ? 97  ALA   E CB     1 
ATOM   14122 N  N      . LYS   E 3  96  ? -38.524 -27.529  -1.426  1.00 45.24  ? 98  LYS   E N      1 
ATOM   14123 C  CA     . LYS   E 3  96  ? -39.411 -27.586  -2.579  1.00 42.75  ? 98  LYS   E CA     1 
ATOM   14124 C  C      . LYS   E 3  96  ? -40.276 -26.345  -2.706  1.00 44.71  ? 98  LYS   E C      1 
ATOM   14125 O  O      . LYS   E 3  96  ? -40.500 -25.861  -3.815  1.00 57.47  ? 98  LYS   E O      1 
ATOM   14126 C  CB     . LYS   E 3  96  ? -40.302 -28.823  -2.495  1.00 39.56  ? 98  LYS   E CB     1 
ATOM   14127 C  CG     . LYS   E 3  96  ? -40.795 -29.364  -3.819  1.00 44.84  ? 98  LYS   E CG     1 
ATOM   14128 C  CD     . LYS   E 3  96  ? -41.767 -30.516  -3.603  1.00 47.20  ? 98  LYS   E CD     1 
ATOM   14129 C  CE     . LYS   E 3  96  ? -42.122 -31.258  -4.891  1.00 50.16  ? 98  LYS   E CE     1 
ATOM   14130 N  NZ     . LYS   E 3  96  ? -41.093 -32.250  -5.306  1.00 53.27  ? 98  LYS   E NZ     1 
ATOM   14131 N  N      . GLU   E 3  97  ? -40.752 -25.796  -1.596  1.00 46.53  ? 99  GLU   E N      1 
ATOM   14132 C  CA     . GLU   E 3  97  ? -41.635 -24.640  -1.703  1.00 46.94  ? 99  GLU   E CA     1 
ATOM   14133 C  C      . GLU   E 3  97  ? -40.881 -23.321  -1.806  1.00 46.20  ? 99  GLU   E C      1 
ATOM   14134 O  O      . GLU   E 3  97  ? -41.306 -22.438  -2.551  1.00 48.61  ? 99  GLU   E O      1 
ATOM   14135 C  CB     . GLU   E 3  97  ? -42.613 -24.608  -0.533  1.00 48.49  ? 99  GLU   E CB     1 
ATOM   14136 C  CG     . GLU   E 3  97  ? -43.683 -25.666  -0.663  1.00 57.74  ? 99  GLU   E CG     1 
ATOM   14137 C  CD     . GLU   E 3  97  ? -44.421 -25.929  0.622   1.00 70.03  ? 99  GLU   E CD     1 
ATOM   14138 O  OE1    . GLU   E 3  97  ? -44.130 -25.235  1.628   1.00 76.75  ? 99  GLU   E OE1    1 
ATOM   14139 O  OE2    . GLU   E 3  97  ? -45.312 -26.812  0.612   1.00 71.25  ? 99  GLU   E OE2    1 
ATOM   14140 N  N      . LYS   E 3  98  ? -39.787 -23.145  -1.060  1.00 49.30  ? 100 LYS   E N      1 
ATOM   14141 C  CA     . LYS   E 3  98  ? -38.974 -21.948  -1.249  1.00 48.76  ? 100 LYS   E CA     1 
ATOM   14142 C  C      . LYS   E 3  98  ? -38.586 -21.793  -2.717  1.00 56.84  ? 100 LYS   E C      1 
ATOM   14143 O  O      . LYS   E 3  98  ? -38.825 -20.749  -3.335  1.00 56.45  ? 100 LYS   E O      1 
ATOM   14144 C  CB     . LYS   E 3  98  ? -37.712 -21.996  -0.386  1.00 46.87  ? 100 LYS   E CB     1 
ATOM   14145 C  CG     . LYS   E 3  98  ? -37.784 -21.400  1.014   1.00 56.39  ? 100 LYS   E CG     1 
ATOM   14146 C  CD     . LYS   E 3  98  ? -38.673 -22.223  1.943   1.00 69.35  ? 100 LYS   E CD     1 
ATOM   14147 C  CE     . LYS   E 3  98  ? -38.654 -21.713  3.388   1.00 71.26  ? 100 LYS   E CE     1 
ATOM   14148 N  NZ     . LYS   E 3  98  ? -39.134 -20.315  3.481   1.00 79.16  ? 100 LYS   E NZ     1 
ATOM   14149 N  N      . LEU   E 3  99  ? -37.961 -22.819  -3.284  1.00 53.50  ? 101 LEU   E N      1 
ATOM   14150 C  CA     . LEU   E 3  99  ? -37.713 -22.890  -4.713  1.00 46.86  ? 101 LEU   E CA     1 
ATOM   14151 C  C      . LEU   E 3  99  ? -38.933 -22.418  -5.488  1.00 50.68  ? 101 LEU   E C      1 
ATOM   14152 O  O      . LEU   E 3  99  ? -38.903 -21.348  -6.091  1.00 53.88  ? 101 LEU   E O      1 
ATOM   14153 C  CB     . LEU   E 3  99  ? -37.343 -24.325  -5.094  1.00 47.78  ? 101 LEU   E CB     1 
ATOM   14154 C  CG     . LEU   E 3  99  ? -36.308 -24.553  -6.179  1.00 46.34  ? 101 LEU   E CG     1 
ATOM   14155 C  CD1    . LEU   E 3  99  ? -35.223 -23.496  -6.084  1.00 50.11  ? 101 LEU   E CD1    1 
ATOM   14156 C  CD2    . LEU   E 3  99  ? -35.718 -25.976  -6.065  1.00 37.67  ? 101 LEU   E CD2    1 
ATOM   14157 N  N      . ALA   E 3  100 ? -40.021 -23.195  -5.459  1.00 56.28  ? 102 ALA   E N      1 
ATOM   14158 C  CA     . ALA   E 3  100 ? -41.195 -22.876  -6.268  1.00 51.49  ? 102 ALA   E CA     1 
ATOM   14159 C  C      . ALA   E 3  100 ? -41.683 -21.463  -6.025  1.00 50.35  ? 102 ALA   E C      1 
ATOM   14160 O  O      . ALA   E 3  100 ? -42.240 -20.837  -6.927  1.00 57.37  ? 102 ALA   E O      1 
ATOM   14161 C  CB     . ALA   E 3  100 ? -42.312 -23.872  -5.991  1.00 45.08  ? 102 ALA   E CB     1 
ATOM   14162 N  N      . GLN   E 3  101 ? -41.501 -20.955  -4.820  1.00 51.59  ? 103 GLN   E N      1 
ATOM   14163 C  CA     . GLN   E 3  101 ? -41.696 -19.544  -4.533  1.00 57.45  ? 103 GLN   E CA     1 
ATOM   14164 C  C      . GLN   E 3  101 ? -40.817 -18.646  -5.404  1.00 58.24  ? 103 GLN   E C      1 
ATOM   14165 O  O      . GLN   E 3  101 ? -41.315 -17.929  -6.276  1.00 57.77  ? 103 GLN   E O      1 
ATOM   14166 C  CB     . GLN   E 3  101 ? -41.411 -19.293  -3.053  1.00 67.98  ? 103 GLN   E CB     1 
ATOM   14167 C  CG     . GLN   E 3  101 ? -41.252 -17.830  -2.691  1.00 78.19  ? 103 GLN   E CG     1 
ATOM   14168 C  CD     . GLN   E 3  101 ? -42.325 -16.985  -3.333  1.00 92.29  ? 103 GLN   E CD     1 
ATOM   14169 O  OE1    . GLN   E 3  101 ? -42.025 -15.996  -4.016  1.00 95.44  ? 103 GLN   E OE1    1 
ATOM   14170 N  NE2    . GLN   E 3  101 ? -43.591 -17.396  -3.164  1.00 91.02  ? 103 GLN   E NE2    1 
ATOM   14171 N  N      . LYS   E 3  102 ? -39.509 -18.663  -5.138  1.00 62.82  ? 104 LYS   E N      1 
ATOM   14172 C  CA     . LYS   E 3  102 ? -38.532 -17.887  -5.899  1.00 57.69  ? 104 LYS   E CA     1 
ATOM   14173 C  C      . LYS   E 3  102 ? -38.749 -18.008  -7.413  1.00 54.32  ? 104 LYS   E C      1 
ATOM   14174 O  O      . LYS   E 3  102 ? -38.780 -17.006  -8.125  1.00 54.18  ? 104 LYS   E O      1 
ATOM   14175 C  CB     . LYS   E 3  102 ? -37.131 -18.369  -5.516  1.00 59.72  ? 104 LYS   E CB     1 
ATOM   14176 C  CG     . LYS   E 3  102 ? -36.412 -17.595  -4.397  1.00 68.84  ? 104 LYS   E CG     1 
ATOM   14177 C  CD     . LYS   E 3  102 ? -34.886 -17.819  -4.484  1.00 73.83  ? 104 LYS   E CD     1 
ATOM   14178 C  CE     . LYS   E 3  102 ? -34.522 -19.322  -4.292  1.00 69.95  ? 104 LYS   E CE     1 
ATOM   14179 N  NZ     . LYS   E 3  102 ? -33.057 -19.638  -4.202  1.00 55.19  ? 104 LYS   E NZ     1 
ATOM   14180 N  N      . MET   E 3  103 ? -38.881 -19.226  -7.943  1.00 54.52  ? 105 MET   E N      1 
ATOM   14181 C  CA     . MET   E 3  103 ? -38.952 -19.328  -9.399  1.00 55.12  ? 105 MET   E CA     1 
ATOM   14182 C  C      . MET   E 3  103 ? -40.145 -18.569  -9.950  1.00 54.12  ? 105 MET   E C      1 
ATOM   14183 O  O      . MET   E 3  103 ? -40.071 -18.047  -11.061 1.00 60.38  ? 105 MET   E O      1 
ATOM   14184 C  CB     . MET   E 3  103 ? -38.989 -20.787  -9.862  1.00 54.78  ? 105 MET   E CB     1 
ATOM   14185 C  CG     . MET   E 3  103 ? -37.774 -21.571  -9.363  1.00 60.05  ? 105 MET   E CG     1 
ATOM   14186 S  SD     . MET   E 3  103 ? -36.143 -20.831  -9.711  1.00 69.71  ? 105 MET   E SD     1 
ATOM   14187 C  CE     . MET   E 3  103 ? -35.547 -21.726  -11.168 1.00 47.54  ? 105 MET   E CE     1 
ATOM   14188 N  N      . GLU   E 3  104 ? -41.234 -18.466  -9.181  1.00 60.18  ? 106 GLU   E N      1 
ATOM   14189 C  CA     . GLU   E 3  104 ? -42.438 -17.760  -9.630  1.00 63.10  ? 106 GLU   E CA     1 
ATOM   14190 C  C      . GLU   E 3  104 ? -42.303 -16.250  -9.461  1.00 58.80  ? 106 GLU   E C      1 
ATOM   14191 O  O      . GLU   E 3  104 ? -42.477 -15.493  -10.417 1.00 58.49  ? 106 GLU   E O      1 
ATOM   14192 C  CB     . GLU   E 3  104 ? -43.659 -18.296  -8.875  1.00 60.53  ? 106 GLU   E CB     1 
ATOM   14193 C  CG     . GLU   E 3  104 ? -45.044 -17.808  -9.357  1.00 70.38  ? 106 GLU   E CG     1 
ATOM   14194 C  CD     . GLU   E 3  104 ? -45.311 -18.058  -10.844 1.00 77.11  ? 106 GLU   E CD     1 
ATOM   14195 O  OE1    . GLU   E 3  104 ? -45.024 -19.164  -11.358 1.00 82.74  ? 106 GLU   E OE1    1 
ATOM   14196 O  OE2    . GLU   E 3  104 ? -45.901 -17.161  -11.483 1.00 78.57  ? 106 GLU   E OE2    1 
ATOM   14197 N  N      . SER   E 3  105 ? -42.004 -15.800  -8.252  1.00 57.73  ? 107 SER   E N      1 
ATOM   14198 C  CA     . SER   E 3  105 ? -41.562 -14.435  -8.001  1.00 57.76  ? 107 SER   E CA     1 
ATOM   14199 C  C      . SER   E 3  105 ? -40.642 -13.930  -9.123  1.00 57.88  ? 107 SER   E C      1 
ATOM   14200 O  O      . SER   E 3  105 ? -40.695 -12.763  -9.536  1.00 57.30  ? 107 SER   E O      1 
ATOM   14201 C  CB     . SER   E 3  105 ? -40.869 -14.406  -6.621  1.00 55.85  ? 107 SER   E CB     1 
ATOM   14202 O  OG     . SER   E 3  105 ? -40.491 -13.108  -6.184  1.00 62.66  ? 107 SER   E OG     1 
ATOM   14203 N  N      . ASN   E 3  106 ? -39.810 -14.823  -9.646  1.00 57.10  ? 108 ASN   E N      1 
ATOM   14204 C  CA     . ASN   E 3  106 ? -38.765 -14.423  -10.572 1.00 51.94  ? 108 ASN   E CA     1 
ATOM   14205 C  C      . ASN   E 3  106 ? -39.303 -14.245  -11.974 1.00 50.82  ? 108 ASN   E C      1 
ATOM   14206 O  O      . ASN   E 3  106 ? -38.961 -13.267  -12.639 1.00 51.03  ? 108 ASN   E O      1 
ATOM   14207 C  CB     . ASN   E 3  106 ? -37.645 -15.454  -10.539 1.00 55.35  ? 108 ASN   E CB     1 
ATOM   14208 C  CG     . ASN   E 3  106 ? -36.397 -14.968  -11.193 1.00 53.65  ? 108 ASN   E CG     1 
ATOM   14209 O  OD1    . ASN   E 3  106 ? -36.195 -15.200  -12.384 1.00 60.49  ? 108 ASN   E OD1    1 
ATOM   14210 N  ND2    . ASN   E 3  106 ? -35.552 -14.286  -10.440 1.00 48.96  ? 108 ASN   E ND2    1 
ATOM   14211 N  N      . LYS   E 3  107 ? -40.146 -15.168  -12.438 1.00 53.45  ? 109 LYS   E N      1 
ATOM   14212 C  CA     . LYS   E 3  107 ? -40.781 -14.996  -13.743 1.00 55.85  ? 109 LYS   E CA     1 
ATOM   14213 C  C      . LYS   E 3  107 ? -41.649 -13.742  -13.769 1.00 55.52  ? 109 LYS   E C      1 
ATOM   14214 O  O      . LYS   E 3  107 ? -41.520 -12.911  -14.674 1.00 58.37  ? 109 LYS   E O      1 
ATOM   14215 C  CB     . LYS   E 3  107 ? -41.575 -16.252  -14.111 1.00 52.06  ? 109 LYS   E CB     1 
ATOM   14216 C  CG     . LYS   E 3  107 ? -41.698 -16.558  -15.607 1.00 52.04  ? 109 LYS   E CG     1 
ATOM   14217 C  CD     . LYS   E 3  107 ? -42.496 -17.865  -15.842 1.00 57.41  ? 109 LYS   E CD     1 
ATOM   14218 C  CE     . LYS   E 3  107 ? -43.998 -17.718  -15.565 1.00 57.10  ? 109 LYS   E CE     1 
ATOM   14219 N  NZ     . LYS   E 3  107 ? -44.720 -19.017  -15.699 1.00 59.29  ? 109 LYS   E NZ     1 
ATOM   14220 N  N      . GLU   E 3  108 ? -42.513 -13.559  -12.768 1.00 51.92  ? 110 GLU   E N      1 
ATOM   14221 C  CA     . GLU   E 3  108 ? -43.284 -12.323  -12.732 1.00 55.03  ? 110 GLU   E CA     1 
ATOM   14222 C  C      . GLU   E 3  108 ? -42.384 -11.107  -12.807 1.00 56.71  ? 110 GLU   E C      1 
ATOM   14223 O  O      . GLU   E 3  108 ? -42.681 -10.144  -13.524 1.00 57.24  ? 110 GLU   E O      1 
ATOM   14224 C  CB     . GLU   E 3  108 ? -44.157 -12.245  -11.484 1.00 54.32  ? 110 GLU   E CB     1 
ATOM   14225 C  CG     . GLU   E 3  108 ? -45.054 -13.437  -11.343 1.00 68.61  ? 110 GLU   E CG     1 
ATOM   14226 C  CD     . GLU   E 3  108 ? -45.729 -13.529  -9.996  1.00 81.82  ? 110 GLU   E CD     1 
ATOM   14227 O  OE1    . GLU   E 3  108 ? -45.641 -12.559  -9.203  1.00 80.28  ? 110 GLU   E OE1    1 
ATOM   14228 O  OE2    . GLU   E 3  108 ? -46.373 -14.578  -9.755  1.00 85.17  ? 110 GLU   E OE2    1 
ATOM   14229 N  N      . ASN   E 3  109 ? -41.273 -11.138  -12.087 1.00 56.52  ? 111 ASN   E N      1 
ATOM   14230 C  CA     . ASN   E 3  109 ? -40.417 -9.968   -12.031 1.00 52.57  ? 111 ASN   E CA     1 
ATOM   14231 C  C      . ASN   E 3  109 ? -39.806 -9.691   -13.389 1.00 51.86  ? 111 ASN   E C      1 
ATOM   14232 O  O      . ASN   E 3  109 ? -39.992 -8.612   -13.952 1.00 51.94  ? 111 ASN   E O      1 
ATOM   14233 C  CB     . ASN   E 3  109 ? -39.351 -10.180  -10.981 1.00 49.41  ? 111 ASN   E CB     1 
ATOM   14234 C  CG     . ASN   E 3  109 ? -39.864 -9.859   -9.642  1.00 52.66  ? 111 ASN   E CG     1 
ATOM   14235 O  OD1    . ASN   E 3  109 ? -40.904 -9.210   -9.538  1.00 55.90  ? 111 ASN   E OD1    1 
ATOM   14236 N  ND2    . ASN   E 3  109 ? -39.154 -10.273  -8.594  1.00 54.30  ? 111 ASN   E ND2    1 
ATOM   14237 N  N      . ARG   E 3  110 ? -39.091 -10.674  -13.942 1.00 51.04  ? 112 ARG   E N      1 
ATOM   14238 C  CA     . ARG   E 3  110 ? -38.430 -10.491  -15.231 1.00 51.65  ? 112 ARG   E CA     1 
ATOM   14239 C  C      . ARG   E 3  110 ? -39.419 -10.051  -16.303 1.00 59.86  ? 112 ARG   E C      1 
ATOM   14240 O  O      . ARG   E 3  110 ? -39.134 -9.144   -17.105 1.00 53.47  ? 112 ARG   E O      1 
ATOM   14241 C  CB     . ARG   E 3  110 ? -37.729 -11.785  -15.642 1.00 44.30  ? 112 ARG   E CB     1 
ATOM   14242 C  CG     . ARG   E 3  110 ? -37.008 -11.672  -16.956 1.00 47.11  ? 112 ARG   E CG     1 
ATOM   14243 C  CD     . ARG   E 3  110 ? -36.067 -12.828  -17.201 1.00 46.51  ? 112 ARG   E CD     1 
ATOM   14244 N  NE     . ARG   E 3  110 ? -35.121 -12.560  -18.278 1.00 49.49  ? 112 ARG   E NE     1 
ATOM   14245 C  CZ     . ARG   E 3  110 ? -35.330 -12.853  -19.557 1.00 51.99  ? 112 ARG   E CZ     1 
ATOM   14246 N  NH1    . ARG   E 3  110 ? -36.451 -13.418  -19.962 1.00 48.74  ? 112 ARG   E NH1    1 
ATOM   14247 N  NH2    . ARG   E 3  110 ? -34.384 -12.580  -20.452 1.00 60.83  ? 112 ARG   E NH2    1 
ATOM   14248 N  N      . GLU   E 3  111 ? -40.599 -10.672  -16.314 1.00 57.61  ? 113 GLU   E N      1 
ATOM   14249 C  CA     . GLU   E 3  111 ? -41.612 -10.309  -17.290 1.00 54.60  ? 113 GLU   E CA     1 
ATOM   14250 C  C      . GLU   E 3  111 ? -42.055 -8.864   -17.095 1.00 55.98  ? 113 GLU   E C      1 
ATOM   14251 O  O      . GLU   E 3  111 ? -42.056 -8.073   -18.041 1.00 61.20  ? 113 GLU   E O      1 
ATOM   14252 C  CB     . GLU   E 3  111 ? -42.773 -11.292  -17.202 1.00 54.23  ? 113 GLU   E CB     1 
ATOM   14253 C  CG     . GLU   E 3  111 ? -42.435 -12.643  -17.851 1.00 50.32  ? 113 GLU   E CG     1 
ATOM   14254 C  CD     . GLU   E 3  111 ? -43.579 -13.659  -17.824 1.00 62.37  ? 113 GLU   E CD     1 
ATOM   14255 O  OE1    . GLU   E 3  111 ? -44.555 -13.497  -17.045 1.00 61.90  ? 113 GLU   E OE1    1 
ATOM   14256 O  OE2    . GLU   E 3  111 ? -43.471 -14.660  -18.557 1.00 69.82  ? 113 GLU   E OE2    1 
ATOM   14257 N  N      . ALA   E 3  112 ? -42.389 -8.482   -15.869 1.00 53.04  ? 114 ALA   E N      1 
ATOM   14258 C  CA     . ALA   E 3  112 ? -42.708 -7.086   -15.606 1.00 51.58  ? 114 ALA   E CA     1 
ATOM   14259 C  C      . ALA   E 3  112 ? -41.692 -6.175   -16.270 1.00 57.48  ? 114 ALA   E C      1 
ATOM   14260 O  O      . ALA   E 3  112 ? -42.046 -5.111   -16.785 1.00 59.60  ? 114 ALA   E O      1 
ATOM   14261 C  CB     . ALA   E 3  112 ? -42.739 -6.808   -14.105 1.00 56.07  ? 114 ALA   E CB     1 
ATOM   14262 N  N      . HIS   E 3  113 ? -40.423 -6.588   -16.264 1.00 61.76  ? 115 HIS   E N      1 
ATOM   14263 C  CA     . HIS   E 3  113 ? -39.371 -5.719   -16.777 1.00 59.99  ? 115 HIS   E CA     1 
ATOM   14264 C  C      . HIS   E 3  113 ? -39.414 -5.648   -18.291 1.00 59.06  ? 115 HIS   E C      1 
ATOM   14265 O  O      . HIS   E 3  113 ? -39.426 -4.558   -18.864 1.00 64.84  ? 115 HIS   E O      1 
ATOM   14266 C  CB     . HIS   E 3  113 ? -37.999 -6.181   -16.286 1.00 56.01  ? 115 HIS   E CB     1 
ATOM   14267 C  CG     . HIS   E 3  113 ? -37.738 -5.844   -14.849 1.00 66.41  ? 115 HIS   E CG     1 
ATOM   14268 N  ND1    . HIS   E 3  113 ? -38.407 -6.446   -13.801 1.00 66.61  ? 115 HIS   E ND1    1 
ATOM   14269 C  CD2    . HIS   E 3  113 ? -36.915 -4.925   -14.286 1.00 72.64  ? 115 HIS   E CD2    1 
ATOM   14270 C  CE1    . HIS   E 3  113 ? -37.979 -5.942   -12.655 1.00 67.01  ? 115 HIS   E CE1    1 
ATOM   14271 N  NE2    . HIS   E 3  113 ? -37.077 -5.013   -12.922 1.00 70.65  ? 115 HIS   E NE2    1 
ATOM   14272 N  N      . LEU   E 3  114 ? -39.447 -6.798   -18.960 1.00 57.84  ? 116 LEU   E N      1 
ATOM   14273 C  CA     . LEU   E 3  114 ? -39.572 -6.782   -20.412 1.00 57.15  ? 116 LEU   E CA     1 
ATOM   14274 C  C      . LEU   E 3  114 ? -40.878 -6.121   -20.836 1.00 59.92  ? 116 LEU   E C      1 
ATOM   14275 O  O      . LEU   E 3  114 ? -40.918 -5.379   -21.824 1.00 63.34  ? 116 LEU   E O      1 
ATOM   14276 C  CB     . LEU   E 3  114 ? -39.490 -8.205   -20.952 1.00 59.42  ? 116 LEU   E CB     1 
ATOM   14277 C  CG     . LEU   E 3  114 ? -38.069 -8.743   -21.015 1.00 63.64  ? 116 LEU   E CG     1 
ATOM   14278 C  CD1    . LEU   E 3  114 ? -38.055 -10.262  -21.066 1.00 66.14  ? 116 LEU   E CD1    1 
ATOM   14279 C  CD2    . LEU   E 3  114 ? -37.352 -8.142   -22.205 1.00 62.43  ? 116 LEU   E CD2    1 
ATOM   14280 N  N      . ALA   E 3  115 ? -41.958 -6.379   -20.093 1.00 57.73  ? 117 ALA   E N      1 
ATOM   14281 C  CA     . ALA   E 3  115 ? -43.250 -5.802   -20.435 1.00 55.18  ? 117 ALA   E CA     1 
ATOM   14282 C  C      . ALA   E 3  115 ? -43.233 -4.291   -20.318 1.00 60.93  ? 117 ALA   E C      1 
ATOM   14283 O  O      . ALA   E 3  115 ? -44.009 -3.608   -20.994 1.00 68.86  ? 117 ALA   E O      1 
ATOM   14284 C  CB     . ALA   E 3  115 ? -44.335 -6.381   -19.544 1.00 49.30  ? 117 ALA   E CB     1 
ATOM   14285 N  N      . ALA   E 3  116 ? -42.366 -3.753   -19.469 1.00 57.78  ? 118 ALA   E N      1 
ATOM   14286 C  CA     . ALA   E 3  116 ? -42.219 -2.315   -19.330 1.00 53.17  ? 118 ALA   E CA     1 
ATOM   14287 C  C      . ALA   E 3  116 ? -41.255 -1.735   -20.331 1.00 59.52  ? 118 ALA   E C      1 
ATOM   14288 O  O      . ALA   E 3  116 ? -41.426 -0.589   -20.739 1.00 69.16  ? 118 ALA   E O      1 
ATOM   14289 C  CB     . ALA   E 3  116 ? -41.733 -1.956   -17.930 1.00 59.23  ? 118 ALA   E CB     1 
ATOM   14290 N  N      . MET   E 3  117 ? -40.230 -2.489   -20.723 1.00 62.81  ? 119 MET   E N      1 
ATOM   14291 C  CA     . MET   E 3  117 ? -39.319 -1.988   -21.743 1.00 63.41  ? 119 MET   E CA     1 
ATOM   14292 C  C      . MET   E 3  117 ? -40.052 -1.794   -23.050 1.00 66.95  ? 119 MET   E C      1 
ATOM   14293 O  O      . MET   E 3  117 ? -39.752 -0.860   -23.802 1.00 70.16  ? 119 MET   E O      1 
ATOM   14294 C  CB     . MET   E 3  117 ? -38.145 -2.939   -21.947 1.00 64.18  ? 119 MET   E CB     1 
ATOM   14295 C  CG     . MET   E 3  117 ? -37.174 -2.448   -23.025 1.00 74.35  ? 119 MET   E CG     1 
ATOM   14296 S  SD     . MET   E 3  117 ? -35.995 -3.689   -23.626 1.00 87.50  ? 119 MET   E SD     1 
ATOM   14297 C  CE     . MET   E 3  117 ? -35.601 -4.592   -22.127 1.00 66.53  ? 119 MET   E CE     1 
ATOM   14298 N  N      . LEU   E 3  118 ? -41.009 -2.684   -23.333 1.00 66.53  ? 120 LEU   E N      1 
ATOM   14299 C  CA     . LEU   E 3  118 ? -41.843 -2.573   -24.525 1.00 62.33  ? 120 LEU   E CA     1 
ATOM   14300 C  C      . LEU   E 3  118 ? -42.846 -1.424   -24.395 1.00 63.01  ? 120 LEU   E C      1 
ATOM   14301 O  O      . LEU   E 3  118 ? -42.844 -0.490   -25.202 1.00 68.67  ? 120 LEU   E O      1 
ATOM   14302 C  CB     . LEU   E 3  118 ? -42.541 -3.912   -24.782 1.00 59.41  ? 120 LEU   E CB     1 
ATOM   14303 C  CG     . LEU   E 3  118 ? -41.639 -5.133   -25.033 1.00 61.25  ? 120 LEU   E CG     1 
ATOM   14304 C  CD1    . LEU   E 3  118 ? -42.461 -6.382   -25.200 1.00 73.39  ? 120 LEU   E CD1    1 
ATOM   14305 C  CD2    . LEU   E 3  118 ? -40.799 -4.961   -26.274 1.00 59.51  ? 120 LEU   E CD2    1 
ATOM   14306 N  N      . GLU   E 3  119 ? -43.692 -1.449   -23.367 1.00 63.10  ? 121 GLU   E N      1 
ATOM   14307 C  CA     . GLU   E 3  119 ? -44.673 -0.380   -23.212 1.00 67.62  ? 121 GLU   E CA     1 
ATOM   14308 C  C      . GLU   E 3  119 ? -44.075 1.008    -23.389 1.00 75.31  ? 121 GLU   E C      1 
ATOM   14309 O  O      . GLU   E 3  119 ? -44.809 1.947    -23.721 1.00 81.46  ? 121 GLU   E O      1 
ATOM   14310 C  CB     . GLU   E 3  119 ? -45.355 -0.444   -21.853 1.00 71.64  ? 121 GLU   E CB     1 
ATOM   14311 C  CG     . GLU   E 3  119 ? -46.426 0.614    -21.699 1.00 79.23  ? 121 GLU   E CG     1 
ATOM   14312 C  CD     . GLU   E 3  119 ? -47.325 0.383    -20.499 1.00 96.32  ? 121 GLU   E CD     1 
ATOM   14313 O  OE1    . GLU   E 3  119 ? -47.067 -0.587   -19.749 1.00 107.47 ? 121 GLU   E OE1    1 
ATOM   14314 O  OE2    . GLU   E 3  119 ? -48.270 1.183    -20.290 1.00 94.07  ? 121 GLU   E OE2    1 
ATOM   14315 N  N      . ARG   E 3  120 ? -42.771 1.176    -23.183 1.00 71.21  ? 122 ARG   E N      1 
ATOM   14316 C  CA     . ARG   E 3  120 ? -42.179 2.463    -23.519 1.00 72.60  ? 122 ARG   E CA     1 
ATOM   14317 C  C      . ARG   E 3  120 ? -41.644 2.481    -24.941 1.00 68.21  ? 122 ARG   E C      1 
ATOM   14318 O  O      . ARG   E 3  120 ? -41.734 3.508    -25.609 1.00 75.94  ? 122 ARG   E O      1 
ATOM   14319 C  CB     . ARG   E 3  120 ? -41.069 2.838    -22.531 1.00 64.82  ? 122 ARG   E CB     1 
ATOM   14320 C  CG     . ARG   E 3  120 ? -39.831 1.996    -22.667 1.00 73.88  ? 122 ARG   E CG     1 
ATOM   14321 C  CD     . ARG   E 3  120 ? -38.680 2.497    -21.806 1.00 76.64  ? 122 ARG   E CD     1 
ATOM   14322 N  NE     . ARG   E 3  120 ? -38.896 2.149    -20.405 1.00 81.98  ? 122 ARG   E NE     1 
ATOM   14323 C  CZ     . ARG   E 3  120 ? -38.233 1.200    -19.752 1.00 77.97  ? 122 ARG   E CZ     1 
ATOM   14324 N  NH1    . ARG   E 3  120 ? -37.296 0.476    -20.344 1.00 72.69  ? 122 ARG   E NH1    1 
ATOM   14325 N  NH2    . ARG   E 3  120 ? -38.540 0.950    -18.481 1.00 76.40  ? 122 ARG   E NH2    1 
ATOM   14326 N  N      . LEU   E 3  121 ? -41.112 1.369    -25.437 1.00 68.38  ? 123 LEU   E N      1 
ATOM   14327 C  CA     . LEU   E 3  121 ? -40.702 1.336    -26.833 1.00 68.30  ? 123 LEU   E CA     1 
ATOM   14328 C  C      . LEU   E 3  121 ? -41.881 1.616    -27.745 1.00 72.44  ? 123 LEU   E C      1 
ATOM   14329 O  O      . LEU   E 3  121 ? -41.736 2.298    -28.766 1.00 76.55  ? 123 LEU   E O      1 
ATOM   14330 C  CB     . LEU   E 3  121 ? -40.085 -0.014   -27.190 1.00 66.46  ? 123 LEU   E CB     1 
ATOM   14331 C  CG     . LEU   E 3  121 ? -38.573 -0.173   -27.103 1.00 65.71  ? 123 LEU   E CG     1 
ATOM   14332 C  CD1    . LEU   E 3  121 ? -38.184 -1.569   -27.536 1.00 67.01  ? 123 LEU   E CD1    1 
ATOM   14333 C  CD2    . LEU   E 3  121 ? -37.854 0.879    -27.934 1.00 67.98  ? 123 LEU   E CD2    1 
ATOM   14334 N  N      . GLN   E 3  122 ? -43.055 1.088    -27.402 1.00 72.37  ? 124 GLN   E N      1 
ATOM   14335 C  CA     . GLN   E 3  122 ? -44.219 1.272    -28.257 1.00 78.39  ? 124 GLN   E CA     1 
ATOM   14336 C  C      . GLN   E 3  122 ? -44.828 2.660    -28.090 1.00 78.14  ? 124 GLN   E C      1 
ATOM   14337 O  O      . GLN   E 3  122 ? -45.296 3.248    -29.068 1.00 75.80  ? 124 GLN   E O      1 
ATOM   14338 C  CB     . GLN   E 3  122 ? -45.243 0.158    -28.000 1.00 77.63  ? 124 GLN   E CB     1 
ATOM   14339 C  CG     . GLN   E 3  122 ? -45.668 -0.034   -26.557 1.00 79.70  ? 124 GLN   E CG     1 
ATOM   14340 C  CD     . GLN   E 3  122 ? -46.921 0.759    -26.179 1.00 91.31  ? 124 GLN   E CD     1 
ATOM   14341 O  OE1    . GLN   E 3  122 ? -47.313 1.702    -26.877 1.00 95.10  ? 124 GLN   E OE1    1 
ATOM   14342 N  NE2    . GLN   E 3  122 ? -47.556 0.374    -25.062 1.00 89.58  ? 124 GLN   E NE2    1 
ATOM   14343 N  N      . GLU   E 3  123 ? -44.791 3.227    -26.888 1.00 78.85  ? 125 GLU   E N      1 
ATOM   14344 C  CA     . GLU   E 3  123 ? -45.104 4.641    -26.767 1.00 76.95  ? 125 GLU   E CA     1 
ATOM   14345 C  C      . GLU   E 3  123 ? -44.178 5.511    -27.628 1.00 77.38  ? 125 GLU   E C      1 
ATOM   14346 O  O      . GLU   E 3  123 ? -44.483 6.687    -27.844 1.00 81.58  ? 125 GLU   E O      1 
ATOM   14347 C  CB     . GLU   E 3  123 ? -45.031 5.026    -25.286 1.00 79.27  ? 125 GLU   E CB     1 
ATOM   14348 C  CG     . GLU   E 3  123 ? -45.048 6.509    -24.984 1.00 86.82  ? 125 GLU   E CG     1 
ATOM   14349 C  CD     . GLU   E 3  123 ? -46.142 7.262    -25.724 1.00 97.64  ? 125 GLU   E CD     1 
ATOM   14350 O  OE1    . GLU   E 3  123 ? -46.979 6.602    -26.388 1.00 95.59  ? 125 GLU   E OE1    1 
ATOM   14351 O  OE2    . GLU   E 3  123 ? -46.152 8.517    -25.647 1.00 97.68  ? 125 GLU   E OE2    1 
ATOM   14352 N  N      . LYS   E 3  124 ? -43.063 4.965    -28.136 1.00 75.66  ? 126 LYS   E N      1 
ATOM   14353 C  CA     . LYS   E 3  124 ? -42.276 5.658    -29.154 1.00 76.67  ? 126 LYS   E CA     1 
ATOM   14354 C  C      . LYS   E 3  124 ? -42.980 5.663    -30.507 1.00 80.60  ? 126 LYS   E C      1 
ATOM   14355 O  O      . LYS   E 3  124 ? -43.010 6.692    -31.191 1.00 83.16  ? 126 LYS   E O      1 
ATOM   14356 C  CB     . LYS   E 3  124 ? -40.889 5.021    -29.298 1.00 77.18  ? 126 LYS   E CB     1 
ATOM   14357 C  CG     . LYS   E 3  124 ? -39.928 5.235    -28.135 1.00 76.65  ? 126 LYS   E CG     1 
ATOM   14358 C  CD     . LYS   E 3  124 ? -38.460 5.105    -28.601 1.00 75.33  ? 126 LYS   E CD     1 
ATOM   14359 C  CE     . LYS   E 3  124 ? -37.881 6.395    -29.200 1.00 73.95  ? 126 LYS   E CE     1 
ATOM   14360 N  NZ     . LYS   E 3  124 ? -37.587 7.445    -28.173 1.00 75.10  ? 126 LYS   E NZ     1 
ATOM   14361 N  N      . ASP   E 3  125 ? -43.533 4.523    -30.921 1.00 79.04  ? 127 ASP   E N      1 
ATOM   14362 C  CA     . ASP   E 3  125 ? -44.228 4.459    -32.205 1.00 82.66  ? 127 ASP   E CA     1 
ATOM   14363 C  C      . ASP   E 3  125 ? -45.411 5.417    -32.236 1.00 81.48  ? 127 ASP   E C      1 
ATOM   14364 O  O      . ASP   E 3  125 ? -45.694 6.034    -33.268 1.00 81.79  ? 127 ASP   E O      1 
ATOM   14365 C  CB     . ASP   E 3  125 ? -44.696 3.030    -32.471 1.00 80.26  ? 127 ASP   E CB     1 
ATOM   14366 C  CG     . ASP   E 3  125 ? -43.581 2.022    -32.309 1.00 82.28  ? 127 ASP   E CG     1 
ATOM   14367 O  OD1    . ASP   E 3  125 ? -42.503 2.419    -31.814 1.00 85.85  ? 127 ASP   E OD1    1 
ATOM   14368 O  OD2    . ASP   E 3  125 ? -43.778 0.839    -32.645 1.00 82.47  ? 127 ASP   E OD2    1 
ATOM   14369 N  N      . LYS   E 3  126 ? -46.111 5.550    -31.107 1.00 75.69  ? 128 LYS   E N      1 
ATOM   14370 C  CA     . LYS   E 3  126 ? -47.247 6.455    -31.035 1.00 77.69  ? 128 LYS   E CA     1 
ATOM   14371 C  C      . LYS   E 3  126 ? -46.797 7.901    -31.197 1.00 88.77  ? 128 LYS   E C      1 
ATOM   14372 O  O      . LYS   E 3  126 ? -47.484 8.706    -31.842 1.00 96.51  ? 128 LYS   E O      1 
ATOM   14373 C  CB     . LYS   E 3  126 ? -47.984 6.256    -29.713 1.00 84.18  ? 128 LYS   E CB     1 
ATOM   14374 C  CG     . LYS   E 3  126 ? -49.231 7.112    -29.540 1.00 95.72  ? 128 LYS   E CG     1 
ATOM   14375 C  CD     . LYS   E 3  126 ? -49.898 7.391    -30.895 1.00 103.63 ? 128 LYS   E CD     1 
ATOM   14376 C  CE     . LYS   E 3  126 ? -51.089 8.321    -30.764 1.00 99.52  ? 128 LYS   E CE     1 
ATOM   14377 N  NZ     . LYS   E 3  126 ? -52.274 7.546    -30.311 1.00 110.05 ? 128 LYS   E NZ     1 
ATOM   14378 N  N      . HIS   E 3  127 ? -45.637 8.250    -30.633 1.00 81.99  ? 129 HIS   E N      1 
ATOM   14379 C  CA     . HIS   E 3  127 ? -45.052 9.554    -30.917 1.00 81.83  ? 129 HIS   E CA     1 
ATOM   14380 C  C      . HIS   E 3  127 ? -44.499 9.650    -32.337 1.00 85.06  ? 129 HIS   E C      1 
ATOM   14381 O  O      . HIS   E 3  127 ? -44.339 10.757   -32.852 1.00 86.69  ? 129 HIS   E O      1 
ATOM   14382 C  CB     . HIS   E 3  127 ? -43.943 9.855    -29.925 1.00 81.54  ? 129 HIS   E CB     1 
ATOM   14383 C  CG     . HIS   E 3  127 ? -43.139 11.071   -30.265 1.00 82.90  ? 129 HIS   E CG     1 
ATOM   14384 N  ND1    . HIS   E 3  127 ? -43.413 12.315   -29.735 1.00 80.67  ? 129 HIS   E ND1    1 
ATOM   14385 C  CD2    . HIS   E 3  127 ? -42.067 11.236   -31.078 1.00 77.56  ? 129 HIS   E CD2    1 
ATOM   14386 C  CE1    . HIS   E 3  127 ? -42.539 13.190   -30.198 1.00 79.07  ? 129 HIS   E CE1    1 
ATOM   14387 N  NE2    . HIS   E 3  127 ? -41.714 12.562   -31.018 1.00 77.74  ? 129 HIS   E NE2    1 
ATOM   14388 N  N      . ALA   E 3  128 ? -44.174 8.533    -32.982 1.00 83.59  ? 130 ALA   E N      1 
ATOM   14389 C  CA     . ALA   E 3  128 ? -43.847 8.627    -34.397 1.00 84.22  ? 130 ALA   E CA     1 
ATOM   14390 C  C      . ALA   E 3  128 ? -45.096 8.878    -35.224 1.00 92.93  ? 130 ALA   E C      1 
ATOM   14391 O  O      . ALA   E 3  128 ? -45.009 9.447    -36.318 1.00 92.34  ? 130 ALA   E O      1 
ATOM   14392 C  CB     . ALA   E 3  128 ? -43.147 7.356    -34.872 1.00 91.04  ? 130 ALA   E CB     1 
ATOM   14393 N  N      . GLU   E 3  129 ? -46.263 8.461    -34.721 1.00 96.67  ? 131 GLU   E N      1 
ATOM   14394 C  CA     . GLU   E 3  129 ? -47.512 8.733    -35.421 1.00 93.21  ? 131 GLU   E CA     1 
ATOM   14395 C  C      . GLU   E 3  129 ? -47.886 10.198   -35.267 1.00 92.68  ? 131 GLU   E C      1 
ATOM   14396 O  O      . GLU   E 3  129 ? -48.139 10.892   -36.256 1.00 97.09  ? 131 GLU   E O      1 
ATOM   14397 C  CB     . GLU   E 3  129 ? -48.636 7.843    -34.889 1.00 88.68  ? 131 GLU   E CB     1 
ATOM   14398 C  CG     . GLU   E 3  129 ? -48.342 6.361    -34.998 1.00 89.66  ? 131 GLU   E CG     1 
ATOM   14399 C  CD     . GLU   E 3  129 ? -47.842 5.958    -36.360 1.00 88.14  ? 131 GLU   E CD     1 
ATOM   14400 O  OE1    . GLU   E 3  129 ? -46.797 6.487    -36.796 1.00 89.97  ? 131 GLU   E OE1    1 
ATOM   14401 O  OE2    . GLU   E 3  129 ? -48.465 5.085    -36.984 1.00 93.75  ? 131 GLU   E OE2    1 
ATOM   14402 N  N      . GLU   E 3  130 ? -47.915 10.688   -34.028 1.00 92.21  ? 132 GLU   E N      1 
ATOM   14403 C  CA     . GLU   E 3  130 ? -48.231 12.092   -33.809 1.00 94.99  ? 132 GLU   E CA     1 
ATOM   14404 C  C      . GLU   E 3  130 ? -47.251 13.017   -34.507 1.00 97.22  ? 132 GLU   E C      1 
ATOM   14405 O  O      . GLU   E 3  130 ? -47.630 14.115   -34.930 1.00 105.21 ? 132 GLU   E O      1 
ATOM   14406 C  CB     . GLU   E 3  130 ? -48.258 12.398   -32.324 1.00 91.17  ? 132 GLU   E CB     1 
ATOM   14407 C  CG     . GLU   E 3  130 ? -49.412 11.750   -31.643 1.00 101.80 ? 132 GLU   E CG     1 
ATOM   14408 C  CD     . GLU   E 3  130 ? -49.542 12.212   -30.221 1.00 121.18 ? 132 GLU   E CD     1 
ATOM   14409 O  OE1    . GLU   E 3  130 ? -48.893 13.222   -29.866 1.00 121.77 ? 132 GLU   E OE1    1 
ATOM   14410 O  OE2    . GLU   E 3  130 ? -50.307 11.579   -29.464 1.00 129.42 ? 132 GLU   E OE2    1 
ATOM   14411 N  N      . VAL   E 3  131 ? -45.989 12.611   -34.620 1.00 96.67  ? 133 VAL   E N      1 
ATOM   14412 C  CA     . VAL   E 3  131 ? -45.007 13.468   -35.275 1.00 99.97  ? 133 VAL   E CA     1 
ATOM   14413 C  C      . VAL   E 3  131 ? -45.300 13.565   -36.766 1.00 96.70  ? 133 VAL   E C      1 
ATOM   14414 O  O      . VAL   E 3  131 ? -45.217 14.648   -37.357 1.00 96.15  ? 133 VAL   E O      1 
ATOM   14415 C  CB     . VAL   E 3  131 ? -43.580 12.956   -34.995 1.00 93.42  ? 133 VAL   E CB     1 
ATOM   14416 C  CG1    . VAL   E 3  131 ? -43.366 11.604   -35.653 1.00 94.93  ? 133 VAL   E CG1    1 
ATOM   14417 C  CG2    . VAL   E 3  131 ? -42.540 13.955   -35.472 1.00 86.27  ? 133 VAL   E CG2    1 
ATOM   14418 N  N      . ARG   E 3  132 ? -45.677 12.443   -37.390 1.00 97.40  ? 134 ARG   E N      1 
ATOM   14419 C  CA     . ARG   E 3  132 ? -45.970 12.422   -38.819 1.00 91.59  ? 134 ARG   E CA     1 
ATOM   14420 C  C      . ARG   E 3  132 ? -47.340 13.021   -39.123 1.00 96.40  ? 134 ARG   E C      1 
ATOM   14421 O  O      . ARG   E 3  132 ? -47.549 13.562   -40.215 1.00 98.01  ? 134 ARG   E O      1 
ATOM   14422 C  CB     . ARG   E 3  132 ? -45.900 10.987   -39.334 1.00 85.97  ? 134 ARG   E CB     1 
ATOM   14423 C  CG     . ARG   E 3  132 ? -44.512 10.518   -39.716 1.00 86.41  ? 134 ARG   E CG     1 
ATOM   14424 C  CD     . ARG   E 3  132 ? -44.571 9.140    -40.379 1.00 88.58  ? 134 ARG   E CD     1 
ATOM   14425 N  NE     . ARG   E 3  132 ? -45.015 8.095    -39.460 1.00 91.51  ? 134 ARG   E NE     1 
ATOM   14426 C  CZ     . ARG   E 3  132 ? -44.237 7.453    -38.599 1.00 89.79  ? 134 ARG   E CZ     1 
ATOM   14427 N  NH1    . ARG   E 3  132 ? -42.935 7.673    -38.542 1.00 86.16  ? 134 ARG   E NH1    1 
ATOM   14428 N  NH2    . ARG   E 3  132 ? -44.780 6.555    -37.783 1.00 90.54  ? 134 ARG   E NH2    1 
ATOM   14429 N  N      . LYS   E 3  133 ? -48.279 12.929   -38.175 1.00 94.29  ? 135 LYS   E N      1 
ATOM   14430 C  CA     . LYS   E 3  133 ? -49.583 13.562   -38.338 1.00 93.99  ? 135 LYS   E CA     1 
ATOM   14431 C  C      . LYS   E 3  133 ? -49.491 15.084   -38.285 1.00 98.27  ? 135 LYS   E C      1 
ATOM   14432 O  O      . LYS   E 3  133 ? -50.327 15.772   -38.880 1.00 104.94 ? 135 LYS   E O      1 
ATOM   14433 C  CB     . LYS   E 3  133 ? -50.550 13.049   -37.269 1.00 90.88  ? 135 LYS   E CB     1 
ATOM   14434 C  CG     . LYS   E 3  133 ? -51.184 11.705   -37.568 1.00 93.76  ? 135 LYS   E CG     1 
ATOM   14435 C  CD     . LYS   E 3  133 ? -52.587 11.635   -36.961 1.00 97.78  ? 135 LYS   E CD     1 
ATOM   14436 C  CE     . LYS   E 3  133 ? -53.529 12.668   -37.573 1.00 99.44  ? 135 LYS   E CE     1 
ATOM   14437 N  NZ     . LYS   E 3  133 ? -54.857 12.686   -36.900 1.00 98.58  ? 135 LYS   E NZ     1 
ATOM   14438 N  N      . ASN   E 3  134 ? -48.504 15.636   -37.586 1.00 92.60  ? 136 ASN   E N      1 
ATOM   14439 C  CA     . ASN   E 3  134 ? -48.380 17.086   -37.588 1.00 95.32  ? 136 ASN   E CA     1 
ATOM   14440 C  C      . ASN   E 3  134 ? -47.825 17.613   -38.904 1.00 100.82 ? 136 ASN   E C      1 
ATOM   14441 O  O      . ASN   E 3  134 ? -48.174 18.726   -39.312 1.00 104.10 ? 136 ASN   E O      1 
ATOM   14442 C  CB     . ASN   E 3  134 ? -47.530 17.537   -36.411 1.00 97.22  ? 136 ASN   E CB     1 
ATOM   14443 C  CG     . ASN   E 3  134 ? -48.371 17.970   -35.255 1.00 104.49 ? 136 ASN   E CG     1 
ATOM   14444 O  OD1    . ASN   E 3  134 ? -48.522 19.166   -34.997 1.00 107.22 ? 136 ASN   E OD1    1 
ATOM   14445 N  ND2    . ASN   E 3  134 ? -48.985 17.004   -34.583 1.00 102.48 ? 136 ASN   E ND2    1 
ATOM   14446 N  N      . LYS   E 3  135 ? -46.990 16.833   -39.593 1.00 98.99  ? 137 LYS   E N      1 
ATOM   14447 C  CA     . LYS   E 3  135 ? -46.488 17.236   -40.903 1.00 97.59  ? 137 LYS   E CA     1 
ATOM   14448 C  C      . LYS   E 3  135 ? -47.489 16.997   -42.032 1.00 107.03 ? 137 LYS   E C      1 
ATOM   14449 O  O      . LYS   E 3  135 ? -47.321 17.556   -43.122 1.00 109.72 ? 137 LYS   E O      1 
ATOM   14450 C  CB     . LYS   E 3  135 ? -45.186 16.502   -41.207 1.00 92.58  ? 137 LYS   E CB     1 
ATOM   14451 C  CG     . LYS   E 3  135 ? -44.649 16.726   -42.603 1.00 93.09  ? 137 LYS   E CG     1 
ATOM   14452 C  CD     . LYS   E 3  135 ? -43.208 16.274   -42.708 1.00 85.30  ? 137 LYS   E CD     1 
ATOM   14453 C  CE     . LYS   E 3  135 ? -42.832 16.118   -44.148 1.00 79.80  ? 137 LYS   E CE     1 
ATOM   14454 N  NZ     . LYS   E 3  135 ? -43.339 14.787   -44.605 1.00 71.78  ? 137 LYS   E NZ     1 
ATOM   14455 N  N      . GLU   E 3  136 ? -48.517 16.177   -41.805 1.00 107.69 ? 138 GLU   E N      1 
ATOM   14456 C  CA     . GLU   E 3  136 ? -49.651 16.126   -42.718 1.00 107.21 ? 138 GLU   E CA     1 
ATOM   14457 C  C      . GLU   E 3  136 ? -50.596 17.304   -42.507 1.00 108.02 ? 138 GLU   E C      1 
ATOM   14458 O  O      . GLU   E 3  136 ? -51.378 17.624   -43.410 1.00 109.24 ? 138 GLU   E O      1 
ATOM   14459 C  CB     . GLU   E 3  136 ? -50.393 14.798   -42.540 1.00 114.43 ? 138 GLU   E CB     1 
ATOM   14460 C  CG     . GLU   E 3  136 ? -49.572 13.578   -42.973 1.00 119.16 ? 138 GLU   E CG     1 
ATOM   14461 C  CD     . GLU   E 3  136 ? -50.416 12.433   -43.522 1.00 129.40 ? 138 GLU   E CD     1 
ATOM   14462 O  OE1    . GLU   E 3  136 ? -51.453 12.098   -42.906 1.00 127.13 ? 138 GLU   E OE1    1 
ATOM   14463 O  OE2    . GLU   E 3  136 ? -50.036 11.862   -44.568 1.00 132.71 ? 138 GLU   E OE2    1 
ATOM   14464 N  N      . LEU   E 3  137 ? -50.526 17.954   -41.339 1.00 107.32 ? 139 LEU   E N      1 
ATOM   14465 C  CA     . LEU   E 3  137 ? -51.226 19.199   -41.039 1.00 106.12 ? 139 LEU   E CA     1 
ATOM   14466 C  C      . LEU   E 3  137 ? -50.431 20.432   -41.478 1.00 106.44 ? 139 LEU   E C      1 
ATOM   14467 O  O      . LEU   E 3  137 ? -50.711 21.546   -41.021 1.00 98.86  ? 139 LEU   E O      1 
ATOM   14468 C  CB     . LEU   E 3  137 ? -51.527 19.268   -39.542 1.00 100.47 ? 139 LEU   E CB     1 
ATOM   14469 C  CG     . LEU   E 3  137 ? -52.388 20.440   -39.087 1.00 108.67 ? 139 LEU   E CG     1 
ATOM   14470 C  CD1    . LEU   E 3  137 ? -53.691 20.453   -39.879 1.00 110.18 ? 139 LEU   E CD1    1 
ATOM   14471 C  CD2    . LEU   E 3  137 ? -52.645 20.380   -37.586 1.00 105.90 ? 139 LEU   E CD2    1 
ATOM   14472 N  N      . LYS   E 3  138 ? -49.429 20.238   -42.333 1.00 107.62 ? 140 LYS   E N      1 
ATOM   14473 C  CA     . LYS   E 3  138 ? -48.660 21.297   -42.965 1.00 105.37 ? 140 LYS   E CA     1 
ATOM   14474 C  C      . LYS   E 3  138 ? -49.015 21.470   -44.437 1.00 114.11 ? 140 LYS   E C      1 
ATOM   14475 O  O      . LYS   E 3  138 ? -48.626 22.476   -45.045 1.00 116.81 ? 140 LYS   E O      1 
ATOM   14476 C  CB     . LYS   E 3  138 ? -47.161 20.989   -42.812 1.00 106.50 ? 140 LYS   E CB     1 
ATOM   14477 C  CG     . LYS   E 3  138 ? -46.165 21.973   -43.443 1.00 117.57 ? 140 LYS   E CG     1 
ATOM   14478 C  CD     . LYS   E 3  138 ? -44.817 21.247   -43.688 1.00 111.37 ? 140 LYS   E CD     1 
ATOM   14479 C  CE     . LYS   E 3  138 ? -43.717 22.132   -44.275 1.00 100.00 ? 140 LYS   E CE     1 
ATOM   14480 N  NZ     . LYS   E 3  138 ? -43.135 23.092   -43.283 1.00 91.96  ? 140 LYS   E NZ     1 
ATOM   14481 N  N      . GLU   E 3  139 ? -49.753 20.527   -45.017 1.00 113.04 ? 141 GLU   E N      1 
ATOM   14482 C  CA     . GLU   E 3  139 ? -50.203 20.620   -46.402 1.00 114.93 ? 141 GLU   E CA     1 
ATOM   14483 C  C      . GLU   E 3  139 ? -51.698 20.304   -46.508 1.00 113.31 ? 141 GLU   E C      1 
ATOM   14484 O  O      . GLU   E 3  139 ? -52.519 20.844   -45.758 1.00 102.27 ? 141 GLU   E O      1 
ATOM   14485 C  CB     . GLU   E 3  139 ? -49.383 19.676   -47.293 1.00 115.31 ? 141 GLU   E CB     1 
ATOM   14486 C  CG     . GLU   E 3  139 ? -47.901 20.054   -47.397 1.00 117.52 ? 141 GLU   E CG     1 
ATOM   14487 C  CD     . GLU   E 3  139 ? -46.982 19.278   -46.445 1.00 112.44 ? 141 GLU   E CD     1 
ATOM   14488 O  OE1    . GLU   E 3  139 ? -46.634 18.112   -46.725 1.00 112.88 ? 141 GLU   E OE1    1 
ATOM   14489 O  OE2    . GLU   E 3  139 ? -46.597 19.847   -45.408 1.00 108.46 ? 141 GLU   E OE2    1 
ATOM   14490 N  N      . MET   F 4  1   ? 4.465   -55.981  58.715  1.00 68.82  ? 1   MET   F N      1 
ATOM   14491 C  CA     . MET   F 4  1   ? 3.832   -55.154  59.720  1.00 70.68  ? 1   MET   F CA     1 
ATOM   14492 C  C      . MET   F 4  1   ? 2.617   -55.794  60.362  1.00 69.69  ? 1   MET   F C      1 
ATOM   14493 O  O      . MET   F 4  1   ? 1.753   -56.353  59.700  1.00 72.93  ? 1   MET   F O      1 
ATOM   14494 C  CB     . MET   F 4  1   ? 3.426   -53.796  59.145  1.00 64.63  ? 1   MET   F CB     1 
ATOM   14495 C  CG     . MET   F 4  1   ? 4.560   -52.810  59.171  1.00 74.46  ? 1   MET   F CG     1 
ATOM   14496 S  SD     . MET   F 4  1   ? 4.000   -51.117  58.927  1.00 94.98  ? 1   MET   F SD     1 
ATOM   14497 C  CE     . MET   F 4  1   ? 2.946   -50.891  60.350  1.00 77.10  ? 1   MET   F CE     1 
ATOM   14498 N  N      . TYR   F 4  2   ? 2.577   -55.673  61.680  1.00 67.45  ? 2   TYR   F N      1 
ATOM   14499 C  CA     . TYR   F 4  2   ? 1.463   -56.103  62.497  1.00 65.06  ? 2   TYR   F CA     1 
ATOM   14500 C  C      . TYR   F 4  2   ? 0.451   -54.983  62.669  1.00 69.75  ? 2   TYR   F C      1 
ATOM   14501 O  O      . TYR   F 4  2   ? 0.808   -53.805  62.760  1.00 73.59  ? 2   TYR   F O      1 
ATOM   14502 C  CB     . TYR   F 4  2   ? 1.975   -56.529  63.856  1.00 65.20  ? 2   TYR   F CB     1 
ATOM   14503 C  CG     . TYR   F 4  2   ? 3.141   -57.467  63.789  1.00 63.73  ? 2   TYR   F CG     1 
ATOM   14504 C  CD1    . TYR   F 4  2   ? 2.986   -58.750  63.311  1.00 53.17  ? 2   TYR   F CD1    1 
ATOM   14505 C  CD2    . TYR   F 4  2   ? 4.397   -57.066  64.200  1.00 63.53  ? 2   TYR   F CD2    1 
ATOM   14506 C  CE1    . TYR   F 4  2   ? 4.034   -59.599  63.273  1.00 53.28  ? 2   TYR   F CE1    1 
ATOM   14507 C  CE2    . TYR   F 4  2   ? 5.450   -57.910  64.153  1.00 56.18  ? 2   TYR   F CE2    1 
ATOM   14508 C  CZ     . TYR   F 4  2   ? 5.264   -59.174  63.691  1.00 55.19  ? 2   TYR   F CZ     1 
ATOM   14509 O  OH     . TYR   F 4  2   ? 6.332   -60.025  63.643  1.00 65.75  ? 2   TYR   F OH     1 
ATOM   14510 N  N      . THR   F 4  3   ? -0.818  -55.357  62.736  1.00 63.72  ? 3   THR   F N      1 
ATOM   14511 C  CA     . THR   F 4  3   ? -1.858  -54.366  62.934  1.00 72.49  ? 3   THR   F CA     1 
ATOM   14512 C  C      . THR   F 4  3   ? -2.473  -54.503  64.319  1.00 70.18  ? 3   THR   F C      1 
ATOM   14513 O  O      . THR   F 4  3   ? -2.432  -55.564  64.949  1.00 66.83  ? 3   THR   F O      1 
ATOM   14514 C  CB     . THR   F 4  3   ? -2.959  -54.494  61.889  1.00 65.25  ? 3   THR   F CB     1 
ATOM   14515 O  OG1    . THR   F 4  3   ? -3.549  -55.785  62.018  1.00 63.65  ? 3   THR   F OG1    1 
ATOM   14516 C  CG2    . THR   F 4  3   ? -2.369  -54.357  60.506  1.00 69.73  ? 3   THR   F CG2    1 
ATOM   14517 N  N      . PHE   F 4  4   ? -3.077  -53.406  64.769  1.00 63.78  ? 4   PHE   F N      1 
ATOM   14518 C  CA     . PHE   F 4  4   ? -3.773  -53.403  66.038  1.00 64.09  ? 4   PHE   F CA     1 
ATOM   14519 C  C      . PHE   F 4  4   ? -4.885  -52.365  66.001  1.00 63.65  ? 4   PHE   F C      1 
ATOM   14520 O  O      . PHE   F 4  4   ? -4.810  -51.380  65.269  1.00 65.52  ? 4   PHE   F O      1 
ATOM   14521 C  CB     . PHE   F 4  4   ? -2.783  -53.171  67.184  1.00 67.68  ? 4   PHE   F CB     1 
ATOM   14522 C  CG     . PHE   F 4  4   ? -2.379  -51.735  67.381  1.00 71.93  ? 4   PHE   F CG     1 
ATOM   14523 C  CD1    . PHE   F 4  4   ? -3.159  -50.871  68.152  1.00 69.46  ? 4   PHE   F CD1    1 
ATOM   14524 C  CD2    . PHE   F 4  4   ? -1.194  -51.257  66.827  1.00 71.91  ? 4   PHE   F CD2    1 
ATOM   14525 C  CE1    . PHE   F 4  4   ? -2.775  -49.565  68.350  1.00 68.94  ? 4   PHE   F CE1    1 
ATOM   14526 C  CE2    . PHE   F 4  4   ? -0.806  -49.947  67.020  1.00 70.49  ? 4   PHE   F CE2    1 
ATOM   14527 C  CZ     . PHE   F 4  4   ? -1.597  -49.103  67.785  1.00 72.04  ? 4   PHE   F CZ     1 
ATOM   14528 N  N      . VAL   F 4  5   ? -5.939  -52.624  66.765  1.00 62.55  ? 5   VAL   F N      1 
ATOM   14529 C  CA     . VAL   F 4  5   ? -7.031  -51.680  66.937  1.00 64.00  ? 5   VAL   F CA     1 
ATOM   14530 C  C      . VAL   F 4  5   ? -6.957  -51.201  68.380  1.00 66.73  ? 5   VAL   F C      1 
ATOM   14531 O  O      . VAL   F 4  5   ? -6.121  -51.674  69.159  1.00 66.65  ? 5   VAL   F O      1 
ATOM   14532 C  CB     . VAL   F 4  5   ? -8.396  -52.321  66.641  1.00 63.81  ? 5   VAL   F CB     1 
ATOM   14533 C  CG1    . VAL   F 4  5   ? -8.413  -52.952  65.253  1.00 61.55  ? 5   VAL   F CG1    1 
ATOM   14534 C  CG2    . VAL   F 4  5   ? -8.714  -53.319  67.720  1.00 58.98  ? 5   VAL   F CG2    1 
ATOM   14535 N  N      . VAL   F 4  6   ? -7.851  -50.291  68.762  1.00 69.34  ? 6   VAL   F N      1 
ATOM   14536 C  CA     . VAL   F 4  6   ? -7.829  -49.700  70.099  1.00 61.16  ? 6   VAL   F CA     1 
ATOM   14537 C  C      . VAL   F 4  6   ? -9.238  -49.336  70.537  1.00 59.71  ? 6   VAL   F C      1 
ATOM   14538 O  O      . VAL   F 4  6   ? -9.829  -48.390  70.010  1.00 71.47  ? 6   VAL   F O      1 
ATOM   14539 C  CB     . VAL   F 4  6   ? -6.916  -48.462  70.145  1.00 60.99  ? 6   VAL   F CB     1 
ATOM   14540 C  CG1    . VAL   F 4  6   ? -7.144  -47.700  71.429  1.00 57.86  ? 6   VAL   F CG1    1 
ATOM   14541 C  CG2    . VAL   F 4  6   ? -5.442  -48.866  69.973  1.00 57.14  ? 6   VAL   F CG2    1 
ATOM   14542 N  N      . ARG   F 4  7   ? -9.769  -50.057  71.525  1.00 57.83  ? 7   ARG   F N      1 
ATOM   14543 C  CA     . ARG   F 4  7   ? -11.159 -49.917  71.929  1.00 59.70  ? 7   ARG   F CA     1 
ATOM   14544 C  C      . ARG   F 4  7   ? -11.357 -49.378  73.345  1.00 62.57  ? 7   ARG   F C      1 
ATOM   14545 O  O      . ARG   F 4  7   ? -12.502 -49.294  73.803  1.00 65.30  ? 7   ARG   F O      1 
ATOM   14546 C  CB     . ARG   F 4  7   ? -11.865 -51.264  71.756  1.00 59.47  ? 7   ARG   F CB     1 
ATOM   14547 C  CG     . ARG   F 4  7   ? -11.698 -51.769  70.322  1.00 65.07  ? 7   ARG   F CG     1 
ATOM   14548 C  CD     . ARG   F 4  7   ? -12.048 -53.222  70.172  1.00 60.23  ? 7   ARG   F CD     1 
ATOM   14549 N  NE     . ARG   F 4  7   ? -13.428 -53.500  70.543  1.00 62.69  ? 7   ARG   F NE     1 
ATOM   14550 C  CZ     . ARG   F 4  7   ? -14.429 -53.586  69.680  1.00 60.99  ? 7   ARG   F CZ     1 
ATOM   14551 N  NH1    . ARG   F 4  7   ? -14.235 -53.415  68.381  1.00 70.20  ? 7   ARG   F NH1    1 
ATOM   14552 N  NH2    . ARG   F 4  7   ? -15.647 -53.876  70.128  1.00 48.60  ? 7   ARG   F NH2    1 
ATOM   14553 N  N      . ASP   F 4  8   ? -10.294 -48.973  74.036  1.00 60.52  ? 8   ASP   F N      1 
ATOM   14554 C  CA     . ASP   F 4  8   ? -10.403 -48.311  75.336  1.00 68.51  ? 8   ASP   F CA     1 
ATOM   14555 C  C      . ASP   F 4  8   ? -9.604  -47.026  75.236  1.00 80.41  ? 8   ASP   F C      1 
ATOM   14556 O  O      . ASP   F 4  8   ? -8.378  -47.045  75.376  1.00 81.44  ? 8   ASP   F O      1 
ATOM   14557 C  CB     . ASP   F 4  8   ? -9.886  -49.168  76.484  1.00 76.82  ? 8   ASP   F CB     1 
ATOM   14558 C  CG     . ASP   F 4  8   ? -10.206 -48.566  77.844  1.00 81.40  ? 8   ASP   F CG     1 
ATOM   14559 O  OD1    . ASP   F 4  8   ? -10.483 -47.349  77.895  1.00 84.91  ? 8   ASP   F OD1    1 
ATOM   14560 O  OD2    . ASP   F 4  8   ? -10.161 -49.297  78.859  1.00 77.66  ? 8   ASP   F OD2    1 
ATOM   14561 N  N      . GLU   F 4  9   ? -10.303 -45.918  75.005  1.00 88.37  ? 9   GLU   F N      1 
ATOM   14562 C  CA     . GLU   F 4  9   ? -9.635  -44.634  74.851  1.00 85.73  ? 9   GLU   F CA     1 
ATOM   14563 C  C      . GLU   F 4  9   ? -9.184  -44.072  76.200  1.00 85.49  ? 9   GLU   F C      1 
ATOM   14564 O  O      . GLU   F 4  9   ? -8.213  -43.314  76.267  1.00 85.53  ? 9   GLU   F O      1 
ATOM   14565 C  CB     . GLU   F 4  9   ? -10.575 -43.669  74.133  1.00 87.79  ? 9   GLU   F CB     1 
ATOM   14566 C  CG     . GLU   F 4  9   ? -10.975 -44.123  72.732  1.00 88.28  ? 9   GLU   F CG     1 
ATOM   14567 C  CD     . GLU   F 4  9   ? -9.853  -43.992  71.718  1.00 94.73  ? 9   GLU   F CD     1 
ATOM   14568 O  OE1    . GLU   F 4  9   ? -8.886  -43.250  71.992  1.00 93.43  ? 9   GLU   F OE1    1 
ATOM   14569 O  OE2    . GLU   F 4  9   ? -9.936  -44.639  70.646  1.00 99.92  ? 9   GLU   F OE2    1 
ATOM   14570 N  N      . ASN   F 4  10  ? -9.848  -44.454  77.281  1.00 83.23  ? 10  ASN   F N      1 
ATOM   14571 C  CA     . ASN   F 4  10  ? -9.488  -43.997  78.612  1.00 80.66  ? 10  ASN   F CA     1 
ATOM   14572 C  C      . ASN   F 4  10  ? -8.312  -44.746  79.211  1.00 78.78  ? 10  ASN   F C      1 
ATOM   14573 O  O      . ASN   F 4  10  ? -8.099  -44.636  80.420  1.00 89.79  ? 10  ASN   F O      1 
ATOM   14574 C  CB     . ASN   F 4  10  ? -10.684 -44.140  79.555  1.00 84.09  ? 10  ASN   F CB     1 
ATOM   14575 C  CG     . ASN   F 4  10  ? -11.925 -43.501  79.005  1.00 90.66  ? 10  ASN   F CG     1 
ATOM   14576 O  OD1    . ASN   F 4  10  ? -12.025 -43.252  77.804  1.00 89.65  ? 10  ASN   F OD1    1 
ATOM   14577 N  ND2    . ASN   F 4  10  ? -12.891 -43.240  79.875  1.00 100.97 ? 10  ASN   F ND2    1 
ATOM   14578 N  N      . SER   F 4  11  ? -7.550  -45.513  78.448  1.00 72.54  ? 11  SER   F N      1 
ATOM   14579 C  CA     . SER   F 4  11  ? -6.493  -46.318  79.057  1.00 81.66  ? 11  SER   F CA     1 
ATOM   14580 C  C      . SER   F 4  11  ? -5.184  -45.531  79.017  1.00 78.77  ? 11  SER   F C      1 
ATOM   14581 O  O      . SER   F 4  11  ? -4.474  -45.516  78.003  1.00 77.72  ? 11  SER   F O      1 
ATOM   14582 C  CB     . SER   F 4  11  ? -6.371  -47.676  78.372  1.00 85.08  ? 11  SER   F CB     1 
ATOM   14583 O  OG     . SER   F 4  11  ? -5.323  -48.456  78.942  1.00 77.64  ? 11  SER   F OG     1 
ATOM   14584 N  N      . SER   F 4  12  ? -4.862  -44.879  80.137  1.00 73.71  ? 12  SER   F N      1 
ATOM   14585 C  CA     . SER   F 4  12  ? -3.582  -44.188  80.249  1.00 75.26  ? 12  SER   F CA     1 
ATOM   14586 C  C      . SER   F 4  12  ? -2.417  -45.120  79.934  1.00 74.39  ? 12  SER   F C      1 
ATOM   14587 O  O      . SER   F 4  12  ? -1.442  -44.720  79.288  1.00 70.06  ? 12  SER   F O      1 
ATOM   14588 C  CB     . SER   F 4  12  ? -3.457  -43.565  81.644  1.00 65.69  ? 12  SER   F CB     1 
ATOM   14589 O  OG     . SER   F 4  12  ? -3.903  -44.445  82.654  1.00 70.75  ? 12  SER   F OG     1 
ATOM   14590 N  N      . VAL   F 4  13  ? -2.522  -46.378  80.338  1.00 75.19  ? 13  VAL   F N      1 
ATOM   14591 C  CA     . VAL   F 4  13  ? -1.461  -47.346  80.094  1.00 78.42  ? 13  VAL   F CA     1 
ATOM   14592 C  C      . VAL   F 4  13  ? -1.316  -47.645  78.611  1.00 73.74  ? 13  VAL   F C      1 
ATOM   14593 O  O      . VAL   F 4  13  ? -0.301  -47.303  78.000  1.00 73.37  ? 13  VAL   F O      1 
ATOM   14594 C  CB     . VAL   F 4  13  ? -1.723  -48.636  80.886  1.00 79.45  ? 13  VAL   F CB     1 
ATOM   14595 C  CG1    . VAL   F 4  13  ? -0.558  -49.607  80.730  1.00 70.85  ? 13  VAL   F CG1    1 
ATOM   14596 C  CG2    . VAL   F 4  13  ? -1.966  -48.295  82.341  1.00 71.51  ? 13  VAL   F CG2    1 
ATOM   14597 N  N      . TYR   F 4  14  ? -2.318  -48.305  78.027  1.00 74.45  ? 14  TYR   F N      1 
ATOM   14598 C  CA     . TYR   F 4  14  ? -2.235  -48.722  76.630  1.00 78.69  ? 14  TYR   F CA     1 
ATOM   14599 C  C      . TYR   F 4  14  ? -2.334  -47.549  75.664  1.00 78.50  ? 14  TYR   F C      1 
ATOM   14600 O  O      . TYR   F 4  14  ? -1.994  -47.711  74.485  1.00 71.82  ? 14  TYR   F O      1 
ATOM   14601 C  CB     . TYR   F 4  14  ? -3.312  -49.774  76.334  1.00 75.63  ? 14  TYR   F CB     1 
ATOM   14602 C  CG     . TYR   F 4  14  ? -3.136  -51.029  77.163  1.00 68.33  ? 14  TYR   F CG     1 
ATOM   14603 C  CD1    . TYR   F 4  14  ? -2.210  -51.999  76.804  1.00 68.63  ? 14  TYR   F CD1    1 
ATOM   14604 C  CD2    . TYR   F 4  14  ? -3.875  -51.228  78.317  1.00 62.33  ? 14  TYR   F CD2    1 
ATOM   14605 C  CE1    . TYR   F 4  14  ? -2.029  -53.140  77.576  1.00 66.13  ? 14  TYR   F CE1    1 
ATOM   14606 C  CE2    . TYR   F 4  14  ? -3.700  -52.353  79.092  1.00 61.35  ? 14  TYR   F CE2    1 
ATOM   14607 C  CZ     . TYR   F 4  14  ? -2.783  -53.313  78.721  1.00 65.04  ? 14  TYR   F CZ     1 
ATOM   14608 O  OH     . TYR   F 4  14  ? -2.633  -54.450  79.499  1.00 62.29  ? 14  TYR   F OH     1 
ATOM   14609 N  N      . ALA   F 4  15  ? -2.793  -46.383  76.131  1.00 77.97  ? 15  ALA   F N      1 
ATOM   14610 C  CA     . ALA   F 4  15  ? -2.483  -45.141  75.435  1.00 73.93  ? 15  ALA   F CA     1 
ATOM   14611 C  C      . ALA   F 4  15  ? -1.008  -45.123  75.039  1.00 70.49  ? 15  ALA   F C      1 
ATOM   14612 O  O      . ALA   F 4  15  ? -0.657  -44.878  73.881  1.00 69.53  ? 15  ALA   F O      1 
ATOM   14613 C  CB     . ALA   F 4  15  ? -2.833  -43.943  76.325  1.00 62.73  ? 15  ALA   F CB     1 
ATOM   14614 N  N      . GLU   F 4  16  ? -0.132  -45.410  76.001  1.00 78.80  ? 16  GLU   F N      1 
ATOM   14615 C  CA     . GLU   F 4  16  ? 1.299   -45.487  75.722  1.00 78.79  ? 16  GLU   F CA     1 
ATOM   14616 C  C      . GLU   F 4  16  ? 1.602   -46.639  74.776  1.00 82.13  ? 16  GLU   F C      1 
ATOM   14617 O  O      . GLU   F 4  16  ? 2.339   -46.476  73.797  1.00 82.95  ? 16  GLU   F O      1 
ATOM   14618 C  CB     . GLU   F 4  16  ? 2.078   -45.652  77.031  1.00 79.26  ? 16  GLU   F CB     1 
ATOM   14619 C  CG     . GLU   F 4  16  ? 2.735   -44.392  77.570  1.00 78.89  ? 16  GLU   F CG     1 
ATOM   14620 C  CD     . GLU   F 4  16  ? 4.029   -44.035  76.869  1.00 82.35  ? 16  GLU   F CD     1 
ATOM   14621 O  OE1    . GLU   F 4  16  ? 5.022   -44.758  77.066  1.00 84.67  ? 16  GLU   F OE1    1 
ATOM   14622 O  OE2    . GLU   F 4  16  ? 4.066   -43.017  76.144  1.00 83.43  ? 16  GLU   F OE2    1 
ATOM   14623 N  N      . VAL   F 4  17  ? 1.028   -47.814  75.049  1.00 83.50  ? 17  VAL   F N      1 
ATOM   14624 C  CA     . VAL   F 4  17  ? 1.360   -49.007  74.273  1.00 82.48  ? 17  VAL   F CA     1 
ATOM   14625 C  C      . VAL   F 4  17  ? 1.033   -48.806  72.796  1.00 85.15  ? 17  VAL   F C      1 
ATOM   14626 O  O      . VAL   F 4  17  ? 1.784   -49.253  71.918  1.00 86.07  ? 17  VAL   F O      1 
ATOM   14627 C  CB     . VAL   F 4  17  ? 0.647   -50.233  74.867  1.00 81.78  ? 17  VAL   F CB     1 
ATOM   14628 C  CG1    . VAL   F 4  17  ? 0.989   -51.486  74.076  1.00 80.25  ? 17  VAL   F CG1    1 
ATOM   14629 C  CG2    . VAL   F 4  17  ? 1.040   -50.397  76.333  1.00 80.33  ? 17  VAL   F CG2    1 
ATOM   14630 N  N      . SER   F 4  18  ? -0.080  -48.128  72.492  1.00 82.90  ? 18  SER   F N      1 
ATOM   14631 C  CA     . SER   F 4  18  ? -0.332  -47.730  71.109  1.00 79.68  ? 18  SER   F CA     1 
ATOM   14632 C  C      . SER   F 4  18  ? 0.745   -46.780  70.614  1.00 83.76  ? 18  SER   F C      1 
ATOM   14633 O  O      . SER   F 4  18  ? 1.289   -46.962  69.517  1.00 82.12  ? 18  SER   F O      1 
ATOM   14634 C  CB     . SER   F 4  18  ? -1.700  -47.070  70.983  1.00 77.83  ? 18  SER   F CB     1 
ATOM   14635 O  OG     . SER   F 4  18  ? -2.681  -47.822  71.668  1.00 84.73  ? 18  SER   F OG     1 
ATOM   14636 N  N      . ARG   F 4  19  ? 1.071   -45.765  71.420  1.00 85.41  ? 19  ARG   F N      1 
ATOM   14637 C  CA     . ARG   F 4  19  ? 2.050   -44.768  71.004  1.00 82.49  ? 19  ARG   F CA     1 
ATOM   14638 C  C      . ARG   F 4  19  ? 3.392   -45.430  70.721  1.00 82.13  ? 19  ARG   F C      1 
ATOM   14639 O  O      . ARG   F 4  19  ? 3.951   -45.281  69.629  1.00 85.30  ? 19  ARG   F O      1 
ATOM   14640 C  CB     . ARG   F 4  19  ? 2.150   -43.672  72.077  1.00 74.18  ? 19  ARG   F CB     1 
ATOM   14641 C  CG     . ARG   F 4  19  ? 3.499   -42.953  72.252  1.00 87.24  ? 19  ARG   F CG     1 
ATOM   14642 C  CD     . ARG   F 4  19  ? 4.335   -43.453  73.449  1.00 90.34  ? 19  ARG   F CD     1 
ATOM   14643 N  NE     . ARG   F 4  19  ? 5.440   -42.554  73.785  1.00 85.24  ? 19  ARG   F NE     1 
ATOM   14644 C  CZ     . ARG   F 4  19  ? 6.656   -42.592  73.248  1.00 90.96  ? 19  ARG   F CZ     1 
ATOM   14645 N  NH1    . ARG   F 4  19  ? 7.005   -43.525  72.378  1.00 82.60  ? 19  ARG   F NH1    1 
ATOM   14646 N  NH2    . ARG   F 4  19  ? 7.548   -41.668  73.598  1.00 95.91  ? 19  ARG   F NH2    1 
ATOM   14647 N  N      . LEU   F 4  20  ? 3.889   -46.227  71.671  1.00 82.65  ? 20  LEU   F N      1 
ATOM   14648 C  CA     . LEU   F 4  20  ? 5.170   -46.906  71.480  1.00 83.64  ? 20  LEU   F CA     1 
ATOM   14649 C  C      . LEU   F 4  20  ? 5.117   -47.879  70.306  1.00 82.04  ? 20  LEU   F C      1 
ATOM   14650 O  O      . LEU   F 4  20  ? 6.067   -47.964  69.519  1.00 80.78  ? 20  LEU   F O      1 
ATOM   14651 C  CB     . LEU   F 4  20  ? 5.575   -47.646  72.758  1.00 89.96  ? 20  LEU   F CB     1 
ATOM   14652 C  CG     . LEU   F 4  20  ? 5.883   -46.897  74.055  1.00 85.85  ? 20  LEU   F CG     1 
ATOM   14653 C  CD1    . LEU   F 4  20  ? 4.693   -46.961  74.973  1.00 82.11  ? 20  LEU   F CD1    1 
ATOM   14654 C  CD2    . LEU   F 4  20  ? 7.088   -47.527  74.731  1.00 86.18  ? 20  LEU   F CD2    1 
ATOM   14655 N  N      . LEU   F 4  21  ? 4.020   -48.634  70.181  1.00 83.90  ? 21  LEU   F N      1 
ATOM   14656 C  CA     . LEU   F 4  21  ? 3.900   -49.615  69.104  1.00 83.95  ? 21  LEU   F CA     1 
ATOM   14657 C  C      . LEU   F 4  21  ? 4.167   -48.979  67.743  1.00 81.89  ? 21  LEU   F C      1 
ATOM   14658 O  O      . LEU   F 4  21  ? 5.120   -49.345  67.045  1.00 75.81  ? 21  LEU   F O      1 
ATOM   14659 C  CB     . LEU   F 4  21  ? 2.514   -50.263  69.143  1.00 81.69  ? 21  LEU   F CB     1 
ATOM   14660 C  CG     . LEU   F 4  21  ? 2.383   -51.513  70.009  1.00 77.67  ? 21  LEU   F CG     1 
ATOM   14661 C  CD1    . LEU   F 4  21  ? 0.936   -51.969  70.043  1.00 78.00  ? 21  LEU   F CD1    1 
ATOM   14662 C  CD2    . LEU   F 4  21  ? 3.274   -52.623  69.457  1.00 69.37  ? 21  LEU   F CD2    1 
ATOM   14663 N  N      . LEU   F 4  22  ? 3.322   -48.023  67.350  1.00 84.45  ? 22  LEU   F N      1 
ATOM   14664 C  CA     . LEU   F 4  22  ? 3.506   -47.313  66.092  1.00 79.29  ? 22  LEU   F CA     1 
ATOM   14665 C  C      . LEU   F 4  22  ? 4.966   -46.933  65.899  1.00 83.21  ? 22  LEU   F C      1 
ATOM   14666 O  O      . LEU   F 4  22  ? 5.586   -47.280  64.888  1.00 85.97  ? 22  LEU   F O      1 
ATOM   14667 C  CB     . LEU   F 4  22  ? 2.608   -46.078  66.075  1.00 75.37  ? 22  LEU   F CB     1 
ATOM   14668 C  CG     . LEU   F 4  22  ? 1.136   -46.482  66.198  1.00 83.60  ? 22  LEU   F CG     1 
ATOM   14669 C  CD1    . LEU   F 4  22  ? 0.247   -45.326  66.662  1.00 73.62  ? 22  LEU   F CD1    1 
ATOM   14670 C  CD2    . LEU   F 4  22  ? 0.616   -47.115  64.900  1.00 82.03  ? 22  LEU   F CD2    1 
ATOM   14671 N  N      . ALA   F 4  23  ? 5.547   -46.270  66.901  1.00 78.11  ? 23  ALA   F N      1 
ATOM   14672 C  CA     . ALA   F 4  23  ? 6.902   -45.736  66.834  1.00 74.98  ? 23  ALA   F CA     1 
ATOM   14673 C  C      . ALA   F 4  23  ? 7.978   -46.796  66.597  1.00 81.58  ? 23  ALA   F C      1 
ATOM   14674 O  O      . ALA   F 4  23  ? 9.157   -46.434  66.530  1.00 85.48  ? 23  ALA   F O      1 
ATOM   14675 C  CB     . ALA   F 4  23  ? 7.205   -44.961  68.114  1.00 71.01  ? 23  ALA   F CB     1 
ATOM   14676 N  N      . THR   F 4  24  ? 7.640   -48.076  66.457  1.00 83.10  ? 24  THR   F N      1 
ATOM   14677 C  CA     . THR   F 4  24  ? 8.637   -49.053  66.040  1.00 84.71  ? 24  THR   F CA     1 
ATOM   14678 C  C      . THR   F 4  24  ? 8.710   -49.170  64.532  1.00 88.64  ? 24  THR   F C      1 
ATOM   14679 O  O      . THR   F 4  24  ? 9.520   -49.956  64.023  1.00 86.06  ? 24  THR   F O      1 
ATOM   14680 C  CB     . THR   F 4  24  ? 8.347   -50.439  66.629  1.00 86.39  ? 24  THR   F CB     1 
ATOM   14681 O  OG1    . THR   F 4  24  ? 7.231   -51.027  65.951  1.00 89.69  ? 24  THR   F OG1    1 
ATOM   14682 C  CG2    . THR   F 4  24  ? 8.025   -50.331  68.100  1.00 85.20  ? 24  THR   F CG2    1 
ATOM   14683 N  N      . GLY   F 4  25  ? 7.866   -48.420  63.820  1.00 90.59  ? 25  GLY   F N      1 
ATOM   14684 C  CA     . GLY   F 4  25  ? 7.765   -48.492  62.379  1.00 90.55  ? 25  GLY   F CA     1 
ATOM   14685 C  C      . GLY   F 4  25  ? 7.269   -49.811  61.844  1.00 90.55  ? 25  GLY   F C      1 
ATOM   14686 O  O      . GLY   F 4  25  ? 7.269   -50.000  60.619  1.00 90.34  ? 25  GLY   F O      1 
ATOM   14687 N  N      . GLN   F 4  26  ? 6.849   -50.732  62.720  1.00 86.39  ? 26  GLN   F N      1 
ATOM   14688 C  CA     . GLN   F 4  26  ? 6.372   -52.040  62.297  1.00 81.56  ? 26  GLN   F CA     1 
ATOM   14689 C  C      . GLN   F 4  26  ? 4.951   -52.331  62.756  1.00 78.46  ? 26  GLN   F C      1 
ATOM   14690 O  O      . GLN   F 4  26  ? 4.443   -53.425  62.487  1.00 75.81  ? 26  GLN   F O      1 
ATOM   14691 C  CB     . GLN   F 4  26  ? 7.299   -53.145  62.809  1.00 76.89  ? 26  GLN   F CB     1 
ATOM   14692 C  CG     . GLN   F 4  26  ? 8.766   -52.869  62.630  1.00 79.73  ? 26  GLN   F CG     1 
ATOM   14693 C  CD     . GLN   F 4  26  ? 9.602   -54.063  63.029  1.00 83.48  ? 26  GLN   F CD     1 
ATOM   14694 O  OE1    . GLN   F 4  26  ? 10.648  -53.930  63.671  1.00 83.44  ? 26  GLN   F OE1    1 
ATOM   14695 N  NE2    . GLN   F 4  26  ? 9.160   -55.249  62.609  1.00 79.52  ? 26  GLN   F NE2    1 
ATOM   14696 N  N      . TRP   F 4  27  ? 4.293   -51.398  63.436  1.00 74.64  ? 27  TRP   F N      1 
ATOM   14697 C  CA     . TRP   F 4  27  ? 2.908   -51.575  63.853  1.00 78.69  ? 27  TRP   F CA     1 
ATOM   14698 C  C      . TRP   F 4  27  ? 2.049   -50.483  63.232  1.00 80.60  ? 27  TRP   F C      1 
ATOM   14699 O  O      . TRP   F 4  27  ? 2.410   -49.305  63.283  1.00 84.67  ? 27  TRP   F O      1 
ATOM   14700 C  CB     . TRP   F 4  27  ? 2.793   -51.585  65.388  1.00 79.77  ? 27  TRP   F CB     1 
ATOM   14701 C  CG     . TRP   F 4  27  ? 3.042   -52.951  65.965  1.00 78.48  ? 27  TRP   F CG     1 
ATOM   14702 C  CD1    . TRP   F 4  27  ? 4.249   -53.512  66.280  1.00 77.38  ? 27  TRP   F CD1    1 
ATOM   14703 C  CD2    . TRP   F 4  27  ? 2.047   -53.923  66.307  1.00 74.78  ? 27  TRP   F CD2    1 
ATOM   14704 N  NE1    . TRP   F 4  27  ? 4.065   -54.783  66.776  1.00 78.15  ? 27  TRP   F NE1    1 
ATOM   14705 C  CE2    . TRP   F 4  27  ? 2.723   -55.056  66.805  1.00 73.32  ? 27  TRP   F CE2    1 
ATOM   14706 C  CE3    . TRP   F 4  27  ? 0.653   -53.947  66.232  1.00 70.93  ? 27  TRP   F CE3    1 
ATOM   14707 C  CZ2    . TRP   F 4  27  ? 2.054   -56.196  67.225  1.00 66.06  ? 27  TRP   F CZ2    1 
ATOM   14708 C  CZ3    . TRP   F 4  27  ? -0.005  -55.072  66.646  1.00 71.23  ? 27  TRP   F CZ3    1 
ATOM   14709 C  CH2    . TRP   F 4  27  ? 0.693   -56.186  67.139  1.00 69.10  ? 27  TRP   F CH2    1 
ATOM   14710 N  N      . LYS   F 4  28  ? 0.936   -50.878  62.620  1.00 72.27  ? 28  LYS   F N      1 
ATOM   14711 C  CA     . LYS   F 4  28  ? -0.033  -49.930  62.104  1.00 70.80  ? 28  LYS   F CA     1 
ATOM   14712 C  C      . LYS   F 4  28  ? -1.341  -50.087  62.865  1.00 69.08  ? 28  LYS   F C      1 
ATOM   14713 O  O      . LYS   F 4  28  ? -1.663  -51.165  63.367  1.00 74.82  ? 28  LYS   F O      1 
ATOM   14714 C  CB     . LYS   F 4  28  ? -0.274  -50.119  60.593  1.00 81.13  ? 28  LYS   F CB     1 
ATOM   14715 C  CG     . LYS   F 4  28  ? -0.190  -51.556  60.060  1.00 82.58  ? 28  LYS   F CG     1 
ATOM   14716 C  CD     . LYS   F 4  28  ? 0.073   -51.561  58.533  1.00 89.57  ? 28  LYS   F CD     1 
ATOM   14717 C  CE     . LYS   F 4  28  ? -1.018  -50.826  57.705  1.00 77.64  ? 28  LYS   F CE     1 
ATOM   14718 N  NZ     . LYS   F 4  28  ? -2.294  -51.584  57.456  1.00 73.38  ? 28  LYS   F NZ     1 
ATOM   14719 N  N      . ARG   F 4  29  ? -2.098  -49.007  62.945  1.00 60.33  ? 29  ARG   F N      1 
ATOM   14720 C  CA     . ARG   F 4  29  ? -3.319  -48.966  63.734  1.00 61.19  ? 29  ARG   F CA     1 
ATOM   14721 C  C      . ARG   F 4  29  ? -4.531  -48.831  62.824  1.00 62.42  ? 29  ARG   F C      1 
ATOM   14722 O  O      . ARG   F 4  29  ? -4.761  -47.765  62.249  1.00 62.54  ? 29  ARG   F O      1 
ATOM   14723 C  CB     . ARG   F 4  29  ? -3.272  -47.821  64.739  1.00 63.60  ? 29  ARG   F CB     1 
ATOM   14724 C  CG     . ARG   F 4  29  ? -4.574  -47.659  65.476  1.00 60.55  ? 29  ARG   F CG     1 
ATOM   14725 C  CD     . ARG   F 4  29  ? -4.511  -46.582  66.520  1.00 57.31  ? 29  ARG   F CD     1 
ATOM   14726 N  NE     . ARG   F 4  29  ? -5.839  -46.327  67.059  1.00 61.49  ? 29  ARG   F NE     1 
ATOM   14727 C  CZ     . ARG   F 4  29  ? -6.102  -45.390  67.956  1.00 65.02  ? 29  ARG   F CZ     1 
ATOM   14728 N  NH1    . ARG   F 4  29  ? -5.139  -44.633  68.456  1.00 58.64  ? 29  ARG   F NH1    1 
ATOM   14729 N  NH2    . ARG   F 4  29  ? -7.358  -45.211  68.365  1.00 65.18  ? 29  ARG   F NH2    1 
ATOM   14730 N  N      . LEU   F 4  30  ? -5.322  -49.898  62.739  1.00 63.76  ? 30  LEU   F N      1 
ATOM   14731 C  CA     . LEU   F 4  30  ? -6.591  -49.925  62.030  1.00 57.82  ? 30  LEU   F CA     1 
ATOM   14732 C  C      . LEU   F 4  30  ? -7.685  -49.210  62.835  1.00 62.18  ? 30  LEU   F C      1 
ATOM   14733 O  O      . LEU   F 4  30  ? -7.451  -48.673  63.923  1.00 60.81  ? 30  LEU   F O      1 
ATOM   14734 C  CB     . LEU   F 4  30  ? -6.967  -51.371  61.737  1.00 58.87  ? 30  LEU   F CB     1 
ATOM   14735 C  CG     . LEU   F 4  30  ? -5.745  -52.231  61.403  1.00 62.45  ? 30  LEU   F CG     1 
ATOM   14736 C  CD1    . LEU   F 4  30  ? -6.032  -53.686  61.671  1.00 65.19  ? 30  LEU   F CD1    1 
ATOM   14737 C  CD2    . LEU   F 4  30  ? -5.301  -52.055  59.960  1.00 66.03  ? 30  LEU   F CD2    1 
ATOM   14738 N  N      . ARG   F 4  31  ? -8.904  -49.193  62.297  1.00 64.07  ? 31  ARG   F N      1 
ATOM   14739 C  CA     . ARG   F 4  31  ? -10.019 -48.526  62.962  1.00 72.22  ? 31  ARG   F CA     1 
ATOM   14740 C  C      . ARG   F 4  31  ? -10.776 -49.480  63.871  1.00 77.00  ? 31  ARG   F C      1 
ATOM   14741 O  O      . ARG   F 4  31  ? -11.021 -50.632  63.504  1.00 76.83  ? 31  ARG   F O      1 
ATOM   14742 C  CB     . ARG   F 4  31  ? -11.000 -47.941  61.950  1.00 76.29  ? 31  ARG   F CB     1 
ATOM   14743 C  CG     . ARG   F 4  31  ? -12.171 -47.259  62.626  1.00 81.87  ? 31  ARG   F CG     1 
ATOM   14744 C  CD     . ARG   F 4  31  ? -11.785 -45.871  63.173  1.00 92.81  ? 31  ARG   F CD     1 
ATOM   14745 N  NE     . ARG   F 4  31  ? -11.769 -45.773  64.635  1.00 89.99  ? 31  ARG   F NE     1 
ATOM   14746 C  CZ     . ARG   F 4  31  ? -10.741 -45.340  65.358  1.00 84.81  ? 31  ARG   F CZ     1 
ATOM   14747 N  NH1    . ARG   F 4  31  ? -9.609  -44.953  64.791  1.00 79.87  ? 31  ARG   F NH1    1 
ATOM   14748 N  NH2    . ARG   F 4  31  ? -10.859 -45.272  66.685  1.00 82.40  ? 31  ARG   F NH2    1 
ATOM   14749 N  N      . LYS   F 4  32  ? -11.168 -48.975  65.046  1.00 74.73  ? 32  LYS   F N      1 
ATOM   14750 C  CA     . LYS   F 4  32  ? -11.925 -49.718  66.051  1.00 79.88  ? 32  LYS   F CA     1 
ATOM   14751 C  C      . LYS   F 4  32  ? -12.529 -51.020  65.531  1.00 87.08  ? 32  LYS   F C      1 
ATOM   14752 O  O      . LYS   F 4  32  ? -12.117 -52.108  65.957  1.00 87.89  ? 32  LYS   F O      1 
ATOM   14753 C  CB     . LYS   F 4  32  ? -13.043 -48.840  66.628  1.00 83.64  ? 32  LYS   F CB     1 
ATOM   14754 C  CG     . LYS   F 4  32  ? -12.606 -47.840  67.693  1.00 76.35  ? 32  LYS   F CG     1 
ATOM   14755 C  CD     . LYS   F 4  32  ? -13.779 -46.965  68.132  1.00 71.61  ? 32  LYS   F CD     1 
ATOM   14756 C  CE     . LYS   F 4  32  ? -15.038 -47.800  68.304  1.00 76.57  ? 32  LYS   F CE     1 
ATOM   14757 N  NZ     . LYS   F 4  32  ? -16.242 -47.022  68.709  1.00 79.70  ? 32  LYS   F NZ     1 
ATOM   14758 N  N      . ASP   F 4  33  ? -13.487 -50.925  64.599  1.00 81.86  ? 33  ASP   F N      1 
ATOM   14759 C  CA     . ASP   F 4  33  ? -14.278 -52.071  64.157  1.00 81.47  ? 33  ASP   F CA     1 
ATOM   14760 C  C      . ASP   F 4  33  ? -13.744 -52.730  62.877  1.00 78.77  ? 33  ASP   F C      1 
ATOM   14761 O  O      . ASP   F 4  33  ? -14.506 -53.375  62.141  1.00 72.93  ? 33  ASP   F O      1 
ATOM   14762 C  CB     . ASP   F 4  33  ? -15.747 -51.670  63.988  1.00 87.53  ? 33  ASP   F CB     1 
ATOM   14763 C  CG     . ASP   F 4  33  ? -15.952 -50.525  62.986  1.00 99.73  ? 33  ASP   F CG     1 
ATOM   14764 O  OD1    . ASP   F 4  33  ? -15.043 -49.664  62.835  1.00 96.57  ? 33  ASP   F OD1    1 
ATOM   14765 O  OD2    . ASP   F 4  33  ? -17.038 -50.496  62.345  1.00 98.90  ? 33  ASP   F OD2    1 
ATOM   14766 N  N      . ASN   F 4  34  ? -12.444 -52.608  62.607  1.00 80.57  ? 34  ASN   F N      1 
ATOM   14767 C  CA     . ASN   F 4  34  ? -11.805 -53.391  61.553  1.00 76.31  ? 34  ASN   F CA     1 
ATOM   14768 C  C      . ASN   F 4  34  ? -11.397 -54.745  62.116  1.00 75.41  ? 34  ASN   F C      1 
ATOM   14769 O  O      . ASN   F 4  34  ? -10.551 -54.800  63.020  1.00 75.17  ? 34  ASN   F O      1 
ATOM   14770 C  CB     . ASN   F 4  34  ? -10.590 -52.667  61.000  1.00 71.07  ? 34  ASN   F CB     1 
ATOM   14771 C  CG     . ASN   F 4  34  ? -9.909  -53.431  59.870  1.00 72.68  ? 34  ASN   F CG     1 
ATOM   14772 O  OD1    . ASN   F 4  34  ? -10.144 -54.631  59.668  1.00 70.92  ? 34  ASN   F OD1    1 
ATOM   14773 N  ND2    . ASN   F 4  34  ? -9.067  -52.729  59.114  1.00 66.79  ? 34  ASN   F ND2    1 
ATOM   14774 N  N      . PRO   F 4  35  ? -11.955 -55.852  61.622  1.00 70.79  ? 35  PRO   F N      1 
ATOM   14775 C  CA     . PRO   F 4  35  ? -11.674 -57.152  62.244  1.00 71.76  ? 35  PRO   F CA     1 
ATOM   14776 C  C      . PRO   F 4  35  ? -10.282 -57.683  61.960  1.00 70.16  ? 35  PRO   F C      1 
ATOM   14777 O  O      . PRO   F 4  35  ? -9.889  -58.682  62.585  1.00 66.71  ? 35  PRO   F O      1 
ATOM   14778 C  CB     . PRO   F 4  35  ? -12.725 -58.066  61.620  1.00 63.01  ? 35  PRO   F CB     1 
ATOM   14779 C  CG     . PRO   F 4  35  ? -12.874 -57.500  60.245  1.00 70.97  ? 35  PRO   F CG     1 
ATOM   14780 C  CD     . PRO   F 4  35  ? -12.744 -55.998  60.389  1.00 73.46  ? 35  PRO   F CD     1 
ATOM   14781 N  N      . ARG   F 4  36  ? -9.534  -57.080  61.041  1.00 66.94  ? 36  ARG   F N      1 
ATOM   14782 C  CA     . ARG   F 4  36  ? -8.304  -57.703  60.562  1.00 65.40  ? 36  ARG   F CA     1 
ATOM   14783 C  C      . ARG   F 4  36  ? -7.088  -57.153  61.297  1.00 65.43  ? 36  ARG   F C      1 
ATOM   14784 O  O      . ARG   F 4  36  ? -6.129  -56.642  60.710  1.00 64.75  ? 36  ARG   F O      1 
ATOM   14785 C  CB     . ARG   F 4  36  ? -8.179  -57.562  59.050  1.00 69.93  ? 36  ARG   F CB     1 
ATOM   14786 C  CG     . ARG   F 4  36  ? -9.488  -57.738  58.318  1.00 71.01  ? 36  ARG   F CG     1 
ATOM   14787 C  CD     . ARG   F 4  36  ? -9.240  -57.702  56.841  1.00 74.71  ? 36  ARG   F CD     1 
ATOM   14788 N  NE     . ARG   F 4  36  ? -8.573  -58.962  56.552  1.00 79.69  ? 36  ARG   F NE     1 
ATOM   14789 C  CZ     . ARG   F 4  36  ? -9.170  -60.058  56.109  1.00 81.04  ? 36  ARG   F CZ     1 
ATOM   14790 N  NH1    . ARG   F 4  36  ? -10.454 -60.062  55.790  1.00 71.08  ? 36  ARG   F NH1    1 
ATOM   14791 N  NH2    . ARG   F 4  36  ? -8.466  -61.187  56.017  1.00 77.26  ? 36  ARG   F NH2    1 
ATOM   14792 N  N      . PHE   F 4  37  ? -7.150  -57.314  62.617  1.00 64.73  ? 37  PHE   F N      1 
ATOM   14793 C  CA     . PHE   F 4  37  ? -6.103  -56.928  63.546  1.00 60.47  ? 37  PHE   F CA     1 
ATOM   14794 C  C      . PHE   F 4  37  ? -5.359  -58.154  64.059  1.00 61.46  ? 37  PHE   F C      1 
ATOM   14795 O  O      . PHE   F 4  37  ? -5.938  -59.240  64.197  1.00 57.70  ? 37  PHE   F O      1 
ATOM   14796 C  CB     . PHE   F 4  37  ? -6.699  -56.168  64.731  1.00 58.89  ? 37  PHE   F CB     1 
ATOM   14797 C  CG     . PHE   F 4  37  ? -7.717  -56.954  65.497  1.00 55.95  ? 37  PHE   F CG     1 
ATOM   14798 C  CD1    . PHE   F 4  37  ? -7.328  -57.903  66.425  1.00 55.02  ? 37  PHE   F CD1    1 
ATOM   14799 C  CD2    . PHE   F 4  37  ? -9.066  -56.746  65.288  1.00 57.89  ? 37  PHE   F CD2    1 
ATOM   14800 C  CE1    . PHE   F 4  37  ? -8.273  -58.626  67.133  1.00 55.28  ? 37  PHE   F CE1    1 
ATOM   14801 C  CE2    . PHE   F 4  37  ? -10.020 -57.471  66.000  1.00 54.87  ? 37  PHE   F CE2    1 
ATOM   14802 C  CZ     . PHE   F 4  37  ? -9.624  -58.404  66.923  1.00 53.33  ? 37  PHE   F CZ     1 
ATOM   14803 N  N      . ASN   F 4  38  ? -4.060  -57.969  64.336  1.00 62.45  ? 38  ASN   F N      1 
ATOM   14804 C  CA     . ASN   F 4  38  ? -3.318  -58.945  65.128  1.00 58.64  ? 38  ASN   F CA     1 
ATOM   14805 C  C      . ASN   F 4  38  ? -3.559  -58.742  66.620  1.00 60.17  ? 38  ASN   F C      1 
ATOM   14806 O  O      . ASN   F 4  38  ? -3.482  -59.693  67.405  1.00 56.30  ? 38  ASN   F O      1 
ATOM   14807 C  CB     . ASN   F 4  38  ? -1.823  -58.850  64.829  1.00 53.17  ? 38  ASN   F CB     1 
ATOM   14808 C  CG     . ASN   F 4  38  ? -1.475  -59.345  63.452  1.00 60.85  ? 38  ASN   F CG     1 
ATOM   14809 O  OD1    . ASN   F 4  38  ? -1.111  -58.567  62.567  1.00 64.79  ? 38  ASN   F OD1    1 
ATOM   14810 N  ND2    . ASN   F 4  38  ? -1.585  -60.650  63.253  1.00 64.92  ? 38  ASN   F ND2    1 
ATOM   14811 N  N      . LEU   F 4  39  ? -3.872  -57.521  67.022  1.00 56.60  ? 39  LEU   F N      1 
ATOM   14812 C  CA     . LEU   F 4  39  ? -3.889  -57.186  68.429  1.00 60.07  ? 39  LEU   F CA     1 
ATOM   14813 C  C      . LEU   F 4  39  ? -5.097  -56.327  68.737  1.00 58.26  ? 39  LEU   F C      1 
ATOM   14814 O  O      . LEU   F 4  39  ? -5.392  -55.375  68.017  1.00 60.43  ? 39  LEU   F O      1 
ATOM   14815 C  CB     . LEU   F 4  39  ? -2.598  -56.467  68.835  1.00 60.58  ? 39  LEU   F CB     1 
ATOM   14816 C  CG     . LEU   F 4  39  ? -2.583  -55.900  70.248  1.00 61.39  ? 39  LEU   F CG     1 
ATOM   14817 C  CD1    . LEU   F 4  39  ? -2.611  -57.033  71.253  1.00 60.02  ? 39  LEU   F CD1    1 
ATOM   14818 C  CD2    . LEU   F 4  39  ? -1.324  -55.103  70.413  1.00 63.37  ? 39  LEU   F CD2    1 
ATOM   14819 N  N      . MET   F 4  40  ? -5.802  -56.684  69.801  1.00 55.09  ? 40  MET   F N      1 
ATOM   14820 C  CA     . MET   F 4  40  ? -6.919  -55.899  70.296  1.00 55.76  ? 40  MET   F CA     1 
ATOM   14821 C  C      . MET   F 4  40  ? -6.548  -55.374  71.675  1.00 60.30  ? 40  MET   F C      1 
ATOM   14822 O  O      . MET   F 4  40  ? -6.457  -56.144  72.636  1.00 61.93  ? 40  MET   F O      1 
ATOM   14823 C  CB     . MET   F 4  40  ? -8.209  -56.714  70.361  1.00 44.49  ? 40  MET   F CB     1 
ATOM   14824 C  CG     . MET   F 4  40  ? -9.251  -55.983  71.140  1.00 45.63  ? 40  MET   F CG     1 
ATOM   14825 S  SD     . MET   F 4  40  ? -10.913 -56.602  71.026  1.00 55.29  ? 40  MET   F SD     1 
ATOM   14826 C  CE     . MET   F 4  40  ? -11.107 -56.741  69.248  1.00 49.46  ? 40  MET   F CE     1 
ATOM   14827 N  N      . LEU   F 4  41  ? -6.336  -54.069  71.775  1.00 59.59  ? 41  LEU   F N      1 
ATOM   14828 C  CA     . LEU   F 4  41  ? -6.332  -53.391  73.063  1.00 57.16  ? 41  LEU   F CA     1 
ATOM   14829 C  C      . LEU   F 4  41  ? -7.779  -52.976  73.306  1.00 55.13  ? 41  LEU   F C      1 
ATOM   14830 O  O      . LEU   F 4  41  ? -8.197  -51.891  72.926  1.00 64.43  ? 41  LEU   F O      1 
ATOM   14831 C  CB     . LEU   F 4  41  ? -5.383  -52.205  73.017  1.00 61.53  ? 41  LEU   F CB     1 
ATOM   14832 C  CG     . LEU   F 4  41  ? -4.011  -52.567  72.442  1.00 62.40  ? 41  LEU   F CG     1 
ATOM   14833 C  CD1    . LEU   F 4  41  ? -3.224  -51.315  72.085  1.00 68.57  ? 41  LEU   F CD1    1 
ATOM   14834 C  CD2    . LEU   F 4  41  ? -3.238  -53.425  73.403  1.00 63.46  ? 41  LEU   F CD2    1 
ATOM   14835 N  N      . GLY   F 4  42  ? -8.563  -53.849  73.943  1.00 52.94  ? 42  GLY   F N      1 
ATOM   14836 C  CA     . GLY   F 4  42  ? -10.009 -53.759  73.888  1.00 55.32  ? 42  GLY   F CA     1 
ATOM   14837 C  C      . GLY   F 4  42  ? -10.664 -53.034  75.055  1.00 56.87  ? 42  GLY   F C      1 
ATOM   14838 O  O      . GLY   F 4  42  ? -10.015 -52.515  75.960  1.00 57.51  ? 42  GLY   F O      1 
ATOM   14839 N  N      . GLU   F 4  43  ? -11.999 -53.013  75.020  1.00 58.92  ? 43  GLU   F N      1 
ATOM   14840 C  CA     . GLU   F 4  43  ? -12.764 -52.290  76.025  1.00 62.73  ? 43  GLU   F CA     1 
ATOM   14841 C  C      . GLU   F 4  43  ? -12.731 -53.035  77.355  1.00 57.53  ? 43  GLU   F C      1 
ATOM   14842 O  O      . GLU   F 4  43  ? -12.237 -54.153  77.462  1.00 55.78  ? 43  GLU   F O      1 
ATOM   14843 C  CB     . GLU   F 4  43  ? -14.227 -52.106  75.612  1.00 64.86  ? 43  GLU   F CB     1 
ATOM   14844 C  CG     . GLU   F 4  43  ? -14.927 -53.380  75.155  1.00 65.31  ? 43  GLU   F CG     1 
ATOM   14845 C  CD     . GLU   F 4  43  ? -14.860 -53.622  73.667  1.00 64.74  ? 43  GLU   F CD     1 
ATOM   14846 O  OE1    . GLU   F 4  43  ? -13.741 -53.538  73.108  1.00 61.28  ? 43  GLU   F OE1    1 
ATOM   14847 O  OE2    . GLU   F 4  43  ? -15.926 -53.949  73.080  1.00 59.13  ? 43  GLU   F OE2    1 
ATOM   14848 N  N      . ARG   F 4  44  ? -13.307 -52.402  78.377  1.00 64.68  ? 44  ARG   F N      1 
ATOM   14849 C  CA     . ARG   F 4  44  ? -13.323 -52.961  79.722  1.00 67.00  ? 44  ARG   F CA     1 
ATOM   14850 C  C      . ARG   F 4  44  ? -14.571 -53.793  79.983  1.00 67.09  ? 44  ARG   F C      1 
ATOM   14851 O  O      . ARG   F 4  44  ? -14.470 -54.905  80.503  1.00 72.90  ? 44  ARG   F O      1 
ATOM   14852 C  CB     . ARG   F 4  44  ? -13.191 -51.844  80.765  1.00 67.65  ? 44  ARG   F CB     1 
ATOM   14853 C  CG     . ARG   F 4  44  ? -11.784 -51.251  80.906  1.00 69.72  ? 44  ARG   F CG     1 
ATOM   14854 C  CD     . ARG   F 4  44  ? -11.750 -50.131  81.944  1.00 75.05  ? 44  ARG   F CD     1 
ATOM   14855 N  NE     . ARG   F 4  44  ? -12.114 -50.600  83.275  1.00 77.95  ? 44  ARG   F NE     1 
ATOM   14856 C  CZ     . ARG   F 4  44  ? -11.974 -49.889  84.386  1.00 92.77  ? 44  ARG   F CZ     1 
ATOM   14857 N  NH1    . ARG   F 4  44  ? -11.430 -48.679  84.374  1.00 91.56  ? 44  ARG   F NH1    1 
ATOM   14858 N  NH2    . ARG   F 4  44  ? -12.402 -50.398  85.539  1.00 100.41 ? 44  ARG   F NH2    1 
ATOM   14859 N  N      . ASN   F 4  45  ? -15.749 -53.294  79.642  1.00 68.01  ? 45  ASN   F N      1 
ATOM   14860 C  CA     . ASN   F 4  45  ? -16.924 -54.137  79.780  1.00 76.96  ? 45  ASN   F CA     1 
ATOM   14861 C  C      . ASN   F 4  45  ? -17.327 -54.669  78.409  1.00 77.49  ? 45  ASN   F C      1 
ATOM   14862 O  O      . ASN   F 4  45  ? -17.104 -54.031  77.377  1.00 76.47  ? 45  ASN   F O      1 
ATOM   14863 C  CB     . ASN   F 4  45  ? -18.125 -53.406  80.390  1.00 86.84  ? 45  ASN   F CB     1 
ATOM   14864 C  CG     . ASN   F 4  45  ? -19.031 -52.782  79.325  1.00 94.27  ? 45  ASN   F CG     1 
ATOM   14865 O  OD1    . ASN   F 4  45  ? -18.556 -52.179  78.362  1.00 99.07  ? 45  ASN   F OD1    1 
ATOM   14866 N  ND2    . ASN   F 4  45  ? -20.345 -52.978  79.471  1.00 91.74  ? 45  ASN   F ND2    1 
ATOM   14867 N  N      . ARG   F 4  46  ? -17.945 -55.844  78.421  1.00 79.66  ? 46  ARG   F N      1 
ATOM   14868 C  CA     . ARG   F 4  46  ? -18.503 -56.477  77.230  1.00 74.70  ? 46  ARG   F CA     1 
ATOM   14869 C  C      . ARG   F 4  46  ? -17.472 -56.580  76.109  1.00 64.60  ? 46  ARG   F C      1 
ATOM   14870 O  O      . ARG   F 4  46  ? -17.816 -56.492  74.931  1.00 64.88  ? 46  ARG   F O      1 
ATOM   14871 C  CB     . ARG   F 4  46  ? -19.757 -55.743  76.746  1.00 80.55  ? 46  ARG   F CB     1 
ATOM   14872 C  CG     . ARG   F 4  46  ? -21.026 -56.229  77.442  1.00 88.22  ? 46  ARG   F CG     1 
ATOM   14873 C  CD     . ARG   F 4  46  ? -21.925 -57.122  76.599  1.00 96.30  ? 46  ARG   F CD     1 
ATOM   14874 N  NE     . ARG   F 4  46  ? -22.451 -56.506  75.389  1.00 106.33 ? 46  ARG   F NE     1 
ATOM   14875 C  CZ     . ARG   F 4  46  ? -22.920 -57.201  74.360  1.00 115.69 ? 46  ARG   F CZ     1 
ATOM   14876 N  NH1    . ARG   F 4  46  ? -22.920 -58.523  74.368  1.00 117.47 ? 46  ARG   F NH1    1 
ATOM   14877 N  NH2    . ARG   F 4  46  ? -23.397 -56.555  73.298  1.00 115.94 ? 46  ARG   F NH2    1 
ATOM   14878 N  N      . LEU   F 4  47  ? -16.198 -56.773  76.462  1.00 62.46  ? 47  LEU   F N      1 
ATOM   14879 C  CA     . LEU   F 4  47  ? -15.191 -57.046  75.446  1.00 54.38  ? 47  LEU   F CA     1 
ATOM   14880 C  C      . LEU   F 4  47  ? -15.591 -58.310  74.702  1.00 57.72  ? 47  LEU   F C      1 
ATOM   14881 O  O      . LEU   F 4  47  ? -15.795 -59.355  75.340  1.00 57.50  ? 47  LEU   F O      1 
ATOM   14882 C  CB     . LEU   F 4  47  ? -13.801 -57.225  76.047  1.00 49.05  ? 47  LEU   F CB     1 
ATOM   14883 C  CG     . LEU   F 4  47  ? -12.675 -57.404  75.013  1.00 51.77  ? 47  LEU   F CG     1 
ATOM   14884 C  CD1    . LEU   F 4  47  ? -11.290 -57.135  75.598  1.00 49.74  ? 47  LEU   F CD1    1 
ATOM   14885 C  CD2    . LEU   F 4  47  ? -12.691 -58.762  74.367  1.00 46.52  ? 47  LEU   F CD2    1 
ATOM   14886 N  N      . PRO   F 4  48  ? -15.680 -58.276  73.363  1.00 60.60  ? 48  PRO   F N      1 
ATOM   14887 C  CA     . PRO   F 4  48  ? -16.307 -59.379  72.585  1.00 56.78  ? 48  PRO   F CA     1 
ATOM   14888 C  C      . PRO   F 4  48  ? -15.365 -60.558  72.348  1.00 52.82  ? 48  PRO   F C      1 
ATOM   14889 O  O      . PRO   F 4  48  ? -14.848 -60.792  71.242  1.00 47.08  ? 48  PRO   F O      1 
ATOM   14890 C  CB     . PRO   F 4  48  ? -16.705 -58.666  71.288  1.00 52.70  ? 48  PRO   F CB     1 
ATOM   14891 C  CG     . PRO   F 4  48  ? -15.574 -57.672  71.087  1.00 54.49  ? 48  PRO   F CG     1 
ATOM   14892 C  CD     . PRO   F 4  48  ? -15.180 -57.200  72.486  1.00 56.61  ? 48  PRO   F CD     1 
ATOM   14893 N  N      . PHE   F 4  49  ? -15.130 -61.349  73.408  1.00 51.95  ? 49  PHE   F N      1 
ATOM   14894 C  CA     . PHE   F 4  49  ? -14.112 -62.398  73.332  1.00 49.37  ? 49  PHE   F CA     1 
ATOM   14895 C  C      . PHE   F 4  49  ? -14.508 -63.505  72.358  1.00 51.07  ? 49  PHE   F C      1 
ATOM   14896 O  O      . PHE   F 4  49  ? -13.633 -64.139  71.761  1.00 52.88  ? 49  PHE   F O      1 
ATOM   14897 C  CB     . PHE   F 4  49  ? -13.837 -63.009  74.710  1.00 46.38  ? 49  PHE   F CB     1 
ATOM   14898 C  CG     . PHE   F 4  49  ? -13.084 -62.116  75.658  1.00 46.98  ? 49  PHE   F CG     1 
ATOM   14899 C  CD1    . PHE   F 4  49  ? -11.719 -61.926  75.523  1.00 49.38  ? 49  PHE   F CD1    1 
ATOM   14900 C  CD2    . PHE   F 4  49  ? -13.723 -61.540  76.742  1.00 44.72  ? 49  PHE   F CD2    1 
ATOM   14901 C  CE1    . PHE   F 4  49  ? -11.015 -61.123  76.423  1.00 46.52  ? 49  PHE   F CE1    1 
ATOM   14902 C  CE2    . PHE   F 4  49  ? -13.023 -60.750  77.634  1.00 40.88  ? 49  PHE   F CE2    1 
ATOM   14903 C  CZ     . PHE   F 4  49  ? -11.671 -60.542  77.476  1.00 40.97  ? 49  PHE   F CZ     1 
ATOM   14904 N  N      . GLY   F 4  50  ? -15.809 -63.764  72.189  1.00 48.83  ? 50  GLY   F N      1 
ATOM   14905 C  CA     . GLY   F 4  50  ? -16.263 -64.781  71.246  1.00 54.08  ? 50  GLY   F CA     1 
ATOM   14906 C  C      . GLY   F 4  50  ? -16.058 -64.459  69.774  1.00 53.33  ? 50  GLY   F C      1 
ATOM   14907 O  O      . GLY   F 4  50  ? -16.376 -65.287  68.912  1.00 52.92  ? 50  GLY   F O      1 
ATOM   14908 N  N      . ARG   F 4  51  ? -15.551 -63.274  69.466  1.00 50.57  ? 51  ARG   F N      1 
ATOM   14909 C  CA     . ARG   F 4  51  ? -15.263 -62.883  68.105  1.00 49.15  ? 51  ARG   F CA     1 
ATOM   14910 C  C      . ARG   F 4  51  ? -13.786 -62.972  67.787  1.00 55.27  ? 51  ARG   F C      1 
ATOM   14911 O  O      . ARG   F 4  51  ? -13.422 -62.901  66.607  1.00 59.89  ? 51  ARG   F O      1 
ATOM   14912 C  CB     . ARG   F 4  51  ? -15.761 -61.453  67.856  1.00 49.13  ? 51  ARG   F CB     1 
ATOM   14913 C  CG     . ARG   F 4  51  ? -17.117 -61.409  67.174  1.00 58.46  ? 51  ARG   F CG     1 
ATOM   14914 C  CD     . ARG   F 4  51  ? -17.999 -60.201  67.557  1.00 56.17  ? 51  ARG   F CD     1 
ATOM   14915 N  NE     . ARG   F 4  51  ? -17.352 -58.914  67.333  1.00 54.37  ? 51  ARG   F NE     1 
ATOM   14916 C  CZ     . ARG   F 4  51  ? -17.860 -57.748  67.708  1.00 56.67  ? 51  ARG   F CZ     1 
ATOM   14917 N  NH1    . ARG   F 4  51  ? -19.048 -57.667  68.285  1.00 50.64  ? 51  ARG   F NH1    1 
ATOM   14918 N  NH2    . ARG   F 4  51  ? -17.167 -56.636  67.476  1.00 66.21  ? 51  ARG   F NH2    1 
ATOM   14919 N  N      . LEU   F 4  52  ? -12.931 -63.137  68.799  1.00 52.97  ? 52  LEU   F N      1 
ATOM   14920 C  CA     . LEU   F 4  52  ? -11.496 -63.238  68.575  1.00 48.21  ? 52  LEU   F CA     1 
ATOM   14921 C  C      . LEU   F 4  52  ? -11.133 -64.640  68.131  1.00 51.80  ? 52  LEU   F C      1 
ATOM   14922 O  O      . LEU   F 4  52  ? -11.829 -65.618  68.434  1.00 53.46  ? 52  LEU   F O      1 
ATOM   14923 C  CB     . LEU   F 4  52  ? -10.715 -62.887  69.835  1.00 43.11  ? 52  LEU   F CB     1 
ATOM   14924 C  CG     . LEU   F 4  52  ? -11.082 -61.556  70.476  1.00 45.45  ? 52  LEU   F CG     1 
ATOM   14925 C  CD1    . LEU   F 4  52  ? -10.305 -61.366  71.749  1.00 46.02  ? 52  LEU   F CD1    1 
ATOM   14926 C  CD2    . LEU   F 4  52  ? -10.758 -60.440  69.496  1.00 44.70  ? 52  LEU   F CD2    1 
ATOM   14927 N  N      . GLY   F 4  53  ? -10.040 -64.717  67.378  1.00 52.65  ? 53  GLY   F N      1 
ATOM   14928 C  CA     . GLY   F 4  53  ? -9.495  -65.989  66.953  1.00 47.88  ? 53  GLY   F CA     1 
ATOM   14929 C  C      . GLY   F 4  53  ? -10.262 -66.660  65.849  1.00 44.46  ? 53  GLY   F C      1 
ATOM   14930 O  O      . GLY   F 4  53  ? -10.246 -67.892  65.747  1.00 55.11  ? 53  GLY   F O      1 
ATOM   14931 N  N      . HIS   F 4  54  ? -10.948 -65.889  65.021  1.00 48.98  ? 54  HIS   F N      1 
ATOM   14932 C  CA     . HIS   F 4  54  ? -11.600 -66.444  63.845  1.00 48.50  ? 54  HIS   F CA     1 
ATOM   14933 C  C      . HIS   F 4  54  ? -11.178 -65.728  62.570  1.00 52.32  ? 54  HIS   F C      1 
ATOM   14934 O  O      . HIS   F 4  54  ? -11.909 -65.759  61.582  1.00 51.16  ? 54  HIS   F O      1 
ATOM   14935 C  CB     . HIS   F 4  54  ? -13.117 -66.401  63.996  1.00 46.29  ? 54  HIS   F CB     1 
ATOM   14936 C  CG     . HIS   F 4  54  ? -13.639 -67.126  65.195  1.00 46.05  ? 54  HIS   F CG     1 
ATOM   14937 N  ND1    . HIS   F 4  54  ? -13.781 -68.494  65.232  1.00 43.72  ? 54  HIS   F ND1    1 
ATOM   14938 C  CD2    . HIS   F 4  54  ? -14.078 -66.669  66.391  1.00 49.62  ? 54  HIS   F CD2    1 
ATOM   14939 C  CE1    . HIS   F 4  54  ? -14.262 -68.852  66.408  1.00 48.83  ? 54  HIS   F CE1    1 
ATOM   14940 N  NE2    . HIS   F 4  54  ? -14.451 -67.763  67.130  1.00 51.53  ? 54  HIS   F NE2    1 
ATOM   14941 N  N      . GLU   F 4  55  ? -10.015 -65.082  62.560  1.00 56.39  ? 55  GLU   F N      1 
ATOM   14942 C  CA     . GLU   F 4  55  ? -9.581  -64.461  61.320  1.00 59.05  ? 55  GLU   F CA     1 
ATOM   14943 C  C      . GLU   F 4  55  ? -8.513  -65.321  60.669  1.00 54.13  ? 55  GLU   F C      1 
ATOM   14944 O  O      . GLU   F 4  55  ? -7.366  -65.327  61.137  1.00 50.97  ? 55  GLU   F O      1 
ATOM   14945 C  CB     . GLU   F 4  55  ? -9.058  -63.048  61.555  1.00 59.75  ? 55  GLU   F CB     1 
ATOM   14946 C  CG     . GLU   F 4  55  ? -10.159 -62.025  61.610  1.00 56.29  ? 55  GLU   F CG     1 
ATOM   14947 C  CD     . GLU   F 4  55  ? -11.003 -62.062  60.358  1.00 62.18  ? 55  GLU   F CD     1 
ATOM   14948 O  OE1    . GLU   F 4  55  ? -10.450 -62.357  59.273  1.00 63.63  ? 55  GLU   F OE1    1 
ATOM   14949 O  OE2    . GLU   F 4  55  ? -12.220 -61.801  60.462  1.00 68.96  ? 55  GLU   F OE2    1 
ATOM   14950 N  N      . PRO   F 4  56  ? -8.830  -66.045  59.601  1.00 50.20  ? 56  PRO   F N      1 
ATOM   14951 C  CA     . PRO   F 4  56  ? -7.824  -66.907  58.982  1.00 57.90  ? 56  PRO   F CA     1 
ATOM   14952 C  C      . PRO   F 4  56  ? -6.617  -66.088  58.574  1.00 57.94  ? 56  PRO   F C      1 
ATOM   14953 O  O      . PRO   F 4  56  ? -6.743  -64.967  58.077  1.00 62.72  ? 56  PRO   F O      1 
ATOM   14954 C  CB     . PRO   F 4  56  ? -8.553  -67.505  57.770  1.00 56.03  ? 56  PRO   F CB     1 
ATOM   14955 C  CG     . PRO   F 4  56  ? -9.734  -66.657  57.551  1.00 49.63  ? 56  PRO   F CG     1 
ATOM   14956 C  CD     . PRO   F 4  56  ? -10.105 -66.067  58.877  1.00 51.40  ? 56  PRO   F CD     1 
ATOM   14957 N  N      . GLY   F 4  57  ? -5.438  -66.649  58.812  1.00 51.25  ? 57  GLY   F N      1 
ATOM   14958 C  CA     . GLY   F 4  57  ? -4.236  -65.902  58.549  1.00 58.22  ? 57  GLY   F CA     1 
ATOM   14959 C  C      . GLY   F 4  57  ? -3.918  -64.805  59.540  1.00 56.93  ? 57  GLY   F C      1 
ATOM   14960 O  O      . GLY   F 4  57  ? -2.971  -64.047  59.318  1.00 58.98  ? 57  GLY   F O      1 
ATOM   14961 N  N      . LEU   F 4  58  ? -4.667  -64.685  60.630  1.00 56.25  ? 58  LEU   F N      1 
ATOM   14962 C  CA     . LEU   F 4  58  ? -4.399  -63.667  61.638  1.00 56.81  ? 58  LEU   F CA     1 
ATOM   14963 C  C      . LEU   F 4  58  ? -4.137  -64.327  62.980  1.00 56.36  ? 58  LEU   F C      1 
ATOM   14964 O  O      . LEU   F 4  58  ? -4.992  -65.049  63.500  1.00 58.92  ? 58  LEU   F O      1 
ATOM   14965 C  CB     . LEU   F 4  58  ? -5.560  -62.686  61.751  1.00 54.43  ? 58  LEU   F CB     1 
ATOM   14966 C  CG     . LEU   F 4  58  ? -5.444  -61.603  60.688  1.00 61.04  ? 58  LEU   F CG     1 
ATOM   14967 C  CD1    . LEU   F 4  58  ? -6.460  -60.502  60.920  1.00 64.27  ? 58  LEU   F CD1    1 
ATOM   14968 C  CD2    . LEU   F 4  58  ? -4.020  -61.060  60.642  1.00 59.54  ? 58  LEU   F CD2    1 
ATOM   14969 N  N      . VAL   F 4  59  ? -2.958  -64.081  63.538  1.00 54.52  ? 59  VAL   F N      1 
ATOM   14970 C  CA     . VAL   F 4  59  ? -2.693  -64.456  64.920  1.00 56.16  ? 59  VAL   F CA     1 
ATOM   14971 C  C      . VAL   F 4  59  ? -3.253  -63.347  65.803  1.00 55.64  ? 59  VAL   F C      1 
ATOM   14972 O  O      . VAL   F 4  59  ? -2.712  -62.239  65.844  1.00 56.65  ? 59  VAL   F O      1 
ATOM   14973 C  CB     . VAL   F 4  59  ? -1.200  -64.665  65.171  1.00 55.36  ? 59  VAL   F CB     1 
ATOM   14974 C  CG1    . VAL   F 4  59  ? -0.898  -64.657  66.671  1.00 46.90  ? 59  VAL   F CG1    1 
ATOM   14975 C  CG2    . VAL   F 4  59  ? -0.746  -65.941  64.509  1.00 55.50  ? 59  VAL   F CG2    1 
ATOM   14976 N  N      . GLN   F 4  60  ? -4.341  -63.631  66.502  1.00 48.51  ? 60  GLN   F N      1 
ATOM   14977 C  CA     . GLN   F 4  60  ? -4.978  -62.613  67.311  1.00 50.13  ? 60  GLN   F CA     1 
ATOM   14978 C  C      . GLN   F 4  60  ? -4.564  -62.721  68.777  1.00 56.53  ? 60  GLN   F C      1 
ATOM   14979 O  O      . GLN   F 4  60  ? -4.373  -63.819  69.309  1.00 57.93  ? 60  GLN   F O      1 
ATOM   14980 C  CB     . GLN   F 4  60  ? -6.491  -62.666  67.105  1.00 48.48  ? 60  GLN   F CB     1 
ATOM   14981 C  CG     . GLN   F 4  60  ? -6.798  -62.234  65.685  1.00 50.86  ? 60  GLN   F CG     1 
ATOM   14982 C  CD     . GLN   F 4  60  ? -8.267  -62.077  65.359  1.00 53.53  ? 60  GLN   F CD     1 
ATOM   14983 O  OE1    . GLN   F 4  60  ? -9.143  -62.686  65.975  1.00 56.10  ? 60  GLN   F OE1    1 
ATOM   14984 N  NE2    . GLN   F 4  60  ? -8.548  -61.194  64.407  1.00 55.53  ? 60  GLN   F NE2    1 
ATOM   14985 N  N      . LEU   F 4  61  ? -4.333  -61.556  69.387  1.00 57.15  ? 61  LEU   F N      1 
ATOM   14986 C  CA     . LEU   F 4  61  ? -3.874  -61.401  70.763  1.00 53.11  ? 61  LEU   F CA     1 
ATOM   14987 C  C      . LEU   F 4  61  ? -4.631  -60.246  71.384  1.00 47.36  ? 61  LEU   F C      1 
ATOM   14988 O  O      . LEU   F 4  61  ? -4.739  -59.183  70.774  1.00 48.40  ? 61  LEU   F O      1 
ATOM   14989 C  CB     . LEU   F 4  61  ? -2.366  -61.116  70.840  1.00 52.25  ? 61  LEU   F CB     1 
ATOM   14990 C  CG     . LEU   F 4  61  ? -1.839  -60.834  72.250  1.00 51.17  ? 61  LEU   F CG     1 
ATOM   14991 C  CD1    . LEU   F 4  61  ? -2.068  -62.023  73.175  1.00 51.58  ? 61  LEU   F CD1    1 
ATOM   14992 C  CD2    . LEU   F 4  61  ? -0.368  -60.483  72.197  1.00 51.73  ? 61  LEU   F CD2    1 
ATOM   14993 N  N      . VAL   F 4  62  ? -5.155  -60.441  72.585  1.00 44.38  ? 62  VAL   F N      1 
ATOM   14994 C  CA     . VAL   F 4  62  ? -5.885  -59.373  73.251  1.00 50.87  ? 62  VAL   F CA     1 
ATOM   14995 C  C      . VAL   F 4  62  ? -5.250  -59.122  74.616  1.00 55.67  ? 62  VAL   F C      1 
ATOM   14996 O  O      . VAL   F 4  62  ? -4.470  -59.934  75.125  1.00 56.34  ? 62  VAL   F O      1 
ATOM   14997 C  CB     . VAL   F 4  62  ? -7.404  -59.671  73.343  1.00 47.56  ? 62  VAL   F CB     1 
ATOM   14998 C  CG1    . VAL   F 4  62  ? -7.687  -60.973  74.080  1.00 49.87  ? 62  VAL   F CG1    1 
ATOM   14999 C  CG2    . VAL   F 4  62  ? -8.142  -58.509  73.955  1.00 48.39  ? 62  VAL   F CG2    1 
ATOM   15000 N  N      . ASN   F 4  63  ? -5.528  -57.943  75.173  1.00 53.05  ? 63  ASN   F N      1 
ATOM   15001 C  CA     . ASN   F 4  63  ? -4.848  -57.461  76.373  1.00 54.61  ? 63  ASN   F CA     1 
ATOM   15002 C  C      . ASN   F 4  63  ? -5.751  -57.585  77.594  1.00 56.20  ? 63  ASN   F C      1 
ATOM   15003 O  O      . ASN   F 4  63  ? -5.709  -56.755  78.504  1.00 56.42  ? 63  ASN   F O      1 
ATOM   15004 C  CB     . ASN   F 4  63  ? -4.374  -56.023  76.187  1.00 53.80  ? 63  ASN   F CB     1 
ATOM   15005 C  CG     . ASN   F 4  63  ? -5.518  -55.032  76.154  1.00 58.23  ? 63  ASN   F CG     1 
ATOM   15006 O  OD1    . ASN   F 4  63  ? -6.667  -55.400  75.923  1.00 57.78  ? 63  ASN   F OD1    1 
ATOM   15007 N  ND2    . ASN   F 4  63  ? -5.202  -53.759  76.335  1.00 59.83  ? 63  ASN   F ND2    1 
ATOM   15008 N  N      . TYR   F 4  64  ? -6.556  -58.652  77.617  1.00 54.06  ? 64  TYR   F N      1 
ATOM   15009 C  CA     . TYR   F 4  64  ? -7.433  -59.008  78.721  1.00 51.94  ? 64  TYR   F CA     1 
ATOM   15010 C  C      . TYR   F 4  64  ? -7.663  -60.516  78.734  1.00 54.78  ? 64  TYR   F C      1 
ATOM   15011 O  O      . TYR   F 4  64  ? -7.629  -61.169  77.685  1.00 50.16  ? 64  TYR   F O      1 
ATOM   15012 C  CB     . TYR   F 4  64  ? -8.771  -58.288  78.621  1.00 50.37  ? 64  TYR   F CB     1 
ATOM   15013 C  CG     . TYR   F 4  64  ? -8.750  -56.926  79.226  1.00 56.78  ? 64  TYR   F CG     1 
ATOM   15014 C  CD1    . TYR   F 4  64  ? -8.934  -56.764  80.598  1.00 61.04  ? 64  TYR   F CD1    1 
ATOM   15015 C  CD2    . TYR   F 4  64  ? -8.570  -55.797  78.444  1.00 56.45  ? 64  TYR   F CD2    1 
ATOM   15016 C  CE1    . TYR   F 4  64  ? -8.931  -55.511  81.183  1.00 60.31  ? 64  TYR   F CE1    1 
ATOM   15017 C  CE2    . TYR   F 4  64  ? -8.564  -54.536  79.022  1.00 60.63  ? 64  TYR   F CE2    1 
ATOM   15018 C  CZ     . TYR   F 4  64  ? -8.749  -54.403  80.395  1.00 60.45  ? 64  TYR   F CZ     1 
ATOM   15019 O  OH     . TYR   F 4  64  ? -8.750  -53.161  80.985  1.00 65.90  ? 64  TYR   F OH     1 
ATOM   15020 N  N      . TYR   F 4  65  ? -7.910  -61.061  79.949  1.00 53.25  ? 65  TYR   F N      1 
ATOM   15021 C  CA     . TYR   F 4  65  ? -8.128  -62.493  80.204  1.00 44.95  ? 65  TYR   F CA     1 
ATOM   15022 C  C      . TYR   F 4  65  ? -9.599  -62.755  80.523  1.00 45.66  ? 65  TYR   F C      1 
ATOM   15023 O  O      . TYR   F 4  65  ? -10.027 -62.623  81.672  1.00 48.98  ? 65  TYR   F O      1 
ATOM   15024 C  CB     . TYR   F 4  65  ? -7.225  -62.987  81.342  1.00 47.76  ? 65  TYR   F CB     1 
ATOM   15025 C  CG     . TYR   F 4  65  ? -5.987  -63.747  80.893  1.00 47.65  ? 65  TYR   F CG     1 
ATOM   15026 C  CD1    . TYR   F 4  65  ? -6.063  -65.095  80.532  1.00 44.01  ? 65  TYR   F CD1    1 
ATOM   15027 C  CD2    . TYR   F 4  65  ? -4.744  -63.118  80.817  1.00 45.50  ? 65  TYR   F CD2    1 
ATOM   15028 C  CE1    . TYR   F 4  65  ? -4.935  -65.792  80.104  1.00 45.67  ? 65  TYR   F CE1    1 
ATOM   15029 C  CE2    . TYR   F 4  65  ? -3.607  -63.807  80.393  1.00 41.72  ? 65  TYR   F CE2    1 
ATOM   15030 C  CZ     . TYR   F 4  65  ? -3.706  -65.143  80.040  1.00 46.53  ? 65  TYR   F CZ     1 
ATOM   15031 O  OH     . TYR   F 4  65  ? -2.580  -65.834  79.619  1.00 48.68  ? 65  TYR   F OH     1 
ATOM   15032 N  N      . ARG   F 4  66  ? -10.370 -63.133  79.502  1.00 49.55  ? 66  ARG   F N      1 
ATOM   15033 C  CA     . ARG   F 4  66  ? -11.753 -63.574  79.677  1.00 47.39  ? 66  ARG   F CA     1 
ATOM   15034 C  C      . ARG   F 4  66  ? -11.850 -64.479  80.910  1.00 55.23  ? 66  ARG   F C      1 
ATOM   15035 O  O      . ARG   F 4  66  ? -11.253 -65.564  80.948  1.00 59.05  ? 66  ARG   F O      1 
ATOM   15036 C  CB     . ARG   F 4  66  ? -12.245 -64.290  78.401  1.00 40.70  ? 66  ARG   F CB     1 
ATOM   15037 C  CG     . ARG   F 4  66  ? -13.710 -64.633  78.392  1.00 42.66  ? 66  ARG   F CG     1 
ATOM   15038 C  CD     . ARG   F 4  66  ? -14.189 -65.393  77.150  1.00 44.72  ? 66  ARG   F CD     1 
ATOM   15039 N  NE     . ARG   F 4  66  ? -15.653 -65.445  77.100  1.00 47.88  ? 66  ARG   F NE     1 
ATOM   15040 C  CZ     . ARG   F 4  66  ? -16.356 -66.305  76.367  1.00 47.94  ? 66  ARG   F CZ     1 
ATOM   15041 N  NH1    . ARG   F 4  66  ? -15.765 -67.157  75.541  1.00 48.39  ? 66  ARG   F NH1    1 
ATOM   15042 N  NH2    . ARG   F 4  66  ? -17.683 -66.341  76.496  1.00 42.89  ? 66  ARG   F NH2    1 
ATOM   15043 N  N      . GLY   F 4  67  ? -12.568 -64.032  81.938  1.00 49.39  ? 67  GLY   F N      1 
ATOM   15044 C  CA     . GLY   F 4  67  ? -12.625 -64.712  83.214  1.00 47.25  ? 67  GLY   F CA     1 
ATOM   15045 C  C      . GLY   F 4  67  ? -11.946 -63.972  84.357  1.00 56.36  ? 67  GLY   F C      1 
ATOM   15046 O  O      . GLY   F 4  67  ? -12.274 -64.233  85.519  1.00 53.20  ? 67  GLY   F O      1 
ATOM   15047 N  N      . ALA   F 4  68  ? -11.030 -63.038  84.061  1.00 57.77  ? 68  ALA   F N      1 
ATOM   15048 C  CA     . ALA   F 4  68  ? -10.229 -62.389  85.101  1.00 58.53  ? 68  ALA   F CA     1 
ATOM   15049 C  C      . ALA   F 4  68  ? -11.071 -61.594  86.090  1.00 61.74  ? 68  ALA   F C      1 
ATOM   15050 O  O      . ALA   F 4  68  ? -10.582 -61.229  87.162  1.00 53.63  ? 68  ALA   F O      1 
ATOM   15051 C  CB     . ALA   F 4  68  ? -9.186  -61.460  84.463  1.00 58.78  ? 68  ALA   F CB     1 
ATOM   15052 N  N      . ASP   F 4  69  ? -12.313 -61.283  85.739  1.00 67.04  ? 69  ASP   F N      1 
ATOM   15053 C  CA     . ASP   F 4  69  ? -13.160 -60.515  86.635  1.00 66.82  ? 69  ASP   F CA     1 
ATOM   15054 C  C      . ASP   F 4  69  ? -13.408 -61.243  87.947  1.00 68.98  ? 69  ASP   F C      1 
ATOM   15055 O  O      . ASP   F 4  69  ? -13.687 -60.587  88.957  1.00 70.41  ? 69  ASP   F O      1 
ATOM   15056 C  CB     . ASP   F 4  69  ? -14.461 -60.183  85.908  1.00 71.51  ? 69  ASP   F CB     1 
ATOM   15057 C  CG     . ASP   F 4  69  ? -15.122 -61.416  85.298  1.00 70.38  ? 69  ASP   F CG     1 
ATOM   15058 O  OD1    . ASP   F 4  69  ? -15.706 -62.228  86.045  1.00 69.24  ? 69  ASP   F OD1    1 
ATOM   15059 O  OD2    . ASP   F 4  69  ? -14.986 -61.609  84.067  1.00 73.74  ? 69  ASP   F OD2    1 
ATOM   15060 N  N      . LYS   F 4  70  ? -13.300 -62.579  87.967  1.00 68.59  ? 70  LYS   F N      1 
ATOM   15061 C  CA     . LYS   F 4  70  ? -13.518 -63.305  89.216  1.00 67.33  ? 70  LYS   F CA     1 
ATOM   15062 C  C      . LYS   F 4  70  ? -12.609 -62.764  90.312  1.00 73.13  ? 70  LYS   F C      1 
ATOM   15063 O  O      . LYS   F 4  70  ? -13.044 -62.562  91.453  1.00 74.66  ? 70  LYS   F O      1 
ATOM   15064 C  CB     . LYS   F 4  70  ? -13.297 -64.806  89.018  1.00 58.03  ? 70  LYS   F CB     1 
ATOM   15065 C  CG     . LYS   F 4  70  ? -14.564 -65.678  88.935  1.00 65.81  ? 70  LYS   F CG     1 
ATOM   15066 C  CD     . LYS   F 4  70  ? -15.578 -65.216  87.893  1.00 76.70  ? 70  LYS   F CD     1 
ATOM   15067 C  CE     . LYS   F 4  70  ? -16.875 -66.023  87.956  1.00 82.71  ? 70  LYS   F CE     1 
ATOM   15068 N  NZ     . LYS   F 4  70  ? -17.837 -65.612  86.897  1.00 93.91  ? 70  LYS   F NZ     1 
ATOM   15069 N  N      . LEU   F 4  71  ? -11.357 -62.480  89.965  1.00 68.64  ? 71  LEU   F N      1 
ATOM   15070 C  CA     . LEU   F 4  71  ? -10.340 -61.968  90.870  1.00 65.05  ? 71  LEU   F CA     1 
ATOM   15071 C  C      . LEU   F 4  71  ? -10.364 -60.453  91.037  1.00 69.70  ? 71  LEU   F C      1 
ATOM   15072 O  O      . LEU   F 4  71  ? -9.698  -59.943  91.943  1.00 75.08  ? 71  LEU   F O      1 
ATOM   15073 C  CB     . LEU   F 4  71  ? -8.963  -62.367  90.352  1.00 59.99  ? 71  LEU   F CB     1 
ATOM   15074 C  CG     . LEU   F 4  71  ? -7.804  -62.516  91.305  1.00 58.69  ? 71  LEU   F CG     1 
ATOM   15075 C  CD1    . LEU   F 4  71  ? -7.856  -63.890  91.896  1.00 57.75  ? 71  LEU   F CD1    1 
ATOM   15076 C  CD2    . LEU   F 4  71  ? -6.523  -62.275  90.530  1.00 52.39  ? 71  LEU   F CD2    1 
ATOM   15077 N  N      . CYS   F 4  72  ? -11.076 -59.721  90.179  1.00 69.78  ? 72  CYS   F N      1 
ATOM   15078 C  CA     . CYS   F 4  72  ? -11.028 -58.262  90.164  1.00 68.82  ? 72  CYS   F CA     1 
ATOM   15079 C  C      . CYS   F 4  72  ? -12.345 -57.612  90.565  1.00 74.76  ? 72  CYS   F C      1 
ATOM   15080 O  O      . CYS   F 4  72  ? -12.489 -56.396  90.427  1.00 77.56  ? 72  CYS   F O      1 
ATOM   15081 C  CB     . CYS   F 4  72  ? -10.636 -57.757  88.781  1.00 67.75  ? 72  CYS   F CB     1 
ATOM   15082 S  SG     . CYS   F 4  72  ? -9.170  -58.497  88.128  1.00 72.74  ? 72  CYS   F SG     1 
ATOM   15083 N  N      . ARG   F 4  73  ? -13.321 -58.384  91.022  1.00 77.47  ? 73  ARG   F N      1 
ATOM   15084 C  CA     . ARG   F 4  73  ? -14.584 -57.837  91.481  1.00 77.94  ? 73  ARG   F CA     1 
ATOM   15085 C  C      . ARG   F 4  73  ? -14.752 -58.205  92.942  1.00 80.04  ? 73  ARG   F C      1 
ATOM   15086 O  O      . ARG   F 4  73  ? -14.582 -59.367  93.320  1.00 81.66  ? 73  ARG   F O      1 
ATOM   15087 C  CB     . ARG   F 4  73  ? -15.744 -58.339  90.632  1.00 83.54  ? 73  ARG   F CB     1 
ATOM   15088 C  CG     . ARG   F 4  73  ? -16.139 -57.274  89.620  1.00 95.86  ? 73  ARG   F CG     1 
ATOM   15089 C  CD     . ARG   F 4  73  ? -16.478 -57.849  88.253  1.00 102.54 ? 73  ARG   F CD     1 
ATOM   15090 N  NE     . ARG   F 4  73  ? -16.676 -56.787  87.271  1.00 110.84 ? 73  ARG   F NE     1 
ATOM   15091 C  CZ     . ARG   F 4  73  ? -15.692 -56.115  86.688  1.00 100.76 ? 73  ARG   F CZ     1 
ATOM   15092 N  NH1    . ARG   F 4  73  ? -14.421 -56.403  86.927  1.00 88.02  ? 73  ARG   F NH1    1 
ATOM   15093 N  NH2    . ARG   F 4  73  ? -15.991 -55.138  85.835  1.00 102.05 ? 73  ARG   F NH2    1 
ATOM   15094 N  N      . LYS   F 4  74  ? -15.061 -57.205  93.761  1.00 81.99  ? 74  LYS   F N      1 
ATOM   15095 C  CA     . LYS   F 4  74  ? -14.835 -57.354  95.188  1.00 82.26  ? 74  LYS   F CA     1 
ATOM   15096 C  C      . LYS   F 4  74  ? -15.660 -58.506  95.755  1.00 82.40  ? 74  LYS   F C      1 
ATOM   15097 O  O      . LYS   F 4  74  ? -15.146 -59.349  96.498  1.00 83.30  ? 74  LYS   F O      1 
ATOM   15098 C  CB     . LYS   F 4  74  ? -15.128 -56.040  95.908  1.00 81.67  ? 74  LYS   F CB     1 
ATOM   15099 C  CG     . LYS   F 4  74  ? -13.839 -55.502  96.435  1.00 86.76  ? 74  LYS   F CG     1 
ATOM   15100 C  CD     . LYS   F 4  74  ? -13.328 -56.541  97.423  1.00 88.29  ? 74  LYS   F CD     1 
ATOM   15101 C  CE     . LYS   F 4  74  ? -11.948 -56.227  97.954  1.00 94.34  ? 74  LYS   F CE     1 
ATOM   15102 N  NZ     . LYS   F 4  74  ? -11.590 -57.187  99.040  1.00 101.30 ? 74  LYS   F NZ     1 
ATOM   15103 N  N      . ALA   F 4  75  ? -16.941 -58.578  95.391  1.00 79.52  ? 75  ALA   F N      1 
ATOM   15104 C  CA     . ALA   F 4  75  ? -17.758 -59.717  95.793  1.00 72.02  ? 75  ALA   F CA     1 
ATOM   15105 C  C      . ALA   F 4  75  ? -17.210 -61.019  95.218  1.00 77.32  ? 75  ALA   F C      1 
ATOM   15106 O  O      . ALA   F 4  75  ? -17.182 -62.048  95.904  1.00 79.37  ? 75  ALA   F O      1 
ATOM   15107 C  CB     . ALA   F 4  75  ? -19.199 -59.490  95.348  1.00 74.06  ? 75  ALA   F CB     1 
ATOM   15108 N  N      . SER   F 4  76  ? -16.768 -60.990  93.955  1.00 83.08  ? 76  SER   F N      1 
ATOM   15109 C  CA     . SER   F 4  76  ? -16.217 -62.176  93.294  1.00 80.58  ? 76  SER   F CA     1 
ATOM   15110 C  C      . SER   F 4  76  ? -14.959 -62.673  93.993  1.00 79.74  ? 76  SER   F C      1 
ATOM   15111 O  O      . SER   F 4  76  ? -14.786 -63.883  94.206  1.00 72.12  ? 76  SER   F O      1 
ATOM   15112 C  CB     . SER   F 4  76  ? -15.888 -61.848  91.838  1.00 77.85  ? 76  SER   F CB     1 
ATOM   15113 O  OG     . SER   F 4  76  ? -17.023 -61.369  91.145  1.00 95.12  ? 76  SER   F OG     1 
ATOM   15114 N  N      . LEU   F 4  77  ? -14.054 -61.743  94.314  1.00 80.31  ? 77  LEU   F N      1 
ATOM   15115 C  CA     . LEU   F 4  77  ? -12.803 -62.078  94.977  1.00 72.39  ? 77  LEU   F CA     1 
ATOM   15116 C  C      . LEU   F 4  77  ? -13.032 -62.823  96.287  1.00 73.58  ? 77  LEU   F C      1 
ATOM   15117 O  O      . LEU   F 4  77  ? -12.332 -63.797  96.585  1.00 74.89  ? 77  LEU   F O      1 
ATOM   15118 C  CB     . LEU   F 4  77  ? -12.007 -60.805  95.204  1.00 69.39  ? 77  LEU   F CB     1 
ATOM   15119 C  CG     . LEU   F 4  77  ? -10.799 -61.133  96.062  1.00 74.80  ? 77  LEU   F CG     1 
ATOM   15120 C  CD1    . LEU   F 4  77  ? -9.921  -62.150  95.360  1.00 66.33  ? 77  LEU   F CD1    1 
ATOM   15121 C  CD2    . LEU   F 4  77  ? -10.035 -59.859  96.352  1.00 80.21  ? 77  LEU   F CD2    1 
ATOM   15122 N  N      . VAL   F 4  78  ? -13.995 -62.372  97.091  1.00 75.88  ? 78  VAL   F N      1 
ATOM   15123 C  CA     . VAL   F 4  78  ? -14.385 -63.130  98.278  1.00 72.09  ? 78  VAL   F CA     1 
ATOM   15124 C  C      . VAL   F 4  78  ? -14.900 -64.502  97.884  1.00 68.63  ? 78  VAL   F C      1 
ATOM   15125 O  O      . VAL   F 4  78  ? -14.431 -65.531  98.386  1.00 62.34  ? 78  VAL   F O      1 
ATOM   15126 C  CB     . VAL   F 4  78  ? -15.424 -62.351  99.103  1.00 73.40  ? 78  VAL   F CB     1 
ATOM   15127 C  CG1    . VAL   F 4  78  ? -15.798 -63.135  100.338 1.00 73.73  ? 78  VAL   F CG1    1 
ATOM   15128 C  CG2    . VAL   F 4  78  ? -14.841 -60.994  99.510  1.00 74.65  ? 78  VAL   F CG2    1 
ATOM   15129 N  N      . LYS   F 4  79  ? -15.877 -64.536  96.981  1.00 71.36  ? 79  LYS   F N      1 
ATOM   15130 C  CA     . LYS   F 4  79  ? -16.389 -65.820  96.528  1.00 73.53  ? 79  LYS   F CA     1 
ATOM   15131 C  C      . LYS   F 4  79  ? -15.258 -66.731  96.074  1.00 72.34  ? 79  LYS   F C      1 
ATOM   15132 O  O      . LYS   F 4  79  ? -15.285 -67.939  96.331  1.00 72.43  ? 79  LYS   F O      1 
ATOM   15133 C  CB     . LYS   F 4  79  ? -17.405 -65.625  95.401  1.00 75.32  ? 79  LYS   F CB     1 
ATOM   15134 C  CG     . LYS   F 4  79  ? -18.021 -66.936  94.909  1.00 77.41  ? 79  LYS   F CG     1 
ATOM   15135 C  CD     . LYS   F 4  79  ? -19.115 -66.686  93.880  1.00 82.67  ? 79  LYS   F CD     1 
ATOM   15136 C  CE     . LYS   F 4  79  ? -19.712 -67.984  93.372  1.00 79.66  ? 79  LYS   F CE     1 
ATOM   15137 N  NZ     . LYS   F 4  79  ? -20.817 -67.702  92.434  1.00 73.44  ? 79  LYS   F NZ     1 
ATOM   15138 N  N      . LEU   F 4  80  ? -14.241 -66.167  95.420  1.00 72.50  ? 80  LEU   F N      1 
ATOM   15139 C  CA     . LEU   F 4  80  ? -13.171 -67.002  94.888  1.00 67.26  ? 80  LEU   F CA     1 
ATOM   15140 C  C      . LEU   F 4  80  ? -12.356 -67.637  96.004  1.00 68.77  ? 80  LEU   F C      1 
ATOM   15141 O  O      . LEU   F 4  80  ? -11.955 -68.800  95.897  1.00 73.05  ? 80  LEU   F O      1 
ATOM   15142 C  CB     . LEU   F 4  80  ? -12.262 -66.187  93.972  1.00 65.40  ? 80  LEU   F CB     1 
ATOM   15143 C  CG     . LEU   F 4  80  ? -11.024 -66.964  93.521  1.00 65.68  ? 80  LEU   F CG     1 
ATOM   15144 C  CD1    . LEU   F 4  80  ? -11.390 -68.274  92.838  1.00 59.59  ? 80  LEU   F CD1    1 
ATOM   15145 C  CD2    . LEU   F 4  80  ? -10.198 -66.131  92.597  1.00 63.24  ? 80  LEU   F CD2    1 
ATOM   15146 N  N      . ILE   F 4  81  ? -12.118 -66.898  97.088  1.00 70.98  ? 81  ILE   F N      1 
ATOM   15147 C  CA     . ILE   F 4  81  ? -11.179 -67.334  98.120  1.00 71.18  ? 81  ILE   F CA     1 
ATOM   15148 C  C      . ILE   F 4  81  ? -11.833 -68.313  99.093  1.00 74.07  ? 81  ILE   F C      1 
ATOM   15149 O  O      . ILE   F 4  81  ? -11.204 -69.276  99.546  1.00 76.95  ? 81  ILE   F O      1 
ATOM   15150 C  CB     . ILE   F 4  81  ? -10.615 -66.098  98.837  1.00 64.35  ? 81  ILE   F CB     1 
ATOM   15151 C  CG1    . ILE   F 4  81  ? -9.698  -65.343  97.881  1.00 61.06  ? 81  ILE   F CG1    1 
ATOM   15152 C  CG2    . ILE   F 4  81  ? -9.864  -66.503  100.078 1.00 67.83  ? 81  ILE   F CG2    1 
ATOM   15153 C  CD1    . ILE   F 4  81  ? -9.012  -64.175  98.474  1.00 62.22  ? 81  ILE   F CD1    1 
ATOM   15154 N  N      . LYS   F 4  82  ? -13.105 -68.089  99.418  1.00 73.79  ? 82  LYS   F N      1 
ATOM   15155 C  CA     . LYS   F 4  82  ? -13.828 -68.987  100.310 1.00 73.30  ? 82  LYS   F CA     1 
ATOM   15156 C  C      . LYS   F 4  82  ? -13.995 -70.380  99.705  1.00 80.31  ? 82  LYS   F C      1 
ATOM   15157 O  O      . LYS   F 4  82  ? -13.946 -71.373  100.436 1.00 90.37  ? 82  LYS   F O      1 
ATOM   15158 C  CB     . LYS   F 4  82  ? -15.188 -68.364  100.631 1.00 72.75  ? 82  LYS   F CB     1 
ATOM   15159 C  CG     . LYS   F 4  82  ? -15.183 -67.386  101.811 1.00 81.10  ? 82  LYS   F CG     1 
ATOM   15160 C  CD     . LYS   F 4  82  ? -16.489 -66.603  101.867 1.00 89.28  ? 82  LYS   F CD     1 
ATOM   15161 C  CE     . LYS   F 4  82  ? -16.915 -66.182  103.264 1.00 98.28  ? 82  LYS   F CE     1 
ATOM   15162 N  NZ     . LYS   F 4  82  ? -18.258 -65.494  103.205 1.00 103.53 ? 82  LYS   F NZ     1 
ATOM   15163 N  N      . THR   F 4  83  ? -14.178 -70.485  98.384  1.00 74.38  ? 83  THR   F N      1 
ATOM   15164 C  CA     . THR   F 4  83  ? -14.607 -71.735  97.764  1.00 72.91  ? 83  THR   F CA     1 
ATOM   15165 C  C      . THR   F 4  83  ? -13.539 -72.410  96.916  1.00 80.14  ? 83  THR   F C      1 
ATOM   15166 O  O      . THR   F 4  83  ? -13.801 -73.480  96.357  1.00 75.02  ? 83  THR   F O      1 
ATOM   15167 C  CB     . THR   F 4  83  ? -15.833 -71.511  96.880  1.00 72.94  ? 83  THR   F CB     1 
ATOM   15168 O  OG1    . THR   F 4  83  ? -15.607 -70.365  96.054  1.00 79.99  ? 83  THR   F OG1    1 
ATOM   15169 C  CG2    . THR   F 4  83  ? -17.079 -71.290  97.724  1.00 68.10  ? 83  THR   F CG2    1 
ATOM   15170 N  N      . SER   F 4  84  ? -12.378 -71.821  96.761  1.00 84.28  ? 84  SER   F N      1 
ATOM   15171 C  CA     . SER   F 4  84  ? -11.428 -72.683  96.069  1.00 78.28  ? 84  SER   F CA     1 
ATOM   15172 C  C      . SER   F 4  84  ? -10.521 -73.341  97.085  1.00 80.10  ? 84  SER   F C      1 
ATOM   15173 O  O      . SER   F 4  84  ? -9.980  -72.649  97.962  1.00 80.18  ? 84  SER   F O      1 
ATOM   15174 C  CB     . SER   F 4  84  ? -10.590 -71.901  95.059  1.00 76.98  ? 84  SER   F CB     1 
ATOM   15175 O  OG     . SER   F 4  84  ? -11.397 -71.095  94.224  1.00 78.82  ? 84  SER   F OG     1 
ATOM   15176 N  N      . PRO   F 4  85  ? -10.351 -74.658  97.011  1.00 79.37  ? 85  PRO   F N      1 
ATOM   15177 C  CA     . PRO   F 4  85  ? -9.408  -75.324  97.926  1.00 78.99  ? 85  PRO   F CA     1 
ATOM   15178 C  C      . PRO   F 4  85  ? -8.037  -74.678  97.930  1.00 75.61  ? 85  PRO   F C      1 
ATOM   15179 O  O      . PRO   F 4  85  ? -7.397  -74.581  98.983  1.00 78.80  ? 85  PRO   F O      1 
ATOM   15180 C  CB     . PRO   F 4  85  ? -9.363  -76.761  97.393  1.00 74.85  ? 85  PRO   F CB     1 
ATOM   15181 C  CG     . PRO   F 4  85  ? -10.672 -76.932  96.688  1.00 83.91  ? 85  PRO   F CG     1 
ATOM   15182 C  CD     . PRO   F 4  85  ? -11.002 -75.597  96.088  1.00 78.03  ? 85  PRO   F CD     1 
ATOM   15183 N  N      . GLU   F 4  86  ? -7.580  -74.212  96.769  1.00 78.35  ? 86  GLU   F N      1 
ATOM   15184 C  CA     . GLU   F 4  86  ? -6.252  -73.621  96.642  1.00 81.83  ? 86  GLU   F CA     1 
ATOM   15185 C  C      . GLU   F 4  86  ? -6.053  -72.458  97.595  1.00 78.28  ? 86  GLU   F C      1 
ATOM   15186 O  O      . GLU   F 4  86  ? -4.908  -72.086  97.865  1.00 73.98  ? 86  GLU   F O      1 
ATOM   15187 C  CB     . GLU   F 4  86  ? -6.033  -73.149  95.202  1.00 80.76  ? 86  GLU   F CB     1 
ATOM   15188 C  CG     . GLU   F 4  86  ? -5.977  -74.285  94.205  1.00 85.21  ? 86  GLU   F CG     1 
ATOM   15189 C  CD     . GLU   F 4  86  ? -7.293  -74.417  93.435  1.00 95.84  ? 86  GLU   F CD     1 
ATOM   15190 O  OE1    . GLU   F 4  86  ? -8.371  -74.601  94.071  1.00 88.61  ? 86  GLU   F OE1    1 
ATOM   15191 O  OE2    . GLU   F 4  86  ? -7.251  -74.313  92.187  1.00 101.42 ? 86  GLU   F OE2    1 
ATOM   15192 N  N      . LEU   F 4  87  ? -7.138  -71.865  98.082  1.00 76.70  ? 87  LEU   F N      1 
ATOM   15193 C  CA     . LEU   F 4  87  ? -7.113  -70.726  98.987  1.00 77.62  ? 87  LEU   F CA     1 
ATOM   15194 C  C      . LEU   F 4  87  ? -7.760  -71.024  100.327 1.00 88.07  ? 87  LEU   F C      1 
ATOM   15195 O  O      . LEU   F 4  87  ? -7.192  -70.681  101.369 1.00 94.47  ? 87  LEU   F O      1 
ATOM   15196 C  CB     . LEU   F 4  87  ? -7.796  -69.522  98.326  1.00 75.90  ? 87  LEU   F CB     1 
ATOM   15197 C  CG     . LEU   F 4  87  ? -7.483  -69.323  96.842  1.00 70.34  ? 87  LEU   F CG     1 
ATOM   15198 C  CD1    . LEU   F 4  87  ? -7.994  -67.986  96.331  1.00 61.30  ? 87  LEU   F CD1    1 
ATOM   15199 C  CD2    . LEU   F 4  87  ? -5.987  -69.413  96.651  1.00 59.35  ? 87  LEU   F CD2    1 
ATOM   15200 N  N      . SER   F 4  88  ? -8.933  -71.660  100.322 1.00 91.92  ? 88  SER   F N      1 
ATOM   15201 C  CA     . SER   F 4  88  ? -9.550  -72.203  101.527 1.00 95.10  ? 88  SER   F CA     1 
ATOM   15202 C  C      . SER   F 4  88  ? -9.988  -71.109  102.493 1.00 98.87  ? 88  SER   F C      1 
ATOM   15203 O  O      . SER   F 4  88  ? -9.396  -70.024  102.526 1.00 100.22 ? 88  SER   F O      1 
ATOM   15204 C  CB     . SER   F 4  88  ? -8.591  -73.188  102.218 1.00 95.13  ? 88  SER   F CB     1 
ATOM   15205 O  OG     . SER   F 4  88  ? -7.488  -72.537  102.823 1.00 96.82  ? 88  SER   F OG     1 
ATOM   15206 N  N      . GLU   F 4  89  ? -11.052 -71.378  103.259 1.00 102.94 ? 89  GLU   F N      1 
ATOM   15207 C  CA     . GLU   F 4  89  ? -11.407 -70.504  104.374 1.00 110.10 ? 89  GLU   F CA     1 
ATOM   15208 C  C      . GLU   F 4  89  ? -10.189 -70.219  105.248 1.00 112.30 ? 89  GLU   F C      1 
ATOM   15209 O  O      . GLU   F 4  89  ? -9.976  -69.085  105.694 1.00 114.37 ? 89  GLU   F O      1 
ATOM   15210 C  CB     . GLU   F 4  89  ? -12.526 -71.144  105.201 1.00 111.03 ? 89  GLU   F CB     1 
ATOM   15211 C  CG     . GLU   F 4  89  ? -12.904 -70.391  106.486 1.00 115.53 ? 89  GLU   F CG     1 
ATOM   15212 C  CD     . GLU   F 4  89  ? -12.850 -68.862  106.372 1.00 119.76 ? 89  GLU   F CD     1 
ATOM   15213 O  OE1    . GLU   F 4  89  ? -12.894 -68.318  105.240 1.00 117.94 ? 89  GLU   F OE1    1 
ATOM   15214 O  OE2    . GLU   F 4  89  ? -12.741 -68.204  107.430 1.00 108.78 ? 89  GLU   F OE2    1 
ATOM   15215 N  N      . SER   F 4  90  ? -9.378  -71.245  105.508 1.00 112.67 ? 90  SER   F N      1 
ATOM   15216 C  CA     . SER   F 4  90  ? -8.091  -71.047  106.157 1.00 112.71 ? 90  SER   F CA     1 
ATOM   15217 C  C      . SER   F 4  90  ? -7.135  -70.423  105.147 1.00 112.20 ? 90  SER   F C      1 
ATOM   15218 O  O      . SER   F 4  90  ? -6.229  -71.083  104.629 1.00 118.91 ? 90  SER   F O      1 
ATOM   15219 C  CB     . SER   F 4  90  ? -7.554  -72.366  106.721 1.00 111.59 ? 90  SER   F CB     1 
ATOM   15220 O  OG     . SER   F 4  90  ? -7.519  -73.384  105.734 1.00 109.74 ? 90  SER   F OG     1 
ATOM   15221 N  N      . CYS   F 4  91  ? -7.372  -69.157  104.827 1.00 103.84 ? 91  CYS   F N      1 
ATOM   15222 C  CA     . CYS   F 4  91  ? -6.478  -68.359  104.004 1.00 96.24  ? 91  CYS   F CA     1 
ATOM   15223 C  C      . CYS   F 4  91  ? -5.884  -67.289  104.902 1.00 91.51  ? 91  CYS   F C      1 
ATOM   15224 O  O      . CYS   F 4  91  ? -6.619  -66.596  105.613 1.00 96.78  ? 91  CYS   F O      1 
ATOM   15225 C  CB     . CYS   F 4  91  ? -7.216  -67.733  102.820 1.00 93.99  ? 91  CYS   F CB     1 
ATOM   15226 S  SG     . CYS   F 4  91  ? -6.155  -66.772  101.741 1.00 85.13  ? 91  CYS   F SG     1 
ATOM   15227 N  N      . THR   F 4  92  ? -4.562  -67.173  104.887 1.00 81.56  ? 92  THR   F N      1 
ATOM   15228 C  CA     . THR   F 4  92  ? -3.852  -66.461  105.940 1.00 76.66  ? 92  THR   F CA     1 
ATOM   15229 C  C      . THR   F 4  92  ? -3.501  -65.022  105.604 1.00 77.33  ? 92  THR   F C      1 
ATOM   15230 O  O      . THR   F 4  92  ? -2.981  -64.322  106.473 1.00 73.25  ? 92  THR   F O      1 
ATOM   15231 C  CB     . THR   F 4  92  ? -2.570  -67.197  106.281 1.00 78.29  ? 92  THR   F CB     1 
ATOM   15232 O  OG1    . THR   F 4  92  ? -2.003  -66.604  107.447 1.00 85.52  ? 92  THR   F OG1    1 
ATOM   15233 C  CG2    . THR   F 4  92  ? -1.593  -67.058  105.138 1.00 76.87  ? 92  THR   F CG2    1 
ATOM   15234 N  N      . TRP   F 4  93  ? -3.741  -64.573  104.367 1.00 78.44  ? 93  TRP   F N      1 
ATOM   15235 C  CA     . TRP   F 4  93  ? -3.396  -63.220  103.937 1.00 72.18  ? 93  TRP   F CA     1 
ATOM   15236 C  C      . TRP   F 4  93  ? -4.597  -62.445  103.405 1.00 73.39  ? 93  TRP   F C      1 
ATOM   15237 O  O      . TRP   F 4  93  ? -4.420  -61.345  102.860 1.00 72.90  ? 93  TRP   F O      1 
ATOM   15238 C  CB     . TRP   F 4  93  ? -2.302  -63.265  102.873 1.00 69.40  ? 93  TRP   F CB     1 
ATOM   15239 C  CG     . TRP   F 4  93  ? -2.567  -64.368  101.930 1.00 70.97  ? 93  TRP   F CG     1 
ATOM   15240 C  CD1    . TRP   F 4  93  ? -2.039  -65.616  101.976 1.00 66.42  ? 93  TRP   F CD1    1 
ATOM   15241 C  CD2    . TRP   F 4  93  ? -3.512  -64.370  100.865 1.00 71.16  ? 93  TRP   F CD2    1 
ATOM   15242 N  NE1    . TRP   F 4  93  ? -2.553  -66.378  100.977 1.00 66.77  ? 93  TRP   F NE1    1 
ATOM   15243 C  CE2    . TRP   F 4  93  ? -3.471  -65.639  100.280 1.00 69.07  ? 93  TRP   F CE2    1 
ATOM   15244 C  CE3    . TRP   F 4  93  ? -4.371  -63.409  100.331 1.00 73.09  ? 93  TRP   F CE3    1 
ATOM   15245 C  CZ2    . TRP   F 4  93  ? -4.257  -65.980  99.187  1.00 71.48  ? 93  TRP   F CZ2    1 
ATOM   15246 C  CZ3    . TRP   F 4  93  ? -5.153  -63.745  99.253  1.00 69.22  ? 93  TRP   F CZ3    1 
ATOM   15247 C  CH2    . TRP   F 4  93  ? -5.093  -65.021  98.690  1.00 75.00  ? 93  TRP   F CH2    1 
ATOM   15248 N  N      . PHE   F 4  94  ? -5.806  -62.981  103.537 1.00 70.01  ? 94  PHE   F N      1 
ATOM   15249 C  CA     . PHE   F 4  94  ? -6.986  -62.222  103.182 1.00 70.81  ? 94  PHE   F CA     1 
ATOM   15250 C  C      . PHE   F 4  94  ? -7.787  -61.919  104.437 1.00 73.26  ? 94  PHE   F C      1 
ATOM   15251 O  O      . PHE   F 4  94  ? -7.978  -62.811  105.272 1.00 77.00  ? 94  PHE   F O      1 
ATOM   15252 C  CB     . PHE   F 4  94  ? -7.840  -62.989  102.159 1.00 69.43  ? 94  PHE   F CB     1 
ATOM   15253 C  CG     . PHE   F 4  94  ? -8.861  -62.140  101.464 1.00 65.65  ? 94  PHE   F CG     1 
ATOM   15254 C  CD1    . PHE   F 4  94  ? -8.485  -60.980  100.810 1.00 68.36  ? 94  PHE   F CD1    1 
ATOM   15255 C  CD2    . PHE   F 4  94  ? -10.194 -62.527  101.425 1.00 65.55  ? 94  PHE   F CD2    1 
ATOM   15256 C  CE1    . PHE   F 4  94  ? -9.424  -60.189  100.171 1.00 68.25  ? 94  PHE   F CE1    1 
ATOM   15257 C  CE2    . PHE   F 4  94  ? -11.139 -61.745  100.787 1.00 66.73  ? 94  PHE   F CE2    1 
ATOM   15258 C  CZ     . PHE   F 4  94  ? -10.752 -60.576  100.154 1.00 69.28  ? 94  PHE   F CZ     1 
ATOM   15259 N  N      . PRO   F 4  95  ? -8.200  -60.671  104.638 1.00 73.04  ? 95  PRO   F N      1 
ATOM   15260 C  CA     . PRO   F 4  95  ? -9.030  -60.340  105.803 1.00 79.44  ? 95  PRO   F CA     1 
ATOM   15261 C  C      . PRO   F 4  95  ? -10.411 -60.970  105.714 1.00 86.02  ? 95  PRO   F C      1 
ATOM   15262 O  O      . PRO   F 4  95  ? -10.974 -61.124  104.629 1.00 83.42  ? 95  PRO   F O      1 
ATOM   15263 C  CB     . PRO   F 4  95  ? -9.123  -58.809  105.747 1.00 88.50  ? 95  PRO   F CB     1 
ATOM   15264 C  CG     . PRO   F 4  95  ? -7.936  -58.375  104.905 1.00 82.52  ? 95  PRO   F CG     1 
ATOM   15265 C  CD     . PRO   F 4  95  ? -7.729  -59.477  103.915 1.00 76.15  ? 95  PRO   F CD     1 
ATOM   15266 N  N      . GLU   F 4  96  ? -10.962 -61.328  106.879 1.00 90.06  ? 96  GLU   F N      1 
ATOM   15267 C  CA     . GLU   F 4  96  ? -12.322 -61.862  106.937 1.00 89.90  ? 96  GLU   F CA     1 
ATOM   15268 C  C      . GLU   F 4  96  ? -13.269 -61.039  106.082 1.00 92.89  ? 96  GLU   F C      1 
ATOM   15269 O  O      . GLU   F 4  96  ? -13.256 -59.807  106.124 1.00 100.49 ? 96  GLU   F O      1 
ATOM   15270 C  CB     . GLU   F 4  96  ? -12.837 -61.873  108.369 1.00 98.51  ? 96  GLU   F CB     1 
ATOM   15271 C  CG     . GLU   F 4  96  ? -12.645 -63.167  109.097 1.00 100.75 ? 96  GLU   F CG     1 
ATOM   15272 C  CD     . GLU   F 4  96  ? -13.482 -63.215  110.347 1.00 103.96 ? 96  GLU   F CD     1 
ATOM   15273 O  OE1    . GLU   F 4  96  ? -14.687 -62.888  110.271 1.00 104.36 ? 96  GLU   F OE1    1 
ATOM   15274 O  OE2    . GLU   F 4  96  ? -12.933 -63.573  111.405 1.00 111.17 ? 96  GLU   F OE2    1 
ATOM   15275 N  N      . SER   F 4  97  ? -14.111 -61.725  105.319 1.00 91.12  ? 97  SER   F N      1 
ATOM   15276 C  CA     . SER   F 4  97  ? -14.944 -61.037  104.349 1.00 91.49  ? 97  SER   F CA     1 
ATOM   15277 C  C      . SER   F 4  97  ? -16.240 -61.798  104.127 1.00 95.79  ? 97  SER   F C      1 
ATOM   15278 O  O      . SER   F 4  97  ? -16.247 -63.029  104.022 1.00 90.55  ? 97  SER   F O      1 
ATOM   15279 C  CB     . SER   F 4  97  ? -14.202 -60.860  103.024 1.00 91.38  ? 97  SER   F CB     1 
ATOM   15280 O  OG     . SER   F 4  97  ? -12.987 -60.162  103.226 1.00 90.29  ? 97  SER   F OG     1 
ATOM   15281 N  N      . TYR   F 4  98  ? -17.330 -61.043  104.033 1.00 101.95 ? 98  TYR   F N      1 
ATOM   15282 C  CA     . TYR   F 4  98  ? -18.658 -61.588  103.824 1.00 104.38 ? 98  TYR   F CA     1 
ATOM   15283 C  C      . TYR   F 4  98  ? -19.349 -60.758  102.749 1.00 110.14 ? 98  TYR   F C      1 
ATOM   15284 O  O      . TYR   F 4  98  ? -19.101 -59.553  102.630 1.00 109.14 ? 98  TYR   F O      1 
ATOM   15285 C  CB     . TYR   F 4  98  ? -19.451 -61.553  105.133 1.00 114.42 ? 98  TYR   F CB     1 
ATOM   15286 C  CG     . TYR   F 4  98  ? -18.767 -62.246  106.303 1.00 108.69 ? 98  TYR   F CG     1 
ATOM   15287 C  CD1    . TYR   F 4  98  ? -18.954 -63.599  106.545 1.00 108.73 ? 98  TYR   F CD1    1 
ATOM   15288 C  CD2    . TYR   F 4  98  ? -17.911 -61.548  107.145 1.00 104.54 ? 98  TYR   F CD2    1 
ATOM   15289 C  CE1    . TYR   F 4  98  ? -18.335 -64.227  107.606 1.00 104.48 ? 98  TYR   F CE1    1 
ATOM   15290 C  CE2    . TYR   F 4  98  ? -17.282 -62.174  108.201 1.00 100.08 ? 98  TYR   F CE2    1 
ATOM   15291 C  CZ     . TYR   F 4  98  ? -17.497 -63.512  108.420 1.00 98.77  ? 98  TYR   F CZ     1 
ATOM   15292 O  OH     . TYR   F 4  98  ? -16.877 -64.143  109.465 1.00 105.07 ? 98  TYR   F OH     1 
ATOM   15293 N  N      . VAL   F 4  99  ? -20.208 -61.409  101.959 1.00 114.16 ? 99  VAL   F N      1 
ATOM   15294 C  CA     . VAL   F 4  99  ? -21.008 -60.729  100.939 1.00 119.22 ? 99  VAL   F CA     1 
ATOM   15295 C  C      . VAL   F 4  99  ? -22.435 -60.577  101.460 1.00 121.08 ? 99  VAL   F C      1 
ATOM   15296 O  O      . VAL   F 4  99  ? -23.112 -61.570  101.763 1.00 120.04 ? 99  VAL   F O      1 
ATOM   15297 C  CB     . VAL   F 4  99  ? -20.974 -61.469  99.588  1.00 113.70 ? 99  VAL   F CB     1 
ATOM   15298 C  CG1    . VAL   F 4  99  ? -19.545 -61.629  99.114  1.00 98.59  ? 99  VAL   F CG1    1 
ATOM   15299 C  CG2    . VAL   F 4  99  ? -21.663 -62.834  99.677  1.00 115.53 ? 99  VAL   F CG2    1 
ATOM   15300 N  N      . ILE   F 4  100 ? -22.882 -59.327  101.581 1.00 123.75 ? 100 ILE   F N      1 
ATOM   15301 C  CA     . ILE   F 4  100 ? -24.222 -58.995  102.049 1.00 127.65 ? 100 ILE   F CA     1 
ATOM   15302 C  C      . ILE   F 4  100 ? -24.899 -58.184  100.950 1.00 127.48 ? 100 ILE   F C      1 
ATOM   15303 O  O      . ILE   F 4  100 ? -24.334 -57.197  100.463 1.00 120.38 ? 100 ILE   F O      1 
ATOM   15304 C  CB     . ILE   F 4  100 ? -24.198 -58.207  103.376 1.00 124.41 ? 100 ILE   F CB     1 
ATOM   15305 C  CG1    . ILE   F 4  100 ? -23.113 -58.731  104.331 1.00 115.63 ? 100 ILE   F CG1    1 
ATOM   15306 C  CG2    . ILE   F 4  100 ? -25.562 -58.255  104.051 1.00 124.83 ? 100 ILE   F CG2    1 
ATOM   15307 C  CD1    . ILE   F 4  100 ? -23.248 -60.178  104.725 1.00 115.77 ? 100 ILE   F CD1    1 
ATOM   15308 N  N      . TYR   F 4  101 ? -26.135 -58.618  100.545 1.00 128.55 ? 101 TYR   F N      1 
ATOM   15309 C  CA     . TYR   F 4  101 ? -26.928 -57.972  99.509  1.00 128.64 ? 101 TYR   F CA     1 
ATOM   15310 C  C      . TYR   F 4  101 ? -27.976 -57.049  100.136 1.00 131.06 ? 101 TYR   F C      1 
ATOM   15311 O  O      . TYR   F 4  101 ? -28.386 -57.258  101.283 1.00 132.20 ? 101 TYR   F O      1 
ATOM   15312 C  CB     . TYR   F 4  101 ? -27.610 -59.029  98.628  1.00 123.54 ? 101 TYR   F CB     1 
ATOM   15313 C  CG     . TYR   F 4  101 ? -26.665 -59.821  97.723  1.00 121.89 ? 101 TYR   F CG     1 
ATOM   15314 C  CD1    . TYR   F 4  101 ? -25.297 -59.582  97.723  1.00 127.79 ? 101 TYR   F CD1    1 
ATOM   15315 C  CD2    . TYR   F 4  101 ? -27.151 -60.801  96.859  1.00 118.28 ? 101 TYR   F CD2    1 
ATOM   15316 C  CE1    . TYR   F 4  101 ? -24.440 -60.298  96.894  1.00 121.35 ? 101 TYR   F CE1    1 
ATOM   15317 C  CE2    . TYR   F 4  101 ? -26.300 -61.515  96.029  1.00 109.46 ? 101 TYR   F CE2    1 
ATOM   15318 C  CZ     . TYR   F 4  101 ? -24.953 -61.257  96.052  1.00 109.27 ? 101 TYR   F CZ     1 
ATOM   15319 O  OH     . TYR   F 4  101 ? -24.113 -61.963  95.235  1.00 108.09 ? 101 TYR   F OH     1 
ATOM   15320 N  N      . PRO   F 4  102 ? -28.415 -55.978  99.438  1.00 132.44 ? 102 PRO   F N      1 
ATOM   15321 C  CA     . PRO   F 4  102 ? -29.421 -55.077  100.027 1.00 140.34 ? 102 PRO   F CA     1 
ATOM   15322 C  C      . PRO   F 4  102 ? -30.843 -55.256  99.501  1.00 139.96 ? 102 PRO   F C      1 
ATOM   15323 O  O      . PRO   F 4  102 ? -31.142 -54.847  98.373  1.00 140.26 ? 102 PRO   F O      1 
ATOM   15324 C  CB     . PRO   F 4  102 ? -28.890 -53.692  99.646  1.00 142.47 ? 102 PRO   F CB     1 
ATOM   15325 C  CG     . PRO   F 4  102 ? -28.296 -53.920  98.300  1.00 140.00 ? 102 PRO   F CG     1 
ATOM   15326 C  CD     . PRO   F 4  102 ? -27.716 -55.333  98.313  1.00 135.10 ? 102 PRO   F CD     1 
ATOM   15327 N  N      . THR   F 4  103 ? -31.729 -55.846  100.302 1.00 135.64 ? 103 THR   F N      1 
ATOM   15328 C  CA     . THR   F 4  103 ? -33.167 -55.806  100.029 1.00 129.20 ? 103 THR   F CA     1 
ATOM   15329 C  C      . THR   F 4  103 ? -33.831 -55.208  101.253 1.00 129.40 ? 103 THR   F C      1 
ATOM   15330 O  O      . THR   F 4  103 ? -33.147 -54.871  102.220 1.00 130.43 ? 103 THR   F O      1 
ATOM   15331 C  CB     . THR   F 4  103 ? -33.784 -57.204  99.719  1.00 129.48 ? 103 THR   F CB     1 
ATOM   15332 O  OG1    . THR   F 4  103 ? -33.004 -57.883  98.727  1.00 127.27 ? 103 THR   F OG1    1 
ATOM   15333 C  CG2    . THR   F 4  103 ? -35.221 -57.070  99.225  1.00 121.32 ? 103 THR   F CG2    1 
ATOM   15334 N  N      . ARG   F 4  128 ? -25.903 -60.689  105.611 1.00 127.00 ? 128 ARG   F N      1 
ATOM   15335 C  CA     . ARG   F 4  128 ? -25.696 -61.036  107.006 1.00 128.76 ? 128 ARG   F CA     1 
ATOM   15336 C  C      . ARG   F 4  128 ? -25.576 -62.543  107.115 1.00 127.38 ? 128 ARG   F C      1 
ATOM   15337 O  O      . ARG   F 4  128 ? -25.595 -63.095  108.220 1.00 121.56 ? 128 ARG   F O      1 
ATOM   15338 C  CB     . ARG   F 4  128 ? -26.845 -60.500  107.862 1.00 131.67 ? 128 ARG   F CB     1 
ATOM   15339 C  CG     . ARG   F 4  128 ? -27.274 -59.113  107.414 1.00 128.10 ? 128 ARG   F CG     1 
ATOM   15340 C  CD     . ARG   F 4  128 ? -28.246 -59.177  106.251 1.00 120.78 ? 128 ARG   F CD     1 
ATOM   15341 N  NE     . ARG   F 4  128 ? -28.411 -57.871  105.626 1.00 129.61 ? 128 ARG   F NE     1 
ATOM   15342 C  CZ     . ARG   F 4  128 ? -29.235 -56.923  106.048 1.00 134.31 ? 128 ARG   F CZ     1 
ATOM   15343 N  NH1    . ARG   F 4  128 ? -29.992 -57.093  107.119 1.00 128.91 ? 128 ARG   F NH1    1 
ATOM   15344 N  NH2    . ARG   F 4  128 ? -29.294 -55.773  105.380 1.00 135.55 ? 128 ARG   F NH2    1 
ATOM   15345 N  N      . GLU   F 4  129 ? -25.440 -63.178  105.938 1.00 134.51 ? 129 GLU   F N      1 
ATOM   15346 C  CA     . GLU   F 4  129 ? -25.425 -64.632  105.766 1.00 132.90 ? 129 GLU   F CA     1 
ATOM   15347 C  C      . GLU   F 4  129 ? -24.928 -65.316  107.031 1.00 134.94 ? 129 GLU   F C      1 
ATOM   15348 O  O      . GLU   F 4  129 ? -25.722 -65.868  107.799 1.00 141.78 ? 129 GLU   F O      1 
ATOM   15349 C  CB     . GLU   F 4  129 ? -24.563 -65.044  104.558 1.00 122.21 ? 129 GLU   F CB     1 
ATOM   15350 C  CG     . GLU   F 4  129 ? -25.265 -65.007  103.195 1.00 113.96 ? 129 GLU   F CG     1 
ATOM   15351 C  CD     . GLU   F 4  129 ? -25.486 -63.606  102.670 1.00 111.91 ? 129 GLU   F CD     1 
ATOM   15352 O  OE1    . GLU   F 4  129 ? -25.160 -62.642  103.382 1.00 116.10 ? 129 GLU   F OE1    1 
ATOM   15353 O  OE2    . GLU   F 4  129 ? -25.988 -63.462  101.542 1.00 112.93 ? 129 GLU   F OE2    1 
ATOM   15354 N  N      . VAL   F 4  130 ? -23.619 -65.267  107.261 1.00 137.03 ? 130 VAL   F N      1 
ATOM   15355 C  CA     . VAL   F 4  130 ? -23.032 -65.696  108.526 1.00 137.28 ? 130 VAL   F CA     1 
ATOM   15356 C  C      . VAL   F 4  130 ? -22.136 -64.567  109.017 1.00 133.32 ? 130 VAL   F C      1 
ATOM   15357 O  O      . VAL   F 4  130 ? -21.213 -64.783  109.812 1.00 130.05 ? 130 VAL   F O      1 
ATOM   15358 C  CB     . VAL   F 4  130 ? -22.249 -67.014  108.384 1.00 132.01 ? 130 VAL   F CB     1 
ATOM   15359 C  CG1    . VAL   F 4  130 ? -21.843 -67.538  109.753 1.00 139.76 ? 130 VAL   F CG1    1 
ATOM   15360 C  CG2    . VAL   F 4  130 ? -23.075 -68.051  107.632 1.00 129.97 ? 130 VAL   F CG2    1 
ATOM   15361 N  N      . PHE   F 4  131 ? -22.389 -63.354  108.518 1.00 132.95 ? 131 PHE   F N      1 
ATOM   15362 C  CA     . PHE   F 4  131 ? -21.668 -62.187  109.007 1.00 127.08 ? 131 PHE   F CA     1 
ATOM   15363 C  C      . PHE   F 4  131 ? -21.996 -61.917  110.461 1.00 138.67 ? 131 PHE   F C      1 
ATOM   15364 O  O      . PHE   F 4  131 ? -21.111 -61.582  111.257 1.00 139.56 ? 131 PHE   F O      1 
ATOM   15365 C  CB     . PHE   F 4  131 ? -22.016 -60.959  108.178 1.00 127.43 ? 131 PHE   F CB     1 
ATOM   15366 C  CG     . PHE   F 4  131 ? -21.733 -59.669  108.890 1.00 133.26 ? 131 PHE   F CG     1 
ATOM   15367 C  CD1    . PHE   F 4  131 ? -20.477 -59.417  109.423 1.00 133.70 ? 131 PHE   F CD1    1 
ATOM   15368 C  CD2    . PHE   F 4  131 ? -22.732 -58.726  109.063 1.00 135.89 ? 131 PHE   F CD2    1 
ATOM   15369 C  CE1    . PHE   F 4  131 ? -20.212 -58.241  110.092 1.00 133.52 ? 131 PHE   F CE1    1 
ATOM   15370 C  CE2    . PHE   F 4  131 ? -22.474 -57.546  109.731 1.00 136.35 ? 131 PHE   F CE2    1 
ATOM   15371 C  CZ     . PHE   F 4  131 ? -21.211 -57.303  110.245 1.00 136.49 ? 131 PHE   F CZ     1 
ATOM   15372 N  N      . LEU   F 4  132 ? -23.275 -62.037  110.816 1.00 144.27 ? 132 LEU   F N      1 
ATOM   15373 C  CA     . LEU   F 4  132 ? -23.715 -61.665  112.153 1.00 145.54 ? 132 LEU   F CA     1 
ATOM   15374 C  C      . LEU   F 4  132 ? -23.025 -62.521  113.210 1.00 144.12 ? 132 LEU   F C      1 
ATOM   15375 O  O      . LEU   F 4  132 ? -22.644 -62.020  114.274 1.00 145.08 ? 132 LEU   F O      1 
ATOM   15376 C  CB     . LEU   F 4  132 ? -25.234 -61.806  112.241 1.00 144.71 ? 132 LEU   F CB     1 
ATOM   15377 C  CG     . LEU   F 4  132 ? -26.060 -60.589  111.803 1.00 139.20 ? 132 LEU   F CG     1 
ATOM   15378 C  CD1    . LEU   F 4  132 ? -27.549 -60.841  112.023 1.00 138.24 ? 132 LEU   F CD1    1 
ATOM   15379 C  CD2    . LEU   F 4  132 ? -25.605 -59.290  112.456 1.00 136.04 ? 132 LEU   F CD2    1 
ATOM   15380 N  N      . ALA   F 4  133 ? -22.836 -63.816  112.922 1.00 144.35 ? 133 ALA   F N      1 
ATOM   15381 C  CA     . ALA   F 4  133 ? -22.285 -64.736  113.915 1.00 146.45 ? 133 ALA   F CA     1 
ATOM   15382 C  C      . ALA   F 4  133 ? -20.815 -64.461  114.192 1.00 146.33 ? 133 ALA   F C      1 
ATOM   15383 O  O      . ALA   F 4  133 ? -20.304 -64.831  115.255 1.00 150.48 ? 133 ALA   F O      1 
ATOM   15384 C  CB     . ALA   F 4  133 ? -22.469 -66.181  113.454 1.00 152.74 ? 133 ALA   F CB     1 
ATOM   15385 N  N      . ALA   F 4  134 ? -20.112 -63.849  113.242 1.00 141.85 ? 134 ALA   F N      1 
ATOM   15386 C  CA     . ALA   F 4  134 ? -18.740 -63.436  113.497 1.00 142.53 ? 134 ALA   F CA     1 
ATOM   15387 C  C      . ALA   F 4  134 ? -18.705 -62.211  114.402 1.00 148.34 ? 134 ALA   F C      1 
ATOM   15388 O  O      . ALA   F 4  134 ? -18.020 -62.208  115.430 1.00 149.49 ? 134 ALA   F O      1 
ATOM   15389 C  CB     . ALA   F 4  134 ? -18.029 -63.159  112.175 1.00 138.84 ? 134 ALA   F CB     1 
ATOM   15390 N  N      . TYR   F 4  135 ? -19.445 -61.163  114.034 1.00 150.77 ? 135 TYR   F N      1 
ATOM   15391 C  CA     . TYR   F 4  135 ? -19.486 -59.950  114.843 1.00 152.58 ? 135 TYR   F CA     1 
ATOM   15392 C  C      . TYR   F 4  135 ? -19.790 -60.260  116.305 1.00 153.90 ? 135 TYR   F C      1 
ATOM   15393 O  O      . TYR   F 4  135 ? -19.176 -59.680  117.209 1.00 151.95 ? 135 TYR   F O      1 
ATOM   15394 C  CB     . TYR   F 4  135 ? -20.527 -58.992  114.268 1.00 148.54 ? 135 TYR   F CB     1 
ATOM   15395 C  CG     . TYR   F 4  135 ? -20.380 -57.558  114.714 1.00 145.04 ? 135 TYR   F CG     1 
ATOM   15396 C  CD1    . TYR   F 4  135 ? -19.263 -57.128  115.418 1.00 142.11 ? 135 TYR   F CD1    1 
ATOM   15397 C  CD2    . TYR   F 4  135 ? -21.368 -56.628  114.424 1.00 144.81 ? 135 TYR   F CD2    1 
ATOM   15398 C  CE1    . TYR   F 4  135 ? -19.144 -55.803  115.816 1.00 140.28 ? 135 TYR   F CE1    1 
ATOM   15399 C  CE2    . TYR   F 4  135 ? -21.257 -55.314  114.818 1.00 138.27 ? 135 TYR   F CE2    1 
ATOM   15400 C  CZ     . TYR   F 4  135 ? -20.151 -54.902  115.509 1.00 138.22 ? 135 TYR   F CZ     1 
ATOM   15401 O  OH     . TYR   F 4  135 ? -20.069 -53.583  115.885 1.00 133.62 ? 135 TYR   F OH     1 
ATOM   15402 N  N      . ASN   F 4  136 ? -20.739 -61.173  116.558 1.00 153.77 ? 136 ASN   F N      1 
ATOM   15403 C  CA     . ASN   F 4  136 ? -21.064 -61.547  117.934 1.00 153.25 ? 136 ASN   F CA     1 
ATOM   15404 C  C      . ASN   F 4  136 ? -19.902 -62.253  118.619 1.00 156.23 ? 136 ASN   F C      1 
ATOM   15405 O  O      . ASN   F 4  136 ? -19.659 -62.030  119.810 1.00 158.22 ? 136 ASN   F O      1 
ATOM   15406 C  CB     . ASN   F 4  136 ? -22.313 -62.423  117.976 1.00 153.71 ? 136 ASN   F CB     1 
ATOM   15407 C  CG     . ASN   F 4  136 ? -23.555 -61.674  117.575 1.00 156.83 ? 136 ASN   F CG     1 
ATOM   15408 O  OD1    . ASN   F 4  136 ? -23.606 -60.452  117.672 1.00 157.06 ? 136 ASN   F OD1    1 
ATOM   15409 N  ND2    . ASN   F 4  136 ? -24.569 -62.401  117.129 1.00 160.46 ? 136 ASN   F ND2    1 
ATOM   15410 N  N      . ARG   F 4  137 ? -19.182 -63.120  117.899 1.00 155.40 ? 137 ARG   F N      1 
ATOM   15411 C  CA     . ARG   F 4  137 ? -17.955 -63.674  118.463 1.00 157.10 ? 137 ARG   F CA     1 
ATOM   15412 C  C      . ARG   F 4  137 ? -17.065 -62.571  119.017 1.00 158.06 ? 137 ARG   F C      1 
ATOM   15413 O  O      . ARG   F 4  137 ? -16.349 -62.777  120.004 1.00 158.63 ? 137 ARG   F O      1 
ATOM   15414 C  CB     . ARG   F 4  137 ? -17.192 -64.487  117.412 1.00 157.51 ? 137 ARG   F CB     1 
ATOM   15415 C  CG     . ARG   F 4  137 ? -15.704 -64.688  117.731 1.00 161.25 ? 137 ARG   F CG     1 
ATOM   15416 C  CD     . ARG   F 4  137 ? -15.502 -65.362  119.088 1.00 167.07 ? 137 ARG   F CD     1 
ATOM   15417 N  NE     . ARG   F 4  137 ? -14.136 -65.261  119.597 1.00 165.59 ? 137 ARG   F NE     1 
ATOM   15418 C  CZ     . ARG   F 4  137 ? -13.697 -64.311  120.416 1.00 159.54 ? 137 ARG   F CZ     1 
ATOM   15419 N  NH1    . ARG   F 4  137 ? -14.483 -63.328  120.825 1.00 155.26 ? 137 ARG   F NH1    1 
ATOM   15420 N  NH2    . ARG   F 4  137 ? -12.437 -64.353  120.840 1.00 157.36 ? 137 ARG   F NH2    1 
ATOM   15421 N  N      . ARG   F 4  138 ? -17.109 -61.389  118.404 1.00 156.59 ? 138 ARG   F N      1 
ATOM   15422 C  CA     . ARG   F 4  138 ? -16.306 -60.273  118.878 1.00 152.54 ? 138 ARG   F CA     1 
ATOM   15423 C  C      . ARG   F 4  138 ? -16.880 -59.653  120.145 1.00 152.89 ? 138 ARG   F C      1 
ATOM   15424 O  O      . ARG   F 4  138 ? -16.123 -59.201  121.011 1.00 154.78 ? 138 ARG   F O      1 
ATOM   15425 C  CB     . ARG   F 4  138 ? -16.181 -59.245  117.764 1.00 149.21 ? 138 ARG   F CB     1 
ATOM   15426 C  CG     . ARG   F 4  138 ? -15.352 -59.733  116.585 1.00 148.23 ? 138 ARG   F CG     1 
ATOM   15427 C  CD     . ARG   F 4  138 ? -13.948 -60.084  117.067 1.00 147.91 ? 138 ARG   F CD     1 
ATOM   15428 N  NE     . ARG   F 4  138 ? -13.015 -60.393  115.988 1.00 143.19 ? 138 ARG   F NE     1 
ATOM   15429 C  CZ     . ARG   F 4  138 ? -12.089 -59.556  115.543 1.00 132.00 ? 138 ARG   F CZ     1 
ATOM   15430 N  NH1    . ARG   F 4  138 ? -11.971 -58.335  116.030 1.00 134.93 ? 138 ARG   F NH1    1 
ATOM   15431 N  NH2    . ARG   F 4  138 ? -11.258 -59.956  114.588 1.00 130.73 ? 138 ARG   F NH2    1 
ATOM   15432 N  N      . ARG   F 4  139 ? -18.203 -59.629  120.285 1.00 151.44 ? 139 ARG   F N      1 
ATOM   15433 C  CA     . ARG   F 4  139 ? -18.770 -59.262  121.573 1.00 146.65 ? 139 ARG   F CA     1 
ATOM   15434 C  C      . ARG   F 4  139 ? -18.280 -60.175  122.684 1.00 148.66 ? 139 ARG   F C      1 
ATOM   15435 O  O      . ARG   F 4  139 ? -18.319 -59.778  123.851 1.00 150.98 ? 139 ARG   F O      1 
ATOM   15436 C  CB     . ARG   F 4  139 ? -20.293 -59.283  121.504 1.00 139.45 ? 139 ARG   F CB     1 
ATOM   15437 C  CG     . ARG   F 4  139 ? -20.975 -58.686  122.711 1.00 131.82 ? 139 ARG   F CG     1 
ATOM   15438 C  CD     . ARG   F 4  139 ? -22.419 -58.393  122.385 1.00 124.57 ? 139 ARG   F CD     1 
ATOM   15439 N  NE     . ARG   F 4  139 ? -22.511 -57.260  121.474 1.00 120.61 ? 139 ARG   F NE     1 
ATOM   15440 C  CZ     . ARG   F 4  139 ? -23.576 -56.962  120.742 1.00 116.53 ? 139 ARG   F CZ     1 
ATOM   15441 N  NH1    . ARG   F 4  139 ? -24.672 -57.699  120.788 1.00 118.88 ? 139 ARG   F NH1    1 
ATOM   15442 N  NH2    . ARG   F 4  139 ? -23.536 -55.902  119.939 1.00 115.33 ? 139 ARG   F NH2    1 
ATOM   15443 N  N      . GLU   F 4  140 ? -17.811 -61.383  122.346 1.00 154.35 ? 140 GLU   F N      1 
ATOM   15444 C  CA     . GLU   F 4  140 ? -17.305 -62.314  123.351 1.00 153.38 ? 140 GLU   F CA     1 
ATOM   15445 C  C      . GLU   F 4  140 ? -15.966 -61.878  123.931 1.00 153.59 ? 140 GLU   F C      1 
ATOM   15446 O  O      . GLU   F 4  140 ? -15.607 -62.330  125.023 1.00 158.31 ? 140 GLU   F O      1 
ATOM   15447 C  CB     . GLU   F 4  140 ? -17.166 -63.725  122.764 1.00 151.71 ? 140 GLU   F CB     1 
ATOM   15448 C  CG     . GLU   F 4  140 ? -16.808 -64.801  123.795 1.00 148.75 ? 140 GLU   F CG     1 
ATOM   15449 C  CD     . GLU   F 4  140 ? -16.094 -66.008  123.192 1.00 151.67 ? 140 GLU   F CD     1 
ATOM   15450 O  OE1    . GLU   F 4  140 ? -16.779 -66.944  122.730 1.00 145.55 ? 140 GLU   F OE1    1 
ATOM   15451 O  OE2    . GLU   F 4  140 ? -14.845 -66.033  123.199 1.00 154.66 ? 140 GLU   F OE2    1 
ATOM   15452 N  N      . GLY   F 4  141 ? -15.219 -61.027  123.233 1.00 150.41 ? 141 GLY   F N      1 
ATOM   15453 C  CA     . GLY   F 4  141 ? -13.940 -60.575  123.745 1.00 148.13 ? 141 GLY   F CA     1 
ATOM   15454 C  C      . GLY   F 4  141 ? -13.751 -59.080  123.625 1.00 145.94 ? 141 GLY   F C      1 
ATOM   15455 O  O      . GLY   F 4  141 ? -12.644 -58.574  123.838 1.00 135.66 ? 141 GLY   F O      1 
ATOM   15456 N  N      . ARG   F 4  142 ? -14.836 -58.367  123.299 1.00 149.38 ? 142 ARG   F N      1 
ATOM   15457 C  CA     . ARG   F 4  142 ? -14.800 -56.945  122.960 1.00 148.62 ? 142 ARG   F CA     1 
ATOM   15458 C  C      . ARG   F 4  142 ? -13.576 -56.618  122.111 1.00 151.91 ? 142 ARG   F C      1 
ATOM   15459 O  O      . ARG   F 4  142 ? -12.968 -55.550  122.259 1.00 149.41 ? 142 ARG   F O      1 
ATOM   15460 C  CB     . ARG   F 4  142 ? -14.827 -56.066  124.214 1.00 149.41 ? 142 ARG   F CB     1 
ATOM   15461 C  CG     . ARG   F 4  142 ? -15.116 -54.599  123.903 1.00 144.08 ? 142 ARG   F CG     1 
ATOM   15462 C  CD     . ARG   F 4  142 ? -15.268 -53.731  125.151 1.00 143.85 ? 142 ARG   F CD     1 
ATOM   15463 N  NE     . ARG   F 4  142 ? -16.250 -54.235  126.106 1.00 146.40 ? 142 ARG   F NE     1 
ATOM   15464 C  CZ     . ARG   F 4  142 ? -15.959 -54.945  127.189 1.00 140.59 ? 142 ARG   F CZ     1 
ATOM   15465 N  NH1    . ARG   F 4  142 ? -14.710 -55.261  127.496 1.00 131.40 ? 142 ARG   F NH1    1 
ATOM   15466 N  NH2    . ARG   F 4  142 ? -16.946 -55.337  127.990 1.00 138.51 ? 142 ARG   F NH2    1 
ATOM   15467 N  N      . GLU   F 4  143 ? -13.216 -57.539  121.221 1.00 153.62 ? 143 GLU   F N      1 
ATOM   15468 C  CA     . GLU   F 4  143 ? -12.106 -57.351  120.304 1.00 145.29 ? 143 GLU   F CA     1 
ATOM   15469 C  C      . GLU   F 4  143 ? -12.425 -56.220  119.326 1.00 134.46 ? 143 GLU   F C      1 
ATOM   15470 O  O      . GLU   F 4  143 ? -13.556 -55.733  119.236 1.00 135.35 ? 143 GLU   F O      1 
ATOM   15471 C  CB     . GLU   F 4  143 ? -11.823 -58.652  119.550 1.00 143.38 ? 143 GLU   F CB     1 
ATOM   15472 C  CG     . GLU   F 4  143 ? -11.306 -59.793  120.425 1.00 145.48 ? 143 GLU   F CG     1 
ATOM   15473 C  CD     . GLU   F 4  143 ? -10.883 -61.016  119.626 1.00 147.46 ? 143 GLU   F CD     1 
ATOM   15474 O  OE1    . GLU   F 4  143 ? -9.789  -61.001  119.020 1.00 150.86 ? 143 GLU   F OE1    1 
ATOM   15475 O  OE2    . GLU   F 4  143 ? -11.658 -61.996  119.604 1.00 144.39 ? 143 GLU   F OE2    1 
ATOM   15476 N  N      . GLY   F 4  144 ? -11.406 -55.798  118.590 1.00 125.40 ? 144 GLY   F N      1 
ATOM   15477 C  CA     . GLY   F 4  144 ? -11.624 -54.816  117.554 1.00 123.57 ? 144 GLY   F CA     1 
ATOM   15478 C  C      . GLY   F 4  144 ? -12.736 -55.258  116.629 1.00 126.63 ? 144 GLY   F C      1 
ATOM   15479 O  O      . GLY   F 4  144 ? -12.732 -56.396  116.156 1.00 129.07 ? 144 GLY   F O      1 
ATOM   15480 N  N      . ASN   F 4  145 ? -13.711 -54.390  116.387 1.00 126.76 ? 145 ASN   F N      1 
ATOM   15481 C  CA     . ASN   F 4  145 ? -14.791 -54.645  115.438 1.00 124.65 ? 145 ASN   F CA     1 
ATOM   15482 C  C      . ASN   F 4  145 ? -14.968 -53.466  114.515 1.00 121.89 ? 145 ASN   F C      1 
ATOM   15483 O  O      . ASN   F 4  145 ? -16.067 -52.945  114.315 1.00 129.34 ? 145 ASN   F O      1 
ATOM   15484 C  CB     . ASN   F 4  145 ? -16.092 -54.978  116.150 1.00 134.61 ? 145 ASN   F CB     1 
ATOM   15485 C  CG     . ASN   F 4  145 ? -16.028 -56.310  116.823 1.00 141.44 ? 145 ASN   F CG     1 
ATOM   15486 O  OD1    . ASN   F 4  145 ? -15.189 -57.128  116.462 1.00 136.92 ? 145 ASN   F OD1    1 
ATOM   15487 N  ND2    . ASN   F 4  145 ? -16.883 -56.538  117.818 1.00 144.74 ? 145 ASN   F ND2    1 
ATOM   15488 N  N      . VAL   F 4  146 ? -13.891 -53.032  113.959 1.00 113.65 ? 146 VAL   F N      1 
ATOM   15489 C  CA     . VAL   F 4  146 ? -13.953 -52.094  112.854 1.00 117.36 ? 146 VAL   F CA     1 
ATOM   15490 C  C      . VAL   F 4  146 ? -14.065 -52.910  111.574 1.00 118.06 ? 146 VAL   F C      1 
ATOM   15491 O  O      . VAL   F 4  146 ? -13.555 -54.031  111.475 1.00 114.67 ? 146 VAL   F O      1 
ATOM   15492 C  CB     . VAL   F 4  146 ? -12.725 -51.168  112.857 1.00 119.85 ? 146 VAL   F CB     1 
ATOM   15493 C  CG1    . VAL   F 4  146 ? -12.854 -50.109  111.764 1.00 121.65 ? 146 VAL   F CG1    1 
ATOM   15494 C  CG2    . VAL   F 4  146 ? -12.560 -50.543  114.235 1.00 123.45 ? 146 VAL   F CG2    1 
ATOM   15495 N  N      . TRP   F 4  147 ? -14.788 -52.368  110.601 1.00 117.62 ? 147 TRP   F N      1 
ATOM   15496 C  CA     . TRP   F 4  147 ? -15.026 -53.037  109.331 1.00 110.25 ? 147 TRP   F CA     1 
ATOM   15497 C  C      . TRP   F 4  147 ? -15.054 -51.962  108.255 1.00 112.41 ? 147 TRP   F C      1 
ATOM   15498 O  O      . TRP   F 4  147 ? -14.809 -50.784  108.534 1.00 114.39 ? 147 TRP   F O      1 
ATOM   15499 C  CB     . TRP   F 4  147 ? -16.312 -53.865  109.402 1.00 109.44 ? 147 TRP   F CB     1 
ATOM   15500 C  CG     . TRP   F 4  147 ? -16.353 -54.843  110.544 1.00 111.87 ? 147 TRP   F CG     1 
ATOM   15501 C  CD1    . TRP   F 4  147 ? -16.734 -54.578  111.826 1.00 120.84 ? 147 TRP   F CD1    1 
ATOM   15502 C  CD2    . TRP   F 4  147 ? -16.157 -56.264  110.478 1.00 117.69 ? 147 TRP   F CD2    1 
ATOM   15503 N  NE1    . TRP   F 4  147 ? -16.697 -55.722  112.586 1.00 125.83 ? 147 TRP   F NE1    1 
ATOM   15504 C  CE2    . TRP   F 4  147 ? -16.360 -56.775  111.780 1.00 124.01 ? 147 TRP   F CE2    1 
ATOM   15505 C  CE3    . TRP   F 4  147 ? -15.800 -57.149  109.456 1.00 119.29 ? 147 TRP   F CE3    1 
ATOM   15506 C  CZ2    . TRP   F 4  147 ? -16.220 -58.129  112.086 1.00 124.82 ? 147 TRP   F CZ2    1 
ATOM   15507 C  CZ3    . TRP   F 4  147 ? -15.655 -58.496  109.763 1.00 119.51 ? 147 TRP   F CZ3    1 
ATOM   15508 C  CH2    . TRP   F 4  147 ? -15.867 -58.971  111.067 1.00 120.37 ? 147 TRP   F CH2    1 
ATOM   15509 N  N      . ILE   F 4  148 ? -15.371 -52.365  107.022 1.00 114.52 ? 148 ILE   F N      1 
ATOM   15510 C  CA     . ILE   F 4  148 ? -15.342 -51.462  105.869 1.00 116.65 ? 148 ILE   F CA     1 
ATOM   15511 C  C      . ILE   F 4  148 ? -16.268 -51.954  104.755 1.00 118.50 ? 148 ILE   F C      1 
ATOM   15512 O  O      . ILE   F 4  148 ? -16.723 -53.104  104.773 1.00 116.76 ? 148 ILE   F O      1 
ATOM   15513 C  CB     . ILE   F 4  148 ? -13.890 -51.279  105.380 1.00 108.57 ? 148 ILE   F CB     1 
ATOM   15514 C  CG1    . ILE   F 4  148 ? -13.814 -50.358  104.155 1.00 106.77 ? 148 ILE   F CG1    1 
ATOM   15515 C  CG2    . ILE   F 4  148 ? -13.238 -52.630  105.144 1.00 112.74 ? 148 ILE   F CG2    1 
ATOM   15516 C  CD1    . ILE   F 4  148 ? -14.441 -49.010  104.345 1.00 116.05 ? 148 ILE   F CD1    1 
ATOM   15517 N  N      . ALA   F 4  149 ? -16.560 -51.080  103.788 1.00 114.64 ? 149 ALA   F N      1 
ATOM   15518 C  CA     . ALA   F 4  149 ? -17.537 -51.356  102.732 1.00 113.93 ? 149 ALA   F CA     1 
ATOM   15519 C  C      . ALA   F 4  149 ? -16.914 -51.959  101.467 1.00 114.80 ? 149 ALA   F C      1 
ATOM   15520 O  O      . ALA   F 4  149 ? -17.624 -52.463  100.585 1.00 110.95 ? 149 ALA   F O      1 
ATOM   15521 C  CB     . ALA   F 4  149 ? -18.288 -50.080  102.385 1.00 109.95 ? 149 ALA   F CB     1 
ATOM   15522 N  N      . LEU   F 4  161 ? -17.875 -45.568  104.799 1.00 113.47 ? 161 LEU   F N      1 
ATOM   15523 C  CA     . LEU   F 4  161 ? -17.926 -47.021  104.692 1.00 115.18 ? 161 LEU   F CA     1 
ATOM   15524 C  C      . LEU   F 4  161 ? -17.464 -47.740  105.980 1.00 115.84 ? 161 LEU   F C      1 
ATOM   15525 O  O      . LEU   F 4  161 ? -17.893 -48.862  106.245 1.00 112.55 ? 161 LEU   F O      1 
ATOM   15526 C  CB     . LEU   F 4  161 ? -17.086 -47.487  103.491 1.00 112.54 ? 161 LEU   F CB     1 
ATOM   15527 C  CG     . LEU   F 4  161 ? -17.146 -46.724  102.166 1.00 106.07 ? 161 LEU   F CG     1 
ATOM   15528 C  CD1    . LEU   F 4  161 ? -16.043 -45.706  102.051 1.00 93.18  ? 161 LEU   F CD1    1 
ATOM   15529 C  CD2    . LEU   F 4  161 ? -17.015 -47.716  101.052 1.00 109.29 ? 161 LEU   F CD2    1 
ATOM   15530 N  N      . ILE   F 4  162 ? -16.605 -47.098  106.781 1.00 118.16 ? 162 ILE   F N      1 
ATOM   15531 C  CA     . ILE   F 4  162 ? -16.037 -47.710  107.985 1.00 120.30 ? 162 ILE   F CA     1 
ATOM   15532 C  C      . ILE   F 4  162 ? -16.907 -47.373  109.188 1.00 127.14 ? 162 ILE   F C      1 
ATOM   15533 O  O      . ILE   F 4  162 ? -17.202 -46.199  109.440 1.00 133.32 ? 162 ILE   F O      1 
ATOM   15534 C  CB     . ILE   F 4  162 ? -14.597 -47.228  108.226 1.00 119.75 ? 162 ILE   F CB     1 
ATOM   15535 C  CG1    . ILE   F 4  162 ? -13.776 -47.286  106.937 1.00 109.86 ? 162 ILE   F CG1    1 
ATOM   15536 C  CG2    . ILE   F 4  162 ? -13.959 -48.054  109.339 1.00 116.22 ? 162 ILE   F CG2    1 
ATOM   15537 C  CD1    . ILE   F 4  162 ? -12.445 -46.585  107.034 1.00 102.84 ? 162 ILE   F CD1    1 
ATOM   15538 N  N      . SER   F 4  163 ? -17.292 -48.395  109.952 1.00 130.67 ? 163 SER   F N      1 
ATOM   15539 C  CA     . SER   F 4  163 ? -18.104 -48.210  111.150 1.00 136.75 ? 163 SER   F CA     1 
ATOM   15540 C  C      . SER   F 4  163 ? -17.536 -49.068  112.270 1.00 133.31 ? 163 SER   F C      1 
ATOM   15541 O  O      . SER   F 4  163 ? -16.479 -49.691  112.133 1.00 125.92 ? 163 SER   F O      1 
ATOM   15542 C  CB     . SER   F 4  163 ? -19.581 -48.570  110.918 1.00 138.25 ? 163 SER   F CB     1 
ATOM   15543 O  OG     . SER   F 4  163 ? -20.139 -47.869  109.822 1.00 139.12 ? 163 SER   F OG     1 
ATOM   15544 N  N      . SER   F 4  164 ? -18.258 -49.096  113.383 1.00 133.73 ? 164 SER   F N      1 
ATOM   15545 C  CA     . SER   F 4  164 ? -17.954 -49.977  114.496 1.00 132.35 ? 164 SER   F CA     1 
ATOM   15546 C  C      . SER   F 4  164 ? -19.136 -50.832  114.909 1.00 132.09 ? 164 SER   F C      1 
ATOM   15547 O  O      . SER   F 4  164 ? -18.940 -51.972  115.332 1.00 130.50 ? 164 SER   F O      1 
ATOM   15548 C  CB     . SER   F 4  164 ? -17.469 -49.163  115.706 1.00 134.56 ? 164 SER   F CB     1 
ATOM   15549 O  OG     . SER   F 4  164 ? -16.331 -48.384  115.373 1.00 129.47 ? 164 SER   F OG     1 
ATOM   15550 N  N      . GLU   F 4  165 ? -20.353 -50.314  114.792 1.00 137.40 ? 165 GLU   F N      1 
ATOM   15551 C  CA     . GLU   F 4  165 ? -21.569 -51.079  115.018 1.00 144.75 ? 165 GLU   F CA     1 
ATOM   15552 C  C      . GLU   F 4  165 ? -22.069 -51.620  113.686 1.00 142.88 ? 165 GLU   F C      1 
ATOM   15553 O  O      . GLU   F 4  165 ? -22.002 -50.932  112.661 1.00 143.22 ? 165 GLU   F O      1 
ATOM   15554 C  CB     . GLU   F 4  165 ? -22.654 -50.214  115.677 1.00 152.03 ? 165 GLU   F CB     1 
ATOM   15555 C  CG     . GLU   F 4  165 ? -22.487 -49.945  117.184 1.00 147.96 ? 165 GLU   F CG     1 
ATOM   15556 C  CD     . GLU   F 4  165 ? -22.825 -51.152  118.056 1.00 148.64 ? 165 GLU   F CD     1 
ATOM   15557 O  OE1    . GLU   F 4  165 ? -23.537 -52.059  117.576 1.00 146.74 ? 165 GLU   F OE1    1 
ATOM   15558 O  OE2    . GLU   F 4  165 ? -22.398 -51.185  119.231 1.00 148.30 ? 165 GLU   F OE2    1 
ATOM   15559 N  N      . ALA   F 4  166 ? -22.566 -52.857  113.703 1.00 138.11 ? 166 ALA   F N      1 
ATOM   15560 C  CA     . ALA   F 4  166 ? -23.076 -53.456  112.475 1.00 137.33 ? 166 ALA   F CA     1 
ATOM   15561 C  C      . ALA   F 4  166 ? -24.209 -52.626  111.882 1.00 142.91 ? 166 ALA   F C      1 
ATOM   15562 O  O      . ALA   F 4  166 ? -24.232 -52.368  110.673 1.00 147.49 ? 166 ALA   F O      1 
ATOM   15563 C  CB     . ALA   F 4  166 ? -23.540 -54.888  112.737 1.00 136.04 ? 166 ALA   F CB     1 
ATOM   15564 N  N      . SER   F 4  167 ? -25.158 -52.196  112.715 1.00 144.46 ? 167 SER   F N      1 
ATOM   15565 C  CA     . SER   F 4  167 ? -26.300 -51.441  112.210 1.00 144.48 ? 167 SER   F CA     1 
ATOM   15566 C  C      . SER   F 4  167 ? -25.847 -50.231  111.400 1.00 149.04 ? 167 SER   F C      1 
ATOM   15567 O  O      . SER   F 4  167 ? -26.365 -49.971  110.308 1.00 150.35 ? 167 SER   F O      1 
ATOM   15568 C  CB     . SER   F 4  167 ? -27.198 -51.010  113.371 1.00 140.59 ? 167 SER   F CB     1 
ATOM   15569 O  OG     . SER   F 4  167 ? -27.561 -52.119  114.172 1.00 136.71 ? 167 SER   F OG     1 
ATOM   15570 N  N      . GLU   F 4  168 ? -24.874 -49.479  111.924 1.00 148.87 ? 168 GLU   F N      1 
ATOM   15571 C  CA     . GLU   F 4  168 ? -24.390 -48.290  111.228 1.00 149.21 ? 168 GLU   F CA     1 
ATOM   15572 C  C      . GLU   F 4  168 ? -24.017 -48.615  109.790 1.00 146.03 ? 168 GLU   F C      1 
ATOM   15573 O  O      . GLU   F 4  168 ? -24.298 -47.838  108.869 1.00 142.96 ? 168 GLU   F O      1 
ATOM   15574 C  CB     . GLU   F 4  168 ? -23.189 -47.709  111.972 1.00 149.26 ? 168 GLU   F CB     1 
ATOM   15575 C  CG     . GLU   F 4  168 ? -23.482 -47.348  113.418 1.00 149.87 ? 168 GLU   F CG     1 
ATOM   15576 C  CD     . GLU   F 4  168 ? -22.277 -46.769  114.127 1.00 154.59 ? 168 GLU   F CD     1 
ATOM   15577 O  OE1    . GLU   F 4  168 ? -21.240 -46.565  113.458 1.00 152.99 ? 168 GLU   F OE1    1 
ATOM   15578 O  OE2    . GLU   F 4  168 ? -22.364 -46.542  115.355 1.00 155.16 ? 168 GLU   F OE2    1 
ATOM   15579 N  N      . LEU   F 4  169 ? -23.395 -49.772  109.580 1.00 147.82 ? 169 LEU   F N      1 
ATOM   15580 C  CA     . LEU   F 4  169 ? -22.963 -50.170  108.247 1.00 149.38 ? 169 LEU   F CA     1 
ATOM   15581 C  C      . LEU   F 4  169 ? -24.110 -50.782  107.441 1.00 154.96 ? 169 LEU   F C      1 
ATOM   15582 O  O      . LEU   F 4  169 ? -24.420 -50.314  106.339 1.00 157.10 ? 169 LEU   F O      1 
ATOM   15583 C  CB     . LEU   F 4  169 ? -21.787 -51.144  108.358 1.00 143.15 ? 169 LEU   F CB     1 
ATOM   15584 N  N      . LEU   F 4  170 ? -24.756 -51.827  107.984 1.00 153.99 ? 170 LEU   F N      1 
ATOM   15585 C  CA     . LEU   F 4  170 ? -25.808 -52.545  107.255 1.00 150.94 ? 170 LEU   F CA     1 
ATOM   15586 C  C      . LEU   F 4  170 ? -26.824 -51.595  106.628 1.00 153.35 ? 170 LEU   F C      1 
ATOM   15587 O  O      . LEU   F 4  170 ? -27.302 -51.833  105.512 1.00 150.65 ? 170 LEU   F O      1 
ATOM   15588 C  CB     . LEU   F 4  170 ? -26.512 -53.543  108.183 1.00 142.49 ? 170 LEU   F CB     1 
ATOM   15589 C  CG     . LEU   F 4  170 ? -25.974 -54.975  108.185 1.00 133.12 ? 170 LEU   F CG     1 
ATOM   15590 C  CD1    . LEU   F 4  170 ? -26.686 -55.849  109.187 1.00 128.22 ? 170 LEU   F CD1    1 
ATOM   15591 C  CD2    . LEU   F 4  170 ? -26.151 -55.548  106.804 1.00 139.49 ? 170 LEU   F CD2    1 
ATOM   15592 N  N      . ASP   F 4  171 ? -27.171 -50.515  107.333 1.00 156.20 ? 171 ASP   F N      1 
ATOM   15593 C  CA     . ASP   F 4  171 ? -28.078 -49.509  106.791 1.00 157.46 ? 171 ASP   F CA     1 
ATOM   15594 C  C      . ASP   F 4  171 ? -27.443 -48.673  105.685 1.00 156.30 ? 171 ASP   F C      1 
ATOM   15595 O  O      . ASP   F 4  171 ? -28.161 -47.926  105.012 1.00 153.64 ? 171 ASP   F O      1 
ATOM   15596 C  CB     . ASP   F 4  171 ? -28.572 -48.595  107.918 1.00 153.56 ? 171 ASP   F CB     1 
ATOM   15597 C  CG     . ASP   F 4  171 ? -29.357 -49.348  108.983 1.00 154.38 ? 171 ASP   F CG     1 
ATOM   15598 O  OD1    . ASP   F 4  171 ? -28.827 -50.334  109.540 1.00 152.60 ? 171 ASP   F OD1    1 
ATOM   15599 O  OD2    . ASP   F 4  171 ? -30.500 -48.940  109.277 1.00 153.81 ? 171 ASP   F OD2    1 
ATOM   15600 N  N      . PHE   F 4  172 ? -26.125 -48.775  105.487 1.00 156.12 ? 172 PHE   F N      1 
ATOM   15601 C  CA     . PHE   F 4  172 ? -25.438 -48.059  104.415 1.00 155.41 ? 172 PHE   F CA     1 
ATOM   15602 C  C      . PHE   F 4  172 ? -25.472 -48.793  103.082 1.00 158.82 ? 172 PHE   F C      1 
ATOM   15603 O  O      . PHE   F 4  172 ? -25.409 -48.145  102.030 1.00 157.15 ? 172 PHE   F O      1 
ATOM   15604 C  CB     . PHE   F 4  172 ? -23.980 -47.783  104.804 1.00 150.81 ? 172 PHE   F CB     1 
ATOM   15605 C  CG     . PHE   F 4  172 ? -23.165 -47.120  103.711 1.00 151.48 ? 172 PHE   F CG     1 
ATOM   15606 C  CD1    . PHE   F 4  172 ? -23.352 -45.784  103.396 1.00 154.39 ? 172 PHE   F CD1    1 
ATOM   15607 C  CD2    . PHE   F 4  172 ? -22.176 -47.823  103.035 1.00 147.19 ? 172 PHE   F CD2    1 
ATOM   15608 C  CE1    . PHE   F 4  172 ? -22.601 -45.171  102.402 1.00 149.86 ? 172 PHE   F CE1    1 
ATOM   15609 C  CE2    . PHE   F 4  172 ? -21.415 -47.211  102.047 1.00 143.28 ? 172 PHE   F CE2    1 
ATOM   15610 C  CZ     . PHE   F 4  172 ? -21.629 -45.885  101.732 1.00 146.99 ? 172 PHE   F CZ     1 
ATOM   15611 N  N      . ILE   F 4  173 ? -25.572 -50.124  103.101 1.00 161.68 ? 173 ILE   F N      1 
ATOM   15612 C  CA     . ILE   F 4  173 ? -25.567 -50.893  101.858 1.00 161.48 ? 173 ILE   F CA     1 
ATOM   15613 C  C      . ILE   F 4  173 ? -26.942 -50.873  101.192 1.00 158.98 ? 173 ILE   F C      1 
ATOM   15614 O  O      . ILE   F 4  173 ? -27.047 -50.716  99.968  1.00 154.16 ? 173 ILE   F O      1 
ATOM   15615 C  CB     . ILE   F 4  173 ? -25.071 -52.332  102.119 1.00 161.19 ? 173 ILE   F CB     1 
ATOM   15616 C  CG1    . ILE   F 4  173 ? -25.948 -53.033  103.163 1.00 158.38 ? 173 ILE   F CG1    1 
ATOM   15617 C  CG2    . ILE   F 4  173 ? -23.596 -52.336  102.531 1.00 152.82 ? 173 ILE   F CG2    1 
ATOM   15618 C  CD1    . ILE   F 4  173 ? -25.494 -54.441  103.490 1.00 149.46 ? 173 ILE   F CD1    1 
ATOM   15619 N  N      . ASP   F 4  174 ? -28.012 -51.042  101.977 1.00 158.30 ? 174 ASP   F N      1 
ATOM   15620 C  CA     . ASP   F 4  174 ? -29.365 -50.875  101.461 1.00 154.52 ? 174 ASP   F CA     1 
ATOM   15621 C  C      . ASP   F 4  174 ? -29.667 -49.433  101.072 1.00 152.80 ? 174 ASP   F C      1 
ATOM   15622 O  O      . ASP   F 4  174 ? -30.648 -49.196  100.360 1.00 151.01 ? 174 ASP   F O      1 
ATOM   15623 C  CB     . ASP   F 4  174 ? -30.382 -51.376  102.490 1.00 149.60 ? 174 ASP   F CB     1 
ATOM   15624 C  CG     . ASP   F 4  174 ? -29.959 -52.683  103.141 1.00 146.54 ? 174 ASP   F CG     1 
ATOM   15625 O  OD1    . ASP   F 4  174 ? -29.961 -53.722  102.450 1.00 142.47 ? 174 ASP   F OD1    1 
ATOM   15626 O  OD2    . ASP   F 4  174 ? -29.613 -52.673  104.340 1.00 148.93 ? 174 ASP   F OD2    1 
ATOM   15627 N  N      . GLU   F 4  175 ? -28.844 -48.475  101.511 1.00 155.10 ? 175 GLU   F N      1 
ATOM   15628 C  CA     . GLU   F 4  175 ? -28.973 -47.088  101.080 1.00 154.25 ? 175 GLU   F CA     1 
ATOM   15629 C  C      . GLU   F 4  175 ? -28.420 -46.869  99.675  1.00 156.32 ? 175 GLU   F C      1 
ATOM   15630 O  O      . GLU   F 4  175 ? -28.814 -45.905  99.011  1.00 155.68 ? 175 GLU   F O      1 
ATOM   15631 C  CB     . GLU   F 4  175 ? -28.251 -46.169  102.073 1.00 153.68 ? 175 GLU   F CB     1 
ATOM   15632 C  CG     . GLU   F 4  175 ? -27.739 -44.851  101.506 1.00 155.76 ? 175 GLU   F CG     1 
ATOM   15633 C  CD     . GLU   F 4  175 ? -28.842 -44.009  100.888 1.00 157.23 ? 175 GLU   F CD     1 
ATOM   15634 O  OE1    . GLU   F 4  175 ? -30.024 -44.364  101.068 1.00 152.59 ? 175 GLU   F OE1    1 
ATOM   15635 O  OE2    . GLU   F 4  175 ? -28.529 -43.001  100.219 1.00 158.76 ? 175 GLU   F OE2    1 
ATOM   15636 N  N      . GLN   F 4  176 ? -27.524 -47.740  99.203  1.00 158.97 ? 176 GLN   F N      1 
ATOM   15637 C  CA     . GLN   F 4  176 ? -26.984 -47.632  97.849  1.00 153.91 ? 176 GLN   F CA     1 
ATOM   15638 C  C      . GLN   F 4  176 ? -27.751 -48.495  96.855  1.00 147.40 ? 176 GLN   F C      1 
ATOM   15639 O  O      . GLN   F 4  176 ? -27.998 -48.061  95.724  1.00 138.91 ? 176 GLN   F O      1 
ATOM   15640 C  CB     . GLN   F 4  176 ? -25.501 -48.012  97.833  1.00 151.65 ? 176 GLN   F CB     1 
ATOM   15641 C  CG     . GLN   F 4  176 ? -24.653 -47.270  98.859  1.00 151.90 ? 176 GLN   F CG     1 
ATOM   15642 C  CD     . GLN   F 4  176 ? -24.459 -45.802  98.517  1.00 145.55 ? 176 GLN   F CD     1 
ATOM   15643 O  OE1    . GLN   F 4  176 ? -24.903 -45.329  97.470  1.00 143.34 ? 176 GLN   F OE1    1 
ATOM   15644 N  NE2    . GLN   F 4  176 ? -23.792 -45.075  99.405  1.00 141.00 ? 176 GLN   F NE2    1 
ATOM   15645 N  N      . GLY   F 4  177 ? -28.126 -49.713  97.253  1.00 150.67 ? 177 GLY   F N      1 
ATOM   15646 C  CA     . GLY   F 4  177 ? -28.992 -50.573  96.470  1.00 150.92 ? 177 GLY   F CA     1 
ATOM   15647 C  C      . GLY   F 4  177 ? -28.300 -51.737  95.788  1.00 150.04 ? 177 GLY   F C      1 
ATOM   15648 O  O      . GLY   F 4  177 ? -28.981 -52.695  95.393  1.00 146.04 ? 177 GLY   F O      1 
ATOM   15649 N  N      . GLN   F 4  178 ? -26.975 -51.683  95.628  1.00 150.65 ? 178 GLN   F N      1 
ATOM   15650 C  CA     . GLN   F 4  178 ? -26.216 -52.730  94.961  1.00 146.11 ? 178 GLN   F CA     1 
ATOM   15651 C  C      . GLN   F 4  178 ? -25.567 -53.652  95.993  1.00 141.69 ? 178 GLN   F C      1 
ATOM   15652 O  O      . GLN   F 4  178 ? -25.739 -53.499  97.205  1.00 143.15 ? 178 GLN   F O      1 
ATOM   15653 C  CB     . GLN   F 4  178 ? -25.157 -52.127  94.034  1.00 137.89 ? 178 GLN   F CB     1 
ATOM   15654 C  CG     . GLN   F 4  178 ? -25.715 -51.273  92.917  1.00 135.32 ? 178 GLN   F CG     1 
ATOM   15655 C  CD     . GLN   F 4  178 ? -25.705 -49.806  93.268  1.00 142.65 ? 178 GLN   F CD     1 
ATOM   15656 O  OE1    . GLN   F 4  178 ? -26.127 -49.413  94.358  1.00 142.60 ? 178 GLN   F OE1    1 
ATOM   15657 N  NE2    . GLN   F 4  178 ? -25.217 -48.982  92.346  1.00 143.31 ? 178 GLN   F NE2    1 
ATOM   15658 N  N      . VAL   F 4  179 ? -24.797 -54.619  95.497  1.00 137.49 ? 179 VAL   F N      1 
ATOM   15659 C  CA     . VAL   F 4  179 ? -24.125 -55.592  96.355  1.00 131.90 ? 179 VAL   F CA     1 
ATOM   15660 C  C      . VAL   F 4  179 ? -22.895 -54.939  96.970  1.00 137.02 ? 179 VAL   F C      1 
ATOM   15661 O  O      . VAL   F 4  179 ? -22.057 -54.367  96.258  1.00 136.96 ? 179 VAL   F O      1 
ATOM   15662 C  CB     . VAL   F 4  179 ? -23.730 -56.846  95.560  1.00 123.02 ? 179 VAL   F CB     1 
ATOM   15663 C  CG1    . VAL   F 4  179 ? -22.642 -57.625  96.291  1.00 116.92 ? 179 VAL   F CG1    1 
ATOM   15664 C  CG2    . VAL   F 4  179 ? -24.946 -57.700  95.263  1.00 120.36 ? 179 VAL   F CG2    1 
ATOM   15665 N  N      . HIS   F 4  180 ? -22.782 -55.013  98.294  1.00 133.82 ? 180 HIS   F N      1 
ATOM   15666 C  CA     . HIS   F 4  180 ? -21.585 -54.564  98.986  1.00 127.03 ? 180 HIS   F CA     1 
ATOM   15667 C  C      . HIS   F 4  180 ? -20.994 -55.718  99.777  1.00 125.10 ? 180 HIS   F C      1 
ATOM   15668 O  O      . HIS   F 4  180 ? -21.689 -56.678  100.127 1.00 128.09 ? 180 HIS   F O      1 
ATOM   15669 C  CB     . HIS   F 4  180 ? -21.871 -53.375  99.906  1.00 124.95 ? 180 HIS   F CB     1 
ATOM   15670 C  CG     . HIS   F 4  180 ? -21.713 -52.052  99.228  1.00 133.87 ? 180 HIS   F CG     1 
ATOM   15671 N  ND1    . HIS   F 4  180 ? -22.375 -50.915  99.640  1.00 140.91 ? 180 HIS   F ND1    1 
ATOM   15672 C  CD2    . HIS   F 4  180 ? -20.952 -51.682  98.171  1.00 134.83 ? 180 HIS   F CD2    1 
ATOM   15673 C  CE1    . HIS   F 4  180 ? -22.038 -49.904  98.859  1.00 136.60 ? 180 HIS   F CE1    1 
ATOM   15674 N  NE2    . HIS   F 4  180 ? -21.175 -50.343  97.961  1.00 135.76 ? 180 HIS   F NE2    1 
ATOM   15675 N  N      . VAL   F 4  181 ? -19.694 -55.626  100.021 1.00 116.49 ? 181 VAL   F N      1 
ATOM   15676 C  CA     . VAL   F 4  181 ? -18.970 -56.589  100.832 1.00 110.81 ? 181 VAL   F CA     1 
ATOM   15677 C  C      . VAL   F 4  181 ? -18.321 -55.834  101.974 1.00 112.31 ? 181 VAL   F C      1 
ATOM   15678 O  O      . VAL   F 4  181 ? -17.862 -54.699  101.794 1.00 110.52 ? 181 VAL   F O      1 
ATOM   15679 C  CB     . VAL   F 4  181 ? -17.910 -57.350  100.018 1.00 108.43 ? 181 VAL   F CB     1 
ATOM   15680 C  CG1    . VAL   F 4  181 ? -16.899 -56.366  99.441  1.00 98.66  ? 181 VAL   F CG1    1 
ATOM   15681 C  CG2    . VAL   F 4  181 ? -17.214 -58.368  100.905 1.00 106.55 ? 181 VAL   F CG2    1 
ATOM   15682 N  N      . ILE   F 4  182 ? -18.287 -56.467  103.147 1.00 109.89 ? 182 ILE   F N      1 
ATOM   15683 C  CA     . ILE   F 4  182 ? -17.734 -55.857  104.349 1.00 114.78 ? 182 ILE   F CA     1 
ATOM   15684 C  C      . ILE   F 4  182 ? -16.579 -56.709  104.846 1.00 108.56 ? 182 ILE   F C      1 
ATOM   15685 O  O      . ILE   F 4  182 ? -16.582 -57.939  104.714 1.00 100.90 ? 182 ILE   F O      1 
ATOM   15686 C  CB     . ILE   F 4  182 ? -18.785 -55.677  105.463 1.00 119.35 ? 182 ILE   F CB     1 
ATOM   15687 C  CG1    . ILE   F 4  182 ? -19.389 -57.029  105.853 1.00 122.55 ? 182 ILE   F CG1    1 
ATOM   15688 C  CG2    . ILE   F 4  182 ? -19.860 -54.692  105.025 1.00 114.61 ? 182 ILE   F CG2    1 
ATOM   15689 C  CD1    . ILE   F 4  182 ? -20.174 -56.998  107.150 1.00 121.86 ? 182 ILE   F CD1    1 
ATOM   15690 N  N      . GLN   F 4  183 ? -15.595 -56.034  105.442 1.00 107.61 ? 183 GLN   F N      1 
ATOM   15691 C  CA     . GLN   F 4  183 ? -14.325 -56.658  105.777 1.00 109.50 ? 183 GLN   F CA     1 
ATOM   15692 C  C      . GLN   F 4  183 ? -13.808 -56.136  107.109 1.00 113.44 ? 183 GLN   F C      1 
ATOM   15693 O  O      . GLN   F 4  183 ? -14.142 -55.027  107.537 1.00 117.35 ? 183 GLN   F O      1 
ATOM   15694 C  CB     . GLN   F 4  183 ? -13.273 -56.405  104.691 1.00 104.69 ? 183 GLN   F CB     1 
ATOM   15695 C  CG     . GLN   F 4  183 ? -12.304 -57.549  104.559 1.00 97.84  ? 183 GLN   F CG     1 
ATOM   15696 C  CD     . GLN   F 4  183 ? -11.401 -57.399  103.376 1.00 97.32  ? 183 GLN   F CD     1 
ATOM   15697 O  OE1    . GLN   F 4  183 ? -10.541 -58.248  103.149 1.00 97.80  ? 183 GLN   F OE1    1 
ATOM   15698 N  NE2    . GLN   F 4  183 ? -11.566 -56.310  102.619 1.00 95.82  ? 183 GLN   F NE2    1 
ATOM   15699 N  N      . LYS   F 4  184 ? -12.973 -56.955  107.758 1.00 103.50 ? 184 LYS   F N      1 
ATOM   15700 C  CA     . LYS   F 4  184 ? -12.298 -56.553  108.986 1.00 105.12 ? 184 LYS   F CA     1 
ATOM   15701 C  C      . LYS   F 4  184 ? -11.312 -55.428  108.714 1.00 107.12 ? 184 LYS   F C      1 
ATOM   15702 O  O      . LYS   F 4  184 ? -10.275 -55.655  108.088 1.00 110.46 ? 184 LYS   F O      1 
ATOM   15703 C  CB     . LYS   F 4  184 ? -11.562 -57.739  109.612 1.00 102.63 ? 184 LYS   F CB     1 
ATOM   15704 N  N      . TYR   F 4  185 ? -11.619 -54.213  109.158 1.00 109.17 ? 185 TYR   F N      1 
ATOM   15705 C  CA     . TYR   F 4  185 ? -10.639 -53.146  109.056 1.00 105.34 ? 185 TYR   F CA     1 
ATOM   15706 C  C      . TYR   F 4  185 ? -9.388  -53.565  109.812 1.00 102.27 ? 185 TYR   F C      1 
ATOM   15707 O  O      . TYR   F 4  185 ? -9.451  -54.333  110.775 1.00 104.20 ? 185 TYR   F O      1 
ATOM   15708 C  CB     . TYR   F 4  185 ? -11.206 -51.840  109.613 1.00 105.63 ? 185 TYR   F CB     1 
ATOM   15709 C  CG     . TYR   F 4  185 ? -10.464 -50.621  109.152 1.00 102.53 ? 185 TYR   F CG     1 
ATOM   15710 C  CD1    . TYR   F 4  185 ? -10.817 -49.999  107.969 1.00 108.12 ? 185 TYR   F CD1    1 
ATOM   15711 C  CD2    . TYR   F 4  185 ? -9.441  -50.074  109.898 1.00 100.81 ? 185 TYR   F CD2    1 
ATOM   15712 C  CE1    . TYR   F 4  185 ? -10.152 -48.883  107.520 1.00 108.88 ? 185 TYR   F CE1    1 
ATOM   15713 C  CE2    . TYR   F 4  185 ? -8.769  -48.951  109.460 1.00 104.94 ? 185 TYR   F CE2    1 
ATOM   15714 C  CZ     . TYR   F 4  185 ? -9.129  -48.358  108.264 1.00 106.66 ? 185 TYR   F CZ     1 
ATOM   15715 O  OH     . TYR   F 4  185 ? -8.473  -47.236  107.797 1.00 104.74 ? 185 TYR   F OH     1 
ATOM   15716 N  N      . LEU   F 4  186 ? -8.235  -53.100  109.339 1.00 97.48  ? 186 LEU   F N      1 
ATOM   15717 C  CA     . LEU   F 4  186 ? -6.957  -53.419  109.976 1.00 101.30 ? 186 LEU   F CA     1 
ATOM   15718 C  C      . LEU   F 4  186 ? -6.641  -52.313  110.971 1.00 98.13  ? 186 LEU   F C      1 
ATOM   15719 O  O      . LEU   F 4  186 ? -5.952  -51.336  110.664 1.00 92.17  ? 186 LEU   F O      1 
ATOM   15720 C  CB     . LEU   F 4  186 ? -5.854  -53.609  108.942 1.00 100.36 ? 186 LEU   F CB     1 
ATOM   15721 C  CG     . LEU   F 4  186 ? -6.150  -54.589  107.801 1.00 99.88  ? 186 LEU   F CG     1 
ATOM   15722 C  CD1    . LEU   F 4  186 ? -5.117  -54.472  106.690 1.00 93.66  ? 186 LEU   F CD1    1 
ATOM   15723 C  CD2    . LEU   F 4  186 ? -6.188  -56.019  108.317 1.00 82.39  ? 186 LEU   F CD2    1 
ATOM   15724 N  N      . GLU   F 4  187 ? -7.159  -52.487  112.190 1.00 97.77  ? 187 GLU   F N      1 
ATOM   15725 C  CA     . GLU   F 4  187 ? -7.070  -51.446  113.202 1.00 96.25  ? 187 GLU   F CA     1 
ATOM   15726 C  C      . GLU   F 4  187 ? -5.627  -51.163  113.591 1.00 97.93  ? 187 GLU   F C      1 
ATOM   15727 O  O      . GLU   F 4  187 ? -5.298  -50.017  113.913 1.00 103.07 ? 187 GLU   F O      1 
ATOM   15728 C  CB     . GLU   F 4  187 ? -7.915  -51.829  114.428 1.00 101.18 ? 187 GLU   F CB     1 
ATOM   15729 C  CG     . GLU   F 4  187 ? -9.375  -52.189  114.100 1.00 103.12 ? 187 GLU   F CG     1 
ATOM   15730 C  CD     . GLU   F 4  187 ? -10.107 -52.909  115.227 1.00 104.27 ? 187 GLU   F CD     1 
ATOM   15731 O  OE1    . GLU   F 4  187 ? -9.442  -53.420  116.148 1.00 104.05 ? 187 GLU   F OE1    1 
ATOM   15732 O  OE2    . GLU   F 4  187 ? -11.356 -52.953  115.198 1.00 109.43 ? 187 GLU   F OE2    1 
ATOM   15733 N  N      . LYS   F 4  188 ? -4.746  -52.173  113.550 1.00 93.56  ? 188 LYS   F N      1 
ATOM   15734 C  CA     . LYS   F 4  188 ? -3.326  -51.918  113.791 1.00 91.43  ? 188 LYS   F CA     1 
ATOM   15735 C  C      . LYS   F 4  188 ? -2.495  -51.988  112.510 1.00 84.62  ? 188 LYS   F C      1 
ATOM   15736 O  O      . LYS   F 4  188 ? -1.852  -53.007  112.238 1.00 78.37  ? 188 LYS   F O      1 
ATOM   15737 C  CB     . LYS   F 4  188 ? -2.765  -52.886  114.839 1.00 90.48  ? 188 LYS   F CB     1 
ATOM   15738 C  CG     . LYS   F 4  188 ? -2.753  -52.320  116.264 1.00 101.89 ? 188 LYS   F CG     1 
ATOM   15739 C  CD     . LYS   F 4  188 ? -1.688  -52.985  117.141 1.00 98.84  ? 188 LYS   F CD     1 
ATOM   15740 C  CE     . LYS   F 4  188 ? -1.356  -52.177  118.407 1.00 101.50 ? 188 LYS   F CE     1 
ATOM   15741 N  NZ     . LYS   F 4  188 ? -0.827  -50.805  118.146 1.00 102.51 ? 188 LYS   F NZ     1 
ATOM   15742 N  N      . PRO   F 4  189 ? -2.462  -50.920  111.712 1.00 81.45  ? 189 PRO   F N      1 
ATOM   15743 C  CA     . PRO   F 4  189 ? -1.600  -50.915  110.528 1.00 81.33  ? 189 PRO   F CA     1 
ATOM   15744 C  C      . PRO   F 4  189 ? -0.186  -50.472  110.833 1.00 79.93  ? 189 PRO   F C      1 
ATOM   15745 O  O      . PRO   F 4  189 ? 0.128   -50.146  111.977 1.00 88.52  ? 189 PRO   F O      1 
ATOM   15746 C  CB     . PRO   F 4  189 ? -2.309  -49.924  109.606 1.00 88.40  ? 189 PRO   F CB     1 
ATOM   15747 C  CG     . PRO   F 4  189 ? -2.888  -48.926  110.548 1.00 87.79  ? 189 PRO   F CG     1 
ATOM   15748 C  CD     . PRO   F 4  189 ? -3.273  -49.694  111.796 1.00 87.04  ? 189 PRO   F CD     1 
ATOM   15749 N  N      . LEU   F 4  190 ? 0.673   -50.468  109.819 1.00 79.26  ? 190 LEU   F N      1 
ATOM   15750 C  CA     . LEU   F 4  190 ? 2.046   -49.994  109.944 1.00 84.84  ? 190 LEU   F CA     1 
ATOM   15751 C  C      . LEU   F 4  190 ? 2.096   -48.530  109.529 1.00 94.61  ? 190 LEU   F C      1 
ATOM   15752 O  O      . LEU   F 4  190 ? 1.634   -48.184  108.438 1.00 102.54 ? 190 LEU   F O      1 
ATOM   15753 C  CB     . LEU   F 4  190 ? 2.982   -50.817  109.055 1.00 74.01  ? 190 LEU   F CB     1 
ATOM   15754 C  CG     . LEU   F 4  190 ? 4.491   -50.670  109.241 1.00 70.96  ? 190 LEU   F CG     1 
ATOM   15755 C  CD1    . LEU   F 4  190 ? 5.005   -51.787  110.109 1.00 68.18  ? 190 LEU   F CD1    1 
ATOM   15756 C  CD2    . LEU   F 4  190 ? 5.245   -50.623  107.928 1.00 75.50  ? 190 LEU   F CD2    1 
ATOM   15757 N  N      . LEU   F 4  191 ? 2.668   -47.672  110.375 1.00 93.34  ? 191 LEU   F N      1 
ATOM   15758 C  CA     . LEU   F 4  191 ? 2.712   -46.241  110.091 1.00 96.16  ? 191 LEU   F CA     1 
ATOM   15759 C  C      . LEU   F 4  191 ? 4.131   -45.767  109.823 1.00 93.41  ? 191 LEU   F C      1 
ATOM   15760 O  O      . LEU   F 4  191 ? 5.057   -46.093  110.570 1.00 96.37  ? 191 LEU   F O      1 
ATOM   15761 C  CB     . LEU   F 4  191 ? 2.098   -45.427  111.225 1.00 94.44  ? 191 LEU   F CB     1 
ATOM   15762 C  CG     . LEU   F 4  191 ? 0.679   -45.895  111.519 1.00 98.71  ? 191 LEU   F CG     1 
ATOM   15763 C  CD1    . LEU   F 4  191 ? 0.683   -47.145  112.382 1.00 97.01  ? 191 LEU   F CD1    1 
ATOM   15764 C  CD2    . LEU   F 4  191 ? -0.148  -44.786  112.133 1.00 106.48 ? 191 LEU   F CD2    1 
ATOM   15765 N  N      . LEU   F 4  192 ? 4.287   -44.988  108.760 1.00 90.00  ? 192 LEU   F N      1 
ATOM   15766 C  CA     . LEU   F 4  192 ? 5.576   -44.399  108.436 1.00 90.17  ? 192 LEU   F CA     1 
ATOM   15767 C  C      . LEU   F 4  192 ? 5.870   -43.251  109.389 1.00 99.75  ? 192 LEU   F C      1 
ATOM   15768 O  O      . LEU   F 4  192 ? 5.034   -42.365  109.588 1.00 105.40 ? 192 LEU   F O      1 
ATOM   15769 C  CB     . LEU   F 4  192 ? 5.575   -43.879  107.003 1.00 92.30  ? 192 LEU   F CB     1 
ATOM   15770 C  CG     . LEU   F 4  192 ? 5.574   -44.849  105.835 1.00 84.07  ? 192 LEU   F CG     1 
ATOM   15771 C  CD1    . LEU   F 4  192 ? 4.280   -45.596  105.864 1.00 94.58  ? 192 LEU   F CD1    1 
ATOM   15772 C  CD2    . LEU   F 4  192 ? 5.691   -44.067  104.558 1.00 78.39  ? 192 LEU   F CD2    1 
ATOM   15773 N  N      . GLU   F 4  193 ? 7.042   -43.259  109.974 1.00 102.56 ? 193 GLU   F N      1 
ATOM   15774 C  CA     . GLU   F 4  193 ? 7.421   -42.068  110.707 1.00 99.58  ? 193 GLU   F CA     1 
ATOM   15775 C  C      . GLU   F 4  193 ? 8.575   -41.386  109.980 1.00 100.93 ? 193 GLU   F C      1 
ATOM   15776 O  O      . GLU   F 4  193 ? 9.453   -42.070  109.450 1.00 101.43 ? 193 GLU   F O      1 
ATOM   15777 C  CB     . GLU   F 4  193 ? 7.832   -42.409  112.145 1.00 98.66  ? 193 GLU   F CB     1 
ATOM   15778 C  CG     . GLU   F 4  193 ? 6.948   -43.445  112.845 1.00 94.52  ? 193 GLU   F CG     1 
ATOM   15779 C  CD     . GLU   F 4  193 ? 5.531   -42.946  113.113 1.00 100.32 ? 193 GLU   F CD     1 
ATOM   15780 O  OE1    . GLU   F 4  193 ? 5.253   -41.757  112.844 1.00 98.80  ? 193 GLU   F OE1    1 
ATOM   15781 O  OE2    . GLU   F 4  193 ? 4.698   -43.745  113.607 1.00 105.30 ? 193 GLU   F OE2    1 
ATOM   15782 N  N      . PRO   F 4  194 ? 8.609   -40.053  109.912 1.00 107.26 ? 194 PRO   F N      1 
ATOM   15783 C  CA     . PRO   F 4  194 ? 7.747   -39.078  110.581 1.00 111.82 ? 194 PRO   F CA     1 
ATOM   15784 C  C      . PRO   F 4  194 ? 6.360   -38.975  109.975 1.00 109.46 ? 194 PRO   F C      1 
ATOM   15785 O  O      . PRO   F 4  194 ? 6.228   -38.800  108.770 1.00 110.80 ? 194 PRO   F O      1 
ATOM   15786 C  CB     . PRO   F 4  194 ? 8.517   -37.770  110.387 1.00 115.33 ? 194 PRO   F CB     1 
ATOM   15787 C  CG     . PRO   F 4  194 ? 9.164   -37.942  109.047 1.00 113.20 ? 194 PRO   F CG     1 
ATOM   15788 C  CD     . PRO   F 4  194 ? 9.546   -39.397  108.981 1.00 110.07 ? 194 PRO   F CD     1 
ATOM   15789 N  N      . GLY   F 4  195 ? 5.313   -39.068  110.790 1.00 105.42 ? 195 GLY   F N      1 
ATOM   15790 C  CA     . GLY   F 4  195 ? 3.978   -38.767  110.322 1.00 101.43 ? 195 GLY   F CA     1 
ATOM   15791 C  C      . GLY   F 4  195 ? 2.884   -39.572  110.985 1.00 98.29  ? 195 GLY   F C      1 
ATOM   15792 O  O      . GLY   F 4  195 ? 1.724   -39.151  111.002 1.00 103.46 ? 195 GLY   F O      1 
ATOM   15793 N  N      . HIS   F 4  196 ? 3.235   -40.729  111.534 1.00 100.50 ? 196 HIS   F N      1 
ATOM   15794 C  CA     . HIS   F 4  196 ? 2.227   -41.687  111.968 1.00 104.04 ? 196 HIS   F CA     1 
ATOM   15795 C  C      . HIS   F 4  196 ? 1.185   -41.793  110.855 1.00 110.49 ? 196 HIS   F C      1 
ATOM   15796 O  O      . HIS   F 4  196 ? 0.079   -41.248  110.974 1.00 112.36 ? 196 HIS   F O      1 
ATOM   15797 C  CB     . HIS   F 4  196 ? 1.628   -41.246  113.305 1.00 96.17  ? 196 HIS   F CB     1 
ATOM   15798 C  CG     . HIS   F 4  196 ? 1.245   -42.376  114.215 1.00 96.82  ? 196 HIS   F CG     1 
ATOM   15799 N  ND1    . HIS   F 4  196 ? 2.177   -43.108  114.921 1.00 95.57  ? 196 HIS   F ND1    1 
ATOM   15800 C  CD2    . HIS   F 4  196 ? 0.034   -42.838  114.608 1.00 98.43  ? 196 HIS   F CD2    1 
ATOM   15801 C  CE1    . HIS   F 4  196 ? 1.559   -44.003  115.671 1.00 94.80  ? 196 HIS   F CE1    1 
ATOM   15802 N  NE2    . HIS   F 4  196 ? 0.258   -43.858  115.503 1.00 94.01  ? 196 HIS   F NE2    1 
ATOM   15803 N  N      . ARG   F 4  197 ? 1.546   -42.487  109.763 1.00 108.15 ? 197 ARG   F N      1 
ATOM   15804 C  CA     . ARG   F 4  197 ? 0.871   -42.386  108.474 1.00 105.67 ? 197 ARG   F CA     1 
ATOM   15805 C  C      . ARG   F 4  197 ? 0.577   -43.766  107.900 1.00 106.99 ? 197 ARG   F C      1 
ATOM   15806 O  O      . ARG   F 4  197 ? 1.382   -44.694  108.021 1.00 108.38 ? 197 ARG   F O      1 
ATOM   15807 C  CB     . ARG   F 4  197 ? 1.735   -41.614  107.483 1.00 100.77 ? 197 ARG   F CB     1 
ATOM   15808 C  CG     . ARG   F 4  197 ? 2.361   -40.388  108.095 1.00 105.85 ? 197 ARG   F CG     1 
ATOM   15809 C  CD     . ARG   F 4  197 ? 3.538   -39.909  107.286 1.00 105.24 ? 197 ARG   F CD     1 
ATOM   15810 N  NE     . ARG   F 4  197 ? 3.254   -39.988  105.863 1.00 102.44 ? 197 ARG   F NE     1 
ATOM   15811 C  CZ     . ARG   F 4  197 ? 4.177   -40.013  104.914 1.00 105.52 ? 197 ARG   F CZ     1 
ATOM   15812 N  NH1    . ARG   F 4  197 ? 5.469   -39.991  105.203 1.00 99.04  ? 197 ARG   F NH1    1 
ATOM   15813 N  NH2    . ARG   F 4  197 ? 3.791   -40.059  103.645 1.00 107.99 ? 197 ARG   F NH2    1 
ATOM   15814 N  N      . LYS   F 4  198 ? -0.569  -43.876  107.235 1.00 105.82 ? 198 LYS   F N      1 
ATOM   15815 C  CA     . LYS   F 4  198 ? -1.078  -45.109  106.649 1.00 100.68 ? 198 LYS   F CA     1 
ATOM   15816 C  C      . LYS   F 4  198 ? -0.714  -45.169  105.169 1.00 105.85 ? 198 LYS   F C      1 
ATOM   15817 O  O      . LYS   F 4  198 ? -0.369  -44.155  104.555 1.00 107.93 ? 198 LYS   F O      1 
ATOM   15818 C  CB     . LYS   F 4  198 ? -2.598  -45.170  106.842 1.00 98.82  ? 198 LYS   F CB     1 
ATOM   15819 C  CG     . LYS   F 4  198 ? -3.283  -46.500  106.600 1.00 90.02  ? 198 LYS   F CG     1 
ATOM   15820 C  CD     . LYS   F 4  198 ? -4.771  -46.267  106.367 1.00 98.63  ? 198 LYS   F CD     1 
ATOM   15821 C  CE     . LYS   F 4  198 ? -5.580  -47.551  106.313 1.00 98.50  ? 198 LYS   F CE     1 
ATOM   15822 N  NZ     . LYS   F 4  198 ? -5.639  -48.254  107.618 1.00 94.69  ? 198 LYS   F NZ     1 
ATOM   15823 N  N      . PHE   F 4  199 ? -0.788  -46.369  104.592 1.00 106.17 ? 199 PHE   F N      1 
ATOM   15824 C  CA     . PHE   F 4  199 ? -0.464  -46.507  103.173 1.00 102.69 ? 199 PHE   F CA     1 
ATOM   15825 C  C      . PHE   F 4  199 ? -0.904  -47.873  102.664 1.00 96.70  ? 199 PHE   F C      1 
ATOM   15826 O  O      . PHE   F 4  199 ? -1.181  -48.790  103.445 1.00 88.55  ? 199 PHE   F O      1 
ATOM   15827 C  CB     . PHE   F 4  199 ? 1.034   -46.339  102.924 1.00 98.34  ? 199 PHE   F CB     1 
ATOM   15828 C  CG     . PHE   F 4  199 ? 1.839   -47.487  103.427 1.00 98.89  ? 199 PHE   F CG     1 
ATOM   15829 C  CD1    . PHE   F 4  199 ? 2.196   -47.563  104.764 1.00 100.42 ? 199 PHE   F CD1    1 
ATOM   15830 C  CD2    . PHE   F 4  199 ? 2.219   -48.505  102.571 1.00 88.45  ? 199 PHE   F CD2    1 
ATOM   15831 C  CE1    . PHE   F 4  199 ? 2.933   -48.628  105.234 1.00 96.79  ? 199 PHE   F CE1    1 
ATOM   15832 C  CE2    . PHE   F 4  199 ? 2.947   -49.575  103.032 1.00 85.51  ? 199 PHE   F CE2    1 
ATOM   15833 C  CZ     . PHE   F 4  199 ? 3.312   -49.639  104.364 1.00 94.54  ? 199 PHE   F CZ     1 
ATOM   15834 N  N      . ASP   F 4  200 ? -0.951  -47.992  101.332 1.00 98.71  ? 200 ASP   F N      1 
ATOM   15835 C  CA     . ASP   F 4  200 ? -1.107  -49.267  100.640 1.00 89.42  ? 200 ASP   F CA     1 
ATOM   15836 C  C      . ASP   F 4  200 ? -0.026  -49.403  99.571  1.00 85.09  ? 200 ASP   F C      1 
ATOM   15837 O  O      . ASP   F 4  200 ? 0.578   -48.416  99.136  1.00 82.98  ? 200 ASP   F O      1 
ATOM   15838 C  CB     . ASP   F 4  200 ? -2.524  -49.454  100.025 1.00 86.42  ? 200 ASP   F CB     1 
ATOM   15839 C  CG     . ASP   F 4  200 ? -2.917  -48.358  99.021  1.00 88.75  ? 200 ASP   F CG     1 
ATOM   15840 O  OD1    . ASP   F 4  200 ? -2.203  -48.141  98.020  1.00 89.11  ? 200 ASP   F OD1    1 
ATOM   15841 O  OD2    . ASP   F 4  200 ? -3.994  -47.753  99.210  1.00 92.72  ? 200 ASP   F OD2    1 
ATOM   15842 N  N      . ILE   F 4  201 ? 0.244   -50.653  99.186  1.00 82.43  ? 201 ILE   F N      1 
ATOM   15843 C  CA     . ILE   F 4  201 ? 1.239   -50.983  98.164  1.00 81.82  ? 201 ILE   F CA     1 
ATOM   15844 C  C      . ILE   F 4  201 ? 0.492   -51.528  96.947  1.00 71.16  ? 201 ILE   F C      1 
ATOM   15845 O  O      . ILE   F 4  201 ? -0.346  -52.432  97.081  1.00 66.71  ? 201 ILE   F O      1 
ATOM   15846 C  CB     . ILE   F 4  201 ? 2.293   -51.988  98.681  1.00 74.39  ? 201 ILE   F CB     1 
ATOM   15847 C  CG1    . ILE   F 4  201 ? 2.818   -51.580  100.061 1.00 75.90  ? 201 ILE   F CG1    1 
ATOM   15848 C  CG2    . ILE   F 4  201 ? 3.493   -52.052  97.752  1.00 61.50  ? 201 ILE   F CG2    1 
ATOM   15849 C  CD1    . ILE   F 4  201 ? 3.653   -52.638  100.763 1.00 71.22  ? 201 ILE   F CD1    1 
ATOM   15850 N  N      . ARG   F 4  202 ? 0.764   -50.950  95.772  1.00 66.13  ? 202 ARG   F N      1 
ATOM   15851 C  CA     . ARG   F 4  202 ? 0.281   -51.472  94.498  1.00 69.95  ? 202 ARG   F CA     1 
ATOM   15852 C  C      . ARG   F 4  202 ? 1.440   -52.084  93.744  1.00 68.30  ? 202 ARG   F C      1 
ATOM   15853 O  O      . ARG   F 4  202 ? 2.375   -51.370  93.359  1.00 63.27  ? 202 ARG   F O      1 
ATOM   15854 C  CB     . ARG   F 4  202 ? -0.335  -50.410  93.595  1.00 71.06  ? 202 ARG   F CB     1 
ATOM   15855 C  CG     . ARG   F 4  202 ? -0.168  -50.807  92.112  1.00 66.70  ? 202 ARG   F CG     1 
ATOM   15856 C  CD     . ARG   F 4  202 ? -1.253  -50.208  91.264  1.00 69.85  ? 202 ARG   F CD     1 
ATOM   15857 N  NE     . ARG   F 4  202 ? -2.551  -50.686  91.713  1.00 70.23  ? 202 ARG   F NE     1 
ATOM   15858 C  CZ     . ARG   F 4  202 ? -3.710  -50.242  91.247  1.00 75.00  ? 202 ARG   F CZ     1 
ATOM   15859 N  NH1    . ARG   F 4  202 ? -3.766  -49.305  90.307  1.00 70.99  ? 202 ARG   F NH1    1 
ATOM   15860 N  NH2    . ARG   F 4  202 ? -4.842  -50.721  91.761  1.00 80.52  ? 202 ARG   F NH2    1 
ATOM   15861 N  N      . SER   F 4  203 ? 1.356   -53.386  93.499  1.00 68.69  ? 203 SER   F N      1 
ATOM   15862 C  CA     . SER   F 4  203 ? 2.264   -54.055  92.584  1.00 68.98  ? 203 SER   F CA     1 
ATOM   15863 C  C      . SER   F 4  203 ? 1.567   -54.222  91.239  1.00 64.30  ? 203 SER   F C      1 
ATOM   15864 O  O      . SER   F 4  203 ? 0.346   -54.409  91.175  1.00 63.79  ? 203 SER   F O      1 
ATOM   15865 C  CB     . SER   F 4  203 ? 2.719   -55.405  93.145  1.00 68.25  ? 203 SER   F CB     1 
ATOM   15866 O  OG     . SER   F 4  203 ? 3.178   -55.286  94.485  1.00 64.51  ? 203 SER   F OG     1 
ATOM   15867 N  N      . TRP   F 4  204 ? 2.335   -54.089  90.166  1.00 58.30  ? 204 TRP   F N      1 
ATOM   15868 C  CA     . TRP   F 4  204 ? 1.819   -54.290  88.824  1.00 58.19  ? 204 TRP   F CA     1 
ATOM   15869 C  C      . TRP   F 4  204 ? 2.376   -55.627  88.369  1.00 59.01  ? 204 TRP   F C      1 
ATOM   15870 O  O      . TRP   F 4  204 ? 3.598   -55.817  88.350  1.00 61.02  ? 204 TRP   F O      1 
ATOM   15871 C  CB     . TRP   F 4  204 ? 2.207   -53.148  87.870  1.00 63.40  ? 204 TRP   F CB     1 
ATOM   15872 C  CG     . TRP   F 4  204 ? 1.486   -51.847  88.194  1.00 63.28  ? 204 TRP   F CG     1 
ATOM   15873 C  CD1    . TRP   F 4  204 ? 0.218   -51.490  87.825  1.00 65.18  ? 204 TRP   F CD1    1 
ATOM   15874 C  CD2    . TRP   F 4  204 ? 2.003   -50.740  88.948  1.00 68.82  ? 204 TRP   F CD2    1 
ATOM   15875 N  NE1    . TRP   F 4  204 ? -0.102  -50.249  88.333  1.00 67.08  ? 204 TRP   F NE1    1 
ATOM   15876 C  CE2    . TRP   F 4  204 ? 0.978   -49.765  89.019  1.00 69.66  ? 204 TRP   F CE2    1 
ATOM   15877 C  CE3    . TRP   F 4  204 ? 3.226   -50.484  89.579  1.00 67.69  ? 204 TRP   F CE3    1 
ATOM   15878 C  CZ2    . TRP   F 4  204 ? 1.145   -48.556  89.684  1.00 72.76  ? 204 TRP   F CZ2    1 
ATOM   15879 C  CZ3    . TRP   F 4  204 ? 3.386   -49.282  90.247  1.00 73.51  ? 204 TRP   F CZ3    1 
ATOM   15880 C  CH2    . TRP   F 4  204 ? 2.353   -48.331  90.292  1.00 75.81  ? 204 TRP   F CH2    1 
ATOM   15881 N  N      . VAL   F 4  205 ? 1.484   -56.568  88.067  1.00 54.44  ? 205 VAL   F N      1 
ATOM   15882 C  CA     . VAL   F 4  205 ? 1.861   -57.888  87.582  1.00 55.01  ? 205 VAL   F CA     1 
ATOM   15883 C  C      . VAL   F 4  205 ? 1.348   -58.045  86.157  1.00 52.25  ? 205 VAL   F C      1 
ATOM   15884 O  O      . VAL   F 4  205 ? 0.229   -57.634  85.845  1.00 54.80  ? 205 VAL   F O      1 
ATOM   15885 C  CB     . VAL   F 4  205 ? 1.306   -58.997  88.498  1.00 51.65  ? 205 VAL   F CB     1 
ATOM   15886 C  CG1    . VAL   F 4  205 ? 1.742   -60.388  88.003  1.00 47.54  ? 205 VAL   F CG1    1 
ATOM   15887 C  CG2    . VAL   F 4  205 ? 1.748   -58.745  89.920  1.00 55.35  ? 205 VAL   F CG2    1 
ATOM   15888 N  N      . LEU   F 4  206 ? 2.166   -58.647  85.299  1.00 51.21  ? 206 LEU   F N      1 
ATOM   15889 C  CA     . LEU   F 4  206 ? 1.829   -58.881  83.896  1.00 52.61  ? 206 LEU   F CA     1 
ATOM   15890 C  C      . LEU   F 4  206 ? 1.819   -60.376  83.605  1.00 51.38  ? 206 LEU   F C      1 
ATOM   15891 O  O      . LEU   F 4  206 ? 2.866   -61.026  83.670  1.00 51.86  ? 206 LEU   F O      1 
ATOM   15892 C  CB     . LEU   F 4  206 ? 2.833   -58.177  82.980  1.00 55.58  ? 206 LEU   F CB     1 
ATOM   15893 C  CG     . LEU   F 4  206 ? 2.620   -58.274  81.474  1.00 52.86  ? 206 LEU   F CG     1 
ATOM   15894 C  CD1    . LEU   F 4  206 ? 1.279   -57.688  81.068  1.00 54.41  ? 206 LEU   F CD1    1 
ATOM   15895 C  CD2    . LEU   F 4  206 ? 3.765   -57.584  80.759  1.00 56.29  ? 206 LEU   F CD2    1 
ATOM   15896 N  N      . VAL   F 4  207 ? 0.655   -60.919  83.268  1.00 48.84  ? 207 VAL   F N      1 
ATOM   15897 C  CA     . VAL   F 4  207 ? 0.555   -62.305  82.820  1.00 47.40  ? 207 VAL   F CA     1 
ATOM   15898 C  C      . VAL   F 4  207 ? 0.546   -62.321  81.299  1.00 49.29  ? 207 VAL   F C      1 
ATOM   15899 O  O      . VAL   F 4  207 ? -0.280  -61.643  80.669  1.00 47.42  ? 207 VAL   F O      1 
ATOM   15900 C  CB     . VAL   F 4  207 ? -0.694  -63.004  83.385  1.00 44.36  ? 207 VAL   F CB     1 
ATOM   15901 C  CG1    . VAL   F 4  207 ? -0.639  -64.476  83.031  1.00 47.90  ? 207 VAL   F CG1    1 
ATOM   15902 C  CG2    . VAL   F 4  207 ? -0.786  -62.846  84.885  1.00 40.21  ? 207 VAL   F CG2    1 
ATOM   15903 N  N      . ASP   F 4  208 ? 1.445   -63.111  80.707  1.00 47.32  ? 208 ASP   F N      1 
ATOM   15904 C  CA     . ASP   F 4  208 ? 1.588   -63.139  79.261  1.00 47.99  ? 208 ASP   F CA     1 
ATOM   15905 C  C      . ASP   F 4  208 ? 0.725   -64.261  78.681  1.00 51.46  ? 208 ASP   F C      1 
ATOM   15906 O  O      . ASP   F 4  208 ? -0.044  -64.926  79.385  1.00 49.03  ? 208 ASP   F O      1 
ATOM   15907 C  CB     . ASP   F 4  208 ? 3.054   -63.305  78.870  1.00 52.66  ? 208 ASP   F CB     1 
ATOM   15908 C  CG     . ASP   F 4  208 ? 3.605   -64.676  79.206  1.00 53.04  ? 208 ASP   F CG     1 
ATOM   15909 O  OD1    . ASP   F 4  208 ? 2.823   -65.547  79.646  1.00 51.15  ? 208 ASP   F OD1    1 
ATOM   15910 O  OD2    . ASP   F 4  208 ? 4.830   -64.878  79.044  1.00 56.91  ? 208 ASP   F OD2    1 
ATOM   15911 N  N      . HIS   F 4  209 ? 0.853   -64.488  77.372  1.00 52.93  ? 209 HIS   F N      1 
ATOM   15912 C  CA     . HIS   F 4  209 ? 0.009   -65.479  76.710  1.00 50.18  ? 209 HIS   F CA     1 
ATOM   15913 C  C      . HIS   F 4  209 ? 0.288   -66.882  77.205  1.00 50.55  ? 209 HIS   F C      1 
ATOM   15914 O  O      . HIS   F 4  209 ? -0.610  -67.731  77.179  1.00 53.39  ? 209 HIS   F O      1 
ATOM   15915 C  CB     . HIS   F 4  209 ? 0.209   -65.397  75.202  1.00 50.77  ? 209 HIS   F CB     1 
ATOM   15916 C  CG     . HIS   F 4  209 ? 1.580   -65.767  74.761  1.00 47.11  ? 209 HIS   F CG     1 
ATOM   15917 N  ND1    . HIS   F 4  209 ? 2.634   -64.885  74.829  1.00 53.47  ? 209 HIS   F ND1    1 
ATOM   15918 C  CD2    . HIS   F 4  209 ? 2.075   -66.911  74.241  1.00 49.55  ? 209 HIS   F CD2    1 
ATOM   15919 C  CE1    . HIS   F 4  209 ? 3.723   -65.470  74.365  1.00 52.21  ? 209 HIS   F CE1    1 
ATOM   15920 N  NE2    . HIS   F 4  209 ? 3.413   -66.702  74.011  1.00 50.48  ? 209 HIS   F NE2    1 
ATOM   15921 N  N      . LEU   F 4  210 ? 1.518   -67.127  77.659  1.00 51.05  ? 210 LEU   F N      1 
ATOM   15922 C  CA     . LEU   F 4  210 ? 2.016   -68.402  78.156  1.00 48.91  ? 210 LEU   F CA     1 
ATOM   15923 C  C      . LEU   F 4  210 ? 1.716   -68.619  79.638  1.00 52.74  ? 210 LEU   F C      1 
ATOM   15924 O  O      . LEU   F 4  210 ? 2.062   -69.672  80.184  1.00 52.12  ? 210 LEU   F O      1 
ATOM   15925 C  CB     . LEU   F 4  210 ? 3.533   -68.467  77.930  1.00 54.02  ? 210 LEU   F CB     1 
ATOM   15926 C  CG     . LEU   F 4  210 ? 4.119   -68.319  76.522  1.00 45.65  ? 210 LEU   F CG     1 
ATOM   15927 C  CD1    . LEU   F 4  210 ? 5.607   -68.481  76.595  1.00 45.37  ? 210 LEU   F CD1    1 
ATOM   15928 C  CD2    . LEU   F 4  210 ? 3.549   -69.354  75.615  1.00 43.27  ? 210 LEU   F CD2    1 
ATOM   15929 N  N      . TYR   F 4  211 ? 1.090   -67.637  80.293  1.00 51.56  ? 211 TYR   F N      1 
ATOM   15930 C  CA     . TYR   F 4  211 ? 0.797   -67.639  81.728  1.00 48.54  ? 211 TYR   F CA     1 
ATOM   15931 C  C      . TYR   F 4  211 ? 2.069   -67.624  82.574  1.00 53.63  ? 211 TYR   F C      1 
ATOM   15932 O  O      . TYR   F 4  211 ? 2.081   -68.103  83.719  1.00 53.52  ? 211 TYR   F O      1 
ATOM   15933 C  CB     . TYR   F 4  211 ? -0.108  -68.801  82.143  1.00 43.83  ? 211 TYR   F CB     1 
ATOM   15934 C  CG     . TYR   F 4  211 ? -1.159  -68.372  83.171  1.00 46.72  ? 211 TYR   F CG     1 
ATOM   15935 C  CD1    . TYR   F 4  211 ? -2.365  -67.794  82.784  1.00 46.74  ? 211 TYR   F CD1    1 
ATOM   15936 C  CD2    . TYR   F 4  211 ? -0.913  -68.489  84.518  1.00 47.04  ? 211 TYR   F CD2    1 
ATOM   15937 C  CE1    . TYR   F 4  211 ? -3.302  -67.397  83.713  1.00 44.08  ? 211 TYR   F CE1    1 
ATOM   15938 C  CE2    . TYR   F 4  211 ? -1.835  -68.085  85.448  1.00 51.78  ? 211 TYR   F CE2    1 
ATOM   15939 C  CZ     . TYR   F 4  211 ? -3.027  -67.545  85.050  1.00 51.80  ? 211 TYR   F CZ     1 
ATOM   15940 O  OH     . TYR   F 4  211 ? -3.933  -67.157  86.020  1.00 49.78  ? 211 TYR   F OH     1 
ATOM   15941 N  N      . ASN   F 4  212 ? 3.152   -67.087  82.016  1.00 49.64  ? 212 ASN   F N      1 
ATOM   15942 C  CA     . ASN   F 4  212 ? 4.185   -66.504  82.854  1.00 50.72  ? 212 ASN   F CA     1 
ATOM   15943 C  C      . ASN   F 4  212 ? 3.574   -65.404  83.718  1.00 52.04  ? 212 ASN   F C      1 
ATOM   15944 O  O      . ASN   F 4  212 ? 2.673   -64.689  83.275  1.00 51.32  ? 212 ASN   F O      1 
ATOM   15945 C  CB     . ASN   F 4  212 ? 5.303   -65.946  81.984  1.00 47.89  ? 212 ASN   F CB     1 
ATOM   15946 C  CG     . ASN   F 4  212 ? 6.081   -67.024  81.316  1.00 58.52  ? 212 ASN   F CG     1 
ATOM   15947 O  OD1    . ASN   F 4  212 ? 6.583   -67.924  81.976  1.00 64.72  ? 212 ASN   F OD1    1 
ATOM   15948 N  ND2    . ASN   F 4  212 ? 6.183   -66.960  79.996  1.00 66.60  ? 212 ASN   F ND2    1 
ATOM   15949 N  N      . ILE   F 4  213 ? 4.047   -65.281  84.961  1.00 50.26  ? 213 ILE   F N      1 
ATOM   15950 C  CA     . ILE   F 4  213 ? 3.592   -64.243  85.877  1.00 48.08  ? 213 ILE   F CA     1 
ATOM   15951 C  C      . ILE   F 4  213 ? 4.764   -63.321  86.196  1.00 52.44  ? 213 ILE   F C      1 
ATOM   15952 O  O      . ILE   F 4  213 ? 5.672   -63.685  86.952  1.00 57.14  ? 213 ILE   F O      1 
ATOM   15953 C  CB     . ILE   F 4  213 ? 2.961   -64.833  87.140  1.00 43.39  ? 213 ILE   F CB     1 
ATOM   15954 C  CG1    . ILE   F 4  213 ? 1.605   -65.412  86.787  1.00 40.36  ? 213 ILE   F CG1    1 
ATOM   15955 C  CG2    . ILE   F 4  213 ? 2.838   -63.802  88.238  1.00 45.42  ? 213 ILE   F CG2    1 
ATOM   15956 C  CD1    . ILE   F 4  213 ? 1.068   -66.342  87.822  1.00 52.87  ? 213 ILE   F CD1    1 
ATOM   15957 N  N      . TYR   F 4  214 ? 4.726   -62.112  85.628  1.00 53.94  ? 214 TYR   F N      1 
ATOM   15958 C  CA     . TYR   F 4  214 ? 5.799   -61.124  85.720  1.00 55.90  ? 214 TYR   F CA     1 
ATOM   15959 C  C      . TYR   F 4  214 ? 5.411   -60.017  86.700  1.00 60.57  ? 214 TYR   F C      1 
ATOM   15960 O  O      . TYR   F 4  214 ? 4.444   -59.276  86.471  1.00 53.18  ? 214 TYR   F O      1 
ATOM   15961 C  CB     . TYR   F 4  214 ? 6.092   -60.513  84.356  1.00 54.33  ? 214 TYR   F CB     1 
ATOM   15962 C  CG     . TYR   F 4  214 ? 6.744   -61.445  83.372  1.00 58.41  ? 214 TYR   F CG     1 
ATOM   15963 C  CD1    . TYR   F 4  214 ? 8.069   -61.814  83.504  1.00 60.08  ? 214 TYR   F CD1    1 
ATOM   15964 C  CD2    . TYR   F 4  214 ? 6.036   -61.934  82.278  1.00 64.38  ? 214 TYR   F CD2    1 
ATOM   15965 C  CE1    . TYR   F 4  214 ? 8.669   -62.669  82.587  1.00 65.39  ? 214 TYR   F CE1    1 
ATOM   15966 C  CE2    . TYR   F 4  214 ? 6.629   -62.797  81.353  1.00 64.79  ? 214 TYR   F CE2    1 
ATOM   15967 C  CZ     . TYR   F 4  214 ? 7.946   -63.156  81.515  1.00 65.80  ? 214 TYR   F CZ     1 
ATOM   15968 O  OH     . TYR   F 4  214 ? 8.542   -64.003  80.610  1.00 68.25  ? 214 TYR   F OH     1 
ATOM   15969 N  N      . LEU   F 4  215 ? 6.177   -59.902  87.780  1.00 63.38  ? 215 LEU   F N      1 
ATOM   15970 C  CA     . LEU   F 4  215 ? 6.032   -58.821  88.739  1.00 59.83  ? 215 LEU   F CA     1 
ATOM   15971 C  C      . LEU   F 4  215 ? 6.906   -57.663  88.282  1.00 63.56  ? 215 LEU   F C      1 
ATOM   15972 O  O      . LEU   F 4  215 ? 8.103   -57.848  88.030  1.00 58.74  ? 215 LEU   F O      1 
ATOM   15973 C  CB     . LEU   F 4  215 ? 6.443   -59.291  90.131  1.00 59.03  ? 215 LEU   F CB     1 
ATOM   15974 C  CG     . LEU   F 4  215 ? 6.469   -58.301  91.290  1.00 52.21  ? 215 LEU   F CG     1 
ATOM   15975 C  CD1    . LEU   F 4  215 ? 5.089   -57.736  91.535  1.00 54.27  ? 215 LEU   F CD1    1 
ATOM   15976 C  CD2    . LEU   F 4  215 ? 6.991   -59.025  92.501  1.00 49.86  ? 215 LEU   F CD2    1 
ATOM   15977 N  N      . TYR   F 4  216 ? 6.305   -56.483  88.147  1.00 67.31  ? 216 TYR   F N      1 
ATOM   15978 C  CA     . TYR   F 4  216 ? 7.084   -55.272  87.927  1.00 68.98  ? 216 TYR   F CA     1 
ATOM   15979 C  C      . TYR   F 4  216 ? 7.839   -54.925  89.193  1.00 66.16  ? 216 TYR   F C      1 
ATOM   15980 O  O      . TYR   F 4  216 ? 7.233   -54.750  90.251  1.00 62.77  ? 216 TYR   F O      1 
ATOM   15981 C  CB     . TYR   F 4  216 ? 6.186   -54.106  87.522  1.00 71.64  ? 216 TYR   F CB     1 
ATOM   15982 C  CG     . TYR   F 4  216 ? 6.941   -52.840  87.147  1.00 70.44  ? 216 TYR   F CG     1 
ATOM   15983 C  CD1    . TYR   F 4  216 ? 8.287   -52.880  86.788  1.00 67.11  ? 216 TYR   F CD1    1 
ATOM   15984 C  CD2    . TYR   F 4  216 ? 6.305   -51.599  87.177  1.00 68.48  ? 216 TYR   F CD2    1 
ATOM   15985 C  CE1    . TYR   F 4  216 ? 8.974   -51.716  86.461  1.00 71.40  ? 216 TYR   F CE1    1 
ATOM   15986 C  CE2    . TYR   F 4  216 ? 6.985   -50.433  86.853  1.00 71.03  ? 216 TYR   F CE2    1 
ATOM   15987 C  CZ     . TYR   F 4  216 ? 8.319   -50.490  86.499  1.00 71.33  ? 216 TYR   F CZ     1 
ATOM   15988 O  OH     . TYR   F 4  216 ? 8.988   -49.320  86.182  1.00 71.78  ? 216 TYR   F OH     1 
ATOM   15989 N  N      . ARG   F 4  217 ? 9.163   -54.815  89.067  1.00 65.35  ? 217 ARG   F N      1 
ATOM   15990 C  CA     . ARG   F 4  217 ? 10.021  -54.594  90.222  1.00 63.61  ? 217 ARG   F CA     1 
ATOM   15991 C  C      . ARG   F 4  217 ? 9.737   -53.258  90.905  1.00 70.98  ? 217 ARG   F C      1 
ATOM   15992 O  O      . ARG   F 4  217 ? 9.887   -53.146  92.130  1.00 71.82  ? 217 ARG   F O      1 
ATOM   15993 C  CB     . ARG   F 4  217 ? 11.469  -54.641  89.787  1.00 60.50  ? 217 ARG   F CB     1 
ATOM   15994 C  CG     . ARG   F 4  217 ? 11.723  -53.533  88.825  1.00 72.66  ? 217 ARG   F CG     1 
ATOM   15995 C  CD     . ARG   F 4  217 ? 13.136  -53.057  88.889  1.00 80.44  ? 217 ARG   F CD     1 
ATOM   15996 N  NE     . ARG   F 4  217 ? 13.485  -52.279  87.711  1.00 77.96  ? 217 ARG   F NE     1 
ATOM   15997 C  CZ     . ARG   F 4  217 ? 14.371  -52.677  86.813  1.00 79.21  ? 217 ARG   F CZ     1 
ATOM   15998 N  NH1    . ARG   F 4  217 ? 14.965  -53.862  86.906  1.00 73.64  ? 217 ARG   F NH1    1 
ATOM   15999 N  NH2    . ARG   F 4  217 ? 14.665  -51.872  85.796  1.00 80.73  ? 217 ARG   F NH2    1 
ATOM   16000 N  N      . GLU   F 4  218 ? 9.345   -52.235  90.142  1.00 69.41  ? 218 GLU   F N      1 
ATOM   16001 C  CA     . GLU   F 4  218 ? 9.005   -50.934  90.713  1.00 66.15  ? 218 GLU   F CA     1 
ATOM   16002 C  C      . GLU   F 4  218 ? 7.628   -50.994  91.354  1.00 63.53  ? 218 GLU   F C      1 
ATOM   16003 O  O      . GLU   F 4  218 ? 6.625   -51.225  90.674  1.00 69.84  ? 218 GLU   F O      1 
ATOM   16004 C  CB     . GLU   F 4  218 ? 9.022   -49.849  89.643  1.00 66.30  ? 218 GLU   F CB     1 
ATOM   16005 C  CG     . GLU   F 4  218 ? 10.361  -49.601  89.031  1.00 68.62  ? 218 GLU   F CG     1 
ATOM   16006 C  CD     . GLU   F 4  218 ? 11.401  -49.380  90.083  1.00 71.89  ? 218 GLU   F CD     1 
ATOM   16007 O  OE1    . GLU   F 4  218 ? 11.037  -48.828  91.153  1.00 73.87  ? 218 GLU   F OE1    1 
ATOM   16008 O  OE2    . GLU   F 4  218 ? 12.573  -49.741  89.830  1.00 73.87  ? 218 GLU   F OE2    1 
ATOM   16009 N  N      . GLY   F 4  219 ? 7.568   -50.776  92.661  1.00 59.69  ? 219 GLY   F N      1 
ATOM   16010 C  CA     . GLY   F 4  219 ? 6.309   -50.682  93.355  1.00 65.28  ? 219 GLY   F CA     1 
ATOM   16011 C  C      . GLY   F 4  219 ? 6.012   -49.241  93.728  1.00 70.36  ? 219 GLY   F C      1 
ATOM   16012 O  O      . GLY   F 4  219 ? 6.816   -48.337  93.506  1.00 75.92  ? 219 GLY   F O      1 
ATOM   16013 N  N      . VAL   F 4  220 ? 4.828   -49.043  94.306  1.00 67.08  ? 220 VAL   F N      1 
ATOM   16014 C  CA     . VAL   F 4  220 ? 4.453   -47.733  94.823  1.00 75.50  ? 220 VAL   F CA     1 
ATOM   16015 C  C      . VAL   F 4  220 ? 3.648   -47.895  96.105  1.00 80.09  ? 220 VAL   F C      1 
ATOM   16016 O  O      . VAL   F 4  220 ? 2.751   -48.740  96.189  1.00 74.90  ? 220 VAL   F O      1 
ATOM   16017 C  CB     . VAL   F 4  220 ? 3.660   -46.908  93.795  1.00 76.40  ? 220 VAL   F CB     1 
ATOM   16018 C  CG1    . VAL   F 4  220 ? 2.202   -47.337  93.765  1.00 70.04  ? 220 VAL   F CG1    1 
ATOM   16019 C  CG2    . VAL   F 4  220 ? 3.794   -45.429  94.113  1.00 82.26  ? 220 VAL   F CG2    1 
ATOM   16020 N  N      . LEU   F 4  221 ? 3.989   -47.087  97.114  1.00 85.74  ? 221 LEU   F N      1 
ATOM   16021 C  CA     . LEU   F 4  221 ? 3.179   -46.923  98.314  1.00 82.58  ? 221 LEU   F CA     1 
ATOM   16022 C  C      . LEU   F 4  221 ? 2.351   -45.659  98.169  1.00 89.70  ? 221 LEU   F C      1 
ATOM   16023 O  O      . LEU   F 4  221 ? 2.894   -44.572  97.947  1.00 88.98  ? 221 LEU   F O      1 
ATOM   16024 C  CB     . LEU   F 4  221 ? 4.032   -46.842  99.576  1.00 84.57  ? 221 LEU   F CB     1 
ATOM   16025 C  CG     . LEU   F 4  221 ? 5.001   -47.971  99.892  1.00 81.34  ? 221 LEU   F CG     1 
ATOM   16026 C  CD1    . LEU   F 4  221 ? 6.370   -47.682  99.320  1.00 79.86  ? 221 LEU   F CD1    1 
ATOM   16027 C  CD2    . LEU   F 4  221 ? 5.090   -48.090  101.398 1.00 79.28  ? 221 LEU   F CD2    1 
ATOM   16028 N  N      . ARG   F 4  222 ? 1.041   -45.812  98.277  1.00 97.95  ? 222 ARG   F N      1 
ATOM   16029 C  CA     . ARG   F 4  222 ? 0.121   -44.687  98.289  1.00 103.00 ? 222 ARG   F CA     1 
ATOM   16030 C  C      . ARG   F 4  222 ? -0.131  -44.336  99.753  1.00 105.85 ? 222 ARG   F C      1 
ATOM   16031 O  O      . ARG   F 4  222 ? -0.732  -45.123  100.494 1.00 100.19 ? 222 ARG   F O      1 
ATOM   16032 C  CB     . ARG   F 4  222 ? -1.164  -45.037  97.541  1.00 101.51 ? 222 ARG   F CB     1 
ATOM   16033 C  CG     . ARG   F 4  222 ? -1.017  -45.052  96.024  1.00 91.91  ? 222 ARG   F CG     1 
ATOM   16034 C  CD     . ARG   F 4  222 ? -2.255  -45.636  95.364  1.00 99.20  ? 222 ARG   F CD     1 
ATOM   16035 N  NE     . ARG   F 4  222 ? -2.629  -46.953  95.864  1.00 92.11  ? 222 ARG   F NE     1 
ATOM   16036 C  CZ     . ARG   F 4  222 ? -3.369  -47.814  95.180  1.00 87.32  ? 222 ARG   F CZ     1 
ATOM   16037 N  NH1    . ARG   F 4  222 ? -3.885  -47.494  94.002  1.00 85.43  ? 222 ARG   F NH1    1 
ATOM   16038 N  NH2    . ARG   F 4  222 ? -3.638  -49.004  95.710  1.00 75.78  ? 222 ARG   F NH2    1 
ATOM   16039 N  N      . THR   F 4  223 ? 0.355   -43.170  100.176 1.00 111.54 ? 223 THR   F N      1 
ATOM   16040 C  CA     . THR   F 4  223 ? 0.431   -42.801  101.583 1.00 108.19 ? 223 THR   F CA     1 
ATOM   16041 C  C      . THR   F 4  223 ? -0.568  -41.704  101.924 1.00 112.92 ? 223 THR   F C      1 
ATOM   16042 O  O      . THR   F 4  223 ? -0.798  -40.783  101.126 1.00 106.65 ? 223 THR   F O      1 
ATOM   16043 C  CB     . THR   F 4  223 ? 1.835   -42.320  101.946 1.00 107.97 ? 223 THR   F CB     1 
ATOM   16044 O  OG1    . THR   F 4  223 ? 2.005   -40.974  101.485 1.00 110.86 ? 223 THR   F OG1    1 
ATOM   16045 C  CG2    . THR   F 4  223 ? 2.889   -43.207  101.307 1.00 105.58 ? 223 THR   F CG2    1 
ATOM   16046 N  N      . SER   F 4  224 ? -1.139  -41.803  103.127 1.00 116.46 ? 224 SER   F N      1 
ATOM   16047 C  CA     . SER   F 4  224 ? -1.996  -40.765  103.685 1.00 114.59 ? 224 SER   F CA     1 
ATOM   16048 C  C      . SER   F 4  224 ? -1.105  -39.728  104.366 1.00 110.38 ? 224 SER   F C      1 
ATOM   16049 O  O      . SER   F 4  224 ? -0.298  -40.072  105.237 1.00 105.07 ? 224 SER   F O      1 
ATOM   16050 C  CB     . SER   F 4  224 ? -3.008  -41.374  104.663 1.00 109.06 ? 224 SER   F CB     1 
ATOM   16051 O  OG     . SER   F 4  224 ? -3.609  -40.407  105.505 1.00 107.48 ? 224 SER   F OG     1 
ATOM   16052 N  N      . SER   F 4  225 ? -1.211  -38.471  103.923 1.00 114.17 ? 225 SER   F N      1 
ATOM   16053 C  CA     . SER   F 4  225 ? -0.525  -37.356  104.567 1.00 113.05 ? 225 SER   F CA     1 
ATOM   16054 C  C      . SER   F 4  225 ? -1.105  -37.044  105.936 1.00 111.99 ? 225 SER   F C      1 
ATOM   16055 O  O      . SER   F 4  225 ? -0.475  -36.333  106.725 1.00 106.70 ? 225 SER   F O      1 
ATOM   16056 C  CB     . SER   F 4  225 ? -0.612  -36.115  103.684 1.00 109.76 ? 225 SER   F CB     1 
ATOM   16057 O  OG     . SER   F 4  225 ? -0.074  -36.381  102.408 1.00 108.25 ? 225 SER   F OG     1 
ATOM   16058 N  N      . GLU   F 4  226 ? -2.245  -37.555  106.219 1.00 113.90 ? 226 GLU   F N      1 
ATOM   16059 C  CA     . GLU   F 4  226 ? -2.982  -37.339  107.449 1.00 117.33 ? 226 GLU   F CA     1 
ATOM   16060 C  C      . GLU   F 4  226 ? -2.533  -38.345  108.501 1.00 118.45 ? 226 GLU   F C      1 
ATOM   16061 O  O      . GLU   F 4  226 ? -2.570  -39.556  108.246 1.00 118.06 ? 226 GLU   F O      1 
ATOM   16062 C  CB     . GLU   F 4  226 ? -4.471  -37.479  107.188 1.00 119.73 ? 226 GLU   F CB     1 
ATOM   16063 C  CG     . GLU   F 4  226 ? -4.892  -36.786  105.902 1.00 121.02 ? 226 GLU   F CG     1 
ATOM   16064 C  CD     . GLU   F 4  226 ? -4.725  -35.283  105.981 1.00 123.73 ? 226 GLU   F CD     1 
ATOM   16065 O  OE1    . GLU   F 4  226 ? -5.603  -34.629  106.589 1.00 126.09 ? 226 GLU   F OE1    1 
ATOM   16066 O  OE2    . GLU   F 4  226 ? -3.702  -34.767  105.469 1.00 114.85 ? 226 GLU   F OE2    1 
ATOM   16067 N  N      . PRO   F 4  227 ? -2.081  -37.889  109.667 1.00 119.21 ? 227 PRO   F N      1 
ATOM   16068 C  CA     . PRO   F 4  227 ? -1.761  -38.827  110.751 1.00 112.92 ? 227 PRO   F CA     1 
ATOM   16069 C  C      . PRO   F 4  227 ? -2.966  -39.684  111.112 1.00 113.22 ? 227 PRO   F C      1 
ATOM   16070 O  O      . PRO   F 4  227 ? -4.088  -39.194  111.252 1.00 114.71 ? 227 PRO   F O      1 
ATOM   16071 C  CB     . PRO   F 4  227 ? -1.342  -37.908  111.905 1.00 113.94 ? 227 PRO   F CB     1 
ATOM   16072 C  CG     . PRO   F 4  227 ? -1.854  -36.542  111.535 1.00 113.88 ? 227 PRO   F CG     1 
ATOM   16073 C  CD     . PRO   F 4  227 ? -1.830  -36.489  110.044 1.00 117.05 ? 227 PRO   F CD     1 
ATOM   16074 N  N      . TYR   F 4  228 ? -2.717  -40.978  111.255 1.00 115.22 ? 228 TYR   F N      1 
ATOM   16075 C  CA     . TYR   F 4  228 ? -3.774  -41.956  111.471 1.00 119.69 ? 228 TYR   F CA     1 
ATOM   16076 C  C      . TYR   F 4  228 ? -4.200  -41.975  112.939 1.00 118.30 ? 228 TYR   F C      1 
ATOM   16077 O  O      . TYR   F 4  228 ? -3.358  -41.905  113.838 1.00 121.39 ? 228 TYR   F O      1 
ATOM   16078 C  CB     . TYR   F 4  228 ? -3.267  -43.330  111.007 1.00 111.67 ? 228 TYR   F CB     1 
ATOM   16079 C  CG     . TYR   F 4  228 ? -4.217  -44.490  111.185 1.00 110.93 ? 228 TYR   F CG     1 
ATOM   16080 C  CD1    . TYR   F 4  228 ? -4.192  -45.250  112.345 1.00 102.26 ? 228 TYR   F CD1    1 
ATOM   16081 C  CD2    . TYR   F 4  228 ? -5.127  -44.836  110.198 1.00 113.34 ? 228 TYR   F CD2    1 
ATOM   16082 C  CE1    . TYR   F 4  228 ? -5.043  -46.307  112.525 1.00 97.68  ? 228 TYR   F CE1    1 
ATOM   16083 C  CE2    . TYR   F 4  228 ? -5.990  -45.903  110.375 1.00 110.25 ? 228 TYR   F CE2    1 
ATOM   16084 C  CZ     . TYR   F 4  228 ? -5.938  -46.633  111.545 1.00 99.36  ? 228 TYR   F CZ     1 
ATOM   16085 O  OH     . TYR   F 4  228 ? -6.786  -47.693  111.741 1.00 101.71 ? 228 TYR   F OH     1 
ATOM   16086 N  N      . ASN   F 4  229 ? -5.514  -42.035  113.184 1.00 114.28 ? 229 ASN   F N      1 
ATOM   16087 C  CA     . ASN   F 4  229 ? -6.026  -42.188  114.545 1.00 119.36 ? 229 ASN   F CA     1 
ATOM   16088 C  C      . ASN   F 4  229 ? -7.349  -42.935  114.508 1.00 118.39 ? 229 ASN   F C      1 
ATOM   16089 O  O      . ASN   F 4  229 ? -8.150  -42.739  113.592 1.00 124.39 ? 229 ASN   F O      1 
ATOM   16090 C  CB     . ASN   F 4  229 ? -6.245  -40.848  115.258 1.00 129.70 ? 229 ASN   F CB     1 
ATOM   16091 C  CG     . ASN   F 4  229 ? -7.350  -40.022  114.628 1.00 134.78 ? 229 ASN   F CG     1 
ATOM   16092 O  OD1    . ASN   F 4  229 ? -7.580  -40.079  113.417 1.00 141.33 ? 229 ASN   F OD1    1 
ATOM   16093 N  ND2    . ASN   F 4  229 ? -8.068  -39.273  115.459 1.00 130.30 ? 229 ASN   F ND2    1 
ATOM   16094 N  N      . SER   F 4  230 ? -7.594  -43.752  115.530 1.00 112.62 ? 230 SER   F N      1 
ATOM   16095 C  CA     . SER   F 4  230 ? -8.690  -44.710  115.509 1.00 121.12 ? 230 SER   F CA     1 
ATOM   16096 C  C      . SER   F 4  230 ? -9.930  -44.257  116.276 1.00 131.33 ? 230 SER   F C      1 
ATOM   16097 O  O      . SER   F 4  230 ? -10.791 -45.089  116.578 1.00 130.32 ? 230 SER   F O      1 
ATOM   16098 C  CB     . SER   F 4  230 ? -8.211  -46.056  116.053 1.00 118.84 ? 230 SER   F CB     1 
ATOM   16099 O  OG     . SER   F 4  230 ? -7.678  -45.922  117.355 1.00 116.20 ? 230 SER   F OG     1 
ATOM   16100 N  N      . ALA   F 4  231 ? -10.055 -42.968  116.591 1.00 137.03 ? 231 ALA   F N      1 
ATOM   16101 C  CA     . ALA   F 4  231 ? -11.258 -42.497  117.269 1.00 134.87 ? 231 ALA   F CA     1 
ATOM   16102 C  C      . ALA   F 4  231 ? -12.327 -42.056  116.276 1.00 139.53 ? 231 ALA   F C      1 
ATOM   16103 O  O      . ALA   F 4  231 ? -13.493 -42.450  116.396 1.00 136.56 ? 231 ALA   F O      1 
ATOM   16104 C  CB     . ALA   F 4  231 ? -10.916 -41.350  118.223 1.00 134.67 ? 231 ALA   F CB     1 
ATOM   16105 N  N      . ASN   F 4  232 ? -11.938 -41.252  115.286 1.00 140.53 ? 232 ASN   F N      1 
ATOM   16106 C  CA     . ASN   F 4  232 ? -12.853 -40.650  114.317 1.00 145.09 ? 232 ASN   F CA     1 
ATOM   16107 C  C      . ASN   F 4  232 ? -12.668 -41.342  112.966 1.00 145.64 ? 232 ASN   F C      1 
ATOM   16108 O  O      . ASN   F 4  232 ? -11.837 -40.940  112.147 1.00 142.23 ? 232 ASN   F O      1 
ATOM   16109 C  CB     . ASN   F 4  232 ? -12.618 -39.140  114.209 1.00 146.68 ? 232 ASN   F CB     1 
ATOM   16110 C  CG     . ASN   F 4  232 ? -11.143 -38.782  114.106 1.00 150.34 ? 232 ASN   F CG     1 
ATOM   16111 O  OD1    . ASN   F 4  232 ? -10.279 -39.507  114.609 1.00 145.16 ? 232 ASN   F OD1    1 
ATOM   16112 N  ND2    . ASN   F 4  232 ? -10.848 -37.666  113.440 1.00 148.21 ? 232 ASN   F ND2    1 
ATOM   16113 N  N      . PHE   F 4  233 ? -13.463 -42.392  112.741 1.00 145.37 ? 233 PHE   F N      1 
ATOM   16114 C  CA     . PHE   F 4  233 ? -13.457 -43.069  111.448 1.00 137.60 ? 233 PHE   F CA     1 
ATOM   16115 C  C      . PHE   F 4  233 ? -14.077 -42.185  110.370 1.00 141.64 ? 233 PHE   F C      1 
ATOM   16116 O  O      . PHE   F 4  233 ? -13.492 -41.996  109.298 1.00 143.33 ? 233 PHE   F O      1 
ATOM   16117 C  CB     . PHE   F 4  233 ? -14.200 -44.404  111.544 1.00 133.98 ? 233 PHE   F CB     1 
ATOM   16118 C  CG     . PHE   F 4  233 ? -13.498 -45.440  112.388 1.00 138.91 ? 233 PHE   F CG     1 
ATOM   16119 C  CD1    . PHE   F 4  233 ? -12.379 -46.108  111.911 1.00 139.73 ? 233 PHE   F CD1    1 
ATOM   16120 C  CD2    . PHE   F 4  233 ? -13.978 -45.768  113.651 1.00 139.79 ? 233 PHE   F CD2    1 
ATOM   16121 C  CE1    . PHE   F 4  233 ? -11.736 -47.065  112.688 1.00 134.91 ? 233 PHE   F CE1    1 
ATOM   16122 C  CE2    . PHE   F 4  233 ? -13.344 -46.727  114.430 1.00 134.14 ? 233 PHE   F CE2    1 
ATOM   16123 C  CZ     . PHE   F 4  233 ? -12.222 -47.374  113.949 1.00 130.85 ? 233 PHE   F CZ     1 
ATOM   16124 N  N      . GLN   F 4  234 ? -15.261 -41.620  110.643 1.00 139.10 ? 234 GLN   F N      1 
ATOM   16125 C  CA     . GLN   F 4  234 ? -15.927 -40.758  109.668 1.00 135.86 ? 234 GLN   F CA     1 
ATOM   16126 C  C      . GLN   F 4  234 ? -14.994 -39.721  109.053 1.00 137.81 ? 234 GLN   F C      1 
ATOM   16127 O  O      . GLN   F 4  234 ? -15.306 -39.191  107.981 1.00 138.04 ? 234 GLN   F O      1 
ATOM   16128 C  CB     . GLN   F 4  234 ? -17.134 -40.045  110.300 1.00 137.60 ? 234 GLN   F CB     1 
ATOM   16129 C  CG     . GLN   F 4  234 ? -18.432 -40.855  110.320 1.00 137.39 ? 234 GLN   F CG     1 
ATOM   16130 C  CD     . GLN   F 4  234 ? -18.802 -41.408  111.687 1.00 135.34 ? 234 GLN   F CD     1 
ATOM   16131 O  OE1    . GLN   F 4  234 ? -19.125 -40.658  112.612 1.00 134.13 ? 234 GLN   F OE1    1 
ATOM   16132 N  NE2    . GLN   F 4  234 ? -18.771 -42.730  111.815 1.00 135.80 ? 234 GLN   F NE2    1 
ATOM   16133 N  N      . ASP   F 4  235 ? -13.868 -39.406  109.703 1.00 137.42 ? 235 ASP   F N      1 
ATOM   16134 C  CA     . ASP   F 4  235 ? -12.832 -38.556  109.105 1.00 139.72 ? 235 ASP   F CA     1 
ATOM   16135 C  C      . ASP   F 4  235 ? -11.902 -39.395  108.227 1.00 139.51 ? 235 ASP   F C      1 
ATOM   16136 O  O      . ASP   F 4  235 ? -10.681 -39.418  108.386 1.00 136.64 ? 235 ASP   F O      1 
ATOM   16137 C  CB     . ASP   F 4  235 ? -12.052 -37.797  110.171 1.00 142.27 ? 235 ASP   F CB     1 
ATOM   16138 C  CG     . ASP   F 4  235 ? -11.319 -36.582  109.601 1.00 137.93 ? 235 ASP   F CG     1 
ATOM   16139 O  OD1    . ASP   F 4  235 ? -10.910 -36.623  108.415 1.00 126.00 ? 235 ASP   F OD1    1 
ATOM   16140 O  OD2    . ASP   F 4  235 ? -11.194 -35.568  110.319 1.00 142.12 ? 235 ASP   F OD2    1 
ATOM   16141 N  N      . LYS   F 4  236 ? -12.529 -40.100  107.284 1.00 138.56 ? 236 LYS   F N      1 
ATOM   16142 C  CA     . LYS   F 4  236 ? -11.848 -40.996  106.361 1.00 134.59 ? 236 LYS   F CA     1 
ATOM   16143 C  C      . LYS   F 4  236 ? -11.033 -40.228  105.324 1.00 128.29 ? 236 LYS   F C      1 
ATOM   16144 O  O      . LYS   F 4  236 ? -11.365 -40.240  104.135 1.00 126.97 ? 236 LYS   F O      1 
ATOM   16145 C  CB     . LYS   F 4  236 ? -12.870 -41.911  105.672 1.00 131.32 ? 236 LYS   F CB     1 
ATOM   16146 N  N      . THR   F 4  237 ? -9.985  -39.537  105.764 1.00 126.87 ? 237 THR   F N      1 
ATOM   16147 C  CA     . THR   F 4  237 ? -8.915  -39.089  104.879 1.00 128.92 ? 237 THR   F CA     1 
ATOM   16148 C  C      . THR   F 4  237 ? -7.569  -39.678  105.257 1.00 126.79 ? 237 THR   F C      1 
ATOM   16149 O  O      . THR   F 4  237 ? -6.700  -39.821  104.391 1.00 120.91 ? 237 THR   F O      1 
ATOM   16150 C  CB     . THR   F 4  237 ? -8.784  -37.559  104.880 1.00 131.25 ? 237 THR   F CB     1 
ATOM   16151 O  OG1    . THR   F 4  237 ? -10.059 -36.972  104.608 1.00 142.35 ? 237 THR   F OG1    1 
ATOM   16152 C  CG2    . THR   F 4  237 ? -7.793  -37.116  103.798 1.00 121.58 ? 237 THR   F CG2    1 
ATOM   16153 N  N      . CYS   F 4  238 ? -7.377  -40.004  106.531 1.00 125.60 ? 238 CYS   F N      1 
ATOM   16154 C  CA     . CYS   F 4  238 ? -6.221  -40.735  107.020 1.00 122.13 ? 238 CYS   F CA     1 
ATOM   16155 C  C      . CYS   F 4  238 ? -6.479  -42.228  107.092 1.00 122.65 ? 238 CYS   F C      1 
ATOM   16156 O  O      . CYS   F 4  238 ? -5.575  -42.983  107.465 1.00 123.11 ? 238 CYS   F O      1 
ATOM   16157 C  CB     . CYS   F 4  238 ? -5.816  -40.224  108.408 1.00 124.52 ? 238 CYS   F CB     1 
ATOM   16158 S  SG     . CYS   F 4  238 ? -6.896  -40.763  109.779 1.00 123.54 ? 238 CYS   F SG     1 
ATOM   16159 N  N      . HIS   F 4  239 ? -7.698  -42.663  106.776 1.00 121.12 ? 239 HIS   F N      1 
ATOM   16160 C  CA     . HIS   F 4  239 ? -8.043  -44.075  106.697 1.00 120.70 ? 239 HIS   F CA     1 
ATOM   16161 C  C      . HIS   F 4  239 ? -8.088  -44.585  105.265 1.00 120.57 ? 239 HIS   F C      1 
ATOM   16162 O  O      . HIS   F 4  239 ? -7.547  -45.659  104.981 1.00 111.96 ? 239 HIS   F O      1 
ATOM   16163 C  CB     . HIS   F 4  239 ? -9.401  -44.332  107.357 1.00 123.56 ? 239 HIS   F CB     1 
ATOM   16164 C  CG     . HIS   F 4  239 ? -9.371  -44.279  108.852 1.00 125.80 ? 239 HIS   F CG     1 
ATOM   16165 N  ND1    . HIS   F 4  239 ? -8.628  -43.350  109.549 1.00 125.39 ? 239 HIS   F ND1    1 
ATOM   16166 C  CD2    . HIS   F 4  239 ? -10.003 -45.033  109.783 1.00 125.35 ? 239 HIS   F CD2    1 
ATOM   16167 C  CE1    . HIS   F 4  239 ? -8.805  -43.535  110.845 1.00 126.63 ? 239 HIS   F CE1    1 
ATOM   16168 N  NE2    . HIS   F 4  239 ? -9.633  -44.552  111.014 1.00 123.04 ? 239 HIS   F NE2    1 
ATOM   16169 N  N      . LEU   F 4  240 ? -8.727  -43.836  104.361 1.00 122.54 ? 240 LEU   F N      1 
ATOM   16170 C  CA     . LEU   F 4  240 ? -8.841  -44.209  102.955 1.00 111.06 ? 240 LEU   F CA     1 
ATOM   16171 C  C      . LEU   F 4  240 ? -7.629  -43.658  102.212 1.00 112.47 ? 240 LEU   F C      1 
ATOM   16172 O  O      . LEU   F 4  240 ? -7.464  -42.439  102.096 1.00 113.14 ? 240 LEU   F O      1 
ATOM   16173 C  CB     . LEU   F 4  240 ? -10.145 -43.687  102.363 1.00 103.25 ? 240 LEU   F CB     1 
ATOM   16174 N  N      . THR   F 4  241 ? -6.795  -44.563  101.695 1.00 115.98 ? 241 THR   F N      1 
ATOM   16175 C  CA     . THR   F 4  241 ? -5.474  -44.256  101.158 1.00 114.01 ? 241 THR   F CA     1 
ATOM   16176 C  C      . THR   F 4  241 ? -5.468  -44.003  99.658  1.00 110.72 ? 241 THR   F C      1 
ATOM   16177 O  O      . THR   F 4  241 ? -4.402  -44.078  99.040  1.00 109.53 ? 241 THR   F O      1 
ATOM   16178 C  CB     . THR   F 4  241 ? -4.489  -45.393  101.475 1.00 109.78 ? 241 THR   F CB     1 
ATOM   16179 O  OG1    . THR   F 4  241 ? -4.988  -46.636  100.953 1.00 109.05 ? 241 THR   F OG1    1 
ATOM   16180 C  CG2    . THR   F 4  241 ? -4.234  -45.514  102.973 1.00 107.30 ? 241 THR   F CG2    1 
ATOM   16181 N  N      . ASN   F 4  242 ? -6.614  -43.711  99.055  1.00 117.32 ? 242 ASN   F N      1 
ATOM   16182 C  CA     . ASN   F 4  242 ? -6.652  -43.532  97.609  1.00 124.62 ? 242 ASN   F CA     1 
ATOM   16183 C  C      . ASN   F 4  242 ? -5.933  -42.252  97.207  1.00 125.61 ? 242 ASN   F C      1 
ATOM   16184 O  O      . ASN   F 4  242 ? -6.175  -41.183  97.776  1.00 123.77 ? 242 ASN   F O      1 
ATOM   16185 C  CB     . ASN   F 4  242 ? -8.094  -43.511  97.108  1.00 126.11 ? 242 ASN   F CB     1 
ATOM   16186 C  CG     . ASN   F 4  242 ? -8.904  -44.680  97.626  1.00 130.13 ? 242 ASN   F CG     1 
ATOM   16187 O  OD1    . ASN   F 4  242 ? -9.196  -44.761  98.820  1.00 128.91 ? 242 ASN   F OD1    1 
ATOM   16188 N  ND2    . ASN   F 4  242 ? -9.273  -45.596  96.730  1.00 130.44 ? 242 ASN   F ND2    1 
ATOM   16189 N  N      . HIS   F 4  243 ? -5.041  -42.370  96.220  1.00 124.95 ? 243 HIS   F N      1 
ATOM   16190 C  CA     . HIS   F 4  243 ? -4.349  -41.197  95.696  1.00 128.29 ? 243 HIS   F CA     1 
ATOM   16191 C  C      . HIS   F 4  243 ? -5.326  -40.084  95.350  1.00 125.76 ? 243 HIS   F C      1 
ATOM   16192 O  O      . HIS   F 4  243 ? -5.064  -38.905  95.615  1.00 122.89 ? 243 HIS   F O      1 
ATOM   16193 C  CB     . HIS   F 4  243 ? -3.540  -41.588  94.462  1.00 129.58 ? 243 HIS   F CB     1 
ATOM   16194 C  CG     . HIS   F 4  243 ? -2.959  -40.421  93.735  1.00 131.12 ? 243 HIS   F CG     1 
ATOM   16195 N  ND1    . HIS   F 4  243 ? -3.741  -39.459  93.132  1.00 132.99 ? 243 HIS   F ND1    1 
ATOM   16196 C  CD2    . HIS   F 4  243 ? -1.675  -40.067  93.497  1.00 131.28 ? 243 HIS   F CD2    1 
ATOM   16197 C  CE1    . HIS   F 4  243 ? -2.964  -38.555  92.565  1.00 137.78 ? 243 HIS   F CE1    1 
ATOM   16198 N  NE2    . HIS   F 4  243 ? -1.706  -38.901  92.769  1.00 138.65 ? 243 HIS   F NE2    1 
ATOM   16199 N  N      . CYS   F 4  244 ? -6.446  -40.444  94.730  1.00 129.73 ? 244 CYS   F N      1 
ATOM   16200 C  CA     . CYS   F 4  244 ? -7.435  -39.456  94.322  1.00 129.04 ? 244 CYS   F CA     1 
ATOM   16201 C  C      . CYS   F 4  244 ? -8.149  -38.874  95.531  1.00 123.32 ? 244 CYS   F C      1 
ATOM   16202 O  O      . CYS   F 4  244 ? -8.116  -37.660  95.762  1.00 126.06 ? 244 CYS   F O      1 
ATOM   16203 C  CB     . CYS   F 4  244 ? -8.426  -40.103  93.359  1.00 130.05 ? 244 CYS   F CB     1 
ATOM   16204 S  SG     . CYS   F 4  244 ? -7.586  -41.082  92.097  1.00 139.01 ? 244 CYS   F SG     1 
ATOM   16205 N  N      . ILE   F 4  245 ? -8.782  -39.732  96.328  1.00 120.57 ? 245 ILE   F N      1 
ATOM   16206 C  CA     . ILE   F 4  245 ? -9.520  -39.299  97.509  1.00 123.86 ? 245 ILE   F CA     1 
ATOM   16207 C  C      . ILE   F 4  245 ? -8.685  -38.327  98.343  1.00 124.90 ? 245 ILE   F C      1 
ATOM   16208 O  O      . ILE   F 4  245 ? -9.234  -37.518  99.098  1.00 130.41 ? 245 ILE   F O      1 
ATOM   16209 C  CB     . ILE   F 4  245 ? -9.985  -40.519  98.331  1.00 123.48 ? 245 ILE   F CB     1 
ATOM   16210 C  CG1    . ILE   F 4  245 ? -11.383 -40.960  97.873  1.00 124.50 ? 245 ILE   F CG1    1 
ATOM   16211 C  CG2    . ILE   F 4  245 ? -9.959  -40.220  99.830  1.00 119.78 ? 245 ILE   F CG2    1 
ATOM   16212 C  CD1    . ILE   F 4  245 ? -11.555 -41.047  96.355  1.00 117.87 ? 245 ILE   F CD1    1 
ATOM   16213 N  N      . GLN   F 4  246 ? -7.358  -38.369  98.198  1.00 124.67 ? 246 GLN   F N      1 
ATOM   16214 C  CA     . GLN   F 4  246 ? -6.496  -37.348  98.799  1.00 122.49 ? 246 GLN   F CA     1 
ATOM   16215 C  C      . GLN   F 4  246 ? -6.458  -36.133  97.865  1.00 125.15 ? 246 GLN   F C      1 
ATOM   16216 O  O      . GLN   F 4  246 ? -5.466  -35.810  97.204  1.00 118.66 ? 246 GLN   F O      1 
ATOM   16217 C  CB     . GLN   F 4  246 ? -5.122  -37.921  99.112  1.00 118.30 ? 246 GLN   F CB     1 
ATOM   16218 C  CG     . GLN   F 4  246 ? -5.223  -39.219  99.926  1.00 116.84 ? 246 GLN   F CG     1 
ATOM   16219 C  CD     . GLN   F 4  246 ? -4.688  -39.100  101.345 1.00 106.46 ? 246 GLN   F CD     1 
ATOM   16220 O  OE1    . GLN   F 4  246 ? -3.528  -38.757  101.557 1.00 101.02 ? 246 GLN   F OE1    1 
ATOM   16221 N  NE2    . GLN   F 4  246 ? -5.540  -39.385  102.326 1.00 110.19 ? 246 GLN   F NE2    1 
ATOM   16222 N  N      . LYS   F 4  247 ? -7.601  -35.457  97.826  1.00 126.14 ? 247 LYS   F N      1 
ATOM   16223 C  CA     . LYS   F 4  247 ? -7.845  -34.312  96.977  1.00 117.60 ? 247 LYS   F CA     1 
ATOM   16224 C  C      . LYS   F 4  247 ? -6.785  -33.238  97.181  1.00 117.69 ? 247 LYS   F C      1 
ATOM   16225 O  O      . LYS   F 4  247 ? -6.679  -32.659  98.261  1.00 119.20 ? 247 LYS   F O      1 
ATOM   16226 C  CB     . LYS   F 4  247 ? -9.240  -33.764  97.270  1.00 110.63 ? 247 LYS   F CB     1 
ATOM   16227 C  CG     . LYS   F 4  247 ? -9.770  -32.828  96.218  1.00 117.40 ? 247 LYS   F CG     1 
ATOM   16228 C  CD     . LYS   F 4  247 ? -10.443 -33.588  95.096  1.00 112.39 ? 247 LYS   F CD     1 
ATOM   16229 C  CE     . LYS   F 4  247 ? -10.813 -32.647  93.958  1.00 113.09 ? 247 LYS   F CE     1 
ATOM   16230 N  NZ     . LYS   F 4  247 ? -9.650  -32.248  93.119  1.00 107.47 ? 247 LYS   F NZ     1 
ATOM   16231 N  N      . ASN   F 4  252 ? -3.012  -31.445  102.186 1.00 116.32 ? 252 ASN   F N      1 
ATOM   16232 C  CA     . ASN   F 4  252 ? -1.832  -32.122  102.720 1.00 119.11 ? 252 ASN   F CA     1 
ATOM   16233 C  C      . ASN   F 4  252 ? -1.058  -32.840  101.621 1.00 115.29 ? 252 ASN   F C      1 
ATOM   16234 O  O      . ASN   F 4  252 ? 0.115   -33.191  101.779 1.00 112.54 ? 252 ASN   F O      1 
ATOM   16235 C  CB     . ASN   F 4  252 ? -2.242  -33.110  103.807 1.00 113.60 ? 252 ASN   F CB     1 
ATOM   16236 C  CG     . ASN   F 4  252 ? -1.745  -32.702  105.169 1.00 114.18 ? 252 ASN   F CG     1 
ATOM   16237 O  OD1    . ASN   F 4  252 ? -0.761  -31.972  105.289 1.00 112.08 ? 252 ASN   F OD1    1 
ATOM   16238 N  ND2    . ASN   F 4  252 ? -2.439  -33.146  106.206 1.00 112.23 ? 252 ASN   F ND2    1 
ATOM   16239 N  N      . TYR   F 4  253 ? -1.751  -33.044  100.505 1.00 116.48 ? 253 TYR   F N      1 
ATOM   16240 C  CA     . TYR   F 4  253 ? -1.248  -33.722  99.318  1.00 116.81 ? 253 TYR   F CA     1 
ATOM   16241 C  C      . TYR   F 4  253 ? 0.156   -33.265  98.928  1.00 118.67 ? 253 TYR   F C      1 
ATOM   16242 O  O      . TYR   F 4  253 ? 0.301   -32.311  98.158  1.00 121.65 ? 253 TYR   F O      1 
ATOM   16243 C  CB     . TYR   F 4  253 ? -2.218  -33.464  98.163  1.00 119.01 ? 253 TYR   F CB     1 
ATOM   16244 C  CG     . TYR   F 4  253 ? -1.943  -34.231  96.900  1.00 120.22 ? 253 TYR   F CG     1 
ATOM   16245 C  CD1    . TYR   F 4  253 ? -0.892  -33.873  96.069  1.00 118.82 ? 253 TYR   F CD1    1 
ATOM   16246 C  CD2    . TYR   F 4  253 ? -2.787  -35.254  96.490  1.00 125.23 ? 253 TYR   F CD2    1 
ATOM   16247 C  CE1    . TYR   F 4  253 ? -0.642  -34.550  94.902  1.00 125.01 ? 253 TYR   F CE1    1 
ATOM   16248 C  CE2    . TYR   F 4  253 ? -2.555  -35.937  95.312  1.00 129.83 ? 253 TYR   F CE2    1 
ATOM   16249 C  CZ     . TYR   F 4  253 ? -1.476  -35.578  94.520  1.00 130.15 ? 253 TYR   F CZ     1 
ATOM   16250 O  OH     . TYR   F 4  253 ? -1.217  -36.239  93.341  1.00 124.71 ? 253 TYR   F OH     1 
ATOM   16251 N  N      . GLY   F 4  254 ? 1.195   -33.929  99.436  1.00 118.06 ? 254 GLY   F N      1 
ATOM   16252 C  CA     . GLY   F 4  254 ? 2.544   -33.671  98.950  1.00 122.49 ? 254 GLY   F CA     1 
ATOM   16253 C  C      . GLY   F 4  254 ? 3.573   -33.307  100.004 1.00 116.33 ? 254 GLY   F C      1 
ATOM   16254 O  O      . GLY   F 4  254 ? 4.724   -32.979  99.682  1.00 105.71 ? 254 GLY   F O      1 
ATOM   16255 N  N      . ARG   F 4  255 ? 3.168   -33.377  101.272 1.00 115.62 ? 255 ARG   F N      1 
ATOM   16256 C  CA     . ARG   F 4  255 ? 4.037   -33.003  102.381 1.00 119.09 ? 255 ARG   F CA     1 
ATOM   16257 C  C      . ARG   F 4  255 ? 5.340   -33.804  102.366 1.00 120.98 ? 255 ARG   F C      1 
ATOM   16258 O  O      . ARG   F 4  255 ? 6.360   -33.316  101.858 1.00 115.81 ? 255 ARG   F O      1 
ATOM   16259 C  CB     . ARG   F 4  255 ? 3.297   -33.178  103.716 1.00 115.21 ? 255 ARG   F CB     1 
ATOM   16260 C  CG     . ARG   F 4  255 ? 4.136   -32.803  104.934 1.00 117.95 ? 255 ARG   F CG     1 
ATOM   16261 C  CD     . ARG   F 4  255 ? 3.335   -31.991  105.951 1.00 122.82 ? 255 ARG   F CD     1 
ATOM   16262 N  NE     . ARG   F 4  255 ? 3.815   -32.157  107.320 1.00 127.58 ? 255 ARG   F NE     1 
ATOM   16263 C  CZ     . ARG   F 4  255 ? 4.829   -31.482  107.850 1.00 129.06 ? 255 ARG   F CZ     1 
ATOM   16264 N  NH1    . ARG   F 4  255 ? 5.537   -30.621  107.134 1.00 121.34 ? 255 ARG   F NH1    1 
ATOM   16265 N  NH2    . ARG   F 4  255 ? 5.136   -31.671  109.133 1.00 121.74 ? 255 ARG   F NH2    1 
ATOM   16266 N  N      . TYR   F 4  256 ? 5.306   -35.041  102.897 1.00 116.06 ? 256 TYR   F N      1 
ATOM   16267 C  CA     . TYR   F 4  256 ? 6.517   -35.836  103.131 1.00 113.56 ? 256 TYR   F CA     1 
ATOM   16268 C  C      . TYR   F 4  256 ? 7.135   -36.401  101.851 1.00 110.16 ? 256 TYR   F C      1 
ATOM   16269 O  O      . TYR   F 4  256 ? 8.367   -36.452  101.722 1.00 97.30  ? 256 TYR   F O      1 
ATOM   16270 C  CB     . TYR   F 4  256 ? 6.211   -36.972  104.109 1.00 110.91 ? 256 TYR   F CB     1 
ATOM   16271 C  CG     . TYR   F 4  256 ? 5.356   -36.564  105.288 1.00 116.88 ? 256 TYR   F CG     1 
ATOM   16272 C  CD1    . TYR   F 4  256 ? 3.969   -36.593  105.218 1.00 114.85 ? 256 TYR   F CD1    1 
ATOM   16273 C  CD2    . TYR   F 4  256 ? 5.948   -36.169  106.489 1.00 118.75 ? 256 TYR   F CD2    1 
ATOM   16274 C  CE1    . TYR   F 4  256 ? 3.192   -36.230  106.312 1.00 117.52 ? 256 TYR   F CE1    1 
ATOM   16275 C  CE2    . TYR   F 4  256 ? 5.180   -35.802  107.583 1.00 115.42 ? 256 TYR   F CE2    1 
ATOM   16276 C  CZ     . TYR   F 4  256 ? 3.803   -35.834  107.492 1.00 116.48 ? 256 TYR   F CZ     1 
ATOM   16277 O  OH     . TYR   F 4  256 ? 3.035   -35.471  108.579 1.00 110.88 ? 256 TYR   F OH     1 
ATOM   16278 N  N      . GLU   F 4  257 ? 6.309   -36.876  100.921 1.00 113.41 ? 257 GLU   F N      1 
ATOM   16279 C  CA     . GLU   F 4  257 ? 6.793   -37.303  99.618  1.00 108.36 ? 257 GLU   F CA     1 
ATOM   16280 C  C      . GLU   F 4  257 ? 5.818   -36.844  98.541  1.00 111.26 ? 257 GLU   F C      1 
ATOM   16281 O  O      . GLU   F 4  257 ? 4.618   -36.674  98.787  1.00 104.95 ? 257 GLU   F O      1 
ATOM   16282 C  CB     . GLU   F 4  257 ? 7.014   -38.825  99.528  1.00 100.80 ? 257 GLU   F CB     1 
ATOM   16283 C  CG     . GLU   F 4  257 ? 5.801   -39.694  99.792  1.00 99.72  ? 257 GLU   F CG     1 
ATOM   16284 C  CD     . GLU   F 4  257 ? 5.334   -39.635  101.230 1.00 107.94 ? 257 GLU   F CD     1 
ATOM   16285 O  OE1    . GLU   F 4  257 ? 6.111   -40.035  102.129 1.00 103.95 ? 257 GLU   F OE1    1 
ATOM   16286 O  OE2    . GLU   F 4  257 ? 4.188   -39.195  101.466 1.00 113.39 ? 257 GLU   F OE2    1 
ATOM   16287 N  N      . GLU   F 4  258 ? 6.366   -36.645  97.341  1.00 115.03 ? 258 GLU   F N      1 
ATOM   16288 C  CA     . GLU   F 4  258 ? 5.619   -36.071  96.232  1.00 110.95 ? 258 GLU   F CA     1 
ATOM   16289 C  C      . GLU   F 4  258 ? 4.404   -36.914  95.856  1.00 110.66 ? 258 GLU   F C      1 
ATOM   16290 O  O      . GLU   F 4  258 ? 4.523   -38.111  95.571  1.00 105.40 ? 258 GLU   F O      1 
ATOM   16291 C  CB     . GLU   F 4  258 ? 6.525   -35.930  95.022  1.00 94.98  ? 258 GLU   F CB     1 
ATOM   16292 C  CG     . GLU   F 4  258 ? 5.779   -35.358  93.862  1.00 98.84  ? 258 GLU   F CG     1 
ATOM   16293 C  CD     . GLU   F 4  258 ? 6.694   -34.887  92.795  1.00 107.52 ? 258 GLU   F CD     1 
ATOM   16294 O  OE1    . GLU   F 4  258 ? 7.918   -35.085  92.964  1.00 109.11 ? 258 GLU   F OE1    1 
ATOM   16295 O  OE2    . GLU   F 4  258 ? 6.189   -34.338  91.791  1.00 107.62 ? 258 GLU   F OE2    1 
ATOM   16296 N  N      . GLY   F 4  259 ? 3.237   -36.266  95.819  1.00 114.88 ? 259 GLY   F N      1 
ATOM   16297 C  CA     . GLY   F 4  259 ? 2.008   -36.894  95.378  1.00 109.12 ? 259 GLY   F CA     1 
ATOM   16298 C  C      . GLY   F 4  259 ? 1.503   -38.003  96.265  1.00 107.82 ? 259 GLY   F C      1 
ATOM   16299 O  O      . GLY   F 4  259 ? 0.771   -38.874  95.789  1.00 108.90 ? 259 GLY   F O      1 
ATOM   16300 N  N      . ASN   F 4  260 ? 1.862   -37.992  97.549  1.00 104.29 ? 260 ASN   F N      1 
ATOM   16301 C  CA     . ASN   F 4  260 ? 1.546   -39.096  98.458  1.00 107.68 ? 260 ASN   F CA     1 
ATOM   16302 C  C      . ASN   F 4  260 ? 1.973   -40.434  97.857  1.00 106.28 ? 260 ASN   F C      1 
ATOM   16303 O  O      . ASN   F 4  260 ? 1.284   -41.450  97.981  1.00 107.08 ? 260 ASN   F O      1 
ATOM   16304 C  CB     . ASN   F 4  260 ? 0.061   -39.121  98.820  1.00 106.32 ? 260 ASN   F CB     1 
ATOM   16305 C  CG     . ASN   F 4  260 ? -0.337  -37.974  99.714  1.00 106.05 ? 260 ASN   F CG     1 
ATOM   16306 O  OD1    . ASN   F 4  260 ? 0.290   -36.916  99.688  1.00 111.94 ? 260 ASN   F OD1    1 
ATOM   16307 N  ND2    . ASN   F 4  260 ? -1.350  -38.191  100.548 1.00 101.63 ? 260 ASN   F ND2    1 
ATOM   16308 N  N      . GLU   F 4  261 ? 3.125   -40.439  97.197  1.00 98.32  ? 261 GLU   F N      1 
ATOM   16309 C  CA     . GLU   F 4  261 ? 3.652   -41.638  96.567  1.00 95.68  ? 261 GLU   F CA     1 
ATOM   16310 C  C      . GLU   F 4  261 ? 5.106   -41.798  96.970  1.00 95.30  ? 261 GLU   F C      1 
ATOM   16311 O  O      . GLU   F 4  261 ? 5.954   -40.988  96.576  1.00 92.83  ? 261 GLU   F O      1 
ATOM   16312 C  CB     . GLU   F 4  261 ? 3.541   -41.564  95.045  1.00 102.77 ? 261 GLU   F CB     1 
ATOM   16313 C  CG     . GLU   F 4  261 ? 2.137   -41.449  94.495  1.00 102.12 ? 261 GLU   F CG     1 
ATOM   16314 C  CD     . GLU   F 4  261 ? 2.130   -41.522  92.978  1.00 105.72 ? 261 GLU   F CD     1 
ATOM   16315 O  OE1    . GLU   F 4  261 ? 3.223   -41.384  92.364  1.00 88.54  ? 261 GLU   F OE1    1 
ATOM   16316 O  OE2    . GLU   F 4  261 ? 1.032   -41.707  92.406  1.00 115.97 ? 261 GLU   F OE2    1 
ATOM   16317 N  N      . MET   F 4  262 ? 5.394   -42.844  97.739  1.00 90.51  ? 262 MET   F N      1 
ATOM   16318 C  CA     . MET   F 4  262 ? 6.761   -43.245  98.028  1.00 87.81  ? 262 MET   F CA     1 
ATOM   16319 C  C      . MET   F 4  262 ? 7.083   -44.535  97.286  1.00 87.77  ? 262 MET   F C      1 
ATOM   16320 O  O      . MET   F 4  262 ? 6.330   -45.514  97.366  1.00 80.40  ? 262 MET   F O      1 
ATOM   16321 C  CB     . MET   F 4  262 ? 6.987   -43.419  99.527  1.00 89.39  ? 262 MET   F CB     1 
ATOM   16322 C  CG     . MET   F 4  262 ? 8.376   -43.939  99.867  1.00 86.35  ? 262 MET   F CG     1 
ATOM   16323 S  SD     . MET   F 4  262 ? 8.541   -44.127  101.640 1.00 81.96  ? 262 MET   F SD     1 
ATOM   16324 C  CE     . MET   F 4  262 ? 6.969   -44.863  102.047 1.00 77.86  ? 262 MET   F CE     1 
ATOM   16325 N  N      . PHE   F 4  263 ? 8.204   -44.525  96.573  1.00 81.85  ? 263 PHE   F N      1 
ATOM   16326 C  CA     . PHE   F 4  263 ? 8.580   -45.619  95.695  1.00 81.94  ? 263 PHE   F CA     1 
ATOM   16327 C  C      . PHE   F 4  263 ? 9.295   -46.689  96.514  1.00 83.81  ? 263 PHE   F C      1 
ATOM   16328 O  O      . PHE   F 4  263 ? 9.332   -46.633  97.748  1.00 81.88  ? 263 PHE   F O      1 
ATOM   16329 C  CB     . PHE   F 4  263 ? 9.425   -45.077  94.550  1.00 92.64  ? 263 PHE   F CB     1 
ATOM   16330 C  CG     . PHE   F 4  263 ? 8.608   -44.525  93.421  1.00 93.77  ? 263 PHE   F CG     1 
ATOM   16331 C  CD1    . PHE   F 4  263 ? 7.495   -43.739  93.687  1.00 88.96  ? 263 PHE   F CD1    1 
ATOM   16332 C  CD2    . PHE   F 4  263 ? 8.961   -44.763  92.107  1.00 97.46  ? 263 PHE   F CD2    1 
ATOM   16333 C  CE1    . PHE   F 4  263 ? 6.734   -43.218  92.672  1.00 93.27  ? 263 PHE   F CE1    1 
ATOM   16334 C  CE2    . PHE   F 4  263 ? 8.201   -44.249  91.085  1.00 104.62 ? 263 PHE   F CE2    1 
ATOM   16335 C  CZ     . PHE   F 4  263 ? 7.089   -43.467  91.364  1.00 103.11 ? 263 PHE   F CZ     1 
ATOM   16336 N  N      . PHE   F 4  264 ? 9.869   -47.692  95.839  1.00 81.85  ? 264 PHE   F N      1 
ATOM   16337 C  CA     . PHE   F 4  264 ? 10.416  -48.821  96.587  1.00 83.76  ? 264 PHE   F CA     1 
ATOM   16338 C  C      . PHE   F 4  264 ? 11.795  -48.542  97.155  1.00 86.24  ? 264 PHE   F C      1 
ATOM   16339 O  O      . PHE   F 4  264 ? 12.165  -49.131  98.177  1.00 84.59  ? 264 PHE   F O      1 
ATOM   16340 C  CB     . PHE   F 4  264 ? 10.476  -50.081  95.731  1.00 74.29  ? 264 PHE   F CB     1 
ATOM   16341 C  CG     . PHE   F 4  264 ? 9.253   -50.906  95.824  1.00 66.46  ? 264 PHE   F CG     1 
ATOM   16342 C  CD1    . PHE   F 4  264 ? 8.244   -50.544  96.695  1.00 65.21  ? 264 PHE   F CD1    1 
ATOM   16343 C  CD2    . PHE   F 4  264 ? 9.133   -52.073  95.111  1.00 63.16  ? 264 PHE   F CD2    1 
ATOM   16344 C  CE1    . PHE   F 4  264 ? 7.109   -51.293  96.810  1.00 57.37  ? 264 PHE   F CE1    1 
ATOM   16345 C  CE2    . PHE   F 4  264 ? 8.008   -52.837  95.231  1.00 60.56  ? 264 PHE   F CE2    1 
ATOM   16346 C  CZ     . PHE   F 4  264 ? 6.993   -52.445  96.086  1.00 57.28  ? 264 PHE   F CZ     1 
ATOM   16347 N  N      . GLU   F 4  265 ? 12.568  -47.669  96.516  1.00 86.00  ? 265 GLU   F N      1 
ATOM   16348 C  CA     . GLU   F 4  265 ? 13.908  -47.404  97.016  1.00 86.94  ? 265 GLU   F CA     1 
ATOM   16349 C  C      . GLU   F 4  265 ? 13.857  -46.650  98.340  1.00 83.50  ? 265 GLU   F C      1 
ATOM   16350 O  O      . GLU   F 4  265 ? 14.581  -46.987  99.286  1.00 78.27  ? 265 GLU   F O      1 
ATOM   16351 C  CB     . GLU   F 4  265 ? 14.691  -46.649  95.950  1.00 86.53  ? 265 GLU   F CB     1 
ATOM   16352 C  CG     . GLU   F 4  265 ? 15.899  -45.931  96.423  1.00 83.39  ? 265 GLU   F CG     1 
ATOM   16353 C  CD     . GLU   F 4  265 ? 16.566  -45.221  95.283  1.00 100.96 ? 265 GLU   F CD     1 
ATOM   16354 O  OE1    . GLU   F 4  265 ? 16.152  -44.082  94.967  1.00 102.67 ? 265 GLU   F OE1    1 
ATOM   16355 O  OE2    . GLU   F 4  265 ? 17.501  -45.809  94.696  1.00 111.64 ? 265 GLU   F OE2    1 
ATOM   16356 N  N      . GLU   F 4  266 ? 12.976  -45.654  98.437  1.00 84.74  ? 266 GLU   F N      1 
ATOM   16357 C  CA     . GLU   F 4  266 ? 12.836  -44.910  99.684  1.00 87.46  ? 266 GLU   F CA     1 
ATOM   16358 C  C      . GLU   F 4  266 ? 12.337  -45.818  100.805 1.00 84.11  ? 266 GLU   F C      1 
ATOM   16359 O  O      . GLU   F 4  266 ? 12.922  -45.858  101.893 1.00 86.07  ? 266 GLU   F O      1 
ATOM   16360 C  CB     . GLU   F 4  266 ? 11.895  -43.715  99.477  1.00 91.45  ? 266 GLU   F CB     1 
ATOM   16361 C  CG     . GLU   F 4  266 ? 11.622  -42.887  100.734 1.00 92.90  ? 266 GLU   F CG     1 
ATOM   16362 C  CD     . GLU   F 4  266 ? 11.352  -41.412  100.428 1.00 98.93  ? 266 GLU   F CD     1 
ATOM   16363 O  OE1    . GLU   F 4  266 ? 12.210  -40.757  99.791  1.00 102.63 ? 266 GLU   F OE1    1 
ATOM   16364 O  OE2    . GLU   F 4  266 ? 10.293  -40.897  100.842 1.00 99.36  ? 266 GLU   F OE2    1 
ATOM   16365 N  N      . PHE   F 4  267 ? 11.269  -46.582  100.546 1.00 85.72  ? 267 PHE   F N      1 
ATOM   16366 C  CA     . PHE   F 4  267 ? 10.636  -47.387  101.594 1.00 82.49  ? 267 PHE   F CA     1 
ATOM   16367 C  C      . PHE   F 4  267 ? 11.593  -48.449  102.143 1.00 80.70  ? 267 PHE   F C      1 
ATOM   16368 O  O      . PHE   F 4  267 ? 11.619  -48.708  103.352 1.00 75.72  ? 267 PHE   F O      1 
ATOM   16369 C  CB     . PHE   F 4  267 ? 9.356   -48.025  101.036 1.00 79.57  ? 267 PHE   F CB     1 
ATOM   16370 C  CG     . PHE   F 4  267 ? 8.579   -48.837  102.037 1.00 76.68  ? 267 PHE   F CG     1 
ATOM   16371 C  CD1    . PHE   F 4  267 ? 8.282   -48.332  103.288 1.00 83.87  ? 267 PHE   F CD1    1 
ATOM   16372 C  CD2    . PHE   F 4  267 ? 8.130   -50.101  101.722 1.00 76.87  ? 267 PHE   F CD2    1 
ATOM   16373 C  CE1    . PHE   F 4  267 ? 7.549   -49.084  104.212 1.00 85.77  ? 267 PHE   F CE1    1 
ATOM   16374 C  CE2    . PHE   F 4  267 ? 7.403   -50.858  102.643 1.00 77.12  ? 267 PHE   F CE2    1 
ATOM   16375 C  CZ     . PHE   F 4  267 ? 7.111   -50.348  103.884 1.00 77.87  ? 267 PHE   F CZ     1 
ATOM   16376 N  N      . ASN   F 4  268 ? 12.378  -49.083  101.267 1.00 80.26  ? 268 ASN   F N      1 
ATOM   16377 C  CA     . ASN   F 4  268 ? 13.367  -50.063  101.711 1.00 75.82  ? 268 ASN   F CA     1 
ATOM   16378 C  C      . ASN   F 4  268 ? 14.414  -49.433  102.613 1.00 75.14  ? 268 ASN   F C      1 
ATOM   16379 O  O      . ASN   F 4  268 ? 14.815  -50.025  103.624 1.00 70.96  ? 268 ASN   F O      1 
ATOM   16380 C  CB     . ASN   F 4  268 ? 14.033  -50.711  100.501 1.00 75.59  ? 268 ASN   F CB     1 
ATOM   16381 C  CG     . ASN   F 4  268 ? 14.946  -51.854  100.883 1.00 74.50  ? 268 ASN   F CG     1 
ATOM   16382 O  OD1    . ASN   F 4  268 ? 14.502  -52.925  101.317 1.00 70.59  ? 268 ASN   F OD1    1 
ATOM   16383 N  ND2    . ASN   F 4  268 ? 16.249  -51.628  100.723 1.00 71.01  ? 268 ASN   F ND2    1 
ATOM   16384 N  N      . GLN   F 4  269 ? 14.893  -48.247  102.239 1.00 80.57  ? 269 GLN   F N      1 
ATOM   16385 C  CA     . GLN   F 4  269 ? 15.812  -47.506  103.096 1.00 80.39  ? 269 GLN   F CA     1 
ATOM   16386 C  C      . GLN   F 4  269 ? 15.191  -47.244  104.462 1.00 75.22  ? 269 GLN   F C      1 
ATOM   16387 O  O      . GLN   F 4  269 ? 15.808  -47.522  105.497 1.00 73.15  ? 269 GLN   F O      1 
ATOM   16388 C  CB     . GLN   F 4  269 ? 16.208  -46.193  102.417 1.00 79.80  ? 269 GLN   F CB     1 
ATOM   16389 C  CG     . GLN   F 4  269 ? 17.366  -45.501  103.074 1.00 73.55  ? 269 GLN   F CG     1 
ATOM   16390 C  CD     . GLN   F 4  269 ? 18.624  -46.318  102.960 1.00 79.73  ? 269 GLN   F CD     1 
ATOM   16391 O  OE1    . GLN   F 4  269 ? 18.984  -47.041  103.894 1.00 84.72  ? 269 GLN   F OE1    1 
ATOM   16392 N  NE2    . GLN   F 4  269 ? 19.300  -46.228  101.809 1.00 74.06  ? 269 GLN   F NE2    1 
ATOM   16393 N  N      . TYR   F 4  270 ? 13.958  -46.721  104.481 1.00 70.66  ? 270 TYR   F N      1 
ATOM   16394 C  CA     . TYR   F 4  270 ? 13.260  -46.491  105.741 1.00 68.09  ? 270 TYR   F CA     1 
ATOM   16395 C  C      . TYR   F 4  270 ? 13.149  -47.765  106.562 1.00 73.93  ? 270 TYR   F C      1 
ATOM   16396 O  O      . TYR   F 4  270 ? 13.363  -47.746  107.777 1.00 77.04  ? 270 TYR   F O      1 
ATOM   16397 C  CB     . TYR   F 4  270 ? 11.870  -45.940  105.494 1.00 68.56  ? 270 TYR   F CB     1 
ATOM   16398 C  CG     . TYR   F 4  270 ? 11.013  -46.013  106.737 1.00 75.87  ? 270 TYR   F CG     1 
ATOM   16399 C  CD1    . TYR   F 4  270 ? 11.141  -45.066  107.746 1.00 84.10  ? 270 TYR   F CD1    1 
ATOM   16400 C  CD2    . TYR   F 4  270 ? 10.092  -47.036  106.918 1.00 74.08  ? 270 TYR   F CD2    1 
ATOM   16401 C  CE1    . TYR   F 4  270 ? 10.356  -45.118  108.890 1.00 82.84  ? 270 TYR   F CE1    1 
ATOM   16402 C  CE2    . TYR   F 4  270 ? 9.307   -47.098  108.057 1.00 77.20  ? 270 TYR   F CE2    1 
ATOM   16403 C  CZ     . TYR   F 4  270 ? 9.442   -46.133  109.041 1.00 80.70  ? 270 TYR   F CZ     1 
ATOM   16404 O  OH     . TYR   F 4  270 ? 8.665   -46.178  110.176 1.00 81.48  ? 270 TYR   F OH     1 
ATOM   16405 N  N      . LEU   F 4  271 ? 12.766  -48.877  105.923 1.00 82.44  ? 271 LEU   F N      1 
ATOM   16406 C  CA     . LEU   F 4  271 ? 12.673  -50.158  106.628 1.00 79.46  ? 271 LEU   F CA     1 
ATOM   16407 C  C      . LEU   F 4  271 ? 14.011  -50.561  107.233 1.00 73.29  ? 271 LEU   F C      1 
ATOM   16408 O  O      . LEU   F 4  271 ? 14.084  -50.965  108.402 1.00 65.93  ? 271 LEU   F O      1 
ATOM   16409 C  CB     . LEU   F 4  271 ? 12.178  -51.255  105.684 1.00 73.45  ? 271 LEU   F CB     1 
ATOM   16410 C  CG     . LEU   F 4  271 ? 10.696  -51.276  105.362 1.00 70.61  ? 271 LEU   F CG     1 
ATOM   16411 C  CD1    . LEU   F 4  271 ? 10.457  -52.076  104.115 1.00 70.99  ? 271 LEU   F CD1    1 
ATOM   16412 C  CD2    . LEU   F 4  271 ? 9.966   -51.877  106.547 1.00 65.30  ? 271 LEU   F CD2    1 
ATOM   16413 N  N      . MET   F 4  272 ? 15.077  -50.499  106.436 1.00 69.06  ? 272 MET   F N      1 
ATOM   16414 C  CA     . MET   F 4  272 ? 16.393  -50.782  106.980 1.00 72.86  ? 272 MET   F CA     1 
ATOM   16415 C  C      . MET   F 4  272 ? 16.645  -49.926  108.215 1.00 79.85  ? 272 MET   F C      1 
ATOM   16416 O  O      . MET   F 4  272 ? 16.877  -50.451  109.314 1.00 75.36  ? 272 MET   F O      1 
ATOM   16417 C  CB     . MET   F 4  272 ? 17.463  -50.547  105.916 1.00 76.11  ? 272 MET   F CB     1 
ATOM   16418 C  CG     . MET   F 4  272 ? 17.449  -51.559  104.784 1.00 76.16  ? 272 MET   F CG     1 
ATOM   16419 S  SD     . MET   F 4  272 ? 18.848  -51.326  103.664 1.00 86.34  ? 272 MET   F SD     1 
ATOM   16420 C  CE     . MET   F 4  272 ? 19.947  -52.614  104.260 1.00 81.69  ? 272 MET   F CE     1 
ATOM   16421 N  N      . ASP   F 4  273 ? 16.542  -48.593  108.051 1.00 83.93  ? 273 ASP   F N      1 
ATOM   16422 C  CA     . ASP   F 4  273 ? 16.927  -47.644  109.098 1.00 69.70  ? 273 ASP   F CA     1 
ATOM   16423 C  C      . ASP   F 4  273 ? 15.982  -47.705  110.283 1.00 64.65  ? 273 ASP   F C      1 
ATOM   16424 O  O      . ASP   F 4  273 ? 16.426  -47.667  111.432 1.00 77.58  ? 273 ASP   F O      1 
ATOM   16425 C  CB     . ASP   F 4  273 ? 16.961  -46.227  108.539 1.00 65.47  ? 273 ASP   F CB     1 
ATOM   16426 C  CG     . ASP   F 4  273 ? 18.045  -46.034  107.485 1.00 72.65  ? 273 ASP   F CG     1 
ATOM   16427 O  OD1    . ASP   F 4  273 ? 19.052  -46.774  107.498 1.00 71.16  ? 273 ASP   F OD1    1 
ATOM   16428 O  OD2    . ASP   F 4  273 ? 17.894  -45.119  106.646 1.00 76.64  ? 273 ASP   F OD2    1 
ATOM   16429 N  N      . ALA   F 4  274 ? 14.681  -47.797  110.031 1.00 61.09  ? 274 ALA   F N      1 
ATOM   16430 C  CA     . ALA   F 4  274 ? 13.713  -47.821  111.119 1.00 67.15  ? 274 ALA   F CA     1 
ATOM   16431 C  C      . ALA   F 4  274 ? 13.521  -49.207  111.737 1.00 74.46  ? 274 ALA   F C      1 
ATOM   16432 O  O      . ALA   F 4  274 ? 13.448  -49.323  112.966 1.00 77.71  ? 274 ALA   F O      1 
ATOM   16433 C  CB     . ALA   F 4  274 ? 12.361  -47.281  110.645 1.00 71.88  ? 274 ALA   F CB     1 
ATOM   16434 N  N      . LEU   F 4  275 ? 13.424  -50.273  110.935 1.00 75.56  ? 275 LEU   F N      1 
ATOM   16435 C  CA     . LEU   F 4  275 ? 13.124  -51.580  111.502 1.00 72.94  ? 275 LEU   F CA     1 
ATOM   16436 C  C      . LEU   F 4  275 ? 14.237  -52.614  111.358 1.00 71.04  ? 275 LEU   F C      1 
ATOM   16437 O  O      . LEU   F 4  275 ? 14.082  -53.738  111.856 1.00 67.56  ? 275 LEU   F O      1 
ATOM   16438 C  CB     . LEU   F 4  275 ? 11.831  -52.142  110.901 1.00 68.67  ? 275 LEU   F CB     1 
ATOM   16439 C  CG     . LEU   F 4  275 ? 10.580  -51.418  111.380 1.00 57.55  ? 275 LEU   F CG     1 
ATOM   16440 C  CD1    . LEU   F 4  275 ? 9.346   -52.254  111.095 1.00 54.53  ? 275 LEU   F CD1    1 
ATOM   16441 C  CD2    . LEU   F 4  275 ? 10.694  -51.061  112.835 1.00 58.74  ? 275 LEU   F CD2    1 
ATOM   16442 N  N      . ASN   F 4  276 ? 15.349  -52.277  110.710 1.00 67.90  ? 276 ASN   F N      1 
ATOM   16443 C  CA     . ASN   F 4  276 ? 16.481  -53.191  110.661 1.00 71.97  ? 276 ASN   F CA     1 
ATOM   16444 C  C      . ASN   F 4  276 ? 16.204  -54.320  109.670 1.00 76.33  ? 276 ASN   F C      1 
ATOM   16445 O  O      . ASN   F 4  276 ? 16.825  -55.390  109.721 1.00 74.39  ? 276 ASN   F O      1 
ATOM   16446 C  CB     . ASN   F 4  276 ? 16.776  -53.740  112.058 1.00 66.66  ? 276 ASN   F CB     1 
ATOM   16447 C  CG     . ASN   F 4  276 ? 18.177  -54.319  112.178 1.00 72.52  ? 276 ASN   F CG     1 
ATOM   16448 O  OD1    . ASN   F 4  276 ? 19.080  -53.985  111.394 1.00 67.52  ? 276 ASN   F OD1    1 
ATOM   16449 N  ND2    . ASN   F 4  276 ? 18.366  -55.192  113.164 1.00 68.99  ? 276 ASN   F ND2    1 
ATOM   16450 N  N      . THR   F 4  277 ? 15.279  -54.090  108.747 1.00 71.26  ? 277 THR   F N      1 
ATOM   16451 C  CA     . THR   F 4  277 ? 14.971  -55.110  107.757 1.00 66.14  ? 277 THR   F CA     1 
ATOM   16452 C  C      . THR   F 4  277 ? 15.007  -54.554  106.344 1.00 65.79  ? 277 THR   F C      1 
ATOM   16453 O  O      . THR   F 4  277 ? 15.479  -53.437  106.115 1.00 70.13  ? 277 THR   F O      1 
ATOM   16454 C  CB     . THR   F 4  277 ? 13.607  -55.728  108.030 1.00 67.47  ? 277 THR   F CB     1 
ATOM   16455 O  OG1    . THR   F 4  277 ? 13.433  -56.897  107.214 1.00 69.35  ? 277 THR   F OG1    1 
ATOM   16456 C  CG2    . THR   F 4  277 ? 12.511  -54.722  107.734 1.00 68.61  ? 277 THR   F CG2    1 
ATOM   16457 N  N      . THR   F 4  278 ? 14.523  -55.333  105.386 1.00 65.08  ? 278 THR   F N      1 
ATOM   16458 C  CA     . THR   F 4  278 ? 14.523  -54.921  103.996 1.00 66.44  ? 278 THR   F CA     1 
ATOM   16459 C  C      . THR   F 4  278 ? 13.169  -55.215  103.391 1.00 65.49  ? 278 THR   F C      1 
ATOM   16460 O  O      . THR   F 4  278 ? 12.378  -55.997  103.927 1.00 66.05  ? 278 THR   F O      1 
ATOM   16461 C  CB     . THR   F 4  278 ? 15.602  -55.631  103.205 1.00 63.33  ? 278 THR   F CB     1 
ATOM   16462 O  OG1    . THR   F 4  278 ? 15.307  -57.030  103.170 1.00 60.73  ? 278 THR   F OG1    1 
ATOM   16463 C  CG2    . THR   F 4  278 ? 16.925  -55.413  103.878 1.00 63.49  ? 278 THR   F CG2    1 
ATOM   16464 N  N      . LEU   F 4  279 ? 12.922  -54.579  102.250 1.00 64.20  ? 279 LEU   F N      1 
ATOM   16465 C  CA     . LEU   F 4  279 ? 11.620  -54.724  101.615 1.00 68.48  ? 279 LEU   F CA     1 
ATOM   16466 C  C      . LEU   F 4  279 ? 11.418  -56.135  101.081 1.00 67.00  ? 279 LEU   F C      1 
ATOM   16467 O  O      . LEU   F 4  279 ? 10.324  -56.701  101.228 1.00 62.85  ? 279 LEU   F O      1 
ATOM   16468 C  CB     . LEU   F 4  279 ? 11.452  -53.671  100.525 1.00 64.48  ? 279 LEU   F CB     1 
ATOM   16469 C  CG     . LEU   F 4  279 ? 10.192  -53.746  99.683  1.00 60.87  ? 279 LEU   F CG     1 
ATOM   16470 C  CD1    . LEU   F 4  279 ? 8.934   -53.716  100.531 1.00 62.57  ? 279 LEU   F CD1    1 
ATOM   16471 C  CD2    . LEU   F 4  279 ? 10.235  -52.550  98.781  1.00 63.86  ? 279 LEU   F CD2    1 
ATOM   16472 N  N      . GLU   F 4  280 ? 12.466  -56.728  100.494 1.00 65.65  ? 280 GLU   F N      1 
ATOM   16473 C  CA     . GLU   F 4  280 ? 12.409  -58.124  100.065 1.00 64.90  ? 280 GLU   F CA     1 
ATOM   16474 C  C      . GLU   F 4  280 ? 11.940  -59.034  101.198 1.00 63.30  ? 280 GLU   F C      1 
ATOM   16475 O  O      . GLU   F 4  280 ? 10.892  -59.676  101.092 1.00 67.05  ? 280 GLU   F O      1 
ATOM   16476 C  CB     . GLU   F 4  280 ? 13.777  -58.577  99.535  1.00 71.29  ? 280 GLU   F CB     1 
ATOM   16477 C  CG     . GLU   F 4  280 ? 13.788  -59.990  98.942  1.00 72.22  ? 280 GLU   F CG     1 
ATOM   16478 C  CD     . GLU   F 4  280 ? 12.869  -60.154  97.725  1.00 80.04  ? 280 GLU   F CD     1 
ATOM   16479 O  OE1    . GLU   F 4  280 ? 12.765  -59.218  96.887  1.00 77.94  ? 280 GLU   F OE1    1 
ATOM   16480 O  OE2    . GLU   F 4  280 ? 12.220  -61.220  97.632  1.00 74.82  ? 280 GLU   F OE2    1 
ATOM   16481 N  N      . ASN   F 4  281 ? 12.689  -59.087  102.309 1.00 61.38  ? 281 ASN   F N      1 
ATOM   16482 C  CA     . ASN   F 4  281 ? 12.408  -60.103  103.322 1.00 58.47  ? 281 ASN   F CA     1 
ATOM   16483 C  C      . ASN   F 4  281 ? 11.092  -59.843  104.036 1.00 61.06  ? 281 ASN   F C      1 
ATOM   16484 O  O      . ASN   F 4  281 ? 10.261  -60.750  104.183 1.00 63.31  ? 281 ASN   F O      1 
ATOM   16485 C  CB     . ASN   F 4  281 ? 13.538  -60.190  104.341 1.00 56.98  ? 281 ASN   F CB     1 
ATOM   16486 C  CG     . ASN   F 4  281 ? 14.867  -60.542  103.715 1.00 58.81  ? 281 ASN   F CG     1 
ATOM   16487 O  OD1    . ASN   F 4  281 ? 15.128  -60.239  102.547 1.00 62.38  ? 281 ASN   F OD1    1 
ATOM   16488 N  ND2    . ASN   F 4  281 ? 15.705  -61.231  104.479 1.00 51.98  ? 281 ASN   F ND2    1 
ATOM   16489 N  N      . SER   F 4  282 ? 10.888  -58.615  104.504 1.00 65.88  ? 282 SER   F N      1 
ATOM   16490 C  CA     . SER   F 4  282 ? 9.769   -58.343  105.406 1.00 72.64  ? 282 SER   F CA     1 
ATOM   16491 C  C      . SER   F 4  282 ? 8.416   -58.302  104.696 1.00 69.25  ? 282 SER   F C      1 
ATOM   16492 O  O      . SER   F 4  282 ? 7.386   -58.579  105.332 1.00 58.82  ? 282 SER   F O      1 
ATOM   16493 C  CB     . SER   F 4  282 ? 10.028  -57.030  106.149 1.00 65.04  ? 282 SER   F CB     1 
ATOM   16494 O  OG     . SER   F 4  282 ? 10.477  -56.038  105.239 1.00 64.55  ? 282 SER   F OG     1 
ATOM   16495 N  N      . ILE   F 4  283 ? 8.400   -57.993  103.391 1.00 64.35  ? 283 ILE   F N      1 
ATOM   16496 C  CA     . ILE   F 4  283 ? 7.148   -57.697  102.701 1.00 69.73  ? 283 ILE   F CA     1 
ATOM   16497 C  C      . ILE   F 4  283 ? 7.072   -58.366  101.329 1.00 63.61  ? 283 ILE   F C      1 
ATOM   16498 O  O      . ILE   F 4  283 ? 6.033   -58.923  100.959 1.00 58.36  ? 283 ILE   F O      1 
ATOM   16499 C  CB     . ILE   F 4  283 ? 6.960   -56.173  102.568 1.00 74.42  ? 283 ILE   F CB     1 
ATOM   16500 C  CG1    . ILE   F 4  283 ? 6.713   -55.544  103.945 1.00 71.83  ? 283 ILE   F CG1    1 
ATOM   16501 C  CG2    . ILE   F 4  283 ? 5.777   -55.849  101.653 1.00 73.04  ? 283 ILE   F CG2    1 
ATOM   16502 C  CD1    . ILE   F 4  283 ? 6.631   -54.017  103.927 1.00 68.42  ? 283 ILE   F CD1    1 
ATOM   16503 N  N      . LEU   F 4  284 ? 8.157   -58.310  100.555 1.00 59.12  ? 284 LEU   F N      1 
ATOM   16504 C  CA     . LEU   F 4  284 ? 8.046   -58.677  99.146  1.00 56.82  ? 284 LEU   F CA     1 
ATOM   16505 C  C      . LEU   F 4  284 ? 7.794   -60.167  98.967  1.00 56.02  ? 284 LEU   F C      1 
ATOM   16506 O  O      . LEU   F 4  284 ? 6.956   -60.558  98.147  1.00 59.57  ? 284 LEU   F O      1 
ATOM   16507 C  CB     . LEU   F 4  284 ? 9.294   -58.253  98.379  1.00 63.47  ? 284 LEU   F CB     1 
ATOM   16508 C  CG     . LEU   F 4  284 ? 8.907   -57.607  97.050  1.00 56.35  ? 284 LEU   F CG     1 
ATOM   16509 C  CD1    . LEU   F 4  284 ? 7.914   -56.509  97.316  1.00 53.93  ? 284 LEU   F CD1    1 
ATOM   16510 C  CD2    . LEU   F 4  284 ? 10.111  -57.070  96.365  1.00 66.34  ? 284 LEU   F CD2    1 
ATOM   16511 N  N      . LEU   F 4  285 ? 8.513   -61.015  99.703  1.00 55.25  ? 285 LEU   F N      1 
ATOM   16512 C  CA     . LEU   F 4  285 ? 8.200   -62.441  99.708  1.00 58.60  ? 285 LEU   F CA     1 
ATOM   16513 C  C      . LEU   F 4  285 ? 6.691   -62.669  99.707  1.00 54.53  ? 285 LEU   F C      1 
ATOM   16514 O  O      . LEU   F 4  285 ? 6.123   -63.166  98.736  1.00 56.10  ? 285 LEU   F O      1 
ATOM   16515 C  CB     . LEU   F 4  285 ? 8.833   -63.131  100.928 1.00 60.30  ? 285 LEU   F CB     1 
ATOM   16516 C  CG     . LEU   F 4  285 ? 10.327  -63.475  100.947 1.00 55.48  ? 285 LEU   F CG     1 
ATOM   16517 C  CD1    . LEU   F 4  285 ? 10.565  -64.652  101.866 1.00 54.59  ? 285 LEU   F CD1    1 
ATOM   16518 C  CD2    . LEU   F 4  285 ? 10.913  -63.707  99.552  1.00 54.50  ? 285 LEU   F CD2    1 
ATOM   16519 N  N      . GLN   F 4  286 ? 6.026   -62.268  100.788 1.00 51.94  ? 286 GLN   F N      1 
ATOM   16520 C  CA     . GLN   F 4  286 ? 4.600   -62.522  100.941 1.00 54.54  ? 286 GLN   F CA     1 
ATOM   16521 C  C      . GLN   F 4  286 ? 3.800   -62.023  99.742  1.00 55.40  ? 286 GLN   F C      1 
ATOM   16522 O  O      . GLN   F 4  286 ? 2.768   -62.604  99.373  1.00 49.54  ? 286 GLN   F O      1 
ATOM   16523 C  CB     . GLN   F 4  286 ? 4.107   -61.816  102.193 1.00 62.08  ? 286 GLN   F CB     1 
ATOM   16524 C  CG     . GLN   F 4  286 ? 5.014   -61.933  103.378 1.00 62.63  ? 286 GLN   F CG     1 
ATOM   16525 C  CD     . GLN   F 4  286 ? 4.364   -61.391  104.617 1.00 62.38  ? 286 GLN   F CD     1 
ATOM   16526 O  OE1    . GLN   F 4  286 ? 3.162   -61.592  104.845 1.00 54.77  ? 286 GLN   F OE1    1 
ATOM   16527 N  NE2    . GLN   F 4  286 ? 5.132   -60.626  105.390 1.00 62.99  ? 286 GLN   F NE2    1 
ATOM   16528 N  N      . ILE   F 4  287 ? 4.226   -60.903  99.164  1.00 55.28  ? 287 ILE   F N      1 
ATOM   16529 C  CA     . ILE   F 4  287 ? 3.523   -60.358  98.013  1.00 58.80  ? 287 ILE   F CA     1 
ATOM   16530 C  C      . ILE   F 4  287 ? 3.682   -61.299  96.840  1.00 57.17  ? 287 ILE   F C      1 
ATOM   16531 O  O      . ILE   F 4  287 ? 2.738   -61.558  96.083  1.00 56.15  ? 287 ILE   F O      1 
ATOM   16532 C  CB     . ILE   F 4  287 ? 4.069   -58.962  97.684  1.00 58.65  ? 287 ILE   F CB     1 
ATOM   16533 C  CG1    . ILE   F 4  287 ? 3.534   -57.963  98.695  1.00 61.64  ? 287 ILE   F CG1    1 
ATOM   16534 C  CG2    . ILE   F 4  287 ? 3.635   -58.549  96.290  1.00 53.13  ? 287 ILE   F CG2    1 
ATOM   16535 C  CD1    . ILE   F 4  287 ? 4.180   -56.625  98.604  1.00 60.89  ? 287 ILE   F CD1    1 
ATOM   16536 N  N      . LYS   F 4  288 ? 4.881   -61.843  96.689  1.00 51.23  ? 288 LYS   F N      1 
ATOM   16537 C  CA     . LYS   F 4  288 ? 5.117   -62.780  95.615  1.00 51.94  ? 288 LYS   F CA     1 
ATOM   16538 C  C      . LYS   F 4  288 ? 4.376   -64.085  95.871  1.00 51.65  ? 288 LYS   F C      1 
ATOM   16539 O  O      . LYS   F 4  288 ? 3.993   -64.769  94.917  1.00 57.77  ? 288 LYS   F O      1 
ATOM   16540 C  CB     . LYS   F 4  288 ? 6.621   -62.985  95.449  1.00 51.21  ? 288 LYS   F CB     1 
ATOM   16541 C  CG     . LYS   F 4  288 ? 7.250   -61.845  94.668  1.00 45.62  ? 288 LYS   F CG     1 
ATOM   16542 C  CD     . LYS   F 4  288 ? 8.726   -61.989  94.515  1.00 47.03  ? 288 LYS   F CD     1 
ATOM   16543 C  CE     . LYS   F 4  288 ? 9.438   -62.102  95.832  1.00 55.86  ? 288 LYS   F CE     1 
ATOM   16544 N  NZ     . LYS   F 4  288 ? 10.886  -62.325  95.541  1.00 65.51  ? 288 LYS   F NZ     1 
ATOM   16545 N  N      . HIS   F 4  289 ? 4.138   -64.433  97.142  1.00 50.26  ? 289 HIS   F N      1 
ATOM   16546 C  CA     . HIS   F 4  289 ? 3.333   -65.609  97.461  1.00 55.11  ? 289 HIS   F CA     1 
ATOM   16547 C  C      . HIS   F 4  289 ? 1.880   -65.382  97.048  1.00 57.28  ? 289 HIS   F C      1 
ATOM   16548 O  O      . HIS   F 4  289 ? 1.246   -66.246  96.425  1.00 48.98  ? 289 HIS   F O      1 
ATOM   16549 C  CB     . HIS   F 4  289 ? 3.379   -65.900  98.958  1.00 46.26  ? 289 HIS   F CB     1 
ATOM   16550 C  CG     . HIS   F 4  289 ? 2.481   -67.023  99.378  1.00 48.59  ? 289 HIS   F CG     1 
ATOM   16551 N  ND1    . HIS   F 4  289 ? 2.562   -68.280  98.820  1.00 53.09  ? 289 HIS   F ND1    1 
ATOM   16552 C  CD2    . HIS   F 4  289 ? 1.401   -67.048  100.197 1.00 54.77  ? 289 HIS   F CD2    1 
ATOM   16553 C  CE1    . HIS   F 4  289 ? 1.632   -69.056  99.346  1.00 51.50  ? 289 HIS   F CE1    1 
ATOM   16554 N  NE2    . HIS   F 4  289 ? 0.902   -68.329  100.171 1.00 51.30  ? 289 HIS   F NE2    1 
ATOM   16555 N  N      . ILE   F 4  290 ? 1.341   -64.210  97.401  1.00 61.25  ? 290 ILE   F N      1 
ATOM   16556 C  CA     . ILE   F 4  290 ? -0.059  -63.893  97.121  1.00 61.49  ? 290 ILE   F CA     1 
ATOM   16557 C  C      . ILE   F 4  290 ? -0.297  -63.802  95.620  1.00 55.65  ? 290 ILE   F C      1 
ATOM   16558 O  O      . ILE   F 4  290 ? -1.241  -64.393  95.086  1.00 55.05  ? 290 ILE   F O      1 
ATOM   16559 C  CB     . ILE   F 4  290 ? -0.460  -62.589  97.832  1.00 62.91  ? 290 ILE   F CB     1 
ATOM   16560 C  CG1    . ILE   F 4  290 ? -0.215  -62.740  99.324  1.00 61.07  ? 290 ILE   F CG1    1 
ATOM   16561 C  CG2    . ILE   F 4  290 ? -1.928  -62.232  97.515  1.00 61.90  ? 290 ILE   F CG2    1 
ATOM   16562 C  CD1    . ILE   F 4  290 ? -0.383  -61.486  100.094 1.00 70.17  ? 290 ILE   F CD1    1 
ATOM   16563 N  N      . ILE   F 4  291 ? 0.540   -63.041  94.919  1.00 53.39  ? 291 ILE   F N      1 
ATOM   16564 C  CA     . ILE   F 4  291 ? 0.370   -62.924  93.478  1.00 53.73  ? 291 ILE   F CA     1 
ATOM   16565 C  C      . ILE   F 4  291 ? 0.427   -64.298  92.825  1.00 52.42  ? 291 ILE   F C      1 
ATOM   16566 O  O      . ILE   F 4  291 ? -0.464  -64.672  92.055  1.00 52.93  ? 291 ILE   F O      1 
ATOM   16567 C  CB     . ILE   F 4  291 ? 1.408   -61.960  92.889  1.00 53.31  ? 291 ILE   F CB     1 
ATOM   16568 C  CG1    . ILE   F 4  291 ? 1.230   -60.568  93.479  1.00 50.29  ? 291 ILE   F CG1    1 
ATOM   16569 C  CG2    . ILE   F 4  291 ? 1.334   -61.948  91.395  1.00 51.28  ? 291 ILE   F CG2    1 
ATOM   16570 C  CD1    . ILE   F 4  291 ? 2.344   -59.650  93.069  1.00 56.17  ? 291 ILE   F CD1    1 
ATOM   16571 N  N      . ARG   F 4  292 ? 1.459   -65.084  93.138  1.00 54.93  ? 292 ARG   F N      1 
ATOM   16572 C  CA     . ARG   F 4  292 ? 1.532   -66.430  92.575  1.00 52.10  ? 292 ARG   F CA     1 
ATOM   16573 C  C      . ARG   F 4  292 ? 0.270   -67.212  92.923  1.00 50.75  ? 292 ARG   F C      1 
ATOM   16574 O  O      . ARG   F 4  292 ? -0.335  -67.854  92.063  1.00 55.75  ? 292 ARG   F O      1 
ATOM   16575 C  CB     . ARG   F 4  292 ? 2.785   -67.143  93.090  1.00 53.14  ? 292 ARG   F CB     1 
ATOM   16576 C  CG     . ARG   F 4  292 ? 3.288   -68.336  92.269  1.00 64.62  ? 292 ARG   F CG     1 
ATOM   16577 C  CD     . ARG   F 4  292 ? 4.533   -68.957  92.944  1.00 66.34  ? 292 ARG   F CD     1 
ATOM   16578 N  NE     . ARG   F 4  292 ? 5.726   -68.140  92.713  1.00 75.76  ? 292 ARG   F NE     1 
ATOM   16579 C  CZ     . ARG   F 4  292 ? 6.416   -67.519  93.668  1.00 71.78  ? 292 ARG   F CZ     1 
ATOM   16580 N  NH1    . ARG   F 4  292 ? 6.109   -67.667  94.944  1.00 72.15  ? 292 ARG   F NH1    1 
ATOM   16581 N  NH2    . ARG   F 4  292 ? 7.450   -66.744  93.335  1.00 62.28  ? 292 ARG   F NH2    1 
ATOM   16582 N  N      . SER   F 4  293 ? -0.190  -67.105  94.168  1.00 51.02  ? 293 SER   F N      1 
ATOM   16583 C  CA     . SER   F 4  293 ? -1.314  -67.917  94.621  1.00 45.18  ? 293 SER   F CA     1 
ATOM   16584 C  C      . SER   F 4  293 ? -2.602  -67.537  93.916  1.00 49.58  ? 293 SER   F C      1 
ATOM   16585 O  O      . SER   F 4  293 ? -3.299  -68.403  93.379  1.00 53.67  ? 293 SER   F O      1 
ATOM   16586 C  CB     . SER   F 4  293 ? -1.481  -67.770  96.124  1.00 52.34  ? 293 SER   F CB     1 
ATOM   16587 O  OG     . SER   F 4  293 ? -0.343  -68.286  96.779  1.00 60.14  ? 293 SER   F OG     1 
ATOM   16588 N  N      . CYS   F 4  294 ? -2.965  -66.250  93.948  1.00 52.55  ? 294 CYS   F N      1 
ATOM   16589 C  CA     . CYS   F 4  294 ? -4.214  -65.834  93.313  1.00 51.65  ? 294 CYS   F CA     1 
ATOM   16590 C  C      . CYS   F 4  294 ? -4.250  -66.241  91.851  1.00 55.51  ? 294 CYS   F C      1 
ATOM   16591 O  O      . CYS   F 4  294 ? -5.278  -66.724  91.358  1.00 56.59  ? 294 CYS   F O      1 
ATOM   16592 C  CB     . CYS   F 4  294 ? -4.428  -64.320  93.433  1.00 49.50  ? 294 CYS   F CB     1 
ATOM   16593 S  SG     . CYS   F 4  294 ? -4.801  -63.684  95.097  1.00 66.19  ? 294 CYS   F SG     1 
ATOM   16594 N  N      . LEU   F 4  295 ? -3.139  -66.048  91.140  1.00 54.68  ? 295 LEU   F N      1 
ATOM   16595 C  CA     . LEU   F 4  295 ? -3.153  -66.302  89.710  1.00 53.66  ? 295 LEU   F CA     1 
ATOM   16596 C  C      . LEU   F 4  295 ? -3.054  -67.791  89.412  1.00 53.46  ? 295 LEU   F C      1 
ATOM   16597 O  O      . LEU   F 4  295 ? -3.742  -68.277  88.506  1.00 54.54  ? 295 LEU   F O      1 
ATOM   16598 C  CB     . LEU   F 4  295 ? -2.040  -65.506  89.007  1.00 51.00  ? 295 LEU   F CB     1 
ATOM   16599 C  CG     . LEU   F 4  295 ? -2.338  -63.987  88.972  1.00 44.05  ? 295 LEU   F CG     1 
ATOM   16600 C  CD1    . LEU   F 4  295 ? -1.150  -63.098  88.530  1.00 39.82  ? 295 LEU   F CD1    1 
ATOM   16601 C  CD2    . LEU   F 4  295 ? -3.640  -63.644  88.243  1.00 43.17  ? 295 LEU   F CD2    1 
ATOM   16602 N  N      . MET   F 4  296 ? -2.231  -68.539  90.168  1.00 48.77  ? 296 MET   F N      1 
ATOM   16603 C  CA     . MET   F 4  296 ? -2.188  -69.984  89.955  1.00 51.47  ? 296 MET   F CA     1 
ATOM   16604 C  C      . MET   F 4  296 ? -3.552  -70.613  90.206  1.00 57.54  ? 296 MET   F C      1 
ATOM   16605 O  O      . MET   F 4  296 ? -3.883  -71.635  89.594  1.00 58.07  ? 296 MET   F O      1 
ATOM   16606 C  CB     . MET   F 4  296 ? -1.140  -70.675  90.833  1.00 46.22  ? 296 MET   F CB     1 
ATOM   16607 C  CG     . MET   F 4  296 ? 0.297   -70.361  90.503  1.00 51.04  ? 296 MET   F CG     1 
ATOM   16608 S  SD     . MET   F 4  296 ? 0.429   -69.984  88.741  1.00 82.59  ? 296 MET   F SD     1 
ATOM   16609 C  CE     . MET   F 4  296 ? 0.681   -71.600  87.989  1.00 80.99  ? 296 MET   F CE     1 
ATOM   16610 N  N      . CYS   F 4  297 ? -4.361  -70.008  91.084  1.00 56.36  ? 297 CYS   F N      1 
ATOM   16611 C  CA     . CYS   F 4  297 ? -5.697  -70.523  91.365  1.00 56.70  ? 297 CYS   F CA     1 
ATOM   16612 C  C      . CYS   F 4  297 ? -6.552  -70.555  90.103  1.00 55.00  ? 297 CYS   F C      1 
ATOM   16613 O  O      . CYS   F 4  297 ? -6.974  -71.624  89.646  1.00 57.41  ? 297 CYS   F O      1 
ATOM   16614 C  CB     . CYS   F 4  297 ? -6.372  -69.670  92.443  1.00 57.06  ? 297 CYS   F CB     1 
ATOM   16615 S  SG     . CYS   F 4  297 ? -7.966  -70.323  92.975  1.00 62.56  ? 297 CYS   F SG     1 
ATOM   16616 N  N      . ILE   F 4  298 ? -6.805  -69.385  89.514  1.00 54.22  ? 298 ILE   F N      1 
ATOM   16617 C  CA     . ILE   F 4  298 ? -7.761  -69.245  88.419  1.00 51.32  ? 298 ILE   F CA     1 
ATOM   16618 C  C      . ILE   F 4  298 ? -7.167  -69.667  87.081  1.00 54.69  ? 298 ILE   F C      1 
ATOM   16619 O  O      . ILE   F 4  298 ? -7.785  -69.447  86.031  1.00 54.39  ? 298 ILE   F O      1 
ATOM   16620 C  CB     . ILE   F 4  298 ? -8.269  -67.796  88.315  1.00 51.55  ? 298 ILE   F CB     1 
ATOM   16621 C  CG1    . ILE   F 4  298 ? -7.125  -66.836  87.991  1.00 52.32  ? 298 ILE   F CG1    1 
ATOM   16622 C  CG2    . ILE   F 4  298 ? -8.891  -67.368  89.616  1.00 59.30  ? 298 ILE   F CG2    1 
ATOM   16623 C  CD1    . ILE   F 4  298 ? -7.570  -65.574  87.285  1.00 44.24  ? 298 ILE   F CD1    1 
ATOM   16624 N  N      . GLU   F 4  299 ? -5.967  -70.254  87.088  1.00 54.12  ? 299 GLU   F N      1 
ATOM   16625 C  CA     . GLU   F 4  299 ? -5.312  -70.545  85.815  1.00 52.01  ? 299 GLU   F CA     1 
ATOM   16626 C  C      . GLU   F 4  299 ? -6.142  -71.462  84.923  1.00 53.80  ? 299 GLU   F C      1 
ATOM   16627 O  O      . GLU   F 4  299 ? -6.356  -71.126  83.746  1.00 52.37  ? 299 GLU   F O      1 
ATOM   16628 C  CB     . GLU   F 4  299 ? -3.930  -71.140  86.060  1.00 45.63  ? 299 GLU   F CB     1 
ATOM   16629 C  CG     . GLU   F 4  299 ? -3.407  -71.818  84.821  1.00 47.77  ? 299 GLU   F CG     1 
ATOM   16630 C  CD     . GLU   F 4  299 ? -1.906  -71.802  84.773  1.00 58.94  ? 299 GLU   F CD     1 
ATOM   16631 O  OE1    . GLU   F 4  299 ? -1.305  -71.218  85.697  1.00 63.72  ? 299 GLU   F OE1    1 
ATOM   16632 O  OE2    . GLU   F 4  299 ? -1.316  -72.316  83.795  1.00 57.78  ? 299 GLU   F OE2    1 
ATOM   16633 N  N      . PRO   F 4  300 ? -6.639  -72.603  85.393  1.00 54.56  ? 300 PRO   F N      1 
ATOM   16634 C  CA     . PRO   F 4  300 ? -7.428  -73.474  84.510  1.00 55.08  ? 300 PRO   F CA     1 
ATOM   16635 C  C      . PRO   F 4  300 ? -8.626  -72.780  83.903  1.00 53.82  ? 300 PRO   F C      1 
ATOM   16636 O  O      . PRO   F 4  300 ? -9.124  -73.223  82.861  1.00 59.49  ? 300 PRO   F O      1 
ATOM   16637 C  CB     . PRO   F 4  300 ? -7.872  -74.609  85.445  1.00 49.98  ? 300 PRO   F CB     1 
ATOM   16638 C  CG     . PRO   F 4  300 ? -6.876  -74.614  86.511  1.00 54.00  ? 300 PRO   F CG     1 
ATOM   16639 C  CD     . PRO   F 4  300 ? -6.520  -73.167  86.742  1.00 53.19  ? 300 PRO   F CD     1 
ATOM   16640 N  N      . ALA   F 4  301 ? -9.123  -71.723  84.529  1.00 48.25  ? 301 ALA   F N      1 
ATOM   16641 C  CA     . ALA   F 4  301 ? -10.338 -71.088  84.067  1.00 44.99  ? 301 ALA   F CA     1 
ATOM   16642 C  C      . ALA   F 4  301 ? -10.082 -69.984  83.049  1.00 52.65  ? 301 ALA   F C      1 
ATOM   16643 O  O      . ALA   F 4  301 ? -11.027 -69.558  82.375  1.00 51.98  ? 301 ALA   F O      1 
ATOM   16644 C  CB     . ALA   F 4  301 ? -11.111 -70.530  85.258  1.00 41.11  ? 301 ALA   F CB     1 
ATOM   16645 N  N      . ILE   F 4  302 ? -8.841  -69.516  82.897  1.00 49.80  ? 302 ILE   F N      1 
ATOM   16646 C  CA     . ILE   F 4  302 ? -8.628  -68.391  82.002  1.00 44.89  ? 302 ILE   F CA     1 
ATOM   16647 C  C      . ILE   F 4  302 ? -7.466  -68.651  81.056  1.00 45.22  ? 302 ILE   F C      1 
ATOM   16648 O  O      . ILE   F 4  302 ? -7.188  -67.845  80.162  1.00 49.36  ? 302 ILE   F O      1 
ATOM   16649 C  CB     . ILE   F 4  302 ? -8.384  -67.103  82.793  1.00 46.14  ? 302 ILE   F CB     1 
ATOM   16650 C  CG1    . ILE   F 4  302 ? -7.082  -67.187  83.549  1.00 47.02  ? 302 ILE   F CG1    1 
ATOM   16651 C  CG2    . ILE   F 4  302 ? -9.406  -66.970  83.866  1.00 49.51  ? 302 ILE   F CG2    1 
ATOM   16652 C  CD1    . ILE   F 4  302 ? -6.646  -65.867  84.075  1.00 42.61  ? 302 ILE   F CD1    1 
ATOM   16653 N  N      . SER   F 4  303 ? -6.760  -69.754  81.242  1.00 45.16  ? 303 SER   F N      1 
ATOM   16654 C  CA     . SER   F 4  303 ? -5.568  -69.986  80.437  1.00 48.97  ? 303 SER   F CA     1 
ATOM   16655 C  C      . SER   F 4  303 ? -5.932  -70.073  78.955  1.00 56.14  ? 303 SER   F C      1 
ATOM   16656 O  O      . SER   F 4  303 ? -6.814  -70.850  78.570  1.00 56.18  ? 303 SER   F O      1 
ATOM   16657 C  CB     . SER   F 4  303 ? -4.876  -71.264  80.897  1.00 48.16  ? 303 SER   F CB     1 
ATOM   16658 O  OG     . SER   F 4  303 ? -3.774  -71.582  80.068  1.00 53.27  ? 303 SER   F OG     1 
ATOM   16659 N  N      . THR   F 4  304 ? -5.266  -69.265  78.121  1.00 52.87  ? 304 THR   F N      1 
ATOM   16660 C  CA     . THR   F 4  304 ? -5.456  -69.330  76.668  1.00 53.23  ? 304 THR   F CA     1 
ATOM   16661 C  C      . THR   F 4  304 ? -4.365  -70.165  75.977  1.00 58.57  ? 304 THR   F C      1 
ATOM   16662 O  O      . THR   F 4  304 ? -3.869  -69.814  74.900  1.00 62.60  ? 304 THR   F O      1 
ATOM   16663 C  CB     . THR   F 4  304 ? -5.551  -67.922  76.063  1.00 48.78  ? 304 THR   F CB     1 
ATOM   16664 O  OG1    . THR   F 4  304 ? -4.283  -67.259  76.106  1.00 51.82  ? 304 THR   F OG1    1 
ATOM   16665 C  CG2    . THR   F 4  304 ? -6.552  -67.087  76.798  1.00 42.06  ? 304 THR   F CG2    1 
ATOM   16666 N  N      . LYS   F 4  305 ? -4.001  -71.309  76.570  1.00 58.36  ? 305 LYS   F N      1 
ATOM   16667 C  CA     . LYS   F 4  305 ? -2.892  -72.124  76.070  1.00 63.07  ? 305 LYS   F CA     1 
ATOM   16668 C  C      . LYS   F 4  305 ? -3.252  -72.845  74.780  1.00 59.65  ? 305 LYS   F C      1 
ATOM   16669 O  O      . LYS   F 4  305 ? -2.467  -72.865  73.829  1.00 59.24  ? 305 LYS   F O      1 
ATOM   16670 C  CB     . LYS   F 4  305 ? -2.474  -73.140  77.138  1.00 67.17  ? 305 LYS   F CB     1 
ATOM   16671 C  CG     . LYS   F 4  305 ? -1.246  -73.974  76.801  1.00 66.35  ? 305 LYS   F CG     1 
ATOM   16672 C  CD     . LYS   F 4  305 ? -0.717  -74.726  78.026  1.00 84.43  ? 305 LYS   F CD     1 
ATOM   16673 C  CE     . LYS   F 4  305 ? -1.215  -76.174  78.134  1.00 95.91  ? 305 LYS   F CE     1 
ATOM   16674 N  NZ     . LYS   F 4  305 ? -0.487  -76.946  79.203  1.00 90.80  ? 305 LYS   F NZ     1 
ATOM   16675 N  N      . HIS   F 4  306 ? -4.410  -73.485  74.742  1.00 59.93  ? 306 HIS   F N      1 
ATOM   16676 C  CA     . HIS   F 4  306 ? -4.812  -74.225  73.561  1.00 66.30  ? 306 HIS   F CA     1 
ATOM   16677 C  C      . HIS   F 4  306 ? -5.962  -73.539  72.830  1.00 63.60  ? 306 HIS   F C      1 
ATOM   16678 O  O      . HIS   F 4  306 ? -6.667  -74.176  72.045  1.00 65.39  ? 306 HIS   F O      1 
ATOM   16679 C  CB     . HIS   F 4  306 ? -5.187  -75.651  73.948  1.00 77.51  ? 306 HIS   F CB     1 
ATOM   16680 C  CG     . HIS   F 4  306 ? -4.082  -76.397  74.633  1.00 87.83  ? 306 HIS   F CG     1 
ATOM   16681 N  ND1    . HIS   F 4  306 ? -2.844  -76.596  74.052  1.00 86.68  ? 306 HIS   F ND1    1 
ATOM   16682 C  CD2    . HIS   F 4  306 ? -4.045  -77.032  75.832  1.00 88.83  ? 306 HIS   F CD2    1 
ATOM   16683 C  CE1    . HIS   F 4  306 ? -2.082  -77.295  74.879  1.00 88.04  ? 306 HIS   F CE1    1 
ATOM   16684 N  NE2    . HIS   F 4  306 ? -2.788  -77.576  75.963  1.00 93.60  ? 306 HIS   F NE2    1 
ATOM   16685 N  N      . LEU   F 4  307 ? -6.169  -72.256  73.087  1.00 58.13  ? 307 LEU   F N      1 
ATOM   16686 C  CA     . LEU   F 4  307 ? -7.316  -71.522  72.589  1.00 50.14  ? 307 LEU   F CA     1 
ATOM   16687 C  C      . LEU   F 4  307 ? -6.980  -70.935  71.219  1.00 50.28  ? 307 LEU   F C      1 
ATOM   16688 O  O      . LEU   F 4  307 ? -5.823  -70.923  70.797  1.00 62.19  ? 307 LEU   F O      1 
ATOM   16689 C  CB     . LEU   F 4  307 ? -7.703  -70.444  73.606  1.00 50.19  ? 307 LEU   F CB     1 
ATOM   16690 C  CG     . LEU   F 4  307 ? -9.155  -70.005  73.739  1.00 43.57  ? 307 LEU   F CG     1 
ATOM   16691 C  CD1    . LEU   F 4  307 ? -10.005 -71.206  73.930  1.00 42.29  ? 307 LEU   F CD1    1 
ATOM   16692 C  CD2    . LEU   F 4  307 ? -9.304  -69.078  74.906  1.00 37.23  ? 307 LEU   F CD2    1 
ATOM   16693 N  N      . HIS   F 4  308 ? -8.010  -70.447  70.517  1.00 49.86  ? 308 HIS   F N      1 
ATOM   16694 C  CA     . HIS   F 4  308 ? -7.867  -69.892  69.172  1.00 45.14  ? 308 HIS   F CA     1 
ATOM   16695 C  C      . HIS   F 4  308 ? -7.508  -68.417  69.153  1.00 48.64  ? 308 HIS   F C      1 
ATOM   16696 O  O      . HIS   F 4  308 ? -7.146  -67.902  68.094  1.00 55.70  ? 308 HIS   F O      1 
ATOM   16697 C  CB     . HIS   F 4  308 ? -9.146  -70.083  68.354  1.00 45.13  ? 308 HIS   F CB     1 
ATOM   16698 C  CG     . HIS   F 4  308 ? -10.406 -69.906  69.142  1.00 47.44  ? 308 HIS   F CG     1 
ATOM   16699 N  ND1    . HIS   F 4  308 ? -10.832 -70.827  70.075  1.00 45.83  ? 308 HIS   F ND1    1 
ATOM   16700 C  CD2    . HIS   F 4  308 ? -11.331 -68.917  69.140  1.00 48.12  ? 308 HIS   F CD2    1 
ATOM   16701 C  CE1    . HIS   F 4  308 ? -11.968 -70.417  70.608  1.00 50.67  ? 308 HIS   F CE1    1 
ATOM   16702 N  NE2    . HIS   F 4  308 ? -12.292 -69.259  70.060  1.00 54.80  ? 308 HIS   F NE2    1 
ATOM   16703 N  N      . TYR   F 4  309 ? -7.650  -67.716  70.262  1.00 51.15  ? 309 TYR   F N      1 
ATOM   16704 C  CA     . TYR   F 4  309 ? -7.016  -66.428  70.489  1.00 49.48  ? 309 TYR   F CA     1 
ATOM   16705 C  C      . TYR   F 4  309 ? -6.197  -66.516  71.760  1.00 51.83  ? 309 TYR   F C      1 
ATOM   16706 O  O      . TYR   F 4  309 ? -6.195  -67.534  72.458  1.00 52.75  ? 309 TYR   F O      1 
ATOM   16707 C  CB     . TYR   F 4  309 ? -8.040  -65.297  70.580  1.00 47.41  ? 309 TYR   F CB     1 
ATOM   16708 C  CG     . TYR   F 4  309 ? -8.882  -65.387  71.824  1.00 48.39  ? 309 TYR   F CG     1 
ATOM   16709 C  CD1    . TYR   F 4  309 ? -10.048 -66.126  71.815  1.00 45.13  ? 309 TYR   F CD1    1 
ATOM   16710 C  CD2    . TYR   F 4  309 ? -8.505  -64.780  73.011  1.00 46.09  ? 309 TYR   F CD2    1 
ATOM   16711 C  CE1    . TYR   F 4  309 ? -10.827 -66.232  72.920  1.00 43.65  ? 309 TYR   F CE1    1 
ATOM   16712 C  CE2    . TYR   F 4  309 ? -9.292  -64.902  74.145  1.00 48.79  ? 309 TYR   F CE2    1 
ATOM   16713 C  CZ     . TYR   F 4  309 ? -10.453 -65.640  74.084  1.00 42.96  ? 309 TYR   F CZ     1 
ATOM   16714 O  OH     . TYR   F 4  309 ? -11.276 -65.806  75.174  1.00 48.46  ? 309 TYR   F OH     1 
ATOM   16715 N  N      . GLN   F 4  310 ? -5.504  -65.432  72.071  1.00 51.13  ? 310 GLN   F N      1 
ATOM   16716 C  CA     . GLN   F 4  310 ? -4.593  -65.459  73.197  1.00 50.99  ? 310 GLN   F CA     1 
ATOM   16717 C  C      . GLN   F 4  310 ? -4.718  -64.174  73.986  1.00 52.85  ? 310 GLN   F C      1 
ATOM   16718 O  O      . GLN   F 4  310 ? -5.031  -63.112  73.440  1.00 50.17  ? 310 GLN   F O      1 
ATOM   16719 C  CB     . GLN   F 4  310 ? -3.170  -65.655  72.743  1.00 46.21  ? 310 GLN   F CB     1 
ATOM   16720 C  CG     . GLN   F 4  310 ? -3.058  -66.860  71.910  1.00 51.16  ? 310 GLN   F CG     1 
ATOM   16721 C  CD     . GLN   F 4  310 ? -2.077  -67.809  72.479  1.00 61.47  ? 310 GLN   F CD     1 
ATOM   16722 O  OE1    . GLN   F 4  310 ? -2.304  -68.370  73.566  1.00 60.03  ? 310 GLN   F OE1    1 
ATOM   16723 N  NE2    . GLN   F 4  310 ? -0.953  -67.994  71.780  1.00 59.41  ? 310 GLN   F NE2    1 
ATOM   16724 N  N      . SER   F 4  311 ? -4.461  -64.290  75.280  1.00 51.78  ? 311 SER   F N      1 
ATOM   16725 C  CA     . SER   F 4  311 ? -4.631  -63.192  76.206  1.00 45.49  ? 311 SER   F CA     1 
ATOM   16726 C  C      . SER   F 4  311 ? -3.300  -62.878  76.862  1.00 44.13  ? 311 SER   F C      1 
ATOM   16727 O  O      . SER   F 4  311 ? -2.500  -63.773  77.120  1.00 43.32  ? 311 SER   F O      1 
ATOM   16728 C  CB     . SER   F 4  311 ? -5.652  -63.556  77.260  1.00 41.63  ? 311 SER   F CB     1 
ATOM   16729 O  OG     . SER   F 4  311 ? -6.943  -63.656  76.701  1.00 49.40  ? 311 SER   F OG     1 
ATOM   16730 N  N      . PHE   F 4  312 ? -3.058  -61.605  77.101  1.00 46.25  ? 312 PHE   F N      1 
ATOM   16731 C  CA     . PHE   F 4  312 ? -2.264  -61.186  78.240  1.00 47.68  ? 312 PHE   F CA     1 
ATOM   16732 C  C      . PHE   F 4  312 ? -3.140  -60.220  79.028  1.00 49.56  ? 312 PHE   F C      1 
ATOM   16733 O  O      . PHE   F 4  312 ? -4.244  -59.874  78.603  1.00 49.77  ? 312 PHE   F O      1 
ATOM   16734 C  CB     . PHE   F 4  312 ? -0.918  -60.573  77.811  1.00 52.45  ? 312 PHE   F CB     1 
ATOM   16735 C  CG     . PHE   F 4  312 ? -1.049  -59.299  77.034  1.00 53.34  ? 312 PHE   F CG     1 
ATOM   16736 C  CD1    . PHE   F 4  312 ? -1.106  -58.083  77.678  1.00 50.28  ? 312 PHE   F CD1    1 
ATOM   16737 C  CD2    . PHE   F 4  312 ? -1.145  -59.320  75.656  1.00 60.22  ? 312 PHE   F CD2    1 
ATOM   16738 C  CE1    . PHE   F 4  312 ? -1.249  -56.909  76.960  1.00 57.80  ? 312 PHE   F CE1    1 
ATOM   16739 C  CE2    . PHE   F 4  312 ? -1.287  -58.146  74.932  1.00 63.24  ? 312 PHE   F CE2    1 
ATOM   16740 C  CZ     . PHE   F 4  312 ? -1.342  -56.937  75.589  1.00 58.85  ? 312 PHE   F CZ     1 
ATOM   16741 N  N      . GLN   F 4  313 ? -2.688  -59.836  80.216  1.00 53.79  ? 313 GLN   F N      1 
ATOM   16742 C  CA     . GLN   F 4  313 ? -3.384  -58.797  80.971  1.00 55.81  ? 313 GLN   F CA     1 
ATOM   16743 C  C      . GLN   F 4  313 ? -2.446  -58.255  82.043  1.00 58.04  ? 313 GLN   F C      1 
ATOM   16744 O  O      . GLN   F 4  313 ? -1.761  -59.035  82.720  1.00 53.72  ? 313 GLN   F O      1 
ATOM   16745 C  CB     . GLN   F 4  313 ? -4.695  -59.322  81.595  1.00 49.58  ? 313 GLN   F CB     1 
ATOM   16746 C  CG     . GLN   F 4  313 ? -5.544  -58.235  82.270  1.00 50.11  ? 313 GLN   F CG     1 
ATOM   16747 C  CD     . GLN   F 4  313 ? -6.861  -58.738  82.845  1.00 54.11  ? 313 GLN   F CD     1 
ATOM   16748 O  OE1    . GLN   F 4  313 ? -7.245  -59.888  82.652  1.00 60.11  ? 313 GLN   F OE1    1 
ATOM   16749 N  NE2    . GLN   F 4  313 ? -7.562  -57.870  83.542  1.00 53.42  ? 313 GLN   F NE2    1 
ATOM   16750 N  N      . LEU   F 4  314 ? -2.392  -56.920  82.162  1.00 56.65  ? 314 LEU   F N      1 
ATOM   16751 C  CA     . LEU   F 4  314 ? -1.744  -56.243  83.281  1.00 51.05  ? 314 LEU   F CA     1 
ATOM   16752 C  C      . LEU   F 4  314 ? -2.746  -56.126  84.419  1.00 52.07  ? 314 LEU   F C      1 
ATOM   16753 O  O      . LEU   F 4  314 ? -3.888  -55.715  84.205  1.00 57.22  ? 314 LEU   F O      1 
ATOM   16754 C  CB     . LEU   F 4  314 ? -1.241  -54.852  82.882  1.00 54.82  ? 314 LEU   F CB     1 
ATOM   16755 C  CG     . LEU   F 4  314 ? -0.523  -53.954  83.904  1.00 57.06  ? 314 LEU   F CG     1 
ATOM   16756 C  CD1    . LEU   F 4  314 ? 0.890   -54.448  84.170  1.00 56.09  ? 314 LEU   F CD1    1 
ATOM   16757 C  CD2    . LEU   F 4  314 ? -0.468  -52.512  83.452  1.00 55.32  ? 314 LEU   F CD2    1 
ATOM   16758 N  N      . PHE   F 4  315 ? -2.329  -56.532  85.616  1.00 57.40  ? 315 PHE   F N      1 
ATOM   16759 C  CA     . PHE   F 4  315 ? -3.107  -56.403  86.840  1.00 56.28  ? 315 PHE   F CA     1 
ATOM   16760 C  C      . PHE   F 4  315 ? -2.415  -55.449  87.796  1.00 56.79  ? 315 PHE   F C      1 
ATOM   16761 O  O      . PHE   F 4  315 ? -1.196  -55.272  87.746  1.00 55.70  ? 315 PHE   F O      1 
ATOM   16762 C  CB     . PHE   F 4  315 ? -3.301  -57.750  87.544  1.00 52.35  ? 315 PHE   F CB     1 
ATOM   16763 C  CG     . PHE   F 4  315 ? -3.946  -58.803  86.690  1.00 54.26  ? 315 PHE   F CG     1 
ATOM   16764 C  CD1    . PHE   F 4  315 ? -3.192  -59.590  85.838  1.00 52.91  ? 315 PHE   F CD1    1 
ATOM   16765 C  CD2    . PHE   F 4  315 ? -5.313  -59.041  86.781  1.00 53.92  ? 315 PHE   F CD2    1 
ATOM   16766 C  CE1    . PHE   F 4  315 ? -3.791  -60.571  85.063  1.00 53.47  ? 315 PHE   F CE1    1 
ATOM   16767 C  CE2    . PHE   F 4  315 ? -5.918  -60.012  86.006  1.00 53.33  ? 315 PHE   F CE2    1 
ATOM   16768 C  CZ     . PHE   F 4  315 ? -5.151  -60.780  85.147  1.00 54.08  ? 315 PHE   F CZ     1 
ATOM   16769 N  N      . GLY   F 4  316 ? -3.207  -54.835  88.666  1.00 55.77  ? 316 GLY   F N      1 
ATOM   16770 C  CA     . GLY   F 4  316 ? -2.638  -54.115  89.783  1.00 55.61  ? 316 GLY   F CA     1 
ATOM   16771 C  C      . GLY   F 4  316 ? -3.088  -54.729  91.090  1.00 65.84  ? 316 GLY   F C      1 
ATOM   16772 O  O      . GLY   F 4  316 ? -4.292  -54.758  91.375  1.00 68.75  ? 316 GLY   F O      1 
ATOM   16773 N  N      . PHE   F 4  317 ? -2.148  -55.250  91.882  1.00 64.96  ? 317 PHE   F N      1 
ATOM   16774 C  CA     . PHE   F 4  317 ? -2.464  -55.818  93.185  1.00 66.12  ? 317 PHE   F CA     1 
ATOM   16775 C  C      . PHE   F 4  317 ? -2.225  -54.770  94.263  1.00 72.20  ? 317 PHE   F C      1 
ATOM   16776 O  O      . PHE   F 4  317 ? -1.206  -54.069  94.239  1.00 71.98  ? 317 PHE   F O      1 
ATOM   16777 C  CB     . PHE   F 4  317 ? -1.621  -57.056  93.487  1.00 65.90  ? 317 PHE   F CB     1 
ATOM   16778 C  CG     . PHE   F 4  317 ? -1.997  -58.257  92.687  1.00 64.36  ? 317 PHE   F CG     1 
ATOM   16779 C  CD1    . PHE   F 4  317 ? -1.730  -58.311  91.333  1.00 60.01  ? 317 PHE   F CD1    1 
ATOM   16780 C  CD2    . PHE   F 4  317 ? -2.668  -59.316  93.285  1.00 60.25  ? 317 PHE   F CD2    1 
ATOM   16781 C  CE1    . PHE   F 4  317 ? -2.091  -59.422  90.593  1.00 58.40  ? 317 PHE   F CE1    1 
ATOM   16782 C  CE2    . PHE   F 4  317 ? -3.028  -60.423  92.559  1.00 57.53  ? 317 PHE   F CE2    1 
ATOM   16783 C  CZ     . PHE   F 4  317 ? -2.743  -60.477  91.208  1.00 56.11  ? 317 PHE   F CZ     1 
ATOM   16784 N  N      . ASP   F 4  318 ? -3.162  -54.677  95.216  1.00 72.30  ? 318 ASP   F N      1 
ATOM   16785 C  CA     . ASP   F 4  318 ? -3.163  -53.632  96.241  1.00 71.82  ? 318 ASP   F CA     1 
ATOM   16786 C  C      . ASP   F 4  318 ? -3.059  -54.292  97.612  1.00 71.28  ? 318 ASP   F C      1 
ATOM   16787 O  O      . ASP   F 4  318 ? -4.023  -54.924  98.064  1.00 72.64  ? 318 ASP   F O      1 
ATOM   16788 C  CB     . ASP   F 4  318 ? -4.437  -52.781  96.157  1.00 73.47  ? 318 ASP   F CB     1 
ATOM   16789 C  CG     . ASP   F 4  318 ? -4.523  -51.938  94.874  1.00 79.75  ? 318 ASP   F CG     1 
ATOM   16790 O  OD1    . ASP   F 4  318 ? -3.472  -51.593  94.279  1.00 70.82  ? 318 ASP   F OD1    1 
ATOM   16791 O  OD2    . ASP   F 4  318 ? -5.662  -51.592  94.480  1.00 87.78  ? 318 ASP   F OD2    1 
ATOM   16792 N  N      . PHE   F 4  319 ? -1.915  -54.129  98.293  1.00 69.46  ? 319 PHE   F N      1 
ATOM   16793 C  CA     . PHE   F 4  319 ? -1.688  -54.765  99.595  1.00 74.24  ? 319 PHE   F CA     1 
ATOM   16794 C  C      . PHE   F 4  319 ? -1.692  -53.775  100.759 1.00 76.35  ? 319 PHE   F C      1 
ATOM   16795 O  O      . PHE   F 4  319 ? -1.609  -52.555  100.599 1.00 70.69  ? 319 PHE   F O      1 
ATOM   16796 C  CB     . PHE   F 4  319 ? -0.364  -55.538  99.647  1.00 69.05  ? 319 PHE   F CB     1 
ATOM   16797 C  CG     . PHE   F 4  319 ? -0.163  -56.507  98.527  1.00 72.85  ? 319 PHE   F CG     1 
ATOM   16798 C  CD1    . PHE   F 4  319 ? 0.441   -56.106  97.331  1.00 71.19  ? 319 PHE   F CD1    1 
ATOM   16799 C  CD2    . PHE   F 4  319 ? -0.586  -57.826  98.670  1.00 67.81  ? 319 PHE   F CD2    1 
ATOM   16800 C  CE1    . PHE   F 4  319 ? 0.639   -57.005  96.308  1.00 64.77  ? 319 PHE   F CE1    1 
ATOM   16801 C  CE2    . PHE   F 4  319 ? -0.409  -58.730  97.660  1.00 63.95  ? 319 PHE   F CE2    1 
ATOM   16802 C  CZ     . PHE   F 4  319 ? 0.208   -58.321  96.469  1.00 70.89  ? 319 PHE   F CZ     1 
ATOM   16803 N  N      . MET   F 4  320 ? -1.729  -54.352  101.959 1.00 78.34  ? 320 MET   F N      1 
ATOM   16804 C  CA     . MET   F 4  320 ? -1.774  -53.606  103.211 1.00 77.86  ? 320 MET   F CA     1 
ATOM   16805 C  C      . MET   F 4  320 ? -0.888  -54.337  104.216 1.00 73.97  ? 320 MET   F C      1 
ATOM   16806 O  O      . MET   F 4  320 ? -1.185  -55.475  104.594 1.00 71.00  ? 320 MET   F O      1 
ATOM   16807 C  CB     . MET   F 4  320 ? -3.228  -53.489  103.704 1.00 81.35  ? 320 MET   F CB     1 
ATOM   16808 C  CG     . MET   F 4  320 ? -3.474  -52.552  104.876 1.00 79.57  ? 320 MET   F CG     1 
ATOM   16809 S  SD     . MET   F 4  320 ? -3.318  -50.800  104.390 1.00 88.87  ? 320 MET   F SD     1 
ATOM   16810 C  CE     . MET   F 4  320 ? -4.022  -50.784  102.753 1.00 90.58  ? 320 MET   F CE     1 
ATOM   16811 N  N      . VAL   F 4  321 ? 0.212   -53.701  104.619 1.00 70.98  ? 321 VAL   F N      1 
ATOM   16812 C  CA     . VAL   F 4  321 ? 1.178   -54.270  105.554 1.00 65.82  ? 321 VAL   F CA     1 
ATOM   16813 C  C      . VAL   F 4  321 ? 0.862   -53.766  106.952 1.00 66.91  ? 321 VAL   F C      1 
ATOM   16814 O  O      . VAL   F 4  321 ? 0.959   -52.563  107.206 1.00 73.45  ? 321 VAL   F O      1 
ATOM   16815 C  CB     . VAL   F 4  321 ? 2.615   -53.890  105.170 1.00 68.72  ? 321 VAL   F CB     1 
ATOM   16816 C  CG1    . VAL   F 4  321 ? 3.593   -54.812  105.859 1.00 71.10  ? 321 VAL   F CG1    1 
ATOM   16817 C  CG2    . VAL   F 4  321 ? 2.810   -53.935  103.663 1.00 66.63  ? 321 VAL   F CG2    1 
ATOM   16818 N  N      . ASP   F 4  322 ? 0.543   -54.675  107.876 1.00 71.08  ? 322 ASP   F N      1 
ATOM   16819 C  CA     . ASP   F 4  322 ? 0.213   -54.271  109.241 1.00 75.88  ? 322 ASP   F CA     1 
ATOM   16820 C  C      . ASP   F 4  322 ? 1.476   -54.088  110.100 1.00 76.47  ? 322 ASP   F C      1 
ATOM   16821 O  O      . ASP   F 4  322 ? 2.614   -54.184  109.628 1.00 71.53  ? 322 ASP   F O      1 
ATOM   16822 C  CB     . ASP   F 4  322 ? -0.776  -55.255  109.895 1.00 71.26  ? 322 ASP   F CB     1 
ATOM   16823 C  CG     . ASP   F 4  322 ? -0.154  -56.603  110.290 1.00 69.21  ? 322 ASP   F CG     1 
ATOM   16824 O  OD1    . ASP   F 4  322 ? 1.069   -56.812  110.169 1.00 71.07  ? 322 ASP   F OD1    1 
ATOM   16825 O  OD2    . ASP   F 4  322 ? -0.912  -57.455  110.793 1.00 63.06  ? 322 ASP   F OD2    1 
ATOM   16826 N  N      . GLU   F 4  323 ? 1.243   -53.812  111.391 1.00 81.66  ? 323 GLU   F N      1 
ATOM   16827 C  CA     . GLU   F 4  323 ? 2.297   -53.495  112.358 1.00 81.84  ? 323 GLU   F CA     1 
ATOM   16828 C  C      . GLU   F 4  323 ? 3.309   -54.629  112.521 1.00 76.47  ? 323 GLU   F C      1 
ATOM   16829 O  O      . GLU   F 4  323 ? 4.492   -54.372  112.775 1.00 66.26  ? 323 GLU   F O      1 
ATOM   16830 C  CB     . GLU   F 4  323 ? 1.625   -53.159  113.694 1.00 86.73  ? 323 GLU   F CB     1 
ATOM   16831 C  CG     . GLU   F 4  323 ? 2.390   -52.316  114.687 1.00 94.78  ? 323 GLU   F CG     1 
ATOM   16832 C  CD     . GLU   F 4  323 ? 1.535   -52.006  115.918 1.00 108.26 ? 323 GLU   F CD     1 
ATOM   16833 O  OE1    . GLU   F 4  323 ? 0.955   -52.958  116.490 1.00 97.65  ? 323 GLU   F OE1    1 
ATOM   16834 O  OE2    . GLU   F 4  323 ? 1.480   -50.828  116.344 1.00 120.89 ? 323 GLU   F OE2    1 
ATOM   16835 N  N      . GLU   F 4  324 ? 2.868   -55.877  112.377 1.00 76.77  ? 324 GLU   F N      1 
ATOM   16836 C  CA     . GLU   F 4  324 ? 3.708   -57.061  112.503 1.00 71.68  ? 324 GLU   F CA     1 
ATOM   16837 C  C      . GLU   F 4  324 ? 4.486   -57.376  111.227 1.00 72.13  ? 324 GLU   F C      1 
ATOM   16838 O  O      . GLU   F 4  324 ? 5.027   -58.481  111.091 1.00 71.34  ? 324 GLU   F O      1 
ATOM   16839 C  CB     . GLU   F 4  324 ? 2.838   -58.260  112.885 1.00 73.55  ? 324 GLU   F CB     1 
ATOM   16840 C  CG     . GLU   F 4  324 ? 2.129   -58.093  114.222 1.00 80.65  ? 324 GLU   F CG     1 
ATOM   16841 C  CD     . GLU   F 4  324 ? 3.069   -58.176  115.415 1.00 97.44  ? 324 GLU   F CD     1 
ATOM   16842 O  OE1    . GLU   F 4  324 ? 4.176   -57.588  115.356 1.00 99.12  ? 324 GLU   F OE1    1 
ATOM   16843 O  OE2    . GLU   F 4  324 ? 2.680   -58.799  116.430 1.00 104.38 ? 324 GLU   F OE2    1 
ATOM   16844 N  N      . LEU   F 4  325 ? 4.549   -56.435  110.291 1.00 69.73  ? 325 LEU   F N      1 
ATOM   16845 C  CA     . LEU   F 4  325 ? 5.143   -56.690  108.987 1.00 66.03  ? 325 LEU   F CA     1 
ATOM   16846 C  C      . LEU   F 4  325 ? 4.510   -57.904  108.316 1.00 64.54  ? 325 LEU   F C      1 
ATOM   16847 O  O      . LEU   F 4  325 ? 5.197   -58.754  107.755 1.00 64.87  ? 325 LEU   F O      1 
ATOM   16848 C  CB     . LEU   F 4  325 ? 6.648   -56.868  109.091 1.00 62.31  ? 325 LEU   F CB     1 
ATOM   16849 C  CG     . LEU   F 4  325 ? 7.329   -55.522  109.216 1.00 63.95  ? 325 LEU   F CG     1 
ATOM   16850 C  CD1    . LEU   F 4  325 ? 8.808   -55.711  109.452 1.00 68.66  ? 325 LEU   F CD1    1 
ATOM   16851 C  CD2    . LEU   F 4  325 ? 7.052   -54.674  107.988 1.00 68.99  ? 325 LEU   F CD2    1 
ATOM   16852 N  N      . LYS   F 4  326 ? 3.190   -57.997  108.399 1.00 63.63  ? 326 LYS   F N      1 
ATOM   16853 C  CA     . LYS   F 4  326 ? 2.420   -58.968  107.639 1.00 60.04  ? 326 LYS   F CA     1 
ATOM   16854 C  C      . LYS   F 4  326 ? 1.770   -58.271  106.461 1.00 68.24  ? 326 LYS   F C      1 
ATOM   16855 O  O      . LYS   F 4  326 ? 1.203   -57.186  106.613 1.00 74.23  ? 326 LYS   F O      1 
ATOM   16856 C  CB     . LYS   F 4  326 ? 1.334   -59.611  108.487 1.00 60.80  ? 326 LYS   F CB     1 
ATOM   16857 C  CG     . LYS   F 4  326 ? 0.363   -60.473  107.695 1.00 60.76  ? 326 LYS   F CG     1 
ATOM   16858 C  CD     . LYS   F 4  326 ? -0.435  -61.371  108.634 1.00 65.20  ? 326 LYS   F CD     1 
ATOM   16859 C  CE     . LYS   F 4  326 ? -1.380  -62.321  107.916 1.00 68.01  ? 326 LYS   F CE     1 
ATOM   16860 N  NZ     . LYS   F 4  326 ? -1.972  -63.308  108.866 1.00 60.36  ? 326 LYS   F NZ     1 
ATOM   16861 N  N      . VAL   F 4  327 ? 1.846   -58.892  105.290 1.00 68.00  ? 327 VAL   F N      1 
ATOM   16862 C  CA     . VAL   F 4  327 ? 1.271   -58.323  104.080 1.00 62.74  ? 327 VAL   F CA     1 
ATOM   16863 C  C      . VAL   F 4  327 ? -0.125  -58.890  103.905 1.00 66.75  ? 327 VAL   F C      1 
ATOM   16864 O  O      . VAL   F 4  327 ? -0.358  -60.085  104.122 1.00 70.93  ? 327 VAL   F O      1 
ATOM   16865 C  CB     . VAL   F 4  327 ? 2.150   -58.605  102.852 1.00 60.17  ? 327 VAL   F CB     1 
ATOM   16866 C  CG1    . VAL   F 4  327 ? 1.509   -58.016  101.613 1.00 62.97  ? 327 VAL   F CG1    1 
ATOM   16867 C  CG2    . VAL   F 4  327 ? 3.567   -58.053  103.067 1.00 61.29  ? 327 VAL   F CG2    1 
ATOM   16868 N  N      . TRP   F 4  328 ? -1.060  -58.029  103.525 1.00 70.47  ? 328 TRP   F N      1 
ATOM   16869 C  CA     . TRP   F 4  328 ? -2.456  -58.404  103.356 1.00 75.09  ? 328 TRP   F CA     1 
ATOM   16870 C  C      . TRP   F 4  328 ? -2.915  -58.013  101.953 1.00 73.71  ? 328 TRP   F C      1 
ATOM   16871 O  O      . TRP   F 4  328 ? -2.437  -57.032  101.373 1.00 68.25  ? 328 TRP   F O      1 
ATOM   16872 C  CB     . TRP   F 4  328 ? -3.341  -57.723  104.423 1.00 76.62  ? 328 TRP   F CB     1 
ATOM   16873 C  CG     . TRP   F 4  328 ? -3.060  -58.157  105.846 1.00 76.07  ? 328 TRP   F CG     1 
ATOM   16874 C  CD1    . TRP   F 4  328 ? -2.086  -57.665  106.681 1.00 73.96  ? 328 TRP   F CD1    1 
ATOM   16875 C  CD2    . TRP   F 4  328 ? -3.794  -59.118  106.618 1.00 72.57  ? 328 TRP   F CD2    1 
ATOM   16876 N  NE1    . TRP   F 4  328 ? -2.153  -58.285  107.911 1.00 69.07  ? 328 TRP   F NE1    1 
ATOM   16877 C  CE2    . TRP   F 4  328 ? -3.193  -59.178  107.897 1.00 68.47  ? 328 TRP   F CE2    1 
ATOM   16878 C  CE3    . TRP   F 4  328 ? -4.882  -59.943  106.349 1.00 69.07  ? 328 TRP   F CE3    1 
ATOM   16879 C  CZ2    . TRP   F 4  328 ? -3.646  -60.033  108.891 1.00 64.07  ? 328 TRP   F CZ2    1 
ATOM   16880 C  CZ3    . TRP   F 4  328 ? -5.329  -60.786  107.340 1.00 69.32  ? 328 TRP   F CZ3    1 
ATOM   16881 C  CH2    . TRP   F 4  328 ? -4.712  -60.828  108.594 1.00 66.66  ? 328 TRP   F CH2    1 
ATOM   16882 N  N      . LEU   F 4  329 ? -3.836  -58.792  101.399 1.00 73.02  ? 329 LEU   F N      1 
ATOM   16883 C  CA     . LEU   F 4  329 ? -4.383  -58.491  100.084 1.00 76.06  ? 329 LEU   F CA     1 
ATOM   16884 C  C      . LEU   F 4  329 ? -5.725  -57.799  100.261 1.00 80.59  ? 329 LEU   F C      1 
ATOM   16885 O  O      . LEU   F 4  329 ? -6.580  -58.265  101.025 1.00 82.51  ? 329 LEU   F O      1 
ATOM   16886 C  CB     . LEU   F 4  329 ? -4.529  -59.749  99.221  1.00 78.23  ? 329 LEU   F CB     1 
ATOM   16887 C  CG     . LEU   F 4  329 ? -5.358  -59.593  97.939  1.00 75.38  ? 329 LEU   F CG     1 
ATOM   16888 C  CD1    . LEU   F 4  329 ? -4.561  -58.838  96.894  1.00 71.90  ? 329 LEU   F CD1    1 
ATOM   16889 C  CD2    . LEU   F 4  329 ? -5.786  -60.954  97.407  1.00 70.57  ? 329 LEU   F CD2    1 
ATOM   16890 N  N      . ILE   F 4  330 ? -5.901  -56.691  99.551  1.00 78.98  ? 330 ILE   F N      1 
ATOM   16891 C  CA     . ILE   F 4  330 ? -7.043  -55.815  99.745  1.00 77.77  ? 330 ILE   F CA     1 
ATOM   16892 C  C      . ILE   F 4  330 ? -7.969  -55.907  98.544  1.00 78.14  ? 330 ILE   F C      1 
ATOM   16893 O  O      . ILE   F 4  330 ? -9.071  -56.445  98.649  1.00 77.57  ? 330 ILE   F O      1 
ATOM   16894 C  CB     . ILE   F 4  330 ? -6.560  -54.379  99.996  1.00 78.73  ? 330 ILE   F CB     1 
ATOM   16895 C  CG1    . ILE   F 4  330 ? -6.027  -54.287  101.420 1.00 80.66  ? 330 ILE   F CG1    1 
ATOM   16896 C  CG2    . ILE   F 4  330 ? -7.654  -53.374  99.713  1.00 86.49  ? 330 ILE   F CG2    1 
ATOM   16897 C  CD1    . ILE   F 4  330 ? -6.949  -54.941  102.421 1.00 86.84  ? 330 ILE   F CD1    1 
ATOM   16898 N  N      . GLU   F 4  331 ? -7.520  -55.397  97.397  1.00 84.56  ? 331 GLU   F N      1 
ATOM   16899 C  CA     . GLU   F 4  331 ? -8.267  -55.395  96.144  1.00 79.05  ? 331 GLU   F CA     1 
ATOM   16900 C  C      . GLU   F 4  331 ? -7.304  -55.867  95.059  1.00 75.10  ? 331 GLU   F C      1 
ATOM   16901 O  O      . GLU   F 4  331 ? -6.100  -55.599  95.141  1.00 75.49  ? 331 GLU   F O      1 
ATOM   16902 C  CB     . GLU   F 4  331 ? -8.823  -53.972  95.828  1.00 79.65  ? 331 GLU   F CB     1 
ATOM   16903 C  CG     . GLU   F 4  331 ? -9.601  -53.784  94.510  1.00 85.88  ? 331 GLU   F CG     1 
ATOM   16904 C  CD     . GLU   F 4  331 ? -9.391  -52.412  93.841  1.00 93.74  ? 331 GLU   F CD     1 
ATOM   16905 O  OE1    . GLU   F 4  331 ? -8.396  -51.721  94.145  1.00 99.77  ? 331 GLU   F OE1    1 
ATOM   16906 O  OE2    . GLU   F 4  331 ? -10.237 -52.011  93.013  1.00 93.43  ? 331 GLU   F OE2    1 
ATOM   16907 N  N      . VAL   F 4  332 ? -7.809  -56.613  94.076  1.00 74.61  ? 332 VAL   F N      1 
ATOM   16908 C  CA     . VAL   F 4  332 ? -7.080  -56.873  92.834  1.00 72.81  ? 332 VAL   F CA     1 
ATOM   16909 C  C      . VAL   F 4  332 ? -7.733  -56.029  91.751  1.00 75.02  ? 332 VAL   F C      1 
ATOM   16910 O  O      . VAL   F 4  332 ? -8.959  -56.075  91.583  1.00 77.70  ? 332 VAL   F O      1 
ATOM   16911 C  CB     . VAL   F 4  332 ? -7.104  -58.360  92.433  1.00 69.82  ? 332 VAL   F CB     1 
ATOM   16912 C  CG1    . VAL   F 4  332 ? -6.190  -58.596  91.234  1.00 61.85  ? 332 VAL   F CG1    1 
ATOM   16913 C  CG2    . VAL   F 4  332 ? -6.764  -59.272  93.609  1.00 75.29  ? 332 VAL   F CG2    1 
ATOM   16914 N  N      . ASN   F 4  333 ? -6.934  -55.251  91.022  1.00 68.65  ? 333 ASN   F N      1 
ATOM   16915 C  CA     . ASN   F 4  333 ? -7.487  -54.324  90.043  1.00 73.54  ? 333 ASN   F CA     1 
ATOM   16916 C  C      . ASN   F 4  333 ? -7.150  -54.789  88.634  1.00 70.03  ? 333 ASN   F C      1 
ATOM   16917 O  O      . ASN   F 4  333 ? -5.970  -54.903  88.279  1.00 69.53  ? 333 ASN   F O      1 
ATOM   16918 C  CB     . ASN   F 4  333 ? -6.986  -52.903  90.280  1.00 80.06  ? 333 ASN   F CB     1 
ATOM   16919 C  CG     . ASN   F 4  333 ? -8.030  -51.849  89.900  1.00 96.41  ? 333 ASN   F CG     1 
ATOM   16920 O  OD1    . ASN   F 4  333 ? -8.404  -51.708  88.717  1.00 87.93  ? 333 ASN   F OD1    1 
ATOM   16921 N  ND2    . ASN   F 4  333 ? -8.532  -51.119  90.915  1.00 100.67 ? 333 ASN   F ND2    1 
ATOM   16922 N  N      . GLY   F 4  334 ? -8.192  -55.016  87.827  1.00 64.40  ? 334 GLY   F N      1 
ATOM   16923 C  CA     . GLY   F 4  334 ? -7.995  -55.557  86.491  1.00 68.68  ? 334 GLY   F CA     1 
ATOM   16924 C  C      . GLY   F 4  334 ? -7.675  -54.534  85.418  1.00 71.83  ? 334 GLY   F C      1 
ATOM   16925 O  O      . GLY   F 4  334 ? -6.950  -54.840  84.463  1.00 67.23  ? 334 GLY   F O      1 
ATOM   16926 N  N      . ALA   F 4  335 ? -8.224  -53.326  85.532  1.00 77.78  ? 335 ALA   F N      1 
ATOM   16927 C  CA     . ALA   F 4  335 ? -7.826  -52.203  84.689  1.00 76.40  ? 335 ALA   F CA     1 
ATOM   16928 C  C      . ALA   F 4  335 ? -7.070  -51.229  85.582  1.00 76.89  ? 335 ALA   F C      1 
ATOM   16929 O  O      . ALA   F 4  335 ? -7.684  -50.429  86.306  1.00 87.58  ? 335 ALA   F O      1 
ATOM   16930 C  CB     . ALA   F 4  335 ? -9.036  -51.533  84.032  1.00 78.31  ? 335 ALA   F CB     1 
ATOM   16931 N  N      . PRO   F 4  336 ? -5.749  -51.284  85.605  1.00 72.91  ? 336 PRO   F N      1 
ATOM   16932 C  CA     . PRO   F 4  336 ? -5.004  -50.537  86.615  1.00 78.05  ? 336 PRO   F CA     1 
ATOM   16933 C  C      . PRO   F 4  336 ? -4.188  -49.428  85.996  1.00 74.80  ? 336 PRO   F C      1 
ATOM   16934 O  O      . PRO   F 4  336 ? -3.534  -49.652  84.978  1.00 76.15  ? 336 PRO   F O      1 
ATOM   16935 C  CB     . PRO   F 4  336 ? -4.087  -51.603  87.216  1.00 72.17  ? 336 PRO   F CB     1 
ATOM   16936 C  CG     . PRO   F 4  336 ? -3.954  -52.653  86.121  1.00 69.41  ? 336 PRO   F CG     1 
ATOM   16937 C  CD     . PRO   F 4  336 ? -4.897  -52.301  84.988  1.00 70.83  ? 336 PRO   F CD     1 
ATOM   16938 N  N      . ALA   F 4  337 ? -4.200  -48.249  86.604  1.00 75.80  ? 337 ALA   F N      1 
ATOM   16939 C  CA     . ALA   F 4  337 ? -3.338  -47.161  86.181  1.00 69.21  ? 337 ALA   F CA     1 
ATOM   16940 C  C      . ALA   F 4  337 ? -1.940  -47.337  86.759  1.00 72.48  ? 337 ALA   F C      1 
ATOM   16941 O  O      . ALA   F 4  337 ? -1.755  -47.937  87.823  1.00 79.48  ? 337 ALA   F O      1 
ATOM   16942 C  CB     . ALA   F 4  337 ? -3.917  -45.817  86.616  1.00 64.94  ? 337 ALA   F CB     1 
ATOM   16943 N  N      . CYS   F 4  338 ? -0.955  -46.810  86.040  1.00 67.91  ? 338 CYS   F N      1 
ATOM   16944 C  CA     . CYS   F 4  338 ? 0.429   -46.749  86.487  1.00 70.56  ? 338 CYS   F CA     1 
ATOM   16945 C  C      . CYS   F 4  338 ? 0.726   -45.430  87.197  1.00 80.22  ? 338 CYS   F C      1 
ATOM   16946 O  O      . CYS   F 4  338 ? -0.052  -44.481  87.145  1.00 91.94  ? 338 CYS   F O      1 
ATOM   16947 C  CB     . CYS   F 4  338 ? 1.375   -46.905  85.309  1.00 70.43  ? 338 CYS   F CB     1 
ATOM   16948 S  SG     . CYS   F 4  338 ? 3.044   -47.130  85.849  1.00 78.42  ? 338 CYS   F SG     1 
ATOM   16949 N  N      . ALA   F 4  339 ? 1.879   -45.366  87.856  1.00 83.59  ? 339 ALA   F N      1 
ATOM   16950 C  CA     . ALA   F 4  339 ? 2.354   -44.116  88.438  1.00 81.21  ? 339 ALA   F CA     1 
ATOM   16951 C  C      . ALA   F 4  339 ? 3.221   -43.396  87.411  1.00 82.79  ? 339 ALA   F C      1 
ATOM   16952 O  O      . ALA   F 4  339 ? 4.139   -43.992  86.835  1.00 79.91  ? 339 ALA   F O      1 
ATOM   16953 C  CB     . ALA   F 4  339 ? 3.133   -44.367  89.731  1.00 81.10  ? 339 ALA   F CB     1 
ATOM   16954 N  N      . GLN   F 4  340 ? 2.924   -42.112  87.193  1.00 86.75  ? 340 GLN   F N      1 
ATOM   16955 C  CA     . GLN   F 4  340 ? 3.521   -41.308  86.131  1.00 83.13  ? 340 GLN   F CA     1 
ATOM   16956 C  C      . GLN   F 4  340 ? 5.013   -41.586  85.952  1.00 80.01  ? 340 GLN   F C      1 
ATOM   16957 O  O      . GLN   F 4  340 ? 5.479   -41.793  84.830  1.00 72.89  ? 340 GLN   F O      1 
ATOM   16958 C  CB     . GLN   F 4  340 ? 3.295   -39.823  86.424  1.00 84.28  ? 340 GLN   F CB     1 
ATOM   16959 C  CG     . GLN   F 4  340 ? 4.091   -38.877  85.534  1.00 93.80  ? 340 GLN   F CG     1 
ATOM   16960 C  CD     . GLN   F 4  340 ? 3.686   -38.985  84.074  1.00 105.39 ? 340 GLN   F CD     1 
ATOM   16961 O  OE1    . GLN   F 4  340 ? 2.747   -39.711  83.739  1.00 109.37 ? 340 GLN   F OE1    1 
ATOM   16962 N  NE2    . GLN   F 4  340 ? 4.405   -38.283  83.194  1.00 98.43  ? 340 GLN   F NE2    1 
ATOM   16963 N  N      . LYS   F 4  341 ? 5.772   -41.600  87.050  1.00 86.15  ? 341 LYS   F N      1 
ATOM   16964 C  CA     . LYS   F 4  341 ? 7.220   -41.773  86.945  1.00 86.64  ? 341 LYS   F CA     1 
ATOM   16965 C  C      . LYS   F 4  341 ? 7.600   -43.033  86.175  1.00 83.02  ? 341 LYS   F C      1 
ATOM   16966 O  O      . LYS   F 4  341 ? 8.666   -43.072  85.544  1.00 79.16  ? 341 LYS   F O      1 
ATOM   16967 C  CB     . LYS   F 4  341 ? 7.850   -41.790  88.344  1.00 87.10  ? 341 LYS   F CB     1 
ATOM   16968 C  CG     . LYS   F 4  341 ? 9.350   -42.095  88.344  1.00 93.04  ? 341 LYS   F CG     1 
ATOM   16969 C  CD     . LYS   F 4  341 ? 9.936   -42.181  89.755  1.00 95.02  ? 341 LYS   F CD     1 
ATOM   16970 C  CE     . LYS   F 4  341 ? 11.291  -42.881  89.734  1.00 98.06  ? 341 LYS   F CE     1 
ATOM   16971 N  NZ     . LYS   F 4  341 ? 12.341  -42.025  89.129  1.00 98.51  ? 341 LYS   F NZ     1 
ATOM   16972 N  N      . LEU   F 4  342 ? 6.742   -44.061  86.196  1.00 83.45  ? 342 LEU   F N      1 
ATOM   16973 C  CA     . LEU   F 4  342 ? 7.089   -45.387  85.691  1.00 86.81  ? 342 LEU   F CA     1 
ATOM   16974 C  C      . LEU   F 4  342 ? 6.457   -45.769  84.353  1.00 87.47  ? 342 LEU   F C      1 
ATOM   16975 O  O      . LEU   F 4  342 ? 6.881   -46.774  83.767  1.00 85.21  ? 342 LEU   F O      1 
ATOM   16976 C  CB     . LEU   F 4  342 ? 6.721   -46.448  86.740  1.00 79.19  ? 342 LEU   F CB     1 
ATOM   16977 C  CG     . LEU   F 4  342 ? 7.364   -46.166  88.088  1.00 79.21  ? 342 LEU   F CG     1 
ATOM   16978 C  CD1    . LEU   F 4  342 ? 6.897   -47.138  89.158  1.00 75.61  ? 342 LEU   F CD1    1 
ATOM   16979 C  CD2    . LEU   F 4  342 ? 8.857   -46.286  87.879  1.00 80.06  ? 342 LEU   F CD2    1 
ATOM   16980 N  N      . TYR   F 4  343 ? 5.474   -45.007  83.849  1.00 87.11  ? 343 TYR   F N      1 
ATOM   16981 C  CA     . TYR   F 4  343 ? 4.790   -45.385  82.612  1.00 76.11  ? 343 TYR   F CA     1 
ATOM   16982 C  C      . TYR   F 4  343 ? 5.774   -45.797  81.531  1.00 77.62  ? 343 TYR   F C      1 
ATOM   16983 O  O      . TYR   F 4  343 ? 5.659   -46.880  80.946  1.00 77.53  ? 343 TYR   F O      1 
ATOM   16984 C  CB     . TYR   F 4  343 ? 3.934   -44.241  82.093  1.00 70.97  ? 343 TYR   F CB     1 
ATOM   16985 C  CG     . TYR   F 4  343 ? 2.535   -44.256  82.614  1.00 75.85  ? 343 TYR   F CG     1 
ATOM   16986 C  CD1    . TYR   F 4  343 ? 2.199   -43.584  83.769  1.00 78.96  ? 343 TYR   F CD1    1 
ATOM   16987 C  CD2    . TYR   F 4  343 ? 1.553   -44.989  81.976  1.00 83.73  ? 343 TYR   F CD2    1 
ATOM   16988 C  CE1    . TYR   F 4  343 ? 0.902   -43.597  84.248  1.00 77.89  ? 343 TYR   F CE1    1 
ATOM   16989 C  CE2    . TYR   F 4  343 ? 0.253   -45.021  82.455  1.00 78.79  ? 343 TYR   F CE2    1 
ATOM   16990 C  CZ     . TYR   F 4  343 ? -0.067  -44.323  83.588  1.00 72.31  ? 343 TYR   F CZ     1 
ATOM   16991 O  OH     . TYR   F 4  343 ? -1.365  -44.360  84.048  1.00 74.76  ? 343 TYR   F OH     1 
ATOM   16992 N  N      . ALA   F 4  344 ? 6.741   -44.931  81.236  1.00 79.95  ? 344 ALA   F N      1 
ATOM   16993 C  CA     . ALA   F 4  344 ? 7.755   -45.280  80.251  1.00 84.83  ? 344 ALA   F CA     1 
ATOM   16994 C  C      . ALA   F 4  344 ? 8.253   -46.699  80.477  1.00 82.88  ? 344 ALA   F C      1 
ATOM   16995 O  O      . ALA   F 4  344 ? 8.156   -47.550  79.587  1.00 88.15  ? 344 ALA   F O      1 
ATOM   16996 C  CB     . ALA   F 4  344 ? 8.911   -44.281  80.300  1.00 91.66  ? 344 ALA   F CB     1 
ATOM   16997 N  N      . GLU   F 4  345 ? 8.749   -46.993  81.683  1.00 83.36  ? 345 GLU   F N      1 
ATOM   16998 C  CA     . GLU   F 4  345 ? 9.393   -48.288  81.888  1.00 81.99  ? 345 GLU   F CA     1 
ATOM   16999 C  C      . GLU   F 4  345 ? 8.386   -49.428  81.787  1.00 74.80  ? 345 GLU   F C      1 
ATOM   17000 O  O      . GLU   F 4  345 ? 8.604   -50.385  81.039  1.00 78.93  ? 345 GLU   F O      1 
ATOM   17001 C  CB     . GLU   F 4  345 ? 10.137  -48.338  83.225  1.00 77.90  ? 345 GLU   F CB     1 
ATOM   17002 C  CG     . GLU   F 4  345 ? 11.118  -49.506  83.280  1.00 71.00  ? 345 GLU   F CG     1 
ATOM   17003 C  CD     . GLU   F 4  345 ? 11.996  -49.504  84.504  1.00 73.61  ? 345 GLU   F CD     1 
ATOM   17004 O  OE1    . GLU   F 4  345 ? 11.524  -49.107  85.588  1.00 75.56  ? 345 GLU   F OE1    1 
ATOM   17005 O  OE2    . GLU   F 4  345 ? 13.164  -49.912  84.378  1.00 77.44  ? 345 GLU   F OE2    1 
ATOM   17006 N  N      . LEU   F 4  346 ? 7.268   -49.343  82.513  1.00 70.95  ? 346 LEU   F N      1 
ATOM   17007 C  CA     . LEU   F 4  346 ? 6.298   -50.438  82.476  1.00 77.01  ? 346 LEU   F CA     1 
ATOM   17008 C  C      . LEU   F 4  346 ? 5.717   -50.645  81.072  1.00 79.73  ? 346 LEU   F C      1 
ATOM   17009 O  O      . LEU   F 4  346 ? 5.649   -51.781  80.586  1.00 75.72  ? 346 LEU   F O      1 
ATOM   17010 C  CB     . LEU   F 4  346 ? 5.184   -50.209  83.508  1.00 75.39  ? 346 LEU   F CB     1 
ATOM   17011 C  CG     . LEU   F 4  346 ? 4.076   -51.277  83.493  1.00 72.64  ? 346 LEU   F CG     1 
ATOM   17012 C  CD1    . LEU   F 4  346 ? 4.603   -52.632  83.935  1.00 68.15  ? 346 LEU   F CD1    1 
ATOM   17013 C  CD2    . LEU   F 4  346 ? 2.917   -50.878  84.384  1.00 69.24  ? 346 LEU   F CD2    1 
ATOM   17014 N  N      . CYS   F 4  347 ? 5.296   -49.570  80.399  1.00 74.94  ? 347 CYS   F N      1 
ATOM   17015 C  CA     . CYS   F 4  347 ? 4.662   -49.749  79.101  1.00 63.30  ? 347 CYS   F CA     1 
ATOM   17016 C  C      . CYS   F 4  347 ? 5.627   -50.252  78.038  1.00 72.87  ? 347 CYS   F C      1 
ATOM   17017 O  O      . CYS   F 4  347 ? 5.185   -50.866  77.062  1.00 76.27  ? 347 CYS   F O      1 
ATOM   17018 C  CB     . CYS   F 4  347 ? 4.027   -48.450  78.655  1.00 63.76  ? 347 CYS   F CB     1 
ATOM   17019 S  SG     . CYS   F 4  347 ? 2.653   -48.010  79.685  1.00 76.52  ? 347 CYS   F SG     1 
ATOM   17020 N  N      . GLN   F 4  348 ? 6.929   -50.009  78.183  1.00 72.26  ? 348 GLN   F N      1 
ATOM   17021 C  CA     . GLN   F 4  348 ? 7.866   -50.644  77.264  1.00 72.43  ? 348 GLN   F CA     1 
ATOM   17022 C  C      . GLN   F 4  348 ? 7.995   -52.133  77.548  1.00 70.88  ? 348 GLN   F C      1 
ATOM   17023 O  O      . GLN   F 4  348 ? 8.144   -52.935  76.620  1.00 66.93  ? 348 GLN   F O      1 
ATOM   17024 C  CB     . GLN   F 4  348 ? 9.240   -49.987  77.330  1.00 72.43  ? 348 GLN   F CB     1 
ATOM   17025 C  CG     . GLN   F 4  348 ? 10.311  -50.744  76.516  1.00 72.01  ? 348 GLN   F CG     1 
ATOM   17026 C  CD     . GLN   F 4  348 ? 10.011  -50.858  75.027  1.00 75.67  ? 348 GLN   F CD     1 
ATOM   17027 O  OE1    . GLN   F 4  348 ? 9.498   -49.921  74.398  1.00 82.77  ? 348 GLN   F OE1    1 
ATOM   17028 N  NE2    . GLN   F 4  348 ? 10.331  -52.008  74.454  1.00 75.06  ? 348 GLN   F NE2    1 
ATOM   17029 N  N      . GLY   F 4  349 ? 7.958   -52.519  78.823  1.00 73.72  ? 349 GLY   F N      1 
ATOM   17030 C  CA     . GLY   F 4  349 ? 8.072   -53.929  79.165  1.00 72.97  ? 349 GLY   F CA     1 
ATOM   17031 C  C      . GLY   F 4  349 ? 6.845   -54.727  78.783  1.00 69.04  ? 349 GLY   F C      1 
ATOM   17032 O  O      . GLY   F 4  349 ? 6.940   -55.931  78.515  1.00 65.72  ? 349 GLY   F O      1 
ATOM   17033 N  N      . ILE   F 4  350 ? 5.681   -54.072  78.756  1.00 67.05  ? 350 ILE   F N      1 
ATOM   17034 C  CA     . ILE   F 4  350 ? 4.478   -54.695  78.224  1.00 62.69  ? 350 ILE   F CA     1 
ATOM   17035 C  C      . ILE   F 4  350 ? 4.706   -55.090  76.776  1.00 63.91  ? 350 ILE   F C      1 
ATOM   17036 O  O      . ILE   F 4  350 ? 4.365   -56.199  76.351  1.00 64.45  ? 350 ILE   F O      1 
ATOM   17037 C  CB     . ILE   F 4  350 ? 3.293   -53.731  78.359  1.00 59.46  ? 350 ILE   F CB     1 
ATOM   17038 C  CG1    . ILE   F 4  350 ? 2.949   -53.552  79.829  1.00 67.53  ? 350 ILE   F CG1    1 
ATOM   17039 C  CG2    . ILE   F 4  350 ? 2.106   -54.284  77.640  1.00 56.20  ? 350 ILE   F CG2    1 
ATOM   17040 C  CD1    . ILE   F 4  350 ? 1.747   -52.672  80.093  1.00 69.55  ? 350 ILE   F CD1    1 
ATOM   17041 N  N      . VAL   F 4  351 ? 5.313   -54.198  75.999  1.00 65.99  ? 351 VAL   F N      1 
ATOM   17042 C  CA     . VAL   F 4  351 ? 5.535   -54.492  74.591  1.00 69.93  ? 351 VAL   F CA     1 
ATOM   17043 C  C      . VAL   F 4  351 ? 6.520   -55.640  74.433  1.00 67.96  ? 351 VAL   F C      1 
ATOM   17044 O  O      . VAL   F 4  351 ? 6.318   -56.538  73.608  1.00 66.46  ? 351 VAL   F O      1 
ATOM   17045 C  CB     . VAL   F 4  351 ? 6.019   -53.238  73.845  1.00 63.44  ? 351 VAL   F CB     1 
ATOM   17046 C  CG1    . VAL   F 4  351 ? 6.505   -53.647  72.473  1.00 57.81  ? 351 VAL   F CG1    1 
ATOM   17047 C  CG2    . VAL   F 4  351 ? 4.907   -52.206  73.761  1.00 58.72  ? 351 VAL   F CG2    1 
ATOM   17048 N  N      . ASP   F 4  352 ? 7.613   -55.616  75.197  1.00 65.95  ? 352 ASP   F N      1 
ATOM   17049 C  CA     . ASP   F 4  352 ? 8.652   -56.617  75.009  1.00 64.66  ? 352 ASP   F CA     1 
ATOM   17050 C  C      . ASP   F 4  352 ? 8.201   -57.976  75.501  1.00 63.34  ? 352 ASP   F C      1 
ATOM   17051 O  O      . ASP   F 4  352 ? 8.575   -58.999  74.922  1.00 66.85  ? 352 ASP   F O      1 
ATOM   17052 C  CB     . ASP   F 4  352 ? 9.951   -56.220  75.727  1.00 78.24  ? 352 ASP   F CB     1 
ATOM   17053 C  CG     . ASP   F 4  352 ? 10.328  -54.738  75.538  1.00 87.72  ? 352 ASP   F CG     1 
ATOM   17054 O  OD1    . ASP   F 4  352 ? 10.439  -54.292  74.370  1.00 89.43  ? 352 ASP   F OD1    1 
ATOM   17055 O  OD2    . ASP   F 4  352 ? 10.571  -54.033  76.557  1.00 84.70  ? 352 ASP   F OD2    1 
ATOM   17056 N  N      . VAL   F 4  353 ? 7.401   -58.011  76.556  1.00 62.86  ? 353 VAL   F N      1 
ATOM   17057 C  CA     . VAL   F 4  353 ? 7.116   -59.274  77.222  1.00 67.40  ? 353 VAL   F CA     1 
ATOM   17058 C  C      . VAL   F 4  353 ? 5.820   -59.899  76.712  1.00 71.00  ? 353 VAL   F C      1 
ATOM   17059 O  O      . VAL   F 4  353 ? 5.771   -61.104  76.451  1.00 66.88  ? 353 VAL   F O      1 
ATOM   17060 C  CB     . VAL   F 4  353 ? 7.092   -59.042  78.749  1.00 67.07  ? 353 VAL   F CB     1 
ATOM   17061 C  CG1    . VAL   F 4  353 ? 6.891   -60.339  79.500  1.00 66.20  ? 353 VAL   F CG1    1 
ATOM   17062 C  CG2    . VAL   F 4  353 ? 8.383   -58.387  79.192  1.00 60.37  ? 353 VAL   F CG2    1 
ATOM   17063 N  N      . ALA   F 4  354 ? 4.765   -59.092  76.542  1.00 68.37  ? 354 ALA   F N      1 
ATOM   17064 C  CA     . ALA   F 4  354 ? 3.438   -59.592  76.213  1.00 64.30  ? 354 ALA   F CA     1 
ATOM   17065 C  C      . ALA   F 4  354 ? 3.052   -59.418  74.748  1.00 62.57  ? 354 ALA   F C      1 
ATOM   17066 O  O      . ALA   F 4  354 ? 2.196   -60.160  74.257  1.00 64.96  ? 354 ALA   F O      1 
ATOM   17067 C  CB     . ALA   F 4  354 ? 2.388   -58.899  77.091  1.00 60.66  ? 354 ALA   F CB     1 
ATOM   17068 N  N      . ILE   F 4  355 ? 3.636   -58.464  74.044  1.00 65.13  ? 355 ILE   F N      1 
ATOM   17069 C  CA     . ILE   F 4  355 ? 3.227   -58.127  72.687  1.00 65.54  ? 355 ILE   F CA     1 
ATOM   17070 C  C      . ILE   F 4  355 ? 4.236   -58.624  71.660  1.00 63.86  ? 355 ILE   F C      1 
ATOM   17071 O  O      . ILE   F 4  355 ? 3.870   -59.298  70.698  1.00 60.58  ? 355 ILE   F O      1 
ATOM   17072 C  CB     . ILE   F 4  355 ? 2.974   -56.609  72.538  1.00 60.68  ? 355 ILE   F CB     1 
ATOM   17073 C  CG1    . ILE   F 4  355 ? 1.783   -56.172  73.408  1.00 63.30  ? 355 ILE   F CG1    1 
ATOM   17074 C  CG2    . ILE   F 4  355 ? 2.748   -56.254  71.093  1.00 63.18  ? 355 ILE   F CG2    1 
ATOM   17075 C  CD1    . ILE   F 4  355 ? 1.295   -54.755  73.158  1.00 57.18  ? 355 ILE   F CD1    1 
ATOM   17076 N  N      . SER   F 4  356 ? 5.517   -58.311  71.853  1.00 65.25  ? 356 SER   F N      1 
ATOM   17077 C  CA     . SER   F 4  356 ? 6.525   -58.779  70.908  1.00 63.16  ? 356 SER   F CA     1 
ATOM   17078 C  C      . SER   F 4  356 ? 6.860   -60.247  71.095  1.00 63.27  ? 356 SER   F C      1 
ATOM   17079 O  O      . SER   F 4  356 ? 7.269   -60.903  70.136  1.00 61.88  ? 356 SER   F O      1 
ATOM   17080 C  CB     . SER   F 4  356 ? 7.798   -57.941  71.022  1.00 66.86  ? 356 SER   F CB     1 
ATOM   17081 O  OG     . SER   F 4  356 ? 7.701   -56.761  70.236  1.00 77.38  ? 356 SER   F OG     1 
ATOM   17082 N  N      . SER   F 4  357 ? 6.699   -60.780  72.305  1.00 67.25  ? 357 SER   F N      1 
ATOM   17083 C  CA     . SER   F 4  357 ? 6.867   -62.213  72.502  1.00 61.36  ? 357 SER   F CA     1 
ATOM   17084 C  C      . SER   F 4  357 ? 6.077   -63.009  71.480  1.00 62.93  ? 357 SER   F C      1 
ATOM   17085 O  O      . SER   F 4  357 ? 6.505   -64.088  71.065  1.00 70.03  ? 357 SER   F O      1 
ATOM   17086 C  CB     . SER   F 4  357 ? 6.429   -62.588  73.909  1.00 67.46  ? 357 SER   F CB     1 
ATOM   17087 O  OG     . SER   F 4  357 ? 5.082   -62.200  74.100  1.00 77.37  ? 357 SER   F OG     1 
ATOM   17088 N  N      . VAL   F 4  358 ? 4.932   -62.486  71.058  1.00 67.08  ? 358 VAL   F N      1 
ATOM   17089 C  CA     . VAL   F 4  358 ? 4.055   -63.126  70.076  1.00 63.61  ? 358 VAL   F CA     1 
ATOM   17090 C  C      . VAL   F 4  358 ? 4.359   -62.659  68.662  1.00 57.22  ? 358 VAL   F C      1 
ATOM   17091 O  O      . VAL   F 4  358 ? 4.506   -63.473  67.758  1.00 60.76  ? 358 VAL   F O      1 
ATOM   17092 C  CB     . VAL   F 4  358 ? 2.574   -62.873  70.437  1.00 61.05  ? 358 VAL   F CB     1 
ATOM   17093 C  CG1    . VAL   F 4  358 ? 1.700   -63.314  69.313  1.00 57.72  ? 358 VAL   F CG1    1 
ATOM   17094 C  CG2    . VAL   F 4  358 ? 2.222   -63.613  71.712  1.00 52.97  ? 358 VAL   F CG2    1 
ATOM   17095 N  N      . PHE   F 4  359 ? 4.453   -61.346  68.450  1.00 62.06  ? 359 PHE   F N      1 
ATOM   17096 C  CA     . PHE   F 4  359 ? 4.682   -60.728  67.147  1.00 59.81  ? 359 PHE   F CA     1 
ATOM   17097 C  C      . PHE   F 4  359 ? 6.092   -60.158  67.042  1.00 62.58  ? 359 PHE   F C      1 
ATOM   17098 O  O      . PHE   F 4  359 ? 6.282   -58.955  67.266  1.00 68.38  ? 359 PHE   F O      1 
ATOM   17099 C  CB     . PHE   F 4  359 ? 3.647   -59.629  66.939  1.00 59.12  ? 359 PHE   F CB     1 
ATOM   17100 C  CG     . PHE   F 4  359 ? 2.245   -60.109  67.089  1.00 61.03  ? 359 PHE   F CG     1 
ATOM   17101 C  CD1    . PHE   F 4  359 ? 1.711   -61.012  66.192  1.00 57.35  ? 359 PHE   F CD1    1 
ATOM   17102 C  CD2    . PHE   F 4  359 ? 1.492   -59.735  68.189  1.00 62.15  ? 359 PHE   F CD2    1 
ATOM   17103 C  CE1    . PHE   F 4  359 ? 0.422   -61.467  66.342  1.00 61.71  ? 359 PHE   F CE1    1 
ATOM   17104 C  CE2    . PHE   F 4  359 ? 0.199   -60.201  68.356  1.00 61.97  ? 359 PHE   F CE2    1 
ATOM   17105 C  CZ     . PHE   F 4  359 ? -0.339  -61.067  67.433  1.00 60.03  ? 359 PHE   F CZ     1 
ATOM   17106 N  N      . PRO   F 4  360 ? 7.103   -60.979  66.727  1.00 61.95  ? 360 PRO   F N      1 
ATOM   17107 C  CA     . PRO   F 4  360 ? 8.494   -60.503  66.794  1.00 59.65  ? 360 PRO   F CA     1 
ATOM   17108 C  C      . PRO   F 4  360 ? 8.878   -59.585  65.648  1.00 68.70  ? 360 PRO   F C      1 
ATOM   17109 O  O      . PRO   F 4  360 ? 8.378   -59.697  64.528  1.00 71.88  ? 360 PRO   F O      1 
ATOM   17110 C  CB     . PRO   F 4  360 ? 9.315   -61.796  66.763  1.00 57.43  ? 360 PRO   F CB     1 
ATOM   17111 C  CG     . PRO   F 4  360 ? 8.420   -62.815  66.172  1.00 61.07  ? 360 PRO   F CG     1 
ATOM   17112 C  CD     . PRO   F 4  360 ? 7.028   -62.442  66.566  1.00 58.79  ? 360 PRO   F CD     1 
ATOM   17113 N  N      . LEU   F 4  361 ? 9.806   -58.674  65.948  1.00 79.14  ? 361 LEU   F N      1 
ATOM   17114 C  CA     . LEU   F 4  361 ? 10.190  -57.597  65.039  1.00 81.14  ? 361 LEU   F CA     1 
ATOM   17115 C  C      . LEU   F 4  361 ? 11.513  -57.872  64.325  1.00 84.67  ? 361 LEU   F C      1 
ATOM   17116 O  O      . LEU   F 4  361 ? 11.764  -58.999  63.880  1.00 84.88  ? 361 LEU   F O      1 
ATOM   17117 C  CB     . LEU   F 4  361 ? 10.285  -56.281  65.808  1.00 75.29  ? 361 LEU   F CB     1 
ATOM   17118 C  CG     . LEU   F 4  361 ? 9.122   -56.008  66.749  1.00 69.91  ? 361 LEU   F CG     1 
ATOM   17119 C  CD1    . LEU   F 4  361 ? 9.575   -55.039  67.807  1.00 72.16  ? 361 LEU   F CD1    1 
ATOM   17120 C  CD2    . LEU   F 4  361 ? 7.919   -55.470  66.000  1.00 79.22  ? 361 LEU   F CD2    1 
ATOM   17121 N  N      . ALA   F 4  362 ? 12.361  -56.845  64.223  1.00 84.10  ? 362 ALA   F N      1 
ATOM   17122 C  CA     . ALA   F 4  362 ? 13.595  -56.905  63.440  1.00 91.99  ? 362 ALA   F CA     1 
ATOM   17123 C  C      . ALA   F 4  362 ? 14.775  -57.557  64.186  1.00 95.37  ? 362 ALA   F C      1 
ATOM   17124 O  O      . ALA   F 4  362 ? 15.810  -57.900  63.589  1.00 87.40  ? 362 ALA   F O      1 
ATOM   17125 C  CB     . ALA   F 4  362 ? 13.970  -55.512  62.996  1.00 89.02  ? 362 ALA   F CB     1 
ATOM   17126 N  N      . THR   F 4  372 ? 18.754  -57.481  84.004  1.00 99.26  ? 372 THR   F N      1 
ATOM   17127 C  CA     . THR   F 4  372 ? 18.346  -57.061  82.669  1.00 104.97 ? 372 THR   F CA     1 
ATOM   17128 C  C      . THR   F 4  372 ? 16.873  -56.634  82.692  1.00 108.58 ? 372 THR   F C      1 
ATOM   17129 O  O      . THR   F 4  372 ? 16.563  -55.448  82.538  1.00 105.41 ? 372 THR   F O      1 
ATOM   17130 C  CB     . THR   F 4  372 ? 18.560  -58.190  81.620  1.00 107.16 ? 372 THR   F CB     1 
ATOM   17131 O  OG1    . THR   F 4  372 ? 19.952  -58.518  81.542  1.00 107.79 ? 372 THR   F OG1    1 
ATOM   17132 C  CG2    . THR   F 4  372 ? 18.092  -57.747  80.237  1.00 99.40  ? 372 THR   F CG2    1 
ATOM   17133 N  N      . SER   F 4  373 ? 15.976  -57.601  82.912  1.00 104.09 ? 373 SER   F N      1 
ATOM   17134 C  CA     . SER   F 4  373 ? 14.537  -57.362  82.850  1.00 87.68  ? 373 SER   F CA     1 
ATOM   17135 C  C      . SER   F 4  373 ? 14.060  -56.437  83.968  1.00 82.95  ? 373 SER   F C      1 
ATOM   17136 O  O      . SER   F 4  373 ? 14.731  -56.247  84.991  1.00 88.15  ? 373 SER   F O      1 
ATOM   17137 C  CB     . SER   F 4  373 ? 13.765  -58.677  82.933  1.00 86.23  ? 373 SER   F CB     1 
ATOM   17138 O  OG     . SER   F 4  373 ? 12.375  -58.445  82.773  1.00 81.58  ? 373 SER   F OG     1 
ATOM   17139 N  N      . ILE   F 4  374 ? 12.866  -55.867  83.759  1.00 79.00  ? 374 ILE   F N      1 
ATOM   17140 C  CA     . ILE   F 4  374 ? 12.199  -55.022  84.752  1.00 75.37  ? 374 ILE   F CA     1 
ATOM   17141 C  C      . ILE   F 4  374 ? 11.166  -55.860  85.490  1.00 74.15  ? 374 ILE   F C      1 
ATOM   17142 O  O      . ILE   F 4  374 ? 10.331  -55.330  86.242  1.00 67.88  ? 374 ILE   F O      1 
ATOM   17143 C  CB     . ILE   F 4  374 ? 11.508  -53.796  84.128  1.00 69.36  ? 374 ILE   F CB     1 
ATOM   17144 C  CG1    . ILE   F 4  374 ? 10.147  -54.218  83.587  1.00 66.57  ? 374 ILE   F CG1    1 
ATOM   17145 C  CG2    . ILE   F 4  374 ? 12.381  -53.162  83.068  1.00 72.72  ? 374 ILE   F CG2    1 
ATOM   17146 C  CD1    . ILE   F 4  374 ? 9.273   -53.088  83.128  1.00 66.04  ? 374 ILE   F CD1    1 
ATOM   17147 N  N      . PHE   F 4  375 ? 11.193  -57.171  85.256  1.00 70.48  ? 375 PHE   F N      1 
ATOM   17148 C  CA     . PHE   F 4  375 ? 10.199  -58.063  85.823  1.00 66.26  ? 375 PHE   F CA     1 
ATOM   17149 C  C      . PHE   F 4  375 ? 10.835  -59.190  86.617  1.00 64.38  ? 375 PHE   F C      1 
ATOM   17150 O  O      . PHE   F 4  375 ? 11.927  -59.667  86.300  1.00 66.56  ? 375 PHE   F O      1 
ATOM   17151 C  CB     . PHE   F 4  375 ? 9.303   -58.674  84.760  1.00 67.46  ? 375 PHE   F CB     1 
ATOM   17152 C  CG     . PHE   F 4  375 ? 8.388   -57.702  84.094  1.00 62.99  ? 375 PHE   F CG     1 
ATOM   17153 C  CD1    . PHE   F 4  375 ? 7.306   -57.191  84.775  1.00 62.62  ? 375 PHE   F CD1    1 
ATOM   17154 C  CD2    . PHE   F 4  375 ? 8.547   -57.374  82.772  1.00 59.25  ? 375 PHE   F CD2    1 
ATOM   17155 C  CE1    . PHE   F 4  375 ? 6.433   -56.328  84.162  1.00 63.07  ? 375 PHE   F CE1    1 
ATOM   17156 C  CE2    . PHE   F 4  375 ? 7.668   -56.514  82.159  1.00 63.01  ? 375 PHE   F CE2    1 
ATOM   17157 C  CZ     . PHE   F 4  375 ? 6.609   -55.991  82.857  1.00 60.77  ? 375 PHE   F CZ     1 
ATOM   17158 N  N      . ILE   F 4  376 ? 10.124  -59.590  87.665  1.00 63.02  ? 376 ILE   F N      1 
ATOM   17159 C  CA     . ILE   F 4  376 ? 10.439  -60.771  88.448  1.00 58.51  ? 376 ILE   F CA     1 
ATOM   17160 C  C      . ILE   F 4  376 ? 9.499   -61.855  87.957  1.00 61.84  ? 376 ILE   F C      1 
ATOM   17161 O  O      . ILE   F 4  376 ? 8.279   -61.675  87.990  1.00 64.52  ? 376 ILE   F O      1 
ATOM   17162 C  CB     . ILE   F 4  376 ? 10.236  -60.512  89.946  1.00 57.72  ? 376 ILE   F CB     1 
ATOM   17163 C  CG1    . ILE   F 4  376 ? 10.873  -59.187  90.353  1.00 62.98  ? 376 ILE   F CG1    1 
ATOM   17164 C  CG2    . ILE   F 4  376 ? 10.852  -61.625  90.755  1.00 57.20  ? 376 ILE   F CG2    1 
ATOM   17165 C  CD1    . ILE   F 4  376 ? 10.529  -58.778  91.793  1.00 70.37  ? 376 ILE   F CD1    1 
ATOM   17166 N  N      . LYS   F 4  377 ? 10.042  -62.953  87.452  1.00 63.57  ? 377 LYS   F N      1 
ATOM   17167 C  CA     . LYS   F 4  377 ? 9.214   -64.079  87.047  1.00 56.51  ? 377 LYS   F CA     1 
ATOM   17168 C  C      . LYS   F 4  377 ? 8.836   -64.861  88.295  1.00 58.68  ? 377 LYS   F C      1 
ATOM   17169 O  O      . LYS   F 4  377 ? 9.712   -65.403  88.975  1.00 72.61  ? 377 LYS   F O      1 
ATOM   17170 C  CB     . LYS   F 4  377 ? 9.978   -64.948  86.054  1.00 60.89  ? 377 LYS   F CB     1 
ATOM   17171 C  CG     . LYS   F 4  377 ? 9.158   -66.001  85.321  1.00 67.51  ? 377 LYS   F CG     1 
ATOM   17172 C  CD     . LYS   F 4  377 ? 10.034  -66.773  84.315  1.00 75.86  ? 377 LYS   F CD     1 
ATOM   17173 C  CE     . LYS   F 4  377 ? 9.229   -67.742  83.454  1.00 75.66  ? 377 LYS   F CE     1 
ATOM   17174 N  NZ     . LYS   F 4  377 ? 9.930   -68.174  82.211  1.00 72.15  ? 377 LYS   F NZ     1 
ATOM   17175 N  N      . LEU   F 4  378 ? 7.550   -64.896  88.629  1.00 53.51  ? 378 LEU   F N      1 
ATOM   17176 C  CA     . LEU   F 4  378 ? 7.079   -65.676  89.773  1.00 63.56  ? 378 LEU   F CA     1 
ATOM   17177 C  C      . LEU   F 4  378 ? 6.850   -67.127  89.342  1.00 76.18  ? 378 LEU   F C      1 
ATOM   17178 O  O      . LEU   F 4  378 ? 5.978   -67.408  88.507  1.00 78.48  ? 378 LEU   F O      1 
ATOM   17179 C  CB     . LEU   F 4  378 ? 5.815   -65.065  90.386  1.00 59.78  ? 378 LEU   F CB     1 
ATOM   17180 C  CG     . LEU   F 4  378 ? 5.811   -63.566  90.721  1.00 53.24  ? 378 LEU   F CG     1 
ATOM   17181 C  CD1    . LEU   F 4  378 ? 4.589   -63.191  91.527  1.00 48.00  ? 378 LEU   F CD1    1 
ATOM   17182 C  CD2    . LEU   F 4  378 ? 7.035   -63.231  91.509  1.00 47.72  ? 378 LEU   F CD2    1 
ATOM   17183 N  N      . HIS   F 4  379 ? 7.633   -68.046  89.914  1.00 80.68  ? 379 HIS   F N      1 
ATOM   17184 C  CA     . HIS   F 4  379 ? 7.771   -69.390  89.363  1.00 84.70  ? 379 HIS   F CA     1 
ATOM   17185 C  C      . HIS   F 4  379 ? 6.693   -70.329  89.901  1.00 97.09  ? 379 HIS   F C      1 
ATOM   17186 O  O      . HIS   F 4  379 ? 6.427   -70.364  91.108  1.00 98.55  ? 379 HIS   F O      1 
ATOM   17187 C  CB     . HIS   F 4  379 ? 9.163   -69.955  89.660  1.00 89.41  ? 379 HIS   F CB     1 
ATOM   17188 C  CG     . HIS   F 4  379 ? 10.215  -69.487  88.697  1.00 91.70  ? 379 HIS   F CG     1 
ATOM   17189 N  ND1    . HIS   F 4  379 ? 11.486  -69.125  89.095  1.00 95.23  ? 379 HIS   F ND1    1 
ATOM   17190 C  CD2    . HIS   F 4  379 ? 10.167  -69.276  87.359  1.00 89.80  ? 379 HIS   F CD2    1 
ATOM   17191 C  CE1    . HIS   F 4  379 ? 12.182  -68.738  88.040  1.00 93.31  ? 379 HIS   F CE1    1 
ATOM   17192 N  NE2    . HIS   F 4  379 ? 11.405  -68.818  86.975  1.00 90.75  ? 379 HIS   F NE2    1 
ATOM   17193 N  N      . HIS   F 4  380 ? 6.087   -71.095  88.995  1.00 98.86  ? 380 HIS   F N      1 
ATOM   17194 C  CA     . HIS   F 4  380 ? 5.015   -72.029  89.331  1.00 96.20  ? 380 HIS   F CA     1 
ATOM   17195 C  C      . HIS   F 4  380 ? 5.230   -73.365  88.600  1.00 103.66 ? 380 HIS   F C      1 
ATOM   17196 O  O      . HIS   F 4  380 ? 4.465   -74.325  88.757  1.00 105.48 ? 380 HIS   F O      1 
ATOM   17197 C  CB     . HIS   F 4  380 ? 3.658   -71.423  88.966  1.00 93.30  ? 380 HIS   F CB     1 
ATOM   17198 C  CG     . HIS   F 4  380 ? 3.625   -70.782  87.608  1.00 92.36  ? 380 HIS   F CG     1 
ATOM   17199 N  ND1    . HIS   F 4  380 ? 3.069   -71.402  86.507  1.00 86.57  ? 380 HIS   F ND1    1 
ATOM   17200 C  CD2    . HIS   F 4  380 ? 4.102   -69.592  87.169  1.00 84.01  ? 380 HIS   F CD2    1 
ATOM   17201 C  CE1    . HIS   F 4  380 ? 3.179   -70.610  85.456  1.00 79.88  ? 380 HIS   F CE1    1 
ATOM   17202 N  NE2    . HIS   F 4  380 ? 3.809   -69.509  85.828  1.00 79.87  ? 380 HIS   F NE2    1 
HETATM 17203 P  PG     . GTP   G 5  .   ? -27.300 -73.591  46.320  0.00 42.82  ? 501 GTP   A PG     1 
HETATM 17204 O  O1G    . GTP   G 5  .   ? -27.059 -72.125  46.590  0.00 41.86  ? 501 GTP   A O1G    1 
HETATM 17205 O  O2G    . GTP   G 5  .   ? -26.097 -74.186  45.629  0.00 45.36  ? 501 GTP   A O2G    1 
HETATM 17206 O  O3G    . GTP   G 5  .   ? -28.519 -73.753  45.444  0.00 42.44  ? 501 GTP   A O3G    1 
HETATM 17207 O  O3B    . GTP   G 5  .   ? -27.539 -74.338  47.727  0.00 43.18  ? 501 GTP   A O3B    1 
HETATM 17208 P  PB     . GTP   G 5  .   ? -26.529 -75.494  48.216  0.00 43.53  ? 501 GTP   A PB     1 
HETATM 17209 O  O1B    . GTP   G 5  .   ? -27.133 -76.197  49.407  0.00 43.47  ? 501 GTP   A O1B    1 
HETATM 17210 O  O2B    . GTP   G 5  .   ? -26.231 -76.468  47.102  0.00 45.21  ? 501 GTP   A O2B    1 
HETATM 17211 O  O3A    . GTP   G 5  .   ? -25.197 -74.707  48.666  0.00 43.74  ? 501 GTP   A O3A    1 
HETATM 17212 P  PA     . GTP   G 5  .   ? -24.145 -75.391  49.678  0.00 43.56  ? 501 GTP   A PA     1 
HETATM 17213 O  O1A    . GTP   G 5  .   ? -24.710 -76.689  50.203  0.00 43.58  ? 501 GTP   A O1A    1 
HETATM 17214 O  O2A    . GTP   G 5  .   ? -22.826 -75.624  48.980  0.00 44.29  ? 501 GTP   A O2A    1 
HETATM 17215 O  "O5'"  . GTP   G 5  .   ? -23.975 -74.333  50.883  0.00 43.18  ? 501 GTP   A "O5'"  1 
HETATM 17216 C  "C5'"  . GTP   G 5  .   ? -22.861 -73.468  50.950  0.00 45.21  ? 501 GTP   A "C5'"  1 
HETATM 17217 C  "C4'"  . GTP   G 5  .   ? -21.993 -73.817  52.154  0.00 45.75  ? 501 GTP   A "C4'"  1 
HETATM 17218 O  "O4'"  . GTP   G 5  .   ? -22.006 -75.214  52.359  0.00 44.26  ? 501 GTP   A "O4'"  1 
HETATM 17219 C  "C3'"  . GTP   G 5  .   ? -20.544 -73.409  51.940  0.00 49.62  ? 501 GTP   A "C3'"  1 
HETATM 17220 O  "O3'"  . GTP   G 5  .   ? -20.176 -72.428  52.881  0.00 49.70  ? 501 GTP   A "O3'"  1 
HETATM 17221 C  "C2'"  . GTP   G 5  .   ? -19.727 -74.665  52.172  0.00 47.32  ? 501 GTP   A "C2'"  1 
HETATM 17222 O  "O2'"  . GTP   G 5  .   ? -18.703 -74.431  53.110  0.00 46.34  ? 501 GTP   A "O2'"  1 
HETATM 17223 C  "C1'"  . GTP   G 5  .   ? -20.719 -75.690  52.698  0.00 44.30  ? 501 GTP   A "C1'"  1 
HETATM 17224 N  N9     . GTP   G 5  .   ? -20.505 -76.996  52.054  0.00 44.27  ? 501 GTP   A N9     1 
HETATM 17225 C  C8     . GTP   G 5  .   ? -20.809 -77.326  50.759  0.00 44.71  ? 501 GTP   A C8     1 
HETATM 17226 N  N7     . GTP   G 5  .   ? -20.472 -78.620  50.558  0.00 44.57  ? 501 GTP   A N7     1 
HETATM 17227 C  C5     . GTP   G 5  .   ? -19.967 -79.122  51.706  0.00 44.42  ? 501 GTP   A C5     1 
HETATM 17228 C  C6     . GTP   G 5  .   ? -19.479 -80.377  52.045  0.00 44.55  ? 501 GTP   A C6     1 
HETATM 17229 O  O6     . GTP   G 5  .   ? -19.459 -81.278  51.208  0.00 45.61  ? 501 GTP   A O6     1 
HETATM 17230 N  N1     . GTP   G 5  .   ? -19.016 -80.606  53.324  0.00 44.15  ? 501 GTP   A N1     1 
HETATM 17231 C  C2     . GTP   G 5  .   ? -19.042 -79.589  54.257  0.00 42.29  ? 501 GTP   A C2     1 
HETATM 17232 N  N2     . GTP   G 5  .   ? -18.597 -79.809  55.491  0.00 41.82  ? 501 GTP   A N2     1 
HETATM 17233 N  N3     . GTP   G 5  .   ? -19.529 -78.344  53.913  0.00 42.19  ? 501 GTP   A N3     1 
HETATM 17234 C  C4     . GTP   G 5  .   ? -19.984 -78.112  52.658  0.00 43.63  ? 501 GTP   A C4     1 
HETATM 17235 CA CA     . CA    H 6  .   ? -33.729 -108.491 58.904  0.00 75.18  ? 502 CA    A CA     1 
HETATM 17236 MG MG     . MG    I 7  .   ? -25.666 -76.749  44.729  0.00 49.88  ? 503 MG    A MG     1 
HETATM 17237 N  N12    . A1D6L J 8  .   ? -17.987 -66.549  41.730  1.00 38.86  ? 501 A1D6L B N12    1 
HETATM 17238 C  C13    . A1D6L J 8  .   ? -17.787 -65.642  42.877  1.00 37.41  ? 501 A1D6L B C13    1 
HETATM 17239 C  C15    . A1D6L J 8  .   ? -19.049 -67.398  44.229  1.00 47.12  ? 501 A1D6L B C15    1 
HETATM 17240 C  C17    . A1D6L J 8  .   ? -19.156 -67.362  41.655  1.00 41.78  ? 501 A1D6L B C17    1 
HETATM 17241 C  C20    . A1D6L J 8  .   ? -16.919 -63.606  43.934  1.00 41.28  ? 501 A1D6L B C20    1 
HETATM 17242 C  C21    . A1D6L J 8  .   ? -17.097 -64.410  42.792  1.00 41.00  ? 501 A1D6L B C21    1 
HETATM 17243 C  C01    . A1D6L J 8  .   ? -13.627 -66.299  42.035  1.00 49.25  ? 501 A1D6L B C01    1 
HETATM 17244 C  C02    . A1D6L J 8  .   ? -12.865 -66.199  40.874  1.00 52.40  ? 501 A1D6L B C02    1 
HETATM 17245 C  C03    . A1D6L J 8  .   ? -13.502 -66.197  39.639  1.00 53.31  ? 501 A1D6L B C03    1 
HETATM 17246 C  C04    . A1D6L J 8  .   ? -14.923 -66.281  39.573  1.00 47.64  ? 501 A1D6L B C04    1 
HETATM 17247 C  C05    . A1D6L J 8  .   ? -15.686 -66.374  40.708  1.00 47.35  ? 501 A1D6L B C05    1 
HETATM 17248 C  C06    . A1D6L J 8  .   ? -15.020 -66.394  41.973  1.00 44.28  ? 501 A1D6L B C06    1 
HETATM 17249 C  C07    . A1D6L J 8  .   ? -17.116 -66.461  40.570  1.00 46.18  ? 501 A1D6L B C07    1 
HETATM 17250 C  C09    . A1D6L J 8  .   ? -16.838 -66.372  38.268  1.00 50.18  ? 501 A1D6L B C09    1 
HETATM 17251 C  C14    . A1D6L J 8  .   ? -18.290 -66.041  44.115  1.00 42.02  ? 501 A1D6L B C14    1 
HETATM 17252 C  C16    . A1D6L J 8  .   ? -19.763 -67.834  42.957  1.00 48.69  ? 501 A1D6L B C16    1 
HETATM 17253 C  C18    . A1D6L J 8  .   ? -18.111 -65.248  45.261  1.00 41.62  ? 501 A1D6L B C18    1 
HETATM 17254 C  C19    . A1D6L J 8  .   ? -17.426 -64.033  45.186  1.00 42.88  ? 501 A1D6L B C19    1 
HETATM 17255 C  C23    . A1D6L J 8  .   ? -17.754 -61.970  46.301  1.00 49.86  ? 501 A1D6L B C23    1 
HETATM 17256 F  F24    . A1D6L J 8  .   ? -12.981 -66.322  43.232  1.00 46.57  ? 501 A1D6L B F24    1 
HETATM 17257 N  N08    . A1D6L J 8  .   ? -17.644 -66.466  39.341  1.00 45.09  ? 501 A1D6L B N08    1 
HETATM 17258 N  N10    . A1D6L J 8  .   ? -15.515 -66.288  38.358  1.00 49.39  ? 501 A1D6L B N10    1 
HETATM 17259 N  N11    . A1D6L J 8  .   ? -17.370 -66.361  36.919  1.00 48.22  ? 501 A1D6L B N11    1 
HETATM 17260 O  O22    . A1D6L J 8  .   ? -17.272 -63.280  46.355  1.00 45.73  ? 501 A1D6L B O22    1 
HETATM 17261 H  H151   . A1D6L J 8  .   ? -18.332 -68.167  44.498  1.00 56.55  ? 501 A1D6L B H151   1 
HETATM 17262 H  H152   . A1D6L J 8  .   ? -19.787 -67.309  45.020  1.00 56.55  ? 501 A1D6L B H152   1 
HETATM 17263 H  H172   . A1D6L J 8  .   ? -18.888 -68.249  41.091  1.00 50.14  ? 501 A1D6L B H172   1 
HETATM 17264 H  H171   . A1D6L J 8  .   ? -19.915 -66.778  41.145  1.00 50.14  ? 501 A1D6L B H171   1 
HETATM 17265 H  H201   . A1D6L J 8  .   ? -16.394 -62.662  43.856  1.00 49.53  ? 501 A1D6L B H201   1 
HETATM 17266 H  H211   . A1D6L J 8  .   ? -16.703 -64.081  41.838  1.00 49.20  ? 501 A1D6L B H211   1 
HETATM 17267 H  H021   . A1D6L J 8  .   ? -11.785 -66.123  40.933  1.00 62.89  ? 501 A1D6L B H021   1 
HETATM 17268 H  H031   . A1D6L J 8  .   ? -12.920 -66.131  38.727  1.00 63.97  ? 501 A1D6L B H031   1 
HETATM 17269 H  H061   . A1D6L J 8  .   ? -15.597 -66.483  42.886  1.00 53.14  ? 501 A1D6L B H061   1 
HETATM 17270 H  H161   . A1D6L J 8  .   ? -19.780 -68.919  42.941  1.00 58.43  ? 501 A1D6L B H161   1 
HETATM 17271 H  H162   . A1D6L J 8  .   ? -20.781 -67.463  43.003  1.00 58.43  ? 501 A1D6L B H162   1 
HETATM 17272 H  H181   . A1D6L J 8  .   ? -18.509 -65.582  46.212  1.00 49.95  ? 501 A1D6L B H181   1 
HETATM 17273 H  H231   . A1D6L J 8  .   ? -18.077 -61.662  47.291  1.00 59.83  ? 501 A1D6L B H231   1 
HETATM 17274 H  H232   . A1D6L J 8  .   ? -18.594 -61.922  45.614  1.00 59.83  ? 501 A1D6L B H232   1 
HETATM 17275 H  H233   . A1D6L J 8  .   ? -16.965 -61.308  45.955  1.00 59.83  ? 501 A1D6L B H233   1 
HETATM 17276 H  H112   . A1D6L J 8  .   ? -16.742 -66.394  36.135  1.00 57.86  ? 501 A1D6L B H112   1 
HETATM 17277 H  H111   . A1D6L J 8  .   ? -18.361 -66.329  36.775  1.00 57.86  ? 501 A1D6L B H111   1 
HETATM 17278 P  PB     . GDP   K 9  .   ? -18.743 -49.286  15.674  0.00 35.37  ? 502 GDP   B PB     1 
HETATM 17279 O  O1B    . GDP   K 9  .   ? -18.244 -50.221  14.598  0.00 37.34  ? 502 GDP   B O1B    1 
HETATM 17280 O  O2B    . GDP   K 9  .   ? -19.228 -50.074  16.867  0.00 34.99  ? 502 GDP   B O2B    1 
HETATM 17281 O  O3B    . GDP   K 9  .   ? -19.882 -48.466  15.116  0.00 34.39  ? 502 GDP   B O3B    1 
HETATM 17282 O  O3A    . GDP   K 9  .   ? -17.558 -48.293  16.120  0.00 36.31  ? 502 GDP   B O3A    1 
HETATM 17283 P  PA     . GDP   K 9  .   ? -16.286 -48.837  16.943  0.00 37.34  ? 502 GDP   B PA     1 
HETATM 17284 O  O1A    . GDP   K 9  .   ? -15.064 -48.893  16.061  0.00 39.65  ? 502 GDP   B O1A    1 
HETATM 17285 O  O2A    . GDP   K 9  .   ? -16.569 -50.199  17.530  0.00 36.71  ? 502 GDP   B O2A    1 
HETATM 17286 O  "O5'"  . GDP   K 9  .   ? -16.067 -47.735  18.096  0.00 36.24  ? 502 GDP   B "O5'"  1 
HETATM 17287 C  "C5'"  . GDP   K 9  .   ? -14.872 -46.958  18.105  0.00 37.96  ? 502 GDP   B "C5'"  1 
HETATM 17288 C  "C4'"  . GDP   K 9  .   ? -14.267 -46.934  19.501  0.00 37.24  ? 502 GDP   B "C4'"  1 
HETATM 17289 O  "O4'"  . GDP   K 9  .   ? -13.931 -48.275  19.856  0.00 36.36  ? 502 GDP   B "O4'"  1 
HETATM 17290 C  "C3'"  . GDP   K 9  .   ? -12.983 -46.123  19.511  0.00 39.21  ? 502 GDP   B "C3'"  1 
HETATM 17291 O  "O3'"  . GDP   K 9  .   ? -12.962 -45.249  20.644  0.00 39.23  ? 502 GDP   B "O3'"  1 
HETATM 17292 C  "C2'"  . GDP   K 9  .   ? -11.862 -47.135  19.622  0.00 37.61  ? 502 GDP   B "C2'"  1 
HETATM 17293 O  "O2'"  . GDP   K 9  .   ? -10.877 -46.693  20.560  0.00 37.53  ? 502 GDP   B "O2'"  1 
HETATM 17294 C  "C1'"  . GDP   K 9  .   ? -12.530 -48.411  20.105  0.00 35.70  ? 502 GDP   B "C1'"  1 
HETATM 17295 N  N9     . GDP   K 9  .   ? -12.012 -49.586  19.363  0.00 35.21  ? 502 GDP   B N9     1 
HETATM 17296 C  C8     . GDP   K 9  .   ? -12.274 -49.885  18.077  0.00 35.73  ? 502 GDP   B C8     1 
HETATM 17297 N  N7     . GDP   K 9  .   ? -11.651 -51.033  17.705  0.00 35.47  ? 502 GDP   B N7     1 
HETATM 17298 C  C5     . GDP   K 9  .   ? -10.976 -51.489  18.776  0.00 35.59  ? 502 GDP   B C5     1 
HETATM 17299 C  C6     . GDP   K 9  .   ? -10.109 -52.651  19.076  0.00 37.31  ? 502 GDP   B C6     1 
HETATM 17300 O  O6     . GDP   K 9  .   ? -9.856  -53.507  18.201  0.00 40.12  ? 502 GDP   B O6     1 
HETATM 17301 N  N1     . GDP   K 9  .   ? -9.606  -52.757  20.313  0.00 38.56  ? 502 GDP   B N1     1 
HETATM 17302 C  C2     . GDP   K 9  .   ? -9.862  -51.850  21.276  0.00 36.86  ? 502 GDP   B C2     1 
HETATM 17303 N  N2     . GDP   K 9  .   ? -9.314  -52.031  22.501  0.00 38.28  ? 502 GDP   B N2     1 
HETATM 17304 N  N3     . GDP   K 9  .   ? -10.647 -50.762  21.071  0.00 35.23  ? 502 GDP   B N3     1 
HETATM 17305 C  C4     . GDP   K 9  .   ? -11.220 -50.534  19.866  0.00 34.72  ? 502 GDP   B C4     1 
HETATM 17306 O  O1     . MES   L 10 .   ? -30.726 -56.317  33.714  0.00 40.92  ? 503 MES   B O1     1 
HETATM 17307 C  C2     . MES   L 10 .   ? -30.308 -57.442  32.945  0.00 40.20  ? 503 MES   B C2     1 
HETATM 17308 C  C3     . MES   L 10 .   ? -31.151 -58.675  33.259  0.00 40.27  ? 503 MES   B C3     1 
HETATM 17309 N  N4     . MES   L 10 .   ? -31.213 -58.837  34.705  0.00 40.52  ? 503 MES   B N4     1 
HETATM 17310 C  C5     . MES   L 10 .   ? -31.596 -57.684  35.506  0.00 40.81  ? 503 MES   B C5     1 
HETATM 17311 C  C6     . MES   L 10 .   ? -30.642 -56.564  35.114  0.00 40.72  ? 503 MES   B C6     1 
HETATM 17312 C  C7     . MES   L 10 .   ? -31.698 -60.127  35.171  0.00 40.66  ? 503 MES   B C7     1 
HETATM 17313 C  C8     . MES   L 10 .   ? -31.560 -60.105  36.689  0.00 40.18  ? 503 MES   B C8     1 
HETATM 17314 S  S      . MES   L 10 .   ? -32.316 -61.450  37.306  0.00 40.77  ? 503 MES   B S      1 
HETATM 17315 O  O1S    . MES   L 10 .   ? -32.175 -62.564  36.342  0.00 41.47  ? 503 MES   B O1S    1 
HETATM 17316 O  O2S    . MES   L 10 .   ? -33.751 -61.168  37.539  0.00 41.50  ? 503 MES   B O2S    1 
HETATM 17317 O  O3S    . MES   L 10 .   ? -31.674 -61.831  38.583  0.00 39.65  ? 503 MES   B O3S    1 
HETATM 17318 O  O1     . MES   M 10 .   ? -4.678  -53.178  48.499  0.00 62.71  ? 504 MES   B O1     1 
HETATM 17319 C  C2     . MES   M 10 .   ? -3.979  -54.134  47.705  0.00 63.19  ? 504 MES   B C2     1 
HETATM 17320 C  C3     . MES   M 10 .   ? -2.636  -53.585  47.233  0.00 65.61  ? 504 MES   B C3     1 
HETATM 17321 N  N4     . MES   M 10 .   ? -2.860  -52.268  46.650  0.00 64.33  ? 504 MES   B N4     1 
HETATM 17322 C  C5     . MES   M 10 .   ? -3.626  -51.292  47.410  0.00 63.83  ? 504 MES   B C5     1 
HETATM 17323 C  C6     . MES   M 10 .   ? -4.934  -51.974  47.784  0.00 63.60  ? 504 MES   B C6     1 
HETATM 17324 C  C7     . MES   M 10 .   ? -1.788  -51.737  45.822  0.00 64.96  ? 504 MES   B C7     1 
HETATM 17325 C  C8     . MES   M 10 .   ? -2.461  -51.070  44.628  0.00 62.10  ? 504 MES   B C8     1 
HETATM 17326 S  S      . MES   M 10 .   ? -1.373  -50.035  43.915  0.00 61.43  ? 504 MES   B S      1 
HETATM 17327 O  O1S    . MES   M 10 .   ? -1.978  -48.691  43.783  0.00 61.31  ? 504 MES   B O1S    1 
HETATM 17328 O  O2S    . MES   M 10 .   ? -1.030  -50.538  42.567  0.00 60.86  ? 504 MES   B O2S    1 
HETATM 17329 O  O3S    . MES   M 10 .   ? -0.154  -49.945  44.750  0.00 63.85  ? 504 MES   B O3S    1 
HETATM 17330 MG MG     . MG    N 7  .   ? -14.089 -47.261  14.255  0.00 46.11  ? 505 MG    B MG     1 
HETATM 17331 P  PG     . GTP   O 5  .   ? -20.476 -18.430  -16.774 0.00 32.74  ? 501 GTP   C PG     1 
HETATM 17332 O  O1G    . GTP   O 5  .   ? -20.407 -17.011  -16.262 0.00 33.23  ? 501 GTP   C O1G    1 
HETATM 17333 O  O2G    . GTP   O 5  .   ? -21.859 -18.691  -17.321 0.00 32.81  ? 501 GTP   C O2G    1 
HETATM 17334 O  O3G    . GTP   O 5  .   ? -19.442 -18.633  -17.856 0.00 35.07  ? 501 GTP   C O3G    1 
HETATM 17335 O  O3B    . GTP   O 5  .   ? -20.187 -19.430  -15.546 0.00 30.84  ? 501 GTP   C O3B    1 
HETATM 17336 P  PB     . GTP   O 5  .   ? -18.807 -20.256  -15.470 0.00 30.77  ? 501 GTP   C PB     1 
HETATM 17337 O  O1B    . GTP   O 5  .   ? -18.900 -21.239  -14.327 0.00 30.12  ? 501 GTP   C O1B    1 
HETATM 17338 O  O2B    . GTP   O 5  .   ? -18.534 -20.967  -16.773 0.00 31.75  ? 501 GTP   C O2B    1 
HETATM 17339 O  O3A    . GTP   O 5  .   ? -17.662 -19.165  -15.156 0.00 31.85  ? 501 GTP   C O3A    1 
HETATM 17340 P  PA     . GTP   O 5  .   ? -16.304 -19.592  -14.397 0.00 31.87  ? 501 GTP   C PA     1 
HETATM 17341 O  O1A    . GTP   O 5  .   ? -16.379 -21.040  -13.975 0.00 31.01  ? 501 GTP   C O1A    1 
HETATM 17342 O  O2A    . GTP   O 5  .   ? -15.106 -19.358  -15.287 0.00 33.20  ? 501 GTP   C O2A    1 
HETATM 17343 O  "O5'"  . GTP   O 5  .   ? -16.246 -18.646  -13.093 0.00 32.83  ? 501 GTP   C "O5'"  1 
HETATM 17344 C  "C5'"  . GTP   O 5  .   ? -15.303 -17.601  -12.987 0.00 34.93  ? 501 GTP   C "C5'"  1 
HETATM 17345 C  "C4'"  . GTP   O 5  .   ? -14.221 -17.958  -11.972 0.00 35.63  ? 501 GTP   C "C4'"  1 
HETATM 17346 O  "O4'"  . GTP   O 5  .   ? -13.809 -19.298  -12.153 0.00 35.03  ? 501 GTP   C "O4'"  1 
HETATM 17347 C  "C3'"  . GTP   O 5  .   ? -12.986 -17.086  -12.132 0.00 39.18  ? 501 GTP   C "C3'"  1 
HETATM 17348 O  "O3'"  . GTP   O 5  .   ? -12.765 -16.359  -10.946 0.00 39.37  ? 501 GTP   C "O3'"  1 
HETATM 17349 C  "C2'"  . GTP   O 5  .   ? -11.836 -18.047  -12.354 0.00 38.90  ? 501 GTP   C "C2'"  1 
HETATM 17350 O  "O2'"  . GTP   O 5  .   ? -10.745 -17.728  -11.522 0.00 40.41  ? 501 GTP   C "O2'"  1 
HETATM 17351 C  "C1'"  . GTP   O 5  .   ? -12.406 -19.417  -12.019 0.00 35.94  ? 501 GTP   C "C1'"  1 
HETATM 17352 N  N9     . GTP   O 5  .   ? -11.910 -20.427  -12.968 0.00 35.34  ? 501 GTP   C N9     1 
HETATM 17353 C  C8     . GTP   O 5  .   ? -12.307 -20.582  -14.269 0.00 34.77  ? 501 GTP   C C8     1 
HETATM 17354 N  N7     . GTP   O 5  .   ? -11.629 -21.623  -14.802 0.00 34.53  ? 501 GTP   C N7     1 
HETATM 17355 C  C5     . GTP   O 5  .   ? -10.811 -22.141  -13.860 0.00 34.91  ? 501 GTP   C C5     1 
HETATM 17356 C  C6     . GTP   O 5  .   ? -9.913  -23.201  -13.880 0.00 34.92  ? 501 GTP   C C6     1 
HETATM 17357 O  O6     . GTP   O 5  .   ? -9.758  -23.863  -14.905 0.00 34.86  ? 501 GTP   C O6     1 
HETATM 17358 N  N1     . GTP   O 5  .   ? -9.198  -23.507  -12.740 0.00 35.36  ? 501 GTP   C N1     1 
HETATM 17359 C  C2     . GTP   O 5  .   ? -9.379  -22.759  -11.594 0.00 34.63  ? 501 GTP   C C2     1 
HETATM 17360 N  N2     . GTP   O 5  .   ? -8.691  -23.052  -10.495 0.00 34.71  ? 501 GTP   C N2     1 
HETATM 17361 N  N3     . GTP   O 5  .   ? -10.273 -21.707  -11.584 0.00 34.47  ? 501 GTP   C N3     1 
HETATM 17362 C  C4     . GTP   O 5  .   ? -10.979 -21.400  -12.699 0.00 35.01  ? 501 GTP   C C4     1 
HETATM 17363 CA CA     . CA    P 6  .   ? -14.327 -55.117  -11.658 0.00 59.85  ? 502 CA    C CA     1 
HETATM 17364 MG MG     . MG    Q 7  .   ? -18.817 -20.039  -19.201 0.00 37.44  ? 503 MG    C MG     1 
HETATM 17365 N  N12    . A1D6L R 8  .   ? -14.933 -8.610   -21.033 1.00 55.08  ? 501 A1D6L D N12    1 
HETATM 17366 C  C13    . A1D6L R 8  .   ? -14.647 -7.924   -19.762 1.00 50.89  ? 501 A1D6L D C13    1 
HETATM 17367 C  C15    . A1D6L R 8  .   ? -15.114 -10.145  -18.570 1.00 50.54  ? 501 A1D6L D C15    1 
HETATM 17368 C  C17    . A1D6L R 8  .   ? -15.691 -9.810   -20.983 1.00 55.47  ? 501 A1D6L D C17    1 
HETATM 17369 C  C20    . A1D6L R 8  .   ? -14.030 -5.935   -18.521 1.00 47.59  ? 501 A1D6L D C20    1 
HETATM 17370 C  C21    . A1D6L R 8  .   ? -14.297 -6.562   -19.741 1.00 52.21  ? 501 A1D6L D C21    1 
HETATM 17371 C  C01    . A1D6L R 8  .   ? -10.715 -7.615   -21.596 1.00 56.67  ? 501 A1D6L D C01    1 
HETATM 17372 C  C02    . A1D6L R 8  .   ? -10.273 -7.223   -22.849 1.00 57.73  ? 501 A1D6L D C02    1 
HETATM 17373 C  C03    . A1D6L R 8  .   ? -11.167 -7.156   -23.898 1.00 64.37  ? 501 A1D6L D C03    1 
HETATM 17374 C  C04    . A1D6L R 8  .   ? -12.536 -7.486   -23.693 1.00 64.51  ? 501 A1D6L D C04    1 
HETATM 17375 C  C05    . A1D6L R 8  .   ? -12.980 -7.861   -22.464 1.00 61.69  ? 501 A1D6L D C05    1 
HETATM 17376 C  C06    . A1D6L R 8  .   ? -12.042 -7.937   -21.400 1.00 57.95  ? 501 A1D6L D C06    1 
HETATM 17377 C  C07    . A1D6L R 8  .   ? -14.370 -8.175   -22.301 1.00 62.25  ? 501 A1D6L D C07    1 
HETATM 17378 C  C09    . A1D6L R 8  .   ? -14.672 -7.725   -24.542 1.00 60.92  ? 501 A1D6L D C09    1 
HETATM 17379 C  C14    . A1D6L R 8  .   ? -14.722 -8.635   -18.555 1.00 49.62  ? 501 A1D6L D C14    1 
HETATM 17380 C  C16    . A1D6L R 8  .   ? -15.178 -10.757  -19.945 1.00 50.09  ? 501 A1D6L D C16    1 
HETATM 17381 C  C18    . A1D6L R 8  .   ? -14.455 -7.990   -17.330 1.00 47.05  ? 501 A1D6L D C18    1 
HETATM 17382 C  C19    . A1D6L R 8  .   ? -14.104 -6.648   -17.320 1.00 44.33  ? 501 A1D6L D C19    1 
HETATM 17383 C  C23    . A1D6L R 8  .   ? -14.999 -5.409   -15.568 1.00 49.89  ? 501 A1D6L D C23    1 
HETATM 17384 F  F24    . A1D6L R 8  .   ? -9.846  -7.705   -20.549 1.00 61.95  ? 501 A1D6L D F24    1 
HETATM 17385 N  N08    . A1D6L R 8  .   ? -15.160 -8.106   -23.361 1.00 61.71  ? 501 A1D6L D N08    1 
HETATM 17386 N  N10    . A1D6L R 8  .   ? -13.402 -7.422   -24.733 1.00 60.55  ? 501 A1D6L D N10    1 
HETATM 17387 N  N11    . A1D6L R 8  .   ? -15.563 -7.639   -25.682 1.00 69.07  ? 501 A1D6L D N11    1 
HETATM 17388 O  O22    . A1D6L R 8  .   ? -13.853 -6.003   -16.124 1.00 50.30  ? 501 A1D6L D O22    1 
HETATM 17389 H  H151   . A1D6L R 8  .   ? -14.382 -10.694  -17.987 1.00 60.65  ? 501 A1D6L D H151   1 
HETATM 17390 H  H152   . A1D6L R 8  .   ? -16.089 -10.250  -18.105 1.00 60.65  ? 501 A1D6L D H152   1 
HETATM 17391 H  H172   . A1D6L R 8  .   ? -15.623 -10.295  -21.951 1.00 66.56  ? 501 A1D6L D H172   1 
HETATM 17392 H  H171   . A1D6L R 8  .   ? -16.716 -9.555   -20.736 1.00 66.56  ? 501 A1D6L D H171   1 
HETATM 17393 H  H201   . A1D6L R 8  .   ? -13.764 -4.885   -18.505 1.00 57.11  ? 501 A1D6L D H201   1 
HETATM 17394 H  H211   . A1D6L R 8  .   ? -14.234 -6.002   -20.666 1.00 62.65  ? 501 A1D6L D H211   1 
HETATM 17395 H  H021   . A1D6L R 8  .   ? -9.230  -6.970   -23.005 1.00 69.28  ? 501 A1D6L D H021   1 
HETATM 17396 H  H031   . A1D6L R 8  .   ? -10.825 -6.853   -24.881 1.00 77.25  ? 501 A1D6L D H031   1 
HETATM 17397 H  H061   . A1D6L R 8  .   ? -12.374 -8.253   -20.418 1.00 69.54  ? 501 A1D6L D H061   1 
HETATM 17398 H  H161   . A1D6L R 8  .   ? -14.181 -11.078  -20.229 1.00 60.11  ? 501 A1D6L D H161   1 
HETATM 17399 H  H162   . A1D6L R 8  .   ? -15.832 -11.622  -19.910 1.00 60.11  ? 501 A1D6L D H162   1 
HETATM 17400 H  H181   . A1D6L R 8  .   ? -14.523 -8.540   -16.400 1.00 56.47  ? 501 A1D6L D H181   1 
HETATM 17401 H  H231   . A1D6L R 8  .   ? -15.676 -5.112   -16.365 1.00 59.87  ? 501 A1D6L D H231   1 
HETATM 17402 H  H232   . A1D6L R 8  .   ? -14.711 -4.533   -14.994 1.00 59.87  ? 501 A1D6L D H232   1 
HETATM 17403 H  H233   . A1D6L R 8  .   ? -15.497 -6.121   -14.917 1.00 59.87  ? 501 A1D6L D H233   1 
HETATM 17404 H  H112   . A1D6L R 8  .   ? -16.541 -7.835   -25.563 1.00 82.89  ? 501 A1D6L D H112   1 
HETATM 17405 H  H111   . A1D6L R 8  .   ? -15.204 -7.393   -26.591 1.00 82.89  ? 501 A1D6L D H111   1 
HETATM 17406 P  PB     . GDP   S 9  .   ? -25.375 10.566   -44.147 0.00 89.92  ? 502 GDP   D PB     1 
HETATM 17407 O  O1B    . GDP   S 9  .   ? -25.167 11.371   -45.407 0.00 91.37  ? 502 GDP   D O1B    1 
HETATM 17408 O  O2B    . GDP   S 9  .   ? -24.684 9.232    -44.303 0.00 89.54  ? 502 GDP   D O2B    1 
HETATM 17409 O  O3B    . GDP   S 9  .   ? -26.840 10.284   -43.947 0.00 88.45  ? 502 GDP   D O3B    1 
HETATM 17410 O  O3A    . GDP   S 9  .   ? -24.761 11.318   -42.856 0.00 89.40  ? 502 GDP   D O3A    1 
HETATM 17411 P  PA     . GDP   S 9  .   ? -23.185 11.662   -42.810 0.00 89.02  ? 502 GDP   D PA     1 
HETATM 17412 O  O1A    . GDP   S 9  .   ? -22.791 12.482   -44.013 0.00 89.73  ? 502 GDP   D O1A    1 
HETATM 17413 O  O2A    . GDP   S 9  .   ? -22.403 10.369   -42.699 0.00 87.39  ? 502 GDP   D O2A    1 
HETATM 17414 O  "O5'"  . GDP   S 9  .   ? -22.915 12.548   -41.494 0.00 86.29  ? 502 GDP   D "O5'"  1 
HETATM 17415 C  "C5'"  . GDP   S 9  .   ? -22.140 13.737   -41.579 0.00 85.17  ? 502 GDP   D "C5'"  1 
HETATM 17416 C  "C4'"  . GDP   S 9  .   ? -21.265 13.790   -40.343 0.00 83.14  ? 502 GDP   D "C4'"  1 
HETATM 17417 O  "O4'"  . GDP   S 9  .   ? -20.580 12.542   -40.257 0.00 82.99  ? 502 GDP   D "O4'"  1 
HETATM 17418 C  "C3'"  . GDP   S 9  .   ? -20.218 14.880   -40.461 0.00 82.37  ? 502 GDP   D "C3'"  1 
HETATM 17419 O  "O3'"  . GDP   S 9  .   ? -20.212 15.655   -39.264 0.00 81.70  ? 502 GDP   D "O3'"  1 
HETATM 17420 C  "C2'"  . GDP   S 9  .   ? -18.887 14.177   -40.578 0.00 81.23  ? 502 GDP   D "C2'"  1 
HETATM 17421 O  "O2'"  . GDP   S 9  .   ? -17.954 14.754   -39.662 0.00 80.62  ? 502 GDP   D "O2'"  1 
HETATM 17422 C  "C1'"  . GDP   S 9  .   ? -19.167 12.732   -40.210 0.00 81.27  ? 502 GDP   D "C1'"  1 
HETATM 17423 N  N9     . GDP   S 9  .   ? -18.511 11.842   -41.194 0.00 79.91  ? 502 GDP   D N9     1 
HETATM 17424 C  C8     . GDP   S 9  .   ? -18.931 11.603   -42.451 0.00 80.85  ? 502 GDP   D C8     1 
HETATM 17425 N  N7     . GDP   S 9  .   ? -18.098 10.738   -43.084 0.00 79.68  ? 502 GDP   D N7     1 
HETATM 17426 C  C5     . GDP   S 9  .   ? -17.121 10.412   -42.216 0.00 77.04  ? 502 GDP   D C5     1 
HETATM 17427 C  C6     . GDP   S 9  .   ? -15.919 9.548    -42.231 0.00 75.23  ? 502 GDP   D C6     1 
HETATM 17428 O  O6     . GDP   S 9  .   ? -15.612 8.893    -43.250 0.00 75.49  ? 502 GDP   D O6     1 
HETATM 17429 N  N1     . GDP   S 9  .   ? -15.173 9.489    -41.121 0.00 74.12  ? 502 GDP   D N1     1 
HETATM 17430 C  C2     . GDP   S 9  .   ? -15.478 10.183   -40.008 0.00 74.99  ? 502 GDP   D C2     1 
HETATM 17431 N  N2     . GDP   S 9  .   ? -14.670 10.069   -38.926 0.00 73.92  ? 502 GDP   D N2     1 
HETATM 17432 N  N3     . GDP   S 9  .   ? -16.563 10.994   -39.922 0.00 76.15  ? 502 GDP   D N3     1 
HETATM 17433 C  C4     . GDP   S 9  .   ? -17.401 11.143   -40.974 0.00 77.77  ? 502 GDP   D C4     1 
HETATM 17434 P  PG     . ACP   T 11 .   ? -8.342  -48.753  93.385  0.00 110.22 ? 401 ACP   F PG     1 
HETATM 17435 O  O1G    . ACP   T 11 .   ? -7.139  -49.492  93.874  0.00 108.48 ? 401 ACP   F O1G    1 
HETATM 17436 O  O2G    . ACP   T 11 .   ? -7.979  -47.626  92.392  0.00 111.98 ? 401 ACP   F O2G    1 
HETATM 17437 O  O3G    . ACP   T 11 .   ? -9.370  -49.674  92.691  0.00 104.91 ? 401 ACP   F O3G    1 
HETATM 17438 P  PB     . ACP   T 11 .   ? -9.879  -49.219  95.894  0.00 110.58 ? 401 ACP   F PB     1 
HETATM 17439 O  O1B    . ACP   T 11 .   ? -8.805  -50.227  96.219  0.00 107.16 ? 401 ACP   F O1B    1 
HETATM 17440 O  O2B    . ACP   T 11 .   ? -11.134 -49.886  95.253  0.00 109.39 ? 401 ACP   F O2B    1 
HETATM 17441 C  C3B    . ACP   T 11 .   ? -9.211  -47.969  94.744  0.00 112.34 ? 401 ACP   F C3B    1 
HETATM 17442 P  PA     . ACP   T 11 .   ? -10.745 -49.462  98.374  0.00 114.51 ? 401 ACP   F PA     1 
HETATM 17443 O  O1A    . ACP   T 11 .   ? -9.697  -50.468  98.638  0.00 111.25 ? 401 ACP   F O1A    1 
HETATM 17444 O  O2A    . ACP   T 11 .   ? -12.072 -50.079  97.923  0.00 115.11 ? 401 ACP   F O2A    1 
HETATM 17445 O  O3A    . ACP   T 11 .   ? -10.302 -48.441  97.239  0.00 114.72 ? 401 ACP   F O3A    1 
HETATM 17446 O  "O5'"  . ACP   T 11 .   ? -10.999 -48.451  99.564  0.00 114.95 ? 401 ACP   F "O5'"  1 
HETATM 17447 C  "C5'"  . ACP   T 11 .   ? -10.702 -48.797  100.933 0.00 112.80 ? 401 ACP   F "C5'"  1 
HETATM 17448 C  "C4'"  . ACP   T 11 .   ? -9.340  -48.294  101.333 0.00 111.54 ? 401 ACP   F "C4'"  1 
HETATM 17449 O  "O4'"  . ACP   T 11 .   ? -9.264  -48.442  102.764 0.00 110.41 ? 401 ACP   F "O4'"  1 
HETATM 17450 C  "C3'"  . ACP   T 11 .   ? -8.274  -49.244  100.807 0.00 109.90 ? 401 ACP   F "C3'"  1 
HETATM 17451 O  "O3'"  . ACP   T 11 .   ? -7.728  -48.601  99.663  0.00 111.14 ? 401 ACP   F "O3'"  1 
HETATM 17452 C  "C2'"  . ACP   T 11 .   ? -7.212  -49.182  101.900 0.00 107.93 ? 401 ACP   F "C2'"  1 
HETATM 17453 O  "O2'"  . ACP   T 11 .   ? -6.571  -47.912  101.854 0.00 107.99 ? 401 ACP   F "O2'"  1 
HETATM 17454 C  "C1'"  . ACP   T 11 .   ? -8.103  -49.156  103.141 0.00 108.33 ? 401 ACP   F "C1'"  1 
HETATM 17455 N  N9     . ACP   T 11 .   ? -8.546  -50.499  103.502 0.00 106.49 ? 401 ACP   F N9     1 
HETATM 17456 C  C8     . ACP   T 11 .   ? -9.132  -51.436  102.688 0.00 105.42 ? 401 ACP   F C8     1 
HETATM 17457 N  N7     . ACP   T 11 .   ? -9.429  -52.560  103.289 0.00 103.96 ? 401 ACP   F N7     1 
HETATM 17458 C  C5     . ACP   T 11 .   ? -9.018  -52.349  104.595 0.00 104.74 ? 401 ACP   F C5     1 
HETATM 17459 C  C6     . ACP   T 11 .   ? -9.057  -53.158  105.744 0.00 104.05 ? 401 ACP   F C6     1 
HETATM 17460 N  N6     . ACP   T 11 .   ? -9.548  -54.400  105.765 0.00 103.01 ? 401 ACP   F N6     1 
HETATM 17461 N  N1     . ACP   T 11 .   ? -8.563  -52.645  106.886 0.00 103.73 ? 401 ACP   F N1     1 
HETATM 17462 C  C2     . ACP   T 11 .   ? -8.067  -51.405  106.877 0.00 103.88 ? 401 ACP   F C2     1 
HETATM 17463 N  N3     . ACP   T 11 .   ? -7.978  -50.547  105.860 0.00 104.83 ? 401 ACP   F N3     1 
HETATM 17464 C  C4     . ACP   T 11 .   ? -8.473  -51.082  104.741 0.00 105.46 ? 401 ACP   F C4     1 
HETATM 17465 H  H3B1   . ACP   T 11 .   ? -8.595  -47.392  95.224  0.00 134.80 ? 401 ACP   F H3B1   1 
HETATM 17466 H  H3B2   . ACP   T 11 .   ? -9.942  -47.439  94.390  0.00 134.80 ? 401 ACP   F H3B2   1 
HETATM 17467 H  "H5'1" . ACP   T 11 .   ? -10.723 -49.762  101.030 0.00 135.35 ? 401 ACP   F "H5'1" 1 
HETATM 17468 H  "H5'2" . ACP   T 11 .   ? -11.369 -48.399  101.514 0.00 135.35 ? 401 ACP   F "H5'2" 1 
HETATM 17469 H  "H4'"  . ACP   T 11 .   ? -9.170  -47.373  101.079 0.00 133.85 ? 401 ACP   F "H4'"  1 
HETATM 17470 H  "H3'"  . ACP   T 11 .   ? -8.607  -50.145  100.674 0.00 131.89 ? 401 ACP   F "H3'"  1 
HETATM 17471 H  "HO3'" . ACP   T 11 .   ? -6.893  -48.762  99.660  0.00 133.37 ? 401 ACP   F "HO3'" 1 
HETATM 17472 H  "H2'"  . ACP   T 11 .   ? -6.608  -49.940  101.866 0.00 129.51 ? 401 ACP   F "H2'"  1 
HETATM 17473 H  "HO2'" . ACP   T 11 .   ? -5.787  -48.036  102.163 0.00 129.59 ? 401 ACP   F "HO2'" 1 
HETATM 17474 H  "H1'"  . ACP   T 11 .   ? -7.658  -48.710  103.879 0.00 130.00 ? 401 ACP   F "H1'"  1 
HETATM 17475 H  H8     . ACP   T 11 .   ? -9.303  -51.285  101.787 0.00 126.51 ? 401 ACP   F H8     1 
HETATM 17476 H  HN61   . ACP   T 11 .   ? -10.160 -54.633  105.207 0.00 123.61 ? 401 ACP   F HN61   1 
HETATM 17477 H  HN62   . ACP   T 11 .   ? -9.251  -54.965  106.342 0.00 123.61 ? 401 ACP   F HN62   1 
HETATM 17478 H  H2     . ACP   T 11 .   ? -7.739  -51.098  107.691 0.00 124.65 ? 401 ACP   F H2     1 
# 
